Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites-Reference-Cited by-同舟云学术

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Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites

Published:2017-12 Issue:1 Volume:8 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Tong Michael,Pelton Jeff G.,Gill Michelle L.,Zhang Weibing,Picart Francis,Seeliger Markus A.

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/s41467-017-02240-6.pdf

Reference68 articles.

1. Thomas, S. M. & Brugge, J. S. Cellular functions regulated by Src family kinases. Annu. Rev. Cell. Dev. Biol. 13, 513–609 (1997).

2. Cohen, P. The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture. Eur. J. Biochem. 268, 5001–5010 (2001).

3. Zhang, S. & Yu, D. Targeting Src family kinases in anti-cancer therapies: turning promise into triumph. Trends Pharmacol. Sci. 33, 122–128 (2012).

4. Boggon, T. J. & Eck, M. J. Structure and regulation of Src family kinases. Oncogene 23, 7918–7927 (2004).

5. Xiao, Y. et al. Phosphorylation releases constraints to domain motion in ERK2. Proc. Natl Acad. Sci. USA 111, 2506–2511 (2014).

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