von Willebrand factor binding to platelet GpIb initiates signals for platelet activation. - Wikidata - wikimedia - TriplyDB

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

http://www.wikidata.org/entity/Q34208569

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Interaction of Bruton's tyrosine kinase and protein kinase Ctheta in platelets. Cross-talk between tyrosine and serine/threonine kinases Glycoprotein Ibalpha forms disulfide bonds with 2 glycoprotein Ibbeta subunits in the resting platelet.Clinical lung xenotransplantation--what donor genetic modifications may be necessary?The unfolded von Willebrand factor response in bloodstream: the self-association perspective Specific heteromeric association of four transmembrane peptides derived from platelet glycoprotein Ib-IX complex Platelet activation by von Willebrand factor requires coordinated signaling through thromboxane A2 and Fc gamma IIA receptor Primary arrest of circulating platelets on collagen involves phosphorylation of Syk, cortactin and focal adhesion kinase: studies under flow conditions Lateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin alpha IIbbeta 3 Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ib alpha Interaction of platelet glycoprotein V with glycoprotein Ib-IX regulates expression of the glycoproteins and binding of von Willebrand factor to glycoprotein Ib-IX in transfected cells Glycoprotein IIb-IIIa-dependent aggregation by glycoprotein Ibalpha is reinforced by a Src family kinase inhibitor (PP1)-sensitive signalling pathway Localization of the adhesion receptor glycoprotein Ib-IX-V complex to lipid rafts is required for platelet adhesion and activation Proteasome proteolysis supports stimulated platelet function and thrombosis [Thrombocytopathy and blood complications in uremia].Low shear stress can initiate von Willebrand factor-dependent platelet aggregation in patients with type IIB and platelet-type von Willebrand disease.Three-dimensional multi-scale model of deformable platelets adhesion to vessel wall in blood flow.Platelet adhesion receptors: novel targets for anti-thrombotic therapy.The human endogenous circadian system causes greatest platelet activation during the biological morning independent of behaviors Regulation of glycoprotein Ib-IX-von Willebrand factor interaction by cAMP-dependent protein kinase-mediated phosphorylation at Ser 166 of glycoprotein Ib(beta).Carboxypeptidase U at the interface between coagulation and fibrinolysis.Role of 14-3-3ζ in platelet glycoprotein Ibα-von Willebrand factor interaction-induced signaling Analysis of the roles of 14-3-3 in the platelet glycoprotein Ib-IX-mediated activation of integrin alpha(IIb)beta(3) using a reconstituted mammalian cell expression model The role of Akt in the signaling pathway of the glycoprotein Ib-IX induced platelet activation Structural basis for the specific inhibition of glycoprotein Ibα shedding by an inhibitory antibody Src family tyrosine kinase Lyn mediates VWF/GPIb-IX-induced platelet activation via the cGMP signaling pathway.LIM kinase-1 selectively promotes glycoprotein Ib-IX-mediated TXA2 synthesis, platelet activation, and thrombosis.Defective Association of the Platelet Glycoprotein Ib-IX Complex with the Glycosphingolipid-Enriched Membrane Domain Inhibits Murine Thrombus and Atheroma Formation The membrane-proximal intermolecular disulfide bonds in glycoprotein Ib influence receptor binding to von Willebrand factor.Distinct mechanisms of platelet aggregation as a consequence of different shearing flow conditions.Multiscale modeling of platelet adhesion and thrombus growth.Platelet receptors activated via mulitmerization: glycoprotein VI, GPIb-IX-V, and CLEC-2.Drug-drug interaction between NSAIDS and low-dose aspirin: a focus on cardiovascular and GI toxicity.The cytoplasmic domain of the alpha-subunit of glycoprotein (GP) Ib mediates attachment of the entire GP Ib-IX complex to the cytoskeleton and regulates von Willebrand factor-induced changes in cell morphology.Dynamic force spectroscopy of glycoprotein Ib-IX and von Willebrand factor.A monoclonal antibody recognizes a von Willebrand factor domain within the amino-terminal portion of the subunit that modulates the function of the glycoprotein IB- and IIB/IIIA-binding domains.Platelet sequestration and activation during GalTKO.hCD46 pig lung perfusion by human blood is primarily mediated by GPIb, GPIIb/IIIa, and von Willebrand Factor.Shear-stress-induced von Willebrand factor binding to platelets causes the activation of tyrosine kinase(s).Platelet dysfunction contributes to bleeding complications in patients with probable leptospirosis.Neutrophil proteinase cathepsin G is proteolytically active on the human platelet glycoprotein Ib-IX receptor: characterization of the cleavage sites within the glycoprotein Ib alpha subunit.A critical role for 14-3-3zeta protein in regulating the VWF binding function of platelet glycoprotein Ib-IX and its therapeutic implications.

P2860

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P2860

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

http://www.wikidata.org/entity/Q34208569

description

1991 nî lūn-bûn

@nan

1991 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1991 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

1991年の論文

@ja

1991年論文

@yue

1991年論文

@zh-hant

1991年論文

@zh-hk

1991年論文

@zh-mo

1991年論文

@zh-tw

1991年论文

@wuu

name

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@ast

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@en

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@nl

type

label

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@ast

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@en

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@nl

prefLabel

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@ast

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@en

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@nl

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Journal of Clinical Investigation

P1476

von Willebrand factor binding to platelet GpIb initiates signals for platelet activation.

@en

P2093

A I Schafer

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

J L Moake

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M H Kroll

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R I Handin

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T S Harris

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A new generation of Ca2+ indicators with greatly improved fluorescence properties

Platelet activation by CD9 monoclonal antibodies is mediated by the Fc gamma II receptor.

Defective ristocetin-induced platelet aggregation in von Willebrand's disease and its correction by factor VIII

Unusually large plasma factor VIII:von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura.

A murine monoclonal antibody that completely blocks the binding of fibrinogen to platelets produces a thrombasthenic-like state in normal platelets and binds to glycoproteins IIb and/or IIIa

Asialo von Willebrand factor interactions with platelets. Interdependence of glycoproteins Ib and IIb/IIIa for binding and aggregation.

A new murine monoclonal antibody reports an activation-dependent change in the conformation and/or microenvironment of the platelet glycoprotein IIb/IIIa complex

Involvement of large plasma von Willebrand factor (vWF) multimers and unusually large vWF forms derived from endothelial cells in shear stress-induced platelet aggregation.

Interaction of asialo von Willebrand factor with glycoprotein Ib induces fibrinogen binding to the glycoprotein IIb/IIIa complex and mediates platelet aggregation.

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1568-1573

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scholarly article

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10.1172/JCI115468

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5

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88

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1991-11-01T00:00:00Z

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1939645

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295673

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