Receptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates the catenin p120(ctn)
about
Impaired flow-induced dilation in mesenteric resistance arteries from receptor protein tyrosine phosphatase-mu-deficient miceE-cadherin promotes retinal ganglion cell neurite outgrowth in a protein tyrosine phosphatase-mu-dependent mannerInvolvement of nectin in inactivation of integrin alpha(v)beta(3) after the establishment of cell-cell adhesionThe receptor protein-tyrosine phosphatase PTPmu interacts with IQGAP1The conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase muThe transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cellsTumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesionVE-cadherin regulates endothelial actin activating Rac and increasing membrane association of TiamVE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contactsMolecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesionIdentification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migrationProteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migrationBCCIP associates with the receptor protein tyrosine phosphatase PTPmuReceptor protein tyrosine phosphatase micro regulates the paracellular pathway in human lung microvascular endotheliaProtein tyrosine phosphatase kappa and SHP-1 are involved in the regulation of cell-cell contacts at adherens junctions in the exocrine pancreasRegulation of development and cancer by the R2B subfamily of RPTPs and the implications of proteolysisStructure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanismAssociation of connexin43 with a receptor protein tyrosine phosphataseThe MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase muRegulation of cell adhesion by protein-tyrosine phosphatases: II. Cell-cell adhesionReactive oxygen species in inflammation and tissue injuryG1 checkpoint failure and increased tumor susceptibility in mice lacking the novel p53 target PtprvIsolation and characterization of XKaiso, a transcriptional repressor that associates with the catenin Xp120(ctn) in Xenopus laevis.PTP-PEST targets a novel tyrosine site in p120 catenin to control epithelial cell motility and Rho GTPase activity.The epithelial splicing factors ESRP1 and ESRP2 positively and negatively regulate diverse types of alternative splicing events.Expression of receptor-type protein tyrosine phosphatase in developing and adult renal vasculaturep120 regulates endothelial permeability independently of its NH2 terminus and Rho bindingTurn-off, drop-out: functional state switching of cadherins.Loss of p120 catenin upregulates transcription of pro-inflammatory adhesion molecules in human endothelial cells.Role of tissue stroma in cancer cell invasion.RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation.Emerging roles for p120-catenin in cell adhesion and cancer.Regulation of adherens junction dynamics by phosphorylation switches.A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cellsPhosphorylation and isoform use in p120-catenin during development and tumorigenesisReceptor protein tyrosine phosphatases and cancer: new insights from structural biologyDiverse injurious stimuli reduce protein tyrosine phosphatase-μ expression and enhance epidermal growth factor receptor signaling in human airway epithelia.p120catenin alteration in cancer and its role in tumour invasion.p120-Catenin: a novel regulator of innate immunity and inflammation.
P2860
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P2860
Receptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates the catenin p120(ctn)
description
2000 nî lūn-bûn
@nan
2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@ast
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@en
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@nl
type
label
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@ast
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@en
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@nl
prefLabel
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@ast
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@en
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@nl
P2093
P2860
P356
P1476
Receptor protein-tyrosine phos ...... orylates the catenin p120(ctn)
@en
P2093
A B Reynolds
G C Zondag
W H Moolenaar
P2860
P304
P356
10.1074/JBC.275.15.11264
P407
P577
2000-04-14T00:00:00Z