CW-EPR studies revealed different motional properties and oligomeric states of the integrin β1a transmembrane domain in detergent micelles or liposomes-Reference-Cited by-同舟云学术

CW-EPR studies revealed different motional properties and oligomeric states of the integrin β1a transmembrane domain in detergent micelles or liposomes

Published:2015-01-19 Issue:1 Volume:5 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Yu Lu,Wang Wei,Ling Shenglong,Liu Sanling,Xiao Liang,Xin Yanlong,Lai Chaohua,Xiong Ying,Zhang Longhua,Tian Changlin

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep07848.pdf

Reference54 articles.

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2. Ginsberg, M. H., Partridge, A. & Shattil, S. J. Integrin regulation. Curr Opin Cell Biol 17, 509–516 (2005).

3. Vinogradova, O. et al. A structural mechanism of integrin alpha(IIb)beta(3) “inside-out” activation as regulated by its cytoplasmic face. Cell 110, 587–597 (2002).

4. Hynes, R. O. Targeted mutations in cell adhesion genes: what have we learned from them? Dev Biol 180, 402–412 (1996).

5. Luo, B. H., Springer, T. A. & Takagi, J. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol 2, e153 (2004).

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