Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation - sprookjes - yvandenbroek - TriplyDB

Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation

Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation

http://www.wikidata.org/entity/Q27667426

about

Platelet Activation and Thrombus Formation over IgG Immune Complexes Requires Integrin αIIbβ3 and Lyn Kinase.Regulation of endothelial cell barrier function by antibody-driven affinity modulation of platelet endothelial cell adhesion molecule-1 (PECAM-1)Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10.Systems model of T cell receptor proximal signaling reveals emergent ultrasensitivity.Juxtamembrane contribution to transmembrane signaling.Distinct sites within the vascular cell adhesion molecule-1 (VCAM-1) cytoplasmic domain regulate VCAM-1 activation of calcium fluxes versus Rac1 during leukocyte transendothelial migration.An immunoreceptor tyrosine-based inhibition motif in varicella-zoster virus glycoprotein B regulates cell fusion and skin pathogenesis.Multisite Phosphorylation Modulates the T Cell Receptor ζ-Chain Potency but not the Switchlike Response.Endothelial functions of platelet/endothelial cell adhesion molecule-1 (CD31).Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs.PECAM-1: regulator of endothelial junctional integrity.ITIM receptors: more than just inhibitors of platelet activation.Immunoreceptor tyrosine-based inhibitory motif (ITIM)-mediated inhibitory signaling is regulated by sequential phosphorylation mediated by distinct nonreceptor tyrosine kinases: a case study involving PECAM-1 The adhesion molecule PECAM-1 enhances the TGF-β-mediated inhibition of T cell function.Ca2+ regulates T-cell receptor activation by modulating the charge property of lipids.CRISPR-mediated deletion of the PECAM-1 cytoplasmic domain increases receptor lateral mobility and strengthens endothelial cell junctional integrity.Mechanotransduction properties of the cytoplasmic tail of PECAM-1.Negative regulators of platelet activation and adhesion.

P2860

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P2860

Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation

http://www.wikidata.org/entity/Q27667426

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Residues within a lipid-associ ...... le, sequential phosphorylation

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Residues within a lipid-associ ...... le, sequential phosphorylation

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Residues within a lipid-associ ...... le, sequential phosphorylation

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Residues within a lipid-associ ...... le, sequential phosphorylation

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Residues within a lipid-associ ...... le, sequential phosphorylation

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Residues within a lipid-associ ...... le, sequential phosphorylation

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Residues within a lipid-associ ...... le, sequential phosphorylation

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Residues within a lipid-associ ...... le, sequential phosphorylation

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Residues within a lipid-associ ...... le, sequential phosphorylation

@en

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Betsy L Lytle

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

Brian F Volkman

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Cathy Paddock

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Debra K Newman

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Francis C Peterson

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Peter J Newman

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Trudy Holyst

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P2860

Intrinsically unstructured proteins and their functions

Platelet-endothelial cell adhesion molecule-1 (CD31), a scaffolding molecule for selected catenin family members whose binding is mediated by different tyrosine and serine/threonine phosphorylation

PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily

Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2

Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Regulation of T Cell Receptor Activation by Dynamic Membrane Binding of the CD3ɛ Cytoplasmic Tyrosine-Based Motif

Refinement of protein structures in explicit solvent

Automated NMR structure calculation with CYANA

The Xplor-NIH NMR molecular structure determination package

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6012-23

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scholarly article

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10.1182/BLOOD-2010-11-317867

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22

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phosphorylation

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