In this study, we theorize humanness in organizations as a property of practice. We apply practice theory to examine how humanness becomes enacted in a business organization as people prioritize organizational and individual ends in their work activities. Our empirical case study examines the everyday interactions of development team members in an R&D organization of a large Nordic cooperative. Challenging the dominant individualist and structuralist approaches in humanness and human dignity studies, we identify and locate four different aspects of humanness in organizational practices. As a result, we show how the emergence of humanness is an ongoing process that transpires through two mechanisms: site shifting and reconciliation; that is, people shift between different sites of the social, consisting of different sets of practices with underlying disparate assumptions of humanness, which requires reconciliation. These findings provide a basis for an alternative theorizing of humanness in organizations.

The knowledge of the binding sites of G protein-coupled cholecystokinin receptors represents important insights that may serve to understand their activation processes and to design or optimize ligands. Our aim was to identify the amino acid of the cholecystokinin-A receptor (CCK-AR) binding site in an interaction with the sulfate of CCK, which is crucial for CCK binding and activity. A three-dimensional model of the [CCK-AR-CCK] complex was built. In this model, Arg197 was the best candidate residue for a ionic interaction with the sulfate of CCK. Arg197 was exchanged for a methionine by site-directed mutagenesis. Wild-type and mutated CCK-AR were transiently expressed in COS-7 cells for pharmacological and functional analysis. The mutated receptor on Arg197 did not bind the agonist radioligand 125I-BH-[Thr, Nle]-CCK-9; however, it bound the nonpeptide antagonist [3H]-SR27,897 as the wild-type receptor. The mutant was ≅1,470- and 3,200-fold less potent than the wild-type CCK-AR to activate G proteins and to induce inositol phosphate production, respectively. This is consistent with the 500-fold lower potency and 800-fold lower affinity of nonsulfated CCK relative to sulfated CCK on the wild-type receptor. These data, together with those showing that the mutated receptor failed to discriminate nonsulfated and sulfated CCK while it retained other pharmacological features of the CCK-AR, strongly support an interaction between Arg197 of the CCK-AR binding site and the sulfate of CCK. In addition, the mutated CCK-AR resembled the low affinity state of the wild-type CCK-AR, suggesting that Arg197–sulfate interaction regulates conformational changes of the CCK-AR that are required for its physiological activation.

For a site ${\mathcal S}$ (with enough points), we construct a topological space X$_($)$ and a full embedding φ$^*$ of the category of sheaves on ${\mathcal S}$ into those on X$_($) (i.e., a morphism of toposes φ:Sh (X$_($) →Sh(${\mathcal S}$)). The embedding will be shown to induce a full embedding of derived categories, hence isomorphisms coh$^*$(${\mathcal S}$,A) =coh$^**$(X$_($), φ$^*$A) for any Abelian sheaf A on ${\mathcal S}$. As a particular case, this will give for any scheme Y a topological space X and a functorial isomorphism between the étale cohomology H$^**$(et{Y},A) and the ordinary sheaf cohomology H$^**$(X,φ$^**$A), for any sheaf A for the étale topology on Y.