Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: Implications for talin activation-Reference-Cited by-同舟云学术

Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: Implications for talin activation

Published:2013-10 Issue:1 Volume:184 Page:21-32
ISSN:1047-8477
Container-title:Journal of Structural Biology
language:en
Short-container-title:Journal of Structural Biology

Author:

Goult Benjamin T.,Xu Xiao-Ping,Gingras Alexandre R.,Swift Mark,Patel Bipin,Bate Neil,Kopp Petra M.,Barsukov Igor L.,Critchley David R.,Volkmann Niels,Hanein Dorit

Funder

NIH Cell Migration Consortium (CMC)

National Institute of General Medical Sciences (NIGMS)

NIH

NIGMS

Publisher

Elsevier BV

Subject

Structural Biology

Reference65 articles.

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3. The structure of an integrin/talin complex reveals the basis of inside-out signal transduction;Anthis;EMBO J.,2009

4. Subcellular localization of talin is regulated by inter-domain interactions;Banno;J. Biol. Chem.,2012

5. Phosphatidylinositol phosphate kinase type 1gamma and beta1-integrin cytoplasmic domain bind to the same region in the talin FERM domain;Barsukov;J. Biol. Chem.,2003

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