نتایج جستجو برای: connexin32

تعداد نتایج: 206  

Journal: :American journal of physiology. Cell physiology 1999
Camillo Peracchia Xiao G Wang Lillian L Peracchia

Connexin channels are gated by transjunctional voltage ( V j) or CO2 via distinct mechanisms. The cytoplasmic loop (CL) and arginines of a COOH-terminal domain (CT1) of connexin32 (Cx32) were shown to determine CO2sensitivity, and a gating mechanism involving CL-CT1 association-dissociation was proposed. This study reports that Cx32 mutants, tandem, 5R/E, and 5R/N, designed to weaken CL-CT1inte...

Journal: :The Journal of biological chemistry 2010
Souvik Chakraborty Shalini Mitra Matthias M Falk Steve H Caplan Margaret J Wheelock Keith R Johnson Parmender P Mehta

It is as yet unknown how the assembly of connexins (Cx) into gap junctions (GJ) is initiated upon cell-cell contact. We investigated whether the trafficking and assembly of Cx43 and Cx32 into GJs were contingent upon cell-cell adhesion mediated by E-cadherin. We also examined the role of the carboxyl termini of these Cxs in initiating the formation of GJs. Using cadherin and Cx-null cells, and ...

Journal: :The Journal of biological chemistry 2011
So Nakagawa Xiang-Qun Gong Shoji Maeda Yuhua Dong Yuko Misumi Tomitake Tsukihara Donglin Bai

The gap junction channel is formed by proper docking of two hemichannels. Depending on the connexin(s) in the hemichannels, homotypic and heterotypic gap junction channels can be formed. Previous studies suggest that the extracellular loop 2 (E2) is an important molecular domain for heterotypic compatibility. Based on the crystal structure of the Cx26 gap junction channel and homology models of...

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