Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.
about
A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion.C-terminal Src kinase associates with ligand-stimulated insulin-like growth factor-I receptorPaxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeletonRoles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factorRNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localizationLeupaxin is a novel LIM domain protein that forms a complex with PYK2Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAKStructural basis for the recognition of c-Src by its inactivator CskAssociation of csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cellsThe tyrosine kinase Csk dimerizes through Its SH3 domainCharacterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cellsIntroduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinasesMonocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteinsMouse disabled (mDab1): a Src binding protein implicated in neuronal developmentSH2 domain-mediated interaction of inhibitory protein tyrosine kinase Csk with protein tyrosine phosphatase-HSCFA new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migrationDok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signalingA truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylationPaxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase.An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organizationOverexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreadingDifferential effects of B cell receptor and B cell receptor-FcgammaRIIB1 engagement on docking of Csk to GTPase-activating protein (GAP)-associated p62Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains.PAG3/Papalpha/KIAA0400, a GTPase-activating protein for ADP-ribosylation factor (ARF), regulates ARF6 in Fcgamma receptor-mediated phagocytosis of macrophagesPaxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling.Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesionA p130Cas tyrosine phosphorylated substrate domain decoy disrupts v-crk signalingStructure of the carboxyl-terminal Src kinase, CskIntegrins regulate the association and phosphorylation of paxillin by c-AblThe MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-KitProtein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesionThe related adhesion focal tyrosine kinase is tyrosine-phosphorylated after beta1-integrin stimulation in B cells and binds to p130casDirect association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytesTwo mechanisms activate PTPalpha during mitosisMultiple stimuli induce tyrosine phosphorylation of the Crk-binding sites of paxillinInteraction of bcl-2 with Paxillin through its BH4 domain is important during ureteric bud branchingp130cas but not paxillin is essential for Caco-2 intestinal epithelial cell spreading and migration on collagen IVCardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillinRole of protein-tyrosine phosphatase SHP2 in focal adhesion kinase down-regulation during neutrophil cathepsin G-induced cardiomyocytes anoikis
P2860
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P2860
Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.
description
1994 nî lūn-bûn
@nan
1994 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Analysis of the binding of the ...... d mitotic activation of c-Src.
@ast
Analysis of the binding of the ...... d mitotic activation of c-Src.
@en
type
label
Analysis of the binding of the ...... d mitotic activation of c-Src.
@ast
Analysis of the binding of the ...... d mitotic activation of c-Src.
@en
prefLabel
Analysis of the binding of the ...... d mitotic activation of c-Src.
@ast
Analysis of the binding of the ...... d mitotic activation of c-Src.
@en
P2093
P2860
P356
P1476
Analysis of the binding of the ...... d mitotic activation of c-Src.
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.9.3984
P407
P577
1994-04-01T00:00:00Z