The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu - Wikidata - awgldk - TriplyDB

The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu

The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu

http://www.wikidata.org/entity/Q28256506

about

Involvement of nectin in inactivation of integrin alpha(v)beta(3) after the establishment of cell-cell adhesion The receptor protein-tyrosine phosphatase PTPmu interacts with IQGAP1 Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesion 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 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 Expression and genomic organization of zonadhesin-like genes in three species of fish give insight into the evolutionary history of a mosaic protein.Role of Neuropilin-1 in Diabetic Nephropathy 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 Laminin L4 domain structure resembles adhesion modules in ephrin receptor and other transmembrane glycoproteins Rho GTPases regulate PTPmu-mediated nasal neurite outgrowth and temporal repulsion of retinal ganglion cell neurons Genome wide SNP comparative analysis between EGFR and KRAS mutated NSCLC and characterization of two models of oncogenic cooperation in non-small cell lung carcinoma Diet1 functions in the FGF15/19 enterohepatic signaling axis to modulate bile acid and lipid levels Comparative description of ten transcriptomes of newly sequenced invertebrates and efficiency estimation of genomic sampling in non-model taxa The role of HOXB9 and miR-196a in head and neck squamous cell carcinoma Hydrogen Sulfide: A Therapeutic Candidate for Fibrotic Disease?Scavenger Receptor C Mediates Phagocytosis of White Spot Syndrome Virus and Restricts Virus Proliferation in Shrimp.Receptor protein tyrosine phosphatases and cancer: new insights from structural biology Diverse injurious stimuli reduce protein tyrosine phosphatase-μ expression and enhance epidermal growth factor receptor signaling in human airway epithelia.Protein tyrosine phosphatases: structure-function relationships.Receptor-type tyrosine phosphatase ligands: looking for the needle in the haystack.The malignant social network: cell-cell adhesion and communication in cancer stem cells Dimerization of protein tyrosine phosphatase sigma governs both ligand binding and isoform specificity.Protease domain glycans affect oligomerization, disulfide bond formation, and stability of the meprin A metalloprotease homo-oligomer.Proteomic Characterization of Pig Sperm Anterior Head Plasma Membrane Reveals Roles of Acrosomal Proteins in ZP3 Binding.Expression of Human MDGA1 Increases Cell Motility and Cell-Cell Adhesion and Reduces Adhesion to Extracellular Matrix Proteins in MDCK Cells Single cell molecular recognition of migrating and invading tumor cells using a targeted fluorescent probe to receptor PTPmu.Hydrogen sulfide attenuates the pathogenesis of pulmonary fibrosis induced by bleomycin in rats.Intersubunit and domain interactions of the meprin B metalloproteinase. Disulfide bonds and protein-protein interactions in the MAM and TRAF domains.Zebrafish Leucocyte tyrosine kinase controls iridophore establishment, proliferation and survival.Cysteines in the neuropilin-2 MAM domain modulate receptor homooligomerization and signal transduction.

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P2860

The MAM (meprin/A5-protein/PTPmu) domain is a homophilic binding site promoting the lateral dimerization of receptor-like protein-tyrosine phosphatase mu

http://www.wikidata.org/entity/Q28256506

description

2004 nî lūn-bûn

@nan

2004 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հունիսին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

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The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

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The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

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type

label

The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

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The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

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The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

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prefLabel

The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

@ast

The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

@en

The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

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P1433

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P1433

Journal of Biological Chemistry

P1476

The MAM (meprin/A5-protein/PTP ...... rotein-tyrosine phosphatase mu

@en

P2093

Hartmut Michel

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

Helmut Reiländer

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

Stefan A Denes

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

Stefan E Szedlacsek

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

Valeriu B Cismasiu

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

P2860

Crystal structure of the tandem phosphatase domains of RPTP LAR

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

Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin alpha8beta1 in the embryonic kidney

Cloning, expression and chromosomal localization of a new putative 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

Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding

Cell surface expression of receptor protein tyrosine phosphatase RPTP mu is regulated by cell-cell contact

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

PTPmu regulates N-cadherin-dependent neurite outgrowth

P304

26922-31

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scholarly article

P356

10.1074/JBC.M313115200

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P407

P433

26

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P478

279

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P577

2004-06-25T00:00:00Z

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P698

15084579

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