Dimerization of receptor protein-tyrosine phosphatase alpha in living cells - Wikidata - thesis-toulmin - TriplyDB

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

http://www.wikidata.org/entity/Q24799594

about

Activation of Src and transformation by an RPTPα splice mutant found in human tumours Structural genomics of protein phosphatases Hydrophobic Matching Controls the Tilt and Stability of the Dimeric Platelet-derived Growth Factor Receptor (PDGFR) Transmembrane Segment Receptor protein tyrosine phosphatases in nervous system development Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu Redox regulation of dimerization of the receptor protein-tyrosine phosphatases RPTPalpha, LAR, RPTPmu and CD45 Regulation of cell adhesion by protein-tyrosine phosphatases: II. Cell-cell adhesion Two mechanisms activate PTPalpha during mitosis Homomultimerization of the coxsackievirus 2B protein in living cells visualized by fluorescence resonance energy transfer microscopy Optical molecular imaging for systems biology: from molecule to organism.Transmembrane homodimerization of receptor-like protein tyrosine phosphatases.Fluorescence lifetime measurements and biological imaging Mechanism of activation of protein kinase JAK2 by the growth hormone receptor.Monitoring caspase activity in living cells using fluorescent proteins and flow cytometry.Identification of function-regulating antibodies targeting the receptor protein tyrosine phosphatase sigma ectodomain.Protein tyrosine phosphatases: regulatory mechanisms.Visualization of protein interactions in living cells.Protein tyrosine phosphatase structure-function relationships in regulation and pathogenesis.Förster resonance energy transfer - an approach to visualize the spatiotemporal regulation of macromolecular complex formation and compartmentalized cell signaling Regulation of receptor protein-tyrosine phosphatase alpha by oxidative stress.Serine dephosphorylation of receptor protein tyrosine phosphatase alpha in mitosis induces Src binding and activation.Dimerization of protein tyrosine phosphatase sigma governs both ligand binding and isoform specificity.Monitoring protein interactions in the living cell through the fluorescence decays of the cyan fluorescent protein.Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase alpha dimers.Visualization of Protein Interactions in Living Cells.Suramin derivatives as inhibitors and activators of protein-tyrosine phosphatases.Defining the molecular basis of interaction between R3 receptor-type protein tyrosine phosphatases and VE-cadherin Reactive oxygen species and epidermal growth factor are antagonistic cues controlling SHP-2 dimerization.Measuring the proximity of T-lymphocyte CXCR4 and TCR by fluorescence resonance energy transfer (FRET).Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases.

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P2860

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

http://www.wikidata.org/entity/Q24799594

description

2001 nî lūn-bûn

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2001 թուականին հրատարակուած գիտական յօդուած

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2001 թվականին հրատարակված գիտական հոդված

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2001年の論文

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年學術文章

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name

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

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Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

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Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

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type

label

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

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Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

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Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

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prefLabel

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

@ast

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

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Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

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BMC Cell Biology

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Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

@en

P2093

C Blanchetot

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

G Jiang

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J Overvoorde

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J den Hertog

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L G Tertoolen

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T Hunter

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T W Gadella

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P2860

Crystal structure of the tandem phosphatase domains of RPTP LAR

Protein tyrosine phosphatase alpha (PTPalpha) and contactin form a novel neuronal receptor complex linked to the intracellular tyrosine kinase fyn

A phosphotyrosine displacement mechanism for activation of Src by PTPalpha

Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta

Intramolecular interactions between the juxtamembrane domain and phosphatase domains of receptor protein-tyrosine phosphatase RPTPmu. Regulation of catalytic activity

Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo

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

The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma

Cloning and expression of a widely expressed receptor tyrosine phosphatase

Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains

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