Gene therapy, regulatory mechanisms, and protein function in vision

James F. McGinnis

doi:10.1017/S0140525X00039388

Gene therapy, regulatory mechanisms, and protein function in vision

Published online by Cambridge University Press: 04 February 2010

James F. McGinnis

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James F. McGinnis*: Affiliation:
Department of Anatomy and Cell Biology, University of California, Los Angeles, Los Angeles, CA 90024. [email protected]

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Abstract

Hereditary retinal degeneration due to mutations in visual genes may be amenable to therapeutic interventions that modulate, either positively or negatively, the amount of protein product. Some of the proteins involved in phototransduction are rapidly moved by a lightdependent mechanism between the inner segment and the outer segment in rod photoreceptor cells, and this phenomenon is important in phototransduction.

Type: Article Commentary
Information: Behavioral and Brain Sciences , Volume 18 , Special Issue 3: An International Journal of Current Research and Theory with Open Peer Commentary , September 1995 , pp. 481 - 482

DOI: https://doi.org/10.1017/S0140525X00039388 [Opens in a new window]
Copyright: Copyright © Cambridge University Press 1995

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References

Abeliovich, A., Chen, C., Goda, Y., Silva, A. J., Stevens, C. F. & Tonegawa, S. (1993a) Modified hippocampal long term potentiation in PKC-gamma mutant mice. Cell 75: 1253–62. [aZX]10.1016/0092-8674(93)90613-UCrossRef Google Scholar PubMed

Abeliovich, A., Paylor, R., Chen, C., Kim, J. J., Wehner, J. M. & Tonegawa, S. (1993b) PKC gamma mutant mice exhibit mild deficits in spatial and contextual learning. Cell 75: 1263–71. [aZX]10.1016/0092-8674(93)90614-VCrossRef Google Scholar PubMed

Abrams, T. W. (1985) Activity-dependent presynaptic facilitation: An associative mechanism in Aplysia. Cellular and Molecular Neurobiology 5: 123–45. [TWA]10.1007/BF00711089CrossRef Google Scholar PubMed

Abrams, T. W., Bernier, L., Hawkins, R. D. & Kandel, E. R. (1984) Possible roles of Ca2+ and cAMP in activity-dependent facilitation, a mechanism for associative learning in Aplysia. Society for Neuroscience Abstracts 10:269. [TWA]Google Scholar

Abrams, T. W. & Galun, J. (1993) Temporal aspects of activation of a Ca2+/CaM-sensitive adenylyl cyclase: Possible contribution to detection of CS-US pairing during conditioning. Society for Neuroscience Abstracts 19: 1065. [TWA]Google Scholar

Abrams, T. W., Jarrard, H. E. & Yovell, Y. (1994) Calcium accelerates adenylyl cyclase deactivation contributing to CS-US sequence requirement during conditioning in Aplysia. Submitted. [TWA]Google Scholar

Abrams, T. W. & Kandel, E. R. (1988) Is contiguity detection in classical conditioning a system or a cellular property? Learning in Aplysia suggests a possible molecular site. Trends in Neuroscience 11: 128–35. [TWA]10.1016/0166-2236(88)90137-3CrossRef Google Scholar PubMed

Abrams, T. W, Karl, K. A. & Kandel, E. R. (1991a) Biochemical studies of stimulus convergence during classical conditioning in Aplysia: Dual regulation of adenylate cyclase by Ca2+/calmodulin and transmitter. Journal of Neuroscience 11: 2655–65. [aZX, WH]10.1523/JNEUROSCI.11-09-02655.1991CrossRef Google Scholar PubMed

Adamus, G., Ortega, H., Witkowska, D. & Polans, A. (1994) Recovorin: A potent uveitogen for the induction of photoreceptor degeneration in Lewis rats. Experimental Eye Research 59: 447–56. [ASP]10.1006/exer.1994.1130CrossRef Google Scholar

Adamus, G., Zam, Z. S., Arendt, A., Palczewski, K., McDowell, J. H. & Hargrave, P. A. (1991) Anti-rhodopsin monoclonal antibodies of defined specificity: Characterization and application. Vision Research 31: 17–31 [aPAH]10.1016/0042-6989(91)90069-HCrossRef Google Scholar PubMed

Agranoff, B. W., Davis, R. E. & Brink, J. J. (1965) Memory fixation in the goldfish. Proceedings of the National Academy of Sciences USA 54: 788– 93. [EDR]10.1073/pnas.54.3.788CrossRef Google Scholar PubMed

Aguirre, G., Farber, D. Lolley, R., Fletcher, R. T. & Chader, C. (1978) Rodcone dysplasia in Irish setters: A defect in cyclic GMP metabolism in visual cells. Science 201: 1133–34. [MWK]10.1126/science.210508CrossRef Google Scholar

Ahlijanian, M. K., Halford, M. K. & Cooper, D. M. F. (1987) Ca²+/ calmodulin distinguishes between guanyl-5'-yl-imidodiphosphate- and opiate-mediated inhibition of rat striatal adenylate cyclase. Journal of Neurochemistry 49: 1308–15. [MMR]10.1111/j.1471-4159.1987.tb10025.xCrossRef Google Scholar PubMed

Ahmad, I., Korbmacher, C., Segal, A. S., Cheung, P., Boulpaep, E. L. & Barnstable, C. J. (1992) Mouse cortical collecting duct cells show nonselective cation channel activity and express a gene related to the cGMP-gated rod photorecoptor channel. Proceedings of the National Academy of Sciences USA 89: 10262–66. [aRSM]10.1073/pnas.89.21.10262CrossRef Google Scholar

Ahmad, I., Redmond, L. J. & Barnstable, C. J. (1990) Developmental and tissue-specific expression of rod photoreceptor cGMP-gated ion channel gene. Biochemical and Biophysical Research Communications 173:463–70. [aRSM]10.1016/S0006-291X(05)81081-2CrossRef Google Scholar PubMed

Akita, H., Tanis, S. P., Adams, M., Balogh-Nair, V. & Nakanishi, K. (1980) Nonbleachable rhodopsins retaining the full natural chromophore. Journal of the American Chemical Society 102: 6370–72. [aPAH]10.1021/ja00540a047CrossRef Google Scholar

Al-Maghtheh, A., Kim, R. Y., Inglehearn, C. & Bhattacharya, S. S. (1994a) A 150 bp insert in the rhodopsin gene of an autosomal dominant retinitis pigmentosa family. Human Molecular Cenetics 3: 205–6. [aSPD]10.1093/hmg/3.1.205CrossRef Google Scholar

Al-Maghtheh, M., Inglehearn, C. F., Keen, T. J., Evans, K., Moore, A. T., Jay, M., Bird, A. C. & Bhattacharya, S. S. (1994) Identification of a sixth locus for autosomal dominant retinitis pigmentosa on chromosome 19. Human Molecular Genetics 3: 351–54. [aSPD]10.1093/hmg/3.2.351CrossRef Google Scholar PubMed

Al-Maghtheh, M., Inglehearn, C., Lunt, P., Jay, M., Bird, A. & Bhattacharya, S. (1994) Two new rhodopsin transversion mutations (C40R; M216K) in families with autosomal dominant retinitis pigmentosa. Human Mutation 3: 409–10. [aSPD]10.1002/humu.1380030417CrossRef Google Scholar

Albert, A. D. & Litman, B. J. (1978) Independent structural domains in the membrane protein bovine rhodopsin. Biochemistry 17: 3893–3900. [ADA]10.1021/bi00612a001CrossRef Google Scholar PubMed

Alexander, K. A., Cimler, B. M., Meier, K. E. & Storm, D. R. (1987) Regulation of cahmodulin binding to P-57. Journal of Biological Chemistry 262: 6108–13. [aZX]10.1016/S0021-9258(18)45544-5CrossRef Google Scholar PubMed

Allen, J. P. & Feher, G. (1991). Crystallization of reaction centers from Rhodobacter sphaervides. In: Crystallization of membrane proteins, ed. Michel, H.. CRC Press. [aPAH]Google Scholar

Altenhnfen, W., Ludwig, J., Eismann, E., Kraus, W., Bönigk, W. & Kaupp, U. B. (1991) Control of ligand specificity in cyclic nucleotide-gated channels from rod photoreceptors and olfactory epithelium. Proceedings of the National Academy of Sciences USA 88: 9868–72. [aRSM]10.1073/pnas.88.21.9868CrossRef Google Scholar

Ames, J. B., Porumbo, T., Tanaka, T., Ikura, M. & Stryer, L. (1995) Aminoturminal myristoylation induces cooperative calcium binding to recoverin. Journal of Biological Chemistry 270: 4526–33. [rJBH]10.1074/jbc.270.9.4526CrossRef Google Scholar PubMed

Amos, L. A., Henderson, R. & Unwin, P. N. T. (1982) Three-dimensional structure determination by electron microscopy of 2-D crystals. Progress in Biophysics and Molecular Biology 39: 183–231. [aPAH]10.1016/0079-6107(83)90017-2CrossRef Google Scholar

Anant, J. S. & Fung, B. K.-K. (1992) In vivo farnesylation of rat rhodopsin kinase. Biochemical and Biophysical Research Communications 183: 468–73. [aMDB]10.1016/0006-291X(92)90505-FCrossRef Google Scholar PubMed

Anant, J. S., Ong, O. C, Xie, H., Clarke, S., O'Brien, P. J. & Fung, B. K.-K. (1992) In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits. Journal of Biological Chemistry 267: 687–90. [aMDB]10.1016/S0021-9258(18)48336-6CrossRef Google Scholar PubMed

Andersson, L. & Porath, J. (1986) Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography. Analytical Biochemistry 154: 250– 54. [aPAH]10.1016/0003-2697(86)90523-3CrossRef Google Scholar PubMed

Andrade, R. (1993) Neuron 10: 83–88. [MMR]10.1016/0896-6273(93)90244-LCrossRef Google Scholar

Andreasen, T. J., Luetje, C. W., Heideman, W. & Storm, D. R. (1983) Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes. Biochemistry 22: 4615–18. [aZX]10.1021/bi00289a001CrossRef Google Scholar PubMed

Andréasson, S., Ehinger, B., Abrahamson, M. & Fex, G. (1992) A six-generation family with autosomal dominant retinitis pigmentosa and a rhodopsin gene mutation (arginine-135-leucine). Ophthalmic Pediatrics and Genetics 13: 145–53. [aSPD]10.3109/13816819209046483CrossRef Google Scholar

Angleson, J. K. & Wensel, T. G. (1993) A GTPase-accelerating factor for transducin, distinct from its effector cGMP phosphodiesterase, in rod outer segment membranes. Neuron 11: 939–49. [aMDB]10.1016/0896-6273(93)90123-9CrossRef Google Scholar PubMed

Angleson, J. K. & Wensel, T. G. (1994) Enhancement of rod outer segment GTPase accelerating protein activity by the inhibitory subunit of cGMP phosphodiesterase. Journal of Biological Chemistry 269: 16290–96. [arMDB]10.1016/S0021-9258(17)34006-1CrossRef Google Scholar PubMed

Antonny, B., Otto-Bruc, A., Chabre, M. & Minh Vuong, T. (1993) GTP hydrolysis by purified α-subunit of transducin and its complex with the cyclic GMP phosphodiesterase inhibitor. Biochemistry 32: 8646– 53. [arMDB, BMW]10.1021/bi00084a036CrossRef Google Scholar PubMed

Apel, E. D., Byford, M. F., Au, D., Walsh, K. A. & Storm, D. R. (1990) Identification of the protein kinase C phosphorylation site in neuromodulin. Biochemistry 29: 2330–35. [aZX]10.1021/bi00461a017CrossRef Google Scholar PubMed

Apfelstedt-Sylla, E., Kunisch, M., Horn, M., Ruther, K., Gal, A. & Zrenner, E. (1992) Diffuse loss of rod function in autosomal dominant retinitis pigmentosa with pro-347-leu mutation of rhodopsin. German Journal of Ophthalmology 1: 319–27. [aSPD]Google Scholar PubMed

Applebury, M. A. (1991) Molecular determinants of visual pigment function. Current Opinion in Neurobiology 1: 263–69. [aPAH]10.1016/0959-4388(91)90088-OCrossRef Google Scholar PubMed

Applebury, M. L. & Hargrave, P. A. (1986) Molecular biology of the visual pigments. Vision Research 26: 1881–95. [aPAH]10.1016/0042-6989(86)90115-XCrossRef Google Scholar PubMed

Arikawa, K., Molday, L. L., Molday, R. S. & Williams, D. (1992) Localization of peripherin/rds in the disk membranes of cone and rod photoreceptors: Relationship to disk membrane morphogenesis and retinal degeneration. Journal of Cell Biology 116: 659–67. [aSPD]10.1083/jcb.116.3.659CrossRef Google Scholar PubMed

Arnoux, B., Ducruix, A., Reiss-Husson, F., Lutz, M., Norris, J., Schiffer, M. & Chang, C. G. (1989) Structure of spheroidene in the photosynthetic reaction center from Y Rhodobacter sphaeroides . FEBS Letters 258: 47–50. [aPAH]10.1016/0014-5793(89)81612-6CrossRef Google Scholar PubMed

Arshavsky, V. Y., Antoch, M. P., Dizhoor, A. M., Rakhilin, S. V. & Philippov, P. P. (1987) Interaction of visual transduction enzymes in a detergent solution. In: Retinal proteins, ed. Ovchinnikov, Y. A.. Utrecht: VNU Science Press. [aMDB]Google Scholar

Arshavsky, V. Y., Antoch, M. P., Lukjanov, K. A. & Philippov, P. P. (1989) Transducin GTPase provides for rapid quenching of the cGMP cascade in rod outer segments. FEBS Letters 250: 353–56. [aMDB]10.1016/0014-5793(89)80754-9CrossRef Google Scholar PubMed

Arshavsky, V. Y. & Bownds, M. D. (1992) Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP. Nature 357: 416–17. [aMDB]10.1038/357416a0CrossRef Google Scholar PubMed

Arshavsky, V. Y., Dizhoor, A. M., Shestakova, I. K. & Philippov, P. P. (1985) The effect of rhodopsin phosphorylation on the light-dependent activation of phosphodiesterase from bovine rod outer segments. FEBS Letters 181: 264–66. [aMDB]10.1016/0014-5793(85)80272-6CrossRef Google Scholar PubMed

Arshavsky, V. Y., Dumke, C. L. & Bownds, M. D. (1992) Non-catalytic cGMP binding sites of amphibian rod cCMP phosphodiesterase control interaction with its inhibitory gamma-subunits—a putative regulatory mechanism of the rod photoresponse. Journal of Biological Chemistry 267: 24501–7. [aMDB]10.1016/S0021-9258(18)35793-4CrossRef Google Scholar

Arshavsky, V. Y., Dumke, C. L. & Bownds, M. D.(1995) Manuscript in preparation. [aMDB]Google Scholar

Arshavsky, V. Y., Dumke, C. L., Zhu, Y., Artemyev, N. O., Skiba, N. P., Hamm, H. E. & Bownds, M. D. (1994) Regulation of transducin GTPase activity in bovine rod outer segments. Journal of Biological Chemistry 269: 19882–87. [arMDB]10.1016/S0021-9258(17)32102-6CrossRef Google Scholar PubMed

Arshavsky, V. Y., Gray-Keller, M. P. & Bownds, M. D. (1991) cGMP suppresses GTPase activity of a portion of transducin equimolar to phosphodiesterase in frog rod outer segments. Light-induced cGMP decreases as a putative feedback mechanism of the photoresponse. Journal of Biological Chemistry 266: 18530–37. [aMDB]Google Scholar PubMed

Artlich, A., Horn, M., Lorenz, B., Bhattacharya, S. & Gal, A. (1992) Recurrent 3-bp deletion at codon 255/256 of the rhodopsin gene in a German pedigree with autosomal dominant retinitis pigmentosa. American Journal of Human Genetics 50: 876–78. [aSPD]Google Scholar

Aton, B. R., Litman, B. J. & Jackson, M. L. (1984) Isolation and Identification of the phosphorylated species of rhodopsin. Biochemistry 23: 1737– 41. [aPAH]10.1021/bi00303a024CrossRef Google Scholar PubMed

Bacskai, B. J., Hochner, B., Mahaut-Smith, M., Adams, S. R., Kaang, B. K., Kandel, E. R. & Tsien, R. Y. (1993) Spatially resolved dynamics of cAMP and protein kinase A subunits in Aplysia sensory neurons. Science 260: 222–26. [aZX]10.1126/science.7682336CrossRef Google Scholar PubMed

Baehr, W., Gorczyca, W., Subbaraya, I., Ohguro, H., Johnson, R. S., Walsh, K. A., Gray-Keller, M. P., Detwiler, P. B., Crabb, J. & Palezewski, K. (1994) Isolation, cloning, and functional characterization of bovine retina guanylate cyclase activating protein (GCAP). Investigative Ophthalmology and Visual Science 35: 1486. [aMDB]Google Scholar

Baehr, W., Morita, E. A., Swanson, R. J. & Applebury, M. L. (1982) Characterization of bovine rod outer segment G-protein. Journal of Biological Chemistry 257: 6452–60. [aMDB]10.1016/S0021-9258(20)65163-8CrossRef Google Scholar PubMed

Bakalyar, H. A. & Reed, R. R. (1990) Identification of a specialized adenylyl cyclase that may mediate odorant detection. Science 250: 1403–6. [aZX]10.1126/science.2255909CrossRef Google Scholar PubMed

Baldwin, J. M. (1993) The probable arrangement of the helices in G proteincoupled receptors. EM BO Journal 12: 1693–1703. [aSPD, SOS]Google Scholar

Baldwin, P. A. & Hubbell, W. L. (1985a) Effects of lipid environment on the light-induced conformational changes of rhodopsin: 1. Absence ofmetarhodopsin II production in dimyristoylphosphatidylcholine recombinant membranes. Biochemistry 24: 2624–32. [ADA]10.1021/bi00332a006CrossRef Google Scholar PubMed

Baldwin, P. A. & Hubbell, W. L. (1985b) Effects of lipid environment on the light-induced conformational changes of rhodopsin: 2. Roles of lipid chain length, unsaturation, and phase state. Biochemistry 24: 2633–39. [ADA]10.1021/bi00332a007CrossRef Google Scholar PubMed

Barker, D., Schafer, M. & White, R. (1984) Restriction sites containing CpG show a higher frequency of polymorphism in human DNA. Cell 6: 131– 38. [aSPD]10.1016/0092-8674(84)90081-3CrossRef Google Scholar

Bascom, R. A., Manara, S., Collins, L., Molday, R. S., Kalnins, V. I. & Mclnnes, R. R. (1992) Cloning of the cDNA for a novel photoreceptor membrane protein (rom-1) identifies a disk rim protein family implicated in human retinopathies. Neuron 8: 1171–84. [aSPD]10.1016/0896-6273(92)90137-3CrossRef Google Scholar PubMed

Baudier, J., Bronner, C., Kligman, D. & Cole, R. D. (1989) Protein kinase C substrates from bovine brain: Purification and characterization of neuromodulin, a neuron-specific calmodulin binding protein. Journal of Biological Chemistry 264: 1824–28. [EDR]10.1016/S0021-9258(18)94262-6CrossRef Google Scholar PubMed

Bauer, P. H., Müller, S., Puzicha, M., Pippig, S., Obermaier, B., Helmreich, E. J. M. & Lohse, M. J. (1992) Phosducin is a protein kinase A-regulated G-protein regulator. Nature 358: 73–76. [BMW]10.1038/358073a0CrossRef Google Scholar PubMed

Baumann, A., Frings, S., Godde, M., Seifert, R. & Kaupp, U. B. (1994) Primary structure and functional expression of a Drosphila cyclic nucleotide-gated channel present in eyes and antennae. EMBO Journal 13: 5040–50. [rRSM]10.1002/j.1460-2075.1994.tb06833.xCrossRef Google Scholar

Baylor, D. A. (1987) Photoreceptor signals and vision. Investigative Ophthalmology and Visual Science 28: 34–49. [aPAH]Google Scholar

Baylor, D. A. & Hodgkin, A. L. (1974) Changes in time scale and sensitivity in turtle photoreceptors. Journal of Physiology (London) 242: 729–58. [aMDB]10.1113/jphysiol.1974.sp010732CrossRef Google Scholar PubMed

Baylor, D. A., Lamb, T. D. & Yau, K.-W. (1979a) The membrane current of single rod outer semgments. Journal of Physiology (London) 288: 589–611. [aMDB]Google Scholar

Baylor, D. A., Lamb, T. D. & Yau, K.-W. (1979b) Responses of retinal rods to single photons. Journal of Physiology (London) 288: 613–34. [aMDB]Google Scholar PubMed

Baylor, D. A., Matthews, G. & Yau, K.-W. (1980) Two components of electrical dark noise in toad retinal rod outer segments. Journal of Physiology (London) 309: 591–621. [aMDB]10.1113/jphysiol.1980.sp013529CrossRef Google Scholar PubMed

Beaudet, A. L. & Tsui, L.-C. (1993) A suggested nomenclature for designating mutations. Human Mutation 2: 245–48. [aSPD]10.1002/humu.1380020402CrossRef Google Scholar PubMed

Bell, C., Converse, C. A., Collins, M. F., Esakowitz, L., Kelly, K. F. & Haites, N. E. (1992) Autosomal dominant retinitis pigmentosa (ADRP): A rhodopsin mutation in a Scottish family. Journal of Medical Genetics 29: 667–68. [aSPD]10.1136/jmg.29.9.667CrossRef Google Scholar

Bennett, A. E., Ok, J. H., Griffin, R. G. & Vega, S. (1992) Chemical shift correlation specetroscopy in rotating solids: Radio frequency-driven dipolar recoupling and logitudinal exchange. Journal of Chemical Physics 96: 8624–27. [SOS]10.1063/1.462267CrossRef Google Scholar

Bennett, N. & Clere, A. (1989) Activation of cGMP phosphodiesterase in retinal rods: Mechanism of interaction with the GTP-binding protein (transducin). Biochemistry 28: 7418–24. [aMDB]10.1021/bi00444a040CrossRef Google Scholar

Bennett, N. & Sitaramayya, A. (1988) Inactivation of photoexcited rhodopsin in retinal rods: The roles of rhodopsin kinase and 48-KDa protein(arrestin). Biochemistry 27: 1710–15. [aMDB]10.1021/bi00405a049CrossRef Google Scholar

Benowitz, L. I. & Routtenberg, A. (1987) A membrane phosphoprotein associated with neural development axonal regeneration, phospholipid metabolism, and synaptic plasticity. Trends in Neuroscience 10: 527– 32. [aZX]10.1016/0166-2236(87)90135-4CrossRef Google Scholar

Berson, E. L. (1993) Retinitis pigmentosa—The Friedenwald Lecture. Investigative Ophthamology and Visual Science 34: 1659–76. [aSPD, aPAH]Google Scholar

Berson, E. L., Rosner, B., Sandberg, M. A. & Dryja, T. P. (1991) Ocular findings in patients with autosomal dominant retinitis pigmentosa and a rhodopsin gene defect (Pro-23-His). Archives of Ophthalmology 109: 92–101. [aSPD]10.1001/archopht.1991.01080010094039CrossRef Google Scholar

Berson, E. L., Rosner, B., Sandberg, M. A., Weigel-DiFranco, C. & Dryja, T. P. (1991a) Ocular findings in patients with autosomal dominant retinitis pigmentosa and rhodopsin, Proline-347-Leucine. American Journal of Ophthalmology 111: 614–23. [aSPD]10.1016/S0002-9394(14)73708-0CrossRef Google Scholar PubMed

Berson, E. L., Sandberg, M. A. & Dryja, T. P. (1991b) Autosomal dominant retinitis pigmentosa with rhodopsin, valine-345-methionine. Transcripts of the American Ophthalmological Society 89: 117–30. [aSPD]Google Scholar PubMed

Bhattacharya, S. S., Ridge, K. D., Knox, B. E. & Khorana, H. G. (1992) Light-stable rhodopsin: 1. A rhodopsin analog reconstituted with a nonisomerizable ll-cis retinal derivative. Journal of Biological Chemistry 267: 6763–69. [aPAH]10.1016/S0021-9258(19)50491-4CrossRef Google Scholar PubMed

Bhattacharya, S. S., Wright, A. F., Clayton, J. F., Price, W. U., Phillips, C. I., McKeown, C. M. E., Jay, M., Bird, A. C, Pearson, P. L., Southern, E. M. & Evans, H. J. (1984) Close genetic linkage between X-linked retinitis pigmentosa and a restriction fragment length polymorphism identified by recombinant DNA probe Ll.28. Nature 309: 253–55. [aSPD]10.1038/309253a0CrossRef Google Scholar

Biel, M., Altenhofen, W., Hullin, R., Ludwig, J., Freichel, M., Flocherzi, V., Dascal, N., Kaupp, U. B. & Hofmann, F. (1993) Primary structure and functional expression of a cyclic nucleotide-gated channel from rabbit aorta. FEBS Letters 329: 134–38. [aRSM]10.1016/0014-5793(93)80209-DCrossRef Google Scholar PubMed

Biel, M., Zong, X., Distler, M., Bosse, R., Klugbauer, N., Murakami, M., Flockerzi, V. & Hoffmann, F. (1994) Another member of the cyclic nucleotide-gated channel family expressed in testis, kidney and heart. Proceedings of the National Academy of Sciences USA 91: 3505–9. [rRSM]10.1073/pnas.91.9.3505CrossRef Google Scholar

Biernbaum, M. S., Binder, B. M. & Bownds, M. D. (1991) Dim background light and Cerenkov radiation from 32P block reversal of rhodopsin phosphorylation in intact frog retinal rods. Visual Neuroscience 7: 499–503. [aMDB]10.1017/S0952523800009780CrossRef Google Scholar PubMed

Biernbaum, M. S. & Bownds, M. D. (1985) Light-induced changes in GTP and ATP in frog rod photoreeeptors: Comparison with recovery of dark current and light sensitivity during dark adaptation. Journal of General Physiology 85: 107–21. [aMDB]10.1085/jgp.85.1.107CrossRef Google Scholar PubMed

Binder, B. M., Biernbaum, M. S. & Bownds, M. D. (1990) Light activation of one rhodopsin molecule causes the phosphorylation of hundreds of others. A reaction observed in electropermeabilized frog rod outer segments exposed to dim illumination. Journal of Biological Chemistry 265: 15333–40. [aMDB]10.1016/S0021-9258(18)77260-8CrossRef Google Scholar PubMed

Binder, B. M., Brewer, E. & Bownds, M. D. (1989) Stimulation of protein phosphorylations in frog rod outer segments by protein kinase activators: Suppression of light-induced changes in membrane current and cGMP by protein kinase C activators. Journal of Biological Chemistry 264: 8857– 64. [aMDB]10.1016/S0021-9258(18)81872-5CrossRef Google Scholar PubMed

Bitensky, M. W, Wheeler, M. A., Yamazaki, A., Rasenick, M. M. & Stein, P. J. (1981) Cyclic nucleotide matabolism in vertebrate photoreceptors: A remarkable analogy and an unraveling enigma. Current Topics in Membrane Transportation 15: 237–71. [TGW]10.1016/S0070-2161(08)60505-5CrossRef Google Scholar

Blanton, S. H., Heckenlively, J. R., Cottingham, A. W, Friedman, J., Sadler, L. A., Wagner, M., Friedman, L. H. & Daiger, S. P. (1991) Linkage mapping of autosomal dominant retinitis pigmentosa (adRP) to the pericentric region of human chromosome 8. Genomics 11: 857–69. [aSPD]10.1016/0888-7543(91)90008-3CrossRef Google Scholar

Blatt, C., Eversole-Cire, P., Colin, V. H., Zollman, S. et al. (1988) Chromosomal localization of genes encoding guanine nuclcotide-binding protein subunits in mouse and human. Proceedings of the National Academy of Sciences USA 85: 7642–46. [aSPD]10.1073/pnas.85.20.7642CrossRef Google Scholar PubMed

Bodoia, R. D. & Detwiler, P. B. (1985) Patch-clamp recordings of the lightsensitive dark noise in retinal rods from the lizard and frog. Journal of Physiology 367: 183–216. [aRSM]CrossRef Google Scholar

Boekema, E. J., Van Heel, M. G. & Van Bruggen, E. F. J. (1986) Preparation of two-dimensional crystals of complex 1 and image analysis. Methods in Enzymology 126: 344–53. [aPAH]10.1016/S0076-6879(86)26034-6CrossRef Google Scholar

Boesze-Battaglia, K. & Albert, A. (1990) Cholesterol modulation of photoreceptor function in bovine rod outer segments. Journal of Biological Chemistry 265: 20727–30. [ADA]10.1016/S0021-9258(17)45275-6CrossRef Google Scholar

Bönigk, W., Altenhofen, W., Muller, F., Dose, A., Illing, M., Molday, R. S. & Kaupp, U. B. (1993) Rod and cone photoreceptor cells express distinct genes for cyclic GMP-gated channels. Neuron 10: 865–77. [aRSM]10.1016/0896-6273(93)90202-3CrossRef Google Scholar

Bornancin, F., Pfister, C. & Chabre, M. (1989) The transitory complex between photoexcited rhodopsin and transducin: Reciprocal interaction between the retinal site in rhodopsin and the nucleotide site in transducin. European Journal of Biochemistry 184: 687–98. [aPAH]10.1111/j.1432-1033.1989.tb15068.xCrossRef Google Scholar PubMed

Bourne, H. R. & Nicoll, R. (1993a) Molecular machines integrate coincident synaptic signals. Cell 72: 65–75. [aZX]10.1016/S0092-8674(05)80029-7CrossRef Google Scholar PubMed

Bourne, H. R. & Nicoll, R. (1993b) Molecular machines integrate coincident synaptic signals. Neuron 10(Suppl.):65–75. [TWA]Google Scholar

Bourne, H. R., Sanders, D. A. & McCormick, F. (1990) The GTPase superfamily: A conserved switch for diverse cell functions. Nature 348: 125–32. [aMDB]10.1038/348125a0CrossRef Google Scholar PubMed

Bourne, H. R., Sanders, D. A. & McCormick, F. (1991) The GTPase superfamily: Conserved structure and molecular mechanism. Nature 349: 117–27. [aMDB]10.1038/349117a0CrossRef Google Scholar PubMed

Bowes, C., Li, T., Danciger, M., Baxter, L. C, Applebury, M. L & Farber, D. B. (1990) Retinal degeneration in the rd mouse is caused by a defect in the β subunit of rod cGMP-phosphodiesterase. Nature 347: 677–80. [aSPD, MWK]10.1038/347677a0CrossRef Google Scholar PubMed

Bowes, C., Li, T., Frankel, W. N., Danciger, M., Coffin, J. M., Applebury, M. L. & Farber, D. B. (1993) Localization of a retroviral element within the rd gene coding for the beta subunit of cGMP phosphodiesterase. Proceedings of the National Academy of Sciences USA 90: 2955–59. [aSPD]10.1073/pnas.90.7.2955CrossRef Google Scholar PubMed

Bowie, J. U., Lüthy, R. & Eisenberg, D. (1991) A method to identify protein sequences that fold into a known three-dimensional structure. Science 253: 164–70. [RMC]10.1126/science.1853201CrossRef Google Scholar PubMed

Bownds, D., Dawes, J., Miller, J. & Stahlman, M. (1972) Phosphorylation of frog photoreceptor membranes induced by light. Nature New Biology 237: 125–27. [aMDB]10.1038/newbio237125a0CrossRef Google Scholar

Bownds, M. D., Arshavsky, V. Y., Calvert, P. D. & Dumke, C. I. (1992) Rod outer segment concentration and structure influence the apparent kinetics of cGMP phosphodiesterase. Investigative Ophthalmology and Visual Science 33: 873. [aMDB]Google Scholar

Bownds, M. D. & Thomson, D. (1988) Control of the sensitivity and kinetics of the vertebrate photoresponse during light adaptation—calculations from simple molecular models. In: Molecular physiology of retinal proteins, ed. Hara, T.. Osaka: Japan Scientific Society Press. [aMDB]Google Scholar

Bradley, J., Li, J., Davidson, N., Lester, H. A. & Zinn, K. (1994) Heteromeric olfactory cyclic nucleotide-gated channels: A subunit that confers increased sensitivity to cAMP. Proceedings of the National Academy of Sciences USA 91: 8890–94. [rRSM]10.1073/pnas.91.19.8890CrossRef Google Scholar

Brann, M. R. & Cohen, L. V. (1987) Diurnal expression of tranducin mRNA and translocation of transducin in rods of rat retina. Science 235: 585–88. [JFM]10.1126/science.3101175CrossRef Google Scholar

Breer, H. & Boekhoff, I. (1992) Second messenger signalling in olfaction. Current Opinion in Neurobiology 2: 439–43. [aMDB]10.1016/0959-4388(92)90177-MCrossRef Google Scholar PubMed

Bressler, N. M., Bressler, S. B. & Fine, S. L. (1988) Age-related macular degeneration. Survey of Ophthalmology 32: 375–413. [aSPD]10.1016/0039-6257(88)90052-5CrossRef Google Scholar PubMed

Brown, N. G., Fowles, C., Sharma, R. & Akhtar, M. (1993) Quantitative characterization of the structure of rhodopsin in disc membrane by means of Fourier transform infrared spectroscopy. Journal of Biological Chemistry 268: 2403–9. [ADA]Google Scholar

Brown, R. L., Bert, R. J., Evans, F. E. & Karpen, J. W. (1993) Activation of retinal rod cGMP-gated channels: What makes for an effective 8-snbstitutecl derivative of cGMP? Biochemistry 32: 10089–95. [RLB]10.1021/bi00089a026CrossRef Google Scholar PubMed

Brown, R. L., Cerber, W. V. & Karpen, J. W. (1993) Specific labeling and permanent activation of the retinal rod cGMP-activated channel by the photaffinity analog 8-p-azidophcnacylthio-cGMP. Proceedings of the National Academy of Sciences USA 90: 5369–73. [aRSM, RLB]10.1073/pnas.90.11.5369CrossRef Google Scholar

Brown, R. L., Cramling, R., Bert, R. J. & Karpen, J. W. (in press) Cyclic GMP contact points within the 63-kDa subunit and a 240-kDa associated protein of retinal rod cGMP-activated channels. Biochemistry. [RLB]Google Scholar

Brown, R. L. & Karpen, J. W. (1994) Dissecting the activation mechanism of retinal rod cGMP-gated channels using covalently tethered ligands. Biophysics Journal 66: A350. [RLB, TGW]Google Scholar

Buczylko, J., Gutmann, C. & Palezewski, K. (1991) Regulation of rhodopsin kinase by autophosphorylation. Proceedings of the National Academy of Sciences USA 88: 2568–72. [aMDB]10.1073/pnas.88.6.2568CrossRef Google Scholar PubMed

Bunge, S., Wedemann, H., David, D., Terwilliger, D. J., Van Den Bom, L. I., Aulehla-Scholz, C., Sammons, C., Horn, M., Ott, J., Schwinger, E., Schinzel, A., Denton, M. J. & Gal, A. (1993) Molecular analysis and genetic mapping of the retinitis pigmentosa gene in families with autosomal dominant retinitis pigmentosa. Genomics 17: 230–33. [aSPD]10.1006/geno.1993.1309CrossRef Google Scholar PubMed

Burks, C., Cinkosky, M. J., Fischer, W. M., Gilna, P., Hayden, J. E.-D., Keen, G. M., Kelly, M., Kristofferson, D. & Lawrence, J. (1992) GenBank. Nucleic Acids Research 20: 2065–69. [aSPD]10.1093/nar/20.suppl.2065CrossRef Google Scholar PubMed

Byrne, J. H. (1987) Presynaptic facilitation as a mechanism for behavioral sensitization in Aplysia. Physiology Review 67: 329–439. [aZX]10.1152/physrev.1987.67.2.329CrossRef Google Scholar

Cali, J. F., Zwaagstra, J. C., Mons, N., Cooper, D. M. F. & Krupinski, J. (1994) Type VIII adenylyl cyclase. Journal of Biological Chemistry 269: 12190–95. [aZX]10.1016/S0021-9258(17)32700-XCrossRef Google Scholar PubMed

Campbell, J. W., Duee, E., Hodgson, G., Mercer, W. D., Stammers, D. K., Wendell, P. L., Muirhead, H. & Watson, H. C. (1971) X-ray diffraction studies on enzymes in the glycolytic pathway. Cold Spring Harbor Symposium on Quantitative Biology 36: 165–70. [aPAH]10.1101/SQB.1972.036.01.023CrossRef Google Scholar

Caretta, A. & Cavaggioni, A. (1983) Fast ionic flux activated by cyclic GMP in the membrane of cattle rod outer segments. European Journal of Biochemistry 132: 1–8. [TGW]10.1111/j.1432-1033.1983.tb07317.xCrossRef Google Scholar PubMed

Caretta, A., Cavaggioni, A., Grimaldi, R. & Sorbi, R. (1988) Regulation of cyclic GMP binding to retinal rod membranes by calcium. European Journal of Biochemistry 177: 139–46. [aRSM]10.1111/j.1432-1033.1988.tb14354.xCrossRef Google Scholar PubMed

Caretta, A., Cavaggioni, A. & Sorbi, R. T. (1979) Cyclic GMP and the permeability of the disks of the frog photoreceptors. Journal of Physiology 295: 171–78. [TGW]10.1113/jphysiol.1979.sp012959CrossRef Google Scholar PubMed

Castellucci, V. F., Blumenfeld, H., Goelet, P. & Kandel, E. R. (1989) Inhibitor of protein synthesis blocks long-term behavioral sensitization in the isolated gill-withdrawal reflex of Aplysia. Journal of Neurobiology 20: 1–9. [aZX]10.1002/neu.480200102CrossRef Google Scholar PubMed

Castellucci, V. F. & Kandel, E. R.(1976) Presynaptic facilitation as a mechanism for behavioral sensitization in Aplysia. Science 194: 1176–78. [aZX]10.1126/science.11560CrossRef Google Scholar PubMed

Cavaggioni, A. & Sorbi, R. T. (1981) Cyelie GMP releases calcium from disc membranes of vertebrate photoreceptors. Proceedings of the National Academy of Science USA 78: 3964–68. [TGW]10.1073/pnas.78.6.3964CrossRef Google Scholar PubMed

Caviness, V. S. Jr, So, D. K. & Sidman, R. L. (1972) The hybrid reeler mouse. Journal of Heredity 63: 341–46. [DW]10.1093/oxfordjournals.jhered.a108286CrossRef Google Scholar PubMed

Cervetto, L., Torre, V., Pasino, E., Marroni, P. & Capovilla, M. (1984) Recovery from light-desensitization in toad rods. In: Photoreceptors, ed. Borcellino, A. & Cervetto, L.. Plenum. [arMDB]Google Scholar

Chabre, M. (1985) Molecular mechanism of visual phototransduction in retinal rod cells. Annual Review of Biophysics and Biophysical Chemistry 14: 331–60. [aPAH]Google Scholar

Chabre, M. & Deterre, P. (1989) Molecular mechanism of visual transduction. European Journal of Biochemistry 179: 255–66. [aMDB, aPAH, aRSM]10.1111/j.1432-1033.1989.tb14549.xCrossRef Google Scholar PubMed

Chakraborty, R. (1993) Generalized occupancy problem and its applications in population genetics. In: Genetics of cellular, individual, family, and population variability, ed. Sing, C. F. & Hanis, C. L.. Oxford University Press. [aSPD]Google Scholar

Chang, B., Heckenlively, J. R., Hawes, N. L. & Roderick, T. H. (1993) New mouse primary retinal degeneration (rd-3). Genomics 16: 45–49. [MWK]10.1006/geno.1993.1138CrossRef Google Scholar

Chang, G.-Q., Hao, Y. & Wong, F. (1993) Apoptosis: Final common pathway of photoreceptor death in rd, rds, and rhodopsin mutant mice. Neuron 11: 595–605. [aSPD, MT]10.1016/0896-6273(93)90072-YCrossRef Google Scholar PubMed

Charbonneau, H., Prusti, R. K., LeTrong, , Sonnenburg, W. K., Mullancy, P. J., Walsh, K. A. & Beavo, J. A. (1990) Identification of a noncatalytic cGMP-binding domain conserved in both the cGMP-stimulated and photoreceptor cyclic nucleotide phosphodiesterase. Proceedings of the National Academy of Sciences USA 87: 288–92. [aMDB]10.1073/pnas.87.1.288CrossRef Google Scholar

Chen, C.-K. & Hurley, J. B. (1994) Calcium-dependent recoverin/rhodopsin kinase interaction. Investigative Ophthalmology and Visual Science 35: 1485. [aMDB, aJBH, AY]Google Scholar

Chen, S., Fry, C. H., Illner, H., Kickenweiz, E., McGuigan, J. A. S., Powell, T. & Twist, V. W. (1992) Measurement of intracellular free magnesium in isolated guinea-pig papillary muscles and ventricular myocytes. Journal of Physiology (London) 452: 194 p.[RLH]Google Scholar

Chen, T. -Y, Illing, M., Molday, L. L., Hsu, T.-T, Yau, K.-W. & Molday, R. S. (1994) subunit 2 (or β) of retinal rod cGMP-gated cation channel is a component of the 240-kDa channel-associated protein and mediates Ca2+-ealmodulin modulation. Proceedings of the National Academy of Sciences USA 91: 11757–61. [rRSM, RLB, DDO]10.1073/pnas.91.24.11757CrossRef Google Scholar PubMed

Chen, T.-Y, Peng, Y.-W, Dhallan, R. S., Ahamed, B., Reed, R. R. & Yau, K.-W. (1993) A new subunit of the cyclic nucleotide-gated cation channel in retinal rods. Nature 362: 764–67. [arRSM, RLB, LWH, RLH, DDO]10.1038/362764a0CrossRef Google Scholar PubMed

Chen, T.-Y. & Yau, K.-W. (1994) Direct modulation by Ca-calmodulin of cyclic nucleotide-activated channel of rat olfactory receptor neurons. Nature 368: 545–48. [rRSM]10.1038/368545a0CrossRef Google Scholar

Chetkovich, D. M., Gray, R., Johnston, D. & Sweatt, J. D. (1991) N-methyl- D-aspartate receptor activation increases cAMP levels and voltage gated Ca2+ channel activity in area CA1 of hippocampus. Proceedings of the National Academy of Sciences USA 88: 6467–71. [aZX, EDR]10.1073/pnas.88.15.6467CrossRef Google Scholar PubMed

Chevkovich, D. M. & Sweatt, J. D. (1993) NMDA receptor activation increases cyclic AMP in area CA1 of the hippocampus via calcium/calmodulin stimulation of adenylyl cyclase. Journal of Neurochemistry 61: 1933–42. [aZX, EDR]10.1111/j.1471-4159.1993.tb09836.xCrossRef Google Scholar

Cheung, W. Y. & Storm, D. R. (1982) Calmodulin regulation of cAMP metabolism. Handbook of Experimental Pharmacology 58: 301–17. [aZX]10.1007/978-3-642-68111-0_7CrossRef Google Scholar

Choi, E. J., Wong, S. T, Dittman, A. H. & Storm, D. R. (1993). Phorbol ester stimulation of the type I & type III adenylyl cyclases in whole cells. Biochemistry 32: 1891–94. [aZX]10.1021/bi00059a001CrossRef Google Scholar PubMed

Choi, E. J., Wong, S. T., Hinds, T. J. & Storm, D. R. (1992a) Calcium and muscarinic agonist stimulation of type I adenylyl cyclase in whole cells. Journal of Biological Chemistry 267: 12440–42. [aZX]10.1016/S0021-9258(18)42296-XCrossRef Google Scholar PubMed

Choi, E. J., Xia, Z. & Storm, D. R. (1992b) Stimulation of the type III olfactory adenylyl cyclase by calcium and calmodulin. Biochemistry 31: 6492–98. [arZX]10.1021/bi00143a019CrossRef Google Scholar PubMed

Cimler, B. M., Andreasen, T. J., Andreasen, K. I. & Storm, D. R. (1985) P–57 is a neural specific calmodulin-binding protein. Journal of Biological Chemistry 260: 10784–88. [aZX]10.1016/S0021-9258(19)85150-5CrossRef Google Scholar PubMed

Clack, J. W. & Pepperberg, D. R. (1982) Desensitization of skate photoreceptor by bleaching and background light. Journal of General Physiology 80: 863–83. [aMDB]10.1085/jgp.80.6.863CrossRef Google Scholar PubMed

Clack, J. W. & Stein, P. J. (1988) Opsin exhibits cCMP-activated single channel activity. Proceedings of the National Academy of Sciences USA 85: 9806–10. [aRSM]10.1073/pnas.85.24.9806CrossRef Google Scholar PubMed

Clore, G. M. & Gronenborn, A. M. (1994a) Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR: Young investigator award lecture. Protein Science 3: 372–90. [RKC]10.1002/pro.5560030302CrossRef Google Scholar PubMed

Clore, G. M. & Gronenborn, A. M. (1994b) Structures of larger proteins, protein-ligand and protein-DNA complexes by multidimensional heteronuclear NMR. Protein Science 3: 372–90. [rPAH]10.1002/pro.5560030302CrossRef Google Scholar PubMed

Coleman, D. L. (1981) Inherited obesity-diabetes syndromes in the mouse. In: Mammalian genetics and cancer. Liss. [DW]Google Scholar

Coles, J. A. & Yamane, S. (1975) Effects of adapting lights on the time course of the receptor potential of the anuran retinal rod. Journal of Physiology (London) 247: 189–207. [arMDB]10.1113/jphysiol.1975.sp010927CrossRef Google Scholar PubMed

Collingridge, G. (1987) Synaptic plasticity: The role of NMDA receptors in learning and memory. Nature 330: 604–5. [TWA]10.1038/330604a0CrossRef Google Scholar PubMed

Cone, R. A. (1972) Rotational diffusion of rhodopsin in the visual receptor membrane. Nature New Biology 236: 39–43. [aPAH]10.1038/newbio236039a0CrossRef Google Scholar PubMed

Connell, G., Bascom, R., Molday, L., Reid, D., Mclnnes, R. R. & Molday, R. S. (1991) Photoreceptor peripherin is the normal product of the gene responsible for retinal degeneration in the rds mouse. Proceedings of the National Academy of Sciences USA 38: 723–36. [aSPD, MWK]10.1073/pnas.88.3.723CrossRef Google Scholar

Cook, N. J., Hanke, W. & Kaupp, U. B. (1987) Identification, purification and functional reconstitution of the cyclic GMP-dependent channel from rod photoreceptors. Proceedings of the National Academy of Sciences USA 84: 585–89. [aRSM, RLB, RLH, TGW]10.1073/pnas.84.2.585CrossRef Google Scholar PubMed

Cook, N. J., Molday, L. L., Reid, D., Kaupp, U. B. & Molday, R. S. (1989) The cGMP- gated channel of bovine rod phororeceptors is localized exclusively in the plasma membrane. Journal of Biological Chemistry 264: 6996–99. [aRSM, RLH, TGW]10.1016/S0021-9258(18)83530-XCrossRef Google Scholar

Corless, J. M., McCaslin, D. R. & Scott, B. L. (1982) Two-dimensional rhodopsin crystals from disk membranes of frog retinal rod outer segments. Proceedings of the National Academy of Sciences USA 79:1116–20. [aPAH EAD]10.1073/pnas.79.4.1116CrossRef Google Scholar PubMed

Cornwall, M. C. & Fain, G. L. (1992) Bleaching of rhodopsin in isolated rods causes a sustained activation of PDE and cyclase which is reversed by pigment regeneration. Investigative Ophthalmology and Visual Science 33: 1103. [aMDB]Google Scholar

Cornwall, M. C. & Fain, G. L. (1994) Bleached pigment activates transduction in isolated rods of the salamander retina. Journal of Physiology (London) 480: 261–279. [rMDB]10.1113/jphysiol.1994.sp020358CrossRef Google Scholar PubMed

Cornwall, M. C. & Fain, G. L. (1994) Bleached pigment activates transduction in isolated rods of the salamander retina. Journal of Physiology 480: 261–79. [RKC]10.1113/jphysiol.1994.sp020358CrossRef Google Scholar PubMed

Cornwall, M. C. & Pan, W.-Z. (1985). Spatial resolution of bleaching and background adaptation in rod photoreceptors of Ambystoma tigrinum. In: The visual system, ed. Fein, A. & Levine, J.. Liss, Alan R.. [RKC]Google Scholar

Cornwall, M. C, Fein, A. & MacNichol, E. F. (1990) Cellular mechanisms that underlie bleaching and background adaptation. Journal of General Physiology 96: 345–72. [RKC]10.1085/jgp.96.2.345CrossRef Google Scholar PubMed

Cornwall, M. C, Fein, A. & MacNichol, E. F. (1983) Spatial localization of bleaching adaptation in isolated vertebrate rod photoreceptors. Proceedings of the National Academy of Sciences USA 80: 2785–88. [RKC]10.1073/pnas.80.9.2785CrossRef Google Scholar PubMed

Corson, D. W., Cornwall, M. C, MaeNichol, E. F., Jin, J., Johnson, R., Derguini, F., Crouch, R. K. & Nakanishi, K. (1990) Sensitization of bleached rod photoreceptors by 11-cis-locked analogues of retinal. Proceedings of the National Academy of Sciences USA 87: 6823–27. [RKC]10.1073/pnas.87.17.6823CrossRef Google Scholar PubMed

Corson, D. W., Cornwall, M. C, MaeNichol, E. F., Tsang, S., Derguini, F., Crouch, R. K. & Nakanishi, K. (1994a) Relief of opsin desensitization and prolonged excitation of rod photoreceptors by 9-desmethyl retinal. Proceedings of the National Academy of Sciences USA 91: 6952–58. [RKC]10.1073/pnas.91.15.6958CrossRef Google Scholar

Corson, D. W., Cornwall, M. C. & Pepperberg, D. R. (1994b) Evidence for the prolonged photoactivated lifetime of an analogue visual pigment containing 11-cis 9-desmethylretinal. Visual Neuroscience 11: 91–98. [RKC]10.1017/S0952523800011135CrossRef Google Scholar PubMed

Cote, R. H. & Brunnock, M. A. (1993) Intracellular cGMP concentration in rod photoreceptors is regulated by binding to high and moderate affinity cGMP binding sites. Journal of Biological Chemistry 268: 17190– 98. [aMDB]10.1016/S0021-9258(19)85321-8CrossRef Google Scholar PubMed

Cote, R. H., Bownds, M. D. & Arshavsky, V. Y. (1994) cGMP binding sites on photoreceptor phosphodiesterase: Role in feedback regulation of visual transduction. Proceedings of the National Academy of Sciences USA 91: 4845–49. [arMDB, BMW]10.1073/pnas.91.11.4845CrossRef Google Scholar PubMed

Creuzet, F., McDermott, A., Gebhard, R., van der Hoef, K., Spijker-Assink, M., Herzfeld, J., Lugtenburg, J., Levitt, M. H. & Griffin, R. G. (1991) Determination of membrane protein structure by rotational resonance NMR: Bacteriorhodopsin. Science 251: 783–86. [SOS]10.1126/science.1990439CrossRef Google Scholar PubMed

Davis, S., Butcher, S. P. & Morris, R. G. (1992) The NMDA receptor antagonist D-2-amino-5-phosphonopentanoate (D-AP5) impairs spatiallearning and LTP in vivo at intracerebral concentrations comparable to those that block LTP in vitro. Journal of Neuroscience 12: 21–34. [aZX, TWA]10.1523/JNEUROSCI.12-01-00021.1992CrossRef Google Scholar

Dawis, S. M. (1991) A molecular basis for Weber's law. Visual Neuroscience 7: 285–320. [aMDB]10.1017/S0952523800004806CrossRef Google Scholar PubMed

Dawis, S. M., Graeff, R. M., Heyman, R. A., Walseth, T. F. & Goldberg, N. D. (1988) Regulation of cyclic GMP metabolism in toad photoreceptors. Journal of Biological Chemistry 263: 8771–85. [arMDB]10.1016/S0021-9258(18)68373-5CrossRef Google Scholar PubMed

de Crip, W. J. (1982a) Purification of bovine rhodopsin over concanavalin A-sepharose. Methods in Enzymology 81: 197–207. [aPAH]10.1016/S0076-6879(82)81032-XCrossRef Google Scholar

de Crip, W. J. (1982b) Thermal stability of rhodopsin and opsin in some novel detergents. Methods in Enzymology 81: 256–65. [aPAH]10.1016/S0076-6879(82)81040-9CrossRef Google Scholar

de Grip, W. J., Olive, J. & Bovee-Geurts, P. H. M. (1983) Reversible modulation of rhodopsin photolysis in pure phosphatidylserine membranes. Biochimica et Biophysica Ada 734: 168–79. [aPAH]10.1016/0005-2736(83)90115-3CrossRef Google Scholar

de Grip, W. J., van Oostrum, J., Bovee-Geurts, P. H. M., van der Steen, R., van Amsterdam, L. J. P., Groesbeek, M. & Lugtenburg, J. (1990) 10,20-methanorhodopsins: (7E.9E, 13E)- 10,20, methanorhodopsin and (7E.9Z, 13Z)-10,20-methanorhodopsin: 11-cis-locked rhodopsin analog pigments with unusual thermal and photo-stability. European Journal of Biochemistry 191: 211–20. [aPAH]10.1111/j.1432-1033.1990.tb19112.xCrossRef Google Scholar

de Grip, W. J., van Oostrum, J. & De Caluw, C. L. J. (1992) Studies towards the crystallization of the rod visual pigment rhodopsin. Journal of Crystal Growth 122: 375–84. [aPAH]10.1016/0022-0248(92)90272-KCrossRef Google Scholar

Deese, A. J., Dratz, E. A., Dahlquist, F. W. & Paddy, M. R. (1981) Interaction of rhodopsin with two unsaturated phosphatidylcholines: A deuterium nuclear magnetic resonance study. Biochemistry 20: 6420–27. [aPAH]10.1021/bi00525a021CrossRef Google Scholar PubMed

Deisenhofer, J. & Michel, H. (1989) The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis . Science 245: 1463–73. [aPAH]10.1126/science.245.4925.1463CrossRef Google Scholar PubMed

Demin, V. V., Yurkova, E. V., Kuzin, A. P., Barnakov, A. N. & Abdulaev, N. G. (1987). Crystallization of bovine retinal rhodopsin. In: Retinal proteins. VNU Science Press. [aPAH]Google Scholar

Dencher, N. A., Dresselhaus, D., Zaccai, G. & Boldt, G. (1989) Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction. Proceedings of the National Academy of Sciences USA 86: 7876–79. [aPAH]10.1073/pnas.86.20.7876CrossRef Google Scholar PubMed

Derguini, F. & Nakanishi, K. (1986) Synthetic rhodopsin analogs. Photobiochemistry & Photobiophysics 13: 259–83. [aPAH]Google Scholar

Deterre, P., Bigay, J., Forguet, F., Robert, M. & Chabre, M. (1988) cGMP of phosphodiesterase of retinal rods is regulated by two inhibitory subunits. Proceedings of the National Academy of Sciences USA 85: 2424–28. [aMDB]10.1073/pnas.85.8.2424CrossRef Google Scholar PubMed

Detwiler, P. B. & Gray-Keller, M. P. (1992) Some unresolved issues in the physiology and biochemistry of phototransduction. Current Opinion in Neurobiology 2: 433–38. [aMDB]10.1016/0959-4388(92)90176-LCrossRef Google Scholar PubMed

Dhallan, R. S., Macke, J. P., Eddy, R. L., Shows, T. B., Reed, R. R., Yau, K. W. & Nathans, J. (1992) Human rod photoreceptor cGMP-gated channel: Amino acid sequence, gene structure, and functional expression. Journal of Neuroscience 12: 3248–56. [aRSM]10.1523/JNEUROSCI.12-08-03248.1992CrossRef Google Scholar PubMed

Dhallan, R. S., Yau, K. W, Schrader, K. A. & Reed, R. R. (1990) Primary structure and functional expression of a cyclic nucleotide-activated channel from olfactory neurons. Nature 347: 184–87. [aRSM]10.1038/347184a0CrossRef Google Scholar PubMed

Dittman, A. H., Weber, J. P., Hinds, T. R., Choi, E. J., Migeon, J. C., Nathanson, N. M. & Storm, D. R. (1994) A novel mechanism for coupling of m4 muscarinic acetylcholine receptors to calmodulin-sensitive adenylyl cyclases: Cross-over from G protein coupled inhibition to stimulation. Biochemistry 33: 943–51. [aZX]10.1021/bi00170a013CrossRef Google Scholar

Dizhoor, A. M., Chen, C.-K., Olshevskaya, E., Sinelnikova, V. V., Philipov, P. & Hurley, J. B. (1993) Role of the acylated amino terminus of recoverin in Ca+2-dcpendcnt membrane iuteraction. Science 259: 829–32. [aJBH, SK]10.1126/science.8430337CrossRef Google Scholar

Dizhnor, A. M., Ericsson, L. H., Johnson, R. S., Kumar, S., Olshevakaya, E., Zozulya, S., Neubert, T. A., Stryer, L., Hurley, J. B. & Walsh, K. A. (1992) The NH2 terminus of retinal recoverin is acylated by a small family of fatty acids. Journal of Biological Chemistry 267: 16033–36. [aJBH, KS]10.1016/S0021-9258(18)41959-XCrossRef Google Scholar

Dizhoor, A. M., Lowe, D. C, Olshevskaya, E. V., Laura, R. P. & Hurley, J. B. (1994) The human photorcceptor membrane guanylyl cyclase, RetGC, is present in outer segments and is regulated by calcium and a soluble activator. Neuron 12: 1345–52. [aMDB]10.1016/0896-6273(94)90449-9CrossRef Google Scholar

Dizhoor, A. M., Ray, S., Kumar, S., Niemi, C., Spencer, M., Brolley, D., Walsh, K. A., Philipov, P. P., Hurley, J. B. & Stryer, L. (1991) Recoverin: A calcium sensitive activator of retinal rod guanylate cyclase. Science 251: 915–18. [aMDB, aJBH, SK, JFM, ASP]10.1126/science.1672047CrossRef Google Scholar PubMed

Dorset, D. L., Engel, A., Honor, M., Massalski, A. & Rosenbusch, J. P. (1983) Two-dimensional crystal packing of matrix porin. Journal of Molecular Biology 165: 701–10. [aPAH]10.1016/S0022-2836(83)80275-7CrossRef Google Scholar PubMed

Downer, N. W. (1985) Cross-linking of dark-adapted frog photoreceptor disk membranes: Evidence for monomeric rhodopsin. Biophysical Journal 47: 285–93. [aPAH]10.1016/S0006-3495(85)83918-7CrossRef Google Scholar PubMed

Dratz, E. A., Furstenau, J., Hamm, H. E. & Hargrave, P. A. (1990) Probing the molecular mechanism of visual excitation using bioactive peptide sequences. Investigative Ophthalmology and Visual Science 31: 79. [EAD]Google Scholar

Dratz, E. A., Furstenau, J., Lambert, C. G., Thireault, D. L., Rarick, H., Schepers, T., Pakhlevaniants, S. & Hamm, H. E. (1993) NMR structure of a receptor-bound G-protein peptide. Nature 363: 276–81. [EAD]10.1038/363276a0CrossRef Google Scholar PubMed

Dratz, E. A., Hamm, H. E., Zwolinski, R., Furstenau, J. & Lambert, C. (1991) The 3D structure of the active interface between rhodopsin and G-protein determined using 2D NMR. Biophysical Journal 59:189a. [EAD]Google Scholar

Dratz, E. A. & Hargrave, P. A. (1983) The structure of rhodopsin and the rod outer segment disk membrane. Trends in Biochemical Sciences 8: 128–31. [aPAH, EAD]10.1016/0968-0004(83)90235-9CrossRef Google Scholar

Dratz, E. A., Lewis, J. W., Schaechter, L. E., Parker, K. R. & Kliger, D. S. (1987) Retinal rod GTPase turnover rate increases with concentration: A key to the control of visual excitation? Biochemical and Biophysical Research Communications 146: 379–86. [aMDB]10.1016/0006-291X(87)90540-7CrossRef Google Scholar

Dratz, E. A., VanBreeinen, J. F. L., Kamps, K. M. P., Keegstra, W. & VanBruggon, E. F. J. (1985) Two-dimensional crystallization of bovine rhodopsin. Biochimica ct Biophysica Acta 832:337–42. [aPAH, EAD]10.1016/0167-4838(85)90268-7CrossRef Google Scholar PubMed

Dryer, S. E. & Henderson, D. (1991) A cyclic GMP-activated channel in dissociated cells of the chick pineal gland. Nature 353: 756–58. [aRSM]10.1038/353756a0CrossRef Google Scholar PubMed

Dryja, T. P. (1992) Doyne lecture: Rhodopsin and autosomal dominant retinitis pigmentosa. Eye 6: 1–10. [aPAH, aSPD]10.1038/eye.1992.2CrossRef Google Scholar PubMed

Dryja, T. P., Berson, E. L., Rao, V. & Oprian, D. D. (1993) Heterozygous missense mutation in the rhodopsin gene as the cause of congenital stationary night blindness. Nature Genetics 4:280–83. [aSPD]10.1038/ng0793-280CrossRef Google Scholar PubMed

Dryja, T. P., Hahn, L. B., McGee, T. L., Cowley, G. S. & Berson, E. L.(1991) Mutation spectrum of the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa. Proceedings of the National Academy of Sciences USA 88: 9370–74. [aSPD]10.1073/pnas.88.20.9370CrossRef Google Scholar PubMed

Dryja, T. P., McGee, T. I., Hahn, L. B., Cowley, G. S., Olsson, J. E., Keichel, E., Sandberg, M. A. & Berson, E. L. (1990) Mutations within the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa. New England Journal of Medicine 323: 1302–7. [aSPD]10.1056/NEJM199011083231903CrossRef Google Scholar PubMed

Dryja, T. P., McGee, T. I., Reichel, E., Hahn, L. B., Cowley, G. S., Yandell, D. W., Sandberg, M. A. & Berson, E. L. (1990a) A point mutation of the rhodopsin gene in one form of retinitis pigmentosa. Nature 343(6256):364–66. [aSPD]10.1038/343364a0CrossRef Google Scholar PubMed

Duclai, V. (1988) Neurogenetic dissection of learning and short-term memory in Drosophila. Annual Review of Neuroscience 11: 537–63. [aZX]Google Scholar

Dudai, Y. & Zvi, S. (1984) Adenylate cyclase in the Drosophila memory mutant rutabaga displays an altered Ca2+ sensitivity. Neuroscience Letters 47: 19–24. [aZX, TWA]10.1016/0304-3940(84)90416-6CrossRef Google Scholar PubMed

Dudai, Y. & Zvi, S. (1985) Multiple defects in the activity of adenylyl cyclase from the Drosophila memory mutant rutabaga. Journal of Neurochemistry 45: 355–64. [aZX]10.1111/j.1471-4159.1985.tb03996.xCrossRef Google Scholar PubMed

Dumke, C. L., Arshavsky, V. Y., Calvert, P. D., Pugh, E. N. & Bownds, M. D. (1994) Rod outer segment structure influences the apparent kinetic parameters of cGMP phosphodiesterase. Journal of General Physiology 103: 1071–98. [aMDB]10.1085/jgp.103.6.1071CrossRef Google Scholar

Durell, S. R. & Guy, R. (1992) Atomic scale structure and functional models of voltage-gated potassium channels. Biophysics Journal 62: 238–50. [aRSM]10.1016/S0006-3495(92)81809-XCrossRef Google Scholar PubMed

Eisman, E., Bönigk, W. & Kaupp, U. B. (1993) Structural features of cyclic nucleotide-gated channels. In: Cellular physiology and biochemistry, ed. Lang, F.. Karger, S. AC. [rRSM]Google Scholar

Eismann, E., Müller, F., Heinemann, S. H. & Kaupp, U. B. (1994) A single negative charge within the pore region of a cGMP-gated channel controls rectification, Ca2+ blockage and ionic selectivity. Proceedings of the National Academy of Sciences USA 91: 1109–13. [rRSM]10.1073/pnas.91.3.1109CrossRef Google Scholar PubMed

Erickson, M. A., Robinson, P. & Lisman, J. (1992) Deactivation of visual transduction without guanosine triphosphate hydrolysis by G protein. Science 257: 1255–58. [aMDB, AY]10.1126/science.1519062CrossRef Google Scholar PubMed

Fahmy, K. & Sakmar, T. P. (1993) Regulation of rhodopsin-transducin interaction by a highly conserved carboxylic acid group. Biochemistry 32: 7229–36. [aSPD]10.1021/bi00079a020CrossRef Google Scholar PubMed

Fain, G. L. (1976) Sensitivity of toad rods: Dependence on wavelength and background illumination. Journal of Physiology (London) 261:71–101. [aMDB]10.1113/jphysiol.1976.sp011549CrossRef Google Scholar

Fain, G. L. & Cornwall, M. C. (1993) Light and dark adaptation in vertebrate photoreceptors. In: Contrast Sensitivity from receptors to clinic, ed. Shapley, R. & Lam, D.-K.. MIT Press. [RKC]Google Scholar

Fain, G. L., Lamb, T. D., Matthews, H. R. & Murphy, R. L. W. (1989) Cytoplasmic calcium concentration as the messenger for light adaptation in salamander rods. Journal of Physiology 416: 215–43. [HRM]10.1113/jphysiol.1989.sp017757CrossRef Google Scholar PubMed

Fain, G. L. & Lisman, J. E. (1993) Photoreceptor degeneration in vitamin A deprivation and retinitis pigmentosa: The equivalent light hypothesis. Experimental Eye Research 57: 335–40. [aMDB]10.1006/exer.1993.1132CrossRef Google Scholar PubMed

Fain, G. L. & Matthews, H. R. (1990) Calcium and the mechanism of light adaptation in vertebrate photoreceptors. Trends in Neuroscience 13: 378– 84. [HRM]10.1016/0166-2236(90)90023-4CrossRef Google Scholar PubMed

Farber, D. B., Seager, , Danciger, J. & Aguirre, G. (1992) The β subunit of cyclic GMP phosphodiesterase mRNA is deficient in canine rod-cone dysplasia l. Neuron 9: 349–56. [MWK]10.1016/0896-6273(92)90173-BCrossRef Google Scholar

Famsworth, C. & Dratz, E. A. (1976) Oxidative damage of retinal rod outer segment membranes and the role of vitamin E. Biochimica et Biophysica Acta 443: 556–70. [aPAH]Google Scholar

Farrar, G. J., Findlay, J. B. C, Kumar-Singh, R., Kenna, P., Humphries, M. M., Sharpe, E. & Humphries, P. (1992) Autosomal dominant retinitis pigmentosa: A novel mutation in the rhodopsin gene in the original 3q linked family. Human Molecular Cenetics 1: 769–71. [aSPD]10.1093/hmg/1.9.769CrossRef Google Scholar PubMed

Farrar, G. J., Jordan, S. A., Kenna, P., Humphries, N. M., Kumar-Singh, R., McWilliams, P., Allamand, V., Sharp, E. & Humphries, P. (1991) Autosomal dominant retinitis pigmentosa: Localization of a disease gene (RP6) to the short arm of chromosome 6. Cenomics 11: 870–4. [aSPD]Google Scholar

Farrar, G. J., Kenna, P., Redmond, R., McWilliams, P., Bradley, D. G., Humphries, M. M., Sharp, E. M., Inglehearn, C. F., Bashir, R., Jay, M., Waytty, A., Ludwig, M., Schinzel, A., Samanns, C., Gal, A., Bhattacharya, S. & Humphries, P. (1990) Autosomal dominant retinitis pigmentosa: Absence of the rhodopsin proline—histidine substitution (codon 23) in pedigrees from Europe. American Journal of Human Genetics 47: 941–45. [aSPD]Google Scholar PubMed

Farrar, G. J., Kenna, P., Redmond, R., Shiels, D., McWilliams, P., Humphries, M. M., Sharp, E. M., Jordan, S., Kumar-Singh, R. & Humphries, P. (1991a) Autosomal dominant retinitis pigmentosa: A mutation in codon 178 of the rhodopsin gene in two families of Celtic origin. Cenomics 11: 1170–71. [aSPD]Google Scholar PubMed

Farrar, G. J., McWilliams, P., Bradley, D. G., Kenna, P., Lawler, M., Sharp, E. M., Humphries, N. M., Eiberg, H., Conneally, P. M., Trofatter, J. A. & Humphries, P.(1990) Autosomal dominant retinitis pigmentosa: Linkage to rhodopsin and evidence for genetic heterogeneity. Genomics 8:35–40. [aSPD]10.1016/0888-7543(90)90223-HCrossRef Google Scholar PubMed

Feany, M. B. (1990) Rescue of the learning defect in dunce, a Drosophila learning mutant, by an allele of rutabaga, a second learning mutant. Proceedings of the National Academy of Sciences USA 87: 2795–99. [aZX]10.1073/pnas.87.7.2795CrossRef Google Scholar PubMed

Federman, A. D., Conklin, B. R., Schrader, K. A., Reed, R. R., Bourne, H. R. (1992) Hormonal stimulation of adenylyl cyclase through G,-protein beta gamma subunits. Nature 356: 159–61.10.1038/356159a0CrossRef Google Scholar PubMed

Feher, G., Atten, J. P., Okamura, M. Y. & Rees, D. C. (1989) Structure and function of bacterial photosynthetic reaction centers. Nature 339: 111– 16. [aPAH]10.1038/339111a0CrossRef Google Scholar

Feinstein, P. G., Schrader, A., Bakalyar, H. A., Tang, W. J., Krupinski, J., Oilman, A. G. & Reed, R. R. (1991) Molecular cloning and characterization of a calcium calmodulin insensitive adenylyl cyclase (typell) from rat brain. Proceedings of the National Academy of Sciences USA 88: 10173– 77. [aZX]10.1073/pnas.88.22.10173CrossRef Google Scholar

Ferrell, R. E., Hittner, H. M. & Antoszyk, J. H. (1983) Linkage of atypical vitelliform macular dystrophy (GPT1) locus. American Journal of Human Genetics 35: 78–84. [aSPD]Google Scholar PubMed

Fesenko, E. E., Kolensnikov, S. S. & Lyubarsky, A. L. (1985) Induction by cyclic GMP of cationic conductance in plasma membrane of retinal rod outer segments. Nature 313: 310–13. [aRSM, DDO, TGW]10.1038/313310a0CrossRef Google Scholar

Findlay, J. B. C. (1986). The biosynthetic, functional, and evolutionary implications of the structure of rhodopsin. In: The molecular mechanismof photoreception. Springor-Verlag. [aPAH]Google Scholar

Firestein, S. (1991) A noseful of odor receptors. Trends in Neuroscience 14:270–72. [aMDB]10.1016/0166-2236(91)90135-HCrossRef Google Scholar PubMed

Fishman, G. A. (1990) Inherited macular dystrophies: A clinical overview. Australia and New Zealand Journal of Ophthalmology 18:123–28. [aSPD]Google Scholar PubMed

Fishman, G. A. (1978) Retinitis pigmentosa: Genetic percentages. Archives of Ophthalmology 96:822–26. [aSPD]10.1001/archopht.1978.03910050428005CrossRef Google Scholar PubMed

Fishman, G. A., Alexander, K. R. & Anderson, R. J. (1985) Autosomal dominant retinitis pigmentosa: A method of classification. Archives of Ophthalmology 103:366–74. [aSPD]10.1001/archopht.1985.01050030062023CrossRef Google Scholar PubMed

Fishman, G. A., Stone, E. M., Gilbert, L. D., Kenna, P. & Sheffield, V. C. (1991) Ocular findings associated with a rhodopsin gene codon 58 transversion mutation in autosomal dominant retinitis pigmentosa. Archives of Ophthalmology 109:1387–93. [aSPD]10.1001/archopht.1991.01080100067044CrossRef Google Scholar PubMed

Fishman, G. A., Stone, E. M., Gilbert, L. D. & Sheffield, V. C. (1992) Ocular findings associated with a rhodopsin gene codon 106 mutation glycine-to-arginine change in autosomal dominant retinitis pigmentosa. Archives of Ophthalmology 110:646–53. [aSPD]10.1001/archopht.1992.01080170068026CrossRef Google Scholar PubMed

Fishman, G. A., Stone, E. M., Sheffield, V. C., Gilbert, L. D. & Kimura, A. E. (1992a) Ocular findings associated with rhodopsin gene eodon 17 and codon 182 transition mutation in dominant retinitis pigmentosa. Archives of Ophthalmology 110:54–62. [aSPD]10.1001/archopht.1992.01080130056026CrossRef Google Scholar PubMed

Fishman, G. A., Vandenburgh, K., Stone, E. M., Gilbert, L. D., Alexander, K. R. & Sheffield, V. C. (1992b) Ocular findings associated with rhodopsin gene codon 267 and codon 190 mutations in dominant retinitispigmentosa. Archives of Ophthalmology 110:1582–88. [aSPD]10.1001/archopht.1992.01080230082026CrossRef Google Scholar

Flaherty, K. M., Zozulya, S., Stryer, L. & McKay, D. B. (1993) Three dimensional structure of recoverin, a calcium sensor in vision. Cell 75:709–16 [aMDB, aJBH, KWK]10.1016/0092-8674(93)90491-8CrossRef Google Scholar PubMed

Flieslcr, S. J. & Anderson, R. E. (1983) Chemistry and metabolism of lipids in the vertebrate retina. Progress in Lipid Research 22:79–131. [aMDB]10.1016/0163-7827(83)90004-8CrossRef Google Scholar

Fong, S.-L., Tsin, A. T. C., Bridges, C. D. B. & Lion, G. I. (1982) Detergents for extraction of visual pigments: Types, solubilization, and stability. Methods in Enzymology 81:133–40. [aPAH]10.1016/S0076-6879(82)81022-7CrossRef Google Scholar PubMed

Forti, S., Menini, A., Rispoli, G. & Torre, V. (1989) Kinetics of phototransduction in retinal rods of the newt Triturus cristatus . Journal of Physiology (London) 419:265–95. [aMDB]10.1113/jphysiol.1989.sp017873CrossRef Google Scholar PubMed

Fowles, C., Charma, R. & Akhtar, M. (1988) Mechanistic studies on the phosphorylation of photoexcited rhodopsin. FEBS Letters 238:56–60. [aMDB]10.1016/0014-5793(88)80224-2CrossRef Google Scholar PubMed

Franke, R. R., Konig, B., Sakmar, T. P., Khorana, H. G. & Hofmann, K. P. (1990) Rhodopsin mutants that bind but fail to activate transducin. Science 250:123–25. [aPAH, EAD]10.1126/science.2218504CrossRef Google Scholar PubMed

Franke, R. R., Sakmar, T. P., Graham, R. M. & Khorana, H. G. (1992) Structure and function in rhodopsin: Studies of the interaction between the rhodopsin cytoplasmic domain and transducin. Journal of Biological Chemistry 267:14767–74. [aPAH]10.1016/S0021-9258(18)42106-0CrossRef Google Scholar PubMed

Franke, R. R., Sakmar, T. P., Oprian, D. D. & Khorana, H. G. (1988) A single amino acid substitution in rhodopsin (Lysine 248 Leucine) prevents activation of transducin. Journal of Biological Chemistry 263:2119–22. [aSPD]10.1016/S0021-9258(18)69178-1CrossRef Google Scholar PubMed

Frey, U., Huang, Y. Y. & Kandel, E. R. (1993) Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons. Science 260:1661–64. [aZX, EDR]10.1126/science.8389057CrossRef Google Scholar PubMed

Frey, U., Krug, M., Reynumn, K. G. & Matthies, H. (1988) Anisomyein, an inhibitor of protein synthesis, blocks late phases of LTP phenomena in the hippocampal CA1 region in vitro. Brain Research 45:257–65. [EDR, aZX]Google Scholar

Frey, U., Matthies, H., Reymann, K. G. & Matthies, H. (1991). The effect of dopaminergic D1 receptor blockade during totalization on the expression of long-term potentiation in the rat CA1 region in vitro. Neuroscience Letters 29:111–14. [aZX]10.1016/0304-3940(91)90732-9CrossRef Google Scholar

Frost, W. N., Castellucei, V. F., Hawkins, R. D. & Kandel, E. R. (1985) Monosynaptic connections from the sensory neurons of the gill- and siphon-withdrawal reflex in Aplysia participate in the storage of long-term memory for sensitization. Proceedings of the National Academy of Sciences USA 82:8266–69. [aZX]10.1073/pnas.82.23.8266CrossRef Google Scholar

Fryxell, K. J. & Meyerowitz, E. M. (1991) The evolution of rhodopsins and neurotransmitter receptors. Journal of Molecular Evolution 33:367–68. [aSPD]10.1007/BF02102867CrossRef Google Scholar PubMed

Fujiki, K., Hotta, Y., Hayakawa, M., Sakuma, H., Shiono, T., Noro, M., Shakuma, T., Tamai, M., Hikiji, K., Kawaguchi, R. & Hoshi, A. (1992) Point mutations of rhodopsin gene found among Japanese families with antosomal dominant retinitis pigmentosa (ADRP). Japanese Journal of Human Genetics 37:125–32. [aSPD]Google Scholar

Fukuda, M. N., Papermaster, D. S. & Hargrave, P. A. (1979) Rhodopsin carbohydrate: Structure of small oligosaecharides attached at two sites near the NH2 terminus. Journal of Biological Chemistry 254:8201–7. [aPAH]10.1016/S0021-9258(19)86876-XCrossRef Google Scholar PubMed

Fukada, Y., Schichida, Y., Yoshizawa, T., Ito, M., Kodama, A. & Tsukida, K. (1984) Studies on structure and function of rhodopsin by use of cyclopentatrienylidene 11-cis-locked-rhodopsin. Biochemistry 23:5826–32. [aPAH]10.1021/bi00319a023CrossRef Google Scholar PubMed

Fukada, Y., Takao, T., Ohguor, H., Yoshizawa, T., Akino, T. & Shimonishi, Y. (1990) Farnesylated gamma subunit of photoreceptor G protein indispensable for GTP-binding. Nature 346:658–60. [aMDB]10.1038/346658a0CrossRef Google Scholar PubMed

Fung, B. K.-K. (1993) Characterization of transducin from bovine retinal rod outer segments: 1. Separation and reconstitution of the subunits. Journal of Biological Chemistry 258:10495–502. [rM DB]10.1016/S0021-9258(17)44483-8CrossRef Google Scholar

Fung, B. K.-K. & Griswold-Prenner, I. (1989) G-protein-effector coupling: Binding of rod phosphodiesterase inhibitory subunit to transducin. Biochemistry 28:3133–37. [AY]10.1021/bi00434a003CrossRef Google Scholar

Fung, B. B.-K., Hurley, J. B. & Stryer, L. (1981) Flow of information in the light-triggered cyclic nucleotide cascade of vision. Proceedings of the National Academy of Sciences USA 78:152–56. [aM DB, AY]10.1073/pnas.78.1.152CrossRef Google Scholar

Fung, B. K.-K., Young, J. H., Yamane, H. K. & Griswold-Prenner, I. (1990) Subunit stoichiometry of retinal rod cGMP phosphodiesterase. Biochemistry 29:2657–64. [aMDB]10.1021/bi00463a006CrossRef Google Scholar PubMed

Furman, R. E. & Tanaka, J. C. (1990) Monovalent selectivity of the cyclic guanosine monophosphatu-activated ion channel. Journal of General Physiology 96:57–82. [aRSM]10.1085/jgp.96.1.57CrossRef Google Scholar PubMed

Gal, A., Artlich, A., Ludwig, M., Niemeyer, C., Olek, K., Schwinger, E. & Schinzel, A. (1991) Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa. Genomics 11:468–70. [aSPD]10.1016/0888-7543(91)90159-CCrossRef Google Scholar PubMed

Gal, A., Orth, U., Baehr, W., Schwinger, E., & Rosenberg, T. (1994) Heterozygous missense mutation in the rod cGMP phosphodiesterase G-subunit gene in autosomal dominant stationary night blindness. Nature Genetics 7, 551:64–67. [aSPD]10.1038/ng0594-64CrossRef Google Scholar

Gannon, A. M., Rodriguez, J. A., Humphries, P., Birch, D. G., Heckenlively, J. R. & Daiger, S. P. (1993) Mutations in peripherin/RDS in patients with retinitis pigmentosa: A 12 base-pair deletion in exon 2. American Journal of Human Genetics 53:1160. [aSPD]Google Scholar

Gao, B. & Gilman, A. (1991) Cloning and expression of a widely distributed (type IV) adenylyl cyclase. Proceedings of the National Academy of Sciences USA 88:10178–82. [aZX]10.1073/pnas.88.22.10178CrossRef Google Scholar PubMed

Garavito, R. M. (1991). Crystallizing membrane proteins: Experiments on different systems. In: Crystallization of membrane proteins, ed. Michel, H.. CRC Press. [aPAH]Google Scholar

Garavito, R. M. (in press) Strategies for crystallizing membrane proteins. Journal of Bioenergetics and Biomembranes. [RMG]Google Scholar

Garavito, R. M. & Picot, D. (1990) The art of membrance protein crystallization. Methods: A Companion to methods in Enzymology 1:57–69. [RMG]10.1016/S1046-2023(05)80147-1CrossRef Google Scholar

Gery, I., Chanaud, N. P. III & Anglade, E. (1994) Recover in is highly uveitogenic in Lewis rats. Investigative Ophthalmology and Visual Science 35:3342–45. [ASP]Google Scholar

Ghirardi, M., Braha, O., Hochner, B., Montarolo, P. G., Kandel, E. R. & Dale, N. (1992) Roles of PKA and PKC in facilitation of evoked and spontaneous transmitter release at depressed and nondepressed synapsesin Aplysia sensory neurons. Neuron 9:479–89. [aZX, TWA]10.1016/0896-6273(92)90185-GCrossRef Google Scholar

Gibson, F., Walsh, J., Mburu, P., Varela, A., Brown, K. A., Antonio, M., Belsel, K. W., Steel, K. P. & Brown, S. D. M. (1995) A type VII myosin encoded by the mouse deafness gene shaker-1. Nature 374:62–64. [rSPD]10.1038/374062a0CrossRef Google Scholar PubMed

Gillespie, P. G. & Beavo, J. A. (1988) Characterization of a bovine cone photoreceptor phosphodiesterase purified by cyclic GMP-sepharose chromatography. Journal of Biological Chemistry 263:8133–41. [aMDB]10.1016/S0021-9258(18)68452-2CrossRef Google Scholar PubMed

Gillespie, P. G. & Beavo, J. A. (1989) cGMP is tightly bound to bovine retinal rod phosphodiesterase. Proceedings of the National Acadenuj of Sciences USA 86:4311–15. [aMDB]10.1073/pnas.86.11.4311CrossRef Google Scholar PubMed

Glatt, C. E. & Snyder, S. H. (1993) Cloning and expression of an adenylyl cyclase localized to the corpus striatum. Nature 363:679–80. [aZX]10.1038/363679b0CrossRef Google Scholar

Gnegy, M., Muirhead, N., Roberts-Lewis, J. M. & Treisman, G. (1984) Calmodulin stimulates adenylyl cyclase activity and increases dopamine activation in bovine retina. Journal of Neuroscience 4:2712–17. [aZX]10.1523/JNEUROSCI.04-11-02712.1984CrossRef Google Scholar PubMed

Gnegy, M. & Treisman, G. (1981) Effect of calmodulin on dopamine-sensitive adenylate cyclase activity in rat striatal membranes. Molecular Pharmacology 19:256–63. [aZX]Google Scholar PubMed

Gold, G. H. & Korenbrot, J. J. (1980) Light-induced calcium release by intact retinal rods. Proceedings of the National Academy of Sciences USA 77:5557–61. [TGW]10.1073/pnas.77.9.5557CrossRef Google Scholar PubMed

Goldberg, M. F. (1994) Molecular heterogeneity in retinitis pigmentosa. Ophthalmic Genetics 15(2):47–50 [AB]10.3109/13816819409098863CrossRef Google Scholar PubMed

Goldsmith, B. A. & Abrams, T. W. (1991) Reversal of synoptic depression by serotonin ut Aplysia sensory neuron synapses involves activation of adenylate cyclase. Proceedings of the National Academy of Sciences USA 88:9021–25. [TWA]10.1073/pnas.88.20.9021CrossRef Google Scholar

Gorczyca, W. A., Gray-Keller, M. P., Detwiler, P. B. & Palczewski, K. (1994) Purification and physiological evaluation of a guanylate eyclase activating protein from retinal rods. Proceedings of the National Academy of Sciences USA 91:4014–18. [aMDB]10.1073/pnas.91.9.4014CrossRef Google Scholar PubMed

Gordon, J. I., Duronio, R. J., Rudnick, D. A., Adams, S. P. & Gokel, G. W. (1991) Protein N-myristoylation. Journal of Biological Chemistry 266:8647–50. [KS]10.1016/S0021-9258(18)31490-XCrossRef Google Scholar PubMed

Gordon, S. E., Brautigan, D. L. & Zimmerman, A. L. (1992) Protein phosphatases modulate the apparent agonist affinity of the ligand regulated ion channel of retinal rods. Neuron 8:739–48. [aMDB, aRSM, RLB. LWH, TGW]10.1016/0896-6273(92)90036-DCrossRef Google Scholar

Gordon, S. E., Downing-Park, J. & Zimmerman, A. L. (in press) Modulation of the cGMP-gated ion channel in frog rods by calmodulin and an endogenous inhibitory factor. Journal of Physiology. [MPG-K, rRSM]Google Scholar

Gordon, S. E. & Zimmerman, A. L. (1994) Modulation of the rod cCMP-gated ion channel by calmodulin and an endogenous factor distinct from calmodulin. Biophysics Journal 66:A355. [MSS, TCW]Google Scholar

Gorodovikova, E. N. & Philippov, P. P. (1993) The presence of a calcium sensitive p26-containing complex in bovine retinal rod cells. FEBS Letters 335:277–79. [SK]10.1016/0014-5793(93)80746-HCrossRef Google Scholar

Goslin, K., Schreyer, D. J., Skene, J. H. P. & Banker, G. (1988) Development of neuronal polarity: GAP-43 distinguishes axonal from dendritic growth cones. Nature 336:672–74. [EDR]10.1038/336672a0CrossRef Google Scholar PubMed

Golliding, E. H., Ngai, J., Kramer, R. H., Colicos, S., Axel, R., Siegelbaum, S. A. & Chess, A. (1992) Molecular cloning and single channel properties of the cyclic nuclco tide-gated channel from catfish olfactory neurons. Neuron 8:45–58. [aRSM]10.1016/0896-6273(92)90107-OCrossRef Google Scholar

Golliding, E. H., Tibbs, G. R., Liu, D. & Siegelbaum, S. A. (1993) Role of the H5 domain in determining pore diameter and ion permeation through cyclic nuclcotide-gated channels. Nature 364:61–64. [aRSM]10.1038/364061a0CrossRef Google Scholar

Golliding, E. H., Tibbs, G. R. & Siegelbaum, S. A. (1994) Molecular mechanism of cyclic-nucleotide-gated channel activation. Nature 372:369–74. [rRSM]10.1038/372369a0CrossRef Google Scholar

Grant, S. G. N., O'Dell, T. J., Karl, K. A., Stein, P. L., Soriano, P. & Kandel, E. R. (1992) Impaired long-term potentiation, spatial learning and hippocampal development in fyn mutant mice. Science 258:1903–92. [aZX]10.1126/science.1361685CrossRef Google Scholar PubMed

Gray-Keller, M. P., Bienibaiim, M. S. & Bownds, M. D. (1990) Transducin activation in electropermeabilized frog rod outer segments is highly amplified, and a portion equivalent to phosphodiesterase remains membrane-bound. Journal of Biological Chemistry 265:15323–32. [aMDB]10.1016/S0021-9258(18)77259-1CrossRef Google Scholar

Gray-Keller, M. P. & Detwiler, P. B. (1994a) Intracellular calcium measurements in isolated rod photoreceptors. Investigative Ophthalmology and Visual Science 35:1486. [aMDB]Google Scholar

Gray-Keller, M. P. & Detwiler, P. B. (1994b) Tlie calcium feedback signal in the phototransduction cascade of vertebrate rods. Neuron 13(4):849–61. [MPC-K, MSS, TCW, rMDB]10.1016/0896-6273(94)90251-8CrossRef Google Scholar

Gray-Keller, M. P., Polans, A. S. Palczewski, K. & Derwiler, P. B. (1993) The effect of recoverin-like calcium-binding proteins on the photoresponse of retinal rods. Neuron 10:523–31. [aMDB, aJBH, MPC-K, LWH]10.1016/0896-6273(93)90339-SCrossRef Google Scholar PubMed

Grecksch, G. & Matthies, H. (1980) Two sensitive periods for the amnesic effect of anisomycin. Pharmacology and Biochemistry of Behavior 12:663–65. [aZX]10.1016/0091-3057(80)90145-8CrossRef Google Scholar PubMed

Greenberg, J., Goliath, R., Brighton, P., & Raniesar, R. (1994) A new locus for autosomal dominant retinitis pitmentosa on the short arm of chromosome 17. Human Molecular Genetics 6:915–18. [aSPD]10.1093/hmg/3.6.915CrossRef Google Scholar

Greenberg, S. M., Castellueci, V. F., Bayley, H. & Schwartz, J. H. (1987) A molecular mechanism for long-term sensitization in Aplysia. Neuron 329:62–65. [aZX]Google Scholar PubMed

Greengard, P. (1979) Cyclic nucleotides, phosphorylated proteins, and the nervous system. Federation Proceedings 38:2208–17. [TWA]Google Scholar PubMed

Groskoph, S. L., Hammett, D. J. & Cote, R. H. (1992) Nucleotide energy metabolism in electropormeabilizcd rod photoreceptors. Investigative Ophthalmology and Visual Science 33:1008. [aM DB]Google Scholar

Gullion, T. & Schaefer, J. (1989) Detection of weak heteronuclear dipolar coupling by rotational echo double resonance nuclear magnetic resonance. In: Advances in magnetic resonance, vol. 13., ed. Warren, W. S.. Academic Press. [SOS]Google Scholar

Gustafsson, B., Wigstrom, H., Abraham, W. C. & Huang, Y. Y. (1987) Longterm potentiation in the hippocampus using depolarizing current pulses as the conditioning stimulus to single volley synaptic potentials. Journal of Neuroscience 7:774–80. [TWA]10.1523/JNEUROSCI.07-03-00774.1987CrossRef Google Scholar

Hagiwara, M., Brindle, P., Harootunian, A., Armstrong, R., Rivier, J., Vale, J., Tsien, R. & Montminy, M. R. (1993) Coupling of hormonal stimulation and transcription via the cAMP responsive factor CREB is rate limited by nuclear entry of protein kinase A. Molecular and Cellular Biology 13:4852–59. [aZX]Google Scholar PubMed

Hakki, S. & Sitaramayya, A. (1990) Guanylate cyclase from bovine rod outer segments: Solubilization, partial purification, and regulation by inorganic pyrophosphate. Biochemistry 29:1088–94. [KWK]10.1021/bi00456a035CrossRef Google Scholar PubMed

Hall, M. D., Hoon, M. A., Ryba, N. J. P., Pottinger, J. D. D., Keen, J. N., Sabil, H. R. & Findlay, J. B. C. (1991) Molecular cloning and primary structure of squid (Loligo forbesi) rhodopsin, a phospholipase C-directed C-protein-linked receptor. Biochemistry Journal 274:35–40. [aPAH]10.1042/bj2740035CrossRef Google Scholar PubMed

Halloran, S. L. (1985) A multidisciplinary analysis of retinitis pigmentosa: Genetic, cpidemiological and clinical parameters. Doctoral thesis, Virginia Commonwealth University. [aSPD]Google Scholar

Hamm, H. (1990) Regulation by light of cyclic nucleotide-dependent protein kinases and their substrates in frog rod outer segments. Journal of General Physiology 95:545–67. [aMDB]10.1085/jgp.95.3.545CrossRef Google Scholar PubMed

Hamm, H. E. & Bownds, M. D. (1986) Protein complement of rod outer segments of frog retina. Biochemistry 25:4512–23. [aMDB]10.1021/bi00364a010CrossRef Google Scholar PubMed

Hamm, H. E., Deretic, D., Arendt, A., Hargrave, P. A., Koenig, B. & Hofmann, K. P. (1988) Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit. Science 241:832–35. [EAD]10.1126/science.3136547CrossRef Google Scholar PubMed

Hamm, H. E. & Rarick, H. M. (1994) Use of synthetic peptides for mapping G protein interaction sites with receptors. Methods in Enzymology 237:423–36. [RKC]10.1016/S0076-6879(94)37079-6CrossRef Google Scholar

Han, M., DeDecker, B. & Smith, S. O. (1993) Localization of the retinal protonated schiff base counterion in rhodopsin. Biophysics Journal 65:899–926. [SOS]10.1016/S0006-3495(93)81117-2CrossRef Google Scholar PubMed

Han, M. & Smith, S. O. (in press) NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin. Biochemistry. [SOS]Google Scholar

Harbison, G. S., Smith, S. O., Pardoen, J. A., Winkel, D. C., Lugtenburg, J., Herzfeld, J., Mathies, R. & Griffln, R. G. (1984) Dark-adapted Bacteriorhodopsin contains 13-cis, 15-syn and all-trans, 15-anti retinal schiff bases. Proceedings of the National Academy of Sciences USA 81:1706–9. [SOS]10.1073/pnas.81.6.1706CrossRef Google Scholar PubMed

Hardie, R. C. & Minke, B. (1992) The trp gene is essential for a light activated Ca2+ channel in Drosophila photoreceptors. Neuron 8:643–51. [aRSM]10.1016/0896-6273(92)90086-SCrossRef Google Scholar PubMed

Hargrave, P. A. & Fong, S.-L. (1977) The amino-and carboxyl-terminal sequence of bovine rhodopsin. Journal of Supramolecular Structure 6:559–70. [rPAH]10.1002/jss.400060409CrossRef Google Scholar PubMed

Hargrave, P. A., Hamm, H. E. & Hofmann, K. P. (1993) Interaction of rhodopsin with the G-protein, transducin. BioEssays 15:43–50. [aPAH]10.1002/bies.950150107CrossRef Google Scholar PubMed

Hargrave, P. A. & McDowell, J. H. (1992a) Rhodopsin and phototransduction: A model system for G protein-linked receptors. FASEB Journal 6:2323–31. [aMDB, aSPD, aPAH]10.1096/fasebj.6.6.1544542CrossRef Google Scholar

Hargrave, P. A. & McDowell, J. H. (1992b) Rhodopsin and phototransduction. International Review of Cytology 137B:49–97. [aSPD]Google Scholar PubMed

Hargrave, P. A. & McDowell, J. H. (1993) Rhodopsin and phototransduction. International Review of Cytology 137B:49–97. [aPAH]10.1016/S0074-7696(08)62600-5CrossRef Google Scholar

Hargrave, P. A., McDowell, J. H., Feldmann, R. J., Atkinson, P. H., Rao, J. K. M. & Argos, P. (1984) Rhodopsin's protein and carbohydrate structure: Selected aspects. Vision Research 24:1487–99. [aPAH]10.1016/0042-6989(84)90311-0CrossRef Google Scholar PubMed

Hargrave, P. A. & O'Brien, P. J. (1991) Speculations of the molecular basis of retinal degeneration in retinitis pigmentosa. In: Retinal degeneration, ed. Hollyfield, J. G., Anderson, R. E. & LaVail, M. M.. CRC Press. [aSPD]Google Scholar

Hayakawa, M., Hotta, Y., Imai, Y., Fujiki, K., Nakamura, A., Yanashima, K. & Kanai, A. (1993) Clinical features of autosomal dominant retinitis pigmentosa with rhodopsin gene codon 17 mutation and retinal neovascularization. American Journal of Ophthalmology 115:168–73. [aSPD]10.1016/S0002-9394(14)73920-0CrossRef Google Scholar PubMed

Hayashi, F. (1994) Light-dependent in vivo phosphorylation of an inhibitory subunit of cGMP-phosphodiesterase in frog rod photoreceptor outer segments. FEBS Letters 338:203–6. [aMDB]10.1016/0014-5793(94)80365-XCrossRef Google Scholar PubMed

Hayashi, F., Lin, G. Y., Matsumoto, H. & Yamazaki, A. (1991) Phosphatidylinositol-stimulated phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in vertebrate rod photoreceptors. Proceedings of the National Academy of Sciences USA 88:4333–37. [aMDB]10.1073/pnas.88.10.4333CrossRef Google Scholar PubMed

Haynes, L. W. (1992) Block of the cyclic CMP-gated channel of vertebrate rod and cone photoreeeptors by L-cis-diltiazem. Journal of General Physiology 100:783–801. [LWH]10.1085/jgp.100.5.783CrossRef Google Scholar PubMed

Haynes, L. W. & Yau, K.-W. (1985) Cyclic GMP-sensitive conductance in outer segment membrane of catfish cones. Nature 317:61–64. [aRSM]10.1038/317061a0CrossRef Google Scholar PubMed

Hearst, E. (1988) Fundamentals of learning and conditioning. In: Steven's handbook of experimental psychology, ed. Atkinson, R. C., Herrnstein, R. J., Lindzey, G. & Luce, R. D.. Wiley Interscience. [TWA]Google Scholar

Hebert, H., Xian, Y., Hacksell, I. & Mårdh, S. (1992) Two-dimensional crystals of membrane-bound gastric H, K-ATPase. FEBS Letters 299:159–62. [aPAH]10.1016/0014-5793(92)80237-BCrossRef Google Scholar PubMed

Heck, M. & Hofmann, K. P. (1993) G-protein-effector coupling: A real-time light-scattering assay for transducin-phosphodiesterase interaction. Biochemistry 32:8220–27. [aMDB]10.1021/bi00083a024CrossRef Google Scholar PubMed

Heckenlively, J. R. (1988) Retinitis pigmentosa. Lippincott. [aSPD]Google Scholar PubMed

Heckenlively, J. R., Rodriguez, J. A. & Daiger, S. P. (1990) Autosomal dominant sectoral retinitis pigmentosa: Two families with transversion mutation in codon 23 of rhodopsin. Archives of Ophthalmology 109:84–91. [aSPD]10.1001/archopht.1991.01080010086038CrossRef Google Scholar

Heginbotham, L., Abramson, T. & MacKinnon, R. (1992) A functional connection between the pores of distantly-related ion channels as revealed by mutant K+ channels. Science 258:1152–55. [aRSM]10.1126/science.1279807CrossRef Google Scholar PubMed

Heinonen, E. & Akerman, K. E. (1987) Intracellular free magnesium in synaptosomes measured with entrapped eriochrome blue. Biochimica et Biophysica Acta 898:331–37. [RLH]10.1016/0005-2736(87)90074-5CrossRef Google Scholar PubMed

Hekman, M., Bauer, P. H., Sohlemann, P. & Lohse, M. J. (1994) Phosducin inhibits receptor phosphorylation by the β-adrenergic receptor kinase in a PKA-regulated manner. FEBS Letters 343:120–24. [BMW]10.1016/0014-5793(94)80302-1CrossRef Google Scholar

Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E. & Downing, K. H. (1990) Model for the structure of baeteriorhodopsin based on high-resolution electron cryomicroscopy. Journal of Molecular Biology 213:899–929. [aPAH, EAD. RMG]10.1016/S0022-2836(05)80271-2CrossRef Google Scholar

Henderson, R. & Unwin, P. N. T. (1975) Three-dimensional model of purple membrane obtained by electron microscopy. Nature (London) 275:28–32. [RMG]Google Scholar

Hermolin, J., Karell, M. A., Hamm, H. E. & Bownds, M. D. (1982) Calcium and cyclic GMP regulation of light-sensitive protein phosphorylation in frog photoreceptor membranes. Journal of General Physiology 79:633–55. [aMDB]10.1085/jgp.79.4.633CrossRef Google Scholar PubMed

Hidaka, H. & Okazaki, K. (1993) Neurocalcin family: A novel calcium-binding protein abundant in bovine central nervous system. Neuroscience Research 16:73–77. [KT]10.1016/0168-0102(93)90074-ZCrossRef Google Scholar PubMed

Hille, B. (1992) Ionic channels of excitable membranes, 2d ed. Sinauer. [TWA]Google Scholar

Hodgkin, A. L., McNaughton, P. A. & Nunn, B. J. (1985) The ionic selectivity and calcium dependence of the light-sensitive pathway in toad rods. Journal of Physiology 358:447–68. [aRSM]10.1113/jphysiol.1985.sp015561CrossRef Google Scholar PubMed

Hodgkin, A. L. & Nunn, B. J. (1988) Control of light-sensitive current in salamander rods. Journal of Physiology (London) 403:439–71. [aMDB]10.1113/jphysiol.1988.sp017258CrossRef Google Scholar PubMed

Hofmann, K. P. (1986) Photoproducts of rhodopsin in the disc membrane. Photochemistry & Photobiophysics 13:309–27. [aPAH]Google Scholar

Hofmann, K. P., Pulvermuller, A., Buczylko, J., Van Hooser, P. & Palczewski, K. (1992) The role of arrestin and retinoids in the regeneration pathway of rhodopsin. Journal of Biological Chemistry 267:15701–6. [aMDB, RKC]10.1016/S0021-9258(19)49592-6CrossRef Google Scholar PubMed

Hong, K. & Hubbell, W. L. (1973) Lipid requirements for rhodopsin regenerability. Biochemistry 12:4517–23. [aPAH]10.1021/bi00746a033CrossRef Google Scholar PubMed

Hopkins, W. F. & Johnston, D. (1988) Noradrenergic enhancement of long-term potentiation at mossy fiber synapses in the hippocampus. Journal of Neurophysiology 59:667–87. [aZX]10.1152/jn.1988.59.2.667CrossRef Google Scholar PubMed

Horn, M., Humphries, P., Kunisch, M., Marchese, C., Apfelstedt-Sylla, E., Fugi, L., Zrenner, E., Kenna, P., Gal, A. & Farrar, J. (1992) Deletions in exon 5 of the human rhodopsin gene causing a shift in reading frame and autosomal dominant retinitis pigmentosa. Human Genetics 90:255–57. [aSPD]10.1007/BF00220073CrossRef Google Scholar PubMed

Hotta, Y., Shiono, T., Hakawa, M., Hashimoto, T., Kanai, A., Nakajima, A., Noro, M., Sakuma, T. & Fujiki, K. (1992) Molecular biological study of the rhodopsin gene in Japanese patients with autosomal dominant retinitis pigmentosa. Nippon Canka Gakkai Zasshi 96:237–42. [aSPD]Google Scholar PubMed

Hovmuller, S., Slaughter, M., Berriman, J., Karlsson, B., Weiss, H. & Leonard, K. (1983) Structural studies of cytochrome reductase: Improved membrane crystals of the enzyme complex and crystallization of a subcomplex. Journal of Molecular Biology 165:401–6. [aPAH]10.1016/S0022-2836(83)80264-2CrossRef Google Scholar

Hsu, Y.-T. & Molday, R. S. (1993) Modulation of the cGMP-gated channel of rod photoreceptor cells by calmodulin. Nature 361:76–79. [aMDB, aJBH, aZX, MPG-K, LWH, DDO]10.1038/361076a0CrossRef Google Scholar PubMed

Hsu, Y.-T. & Molday, R. S. (1994) Interaction of calmodulin with the cyclic GMP-gated channel of rod photoreceptor cells. Journal of Biological Chemistry 269:29765–70. [rRSM]10.1016/S0021-9258(18)43947-6CrossRef Google Scholar PubMed

Hu, S., Franklin, P. J., Wang, J., Ruiz Silva, B. E., Derguini, F. & Nakanishi, K. (1994) Unbleachable rhodopsin with an 11-cis-locked eightmembered ring retinal: The visual transduction process. Biochemistry 33:408–16. [aPAH]10.1021/bi00168a004CrossRef Google Scholar

Huang, P. C., Gaitan, A. E., Hao, Y., Petters, R. M. & Wong, F. (1993) Cellular interactions implicated in the mechanism of photoreceptor degeneration in transgenic mice expressing a mutant rhodopsin gene. Proceedings of the National Academy of Sciences USA 90:8484–88. [MWK]10.1073/pnas.90.18.8484CrossRef Google Scholar PubMed

Humphries, P., Farrar, G. J. & Kenna, P. (1993) Autosomal dominant retinitis pigmentosa: Molecular, genetic and clinical aspects. Progress in Retinal Research 12:231–45. [aSPD]10.1016/0278-4327(93)90011-HCrossRef Google Scholar

Humphries, P., Kenna, P. & Farrar, G. J. (1992) On the molecular genetics of retinitis pigmentosa. Science 256:804–8. [aSPD]10.1126/science.256.5058.804CrossRef Google Scholar PubMed

Hundal, S. P., Difrancesco, D., Mangoni, M., Grammar, W. J. & Conley, E. C. (1993) An iso form of the cGMP-gated retinal photoreceptor channel gene expressed in the sinoa trial node (pacemaker) region of rabbit heart. Biochemical Society Transcripts 21:119S. [aRSM]10.1042/bst021119sCrossRef Google Scholar

Hurley, J. B. (1992) Signal transduction enzymes of vertebrate photoreceptors. Journal of Bioenergetics and Biomembranes 24:219–26. [aMDB]10.1007/BF00762680CrossRef Google Scholar PubMed

Hurley, J. B., Dizhoor, A. M., Ray, S. & Stryer, L. (1993) Recovering role: Conclusion withdrawn. Science 260:740. [aMDB, aJBH]10.1126/science.8097896CrossRef Google Scholar

Hurley, J. B. & Stryer, L. (1982) Purification and characterization of the gamma regulatory subunit of the cGMP phosphodiesterase from retinal rod outer segments. Journal of Biological Chemistry 257:11094–99. [aMDB]10.1016/S0021-9258(18)33937-1CrossRef Google Scholar

Hurwitz, R. & Holcombe, V. (1991) Affinity purification of the photoreceptor cGMP- gated cation channel. Journal of Biological Chemistry 266:7975–77. [aRSM, RLH, TGW]10.1016/S0021-9258(18)92925-XCrossRef Google Scholar PubMed

Illing, M., Colville, D. A., Williams, A. J. & Molday, R. S. (1994) Sequencing, cloning and characterization of the cyclic nucleotide-gated channel complex of rod outer segments. Investigative Ophthalmology and Visual Science [Abstract 1022] 35:1474. [rRSM]Google Scholar

Impey, S., Wayman, G., Wu, Z. & Storm, D. R. (in press) The type I adenylyl cyclase functions as a coincidence detector for control of CRE-mediated transcription by Ca²⁺ and isoproterenol. Molecular and Cellular Biology.Google Scholar

Inglehearn, C. F., Bashir, R., Lester, D. H., Jay, M., Bird, A. C. & Bhattacharya, S. S. (1991) A 3-bp deletion in the rhodopsin gene in a family with autosomal dominant retinitis pigmentosa. American Journal of Human Genetics 48:26–30. [aSPD]Google Scholar

Inglehearn, C. F., Carter, S. A., Keen, T. J., Lindsey, J., Stephenson, A. M., Bashir, R., Al-Maghtheh, M., Moore, A. T., Jay, M., Bird, A. C. & Bhattacharya, S. S. (1993) A new locus for autosomal dominant retinitis pigmentosa (adRP) on chromosome 7p. Nature Genetics 4:51–53. [aSPD]10.1038/ng0593-51CrossRef Google Scholar PubMed

Inglehearn, C. F., Keen, T. J., Bashir, R., Jay, M., Fitzke, F., Bird, A. C., Crombie, A. & Bhattacharya, S. S. (1992) A complete screen for mutations of the rhodopsin gene in a panel of patients with autosomal dominant retinitis pigmentosa. Human Molecular Genetics 1:41–45. [aSPD]10.1093/hmg/1.1.41CrossRef Google Scholar

Inglese, J., Freedman, N. J., Koch, W. J. & Lefkowitz, R. J. (1993) Structure and mechanism of the G protein-coupled receptor kinases. Journal of Biological Chemistry 268:23735–38. [KT]10.1016/S0021-9258(20)80439-6CrossRef Google Scholar PubMed

Ishikawa, Y., Katsushika, S., Chen, L., Halnon, N. J., Kawabe, J. & Homey, C. J. (1992) Isolation and characterization of a novel cardiac adenylyl cyclase cDNA. Journal of Biological Chemistry 267:13553–57. [aZX]10.1016/S0021-9258(18)42247-8CrossRef Google Scholar

Ito, M., Kodama, A., Tsukida, K., Fukada, Y., Shichida, Y. & Yoshizawa, T. (1982) A novel rhodopsin analogue possessing the cyclopentatrienylidene structure as the 11-cis-locked and the full planar chromophore. Chemical & Pharmaceutical Bulletin 30:1913–16. [aPAH]10.1248/cpb.30.1913CrossRef Google Scholar

Itoh, S., Takshima, A. & Macda, Y. (1992) Protective effect of cerulein on memory impairment induced by protein synthesis inhibitors in rats. Peptides 13:1007–12. [EDR]10.1016/0196-9781(92)90063-9CrossRef Google Scholar PubMed

Jacobowitz, O., Chen, J., Premont, R. T. & Iyengar, R. (1993) Stimulation of specific types of Gs-stimulated adenylyl cyclases by phorbol ester treatment. Journal of Biological Chemistry 268:3829–32. [aZX]10.1016/S0021-9258(18)53547-XCrossRef Google Scholar PubMed

Jacobson, F. A. S. & Baseom, G. I. (1993) Phosducin as a candidate gene for retinitis pigmentosa and Usher syndrome type H. InvestigativeOphthalmology and Visual Science 34:1458. [aSPD]Google Scholar

Jacobson, S. G., Kemp, C. M., Cideciyan, A. V., Macke, J. P., Sung, C.-H. & Nathans, J. (1994) Phenotypes of stop codon and splice site rhodopsin mutations causing retinitis pigmentosa. Investigative Ophthalmology and Visual Science 35:2521–34. [aSPD, AB]Google Scholar PubMed

Jacobson, S. G., Kemp, C. M., Sung, C.-H. & Nathans, J. (1991) Retinal function and rhodopsin levels in autosomal dominant retinitis pigmentosa with rhodopsin mutations. American Journal of Ophthalmology 112:256–71. [aSPD]10.1016/S0002-9394(14)76726-1CrossRef Google Scholar PubMed

Jan, L. Y. & Jan, Y. N. (1989) Voltage-sensitive ion channels. Cell 56:13–25. [aRSM]10.1016/0092-8674(89)90979-3CrossRef Google Scholar PubMed

Jan, L. Y. & Jan, Y. N. (1990) A superfamily of ion channels. Nature 345:672. [aRSM]10.1038/345672a0CrossRef Google Scholar PubMed

Jansen, J. J. M., Mulder, W. R., De Caluw, G. L. J., Vlak, J. M. & DeGrip, W. J. (1991) In vitro expression of bovine opsin using recombinant baculovirus: The role of glutamic acid (134) in opsin biosynthesis and glycosylation. Biochimica et Biophysica Acta 1089:68–76. [aPAH]10.1016/0167-4781(91)90086-2CrossRef Google Scholar PubMed

Jin, J., Crouch, R. K., Corson, D. W., Katz, B. M., MacNichol, E. F. & Cornwall, M. C. (1993) Noncovalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones. Neuron 11:513–22. [aMDB, RKC]10.1016/0896-6273(93)90155-KCrossRef Google Scholar PubMed

Johnson, R. S., Ohguro, H., Palczewski, K., Hurley, J. B., Walsh, K. A. & Neubert, T. A. (1994) Heterogeneous N-acylation is a tissue- and speciesspecific posttranshitional modification. Journal of Biological Chemistry 269:21067–71. [KS]10.1016/S0021-9258(17)31930-0CrossRef Google Scholar

Jones, G. J., Crouch, R. K., Wiggcrt, B., Cornwall, M. C. & Ghader, G. J. (1989) Retinoid requirements for recovery of sensitivity after visual pigment bleaching in isolated photoreccptors. Proceedings of the National Academy of Sciences USA 86:9606–10. [RKC]10.1073/pnas.86.23.9606CrossRef Google Scholar

Jordan, S. A., Farrar, C. J., Kenna, P., Humphries, N. M., Shells, D. M., Kumar-Singh, R., Sharp, E. M., Ayuso, C., Benitez, J. & Humphries, P. (1993) Localization of an autosomal dominant retinitis pigmentosa gene to chromosome 7q. Nature Cenctics 4:54–58. [aSPD]10.1038/ng0593-54CrossRef Google Scholar PubMed

Jordan, S. A., Farrar, G. J., Kumar-Singh, R., Kenna, P., Humphries, M. M., Allamand, V., Sharp, E. M. & Humphries, P. (1992) Autosomal dominant retinitis pigmentosa (adRP; RP6): Cosegregation of RP6 and the peripherin-RDS locus in a late-onset family of Irish origin. American Journal of Human Genetics 50:634–39. [aSPD]Google Scholar

Kanng, B. K., Kandel, E. R. & Grant, S. G. (1993) Activation of cAMP-responsive genes by stimuli that produce long-term facilitation in Aplysia sensory neurons. Neuron 10:427–35. [aZX]10.1016/0896-6273(93)90331-KCrossRef Google Scholar

Kahlert, M. & Hofmann, K.-P. (1991) Reaction rate and collisioal efficiency of the rhodopsin-transducin system in intact retinal rods. Biophysical Journal 59:375–86. [KWK]10.1016/S0006-3495(91)82231-7CrossRef Google Scholar PubMed

Kahlert, M., Pepperberg, D. R. & Hofmann, K. P. (1990) Effect of bleached rhodopsin on signal amplification in rod visual receptors. Nature 345:537–39. [aMDB]10.1038/345537a0CrossRef Google Scholar PubMed

Kajimoto, Y., Shirai, Y., Mukai, H., Kuno, T. & Tanaka, C. (1993) Molecular cloning of two additional members of the neural visinin-like Ca2+- binding protein gene family. Journal of Neurochemistry 61:1091–96. [KT]10.1111/j.1471-4159.1993.tb03624.xCrossRef Google Scholar

Kajiwara, K., Berson, E. L. & Dryja, T. P. (1994) Digenic retinitis pigmentosa due to mutations at the unlinked pheripherin/RDS and ROM-1 loci. Science 264:1604–8. [aSPD, AB]10.1126/science.8202715CrossRef Google Scholar

Kajiwara, K., Huhn, L. B., Mukai, S., Travis, G. H., Berson, E. L. & Dryja, T. P. (1991) Mutations in the human retinal degeneration slow gene in autosomal dominant retinitis pigmentosa. Nature 354:480–3. [aSPD]10.1038/354480a0CrossRef Google Scholar PubMed

Kajiwara, K., Sandberg, M. A., Berson, E. L. & Dryja, T. P. (1993) A null mutation in the human periphcrin/RDS gene in a family with autosomal dominant retinitis punctata albescens. Nature Genetics 3:208–12. [aSPD]10.1038/ng0393-208CrossRef Google Scholar

Kandel, E. R., Abrams, T., Bernier, L., Caruw, T. J., Hawkins, R. D. & Schwartz, J. H. (1983) Classical conditioning and sensitization share aspects of the same molecular cascade in Aplysia. Cold Spring Harbor Symposium on Quantitative Biology 2:821–30. [TWA]10.1101/SQB.1983.048.01.085CrossRef Google Scholar

Kandel, E. R. & Schwartz, J. H. (1982) Molecular biology of learning: Modulation of transmitter release. Science 218:433–43. [aZX, TWA]10.1126/science.6289442CrossRef Google Scholar PubMed

Kaplan, J., Gerber, S., Bonneau, D., Rozet, J., Briard, M., Dufler, J., Munnich, A. & Frezal, J. (1991) Probable location of Usher type I gene on chromosome 14q by linkage with D14S13 (MLJ14 probe). Cytogenetics and Cell Genetics 58:1988. [aSPD]Google Scholar

Karnik, S. S. & Khorana, H. C. (1990) Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. Journal of Biological Chemistry 265:17520–24. [aSPD]10.1016/S0021-9258(18)38195-XCrossRef Google Scholar PubMed

Kauer, J. A., Malenka, R. C. & Nicoll, R. A. (1988) NMDA application potentiates synaptic transmission in the hippocampus. Nature 334:250–52. [aZX]10.1038/334250a0CrossRef Google Scholar PubMed

Kaupp, U. B. (1991) The cyclic nucleotide-gated channels of vertebrate photoreccptors and olfactory epithelium. Trends in Neuroscience 14:150–57. [aRSM, DDO]10.1016/0166-2236(91)90087-BCrossRef Google Scholar PubMed

Kaupp, U. B. & Koch, K.-W. (1992) Role of cCMP and Ca2+ in vertebrate photoreceptor excitation and adaptation. Annual Review of Physiology 54:153–75. [aMDB, aRSM]10.1146/annurev.ph.54.030192.001101CrossRef Google Scholar

Kaupp, U. B., Niidoine, T., Tanabe, T., Terada, S., Bönigk, W., Stuhmer, W., Cook, N. J., Kangawa, K., Matsuo, H., Hirose, T., Miyata, T. & Numa, S. (1989) Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel. Nature 342:762–66. [aRSM, LWH, TGW]CrossRef Google Scholar PubMed

Kawaniura, S. (1983) Involvement of ATP in activation and inactivation sequence of phosphodicsterase in frog rod outer segments. Biochimica Biophysica Acta 732:276–81. [SK]10.1016/0005-2736(83)90212-2CrossRef Google Scholar

Kawaniura, S. (1992) Light-sensitivity modulating protein in frog rods. Photochemistry and Photohiology. 56:1173–80. [SK]10.1111/j.1751-1097.1992.tb09742.xCrossRef Google Scholar

Kawaniura, S. (1993) Rhodopsin phosphorylation as a mechanism of cyclic GMP phosphodiesterase regulation by S-modulin. Nature 362:855–57. [aMDB, aJBH, aRSM, SK, KT, AY]10.1038/362855a0CrossRef Google Scholar

Kawaniura, S. (1994) Photoreceptor light-adaptation mediated by S-modulin, a member of a possible regulatory protein family of protein phosphorylation in signal transduction. Neuroscience Research 20:293–98. [SK, KT]10.1016/0168-0102(94)90050-7CrossRef Google Scholar

Kawamura, S. & Bownds, M. D. (1981) Light adaptation of the cyclic GMP phosphodiesterase of frog photoreceptor membranes mediated by ATP and calcium ions. Journal of General Physiology 77:571–91. [aMDB]10.1085/jgp.77.5.571CrossRef Google Scholar

Kawamura, S., Cox, J. A. & Nef, P. (1994) Inhibition of rhodopsin phosphorylation by non-myristoylated recombinated recoverin. Biochemical and Biophysical Research Communications 203:121–27. [SK]10.1006/bbrc.1994.2157CrossRef Google Scholar

Kawamura, S., Hisatomi, O., Kayada, S., Tokunaga, F. & Kuo, C. H. (1993) Recoverin has S-modulin activity in frog rods. Journal of Biological Chemistry 268:14579–82. [aJBH, KT, AY]10.1016/S0021-9258(18)82369-9CrossRef Google Scholar PubMed

Kawamura, S. & Murakami, M. (1991) Calcium-dependent regulation of cyclic GMP phosphodiesterase by a protein from frog retinal rods. Nature 349:420–23. [aMDB, aJBH, JFM, SK, ASP, KT, AY]10.1038/349420a0CrossRef Google Scholar PubMed

Kawamura, S., Takamatsu, K. & Kitamura, K. (1992) Purification and characterization of S-modulin, a calcium-dependent regulator on cGMP phosphodiesterase in frog rod photoreceptors. Biochemical and Biophysical Research Communications 186:411–17. [aMDB, SK]10.1016/S0006-291X(05)80823-XCrossRef Google Scholar PubMed

Keen, T. J., Inglehearn, C. F., Lester, D. H., Bashir, R., Jay, M., Bird, A. C., Jay, B. & Bhattacharya, S. S. (1994) Autosomal dominant retinitis pigmentosa: Four new mutations in rhodopsin, one of them in the retinal attachment site. Genomics 11:199–205. [aSPD]10.1016/0888-7543(91)90119-YCrossRef Google Scholar

Khan, S. M. A., Bolen, W., Hargrave, P. A., Santoro, M. M. & McDowell, J. H. (1991) Differential scanning calorimetry of bovine rhodópsin in rod outer segment disk membranes. European Journal of Biochemisty 200:53–59. [aPAH]10.1111/j.1432-1033.1991.tb21047.xCrossRef Google Scholar PubMed

Khorana, H. G. (1992) Rhodopsin, photoreceptor of the rod cell: An emerging pattern for structure and function. Journal of Biological Chemistry 267:1–4. [aMDB, aPAH]10.1016/S0021-9258(18)48444-XCrossRef Google Scholar PubMed

Kim, R. Y., Al-Maghtheh, M., Fitzke, F. W., Arden, G. B., Jay, M., Bhattacharya, S. S. & Bird, A. C. (1993) Dominant retinitis pigmentosa associated with two rhodopsin gene mutations. Leu-40-Arg and an insertion disrupting the 5'-splice junction of exon 5. Archives of Ophthalmology 111:1518–24. [aSPD]10.1001/archopht.1993.01090110084030CrossRef Google Scholar

Kimberling, W. J., Moller, C. G., Davenport, S., Priluck, A., Beighton, P. H., Greenberg, J., Reardon, W., Weston, M. D., Kenyon, J. B., Grunkemeyer, J. A., Dahl, S. P., Overbeck, L. D., Blackwood, D. J., Brower, A. M., Hoover, D. M., Rowland, P. & Smith, R. J. H. (1992) Linkage of Usher syndrome type I gene (USH1B) to the long arm of chromosome 11. Genomics 14:988–94. [aSPD]10.1016/S0888-7543(05)80121-1CrossRef Google Scholar

Kimberling, W. J., Weston, M. D., Moller, C., Davenport, S. L. H., Shugart, Y. Y., Priluck, I. A., Martini, A., Milani, M. & Smith, R. J. (1990) Localization of Usher syndrome type II to chromosome lq. Genomics 7:245–49. [aSPD]10.1016/0888-7543(90)90546-7CrossRef Google Scholar

Kjelsberg, M. A., Cotecchia, S., Ostrowski, J., Caron, M. G. & Lelkowitz, R. J. (1992) Constitutive activation of the alpha-lB-adrenergic receptor by all amino acid substitutions at a single site: Evidence for a region which constrains receptor activation. Journal of Biological Chemistry 267:1430–33. [aPAH]10.1016/S0021-9258(18)45962-5CrossRef Google Scholar

Klann, E., Chen, S.-J. & Sweatt, J. D. (1991) Persistent protein kinase activation in the maintenance phase of long-term potentiation. Journal of Biological Chemistry 266:24253–56. [EDR]10.1016/S0021-9258(18)54221-6CrossRef Google Scholar PubMed

Klann, E., Chen, S.-J. & Sweatt, J. D. (1992) Increased phosphorylation of a 17-kDa protein kinase C substrate in long-term potentiation. Journal of Neurochemistry 58:1576–79. [EDR]10.1111/j.1471-4159.1992.tb11382.xCrossRef Google Scholar PubMed

Klann, E., Chen, S.-J. & Sweatt, J. D. (1993) Mechanism of protein kinase C activation during the induction and maintenance of long-term potentiation probe using a selective peptide substrate. Proceedings of the National Academy of Sciences USA 90:8337–41. [EDR]10.1073/pnas.90.18.8337CrossRef Google Scholar

Klausner, R. D. & Sitia, R. (1990) Protein degradation in the endoplasmic reticulum. Cell 62:611–14. [aSPD]10.1016/0092-8674(90)90104-MCrossRef Google Scholar PubMed

Knowles, J. A., Shugart, Y., Banerjee, P., Gilliam, T. C., Lewis, C. A., Jacobson, S. G. & Ott, J. (1994) Identification of a locus, distinct from RDS-peripherin, for autosomal recessive retinitis pigmeutosa on chromosome 6p. Human Molecular Genetics 3:1401–3. [rSPD]10.1093/hmg/3.8.1401CrossRef Google Scholar PubMed

Kobayashi, M., Takamatsu, K., Saitoh, S. & Noguchi, T. (1993) Myristoylation of hippocalcin is linked to its calcium-dependent membrane association properties. Journal of Biological Chemistry 268:18898–904. [KT]10.1016/S0021-9258(17)46711-1CrossRef Google Scholar PubMed

Kobayashi, M., Takamatsu, K., Saitoh, S., Miura, M. & Noguchi, T. (1992) Molecular cloning of hippocalcin, a novel calcium-binding protein of the recoverin family exclusively expressed in hippocampus. Biochemical and Biophysical Research Communications 189:511–17. [aJBH, KT]10.1016/0006-291X(92)91587-GCrossRef Google Scholar PubMed

Koch, K.-W. (1991) Purification and identification of photoreeeptor guanylate cyclase. Journal of Biological Chemistry 266:8634–37. [KWK]10.1016/S0021-9258(18)93021-8CrossRef Google Scholar PubMed

Koch, K.-W. (1992) Biochemical mechanism of light adaptation in vertebrate photoreceptors. Trends in Biochemical Science 17:307–11. [aMDB]10.1016/0968-0004(92)90442-CCrossRef Google Scholar PubMed

Koch, K.-W. (1994) Calcium as modulator of phototransduction in vertebrate photoreceptor cells. Reviews of Physiology, Biochemistry and Pharmacology 125:149–92. [KWK]Google Scholar PubMed

Koch, K.-W., Eckstein, F. & Stryer, L. (1990) Stereochemical course of the reaction catalyzed by guanylate cyclase from bovine retinal rod outer segments. Journal of Biological Chemistry 265:9659–63. [KWK]10.1016/S0021-9258(19)38720-4CrossRef Google Scholar PubMed

Koch, K.-W. & Kaupp, U. B. (1985) Cyclic GMP directly regulates a cationic conductance in membranes of bovine rods by a cooperative mechanism. Journal of Biological Chemistry 260:6788–6800. [aRSM, TGW]10.1016/S0021-9258(18)88849-4CrossRef Google Scholar PubMed

Koch, K.-W. & Stryer, L. (1988) Highly cooperative feedback control of retinal rod guanylate cyclase by calcium ions. Nature 334:64–66. [arMDB, aJBH, aRSM]10.1038/334064a0CrossRef Google Scholar PubMed

Kohn, H. (1980) Light-and GTP-regulated interaction of CTPase and other proteins with bovine photoreceptor membranes. Nature 283:587–89. [aPAH]10.1038/283587a0CrossRef Google Scholar

Kohn, H. & McDowell, J. H. (1977) Isoelectric focusing of phosphorylated cattle rhodopsin. Biophysics of Structure and Mechanism 3:199–203. [aPAH]10.1007/BF00535820CrossRef Google Scholar

Kohnken, R. E., Chafouleas, J. G., Eadie, D. M., Means, A. R. & McConnell, D. G. (1981) Calmodulin in bovine rod outer segments. Journal of Biological Chemistry 256:12517–22. [aRSM]10.1016/S0021-9258(18)43305-4CrossRef Google Scholar PubMed

Kokame, K., Fukada, Y., Yoshizawa, T., Takao, T. & Shimonishi, Y. (1992) Lipid modification at the N terminus of photoreceptor G-protein α-subunit. Nature 359:749–52. [KS]10.1038/359749a0CrossRef Google Scholar

Konig, B., Arendt, A., McDowell, J. H., Kahlert, M., Hargrave, P. A. & Hofmann, K. P. (1989) Three cytoplasmic loops of rhodopsin interact with transducin. Proceedings of the National Academy of Sciences USA 86:6878–82. [aSPD, aPAH, EAD]10.1073/pnas.86.18.6878CrossRef Google Scholar PubMed

Korenbrot, J. I., Brown, D. T. & Cone, R. A. (1973) Membrane characteristics and osmotic behavior of isolated rod outer segments. Journal of Cell Biology 56:389–98. [aMDB]10.1083/jcb.56.2.389CrossRef Google Scholar PubMed

Koutalos, Y., Nakatani, L. & Yau, K.-W. (1994) Modulation of the cGMP-gated channel of retinal rods by Ca2+. Investigative Ophthalmology and Visual Science [Abstract 1023] 35:1474. [HRM, rRSM]Google Scholar

Koutalos, Y. & Yau, K.-W. (1993) A rich complexity emerges in phototransduction. Current Opinion in Neurobiology 3:513–19. [aMDB]10.1016/0959-4388(93)90049-5CrossRef Google Scholar PubMed

Kramer, R. H. & Siegelbaum, S. A. (1992) Intracellular Ca2+ regulates the sensitivity of cyclic nucleotide-gated channels in olfactory receptor neurons. Neuron 9:897–906. [aRSM, MSS]10.1016/0896-6273(92)90242-6CrossRef Google Scholar PubMed

Kranich, H., Bartkowski, S., Denton, M. J., Krey, S., Dickinson, P., Duvigneau, C. & Gal, A. (1993) Autosotnal dominant “sector” retinitis pigmentosa due to a point mutation predicting an Asn-15-Ser substitution of rhodopsin. Human Molecular Genetics 2:813–14. [aSPD]10.1093/hmg/2.6.813CrossRef Google Scholar PubMed

Krebs, E. G. & Beavo, J. A (1979) Phosphorylation-dephosphorylation of enzymes. Annual Review of Biochemistry 48:923–59. [aZX]10.1146/annurev.bi.48.070179.004423CrossRef Google Scholar PubMed

Kremer, H., Pinckers, A., van den Helm, B., Deutman, A. F., Ropers, H. H. & Mariman, E. C. M. (1994) Localization of the gene for dominant cystoid macular dystrophy on chromosome 7p. Human Molecular Genetics 3:299–302. [aSPD]10.1093/hmg/3.2.299CrossRef Google Scholar PubMed

Krug, M., Lossner, B. & Ott, T. (1984) Anisomycin blocks the late phase of long-term potentiation in the dentate gyrus of freely moving rats. Brain Research Bulletin 13:39–42. [aZX]10.1016/0361-9230(84)90005-4CrossRef Google Scholar PubMed

Krupinski, J., Coussen, F., Bakalyar, H. A., Tang, W. J., Feinstein, P. G., Orth, K., Slaughter, C., Reed, R. R. & Gilman, A. G. (1989) Adenylyl cyclase amino acid sequence: Possible channel- or transporter-like structure. Science 244:1558–64. [aZX]10.1126/science.2472670CrossRef Google Scholar PubMed

Krupnick, J. G., Gurevich, V. V., Schepers, T., Hamm, H. E. & Benovic, J. L. (1994) Arrestin-rhodopsin interaction: Multi-site binding delineated by peptide inhibition. Journal of Biological Chemistry 269:3226–32. [ADA]10.1016/S0021-9258(17)41852-7CrossRef Google Scholar PubMed

Kühlbrandt, W. (1984) Three-dimensional structure of the light-harvesting chlorophyl a/b-protein complex. Nature 307:478–80. [aPAH]10.1038/307478a0CrossRef Google Scholar

Kühlbrandt, W. (1988) Three-dimensional crystallization of membrane proteins. Quarterly Reviews of Biophysics 21:429–77. [aPAH, RMG]10.1017/S0033583500004625CrossRef Google Scholar PubMed

Kühlbrandt, W. (1992) Two-dimensional crystallization of membrane proteins. Quarterly Reviews of Biophysics 25:1–49. [aPAH, RMG]10.1017/S0033583500004716CrossRef Google Scholar PubMed

Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. (1994) Atomic model of plant light-harvesting complex by electron crystallography. Nature 367:614–21. [aPAH, RMG]10.1038/367614a0CrossRef Google Scholar PubMed

Kuhn, H. (1980) Light- and CTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes. Nature 283:587–89. [AY]10.1038/283587a0CrossRef Google Scholar

Kumar, V. D. & Weber, I. T. (1992) Molecular model of the cyclic GMP-binding domain of the cyclic GMP-gated ion channel. Biochemistry 31:4643–49. [RLB]10.1021/bi00134a015CrossRef Google Scholar PubMed

Kumar-Singh, R., Farrar, G. J., Mansergh, F., Kenna, P., Bhattacharya, S., Gal, S. & Humphries, P. (1993) Exclusion of the involvement of all known retinitis pigmentosa loci in the disease present in a family of Irish origin provides evidence for a sixth autosomal dominant locus (RP8). Human Molecular Genetics 2:875–78. [aSPD]10.1093/hmg/2.7.875CrossRef Google Scholar

Kure, S., Tominago, T., Yoshimoto, T., Tada, K. & Narisawa, K. (1991) Glutamate triggers internucleosomal DNA cleavage in neuronal cells. Biochemical and Biophysical Research Communications 179:39–45. [MT]10.1016/0006-291X(91)91330-FCrossRef Google Scholar PubMed

Kutuzov, M. & Pfister, C. (1994) Activation of the retinal cGMP-specific phosphodiesterase by the GDP-loaded α-subunit of transducin. European Journal of Biochemistry 220:963–71. [rMDB]10.1111/j.1432-1033.1994.tb18700.xCrossRef Google Scholar PubMed

Lagnado, L. & Baylor, D. (1992) Signal flow in visual transduction. Neuron 8:995–1002. [aMDB, aJBH]10.1016/0896-6273(92)90122-TCrossRef Google Scholar PubMed

Lagnado, L. & Baylor, D. (1994) Calcium controls light-triggered formation of catalytically active rhodopsin. Nature 367:273–77. [aMDB, RKC, MPG-K, SK, MSS, KT]10.1038/367273a0CrossRef Google Scholar PubMed

Lagnado, L., Cervetto, L. & McNaughton, P. (1992) Calcium homeostasis in the outer segment of retinal rods from the tiger salamander. Journal of Physiology (London) 455:111–42. [aMDB, KWK]10.1113/jphysiol.1992.sp019293CrossRef Google Scholar PubMed

Lagnado, L. & McNaughton, P. A. (1990) Electrogenic properties of the Na:Ca exchange. Journal of Membrane Biology 113:177–91. [PPMS]10.1007/BF01870070CrossRef Google Scholar PubMed

Lakshmi, K. V., Auger, M., Raap, J., Lugtenburg, J., Griffin, R. G., & Herzfeld, J. (1993) Solid-state 13C NMR rotational resonance distance measurement in the M photointermediate of bacteriorhodopsin: Determination of the configuration about the Schiff base. Biophysics Journal 64:A212. [SOS]Google Scholar

Lamb, T. D. (1984) Effects of temperature changes on toad rod photocurrents. Journal of Physiology (London) 346:557–78. [aMDB]10.1113/jphysiol.1984.sp015041CrossRef Google Scholar PubMed

Lamb, T. D. (1990) Dark adaptation: A re-examination. In: Night vision: Basic, clinical and applied aspects, ed. Hess, R. F., Sharp, L. T. & Nordby, K.. Cambridge University Press. [RKC]Google Scholar

Lamb, T. D., Matthews, H. R. & Torre, V. (1986) Incorporation of calcium buffers into salamander retinal rods: A rejection of the calcium hypothesis of phototransduction. Journal of Physiology (London) 372:315–49. [aMDB]10.1113/jphysiol.1986.sp016011CrossRef Google Scholar PubMed

Lamb, T. D., McNaughton, P. A. & Yau, K.-W. (1981) Spatial spread of activation and background desensitization in toad rod outer segments. Journal of Physiology (London) 319:463–96. [aMDB]10.1113/jphysiol.1981.sp013921CrossRef Google Scholar PubMed

Lamb, T. D. & Pugh, E. N. Jr (1992) A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors. Journal of Physiology (London) 449:719–58. [aMDB]10.1113/jphysiol.1992.sp019111CrossRef Google Scholar PubMed

Lamba, O. P., Borchman, D. & O'Brien, P. J. (1994) Fourier transform infrared study of the rod outer segment disk and plasma membranes of vertebrate retina. Biochemistry 33:1704–12. [ADA]10.1021/bi00173a012CrossRef Google Scholar PubMed

Lambrecht, H. G. & Koch, K.-W. (1991) A 26 kd calcium binding protein from bovine rod outer segments as modulator of photoreceptor guanylate cyclase. EMBO Journal 10:793–98. [aMDB, aJBH, ASP]10.1002/j.1460-2075.1991.tb08011.xCrossRef Google Scholar PubMed

Lambrecht, H. G. & Koch, K.-W. (1992) Recoverin, a novel calcium-binding protein from vertebrate photoreceptors. Biochimica et Biophysica Acta 1160:63–66. [aJBH]10.1016/0167-4838(92)90038-FCrossRef Google Scholar PubMed

Lambright, D. G., Noel, J. P., Hamm, H. E. & Sigler, P. B. (1994) Structural determinants for activation of the alpha subunit of a heterotrimeric G protein. Nature 369:621–28. [aMDB, EAD]10.1038/369621a0CrossRef Google Scholar PubMed

Lee, R. H., Brown, B. M. & Lolley, R. N. (1984) Light-induced dephosphorylation of a 33K protein in rod outer segments of rat retina. Biochemistry 23:1972–77. [BMW]10.1021/bi00304a014CrossRef Google Scholar PubMed

Lee, R. H., Brown, B. M. & Lolley, R. N. (1990) Protein kinase A phosphorylates retinal phosducin on serine 73 in situ. Journal of Biological Chemistry 265:15860–66. [BMW]10.1016/S0021-9258(18)55478-8CrossRef Google Scholar PubMed

Lee, R. H., Fowler, A., McCinnis, J. F., Lolley, R. N. & Craft, C. M. (1990a) Amino acid and cDNA sequence of bovine phosducin, a soluble phosphoprotein from photoreceptor cells. Journal of Biological Chemistry 265:15867–73. [aMDB]10.1016/S0021-9258(18)55479-XCrossRef Google Scholar PubMed

Lee, R. H., Lieberman, B. S. & Lolley, R. N. (1987) A novel complex from bovine visual cells of a 33,000-dalton phosphoprotein with beta and gamma transducin: Purification and subunit structure. Biochemistry 28:3983–90. [aMDB]10.1021/bi00387a036CrossRef Google Scholar

Lee, R. H., Lieberman, B. S. & Lolley, R. N. (1990b) Retinal accumulation of the phosducin/Tgamma and transducin complexes in developing normal mice and in mice and dogs with inherited retinal degeneration. Experimental Eye Research 51:325–33. [aMDB]10.1016/0014-4835(90)90029-TCrossRef Google Scholar

Lee, R. H., Ting, T. D., Lieberman, B. S., Tobias, D. E., Lolley, R. N. & Ho, Y.-K. (1992) Regulation of retinal cGMP cascade by phosducin in bovine rod photoreceptor cells. Journal of Biological Chemistry 267:25104–12. [BMW]10.1016/S0021-9258(19)74012-5CrossRef Google Scholar PubMed

Lee, R. H., Whelan, J. P., Lolley, R. N. & McGinnis, J. F. (1988) The photoreceptor-specific 33 kDa phosphoprotein of mammalian retina: Generation of monospecific antibodies and localization by immunocytochemistry. Experimental Eye Research 46:829–40. ]aMDB]10.1016/S0014-4835(88)80035-6CrossRef Google Scholar PubMed

Lee, S. M. & Bressler, R. (1981) Prevention of diabetic nephropathy by diet control in the db/db mouse. Diabetes 30:106–11. [DW]10.2337/diab.30.2.106CrossRef Google Scholar PubMed

Leibrock, C. S., Reuter, T. & Lamb, T. D. (1994) Dark adaptation of toad rod photorcceptors following small bleaches. Vision Research 34:2787–2800. [rMDB]10.1016/0042-6989(94)90048-5CrossRef Google Scholar PubMed

Lenz, S. E., Henschel, Y., Zopf, D., Voss, B. & Gundelfinger, E. D. (1992) VILIP, a cognate protein of the retinal calcium binding proteins visinin and recoverin, is expressed in the developing chicken brain. Brain Research 15:133–40. [aJBH]Google Scholar PubMed

Levin, L. R., Han, P. L., Hwang, P. M., Feinstein, P. C., Davis, R. L. & Reed, R. R. (1992) The Drosophila learning and memory gene rutabaga encodes a Ca2+/calmodulin-responsive adenylyl cyclase. Cell 68:479–89. [aZX, TWA]10.1016/0092-8674(92)90185-FCrossRef Google Scholar PubMed

Levine, M. A., Modi, W. S. & O'Brien, S. J. (1990) Chromosomal localization of the genes encoding two forms of the G protein β polypeptide, β1 and β3, in man. Genomics 8:380–86. [aSPD]10.1016/0888-7543(90)90296-7CrossRef Google Scholar

Lewis, R. A., Otterud, B., Stauffer, D., Lalouel, J.-M. & Leppert, M. (1990) Mapping recessive ophthalmic diseases: Linkage of the locus for Usher syndrome type III to a DNA marker on chromosome lq. Genomics 7:250–56. [aSPD]10.1016/0888-7543(90)90547-8CrossRef Google Scholar

Li, H., Volpp, K. & Applebury, M. L. (1990) Bovine cone photoreceptor cGMP phosphodiesterase structure deduced from a cDNA clone. Proceedings of the National Academy of Sciences USA 87:293–97. [aMDB]10.1073/pnas.87.1.293CrossRef Google Scholar PubMed

Liang, C.-J., Yamashita, K., Muellenberg, C. G., Shichi, H. & Kobata, A. (1979) Structure of the carbohydrate moieties of bovine rhodopsin. Journal of Biological Chemistry 254:6414–18. [aPAH]10.1016/S0021-9258(18)50382-3CrossRef Google Scholar PubMed

Liebman, P. A. & Entine, G. (1968) Visual pigments of frog and tadpole. Vision Research 8:761–75. [aMDB]10.1016/0042-6989(68)90128-4CrossRef Google Scholar PubMed

Liebman, P. A., Parker, K. R. & Dratz, E. A. (1987) The molecular mechanism of visual excitation and its relation to the structure and composition of the rod outer segment. Annual Review of Physiology 491:765–91. [aMDB, aPAH]10.1146/annurev.ph.49.030187.004001CrossRef Google Scholar

Liebman, P. A. & Pugh, E. N. (1979) The control of phosphodiesterase in rod disk membranes: Kinetics, possible mechanisms and significance for vision. Vision Research 19:375–80. [aMDB]10.1016/0042-6989(79)90097-XCrossRef Google Scholar PubMed

Liebman, P. A. & Pugh, E. N. (1980) ATP mediates rapid reversal of cyclic GMP phosphodiesterase activation in visual receptor membranes. Nature 287:734–37. [aMDB]10.1038/287734a0CrossRef Google Scholar PubMed

Light, D. B., Corbin, J. D. & Stanton, B. A. (1990) Dualion-channel regulation by cyclic GMP and cyclic GMP-dependent protein kinase. Nature 344:336–39. [aRSM]10.1038/344336a0CrossRef Google Scholar PubMed

Liman, E. R. & Buck, L. B. (1994) A second subunit of the olfactory cyclic nucleotide-gated channel confers high sensitivity to cAMP. Neuron 13:611–21. [rRSM]10.1016/0896-6273(94)90029-9CrossRef Google Scholar

Linden, D. J. & Routtceberg, A. (1989) The role of protein kinase C in longterm potentiation: A testable model. Brain Research Reviews 14:279–96. [aZX]10.1016/0165-0173(89)90004-0CrossRef Google Scholar

Litman, B. J. (1982) Purification of rhodopsin by concanavalin A affinity chromatography. Methods in Enzymology 81:150–53. [aPAH]10.1016/S0076-6879(82)81025-2CrossRef Google Scholar PubMed

Litman, B. J., Aton, B. & Hartley, J. B. (1982) Functional domains of rhodopsin. Vision Research 22:1439–42. [ADA]10.1016/0042-6989(82)90206-1CrossRef Google Scholar PubMed

Liu, M., Chen, T.-Y., Ahamed, B., Li, J. & Yau, K.-W. (1994) Calciumcalmodulin modulation of the olfactory cyclic nucleotide-gated cation channel. Science 266:1348–54. [rRSM]10.1126/science.266.5189.1348CrossRef Google Scholar

Liu, Y. L. & Storm, D. R. (1989) Dephosphorylation of neuromodulin by calcineurin. Journal of Biological Chemistry 264:12800–4. [aZX]10.1016/S0021-9258(18)51557-XCrossRef Google Scholar PubMed

Liu, Y. L. & Storm, D. R. (1990) Regulation of free calmodulin levels in neurons by neuromodulin: Relationship to neuron growth and regeneration. Trends in Pharmacological Sciences 11:107–11. [aZX]Google Scholar

Livingston, M. S. (1985) Genetic dissection of Drosophila adenylyl cyclase. Proceedings of the National Academy of Sciences USA 82:5992–96. [aZX]10.1073/pnas.82.17.5992CrossRef Google Scholar

Livingston, M. S., Sziber, P. P. & Quinn, W. G. (1984). Loss of calcium/calmodulin responsiveness in adenylyl cyclase of rutabaga, a Drosophila learning mutant. Cell 37:205–15. [aZX, TWA]10.1016/0092-8674(84)90316-7CrossRef Google Scholar

Lolley, R. N., Farber, D. B., Rayborn, M. E. & Hollyfield, J. G. (1977) Cyclic GMP accumulation causes degeneration of photoreceptor cells: Simulation of an inherited disease. Science 196:664–66. [aSPD]10.1126/science.193183CrossRef Google Scholar PubMed

Lolley, R. N., Rong, H. & Craft, C. M. (1994) Linkage of photoreceptor degeneration by apoptosis with inherited defect in phototransduction. Investigative Ophthalmology and Visual Science 35:358–62. [aSPD]Google Scholar PubMed

Ludwig, J., Marglit, T., Eismann, E., Lancet, D. & Kaupp, U. B. (1990) Primary structure of a cAMP-gated channel from bovine olfactory epithelium. FEBS Letters 270:24–29. [aRSM]10.1016/0014-5793(90)81226-ECrossRef Google Scholar PubMed

Lyness, A. L., Ernst, W., Quinlan, M. P., Clover, G. M., Arden, G. B., Carter, R. M., Bird, A. C. & Parker, J. A. (1985) A clinical, psychophysical and electroretinographic survey of patients with autosomal dominant retinitis pigmentosa. British Journal of Ophthalmology 69:326–39. [aSPD]10.1136/bjo.69.5.326CrossRef Google Scholar PubMed

Macke, J. P., Davenport, C. M., Jacobson, S. G., Hennessey, J. C., Gonzales-Fernandez, F., Conway, B. P., Heckenlively, J., Palmer, R., Maumenee, I. H., Sieving, P., Gouras, P., Good, W. & Nathans, J. (1993) Identification of novel rhodopsin mutations responsible for retinitis pigmentosa: Implications for the structure and function of rhodopsin. American Journal of Human Genetics 53:80–89. [aSPD]Google Scholar PubMed

Mackler, S. A., Brooks, B. P. & Eberwine, J. H. (1992) Stimulus-induced coordinate changes in mRNA abundance in single postsynaptic hippocampal CA1 neurons. Neuron 9:539–48. [EDR]10.1016/0896-6273(92)90191-FCrossRef Google Scholar PubMed

MacNicol, M. & Schulman, H. (1992) Cross-talk between protein kinase C and multifunctional Ca2+/calmodulin-dependent protein kinase. Journal of Biological Chemistry 267:12197–201. [aZX]10.1016/S0021-9258(19)49824-4CrossRef Google Scholar PubMed

Madison, D. V., Malenka, R. C. & Nicoll, R. A. (1991) Mechanisms underlying long-term potentiation of synaptic transmission. Annual Review of Neuroscience 14:379–97. [TWA]10.1146/annurev.ne.14.030191.002115CrossRef Google Scholar PubMed

Malenka, R. C., Kauer, J. A., Perkel, D. J., Mauk, M. D., Kelly, P. T., Nicoll, R. A. & Waxham, M. N. (1989) An essential role for postsynaptic calmodulin and protein kinase activity in long-term potentiation. Nature 340:554–57. [TWA]10.1038/340554a0CrossRef Google Scholar PubMed

Malenka, R. C., Kauer, J. A., Zucker, R. S. & Nicoll, R. A. (1988) Postsynaptic calcium is sufficient for potentiation of hippocampal synaptic transmission. Science 242:81–84. [aZX]10.1126/science.2845577CrossRef Google Scholar PubMed

Malinow, R., Schulman, H. & Tsien, R. W. (1989) Inhibition of postsynaptic PKC or CaMKII blocks induction but not expression of LTP. Science 245:862–66. [TWA]10.1126/science.2549638CrossRef Google Scholar

Mangels, L. A. & Gnegy, M. E. (1990) Muscarinic receptor mediated transolocation of calmodulin in SK-N-SH human neuroblastoma cells. Molecular Pharmacology 37:820–26. [aZX]Google Scholar

Mangini, N. J., Gamer, G. L., Okajima, T.-L. L., Donoso, L. A. & Pepperberg, D. R. (1994) Effect of hydroxylamine on the subcellular distribution of arrestin (S-antigen) in rod photoreceptors. Visual Neuroscience 11:561–68. [rMDB]10.1017/S0952523800002467CrossRef Google Scholar

Mangini, N. J. & Pepperberg, D. R. (1988) Immunolocalization of 48K in rod photoreceptors: Light and ATP increase OS labeling. Investigative Ophthamology and Visual Science 29:1221–34. [JFM]Google Scholar PubMed

Mariuzza, R. A., Phillips, S. E. V. & Poljak, R. J. (1987) The structural basis of antigen-antibody recognition. Annual Review of Biophysics and Biophysical Chemistry 16:139–59. [aPAH]10.1146/annurev.bb.16.060187.001035CrossRef Google Scholar PubMed

Massof, R. W. & Finkelstein, D. (1981) Two forms of autosomal dominant primary retinitis pigmentosa. Documenta Ophthalmologica 51:289–346. [aSPD]10.1007/BF00143336CrossRef Google Scholar PubMed

Matesic, D. & Liebman, P. A. (1987) cGMP-dependent cation channel of retinal rod outer segments. Nature 326:600–3. [uRSM]10.1038/326600a0CrossRef Google Scholar PubMed

Matsuoka, S., Nicoll, D. A., Reilly, R. F., Hilgemann, D. W. & Philipson, K. D. (1993) Initial localization of regulatory regions of the cardiac sarcolemmal Na+-Ca2+ exchanger. Proceedings of the National Academy of Sciences USA 90:3870–74. [PPMS]10.1073/pnas.90.9.3870CrossRef Google Scholar PubMed

Matthews, G. (1986) Spread of the light response along the rod outer segment: An estimate from patch-clamp recordings. Vision Research 26:535–41. [aMDB]10.1016/0042-6989(86)90002-7CrossRef Google Scholar PubMed

Matthews, H. R. (1992a) Effects of lowered cytoplasmic calcium concentration and light on the responses of rod photoreceptors isolated from the retina of the tiger salamander. Journal of Physiology 446:109 p.[HRM]Google Scholar

Matthews, H. R. (1992b) Inability of light to accelerate the dim flash response without lowered calcium concentration in rod photoreceptors isolated from the retina of the tiger salamander. Journal of Physiology 44:559 p.[HRM]Google Scholar

Matthews, H. R. (in press) Effects of lowered cytoplasmic calcium concentration and light on the responses of salamander rod photoreceptors. Journal of Physiology. [HRM]Google Scholar

Matthews, H. R., Murphy, R. L. W., Fain, G. L. & Lamb, T. D. (1988) Photoreceptor light adaptation is mediated by cytoplasmic calcium concentration. Nature 334:67–69. [aMDB, aRSM, KWK, HRM]10.1038/334067a0CrossRef Google Scholar PubMed

Matthies, H., Frey, U., Reymann, K., Krug, M., Jork, R. & Schroeder, H. (1990) Different mechanisms and multiple stages of LTP. Advances in Experimental Medical Biology 268:359–68. [aZX]10.1007/978-1-4684-5769-8_39CrossRef Google Scholar PubMed

May, D., Ross, E., Gilman, A. & Smigel, M. (1985). Reconstitution of catecholamine-stimulatcd adenylate cyclase activity using three purified proteins. Journal of Biological Chemistry 260:15829–33. [aZX]10.1016/S0021-9258(17)36333-0CrossRef Google Scholar PubMed

McCarthy, S. T., Younger, J. P. & Owen, W. G. (1993) Disc structure, buffering and kinetics of cytosolic free calcium in bullfrog rod outer segments. Investigative Ophthalmology and Visual Science 34:1327. [aMDB]Google Scholar

McCarthy, S. T., Younger, J. P. & Owen, W. G. (1994) Free calcium concentrations in bulfrog rods determined in the presence of multiple forms of Fura-2. Biophysics Journal 67:2076–89. [rMDB]10.1016/S0006-3495(94)80691-5CrossRef Google Scholar

McDowell, J. H. (1993) Preparing rod outer segment membranes, regenerating, and determining rhodopsin concentration. In: Photoreceptor cells, ed. Hargrave, P. A.. Academic Press. [aPAH]Google Scholar

McDowell, J. H., Khan, S. M. A., Bolen, D. W., Santoro, M. M. & Hargrave, P. A. (1992) Structural stability of rhodopsin and opsin studied by differential scanning calorimetry. In: Signal transduction in photoreceptor cells, ed. Hargrave, P. A., Hofmann, K. P. & Kaupp, U. B.. Springer-Verlag. [aPAH]Google Scholar

McDowell, J. H., Nawrocki, J. P. & Hargrave, P. A. (1993) Phosphorylation sites in bovine rhodopsin. Biochemistry 32:4968–74. [aMDB]10.1021/bi00069a036CrossRef Google Scholar PubMed

McFall-Ngai, M. J. & Horwitz, J. (1990) A comparative study of the thermal stability of the vertebrate eye lens: Antarctic ice fish to the desert iguana. Experimental Eye Research 50:703–9. [aPAH]10.1016/0014-4835(90)90117-DCrossRef Google Scholar

McGee, T. L., Berson, E. L. & Dryja, T. P. (1992) Search for point mutations in the interstitial retinoid binding protein gene in patients with hereditary retinal degenerations. Investigative Ophthalmology and Visual Science 33:1396. [aSPD]Google Scholar

McCee, T. L., Lin, D., Berson, E. L. & Dryja, T. P. (1994) Defects in the rod cGMP-gated gene in patients with retinits pigmentosa. Investigative Ophthalmology and Visual Science 35:1716. [aSPD]Google Scholar

McGinnis, J. F., Austin, B. J., Klisak, I., Heinzmann, C., Kojis, J., Sparkes, R. S., Bateman, B. J. & Lerious, V. (1995) Chromosomal assignment of the human gene for the cancer associated retinopathy protein (recoverin). Journal of Neuroscience Research 40:165–168. [JFM]10.1002/jnr.490400204CrossRef Google Scholar

McGinnis, J. F., Lerious, V., Pazik, J. & Elliott, R. W. (1993) Chromosomal assignment of the recoverin gene and cancer-associated retinopathy. Mammalian. Genome 4:43–45. [JFM]10.1007/BF00364662CrossRef Google Scholar PubMed

McGinnis, J. F. & Leveille, P. J. (1985) Soluble proteins associated with photoreceptor cell death in the rd mouse. Current Eye Research 4:1127–35. [JFM]10.3109/02713688509003359CrossRef Google Scholar PubMed

McGinnis, J. F., Stepanik, P. L., Baehr, W., Subbaraya, I. & Lerious, V. (1992a) Cloning and sequencing of the 23 kDa mouse photoreceptor cellspecific protein. FEBS Letters 302:172–76. [JFM]10.1016/0014-5793(92)80433-HCrossRef Google Scholar

McGinnis, J. F., Whelan, J. P. & Donoso, L. A. (1992b) Transient, cyclic changes in mouse visual cell gene products during the light-dark cycle. Journal of Neuroscience Research 31:584–90. [JFM]10.1002/jnr.490310325CrossRef Google Scholar PubMed

McGuire, R. E., Sullivan, L. S., Blanton, S. H., Church, M., Heckenlively, J. R. & Daiger, S. P. (in press) X-linked dominant cone-rod dystrophy: Linkage mapping of a new locus (CORD3) to Xp22.13—p22.11. American Journal of Human Genetics. [rSPD]Google Scholar

McKusick, V. A. (1994) Mendelian inheritance in man, 11th ed. The Johns Hopkins University Press. [arSPD]Google Scholar

McLaughlin, M. E., Sandberg, M. A., Berson, E. L. & Dryja, T. P. (1993) Recessive mutations in the gene encoding the β-subunit of rod phosphodiesterase in patients with retinitis pigmentosa. Nature Genetics 4:130–34. [aSPD]10.1038/ng0693-130CrossRef Google Scholar PubMed

McNaughton, P. A. (1990) Light response of vertebrate photoreceptors. Physiological Reviews 70:847–84. [aMDB]10.1152/physrev.1990.70.3.847CrossRef Google Scholar PubMed

McWilliams, P., Farrar, G. J., Kenna, P., Bradley, D. G., Humphries, M. M., Sharp, E. M., McConnell, D. J., Lawler, M., Shiels, D., Ryan, C., Stephens, K., Daiger, S. P. & Humphries, P. (1989) Autosomal dominant retinitis pigmentosa (ADRP): Localization of an ADRP gene to the long arm of chromosome 3. Genomics 5:619–22. [aSPD]10.1016/0888-7543(89)90031-1CrossRef Google Scholar

Michel, H. (1982) Characterization and crystal packing of three-dimension bacteriorhodopsin crystals. EMBO Journal 1:1267–71. [RMG]10.1002/j.1460-2075.1982.tb00023.xCrossRef Google Scholar

Michel, H. (1991) General and practical aspects of membrane protein crystallization. In: Crystallization of membrane proteins, ed. Michel, H.. CRC Press. [aPAH]Google Scholar

Michel, H. & Oesterhelt, D. (1980) Three-dimensional srystals of membrane proteins: Bacteriorhodopsin. Proceedings of the National Academy of Sciences USA 77:1283–85. [RMG]10.1073/pnas.77.3.1283CrossRef Google Scholar

Milam, A. H., Dacey, D. M. & Dizhoor, A. M. (1992) Recoverin immunoreactivity in mammalian cone bipolar cells. Visual Neuroscience 10:1–12. [aJBH]10.1017/S0952523800003175CrossRef Google Scholar

Miljanich, G. P., Brown, M. F., Mabry-Gaud, S., Dratz, E. A. & Sturtevant, J. M. (1985) Thermotropic behavior of retinal rod membranes and dispersions of extracted phospholipids. Journal of Membrane Biology 85:79–86. [aPAH]10.1007/BF01872007CrossRef Google Scholar PubMed

Miller, C. (1989) Genetic manipulation of ion channels: A new approach to structure and mechanism. Neuron 2:1195–1205. [aRSM]10.1016/0896-6273(89)90304-8CrossRef Google Scholar PubMed

Miller, C. (1991) Annus mirabilis of potassium channels. Science 252:1092–96. [aRSM]10.1126/science.252.5009.1092CrossRef Google Scholar PubMed

Miller, J. L., Fox, D. A. & Litman, B. J. (1986) Amplification of phosphodiesterase activation is greatly reduced by rhodopsin phosphorylation. Journal of Biological Chemistry 25:4983–88. [aMDB]Google Scholar PubMed

Miller, J. L. & Korenbrot, J. I. (1993) In retinal cones, membrane depolarization in darkness activates the cGMP-dependent conductance. Journal of General Physiology 101:933–61. [KWK]10.1085/jgp.101.6.933CrossRef Google Scholar PubMed

Miller, K. R. & Jacobs, J. S. (1983) Two-dimensional crystals formed from photosynthetic reaction centers. Journal of Cell Biology 97:1266–70. [aPAH]10.1083/jcb.97.4.1266CrossRef Google Scholar PubMed

Min, K. C., Zvyaga, T. A., Cypess, A. M. & Sakmar, T. P. (1993) Characterization of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa: Mutations on the cytoplasmic surface affect transducin activation. Journal of Biological Chemistry 268:9400–4. [aSPD]10.1016/S0021-9258(18)98364-XCrossRef Google Scholar PubMed

Minocherhomjee, A. M., Selfe, S., Flowers, N. W. & Storm, D. R. (1987) Interaction between the catalytic subunit of the calmodulin sensitive adenylate cyclase with [¹²⁵I] and [¹²⁵I] calcodulin. Biochemistry 26:4444–48. [aZX]10.1021/bi00388a038CrossRef Google Scholar

Mitchell, D. C., Straume, M. & Litman, B. J. (1992) Role of sn-1-saturated, sn-2-polyunsaaturated phospholipids in control of membrane receptor conformational equilibrium: Effects of cholesterol and acyl chain unsaturation on the metarhodopsin I—Metarhodopsin II equilibrium. Biochemistry 31:662–70. [aPAH]10.1021/bi00118a005CrossRef Google Scholar

Mitchell, D. C., Straume, M., Miller, J. L. & Litman, B. J. (1990) Modulation of metarhodopsin formation by cholesterol-induced ordering of bilayer lipids. Biochemistry 29:9143. [ADA]10.1021/bi00491a007CrossRef Google Scholar PubMed

Mitchell, P. J. & Tjian, R. (1989) Transcriptional regulation in mammalian cells by sequence specific DNA binding proteins. Science 245:371–78. [aZX]10.1126/science.2667136CrossRef Google Scholar PubMed

Moench, S. J., Terry, C. E. & Dewey, T. G. (1994) Fluorescence labeling of the palmitoylation sites of rhodopsin. Biochemistry 33:5783–89. [ADA]10.1021/bi00185a016CrossRef Google Scholar PubMed

Molday, L. L., Cook, N. J., Kaupp, U. B. & Molday, R. S. (1990) The cGMP gated cation channel of bovine rod photoreceptor cells is associated with a 240 kDa protein exhibiting immunochemical cross-reactivity with spectrin. Journal of Biological Chemistry 265:18690–95. [aRSM, TGW]10.1016/S0021-9258(17)44807-1CrossRef Google Scholar PubMed

Molday, R. S. (1989) Monoclonal antibodies to rhodopsin and other proteins of rod outer segments. Progress in Retinal Research 8:173–209. [aPAH]10.1016/0278-4327(88)90025-9CrossRef Google Scholar

Molday, R. S. & Molday, L. L. (1987) Differences in the protein composition of bovine retinal rod outer segment disk and plasma membranes isolated by a ricin-gold-dextran density perturbation method. Journal of Cell Biology 105:2589–2601. [TGW]10.1083/jcb.105.6.2589CrossRef Google Scholar PubMed

Molday, R. S., Molday, L. L., Dose, A., Clark-Lewis, I., Illing, M., Cook, N. J., Eismann, E. & Kaupp, U. B. (1991) The cGMP-gated channel of the rod photoreceptor cell: Characterization and orientation of the amino terminus. Journal of Biological Chemistry 266:21917–22. [aRSM, RLH]10.1016/S0021-9258(18)54724-4CrossRef Google Scholar PubMed

Molday, R. S., Reid, D. M., Connell, G. & Molday, L. L. (1992) Molecular properties of the cGMP-gated channel of rod photoreceptor cells as probed with monoclonal antibodies. In: Signal transduction in photoreceptor cells, ed. Hargrave, P. A., Hofmann, K. P. & Kaupp, U. B.. Springer-Verlag. [aRSM]Google Scholar

Mollner, S. & Pfeuffer, T. (1988) Two different adenylyl cyclases in brain distinguished by monoclonal antibodies. European Journal of Biochemistry 171:265–71. [aZX]10.1111/j.1432-1033.1988.tb13785.xCrossRef Google Scholar PubMed

Mollner, S., Simmoteit, R., Palm, D. & Pfeuffer, T. (1991) Monoclonal antibodies against various forms of the adenylyl cyclase catalytic subunit and associated proteins. European Journal of Biochemistry 195:281–86. [aZX]10.1111/j.1432-1033.1991.tb15704.xCrossRef Google Scholar PubMed

Montarolo, P. G., Goelet, P., Castellucci, V. F., Morgan, J., Kandel, E. R. & Schacher, S. (1986) A critical period for macromolecular synthesis in long-term heterosynaptic facilitation in Aplysia. Science 234:1249–54. [aZX]10.1126/science.3775383CrossRef Google Scholar PubMed

Moore, A. T., Fitzke, F. W., Kemp, C. M., Arden, C. B., Keen, T. J., Inglehearn, C. F., Bhattacharya, S. S. & Bird, A. C. (1992) Abnormal dark adaptation kinetics in autosomal dominant sector retinitis pigmentosa due to rhodopsin mutation. British Journal of Ophthalmology 76:465–69. [aSPD]10.1136/bjo.76.8.465CrossRef Google Scholar

Morris, R. G. (1990) Toward a representational hypothesis of the role of hippocampal synaptic plasticity in spatial and other forms of learning. Cold Spring Harbor Symposium on Quantative Biology 50:161–73. [aZX]10.1101/SQB.1990.055.01.019CrossRef Google Scholar

Morris, R. G., Anderson, E., Lynch, C. S. & Baudry, M. (1986) Selective impairment of learning and blockade of long-term potentiation by an N-methyl-D-aspartate receptor antagonist, AP5. Nature 319:774–76. [aZX]10.1038/319774a0CrossRef Google Scholar PubMed

Morris, R. G., Garrud, P., Rawlins, J. N. & O'Keefe, J. (1982) Place navigation impaired in rats with hippocampal lesions. Nature 297:681–83. [aZX]10.1038/297681a0CrossRef Google Scholar PubMed

Mullen, R. J., Eicher, E. M. & Sidman, R. L. (1976) Purkinje cell degeneration, a new neurological mutation in the mouse. Proceedings of the National Academy of Sciences USA 73:208–12. [MWK]10.1073/pnas.73.1.208CrossRef Google Scholar PubMed

Musarella, M. A. (1992) Gene mapping of ocular diseases. Survey of Ophthalmology 36:285–312. [aSPD]10.1016/0039-6257(92)90096-CCrossRef Google Scholar PubMed

Musarella, M. A., Anson-Cartwright, L., Leal, S. M., Gilbert, L. D., Worton, R. G., Fishman, G. A. & Ott, J. (1990) Multipoint linkage analysis and heterogeneity testing in 20 X-linked retinitis pigmentosa families. Genomics 8:286–96. [aSPD]10.1016/0888-7543(90)90284-2CrossRef Google Scholar PubMed

Naash, M. I., Hollyfield, J. G., Al-Ubaidi, M. R. & Baehr, W. (1993) Simulation of human autosomal dominant retinitis pigmentosa in transgenic mice expressing a mutated murine opsin gene. Proceedings of the national Academy of Sciences USA 90:5499–5503. [MWK]10.1073/pnas.90.12.5499CrossRef Google Scholar PubMed

Nairn, A. C., Hemmings, H. C. & Greengard, P. (1985) Protein kinases in the brain. Animal Review of Biochemistry 54:931–76. [aZX]10.1146/annurev.bi.54.070185.004435CrossRef Google Scholar

Nakamura, T. & Gold, G. H. (1987) A cyclic nucleotide-gated conductance in olfactory receptor cilia. Nature 325:342–44. [aRSM]10.1038/325442a0CrossRef Google Scholar PubMed

Nakano, A., Terasawa, M., Watanabe, M., Usuda, N., Morita, T. & Hidaka, H. (1992) Neurocalcin, a novel calcium binding protein with three EF-hand domains, expressed in retinal amacrine cells and ganglion cells. Biochem, Biophys, Res.Commun. 186:1207–11. [aJBH]10.1016/S0006-291X(05)81534-7CrossRef Google Scholar PubMed

Nakatani, K., Koutalos, Y. & Yau, K.-W. (1995) Ca+2 modultion of the cGMP-dated channel of bullfrog retinal rod photoreceptors. Journal of Physiology 484:1:69–76. [MPC-K]10.1113/jphysiol.1995.sp020648CrossRef Google Scholar

Nakatani, K., Tamura, T. & Yau, K.-W. (1991) Light adaptation in retinal rods of the rabbit and two other nonprimate mammals. Journal of General Physiology 97:413–35. [aMDB, KWK]10.1085/jgp.97.3.413CrossRef Google Scholar PubMed

Nakatani, K. & Yau, K.-W. (1988a) Calcium and light adaptation in retinal rods and cones. Nature 334:69–71. [aMDB, KWK, HRM]10.1038/334069a0CrossRef Google Scholar PubMed

Nakatani, K. & Yau, K.-W. (1988b) Guanosine 3'-5'-cyclic monophosphate-activatcd conductance studied in a truncated rod outer segment of the toad. Journal of Physiology (London) 395:731–53. [aMDB]10.1113/jphysiol.1988.sp016943CrossRef Google Scholar

Nakazawa, M., Kikawa-Araki, E., Shiono, T. & Tamai, M. (1991) Analysis of rhodopsin gene in patients with retinitis pigmentosa using allele-specific polymerase chain reaction. Japanese Journal of Ophthalmology 35:386–93. [aSPD]Google Scholar PubMed

Näirfström, K. (1983) Hereditary progressive retinal atrophy in the Abyssinian cat. The Journal of Heredity 74:273–76. [MWK]10.1093/oxfordjournals.jhered.a109782CrossRef Google Scholar

Nathans, J. (1990) Determinants of visual pigment absorbance: Role of charged amino acids in the putative transmembrane segment. Biochemistry 29:937–42. [aPAH]10.1021/bi00456a013CrossRef Google Scholar

Nathans, J. (1992) Rhodopsin: Structure, function, and genetics. Biochemistry 31:4923–31. [aMDB, aSPD, aPAH]10.1021/bi00136a001CrossRef Google Scholar

Nathans, J., Maumenee, I. H., Zrenner, E., Sadowski, B., Sharpe, L. T., Lewis, R. A., Hansen, E., Rosenberg, T. et al. (1993) Genetic heterogeneity among blue-cone monochromats. American Journal of Human Genetics 53:987–1000. [aSPD]Google Scholar PubMed

Nathans, J., Merbs, S. L., Sung, C.-H., Weitz, C. J. & Wang, Y. (1992a) Molecular genetics of human visual pigments. Annual Review of Genetics 26:403–24. [aSPD]10.1146/annurev.ge.26.120192.002155CrossRef Google Scholar PubMed

Nathans, J., Weitz, C. J., Agarwal, N., Nir, I. & Papermaster, D. S. (1989) Production of bovine rhodopsin by mammalian cell lines expressing cluned cDNA: Spectrophotometry and subcellular localization. Vision Research 29:907–14. [aPAH]10.1016/0042-6989(89)90105-3CrossRef Google Scholar PubMed

Natsukari, N., Hanai, H., Matsunaga, T. & Fujita, M. (1990) Synergistic activation of brain adenylate cyclase by calmodulin, and either GTP or catecholamines including dopamine. Brain Research 534:170–76. [aZX]10.1016/0006-8993(90)90126-VCrossRef Google Scholar PubMed

Nawy, S. & Jahr, C. E. (1990) Suppression by glutamate of cGMP-activated conductance in retinal bipolar cells. Nature 346:269–71. [aRSM]10.1038/346269a0CrossRef Google Scholar PubMed

Nef, S., De Castro, E., Martone, M. E., Edelman, V. M., Ellisman, M. H., Fiumelli, H., Comte, M., Cox, J. A., Lenz, S. E., Kawamura, S. & Nef, P. (in press) Relgulation of receptor phosphorylation by a novel family of neuronal calcium sensors (NCS) and distribution of NCS-1 in the avian and rodent nervous systen. Neuron. [SK]Google Scholar

Nef, S., Fiumelli, H., De Castro, E., Raes, M. B. & Nef, P. (in press) Identification of a neuronal calcium sensor (NCS-1) possibly involved in the regulation of receptor phosphorylation. Journal of Receptor Research [KT]Google Scholar

Nei, M. (1987) Molecular evolutionary genetics. Columbia University Press. [aSPD]10.7312/nei-92038CrossRef Google Scholar

Nelson, R. B. & Routtenberg, A. (1985) Characterization of protein Fl: A kinase C substrate directly related to neural plasticity. Experimental Neurology 89:213–24. [aZX]10.1016/0014-4886(85)90277-8CrossRef Google Scholar

Nestler, E. J. & Greengard, P. (1983) Protein phosphorylation in the brain. Nature 305:583–88. [aZX]10.1038/305583a0CrossRef Google Scholar

Neubert, T. A., Johnson, R. S., Hurley, J. B. & Walsh, K. A. (1992) The rod transducin a subunit amino terminus is heterogeneously fatty acylated. Journal of Biological Chemistry 267:18274–77. [aMDB, aJBH, KS]10.1016/S0021-9258(19)36955-8CrossRef Google Scholar PubMed

Newton, A. C. & Williams, D. S. (1991) Involvement of protein kinase C in the phosphorylation of rhodopsin. Journal of Biological Chemistry 266:17725–28. [aMDB]10.1016/S0021-9258(18)55183-8CrossRef Google Scholar PubMed

Newton, A. C. & Williams, D. S. (1993) Rhodopsin is the major in situ substrate of protein kinase C in rod outer segments of photoreceptors. Journal of Biological Chemistry 268:18181–86. [aMDB]10.1016/S0021-9258(17)46827-XCrossRef Google Scholar PubMed

Nicol, G. D. & Bownds, M. D. (1989) Calcium regulates some, but not all, aspects of light adaptation in rod photoreceptors. Journal of General Physiology 94:233–59. [aMDB]10.1085/jgp.94.2.233CrossRef Google Scholar

Nicol, G. D., Kaupp, U. B. & Bownds, M. D. (1987) Transduction persists in rod photoreceptors after depletion of intracellular calcium. Journal of General Physiology 89:297–319. [aMDB]10.1085/jgp.89.2.297CrossRef Google Scholar PubMed

Nicoll, R. A., Kauer, J. A. & Malenka, R. C. (1988) The current excitement in long-term potentiation. Neuron 1:97–103. [aZX]10.1016/0896-6273(88)90193-6CrossRef Google Scholar PubMed

Nichols, B. E., Sheffield, V. C., Vandenburgh, K., Drack, A. V., Kimura, A. E. & Stone, E. M. (1993) Butterfly-shaped pigment dystrophy of the fovea caused by a point mutation in codon 167 of the RDS gene. Nature Genetics 3:202–6. [aSPD]10.1038/ng0393-202CrossRef Google Scholar PubMed

Niemeyer, G., Trub, P., Schinzel, A. & Gal, A. (1992) Clinical and ERG data in a family with autosomal dominant RP and Pro-347-Arg mutation in the rhodopsin gene. Documenta Ophthalmologica 79:303–11. [aSPD]10.1007/BF00160945CrossRef Google Scholar

Nigg, E. A., Hilz, H., Eppenberger, H. M. & Dutly, F. (1985) Rapid and reversible translocation of the catalytic subunit of cAMP-dependent protein kinase type II from the Golgi complex to the nucleus. EMBO Journal 4:2801–6. [aZX]10.1002/j.1460-2075.1985.tb04006.xCrossRef Google Scholar PubMed

Noel, J. P., Hamm, H. E. & Sigler, P. B. (1993) The 2.2 Å crystal structure of transducin- complexed with GTPgammaS. Nature 366:654–63. [aMDB, RKC, EAD]10.1038/366654a0CrossRef Google Scholar

Noro, Y., Ishiguro, S.-I. & Tamal, M. (1994) Accumulation of glutamate-like reactivity in the rds/rds mouse retina. Investigative Ophthalmology and Visual Science 35:1362. [MT]Google Scholar

Nussberger, S., Dörr, K., Wang, D. N. & Kühlbrandt, W. (1993) Lipid-protein interactions in crystals of plant light-harvesting complex. Journal of Molecular Biology 234:347–56. [RMG]10.1006/jmbi.1993.1591CrossRef Google Scholar PubMed

O'Brien, P. J., StJules, R. S., Reddy, T. S., Bazan, N. G. & Zatz, M. (1987) Acylation of disc membrane rhodopsin may be nonenzymatic. Journal of Biological Chemistry 262:5210–15. [aPAH]10.1016/S0021-9258(18)61175-5CrossRef Google Scholar PubMed

O'Brien, P. J. & Zatz, M. (1984) Acylation of bovine rhodopsin by [3H]palmitic acid. Journal of Biological Chemistry 259:5054–57. [aPAH]10.1016/S0021-9258(17)42954-1CrossRef Google Scholar

Ocorr, K. A., Walters, E. T. & Byrne, J. H. (1985) Associative conditioning analog selectively increases cAMP levels of tail sensory neurons in Aplysia. Proceedings of the National Academy of Sciences USA 82:2548–52. [TWA]10.1073/pnas.82.8.2548CrossRef Google Scholar PubMed

Ohguro, H., Fukada, Y., Takao, T., Shimonishi, Y., Yoshizawa, T. & Akino, T. (1991) Carboxyl methylation and farnesylation of transducin gammasubunit synergistically enhance its coupling with metarhodopsin II. EMBO Journal 10:3669–74. [aMDB]10.1002/j.1460-2075.1991.tb04934.xCrossRef Google Scholar

Ohguro, H., Palczewski, K., Ericsson, L. H., Walsh, K. A. & Johnson, R. S. (1993) Sequential phosphorylation of rhodopsin at multiple sites. Biochemistry 32:5718–24. [aMDB]10.1021/bi00072a030CrossRef Google Scholar PubMed

Okazaki, K., Watanabe, M., Ando, Y., Hagiwara, M., Terasawa, M. & Hidaka, H. (1992) Full sequence of neurocalcin, a novel calcium-binding protein abundant in central nervous system. Biochemical and Biophysical Research Communications 185:147–53. [aJBH]10.1016/S0006-291X(05)80968-4CrossRef Google Scholar PubMed

Oprian, D. D. (1992) The ligand-binding domain of rhodopsin and other G protein-linked receptors. Journal of Bioenergetics & Biomembranes 24:211–17. [aPAH]10.1007/BF00762679CrossRef Google Scholar PubMed

Oprian, D. D., Molday, R. S., Kaufman, R. J. & Khorana, H. G. (1987) Expression of a synthetic bovine rhodopsin gene in monkey kidney cells. Proceedings of the National Academy of Sciences USA 84:8874–78. [aPAH]10.1073/pnas.84.24.8874CrossRef Google Scholar PubMed

Orth, U., Samanns, C., Gusseck, H., Niemeyer, G., Ludwig, M., Meitinger, T., Schinzel, A., Schwinger, E. & Gal, A. (1991) Autosomal dominant hereditary retinopathia pigmentosa with genetic heterogeneity. Fortschritte der Opththalmologie. 88:455–59. [aSPD]Google Scholar PubMed

Ott, J., Bhattacharya, S. S., Chen, J. D., Denton, M. J., Donald, J., DuBay, C., Farrar, G. J., Fishman, G. A. et al. (1990) Localizing multiple X chromosome-linked retinitis pigmentosa loci using multilocus homogeneity tests. Proceedings of the National Academy of Sciences USA 87:701–4. [aSPD]10.1073/pnas.87.2.701CrossRef Google Scholar PubMed

Ovchinnikov, Y. A., Abdulaev, N. G. & Bogachuk, A. S. (1988) Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated. FEBS Letters 230:1–5. [aPAH]10.1016/0014-5793(88)80628-8CrossRef Google Scholar PubMed

Ovchinnikov, Y. A., Abdulaev, N. G., Zolotarev, A. S., Artamonov, I. D., Bespalov, I. A., Dergachev, A. E & Tsuda, M. (1988) Octopus rhodopsin: Amino acid sequence deduced from cDNA. FEBS Letters 232:69–72. [aPAH]10.1016/0014-5793(88)80388-0CrossRef Google Scholar PubMed

Pagés, F., Deterre, P. & Pfister, C. (1992) Enhanced GTPase activity of transducin when bound to cGMP phosphodiesterase in bovine retinal rods. Journal of Biological Chemistry 267:22018–21. [aMDB]10.1016/S0021-9258(18)41629-8CrossRef Google Scholar PubMed

Pagés, F., Deterre, P. & Pfister, C. (1993) Enhancement by phosphodiesterase subunits of the rate of GTP hydrolysis by transducin in bovine retinal rods. Essential role of the phosphodiesterase catalytic core. Journal of Biological Chemistry 268:26358–64. [arMDB, BMW]10.1016/S0021-9258(19)74323-3CrossRef Google Scholar PubMed

Palczewski, K., Buczylko, J., Kaplan, M. W., Polans, A. S. & Crabb, J. W. (1991) Mechanism of rhodopsin kinase activation. Journal of Biological Chemistry 266:12949–55. [aMDB]10.1016/S0021-9258(18)98787-9CrossRef Google Scholar PubMed

Palczewski, K., Jager, S., Buczylko, J., Crouch, R. K., Bredberg, D. L., Hofmann, K. P., Asson-Batres, M. A. & Saari, J. C. (1994) Rod outer segment retinol dehydrogenase: Substrate specificity and role in phototransduction. Biochemistry 38:13741–50. [RKC]10.1021/bi00250a027CrossRef Google Scholar

Palczewski, K., McDowell, J. H. & Hargrave, P.A. (1988a) Purification and characterization of rhodopsin kinase. Journal of Biological Chemistry 263:14067–73. [aMDB]10.1016/S0021-9258(18)68185-2CrossRef Google Scholar PubMed

Palczewski, K., McDowell, J. H. & Hargrave, P.A. (1988b) Rhodopsin kinase: Substrate specificity and factors that influence activity. Biochemistry 27:2306–12. [aMDB]10.1021/bi00407a010CrossRef Google Scholar PubMed

Palczewski, K., Rispoli, G. & Detwiler, P. B. (1992) The influence of arrestin (48K protein) and rhodopsin kinase on visual transduction. Neuron 8:117–26. [aMDB]10.1016/0896-6273(92)90113-RCrossRef Google Scholar PubMed

Palczewski, K., Subbaraya, I., Gorczyca, W. A., Helekar, B. S., Ruiz, C. C., Ohguro, H., Huang, J., Zhao, X., Crabb, J. W., Johnson, R. S., Walsh, K. A., Gray-Keller, M. P., Detwiler, P. B. & Baehr, W. (1994) Molecular cloning and characterization of retinal photoreceptor guanylyl cyclaseactivating protein. Neuron 13:395–404. [KS]10.1016/0896-6273(94)90355-7CrossRef Google Scholar

Papac, D. I., Oatis, J. E. Jr, Crouch, R. K. & Knapp, D. R. (1993) Mass spectrometric identification of phosphorylation sites in bleached bovine rhodopsin. Biochemistry 32:5930–34. [aMDB]10.1021/bi00074a002CrossRef Google Scholar PubMed

Papac, D. I., Thornburg, K. R., Bullesbach, E. E., Crouch, R. K. & Knapp, D. R. (1992) Palmitylation of a G-protein coupled receptor: Direct analysis by tandem mass spectrometry. Journal of Biological Chemistry 267:16889–94. [aPAH]10.1016/S0021-9258(18)41868-6CrossRef Google Scholar PubMed

Papermaster, D. S. & Dreyer, W. J. (1974) Rhodopsin content in the outer segment membranes of bovine and frog retinal rods. Biochemistry 13:2438–44. [aPAH]10.1021/bi00708a031CrossRef Google Scholar PubMed

Pearson, P. L., Matheson, N. W., Flescher, D. C., Robbins, F. J. (1992) The GDB[TM] human genome data base anno 1992. Nucleic Acids Research 20:2201–6. [aSPD]10.1093/nar/20.suppl.2201CrossRef Google Scholar PubMed

Peng, Y.-W., Robishaw, J. D., Levine, M. A. & Yau, K.-W. (1992) Retinal rods and cones have distinct G protein β and γ subunits. Proceedings of the National Academy of Sciences USA 89:10882–86. [aSPD]10.1073/pnas.89.22.10882CrossRef Google Scholar PubMed

Pepperberg, D. R., Cornwall, M. C., Kahlert, M., Hofmann, K. P., Jin, J., Jones, G. J. & Ripps, H. (1992) Light-dependent delay in the falling phase of the retinal rod photoresponse. Visual Neuroscience 8:9–18. [aMDB, RKC]10.1017/S0952523800006441CrossRef Google Scholar PubMed

Pepperberg, D. R., Jin, J. & Jones, G. J. (1994) Modulation of transduction gain in light adaptation of retinal rods. Visual Neuroscience 11:53–62. [aMDB, RKC]10.1017/S095252380001110XCrossRef Google Scholar PubMed

Perez-Sala, D., Tan, E. W., Canada, F. J. & Rando, R. R. (1991) Methylation and demethylation reactions of guanine nucleotide-binding proteins of retinal rod outer segments. Proceedings of the National Academy of Sciences USA 88:3043–46. [aMDB]10.1073/pnas.88.8.3043CrossRef Google Scholar PubMed

Perlman, J. I., Nodes, B. R. & Pepperberg, D. R. (1982) Utilization of retinoids in the bullfrog retina. Journal of General Physiology 80:885–913. [RKC]10.1085/jgp.80.6.885CrossRef Google Scholar PubMed

Pfenninger, K. H., Ellis, L., Johnson, M. P., Friedman, L. B. & Somlo, S. (1983) Nerve growth cones isolated from fetal rat brain: Subcellular fractionation and characterization. Cell 35:573–84. [aZX]10.1016/0092-8674(83)90191-5CrossRef Google Scholar PubMed

Pfister, C., Bennett, N., Bruckert, F., Catty, P., Clerc, A., Pagès, F. & Deterre, P. (1993) Interactions of a G-protein with its effector: Transducin and cGMP phosphodiesterase in retinal rods. Cellular Signalling 5:235–51. [aMDB]10.1016/0898-6568(93)90015-ECrossRef Google Scholar PubMed

Philip, N. J., Chang, W. & Long, K. (1987) Light-stimulated movement in rod photoreceptor cells of the rat retina. FEBS Letters 225:127–31. [JFM]10.1016/0014-5793(87)81144-4CrossRef Google Scholar

Phillips, W. J. & Cerione, R. A. (1994) A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation. Biochemical Journal 299(Pt 2):351–57. [ADA]10.1042/bj2990351CrossRef Google Scholar

Piascik, M. T., Piascik, M. F., Hitzemann, R. J. & Potter, J. D. (1981) Ca2+ -dependent regulation of rat caudate nucleus adenylate cyclase and effects on the response to dopamine. Mol Pharmacol. 20, 2: 319–25. [aZX]Google Scholar

Picones, A. & Korenbrot, J. I. (1992) Permeation and interaction of monovalent cations with the cGMP-gated channel of cone photoreceptors. Journal of Ceneral Physiology 100:647–73. [aRSM]10.1085/jgp.100.4.647CrossRef Google Scholar PubMed

Pistorius, A. M. & deGrip, W. J. (1994) Rhodopsin's secondary structure revisited: Assignment of structural elements. Biochemical and Biophysical Research Communications 3:1040–45. [ADA]10.1006/bbrc.1994.1148CrossRef Google Scholar

Pittler, S. J. & Baehr, W. (1991) Identification of a nonsense mutation in the rod photoreceptor cGMP phosphodiesterase β-subunit gene of the rd mouse. Proceedings of the National Academy of Sciences USA 88:8322–26. [aSPD, MWK]10.1073/pnas.88.19.8322CrossRef Google Scholar PubMed

Pittler, S. J., Keeler, C. E., Sidman, R. L. & Baehr, W. (1993) PCR analysis of DNA from 70-year-old sections of rodless retina demonstrates identity with the mouse rd defect. Proceedings of the National Academy of Sciences USA 90:9616–19. [aSPD]10.1073/pnas.90.20.9616CrossRef Google Scholar PubMed

Pittler, S. J., Lee, A. K., Altherr, M. R., Howard, T. A., Seldin, M. F., Hurwitz, R. L., Wasmuth, J. J. & Baehr, W. (1992) Primary structure and chromosomal localization of human and mouse rod photoreceptor cGMP-gated cation channel. Journal of Biological Chemistry 267:6257–62. [aRSM]10.1016/S0021-9258(18)42689-0CrossRef Google Scholar PubMed

Plantner, J. J., Le, M.-L. & Kean, E. L. (1991) Enzymatic deglycosylation of bovine rhodopsin. Experimental Eye Research 53:269–74. [aPAH]10.1016/0014-4835(91)90083-QCrossRef Google Scholar PubMed

Pober, J. S. & Stryer, L. (1975) Light dissociates enzymatically-cleaved rhodopsin into two different fragments. Journal of Molecular Biology 95:477–81. [rPAH]10.1016/0022-2836(75)90204-1CrossRef Google Scholar PubMed

Polans, A. S., Buczylko, J., Crabb, J. & Palczewski, K. (1991) A photoreceptor calcium binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy. Journal of Cell Biology 112:981–89. [aJBH, JFM, ASP]10.1083/jcb.112.5.981CrossRef Google Scholar PubMed

Polans, A. S., Burton, M. D., Haley, T. L., Crabb, J. W. & Palczewski, K. (1993) Recoverin, but not visinin, is an autoantigen in the human retina identified with a cancer-associated retinopathy. Investigative Ophthalmology and Visual Science 34:81–90. [aJBH, ASP]Google Scholar

Polans, A. S., Hermolin, J. & Bownds, M. D. (1979) Light-induced phosphorylation of two proteins in frog rod outer segments. Journal of General Physiology 74:595–613. [aMDB]10.1085/jgp.74.5.595CrossRef Google Scholar PubMed

Pongs, O., Lindemeier, J., Zhu, X. R., Theil, T., Engelkamp, D., Krah-Jentgens, I., Lambrecht, H. G., Koch, K. W., Schwemer, J., Rivosecchi, R., Mallart, A., Galceran, J., Canal, I., Barbas, J. A. & Ferrus, A. (1993) Frequenin: A novel calcium-binding protein that modulates synaptic efficacy in the Drosophila nervous system. Neuron 11:15–28. [KT]10.1016/0896-6273(93)90267-UCrossRef Google Scholar PubMed

Popova, J. S., Johnson, G. L. & Rasenick, M. M. (1994) Journal of Biological Chemistry 269:21748–54. [MMR]10.1016/S0021-9258(17)31868-9CrossRef Google Scholar

Poulain, C., Ferrus, A. & Mallart, A. (1994) Modulation of type A K+ current in Drosophila larval muscle by internal Ca2+; effects of the overexpression of frequenin. European Journal of Physiology 427:71–79. [KT]10.1007/BF00585944CrossRef Google Scholar

Probst, W. C., Snyder, L. A., Schuster, D. I., Brosius, J. & Sealfon, S. C. (1992) Sequence alignment of the G-protein coupled receptor superfamily. DNA and Cell Biology 11:1–20. [aPAH]10.1089/dna.1992.11.1CrossRef Google Scholar PubMed

Pugh, E. N. Jr & Lamb, T. D. (1990) Cyclic GMP and calcium: The internal messengers of excitation and adaptation in vertebrate photoreceptors. Vision Research 30:1923–48. [aMDB]10.1016/0042-6989(90)90013-BCrossRef Google Scholar PubMed

Pugh, E. N. Jr & Lamb, T. D. (1993) Amplification and kinetics of the activation steps in phototransduction. Biochimica et Biophysica Acta 1141:111–49. [aMDB, KWK]10.1016/0005-2728(93)90038-HCrossRef Google Scholar PubMed

Pullen, N., Brown, N. C., Sharma, R. P. & Akhtar, M. (1993) Cooperativity during multiple phosphorylations chatlyzed by rhodopsin kinase: Supporting evidence using synthetic phosphopeptides. Biochemistry 32:3958–64. [ADA]10.1021/bi00066a016CrossRef Google Scholar PubMed

Pulvermuller, A., Palczewski, K. & Hofmann, K. P. (1993) Interaction between photoaetivated rhodopsin and its kinase: Stability and kinetics of complex formation. Biochemistry 32:14082–88. [aMDB]10.1021/bi00214a002CrossRef Google Scholar PubMed

Quamme, G. A. & Rabkin, S. W. (1990) Cytosolic free magnesium in cardiac myocytes: Identification of a Mg2+ influx pathway. Biochemical and Biophysical Research Communications 167:1406–12. [RLH]10.1016/0006-291X(90)90679-HCrossRef Google Scholar PubMed

Radmacher, M., Fritz, M., Hansma, H. C. & Hansma, P. K. (1994) Direct observation of enzyme activity with the atomic force microscope. Science 265:1577–79. [ADA]10.1126/science.8079171CrossRef Google Scholar PubMed

Raju, B., Murphy, E., Levy, L. A., Hall, R. D. & London, R. E. (1989) A fluorescent indicator for measuring cytosolic free magnesium. American Journal of Physiology 256:C540–48. [RLH]10.1152/ajpcell.1989.256.3.C540CrossRef Google Scholar PubMed

Raleigh, D. P., Levitt, M. H. & Griffin, R. G. (1988) Rotational resonance in solid state NMR. Chemistry & Physics Letters 146:71–76. [SOS]10.1016/0009-2614(88)85051-6CrossRef Google Scholar

Rao, V. R., Cohen, G. B. & Oprian, D. D. (1994) Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature 367:639–42. [aSPD]10.1038/367639a0CrossRef Google Scholar

Ratan, R. R., Murphy, T. H. & Baraban, J. M. (1994) Oxidative stress induces apoptosis in embryonic cortical neurons. Journal of Neurochemistry 62:376–79. [MT]10.1046/j.1471-4159.1994.62010376.xCrossRef Google Scholar PubMed

Ratto, G. M., Payne, R., Owen, W. G. & Tsien, R. Y. (1988) The concentration of cytosolic free calcium in vertebrate rod outer segments measured with Fura-2. Journal of Neuroscience 8:3240–46. [aMDB]10.1523/JNEUROSCI.08-09-03240.1988CrossRef Google Scholar PubMed

Ray, S., Zozulya, S., Niemi, G. A. et al. (1992) Cloning, expression and crystallization of recoverin, a calcium sensor in vision. Proceedings of the National Academy of Sciences USA 89:5705–9. [aJBH]10.1073/pnas.89.13.5705CrossRef Google Scholar PubMed

Reig, C., Llecha, N., Antich, J., Gaen, E., Tejada, I., Molina, M., Revents, J. & Carballa, M. (1994) A missense mutation (211HisArg) and a silent (160Thr) mutation within the rhodopsin gene in a Spanish autosomal dominant retinitis pigmentosa family. Human Molecular Genetics 3:195–96. [aSPD]10.1093/hmg/3.1.195CrossRef Google Scholar

Represa, A., Deloulme, J. C., Sensenbrenner, M., Ben-Ari, Y. & Baudier, J. (1990) Neurogranin: Immunocytochemical localization of a brain specific protein kinase C substrate. Journal of Neuroscience 10:3782–92. [EDR]10.1523/JNEUROSCI.10-12-03782.1990CrossRef Google Scholar PubMed

Rescorla, R. A. (1988) Behavioral studies of Pavlovian conditioning. Annual Review of Neuroscience 11:329–52. [TWA]10.1146/annurev.ne.11.030188.001553CrossRef Google Scholar PubMed

Restagno, C., Maghtheh, M., Ghattacharya, S., Ferrone, M., Garnersoe, S., Samuelly, R. & Carbonara, A. (1992) A large deletion at the 3' end of the rhodopsin gene in an Italian family with a diffuse form of autosomal dominant retinitis pigmentosa. Human Molecular Genetics 2:207–8. [aSPD]10.1093/hmg/2.2.207CrossRef Google Scholar

Richards, J. E., Kuo, C. Y., Boehnke, M. & Sieving, P. A. (1991) Rhodopsin Thr58Arg mutation in a family with autosomal dominant retinitis pigmentosa. Ophthalmology 98:1797–1805. [aSPD]10.1016/S0161-6420(91)32047-5CrossRef Google Scholar

Ridge, K. D., Bhattacharya, S., Nakayama, T. A. & Khorana, H. G. (1992) Light-stable rhodopsin: 2. An opsin mutant (Trp-265 → Phe) and a retinal analog with a nonisomerizable 11-Cis configuration form a photostable chromophore. Journal of Biological Chemistry 267:6770–75. [aPAH]10.1016/S0021-9258(19)50492-6CrossRef Google Scholar

Ridge, K. D., Lee, S. S. J. & Yao, L. L. (in press) In vivo assembly of rhodopsin from expressed polypeptide fragments. Proceedings of the National Academy of Sciences USA. [rPAH]Google Scholar

Ricke, F. & Schwartz, E. A. (1994) A cGMP-gated current can control exocytosis at cone synapses. Neuron 13:863–73. [TGW]10.1016/0896-6273(94)90252-6CrossRef Google Scholar

Ringens, P. J., Fang, M., Shinohara, T., Bridges, C. D., Lerea, C. L., Berson, E. L. & Dryja, T. P. (1990) Analysis of genes coding for S-antigen, interstitial retinol binding protein, and the alpha-subunit of cone transducin in patients with retinitis pigmentosa. Investigative Ophthalmology and Visual Science 31:1421–26. [aSPD]Google Scholar PubMed

Rispoli, C. & Detwiler, P. B. (1989) Light adaptation in Gecko rods may involve changes in both the initial and terminal stage of the transduction cascade. Biophysical Journal 55:380. [aMDB]Google Scholar

Rispoli, C. & Detwiler, P. B. (1991) Interactions between calcium and cGMP in dialyzed detached retinal rod outer segments. In: Signal transduction in photoreceptor cells, ed. Hargrave, P. A. & Hofmann, K. P.. Springer-Verlag. [aMDB]Google Scholar

Rispoli, G., Sather, W. A. & Detwiler, P. B. (1993) Visual transduction in dialysed detached rod outer segments from lizard retina. Journal of Physiology (London) 465:513–37. [aMDB]10.1113/jphysiol.1993.sp019691CrossRef Google Scholar PubMed

Robinson, P. R., Cohen, G. B., Zhukovsky, E. A. & Oprian, D. D. (1992) Constitutively active mutants of rhodopsin. Neuron 9:719–25. [aMDB, aSPD, aPAH]10.1016/0896-6273(92)90034-BCrossRef Google Scholar PubMed

Robinson, P. R., Kawamura, S., Abramson, B. & Bownds, M. D. (1980) Control of the cyclic GMP phosphodiesterase of frog photoreceptor membranes. Journal of General Physiology 76:631–45. [aMDB]10.1085/jgp.76.5.631CrossRef Google Scholar PubMed

Rodriquez, J. A., Herrera, C. A., Birch, D. C. & Daiger, S. P. (1993) A leucine to arginine amino acid substitution at codon 46 of rhodopsin is responsible for a severe form of autosomal dominant retinitis pigmentosa. Human Mutation 2:205–13. [aSPD]10.1002/humu.1380020309CrossRef Google Scholar

Rodriguez, J. A., Herrera, C. A., Birch, D. G., Heckenlively, J. R. & Daiger, S. P. (1993a) Rhodopsin mutations in patients with retinitis pigmentosa. American Journal of Human Genetics 53:1224. [aSPD]Google Scholar

Ronnett, G. V. & Snyder, S. H. (1992) Molecular messengers of olfaction. Trends in Neuroscience 15:508–13. [aMDB]10.1016/0166-2236(92)90104-GCrossRef Google Scholar PubMed

Roof, D. J., Adamian, M. & Hayes, A. (1994) Rhodopsin accumulation at abnormal sites in retinas of mice with a human P23H rhodopsin transgene. Investigative Ophthalmology and Visual Science 35:4049–62. [MWK]Google Scholar PubMed

Root, M. J. & MacKinnon, R. (1993) Identification of an external divalent cation-binding site in the pore of a cGMP-activated channel. Neuron 11:459–66. [arRSM]10.1016/0896-6273(93)90150-PCrossRef Google Scholar PubMed

Rosenberg, C.B., Minocherhomjee, A. & Storm, D. R. (1987b) Reconstitution of calmodulin-sensitive adenylate cyclase. Methods in Enzymology 139:776–79. [aZX]10.1016/0076-6879(87)39126-8CrossRef Google Scholar PubMed

Rosenberg, G. B. & Storm, D. R. (1987a) Immunological distinction between calmodulin-sensitive and calmodulin-insensitive adenylyl cyclases. Journal of Biological Chemistry 262:7623–28. [oZX]10.1016/S0021-9258(18)47611-9CrossRef Google Scholar

Rosenfeld, P. J., Cowley, G. S., McGee, T. L., Sandberg, M. A., Berson, E. L. & Dryja, T. P. (1992) A null mutation in the rhodopsin gene causes rod photoreceptor dysfunction and autosomal recessive retinitis pigmentosa. Nature Genetics 1:209–13. [aSPD]10.1038/ng0692-209CrossRef Google Scholar

Ross, E. M. & Gilman, A. G. (1980) Biochemical properties of hormonesensitive adenylyl cyclase. Annual Review of Biochemistry 49:533–64. [aZX]10.1146/annurev.bi.49.070180.002533CrossRef Google Scholar

Roth, N. S., Campbell, P. T., Caron, M. G., Lefkowitz, R. J. & Lohse, M. J. (1991) Comparative rates of desensitization of β-adrenergic receptors by the β-adrenergic receptor kinase and the cyclic AMP-dependent protein kinase. Proceedings of the National Academy of Sciences USA 88:6201–4. [aMDB]10.1073/pnas.88.14.6201CrossRef Google Scholar PubMed

Routtenberg, A. (1995) Phosphoprotein regulation of memory formation: enhancement and control of synaptic plasticity by protein kinase C and F₁ . Annual of the New York Academy of Sciences 444:203–11.10.1111/j.1749-6632.1985.tb37590.xCrossRef Google Scholar

Roychowdhury, S. & Rasenick, M. M. (1994) Tubulin-G protein associations stabilizes GTP binding and activates GTPase. Biochemistry 33:9800–5. [MMR]10.1021/bi00198a052CrossRef Google Scholar PubMed

Roychowdhury, S., Wang, N. & Rasenick, M. M. (1993) Biochemistry 32:4955–61. [MMR]10.1021/bi00069a034CrossRef Google Scholar

Ryba, N. J. P. & Marsh, D. (1992) Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance. Biochemistry 31:7511–18. [aPAH]10.1021/bi00148a011CrossRef Google Scholar PubMed

Saga, M., Mashima, Y., Kawashima, S., Akeo, K., Oguchi, Y., Kudoh, J. & Shimizu, N. (1993) Rhodopsin gene analysis for Japanese autosomal dominant retinitis pigmentosa patients. Investigative Ophthalmology and Visual Science 34:1459. [aSPD]Google Scholar

Saitoh, S., Takamatsu, K., Kobayashi, M. & Noguchi, T. (1993) Distribution of hippocalcin mRNA and immunoreactivity in rat brain. Neuroscience Letters 157:107–10. [KT]10.1016/0304-3940(93)90654-4CrossRef Google Scholar PubMed

Saitoh, S., Takamatsu, K., Kobayashi, M. & Noguchi, T. (1994) Immunohistochemical localization of neural visinin-like Ca2+-binding protein 2 in adult rat brain. Neuroscience Letters 171:155–58. [KT]10.1016/0304-3940(94)90628-9CrossRef Google Scholar

Sakmar, T. P., Franke, R. R. & Khorana, H. G. (1989) Glutamic acid-113 serves as the retinylidine schiff base counterion in bovine rhodopsin. Proceedings of the National Academy of Sciences USA 86:8309–13. [aPAH]10.1073/pnas.86.21.8309CrossRef Google Scholar

Salter, R. S., Krinks, M. H., Klee, C. B. & Neer, E. J. (1981) Calmodulin activates the isolated catalytic unit of brain adenylate cyclase. Journal of Biological Chemistry 256:9830–33. [aZX]10.1016/S0021-9258(19)68703-XCrossRef Google Scholar PubMed

Sanada, K., Kokame, K., Yoshizawa, T., Takao, T. & Fukada, Y. (1995) Role of heterogeneneous N-terminal acylation of recoverin in rhodopsin phosphorylation. Journal of Biological Chemistry 267:18274–18277 Google Scholar

Sankila, E.-M., Pakarinen, L., Kääriäinen, H., Aittomäki, K., Karjalainen, S., Sistonen, P. & de la Chapelle, A. (1995) Assignment of an Usher syndrome type III (USH3) gene to chromosome 3q. Human Molecular Genetics 4:93–98. [rSPD]10.1093/hmg/4.1.93CrossRef Google Scholar PubMed

Sano, M. (1985) Calmodulin-dependent adenylate cyclase in rat retina and the response to dopamine. Brain Research 345:337–40. [aZX]10.1016/0006-8993(85)91012-1CrossRef Google Scholar

Sather, W. A. & Detwiler, P. B. (1987) Intracellular biochemical manipulation of phototransduction in detached rod outer segments. Proceedings of the National Academy of Sciences USA 84:9290–94. [aM DB]10.1073/pnas.84.24.9290CrossRef Google Scholar PubMed

Schacher, S., Castellucci, V. F. & Kandel, E. R. (1988) cAMP evokes longterm facilitation in Aplysia sensory neurons that requires new protein synthesis. Science 240:1667–69. [aZX]10.1126/science.2454509CrossRef Google Scholar

Schafmeister, C. E., Miercke, L. J. W. & Stroud, R. M. (1993) Structure at 2.5 Å of a designed peptide that maintains solubility of membrane proteins. Science 262:734–39. [RKC]10.1126/science.8235592CrossRef Google Scholar PubMed

Schertler, G. F. X. (1992) Overproduction of membrane proteins. Current Opinion in Structural Biology 2:53444. [aPAH]10.1016/0959-440X(92)90083-JCrossRef Google Scholar

Schertler, G. F. X., Bartunik, H. D., Michel, H. & Oesterhelt, D. (1993) Orthorhombic crystal form of bacteriorhodopsin nucleated on benzamidine diffracting to 3.6 Å resolution. Journal of Molecular Biology 234:156–64. [RMG]10.1006/jmbi.1993.1570CrossRef Google Scholar PubMed

Schertler, G. F. X. & Hargrave, P. A. (in press) Projection structures of frog rhodopsin in two crystal forms. Proceedings of the National Academy of Sciences USA. [raPAH]Google Scholar

Schertler, G. F. X., Villa, C. & Henderson, R. (1993) Projection structure of rhodopsin. Nature 362:770–72. [aPAH, EAD, RMG]10.1038/362770a0CrossRef Google Scholar PubMed

Schnetkamp, P. P. M. (1989) Na-Ca or Na-Ca-K exchange in the outer segments of vertebrate rod photoreceptors. Progress in Biophysics and Molecular Biology 54:1–29. [PPMS]10.1016/0079-6107(89)90007-2CrossRef Google Scholar PubMed

Schnetkamp, P. P. M. (1990) Cation selectivity of and cation binding to the cGMP-dependent channel in bovine rod outer segment membranes. Journal of General Physiology 96:517–34. [aRSM]10.1085/jgp.96.3.517CrossRef Google Scholar

Schnetkamp, P. P. M., Li, X-.B., Basu, D. K. & Szerencsei, R. T. (1991) Regulation of free cytosolic Ca2+ concentration in the outer segments of bovine retinal rods by Na-Ca-K exchange measured with Fluo-3. Journal of Biological Chemistry 266:22975–82. [PPMS]10.1016/S0021-9258(18)54450-1CrossRef Google Scholar PubMed

Schnetkamp, P. P. M. & Szerencsei, R. T. (1993) Intracellular Ca2+ sequestration and release in intact bovine retinal rod outer segments. Journal of Biological Chemistry 268:12449–57. [PPMS]10.1016/S0021-9258(18)31410-8CrossRef Google Scholar PubMed

Scholz, K. P. & Byrne, J. H. (1988) Intracellular injection of cAMP induces a long-term reduction of neuronal K+ currents. Science 240:1664–66. [aZX]10.1126/science.2837826CrossRef Google Scholar PubMed

Schulte, T. H. & Marchesi, V. T. (1979) Conformation of the human erythrocyte glycophorin A and its constituent peptides. Biochemistry 18:275–80. [ADA]10.1021/bi00569a006CrossRef Google Scholar PubMed

Scott, K., Sieving, P. A., Bingham, E., Bhagat, V. J., Sullivan, J., Alpern, M. & Richards, J. E. (1993) Rhodopsin mutations associated with autosomal dominant retinitis pigmentosa. American Journal of Human Genetics 53:147. [aSPD]Google Scholar

Shapley, R. & Enroth-Cugell, C. (1984) Visual adaptation and retinal gain controls. Progress in Retinal Research 3:263–46. [aMDB]10.1016/0278-4327(84)90011-7CrossRef Google Scholar

Sheffield, V. C., Fishman, G. A., Beck, J. S., Kimura, A. E. & Stone, E. M. (1991) Identification of novel rhodopsin mutations associated with retinitis pigmentosa by GC-damped denaturing gradient gel electrophoresis. American Journal of Human Genetics 49:699–706. [aSPD]Google Scholar PubMed

Shichi, H., Lewis, M. S., Irreverre, F. & Stone, A. L. (1969) Biochemistry of visual pigments: 1. Purification and properties of bovine rhodopsin. Journal of Biological Chemistry 244:529–36. [aPAH]10.1016/S0021-9258(18)94389-9CrossRef Google Scholar

Shinozawa, T., Sokabe, M., Terada, S., Matsusaka, H. & Yoshizawa, T. (1987) Detection of cyclic GMP binding protein and ion channel activity in frog rod outer segments. Journal of Biochemistry 102:281–20. [aRSM]10.1093/oxfordjournals.jbchem.a122052CrossRef Google Scholar PubMed

Shiono, T., Hotta, Y., Noro, M., Sakuma, T., Tamai, M., Hayakawa, M., Hashimoto, T., Fujiki, K., Kanai, A. & Nakajima, A. (1992) Clinical features of Japanese family with autosomal dominant retinitis pigmentosa caused by a single point mutation in codon 347 of rhodopsin gene. Japanese Journal of Ophthalmology 36:69–75. [aSPD]Google Scholar PubMed

Shnyrov, V. L. & Berman, A. L. (1988) Calorimetric study of thermal denaturation of vertebrate visual pigments. Biomedica et Biochimica Acta 47:355–62. [aPAH]Google Scholar PubMed

Shuster, T. A. & Farber, D. B. (1984) Phosphorylation in sealed rod outer segments: Effects of cyclic nucleotides. Biochemistry 23:515–21. [aMDB]10.1021/bi00298a018CrossRef Google Scholar PubMed

Shuster, T. A., Nagy, A. K., Conly, D. C. & Farber, D. B. (1992) Direct zinc binding to purified rhodopsin and disc membranes. Biochemical Journal 282:123–28. [aPAH]10.1042/bj2820123CrossRef Google Scholar PubMed

Sidman, R. L. & Green, M. D. (1965) Retinal degeneration in the mouse: Location of the rd locus in linkage group XVII. Journal of Heredity 56:23–29. [MWK]10.1093/oxfordjournals.jhered.a107364CrossRef Google Scholar PubMed

Sidman, R. L. & Green, M. D. (1970) Nervous, a new mutant mouse with cerebellar disease. In: Les mutants pathologiques chez l'animal, ed. Sabourdy, M.. Centre National de la Recherche Scientifique. [MWK]Google Scholar

Sieving, P. A., Richards, J. E., Bingham, E. L. & Naarendorp, F. (1992) Dominant congenital complete nyctalopia and Gly90Asp rhodopsin mutation. Investigative Ophthalmology and Visual Science 33:1397. [aSPD]Google Scholar

Silva, A. J., Paylor, R., Wehner, J. M. & Tanegawa, S. (1992) Impaired spatial learning in a-calcium-calmodulin kinase II mutant mice. Science 257:206–211. [aZX, TWA, EDR]10.1126/science.1321493CrossRef Google Scholar PubMed

Silva, A. J., Stevens, C. F., Tonegawa, S. & Wang, Y. (1992) Deficient hippocampal long-term potentiation in alpha-calmodulin kinase II mutant mice. Science 257:201–6. [aZX, EDR]10.1126/science.1378648CrossRef Google Scholar

Sitaramayya, A. (1986) Rhodopsin kinase prepared from bovine rod disk membranes quenches light activation of cGMP phosphodiesterase in a reconstituted system. Biochemistry 25:5460–68. [aMDB]10.1021/bi00367a017CrossRef Google Scholar

Sitaramayya, A. & Liebman, P. A. (1983a) Mechanism of ATP quench of phosphodiesterase activation in rod disc membranes. Journal of Biological Chemistry 258:1205–9. [aMDB]10.1016/S0021-9258(18)33179-XCrossRef Google Scholar PubMed

Sitaramayya, A. & Liebman, P. A. (1983b) Phosphorylation of rhodopsin and quenching of cyclic GMP phosphodiesterase activation by ATP at weak bleaches. Journal of Biological Chemistry 258:12106–9. [aMDB]10.1016/S0021-9258(17)44137-8CrossRef Google Scholar PubMed

Skene, J. H. P. (1989) Axonal growth-associated proteins. Annual Review of Neuroscience 12:127–56. [aZX]10.1146/annurev.ne.12.030189.001015CrossRef Google Scholar PubMed

Skene, J. H. P., Jacobson, R. D., Snipes, G. J., McGuire, C. B., Norden, J. J. & Freeman, J. A. (1986) A protein induced during nerve growth (GAP-43) is a major component of growth-cone membranes. Science 233:783–86. [aZX]10.1126/science.3738509CrossRef Google Scholar PubMed

Skene, J. H. P. & Willard, M. J. (1981a) Changes in axonally transported proteins during axon regeneration in toad retinal ganglion cells. Journal of Cell Biology 89:86–95. [aZX]10.1083/jcb.89.1.86CrossRef Google Scholar PubMed

Slack, J. R. & Pockett, S. (1991) Cyclic AMP induces long-term increase in synaptic efficacy in CA1 region of rat hippocampus. Neuroscience Letters 130:69–72. [aZX]10.1016/0304-3940(91)90229-MCrossRef Google Scholar PubMed

Small, K. W., Weber, J. L., Roses, A., Lennon, F., Vance, J. M. & Pericak-Vance, N. U. (1992) North Carolina macular dystrophy is assigned to chromosome 6. Genomics 13:681–85. [aSPD]10.1016/0888-7543(92)90141-ECrossRef Google Scholar PubMed

Smigel, M. D. (1986) Purification of brain adenylyl cyclase using forskolin affinity chromatography and WGA-Sepharose. Journal of Biological Chemistry 261:1976–82. [aZX]10.1016/S0021-9258(17)36039-8CrossRef Google Scholar

Smith, R. J. H., Lee, E. C., Kimberling, W. J., Daiger, S. P., Pelias, M. Z., Keats, B. J. B., Jay, M. L., Bird, A., Reardon, W., Guest, M., Agyagri, R. & Hejtmancik, F. (1992) Localization of two genes for Usher syndrome type I to chromosome 11. Genomics 14:995–1002. [aSPD]10.1016/S0888-7543(05)80122-3CrossRef Google Scholar PubMed

Smith, S. J. & Augustine, G. J. (1988) Calcium ions, active zones and synaptic transmitter release. Trends in Neuroscience 11:458–64. [aZX]10.1016/0166-2236(88)90199-3CrossRef Google Scholar PubMed

Smith, S. O., Courtin, J., de Groot, H., Gebhard, R. & Lugtenburg, J. (1991) ¹³C magic angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin. Biochemistry 30:7409–15. [SOS]10.1021/bi00244a007CrossRef Google Scholar PubMed

Smith, S. O., de Groot, H., Gebhard, R. & Lugtenburg, J. (1992) Magic angle spinning NMR studies on the metarhodopsin II intermediate of bovine rhodopsin: Evidence for an unprotonated Scruff base. Photochemistry & Photobiology 56:1035–39. [SOS]10.1111/j.1751-1097.1992.tb09726.xCrossRef Google Scholar

Smith, S. O. & Peersen, O. B. (1992) Solid-state NMR approaches for studying membrane protein structure. Annual Review of Biophysical and Biomolecular Structure 21:25–47. [SOS]10.1146/annurev.bb.21.060192.000325CrossRef Google Scholar PubMed

Sneyd, J. & Tranchina, D. (1989) Phototransduction in cones: An inverse problem in enzyme kinetics. Bulletin of Mathematical Biology 51:749–84. [aMDB]10.1007/BF02459659CrossRef Google Scholar PubMed

Somlyo, A. P. & Walz, B. (1985) Elemental distribution in rana pipiens retinal rods: Quantitative electron probe analysis. Journal of Physiology (London) 358:183–95. [RLH]10.1113/jphysiol.1985.sp015547CrossRef Google Scholar PubMed

Sowadski, J. M. (1994) Crystallization of membrane proteins. Current Opinion in Structural Biology 4:761–64. [RMG]10.1016/S0959-440X(94)90176-7CrossRef Google Scholar

Squire, L. R. & Davis, H. P. (1981) The pharmacology of memory: A neurobiological perspective. Annual Review of Pharmacology and Toxicology 21:323–56. [aZX]10.1146/annurev.pa.21.040181.001543CrossRef Google Scholar PubMed

Srivastava, D., Fox, D. A. & Hurwitz, R. L. (in press) The role of magnesium in the hydrolysis of cGMP by the bovine retinal rod cGMP phosphodiesterase. Biochemical Journal. [RLH]Google Scholar

Srivastava, D., Hurwitz, R. L. & Fox, D. A. (submitted) Effects of magnesium on cyclic GMP hydrolysis by the bovine retinal rod cyclic GMP phosphodiesterase. [RLH]Google Scholar

Stanton, P. K. & Sarvey, J. M. (1985a) The effect of high-frequency electrical stimulation and norepinephrine on cyclic AMP levels in normal versus norepinephrine-depleted rat hippocampal slices. Brain Research 358:343–48. [aZX]10.1016/0006-8993(85)90981-3CrossRef Google Scholar PubMed

Stanton, P. K. & Sarvey, J. M. (1985b) Depletion of norepinephrine, but not serotonin, reduces long-term potentiation in the dentate gyrus of rat hippocampal slices. Journal of Neuroscience 5:2169–76. [aZX]10.1523/JNEUROSCI.05-08-02169.1985CrossRef Google Scholar

Steinberg, R. H., Fisher, S. K. & Anderson, D. H. (1980) Disc morphogenesis in vertebrate photoreceptors. Journal of Comparative Neurology 190:501–18. [aMDB]10.1002/cne.901900307CrossRef Google Scholar PubMed

Stepanik, P. L., Lerious, V. & McGinnis, J. F. (1993) Developmental appearance, species and tissue specificity of mouse 23-kDa, a retinal calcium-binding protein (recoverin). Experimental Eye Research 57:189–97. [JFM]10.1006/exer.1993.1114CrossRef Google Scholar

Stern, J. H., Kaupp, U. B. & MacLeish, P. R. (1986) Control of the light regulated current in rod photoreceptors by cyclic GMP, calcium and L-cis-diltiazem. Proceedings of the National Academy of Sciences USA 83:1167. [aRSM]10.1073/pnas.83.4.1163CrossRef Google Scholar PubMed

Stone, E. M., Kimura, A. E., Nichols, B. E., Khadivi, P., Fishman, G. A. & Sheffield, V. C. (1991) Regional distribution of retinal degeneration in patients with proline to histidine mutation in codon-23 of the rhodopsin gene. Ophthalmology 98:1806–13. [aSPD]10.1016/S0161-6420(91)32046-3CrossRef Google Scholar PubMed

Stone, E. M., Nichols, B. E., Streb, L. M., Kimura, A. E. & Sheffield, V. C. (1992a) Genetic linkage of vitelliform macular degeneration (Best's disease) to chromosome llql3. Nature Cenetics 1:246–50. [aSPD]10.1038/ng0792-246CrossRef Google Scholar

Stone, E. M., Vandenburgh, K., Kimura, A. E., Lam, B. L., Fishman, G. A., Heckenlively, J. R., Castillo, T. A. & Sheffield, V. C. (1993) Novel mutations in the peripherin (RDS) and rhodopsin genes associated with autosomal dominant retinitis pigmentosa (ADRP). Investigative Ophthalmology and Visual Science 34:1149. [aSPD]Google Scholar

Straume, M., Mitchell, D., Miller, J. & Litman, B. J.. (1990) Interconversions of metarhodopsins I and II: A branched photointermediate decay model. Biochemistry 29:9135–42. [ADA]10.1021/bi00491a006CrossRef Google Scholar

Stryer, L. (1986) Cyclic GMP cascade of vision. Annual Review of Neuroscience 9:87–119. [aSPD, aRSM]10.1146/annurev.ne.09.030186.000511CrossRef Google Scholar

Stryer, L. (1991) Visual excitation and recovery. Journal of Biological Chemistry 266:10711–14. [aMDB, aJBH, aRSM]10.1016/S0021-9258(18)99072-1CrossRef Google Scholar PubMed

Subbaraya, I., Qin, N., McGinness, J. F. & Baehr, W. (1994) Cloning and expression of frog recoverin and its interaction with rhodopsin kinase. Investigative Ophthalmology and Visual Science 35:1485. [aJBH, JFM, AY]Google Scholar

Suber, M. L., Pittler, S. J., Qin, N., Wright, G. C., Holcombe, V., Lee, R. H., Craft, C. M., Lolley, R. N., Baehr, W. & Hurwitz, R. L. (1993) Irish setter dogs affected with rod/cone dysplasia contain a nonsense mutation in the rod cGMP phosphodiesterase β-subunit gene. Proceedings of the National Academy of Sciences USA 90:3968–72. [aSPD, MWK]10.1073/pnas.90.9.3968CrossRef Google Scholar PubMed

Subramaniam, S., Gerstein, M., Osterhelt, D. & Henderson, R. (1993) Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO Journal 12:1–8. [aPAH, RMG]10.1002/j.1460-2075.1993.tb05625.xCrossRef Google Scholar PubMed

Sugimoto, Y., Yatsunami, K., Tsujimoto, M., Khorana, H. G. & Ichikawa, A. (1991) The amino acid sequence of a glutamic acid-rich protein from bovine retina as deduced from the cDNA sequence. Proceedings of the National Academy of Sciences USA 88:3116–19. [rRSM]10.1073/pnas.88.8.3116CrossRef Google Scholar PubMed

Suh, K. H. & Hamm, H. (1988) Components I and II form a complex with the beta gamma subunils of G protein in frog rod outer segments. Investigative Ophthalmology and Visual Science 28: 218. [aMDB]Google Scholar

Sullivan, J. M., Makris, G. S., Dickinson, P., Mulhall, L. E. M., Sc, D. A., Forrest, S., Cotton, R. G. H. & Loughnan, M. S. (1993) A new codon 15 rhodopsin gene mutation in autosomal dominant retinitis pigmentosa is associated with sectorial disease. Archives of Ophthalmology 111: 1512–17. [aSPD]10.1001/archopht.1993.01090110078029CrossRef Google Scholar PubMed

Sullivan, J. M., Scott, K. M., Falls, B. E., Richards, J. E. & Sieving, P. A. (1993) A novel rhodopsin mutation at the retinal binding site (LYS-296-MET) in ADRP. Investigative Ophthalmology and Visual Science 34: 1149. [aSPD]Google Scholar

Sung, C.-H., Davenport, C. M., Hennessy, J. C., Maumenee, I. H., Jacobson, S. G., Heckenlively, J. R., Nowakowski, R., Fishman, G., Gouras, P. & Nathans, J. (1991) Rhodopsin mutations in autosomal dominant retinitis pigmentosa. Proceedings of the National Academy of Sciences USA 88:6481–85. [aSPD]10.1073/pnas.88.15.6481CrossRef Google Scholar PubMed

Sung, C.-H., Davenport, C. M. & Nathans, J. (1993) Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain. Journal of Biological Chemistry 268: 26645–49. [aSPD]10.1016/S0021-9258(19)74360-9CrossRef Google Scholar PubMed

Sung, C.-H., Schneider, B. G., Agarwal, N., Papermaster, D. S. & Nathans, J. (1991) Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Proceedings of the National Academy of Sciences USA 88: 8840–44. [aSPD]10.1073/pnas.88.19.8840CrossRef Google Scholar PubMed

Sutkowski, E. M., Tang, W., Broome, C. W., Robbins, J. D. & Seamon, K. B. (1994) Biochemistry 33: 12852–859. [MMR]10.1021/bi00209a017CrossRef Google Scholar

Takamatsu, K. & Uyemura, K. (1992) Identification of recoverin-like immunorcactivity in mouse brain. Brain Research 571:350–53. [KT]10.1016/0006-8993(92)90676-ZCrossRef Google Scholar PubMed

Tamura, T., Nakatani, K. & Yau, K.-W. (1991) Calcium feedback and sensitivity regulation in primate rods. Journal of General Physiology 98: 95–130. [aMDB]10.1085/jgp.98.1.95CrossRef Google Scholar PubMed

Tang, W. J. & Gilman, A. G. (1991) Type-specific regulation of adenylyl cyclase by G protein beta gamma subunits. Science 254: 1500–03. [TWA]10.1126/science.1962211CrossRef Google Scholar PubMed

Tang, W. J., Krupinski, J. & Gilman, A. G. (1991) Expression and characterization of calmodulin-activated (type I) adenylyl cyclase. Journal of Biological Chemistry 266: 8595–8603. [arZX, TWA, MMR]10.1016/S0021-9258(18)93016-4CrossRef Google Scholar

Taussig, R. T., Quarmby, L. R. & Gilman, A. G. (1993) Regulation of purified type I & type III adenylyl cyclases by C protein beta/gamma subunits. Journal of Biological Chemistry 268:9–12. [aZX]10.1016/S0021-9258(18)54106-5CrossRef Google Scholar

Thirkill, C. E., Tait, R. C., Tyler, N. K., Roth, A. M. & Keltner, J. L. (1992) The cancer-associated retinopathy antigen is a recoverin-like protein. Investigative Ophthalmology and Visual Science 33: 2768–72. [aJBH, JFM]Google Scholar PubMed

Tiberi, M. & Caron, M. G. (in press) Journal of Biolgical Chemistry. [MMR]Google Scholar

Ting, T. D. & Ho, Y.-K. (1991) Molecular mechanism of GTP hydrolysis by bovine transducin: Pre-steady-state kinetic analyses. Biochemistry 30: 8996–9007. [aMDB]10.1021/bi00101a013CrossRef Google Scholar PubMed

Toscano, W. A. Jr, Westcott, K. R., LaPorte, D. C. & Storm, D. R. (1979) Evidence for a dissociable protein subunit required for calmodulin stimulation of brain adenylate cyclase. Proceedings of the National Academy of Sciences USA 76: P5582–86. [aZX]10.1073/pnas.76.11.5582CrossRef Google Scholar PubMed

Tola, M. R., Xia, Z., Storm, D. R. & Schimerlik, M. I. (1990). Reconstitution of muscarinic receptor mediated inhibition of adenylyl cyclase. Molecular Pharmacology 37: 950–57. [aZX]Google Scholar

Toyoshima, C. & Unwin, N. (1990) Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction. Journal of Cell Biology 111:2623–35. [aPAH]10.1083/jcb.111.6.2623CrossRef Google Scholar PubMed

Tranchina, D., Sneyd, J. & Cadenas, I. D. (1991) Light adaptation in turtle cones: Testing and analysis of a model for phototransduction. Biophysical Journal 60: 217–37. [aMDB]10.1016/S0006-3495(91)82045-8CrossRef Google Scholar

Travis, G. H. (1991) Name dropping. Nature 349: 24. [aSPD]10.1038/349024b0CrossRef Google Scholar PubMed

Travis, G. H., Brennan, M. B., Danielson, P. E., Kozak, C. A. & Sutcliffe, J. G. (1989) Identification of photoreceptor-specific mRNA encoded by the gene responsible for retinal degeneration slow (rds). Nature 338: 70–73. [MWK]10.1038/338070a0CrossRef Google Scholar

Travis, G. H., Sutcliffe, J. G. & Bok, D. (1991a) The retinal degeneration slow (rds) gene product is a photoreceptor disc membrane-associated glycoprotein. Neuron 6: 61–70. [aSPD, MWK]10.1016/0896-6273(91)90122-GCrossRef Google Scholar PubMed

Treisman, G., Bagley, S. & Gnegy, M. (1983) Calmodulin-sensitive and calmodulin-insensitive components of adenylate cyclase activity in rat striatum have differential responsiveness to guanyl nucleotides. Journal of Neurochemistry 41: 1398–1406. [MMR]10.1111/j.1471-4159.1983.tb00838.xCrossRef Google Scholar PubMed

Tsuboi, S. Matsumoto, H., Jackson, K. W., Tsujimoto, K., Williams, T. & Yamazaki, A. (1994a) Phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in Rana catesbiana rod photoreceptors: 1. Characterization of the phosphorylation. Journal of Biological Chemistry 269: 15016–23. [aMDB]10.1016/S0021-9258(17)36568-7CrossRef Google Scholar

Tsuboi, S., Matsumoto, H. & Yamazaki, A. (1994) Phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in Rana catesbiana rod photoreceptors: 2. A possible mechanism for the turnoff of cGMP phosphodiesterase without GTP hydrolysis. Journal of Biological Chemistry 269: 15024–29. [aMDB, AY]10.1016/S0021-9258(17)36569-9CrossRef Google Scholar

Tully, T., Preat, T., Boynton, S. C. & Del Vecchio, M. (in press). Genetic dissection of consolidated memory in Drosophila melanogaster. Cell. [EDR]Google Scholar

Tycko, R. & Smith, S. O. (1993) Symmetry principles in the design of pulse sequences for structural measurements in magic angle spinning nuclear magnetic resonance. Journal of Chemical Physics 98: 932– 43. [SOS]10.1063/1.465078CrossRef Google Scholar

Udovichenko, I. P., Cunnick, J., Gonzalez, K. & Takemoto, D. J. (1994) Functional effect of phosphorylation of the photoreceptor phosphodiesterase inhibitory subunit by protein kinase C. Journal of Biological Chemistry 269: 9850–56. [aMDB]10.1016/S0021-9258(17)36961-2CrossRef Google Scholar PubMed

Uhl, R., Wagner, R. & Ryba, N. (1990) Watching C proteins at work. Trends in Neuroscience 13:64–70. [aMDB]10.1016/0166-2236(90)90070-QCrossRef Google Scholar

Ulshafer, R. J., Garcia, C. A. & Hollyfield, J. G. (1980) Sensitivity of photoreceptors to elevated levels of cGMP in the human retina. Investigative Ophthamology and Visual Science 19: 1236–41. [aSPD]Google Scholar PubMed

Ulshafer, R. J., Sherry, D. M., Dawson, R. Jr, & Wallace, D. R. (1990) Excitatory amino acid involvement in retinal degeneration. Brain Research 531: 350–54. [MT]10.1016/0006-8993(90)90800-QCrossRef Google Scholar PubMed

Unger, V. M., Hargrave, P. A. & Schertler, G. F. X. (1995) Localization of the transmembrane helices in the three-dimensional structure of frog rhodopsin. Biophysics Journal 68: A330. [rPAH]Google Scholar

Unwin, P. N. T. & Zampighi, G. (1980) Structure of the junction between communicating cells. Nature 283: 545–49. [aPAH]10.1038/283545a0CrossRef Google Scholar PubMed

Vaithinathan, R., Berson, E. L. & Dryja, T. P. (1993) Further screening of the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa. Investigative Ophthalmology and Visual Science 34:1149. [aSPD]Google Scholar

van der Steen, R., Groesbeek, M., van Amsterdam, L. J. P., Lugtenburg, J., van Oostrum, J. & de Grip, W. J. (1989) All E–10,20-methanoretinylopsin, light-stable rhodopsin. Synthesis and spectroscopy of all E–10,20-methano- and all-E-retinoyl fluoride and their reaction with bovine opsin. Recueil des Travauz Chimiques des Pays-Bos 108:20–27. [aPAH]10.1002/recl.19891080105CrossRef Google Scholar

Van Nie, R., Ivanyi, D. & Demant, P. 91978) A new H-2 linked mutation, rds, causing retinal degeneration in the mouse. Tissue Antigens 12: 106–8. [MWK]Google Scholar

van Soest, S., van den Bora, L. I., Gal, A., Farrar, G. J., Bleeker, Wagemakers L. M., Westerveld, A., Humphries, P., Sandkuijl, L. A. & Bergen, A. A. B. (1994) Assignment of a gene for autosomal dominant recessive retinitis pigmentosa (RP12) to chromosome lq31-q32.1 in an inbred and genetically heterogeneous disease population. Genomics 22: 499–504. [aSPD, AB]10.1006/geno.1994.1422CrossRef Google Scholar

Vanderkooi, G. (1974) Organisation of proteins in membranes with special reference to the cytochrome oxidase system. Biochimica et Biophysica Acta 344: 307–45. [aPAH]10.1016/0304-4157(74)90011-2CrossRef Google Scholar

Villacres, E. C., Xia, Z., Bookbinder, L. H., Edelhoff, S., Adler, D. A., Disteche, C. M. & Storm, D. R. (1993) Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics 16: 473–78. [aZX]10.1006/geno.1993.1213CrossRef Google Scholar PubMed

Vuong, T. M. & Chabre, M. (1990) Subsecond deactivation of transducin by endogenous GTP hydrolysis. Nature 346: 71–74. [aMDB]10.1038/346071a0CrossRef Google Scholar PubMed

Vuong, T. M. & Chabre, M. (1991) Deactivation kinetics of the transduction cascade of vision. Proceedings of the National Academy of Sciences USA 88: 9813–17. [aMDB]10.1073/pnas.88.21.9813CrossRef Google Scholar

Vuong, R. M., Chabre, M. & Stryer, L. (1984) Millisecond activation of transducin in the cyclic nucleotide cascade of vision. Nature 311:659–61. [aMDB]10.1038/311659a0CrossRef Google Scholar

Wagner, R., Ryba, N. & Uhl, R. (1988) Sub-second turnover of transducin GTPase in bovine rod outer segments. FEBS Letters 234:44–48. [aMDB]10.1016/0014-5793(88)81299-7CrossRef Google Scholar PubMed

Wagner, R., Ryba, N. & Uhl, R. (1989) Calcium regulates the rate of rhodopsin disactivation and the primary amplification step in visual transduction. FEBS Letters 242:249–54. [aMDB]10.1016/0014-5793(89)80479-XCrossRef Google Scholar PubMed

Wahlsten, D. (1991) Sample size to detect a planned contrast and a one degree-of-freedom interaction effect. Psychological Bulletin 110:587–95. [DW]10.1037/0033-2909.110.3.587CrossRef Google Scholar

Walsh, M. P., Valentine, K. A., Ngai, P. K., Carruthers, C. A. & Hollenberg, M. D. (1984) Ca2+-dependent hydrophobic-interaction chromatography: Isolation of a novel Ca2+-binding protein and protein kinase C from bovine brain. Biochemistry Journal 224:117–27. [KT]10.1042/bj2240117CrossRef Google Scholar PubMed

Wang, N. & Rasenick, M. M. (1991) Tubulin-G protein interactions involve microtubule polymerization domains. Biochemistry 30: 10957– 65. [MMR]10.1021/bi00109a021CrossRef Google Scholar PubMed

Wang, N., Yan, K. & Rasenick, M. M. (1990) Tubulin binds specifically to the signal-transducing proteins, Csa and Gial. Journal of Biological Chemistry 265: 1239–42. [MMR]10.1016/S0021-9258(19)40002-1CrossRef Google Scholar

Watanabe, S. I. & Murakami, M. (1991) Similar properties of the cGMPactivated channels between cones and rods in the carp retina. Visual Neuroscience 6:563–68. [aRSM]10.1017/S0952523800002546CrossRef Google Scholar PubMed

Watson, J. B., Battenberg, E. F., Wong, K. K., Bloom, F. E. & Sutcliffe, J. G. (1990) Subtractive cDNA cloning of RC3, a rodent cortex-enriched mRNA encoding a novel 78 residue protein. Journal of Neuroscience Research 26:397–408. [EDR]10.1002/jnr.490260402CrossRef Google Scholar PubMed

Watson, J. B., Sutcliffe, J. G. & Fisher, R. S. (1992) Localization of the protein kinase C phosphorylation/calmodulin binding substrate RC3 in dendritic spines of neostriatal neurons. Proceedings of the National Academy of Sciences USA 89: 8581–85. [EDR]10.1073/pnas.89.18.8581CrossRef Google Scholar

Wayman, G. A., Impey, S., Wu, Z., Kinsvogel, W., Prichard, L. & Storm, D. R. (1994) Synergistic activation of the type I adenylyl cyclase by Ca2+ and Gs coupled receptors in vivo. Journal of Biological Chemistry 269: 25400–5. [arZX, TWA, MMR]10.1016/S0021-9258(18)47263-8CrossRef Google Scholar PubMed

Weber, B. H. F., Vogt, G., Pruett, R. C., Stöhr, H. & Felbor, U. (1994) Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorby's fundus dystrophy. Nature Genetics 8: 352–55. [rSPD]10.1038/ng1294-352CrossRef Google Scholar

Wehner, R., Marsh, A. C. & Wehner, S. (1992) Desert ants on a thermal tightrope. Nature 357: 586–87. [aPAH]10.1038/357586a0CrossRef Google Scholar

Weitz, C. J. & Nathans, J. (1992) Histidine residues regulate the transition of photoexcited rhodopsin to its active conformation, metarhodopsin II. Neuron 8:465–72. [aSPD]10.1016/0896-6273(92)90274-HCrossRef Google Scholar PubMed

Weitz, C. J., Went, L. N. & Nathans, J. (1992a) Human tritanopia associated with a third amino acid substitution in the blue-sensitive visual pigment. American Journal of Human Genetics 51:444–46. [aSPD]Google Scholar PubMed

Weleber, R. G., Carr, R. E., Murphey, W. H., Sheffield, V. & Stone, E. M. (1993) Phenotypic variation including retinitis pigmentosa, pattern dystrophy and fundus flavimaculatis in a single family with a deletion of codon 153 or 154 of the pheripherin/RDS gene. Archives of Ophthalmology 111: 1531–42. [AB, aSPD]10.1001/archopht.1993.01090110097033CrossRef Google Scholar

Well, D., Blanchard, S., Kaplan, J., Guilford, P., Gibson, F., Walsh, J., Mburu, P., Varela, A., Levillers, J., Weston, M. D., Kelly, P. M., Kimberling, W. J., Wagenaar, M., Levi-Acobas, F., Larget-Piet, D., Munnich, A., Steel, K. P., Brown, S. D. M. & Petit, C. (1995) Defective mysin VIIA gene responsible for Usher syndrome type IB. Nature 374:60–61. [rSPD]10.1038/374060a0CrossRef Google Scholar

Wells, J., Wroblewski, J., Keen, J., Inglehearn, C., Jubb, C., Eckstein, A., Jay, M., Arden, G., Bhattacharya, S., Fitzke, F. & Bird, A. (1993) Mutations in the human retinal degeneration slow (rds) gene can cause either retinitis pigmentosa or macular dystrophy. Nature Genetics 3: 213–18. [aSPD]10.1038/ng0393-213CrossRef Google Scholar PubMed

Welte, W. & Wacker, T. (1991). Protein-detergent micellar solutions for the crystallization of membrane proteins: Some general approaches and experiences with the crystallization of pigment-protein complexes from purple bacteria. In: Crystallization of membrane proteins, ed. Michel, H.. CRC Press. [aPAH]Google Scholar

Westcott, K. R., LaPorte, D. C. & Storm, D. R. (1979) Resolution of adenylyl cyclase sensitive and insensitive to Ca2+ and CDR by CDR-sepharose affinity chromatography. Proceedings of the National Academy of Sciences USA 76: 204–28. [WH, aZX]10.1073/pnas.76.1.204CrossRef Google Scholar PubMed

Weyand, I., Godde, M., Frings, S., Weiner, J., Müller, , Altenhofen, W., Hatt, H. & Kaupp, U. B. (1994) Cloning and functional expression of a cyclicnucleotide-gated channel from mammalian sperm. Nature 368: 859–63. [rRSM]10.1038/368859a0CrossRef Google Scholar

Whelan, J. P. & McGinnis, J. F. (1988) Light-dependent subcellular movement of photoreceptor proteins. Journal of Neuroscience Research 20: 263–70. [JFM]10.1002/jnr.490200216CrossRef Google Scholar PubMed

Wilden, U., Hall, S. W. & Kuhn, H. (1986) Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48 KDa protein of rod outer segments. Proceedings of the National Academy of Sciences USA 83:1174–78. [aMDB]10.1073/pnas.83.5.1174CrossRef Google Scholar PubMed

Wilden, U. & Kuhn, H. (1982) Light-dependent phosphorylation of rhodopsin: Number of phosphorylation sites. Biochemistry 21: 3014–22. [aMDB]10.1021/bi00541a032CrossRef Google Scholar PubMed

Williams, D. S., Linberg, K. A., Vaughan, D. K., Fariss, R. N. & Fisher, S. K. (1988) Disruption of microfilament organization and deregulation of disk membrane morphogenesis by cytochalasin D in rod and cone photoreceptors. Journal of Comparative Neurology 272:161–76. [aMDB]10.1002/cne.902720202CrossRef Google Scholar PubMed

Wohlfart, P., Haase, H., Molday, R. S. & Cook, N. J. (1992) Antibodies against synthetic peptides used to determine the topology and site of glycosylation of the cGMP-gated channel from bovine rod photoreceptors. Journal of Biological Chemistry 267:644–48. [aRSM]10.1016/S0021-9258(18)48542-0CrossRef Google Scholar PubMed

Wohlfart, P., Muller, H. & Cook, N. J. (1989) Lectin binding and enzymatic deglycosylation of cGMP-gated channel from bovine rod photoreceptors. Journal of Biological Chemistry 264:20934–39. [aRSM]10.1016/S0021-9258(19)30026-2CrossRef Google Scholar PubMed

Wong, S. & Molday, R. S. (1986) A spectrin-like protein in retinal rod outer segments. Biochemistry 25: 6294–6300. [aRSM]10.1021/bi00368a069CrossRef Google Scholar PubMed

Wu, S. M., Qiao, X., Noebels, J. L. & Yang, X. L.: Localization and modulatory actions of zinc in vertebrate retina. Vision Research 33:2611–16. [MT]10.1016/0042-6989(93)90219-MCrossRef Google Scholar

Wu, Z., Thomas, S. A., Xia, Z., Willacres, E. C., Palmiter, R. D. & Storm, D. R. (in press) Deficient spatial memory and altered LTP in type 1 adenylyl cyclase mutant mice. Proceedings of the National Academy of Sciences 92: 220–4. [arZX]10.1073/pnas.92.1.220CrossRef Google Scholar

Wu, Z., Wong, S. T. & Storm, D. R. (1993) Modification of the calcium and calmodulin sensitivity of the type I adenylyl cyclase by mutagenesis of its calmodulin binding domain. Journal of Biological Chemistry 268:23766–68. [aZX]10.1016/S0021-9258(20)80447-5CrossRef Google Scholar PubMed

Xia, Z., Choi, E. J., Wang, F., Blazynski, C., & Storm, D. R. (1993) The type I calmodulin sensitive adenylyl cyclase is neural specific. Journal of Neurochemistry 60: 305–11. [aZX]10.1111/j.1471-4159.1993.tb05852.xCrossRef Google Scholar PubMed

Xia, Z., Choi, E. J., Wang, F. & Storm, D. R. (1992) The type III calcium/calmodulin-sensitive adenylyl cyclase is not specific to olfactory sensory neurons. Neuroscience Letters 144:169–73. [aZX]10.1016/0304-3940(92)90742-PCrossRef Google Scholar

Xia, Z., Refsdal, C. D., Merchant, K. M., Dorsa, D. M. & Storm, D. R. (1991) Distinct patterns for the distribution of mRNA for the calmodulinsensitive adenylyl cyclase in rat brain: Expression in areas associated with learning and memory. Neuron 6: 431–43. [aZX]10.1016/0896-6273(91)90251-TCrossRef Google Scholar

Yamagata, K., Goto, K., Kuo, C.-H., Kondo, H. & Miki, N. (1990) Visinin: A novel calcium binding protein expressed in retinal cone cells. Neuron 2:469–76. [aJBH, KT]10.1016/0896-6273(90)90059-OCrossRef Google Scholar

Yamazaki, A., Hayashi, F., Tatsumi, M., Bitenski, M. W. & George, J. S. (1990) Interaction between the subunits of transducin and cyclic GMP phosphodiesterase in Rana catesbiana rod photoreceptors. Journal of Biological Chemistry 265: 11539–48. [aMDB, AY]10.1016/S0021-9258(19)38431-5CrossRef Google Scholar PubMed

Yamazaki, A., Yamazaki, M., Tsuboi, S., Kishigami, A., Umbarger, K. O., Hutson, L. D., Madland, W. T. & Hayashi, F. (1993) Regulation of G protein function by an effector in GTP-dependent signal transduction. An inhibitory subunit of cGMP phosphodiesterase inhibits GTP hydrolysis by transducin in vertebrate rod photoreceptors. Journal of Biological Chemistry 268:8899–8907. [rMDB]10.1016/S0021-9258(18)52958-6CrossRef Google Scholar PubMed

Yarfitz, S. & Hurley, J. B. (1994) Transduction mechanisms of vertebrate and invertebrate photoreceptors. Journal of Biological Chemistry 269: 14329–32. [aMDB]10.1016/S0021-9258(17)36620-6CrossRef Google Scholar PubMed

Yau, K.-W. (1994) Phototransduction mechanism in retinal rods and cones: The Friedenwald lecture. Investigative Ophthalmology and Visual Science 35: 9–32. [aMDB]Google Scholar PubMed

Yau, K.-W. & Baylor, D. A. (1989) Cyclic GMP-activated conductance of retinal photoreceptor cells. Annual Review of Neuroscience 12:289–327. [arMDB, aRSM, LWH, RLH]10.1146/annurev.ne.12.030189.001445CrossRef Google Scholar PubMed

Yau, K.-W & Nakatani, K. (1984a) Electrogenic Na-Ca exchange in retinal rod outer segment. Nature 311:661–63. [aRSM]10.1038/311661a0CrossRef Google Scholar PubMed

Yau, K.-W & Nakatani, K.(1984b) Cation selectivity of light-sensitive conductance in retinal rods. Nature 309:352–54. [aRSM]10.1038/309352a0CrossRef Google Scholar PubMed

Yau, K.-W & Nakatani, K.(1985a) Light-suppressible, cyclic GMP-sensitive conductance in the plasma membrane of a truncated rod outer segment. Nature 317: 252–55. [aRSM]10.1038/317252a0CrossRef Google Scholar PubMed

Yau, K.-W & Nakatani, K. (1985b) Light-induced reduction of cytoplasmic free calcium in retinal rod outer segment. Nature 313: 579–82. [aRSM]10.1038/313579a0CrossRef Google Scholar PubMed

Yeager, R. E., Heideman, W., Rosenberg, G. B. & Storm, D. R. (1985) Purification of the calmodulin-sensitive sensitive adenylyl cyclase from bovine brain. Biochemistry 24:3776–83. [aZX]10.1021/bi00335a054CrossRef Google Scholar

Yellen, G., Jurman, M. E., Abramson, T. & MacKinnon, R. (1991) Mutations affecting internal TEA blockage identify the probable pore-forming region of K+ channels. Science 251:939–42. [aRSM]10.1126/science.2000494CrossRef Google Scholar

Yool, A. J. & Schwartz, T. L. (1991) Alteration of ionic selectivity of a K+ channel by mutation of the H5 region. Nature 349:700–4.[aRSM]10.1038/349700a0CrossRef Google Scholar

Yoshida, T., Willardson, B. M., Wilkins, J. F., Jensen, G. J., Thornton, B. D. & Bitensky, M. W. (1994) The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin. Journal of Biological Chemistry 269: 24050–57. [BMW]10.1016/S0021-9258(19)51046-8CrossRef Google Scholar PubMed

Yoshikami, S., George, J. S. & Hagins, W. A. (1980) Light-induced calcium fluxes from outer segment layer of vertebrate retinas. Nature 287:395–98. [TGW]10.1038/286395a0CrossRef Google Scholar

Yoshimura, M. & Cooper, D. M. (1992) Cloning and expression of a Ca2+ inhibitable adenylyl cyclase from NCB-20 cells. Proceedings of National Academy of Sciences USA 89: 6716–20. [aZX]10.1073/pnas.89.15.6716CrossRef Google Scholar PubMed

Younger, J. P., McCarthy, S. T. & Owen, W. G. (1992) Modulation of cytosolic free calcium and changes in sensitivity and circulating current occur over the same range of steady-state adapting lights in rod photoreceptors. Incostigatice Ophthalmology and Visual Science 33: 1104. [aMDB]Google Scholar

Yovell, Y. & Abrams, T. W. (1992) Temporal asymmetry in activation of Aplysia adenylyl cyclase may explain properties of conditioning. Proceedings of the National Academy of Sciences USA 89: 6526–30. [TWA]10.1073/pnas.89.14.6526CrossRef Google Scholar

Yovell, Y., Kandel, E. R., Dudai, Y. & Abrams, T. W. (1992) A quantitative study of the Ca2+/calmodulin sensitivity of adenylyl cyclase in Aplysia, Drosophila, and rat. Journal of Ncurochemistry 59: 1736–44. [aZX]10.1111/j.1471-4159.1992.tb11005.xCrossRef Google Scholar PubMed

Yurkova, E. V., Demin, V. V. & Abdulaev, N. G. (1990) Crystallization of membrane proteins: Bovine rhodopsin. Biotnedical Science 1: 585–90. [aPAH]Google Scholar PubMed

Zankel, T., Ok, H., Johnson, R., Chang, C. W., Sekiya, N., Naoki, H., Yoshihara, K. & Nakanishi, K. (1990) Bovine rhodopsin with 11-cis-locked retinal chromophore neither activates rhodopsin kinase nor undergoes conformational change upon irradiation. Journal of the American Chemical Society 112: 5387–88. [aPAH]10.1021/ja00169a077CrossRef Google Scholar

Zhong, Y. & Wu, C. F. (1991) Altered synaptic plasticity in Drosophila memory mutants with a defective cyclic AMP cascade. Science 251:198–201. [aZX]10.1126/science.1670967CrossRef Google Scholar PubMed

Zhukovsky, E. A. & Oprian, D. D. (1989) Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science 245:928–30. [aPAH]10.1126/science.2573154CrossRef Google Scholar

Zimmerman, A. L. & Baylor, D. A. (1986) Cyclic GMP-sensitive conductance of retinal rods consists of aqueous pores. Nature 321:70–72. [aRSM]10.1038/321070a0CrossRef Google Scholar PubMed

Zimmmerman, A. L., Yamanaka, G., Eckstein, F., Baylor, D. A., & Stryer, L. (1985) Interaction of hydrolysis-resistant analogs of cyclic GMP with the phosphodiesterase and light-sensitive channel of retinal rod outer segments. Proceedings of the National Academy of Sciences USA 82:8813–17. [aRSM]10.1073/pnas.82.24.8813CrossRef Google Scholar

Zong-Yi, L., Jacobson, S. G. & Milam, S. G. (1994) Autosomal dominant retinitis pigmentosa caused by the threonine-17-methionine rhodopsin mutation: Retinal histopathology and immunochemistry. Experimental Eye Research 58:397–408. [AB]Google Scholar

Zozulya, S. & Stryer, L. (1992) Calcium-myristoyl protein switch. Proceedings of the National Academy of Sciences USA 89:11569–73. [aJBH, SK]10.1073/pnas.89.23.11569CrossRef Google Scholar PubMed

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Gene therapy, regulatory mechanisms, and protein function in vision

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