Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
about
The ability of Sos1 to oligomerize the adaptor protein LAT is separable from its guanine nucleotide exchange activity in vivo.Grb2 promotes integrin-induced focal adhesion kinase (FAK) autophosphorylation and directs the phosphorylation of protein tyrosine phosphatase α by the Src-FAK kinase complex.Grb2 Is Important for T Cell Development, Th Cell Differentiation, and Induction of Experimental Autoimmune Encephalomyelitis.Non-canonical dynamic mechanisms of interaction between the p66Shc protein and Met receptor
P2860
Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
description
2013 nî lūn-bûn
@nan
2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
@ast
Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
@en
type
label
Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
@ast
Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
@en
prefLabel
Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
@ast
Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
@en
P2093
P2860
P3181
P356
P1476
Allostery mediates ligand binding to Grb2 adaptor in a mutually exclusive manner.
@en
P2093
Amjad Farooq
Brian J Deegan
Caleb B McDonald
David C Mikles
Jimmy El Hokayem
Jordan E Balke
Kenneth L Seldeen
Nawal Zafar
Vikas Bhat
P2860
P304
P3181
P356
10.1002/JMR.2256
P577
2013-02-01T00:00:00Z