Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion - sprookjes - yvandenbroek - TriplyDB

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

http://www.wikidata.org/entity/Q24541392

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Tumor-derived extracellular mutations of PTPRT /PTPrho are defective in cell adhesion Large-scale screening for novel low-affinity extracellular protein interactions A novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase mu Tumour suppressor function of protein tyrosine phosphatase receptor-T 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 Meprins, membrane-bound and secreted astacin metalloproteinases 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 Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2 Structural Plasticity of Eph Receptor A4 Facilitates Cross-Class Ephrin Signaling Crystal Structure of the Neuropilin-1 MAM Domain: Completing the Neuropilin-1 Ectodomain Picture Rho GTPases regulate PTPmu-mediated nasal neurite outgrowth and temporal repulsion of retinal ganglion cell neurons Targeting Neuroblastoma Cell Surface Proteins: Recommendations for Homology Modeling of hNET, ALK, and TrkB Role of Plasmodium falciparum thrombospondin-related anonymous protein in host-cell interactions.Redox modifier genes and pathways in amyotrophic lateral sclerosis.Genome-wide association study for backfat thickness in Canchim beef cattle using Random Forest approach Receptor protein tyrosine phosphatases and cancer: new insights from structural biology Protein-tyrosine phosphatases and cancer.High-throughput mutational analysis of the human cancer genome.Diverse injurious stimuli reduce protein tyrosine phosphatase-μ expression and enhance epidermal growth factor receptor signaling in human airway epithelia.Meprin A metalloproteinase and its role in acute kidney injury.Protein tyrosine phosphatases: structure-function relationships.Receptor-type tyrosine phosphatase ligands: looking for the needle in the haystack.Proteolytic maturation of α2δ represents a checkpoint for activation and neuronal trafficking of latent calcium channels.Phosphatase regulation of intercellular junctions.Loss of PTPRM associates with the pathogenic development of colorectal adenoma-carcinoma sequence.Expression of recombinant glycoproteins in mammalian cells: towards an integrative approach to structural biology.Disruption of alpha-mannosidase processing induces non-canonical hybrid-type glycosylation.Glycoprotein structural genomics: solving the glycosylation problem.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.Differential activities in adhesion and neurite growth of fibronectin type III repeats in the PTP-delta extracellular domain.Structural Mechanism for Modulation of Synaptic Neuroligin-Neurexin Signaling by MDGA Proteins.Stability of proICA512/IA-2 and its targeting to insulin secretory granules require β4-sheet-mediated dimerization of its ectodomain in the endoplasmic reticulum.Single cell molecular recognition of migrating and invading tumor cells using a targeted fluorescent probe to receptor PTPmu.Cysteines in the neuropilin-2 MAM domain modulate receptor homooligomerization and signal transduction.Detection and Identification of Ligands for Mammalian RPTP Extracellular Domains.

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P2860

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

http://www.wikidata.org/entity/Q24541392

description

2006 nî lūn-bûn

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2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2006 թվականի փետրվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

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Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

@en

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

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type

label

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

@ast

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

@en

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

@nl

prefLabel

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

@ast

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

@en

Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

@nl

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SJ.EMBOJ.7600974

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The EMBO Journal

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Molecular analysis of receptor protein tyrosine phosphatase mu-mediated cell adhesion

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P2093

Alexandru Radu Aricescu

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

Philip Anton van der Merwe

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Wai-Ching Hon

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Weixian Lu

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P2860

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

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

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

Identification and characterization of RPTP rho, a novel RPTP mu/kappa-like receptor protein tyrosine phosphatase whose expression is restricted to the central nervous system

Dynamic interaction of PTPmu with multiple cadherins in vivo

High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells

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

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701-12

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10.1038/SJ.EMBOJ.7600974

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4

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25

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Christian Siebold

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2006-02-22T00:00:00Z

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7316785

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16456543

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1383555

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