Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
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A phosphotyrosine displacement mechanism for activation of Src by PTPalphaProtein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylationThe conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase muActivation of Src and transformation by an RPTPα splice mutant found in human tumoursReceptor protein tyrosine phosphatase-receptor tyrosine kinase substrate screen identifies EphA2 as a target for LAR in cell migrationA novel mechanism for Wnt activation of canonical signaling through the LRP6 receptorMolecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesionThe crystal structure of human receptor protein tyrosine phosphatase kappa phosphatase domain 1Dimerization of receptor protein-tyrosine phosphatase alpha in living cellsStructure determination of T cell protein-tyrosine phosphataseStructural genomics of protein phosphatasesStructure of the catalytic domain of protein tyrosine phosphatase sigma in the sulfenic acid formMultiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPsReceptor protein tyrosine phosphatases in nervous system developmentMultimerization of the protein-tyrosine phosphatase (PTP)-like insulin-dependent diabetes mellitus autoantigens IA-2 and IA-2beta with receptor PTPs (RPTPs). Inhibition of RPTPalpha enzymatic activityIntra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatasesMeeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalphaModulation of the proteoglycan receptor PTPσ promotes recovery after spinal cord injuryThe MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase muRedox regulation of dimerization of the receptor protein-tyrosine phosphatases RPTPalpha, LAR, RPTPmu and CD45Regulation of cell adhesion by protein-tyrosine phosphatases: II. Cell-cell adhesionReciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatasesTwo mechanisms activate PTPalpha during mitosisDimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilonProtein tyrosine phosphatase receptor type Z is inactivated by ligand-induced oligomerizationGain control of N-methyl-D-aspartate receptor activity by receptor-like protein tyrosine phosphatase alphaAssociation of tyrosine phosphatase epsilon with microtubules inhibits phosphatase activity and is regulated by the epidermal growth factor receptor.Neuroblastoma tumorigenesis is regulated through the Nm23-H1/h-Prune C-terminal interaction.A directed screen for genes involved in Drosophila blood cell activationA monoclonal antibody against CD148, a receptor-like tyrosine phosphatase, inhibits endothelial-cell growth and angiogenesisAn extracellular ligand increases the specific activity of the receptor-like protein tyrosine phosphatase DEP-1.Transmembrane homodimerization of receptor-like protein tyrosine phosphatases.Protein tyrosine phosphatases ε and α perform nonredundant roles in osteoclasts.Receptor-like protein tyrosine phosphatase alpha homodimerizes on the cell surface.Laforin, a dual specificity phosphatase involved in Lafora disease, is present mainly as monomeric form with full phosphatase activityStructure and catalytic mechanism of human protein tyrosine phosphatome.Selected glimpses into the activation and function of Src kinase.Purification and characterization of protein tyrosine phosphatase PTP-MEG2.Signaling receptome: a genomic and evolutionary perspective of plasma membrane receptors involved in signal transduction.Functional significance of the LAR receptor protein tyrosine phosphatase family in development and diseases.
P2860
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P2860
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@ast
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@en
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@nl
type
label
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@ast
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@en
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@nl
prefLabel
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@ast
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@en
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@nl
P2093
P2860
P356
P1433
P1476
Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
@en
P2093
P2860
P2888
P304
P356
10.1038/44170
P407
P577
1999-10-07T00:00:00Z
P6179
1005592473