Receptor protein tyrosine phosphatase micro regulates the paracellular pathway in human lung microvascular endothelia - Wikidata - wikimedia - TriplyDB

Receptor protein tyrosine phosphatase micro regulates the paracellular pathway in human lung microvascular endothelia

Receptor protein tyrosine phosphatase micro regulates the paracellular pathway in human lung microvascular endothelia

http://www.wikidata.org/entity/Q24675717

about

E-cadherin promotes retinal ganglion cell neurite outgrowth in a protein tyrosine phosphatase-mu-dependent manner Involvement of nectin in inactivation of integrin alpha(v)beta(3) after the establishment of cell-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 Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration BCCIP associates with the receptor protein tyrosine phosphatase PTPmu Regulation of Endothelial Adherens Junctions by Tyrosine Phosphorylation Regulation of development and cancer by the R2B subfamily of RPTPs and the implications of proteolysis Ve-ptp modulates vascular integrity by promoting adherens junction maturation Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism Regulation of cell adhesion by protein-tyrosine phosphatases: II. Cell-cell adhesion Expression of receptor-type protein tyrosine phosphatase in developing and adult renal vasculature Role of protein tyrosine phosphatase SHP2 in barrier function of pulmonary endothelium.Fibroblast growth factor signaling potentiates VE-cadherin stability at adherens junctions by regulating SHP2 Thrombospondin-1 opens the paracellular pathway in pulmonary microvascular endothelia through EGFR/ErbB2 activation.Angiopoietin-1 protects heart against ischemia/reperfusion injury through VE-cadherin dephosphorylation and myocardiac integrin-β1/ERK/caspase-9 phosphorylation cascade TRAF6 protein couples Toll-like receptor 4 signaling to Src family kinase activation and opening of paracellular pathway in human lung microvascular endothelia.Tyrosine phosphorylation and endothelial cell barrier regulation A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cells The tyrosine phosphatase SHP2 regulates recovery of endothelial adherens junctions through control of β-catenin phosphorylation Protein-tyrosine phosphatases and cancer.Diverse injurious stimuli reduce protein tyrosine phosphatase-μ expression and enhance epidermal growth factor receptor signaling in human airway epithelia.Cell-cell adhesion in lung endothelium.Adhesion and signaling molecules controlling the transmigration of leukocytes through endothelium.Deciphering the functional role of endothelial junctions by using in vivo models The counteradhesive proteins, thrombospondin 1 and SPARC/osteonectin, open the tyrosine phosphorylation-responsive paracellular pathway in pulmonary vascular endothelia.The regulation of vascular endothelial growth factor-induced microvascular permeability requires Rac and reactive oxygen species.The regulation of leucocyte transendothelial migration by endothelial signalling events.Phosphatase regulation of intercellular junctions.Relevance of endothelial junctions in leukocyte extravasation and vascular permeability.The malignant social network: cell-cell adhesion and communication in cancer stem cells Phosphatases and kinases as regulators of the endothelial barrier function.Similarities and differences in the regulation of leukocyte extravasation and vascular permeability.TLR4 signaling is coupled to SRC family kinase activation, tyrosine phosphorylation of zonula adherens proteins, and opening of the paracellular pathway in human lung microvascular endothelia.VE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF.Correlation of perfusion parameters with genes related to angiogenesis regulation in glioblastoma: a feasibility study.

P2860

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P2860

Receptor protein tyrosine phosphatase micro regulates the paracellular pathway in human lung microvascular endothelia

http://www.wikidata.org/entity/Q24675717

description

2005 nî lūn-bûn

@nan

2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի ապրիլին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

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2005年论文

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name

Receptor protein tyrosine phos ...... lung microvascular endothelia

@ast

Receptor protein tyrosine phos ...... lung microvascular endothelia

@en

Receptor protein tyrosine phos ...... lung microvascular endothelia

@nl

type

label

Receptor protein tyrosine phos ...... lung microvascular endothelia

@ast

Receptor protein tyrosine phos ...... lung microvascular endothelia

@en

Receptor protein tyrosine phos ...... lung microvascular endothelia

@nl

prefLabel

Receptor protein tyrosine phos ...... lung microvascular endothelia

@ast

Receptor protein tyrosine phos ...... lung microvascular endothelia

@en

Receptor protein tyrosine phos ...... lung microvascular endothelia

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S0002-9440(10)62343-7

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The American Journal of Pathology

P1476

Receptor protein tyrosine phos ...... lung microvascular endothelia

@en

P2093

Antonino Passaniti

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

Bradford A Young

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

Daniel J Angelini

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

Jeffrey D Hasday

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

Lewis H Romer

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

Nicholas K Tonks

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

Robert L Del Vecchio

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

Sang Won Hyun

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

Simeon E Goldblum

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

Timothy D Kiser

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

P2860

Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1

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

Contact inhibition of VEGF-induced proliferation requires vascular endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148

The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)

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

Association of human protein-tyrosine phosphatase kappa with members of the armadillo family

Dynamic interaction of PTPmu with multiple cadherins in vivo

Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases

Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density

E-cadherin and APC compete for the interaction with beta-catenin and the cytoskeleton

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1247-58

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scholarly article

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10.1016/S0002-9440(10)62343-7

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4

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166

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7943205

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15793303

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1602370

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