A critical role for extracellular protein disulfide isomerase during thrombus formation in mice. - Wikidata - awgldk - TriplyDB

A critical role for extracellular protein disulfide isomerase during thrombus formation in mice.

A critical role for extracellular protein disulfide isomerase during thrombus formation in mice.

http://www.wikidata.org/entity/Q33320817

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Key role of glycoprotein Ib/V/IX and von Willebrand factor in platelet activation-dependent fibrin formation at low shear flow The protein disulfide isomerase AGR2 is essential for production of intestinal mucus Imaging coagulation reactions in vivo Complement-Coagulation Cross-Talk: A Potential Mediator of the Physiological Activation of Complement by Low pH A substrate-driven allosteric switch that enhances PDI catalytic activity The C-terminal CGHC motif of protein disulfide isomerase supports thrombosis.Vascular thiol isomerases.Endothelium-derived but not platelet-derived protein disulfide isomerase is required for thrombus formation in vivo.Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.Protein disulfide isomerase capture during thrombus formation in vivo depends on the presence of β3 integrins Extracellular protein disulfide isomerase regulates ligand-binding activity of αMβ2 integrin and neutrophil recruitment during vascular inflammation Platelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in mice Laser-induced endothelial cell activation supports fibrin formation.Post-streptococcal auto-antibodies inhibit protein disulfide isomerase and are associated with insulin resistance Role of PDI in regulating tissue factor: FVIIa activity.HPW-RX40 prevents human platelet activation by attenuating cell surface protein disulfide isomerases.Platelets generated from human embryonic stem cells are functional in vitro and in the microcirculation of living mice Thiol isomerases in thrombus formation.β₂-Glycoprotein-1 autoantibodies from patients with antiphospholipid syndrome are sufficient to potentiate arterial thrombus formation in a mouse model.Protein disulfide isomerase in thrombosis and vascular inflammation Features of a spatially constrained cystine loop in the p10 FAST protein ectodomain define a new class of viral fusion peptides.Cystine 186-cystine 209 disulfide bond is not essential for the procoagulant activity of tissue factor or for its de-encryption Post-streptococcal antibodies are associated with metabolic syndrome in a population-based cohort.Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure.The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.Small molecule-induced oxidation of protein disulfide isomerase is neuroprotective.Redox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1.Real-time imaging of heterotypic platelet-neutrophil interactions on the activated endothelium during vascular inflammation and thrombus Formation in live mice.Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease.Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis.Delivery of nanoparticle: complexed drugs across the vascular endothelial barrier via caveolae Defective PDI release from platelets and endothelial cells impairs thrombus formation in Hermansky-Pudlak syndrome Inhibitory effects of yuzu and its components on human platelet aggregation Tissue factor, blood coagulation, and beyond: an overview.The disulfide isomerase ERp57 is required for fibrin deposition in vivo.Both platelet- and endothelial cell-derived ERp5 support thrombus formation in a laser-induced mouse model of thrombosis.The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis Platelet-targeting thiol reduction sensor detects thiol isomerase activity on activated platelets in mouse and human blood under flow Tissue factor encryption and decryption: facts and controversies Histones Induce the Procoagulant Phenotype of Endothelial Cells through Tissue Factor Up-Regulation and Thrombomodulin Down-Regulation.

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P2860

A critical role for extracellular protein disulfide isomerase during thrombus formation in mice.

http://www.wikidata.org/entity/Q33320817

description

2008 nî lūn-bûn

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2008 թուականի Մարտին հրատարակուած գիտական յօդուած

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2008 թվականի մարտին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

A critical role for extracellu ...... ng thrombus formation in mice.

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A critical role for extracellu ...... ng thrombus formation in mice.

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A critical role for extracellu ...... ng thrombus formation in mice.

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type

label

A critical role for extracellu ...... ng thrombus formation in mice.

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A critical role for extracellu ...... ng thrombus formation in mice.

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A critical role for extracellu ...... ng thrombus formation in mice.

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prefLabel

A critical role for extracellu ...... ng thrombus formation in mice.

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A critical role for extracellu ...... ng thrombus formation in mice.

@en

A critical role for extracellu ...... ng thrombus formation in mice.

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Journal of Clinical Investigation

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A critical role for extracellu ...... ng thrombus formation in mice.

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P2093

Barbara C Furie

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Bruce Furie

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Jaehyung Cho

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

Shaun R Coughlin

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P2860

A role for the thiol isomerase protein ERP5 in platelet function

Glycoprotein VI-dependent and -independent pathways of thrombus formation in vivo

Thrombin-initiated platelet activation in vivo is vWF independent during thrombus formation in a laser injury model

Mechanism of integrin activation by disulfide bond reduction.

Accumulation of tissue factor into developing thrombi in vivo is dependent upon microparticle P-selectin glycoprotein ligand 1 and platelet P-selectin.

Importance of platelet phospholipase Cgamma2 signaling in arterial thrombosis as a function of lesion severity.

Par4 is required for platelet thrombus propagation but not fibrin generation in a mouse model of thrombosis.

Role of thrombin signalling in platelets in haemostasis and thrombosis.

Disulfide isomerization switches tissue factor from coagulation to cell signaling

Disulfide bonds as switches for protein function.

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1123-1131

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10.1172/JCI34134

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3

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118

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2008-03-01T00:00:00Z

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5559066

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18292814

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2248441

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