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Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

http://www.wikidata.org/entity/Q24615716

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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 activity Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo The lysyl oxidase propeptide interacts with the receptor-type protein tyrosine phosphatase kappa and inhibits β-catenin transcriptional activity in lung cancer cells The 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.1 Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesion Molecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoforms Dynamic interaction of PTPmu with multiple cadherins in vivo The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma Molecular cloning and characterization of PTP pi, a novel receptor-like protein-tyrosine phosphatase VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion Furin-, ADAM 10-, and gamma-secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of beta-catenin's transcriptional activity Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains Protein tyrosine phosphatases expression during development of mouse superior colliculus Protein tyrosine phosphatases--from housekeeping enzymes to master regulators of signal transduction Cancer-derived mutations in the fibronectin III repeats of PTPRT/PTPrho inhibit cell-cell aggregation Genomic organization and alternative splicing of the human and mouse RPTPrho genes Tumor-derived extracellular fragments of receptor protein tyrosine phosphatases (RPTPs) as cancer molecular diagnostic tools Characterization of the adhesive properties of the type IIb subfamily receptor protein tyrosine phosphatases PTPmu suppresses glioma cell migration and dispersal Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing Therapeutic approaches for celiac disease Regulation of development and cancer by the R2B subfamily of RPTPs and the implications of proteolysis Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu Structural basis of interaction between protein tyrosine phosphatase PCP-2 and beta-catenin Rho GTPases regulate PTPmu-mediated nasal neurite outgrowth and temporal repulsion of retinal ganglion cell neurons Regulation of cell adhesion by protein-tyrosine phosphatases: II. Cell-cell adhesion RPTP delta and the novel protein tyrosine phosphatase RPTP psi are expressed in restricted regions of the developing central nervous system Human protein tyrosine phosphatase-sigma: alternative splicing and inhibition by bisphosphonates Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain A novel protein-tyrosine phosphatase related to the homotypically adhering kappa and mu receptors Characterization of PTPRG in knockdown and phosphatase-inactive mutant mice and substrate trapping analysis of PTPRG in mammalian cells A mutant receptor tyrosine phosphatase, CD148, causes defects in vascular development

P2860

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P2860

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

http://www.wikidata.org/entity/Q24615716

description

1994 nî lūn-bûn

@nan

1994 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1994 թվականի հունվարին հրատարակված գիտական հոդված

@hy

1994年の論文

@ja

1994年論文

@yue

1994年論文

@zh-hant

1994年論文

@zh-hk

1994年論文

@zh-mo

1994年論文

@zh-tw

1994年论文

@wuu

name

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@ast

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@en

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@nl

type

label

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@ast

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@en

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@nl

prefLabel

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@ast

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@en

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@nl

P1433

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P1433

Molecular and Cellular Biology

P1476

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

@en

P2093

D Friedlander

http://www.w3.org/2001/XMLSchema#string

J Sap

http://www.w3.org/2001/XMLSchema#string

J Schlessinger

http://www.w3.org/2001/XMLSchema#string

M Grumet

http://www.w3.org/2001/XMLSchema#string

Y P Jiang

http://www.w3.org/2001/XMLSchema#string

P2860

Structural diversity and evolution of human receptor-like protein tyrosine phosphatases

Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase

Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases

The cloning of a receptor-type protein tyrosine phosphatase expressed in the central nervous system

Cell-cell adhesion mediated by a receptor-like protein tyrosine phosphatase

A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases

Expression of the receptor-linked protein tyrosine phosphatase LAR: proteolytic cleavage and shedding of the CAM-like extracellular region

Cell binding function of E-cadherin is regulated by the cytoplasmic domain

Cloning and characterization of R-PTP-kappa, a new member of the receptor protein tyrosine phosphatase family with a proteolytically cleaved cellular adhesion molecule-like extracellular region

Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation

P304

1-9

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scholarly article

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2796884

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P356

10.1128/MCB.14.1.1

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P433

1

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14

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1994-01-01T00:00:00Z

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8264577

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358350

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