The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin. - Test2 - elhamkhani - TriplyDB

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

http://www.wikidata.org/entity/Q36375314

about

ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factor Deadly allies: the fatal interplay between platelets and metastasizing cancer cells P-Selectin glycoprotein ligand 1 (PSGL-1) is expressed on platelets and can mediate platelet-endothelial interactions in vivo Platelets in Pulmonary Immune Responses and Inflammatory Lung Diseases Crystal structure of the platelet glycoprotein Ib(alpha) N-terminal domain reveals an unmasking mechanism for receptor activation Platelets and platelet adhesion molecules: novel mechanisms of thrombosis and anti-thrombotic therapies Redistribution of glycoprotein Ib within platelets in response to protease-activated receptors 1 and 4: roles of cytoskeleton and calcium Biosynthesis and intracellular post-translational processing of normal and mutant platelet glycoprotein GPIb-IX Bernard-Soulier syndrome The role of platelets in acute lung injury (ALI)Complete reversal of acid-induced acute lung injury by blocking of platelet-neutrophil aggregation.The role of platelet adhesion receptor GPIbalpha far exceeds that of its main ligand, von Willebrand factor, in arterial thrombosis.Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF.Alpha1G T-type calcium channel selectively regulates P-selectin surface expression in pulmonary capillary endothelium.Genetic deletion of platelet glycoprotein Ib alpha but not its extracellular domain protects from atherosclerosis.Multi-ligand poly(L-lactic-co-glycolic acid) nanoparticles inhibit activation of endothelial cells.Hemostatic and hematological abnormalities in gain-of-function fps/fes transgenic mice are associated with the angiogenic phenotype.Role for platelet glycoprotein Ib-IX and effects of its inhibition in endotoxemia-induced thrombosis, thrombocytopenia, and mortality.Force-induced cleavage of single VWFA1A2A3 tridomains by ADAMTS-13.Large-scale genomic studies reveal central role of ABO in sP-selectin and sICAM-1 levels GPVI and GPIbα mediate staphylococcal superantigen-like protein 5 (SSL5) induced platelet activation and direct toward glycans as potential inhibitors.Platelet recruitment to the inflamed glomerulus occurs via an alphaIIbbeta3/GPVI-dependent pathway.The organizing principle of the platelet glycoprotein Ib-IX-V complex.Platelet glycoprotein gene polymorphisms and risk of thrombosis: facts and fancies.Platelet adhesion under flow.Defect in regulated secretion of P-selectin affects leukocyte recruitment in von Willebrand factor-deficient mice P-selectin-mediated platelet adhesion promotes tumor growth.Platelet-neutrophil interactions under thromboinflammatory conditions Platelet glycoprotein Ib alpha supports experimental lung metastasis Tissue factor expressed by circulating cancer cell-derived microparticles drastically increases the incidence of deep vein thrombosis in mice P-selectin in haemostasis.HbS Binding to GP1bα Activates Platelets in Sickle Cell Disease P-selectin can promote thrombus propagation independently of both von Willebrand factor and thrombospondin-1 in mice.The P-selectin, tissue factor, coagulation triad.Platelets in inflammation and atherogenesis.Platelet glycoprotein ibalpha is a counterreceptor for the leukocyte integrin Mac-1 (CD11b/CD18)A functional 14-3-3zeta-independent association of PI3-kinase with glycoprotein Ib alpha, the major ligand-binding subunit of the platelet glycoprotein Ib-IX-V complex The vessel wall and its interactions.Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbalpha.Inhibition of platelet activation by clopidogrel prevents hypertension-induced cardiac inflammation and fibrosis.

P2860

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P2860

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

http://www.wikidata.org/entity/Q36375314

description

1999 nî lūn-bûn

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1999年の論文

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1999年学术文章

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1999年学术文章

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1999年学术文章

@zh-hans

1999年学术文章

@zh-my

1999年学术文章

@zh-sg

1999年學術文章

@yue

1999年學術文章

@zh

1999年學術文章

@zh-hant

name

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

@ast

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

@en

type

label

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

@ast

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

@en

prefLabel

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

@ast

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

@en

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P1433

Journal of Experimental Medicine

P1476

The glycoprotein Ib-IX-V complex is a platelet counterreceptor for P-selectin.

@en

P2093

A J Schade

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

C Q Li

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

E E Gardiner

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

G M Romo

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

G S Kansas

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

J A López

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

J F Dong

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

L V McIntire

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

M C Berndt

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P2860

Expression cloning of a functional glycoprotein ligand for P-selectin

Identification of three tyrosine residues of glycoprotein Ib alpha with distinct roles in von Willebrand factor and alpha-thrombin binding

Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor

Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein

P-selectin mediates neutrophil rolling on histamine-stimulated endothelial cells.

Platelets roll on stimulated endothelium in vivo: an interaction mediated by endothelial P-selectin

Identification of the disulphide bonds in human platelet glycocalicin.

Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin.

A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding.

PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus.

P304

803-814

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P31

scholarly article

P356

10.1084/JEM.190.6.803

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P407

P433

6

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

P478

190

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P577

1999-09-01T00:00:00Z

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P5875

12800296

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P698

10499919

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P932

2195629

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