Distal Interactions within the par3−VE-Cadherin Complex, - Wikidata - awgldk - TriplyDB

Distal Interactions within the par3−VE-Cadherin Complex,

Distal Interactions within the par3−VE-Cadherin Complex,

http://www.wikidata.org/entity/Q27658843

about

The Tiam1 PDZ domain couples to Syndecan1 and promotes cell-matrix adhesion Membrane Binding and Modulation of the PDZ Domain of PICK1 A Conformational Switch in the CRIB-PDZ Module of Par-6 The Structure of the Tiam1 PDZ Domain/ Phospho-Syndecan1 Complex Reveals a Ligand Conformation that Modulates Protein Dynamics High-resolution structure of the Tiam1 PHn-CC-Ex domain Binding of Crumbs to the Par-6 CRIB-PDZ Module Is Regulated by Cdc42 Beyond the binding site: the role of the β₂-β₃ loop and extra-domain structures in PDZ domains Phosphorylation of a PDZ domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (PSD-95) protein, a membrane-associated guanylate kinase (MAGUK).Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligands.VE-PTP regulates VEGFR2 activity in stalk cells to establish endothelial cell polarity and lumen formation VE-cadherin interacts with cell polarity protein Pals1 to regulate vascular lumen formation.Structural and thermodynamic analysis of PDZ-ligand interactions.A VE-cadherin-PAR3-α-catenin complex regulates the Golgi localization and activity of cytosolic phospholipase A(2)α in endothelial cells.Conformational stabilization of FOX-DNA complex architecture to sensitize prostate cancer chemotherapy.Rab5-mediated VE-cadherin internalization regulates the barrier function of the lung microvascular endothelium.A novel pathway spatiotemporally activates Rac1 and redox signaling in response to fluid shear stress The emerging contribution of sequence context to the specificity of protein interactions mediated by PDZ domains.Polarizing pathways: balancing endothelial polarity, permeability, and lumen formation.Structures and target recognition modes of PDZ domains: recurring themes and emerging pictures.Selective targeting of MAPK family kinases JNK over p38 by rationally designed peptides as potential therapeutics for neurological disorders and epilepsy.Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.Structures of the human Pals1 PDZ domain with and without ligand suggest gated access of Crb to the PDZ peptide-binding groove

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P2860

Distal Interactions within the par3−VE-Cadherin Complex,

http://www.wikidata.org/entity/Q27658843

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Distal Interactions within the par3−VE-Cadherin Complex,

@ast

Distal Interactions within the par3−VE-Cadherin Complex,

@en

Distal Interactions within the par3−VE-Cadherin Complex,

@nl

type

label

Distal Interactions within the par3−VE-Cadherin Complex,

@ast

Distal Interactions within the par3−VE-Cadherin Complex,

@en

Distal Interactions within the par3−VE-Cadherin Complex,

@nl

prefLabel

Distal Interactions within the par3−VE-Cadherin Complex,

@ast

Distal Interactions within the par3−VE-Cadherin Complex,

@en

Distal Interactions within the par3−VE-Cadherin Complex,

@nl

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Distal Interactions within the par3−VE-Cadherin Complex,

@en

P2093

Brian F Volkman

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

Francis C Peterson

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

Robert C Tyler

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

P2860

ERBIN: a basolateral PDZ protein that interacts with the mammalian ERBB2/HER2 receptor

Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions

A distinct PAR complex associates physically with VE-cadherin in vertebrate endothelial cells

CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins

The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)

Internal recognition through PDZ domain plasticity in the Par-6-Pals1 complex

Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex

Novel mode of ligand recognition by the Erbin PDZ domain

Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm

PDZ domains of Par-3 as potential phosphoinositide signaling integrators

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951-7

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scholarly article

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4281015

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10.1021/BI9017335

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5

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49

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2010-02-09T00:00:00Z

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40846340

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20047332

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2819025

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