Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation. - Wikidata - wikimedia - TriplyDB

Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation.

Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation.

http://www.wikidata.org/entity/Q41975370

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The protein disulfide isomerase AGR2 is essential for production of intestinal mucus Imaging coagulation reactions in vivo PAMPs and DAMPs as triggers for DIC Complement-Coagulation Cross-Talk: A Potential Mediator of the Physiological Activation of Complement by Low pH Anti-Inflammatory and Anti-Thrombotic Effects of the Fungal Metabolite Galiellalactone in Apolipoprotein E-Deficient Mice Bothrops jararaca venom metalloproteinases are essential for coagulopathy and increase plasma tissue factor levels during envenomation A substrate-driven allosteric switch that enhances PDI catalytic activity The C-terminal CGHC motif of protein disulfide isomerase supports thrombosis.Potential Role of Protein Disulfide Isomerase in Metabolic Syndrome-Derived Platelet Hyperactivity The effect of oxidant and the non-oxidant alteration of cellular thiol concentration on the formation of protein mixed-disulfides in HEK 293 cells 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 Platelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in mice Carbohydrates and activity of natural and recombinant tissue factor Post-streptococcal auto-antibodies inhibit protein disulfide isomerase and are associated with insulin resistance Systems biology of coagulation initiation: kinetics of thrombin generation in resting and activated human blood.Role of PDI in regulating tissue factor: FVIIa activity.Thiol isomerases in thrombus formation.Protein disulfide isomerase in thrombosis and vascular inflammation 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.Redox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1.Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease.Microparticles in hemostasis and thrombosis.The nairovirus nairobi sheep disease virus/ganjam virus induces the translocation of protein disulphide isomerase-like oxidoreductases from the endoplasmic reticulum to the cell surface and the extracellular space.Defective PDI release from platelets and endothelial cells impairs thrombus formation in Hermansky-Pudlak syndrome 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.Protein S-glutathiolation: redox-sensitive regulation of protein function.Posttranslational modifications of tissue factor.Procoagulant activity in hemostasis and thrombosis: Virchow's triad revisited.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 Monocytes, neutrophils, and platelets cooperate to initiate and propagate venous thrombosis in mice in vivo.Decryption of tissue factor.

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P2860

Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation.

http://www.wikidata.org/entity/Q41975370

description

2008 nî lūn-bûn

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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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2008年论文

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2008年论文

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name

Protein disulfide isomerase ac ...... via tissue factor activation.

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type

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Protein disulfide isomerase ac ...... via tissue factor activation.

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Protein disulfide isomerase ac ...... via tissue factor activation.

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Journal of Clinical Investigation

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Protein disulfide isomerase ac ...... via tissue factor activation.

@en

P2093

Berid Altmann

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Bernd Engelmann

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Christoph Reinhardt

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Davit Manukyan

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

Ildiko Konrad

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

Lena Orschiedt

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

Lenka Grahl

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Lloyd Ruddock

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Marie-Luise von Brühl

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Michael Lorenz

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P2860

Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing

The human protein disulphide isomerase family: substrate interactions and functional properties

Platelets mediate cytotoxic T lymphocyte-induced liver damage.

Oxidative protein folding in eukaryotes: mechanisms and consequences

Crystal structure of the extracellular region of human tissue factor

The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor

Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin

Protein disulfide isomerase

Initiation of coagulation by tissue factor carriers in blood

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

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1110-1122

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10.1172/JCI32376

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3

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118

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2008-03-01T00:00:00Z

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5576743

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18274674

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2242616

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