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Role of DDR2 ECD Oligomerization in Binding to Collagen

Published online by Cambridge University Press:  25 July 2016

Carolyn Wang
Affiliation:
Biomedical Engineering Department, the Ohio State University Columbus, Ohio 43210, USA
David Yeung
Affiliation:
Biomedical Engineering Department, the Ohio State University Columbus, Ohio 43210, USA
Jack Wellerming
Affiliation:
Biophysics Program, the Ohio State University, Columbus, Ohio 43210, USA
Andrew Herr
Affiliation:
Department of Biochemistry and Molecular Genetics, University of Cincinnati, Cincinnati, OH, USA
Jeanette Miller
Affiliation:
Department of Biochemistry and Molecular Genetics, University of Cincinnati, Cincinnati, OH, USA
Rafael Fridman
Affiliation:
Department of Pathology, Wayne State University, Detroit, MI, USA
Gunjan Agarwal
Affiliation:
Biomedical Engineering Department, the Ohio State University Columbus, Ohio 43210, USA Biophysics Program, the Ohio State University, Columbus, Ohio 43210, USA

Abstract

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Type
Abstract
Copyright
© Microscopy Society of America 2016 

References

References:

[1] Fu, H. L., et al, Discoidin domain receptors: unique receptor tyrosine kinases in collagen-mediated signaling. J. Biol. Chem 288 (2013). no. 11, p. 74307437.Google Scholar
[2] Vogel, W, et al, The Discoidin Domain Receptor Tyrosine Kinases Are Activated by Collagen. Mol. Cell 1 (1997). no.1, p. 1323.CrossRefGoogle ScholarPubMed
[3] Xu, H., et al, Collagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1. Matrix Biol 30 (2011). no. 1, p. 1626.Google Scholar
[4] Mihai, C. Mapping of DDR1 Distribution and Oligomerization on the Cell Surface by FRET Micrscopy. J. Miol. Biol 30 (2009). no. 2, p. 432435.Google Scholar
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[7] The authors acknowledge funding from NSF CMMI award 1201111.Google Scholar