Structural basis for the recognition of c-Src by its inactivator Csk
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The tyrosine kinase Csk dimerizes through Its SH3 domainComparative Analysis of Mutant Tyrosine Kinase Chemical Rescue † ‡Novel Isoform-Specific Interfaces Revealed by PKA RIIβ Holoenzyme StructuresSplit green fluorescent protein as a modular binding partner for protein crystallizationCrystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motifDynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its ActivityPIP kinases define PI4,5P₂signaling specificity by association with effectorsTheoretical Insights Reveal Novel Motions in Csk's SH3 Domain That Control Kinase Activation.SH2-catalytic domain linker heterogeneity influences allosteric coupling across the SFK family.Distal loop flexibility of a regulatory domain modulates dynamics and activity of C-terminal SRC kinase (csk)Two-state dynamics of the SH3-SH2 tandem of Abl kinase and the allosteric role of the N-capThe autoimmunity risk variant LYP-W620 cooperates with CSK in the regulation of TCR signaling.Protein kinases: evolution of dynamic regulatory proteinsProteins at work: a combined small angle X-RAY scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscapeSH2-dependent autophosphorylation within the Tec family kinase Itk.Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases.Application of protein engineering to enhance crystallizability and improve crystal properties.It's all in the crystals…The role of entropy and polarity in intermolecular contacts in protein crystalsInhibition of gluconeogenesis in primary hepatocytes by stromal cell-derived factor-1 (SDF-1) through a c-Src/Akt-dependent signaling pathwayLigand-induced global transitions in the catalytic domain of protein kinase A.Defining the substrate specificity determinants recognized by the active site of C-terminal Src kinase-homologous kinase (CHK) and identification of β-synuclein as a potential CHK physiological substrate.C-terminal Src kinase (Csk)-mediated phosphorylation of eukaryotic elongation factor 2 (eEF2) promotes proteolytic cleavage and nuclear translocation of eEF2The Haemophilus ducreyi LspA1 protein inhibits phagocytosis by using a new mechanism involving activation of C-terminal Src kinase.PSTPIP2 dysregulation contributes to aberrant terminal differentiation in GATA-1-deficient megakaryocytes by activating LYNIdentification of the PTPN22 functional variant R620W as susceptibility genetic factor for giant cell arteritis.Profiling the substrate specificity of protein kinases by on-bead screening of peptide librariesSystems level analysis of systemic sclerosis shows a network of immune and profibrotic pathways connected with genetic polymorphisms.Improvement of the crystallizability and expression of an RNA crystallization chaperoneRedox regulation of protein kinases.Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms.Small molecule inhibition of Csk alters affinity recognition by T cells.Phospho-selective mechanisms of arrestin conformations and functions revealed by unnatural amino acid incorporation and (19)F-NMR.Structural Basis for Noncanonical Substrate Recognition of Cofilin/ADF Proteins by LIM KinasesDirect and specific inactivation of protein tyrosine kinases in the Src and FGFR families by reversible cysteine oxidation.Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomicsSrc family kinases as mediators of endothelial permeability: effects on inflammation and metastasis.Tyrosine phosphorylation: thirty years and counting.Conformational snapshots of Tec kinases during signaling.Substrate recognition of PLCγ1 via a specific docking surface on Itk.
P2860
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P2860
Structural basis for the recognition of c-Src by its inactivator Csk
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structural basis for the recognition of c-Src by its inactivator Csk
@ast
Structural basis for the recognition of c-Src by its inactivator Csk
@en
Structural basis for the recognition of c-Src by its inactivator Csk
@en-gb
Structural basis for the recognition of c-Src by its inactivator Csk
@nl
type
label
Structural basis for the recognition of c-Src by its inactivator Csk
@ast
Structural basis for the recognition of c-Src by its inactivator Csk
@en
Structural basis for the recognition of c-Src by its inactivator Csk
@en-gb
Structural basis for the recognition of c-Src by its inactivator Csk
@nl
altLabel
Structural Basis for the Recognition of c-Src by Its Inactivator Csk
@en
prefLabel
Structural basis for the recognition of c-Src by its inactivator Csk
@ast
Structural basis for the recognition of c-Src by its inactivator Csk
@en
Structural basis for the recognition of c-Src by its inactivator Csk
@en-gb
Structural basis for the recognition of c-Src by its inactivator Csk
@nl
P2860
P1433
P1476
Structural basis for the recognition of c-Src by its inactivator Csk
@en
P2093
Nicholas M Levinson
Philip A Cole
P2860
P304
P356
10.1016/J.CELL.2008.05.051
P407
P577
2008-07-11T00:00:00Z