Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain - Wikidata - wikimedia - TriplyDB

Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain

Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain

http://www.wikidata.org/entity/Q28303275

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Leukocyte tyrosine kinase functions in pigment cell development 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 The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts Impaired flow-induced dilation in mesenteric resistance arteries from receptor protein tyrosine phosphatase-mu-deficient mice The lysyl oxidase propeptide interacts with the receptor-type protein tyrosine phosphatase kappa and inhibits β-catenin transcriptional activity in lung cancer cells Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesion Dynamic interaction of PTPmu with multiple cadherins in vivo Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn 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 Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion A novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase mu 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 Meprins, membrane-bound and secreted astacin metalloproteinases Cell surface expression of receptor protein tyrosine phosphatase RPTP mu is regulated by cell-cell contact Protein tyrosine phosphatase kappa and SHP-1 are involved in the regulation of cell-cell contacts at adherens junctions in the exocrine pancreas PTPmu regulates N-cadherin-dependent neurite outgrowth 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 Receptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates the catenin p120(ctn)Expression of receptor tyrosine phosphatases during development of the retinotectal projection of the chick Receptor protein tyrosine phosphatases in nervous system development Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers Multimeric structure of the secreted meprin A metalloproteinase and characterization of the functional protomer Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells 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 Rho GTPases regulate PTPmu-mediated nasal neurite outgrowth and temporal repulsion of retinal ganglion cell neurons RPTP delta and the novel protein tyrosine phosphatase RPTP psi are expressed in restricted regions of the developing central nervous system A novel protein-tyrosine phosphatase related to the homotypically adhering kappa and mu receptors Molecular cloning of POEM: a novel adhesion molecule that interacts with alpha8beta1 integrin The transmembrane protein-tyrosine phosphatase LAR modulates signaling by multiple receptor tyrosine kinases Receptor type protein tyrosine phosphatase-kappa mediates cross-talk between transforming growth factor-beta and epidermal growth factor receptor signaling pathways in human keratinocytes An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells Involvement of breast epithelial-stromal interactions in the regulation of protein tyrosine phosphatase-gamma (PTPgamma) mRNA expression by estrogenically active agents.Protein tyrosine phosphatase kappa (PTPRK) is a negative regulator of adhesion and invasion of breast cancer cells, and associates with poor prognosis of breast cancer.

P2860

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P2860

Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain

http://www.wikidata.org/entity/Q28303275

description

1995 nî lūn-bûn

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1995 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի հունիսին հրատարակված գիտական հոդված

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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name

Homophilic interactions mediat ...... novel extracellular MAM domain

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Homophilic interactions mediat ...... novel extracellular MAM domain

@en

Homophilic interactions mediat ...... novel extracellular MAM domain

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type

label

Homophilic interactions mediat ...... novel extracellular MAM domain

@ast

Homophilic interactions mediat ...... novel extracellular MAM domain

@en

Homophilic interactions mediat ...... novel extracellular MAM domain

@nl

prefLabel

Homophilic interactions mediat ...... novel extracellular MAM domain

@ast

Homophilic interactions mediat ...... novel extracellular MAM domain

@en

Homophilic interactions mediat ...... novel extracellular MAM domain

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P1433

Journal of Biological Chemistry

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Homophilic interactions mediat ...... novel extracellular MAM domain

@en

P2093

G C Zondag

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

G M Koningstein

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J Sap

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

M F Gebbink

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W H Moolenaar

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Y P Jiang

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P2860

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

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

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

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A comprehensive set of sequence analysis programs for the VAX

An adhesive domain detected in functionally diverse receptors.

The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors.

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14247-50

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