Structural differences between repressed and derepressed forms of p60c-src
about
Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinasesMutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactionsExpressed protein ligation: a general method for protein engineeringThe Activation of c-Src Tyrosine Kinase: Conformational Transition Pathway and Free Energy Landscape.An intramolecular SH3-domain interaction regulates c-Abl activity.Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527.Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-srcSrc kinase conformational activation: thermodynamics, pathways, and mechanisms.Integrin alpha9beta1: Unique signaling pathways reveal diverse biological roles.Regulation of T-cell receptor signalling by membrane microdomains.Src regulated by C-terminal phosphorylation is monomericConformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides.Src as a potential therapeutic target in non-small-cell lung cancer.Replacement of threonine 558, a critical site of phosphorylation of moesin in vivo, with aspartate activates F-actin binding of moesin. Regulation by conformational change.Selective interaction of LAT (linker of activated T cells) with the open-active form of Lck in lipid rafts reveals a new mechanism for the regulation of Lck in T cells.Attenuation of adhesion-dependent signaling and cell spreading in transformed fibroblasts lacking protein tyrosine phosphatase-1B.CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck.Conformation-selective inhibitors reveal differences in the activation and phosphate-binding loops of the tyrosine kinases Abl and Src.The catalytic activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motilityAC-93253 iodide, a novel Src inhibitor, suppresses NSCLC progression by modulating multiple Src-related signaling pathways.TCR-induced T cell activation leads to simultaneous phosphorylation at Y505 and Y394 of p56(lck) residues.Src Promotes Metastasis of Human Non-Small Cell Lung Cancer Cells through Fn14-Mediated NF-κB Signaling.
P2860
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P2860
Structural differences between repressed and derepressed forms of p60c-src
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Structural differences between repressed and derepressed forms of p60c-src
@ast
Structural differences between repressed and derepressed forms of p60c-src
@en
type
label
Structural differences between repressed and derepressed forms of p60c-src
@ast
Structural differences between repressed and derepressed forms of p60c-src
@en
prefLabel
Structural differences between repressed and derepressed forms of p60c-src
@ast
Structural differences between repressed and derepressed forms of p60c-src
@en
P2860
P356
P1476
Structural differences between repressed and derepressed forms of p60c-src
@en
P2093
A MacAuley
J A Cooper
P2860
P304
P356
10.1128/MCB.9.6.2648
P407
P577
1989-06-01T00:00:00Z