Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents. - Wikidata - thesis-toulmin - TriplyDB

Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

http://www.wikidata.org/entity/Q30514535

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Protein disulfide isomerase a multifunctional protein with multiple physiological roles 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.A specific plasminogen activator inhibitor-1 antagonist derived from inactivated urokinase.Vascular thiol isomerases.Dynamin-related protein-1 controls fusion pore dynamics during platelet granule exocytosis.Differential proteomics study of platelets in asymptomatic constitutional macrothrombocytopenia: altered levels of cytoskeletal proteins.HPW-RX40 prevents human platelet activation by attenuating cell surface protein disulfide isomerases.Thiol isomerases in thrombus formation.Ruthenium-conjugated chrysin analogues modulate platelet activity, thrombus formation and haemostasis with enhanced efficacy Platelets are required for enhanced activation of the endothelium and fibrinogen in a mouse thrombosis model of APS.Small molecule-induced oxidation of protein disulfide isomerase is neuroprotective.Revisiting the mechanistic basis of the French Paradox: Red wine inhibits the activity of protein disulfide isomerase in vitro.Fruitflow®: the first European Food Safety Authority-approved natural cardio-protective functional ingredient.Nontoxic polyphosphate inhibitors reduce thrombosis while sparing hemostasis.Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease.Analysis of the isomerase and chaperone-like activities of an amebic PDI (EhPDI).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 Both platelet- and endothelial cell-derived ERp5 support thrombus formation in a laser-induced mouse model of thrombosis.Treatment of Thrombotic Antiphospholipid Syndrome: The Rationale of Current Management-An Insight into Future Approaches.Novel roles for protein disulphide isomerase in disease states: a double edged sword?Platelet-targeting thiol reduction sensor detects thiol isomerase activity on activated platelets in mouse and human blood under flow VAMP-7 links granule exocytosis to actin reorganization during platelet activation.Broad-spectrum antivirals against viral fusion.Quercetin-3-rutinoside Inhibits Protein Disulfide Isomerase by Binding to Its b'x Domain.Thioredoxin Inhibitors Attenuate Platelet Function and Thrombus Formation.Anti-Proliferative Effects of Rutin on OLETF Rat Vascular Smooth Muscle Cells Stimulated by Glucose Variability.Rapid activation of monocyte tissue factor by antithymocyte globulin is dependent on complement and protein disulfide isomerase.Protein disulfide isomerase as an antithrombotic target Protein disulfide isomerase inhibition blocks thrombin generation in humans by interfering with platelet factor V activation.Protein disulfide isomerase secretion following vascular injury initiates a regulatory pathway for thrombus formation.Control of blood proteins by functional disulfide bonds.Formation of the clot.Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.Encryption and decryption of tissue factor.Nox NADPH oxidases and the endoplasmic reticulum Methods of measuring protein disulfide isomerase activity: a critical overview.An ERp57-mediated disulphide exchange promotes the interaction between Burkholderia cenocepacia and epithelial respiratory cells

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P2860

Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

http://www.wikidata.org/entity/Q30514535

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2012 nî lūn-bûn

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2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2012 թվականի մայիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

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Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

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type

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Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

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Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

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Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

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Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

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Journal of Clinical Investigation

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Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.

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P2093

Barbara C Furie

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Bruce Furie

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Daniel R Kennedy

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Freda H Passam

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James R Dilks

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Lin Lin

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Lotte van Hessem

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Reema Jasuja

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Robert Flaumenhaft

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Sarah H Kim

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P2860

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

Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation

Endothelium-derived but not platelet-derived protein disulfide isomerase is required for thrombus formation in vivo.

Uptake and localisation of O-(beta-hydroxyethyl)-rutosides in the venous wall, measured by laser scanning microscopy.

A high-throughput turbidometric assay for screening inhibitors of protein disulfide isomerase activity.

A critical review of the data related to the safety of quercetin and lack of evidence of in vivo toxicity, including lack of genotoxic/carcinogenic properties.

Thrombus formation: direct real-time observation and digital analysis of thrombus assembly in a living mouse by confocal and widefield intravital microscopy.

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

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

Laser-induced endothelial cell activation supports fibrin formation.

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2104-2113

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10.1172/JCI61228

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6

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122

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22565308

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