Highly conserved eight amino acid sequence in SH2 is important for recognition of phosphotyrosine site.
about
Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptorConservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domainsImmunoinhibitory adapter protein Src homology domain 3 lymphocyte protein 2 (SLy2) regulates actin dynamics and B cell spreading.An active form of Vav1 induces migration of mammary epithelial cells by stimulating secretion of an epidermal growth factor receptor ligandInhibition of PI3K binding to activators by serine phosphorylation of PI3K regulatory subunit p85alpha Src homology-2 domainsCharacterizing SH2 Domain Specificity and Network Interactions Using SPOT Peptide Arrays.Two FGF Receptor Kinase Molecules Act in Concert to Recruit and Transphosphorylate Phospholipase CγGlobal transformation of erythrocyte properties via engagement of an SH2-like sequence in band 3.Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.Introduction: History of SH2 Domains and Their Applications.
P2860
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P2860
Highly conserved eight amino acid sequence in SH2 is important for recognition of phosphotyrosine site.
description
1991 nî lūn-bûn
@nan
1991 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Highly conserved eight amino a ...... ition of phosphotyrosine site.
@ast
Highly conserved eight amino a ...... ition of phosphotyrosine site.
@en
type
label
Highly conserved eight amino a ...... ition of phosphotyrosine site.
@ast
Highly conserved eight amino a ...... ition of phosphotyrosine site.
@en
prefLabel
Highly conserved eight amino a ...... ition of phosphotyrosine site.
@ast
Highly conserved eight amino a ...... ition of phosphotyrosine site.
@en
P2093
P1476
Highly conserved eight amino a ...... ition of phosphotyrosine site.
@en
P2093
P304
P356
10.1016/S0006-291X(05)81364-6
P407
P577
1991-11-01T00:00:00Z