Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation
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Genomic structure and alternative splicing of murine R2B receptor protein tyrosine phosphatases (PTPkappa, mu, rho and PCP-2)Intramolecular interactions between the juxtamembrane domain and phosphatase domains of receptor protein-tyrosine phosphatase RPTPmu. Regulation of catalytic activityThe PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contactsReceptor-type protein-tyrosine phosphatase-kappa regulates epidermal growth factor receptor functionE-cadherin promotes retinal ganglion cell neurite outgrowth in a protein tyrosine phosphatase-mu-dependent mannerThe receptor protein-tyrosine phosphatase PTPmu interacts with IQGAP1Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivoThe conserved immunoglobulin domain controls the subcellular localization of the homophilic adhesion receptor protein-tyrosine phosphatase muThe LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesionMolecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoformsDynamic interaction of PTPmu with multiple cadherins in vivoThe LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesionsExpression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell densityThe second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigmaIncrease in receptor-like protein tyrosine phosphatase activity and expression level on density-dependent growth arrest of endothelial cellsMolecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphataseVE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contactsMolecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesionFurin-, ADAM 10-, and gamma-secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of beta-catenin's transcriptional activityTight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domainsA novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase muReceptor tyrosine phosphatase R-PTP-kappa mediates homophilic bindingProtein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transductionCancer-derived mutations in the fibronectin III repeats of PTPRT/PTPrho inhibit cell-cell aggregationGenomic organization and alternative splicing of the human and mouse RPTPrho genesIdentification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migrationTumor-derived extracellular fragments of receptor protein tyrosine phosphatases (RPTPs) as cancer molecular diagnostic toolsCharacterization of the adhesive properties of the type IIb subfamily receptor protein tyrosine phosphatasesPTPmu suppresses glioma cell migration and dispersalProteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migrationReceptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivoBCCIP associates with the receptor protein tyrosine phosphatase PTPmualpha3beta1 integrin-CD151, a component of the cadherin-catenin complex, regulates PTPmu expression and cell-cell adhesionCell surface expression of receptor protein tyrosine phosphatase RPTP mu is regulated by cell-cell contactReceptor protein tyrosine phosphatase micro regulates the paracellular pathway in human lung microvascular endotheliaCellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processingProtein tyrosine phosphatase kappa and SHP-1 are involved in the regulation of cell-cell contacts at adherens junctions in the exocrine pancreasPTPmu regulates N-cadherin-dependent neurite outgrowthDimerization of receptor protein-tyrosine phosphatase alpha in living cells
P2860
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P2860
Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation
description
1993 nî lūn-bûn
@nan
1993 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@ast
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@en
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@nl
type
label
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@ast
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@en
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@nl
prefLabel
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@ast
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@en
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@nl
P2093
P2860
P356
P1476
Homophilic binding of PTP mu, ...... mediate cell-cell aggregation
@en
P2093
S M Brady-Kalnay
P2860
P304
P356
10.1083/JCB.122.4.961
P407
P577
1993-08-01T00:00:00Z