Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
about
Characterization of the interactions between the active site of a protein tyrosine kinase and a divalent metal activator.Structural basis for the recognition of c-Src by its inactivator CskDistal loop flexibility of a regulatory domain modulates dynamics and activity of C-terminal SRC kinase (csk)Proteins at work: a combined small angle X-RAY scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscapeIdentification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases.Conformational basis for SH2-Tyr(P)527 binding in Src inactivation.C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)--endogenous negative regulators of Src-family protein kinases.c-Src-mediated epithelial cell migration and invasion regulated by PDZ binding site.Microtubule-mediated Src tyrosine kinase trafficking in neuronal growth cones.Determination of the substrate-docking site of protein tyrosine kinase C-terminal Src kinaseProfiling the substrate specificity of protein kinases by on-bead screening of peptide librariesExpression and purification of Src-family kinases for solution NMR studies.Variant estrogen receptor-c-Src molecular interdependence and c-Src structural requirements for endothelial NO synthase activation.Direct and specific inactivation of protein tyrosine kinases in the Src and FGFR families by reversible cysteine oxidation.Optimized bacterial expression and purification of the c-Src catalytic domain for solution NMR studies.Structural elements and allosteric mechanisms governing regulation and catalysis of CSK-family kinases and their inhibition of Src-family kinases.A novel non-catalytic mechanism employed by the C-terminal Src-homologous kinase to inhibit Src-family kinase activity.Mechanistic insights into the activation of oncogenic forms of EGF receptor.Csk mediates G-protein-coupled lysophosphatidic acid receptor-induced inhibition of membrane-bound guanylyl cyclase activity.Docking-based substrate recognition by the catalytic domain of a protein tyrosine kinase, C-terminal Src kinase (Csk).Immunoreceptor tyrosine-based inhibitory motif (ITIM)-mediated inhibitory signaling is regulated by sequential phosphorylation mediated by distinct nonreceptor tyrosine kinases: a case study involving PECAM-1Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine.The C-terminal Src inhibitory kinase (Csk)-mediated tyrosine phosphorylation is a novel molecular mechanism to limit P2X3 receptor function in mouse sensory neurons.SRC tail phosphorylation is limited by structural changes in the regulatory tyrosine kinase Csk.Phosphoryl transfer step in the C-terminal Src kinase controls Src recognition.
P2860
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P2860
Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
@ast
Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
@en
type
label
Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
@ast
Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
@en
prefLabel
Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
@ast
Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
@en
P2093
P356
P1433
P1476
Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.
@en
P2093
P304
P356
10.1021/BI002342N
P407
P577
2001-02-01T00:00:00Z