Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1. - Wikidata - wikimedia - TriplyDB

Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1.

Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1.

http://www.wikidata.org/entity/Q42600965

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Inflammatory and oxidative stress in rotavirus infection The C-terminal CGHC motif of protein disulfide isomerase supports thrombosis.Potential Role of Protein Disulfide Isomerase in Metabolic Syndrome-Derived Platelet Hyperactivity Effects of UVB-induced oxidative stress on protein expression and specific protein oxidation in normal human epithelial keratinocytes: a proteomic approach 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.T granules in human platelets function in TLR9 organization and signaling.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 Caspase-1-mediated pathway promotes generation of thromboinflammatory microparticles.SHP2 binds catalase and acquires a hydrogen peroxide-resistant phosphatase activity via integrin-signaling.A critical role for extracellular protein disulfide isomerase during thrombus formation in mice.Thiol isomerases in thrombus formation.Bacitracin is not a specific inhibitor of protein disulfide isomerase.Ribozyme-mediated gene knock down strategy to dissect the consequences of PDGF stimulation in vascular smooth muscle cells.Redox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1.Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease.Disulfide isomerization switches tissue factor from coagulation to cell signaling 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 Selective redox regulation of cytokine receptor signaling by extracellular thioredoxin-1.Platelet-targeting thiol reduction sensor detects thiol isomerase activity on activated platelets in mouse and human blood under flow Binding and lubrication of biomimetic boundary lubricants on articular cartilage.NOV-002, a glutathione disulfide mimetic, as a modulator of cellular redox balance.Protection against cerebral malaria by the low-molecular-weight thiol pantethine.Site-specific S-nitrosylation of integrin α6 increases the extent of prostate cancer cell migration by enhancing integrin β1 association and weakening adherence to laminin-1.Bacitracin Inhibits the Migration of U87-MG Glioma Cells via Interferences of the Integrin Outside-in Signaling Pathway.In vitro and in vivo evidence for shear-induced activation of latent transforming growth factor-beta1.Radical-free biology of oxidative stress.Protein disulfide isomerase as an antithrombotic target Platelet-derived ERp57 mediates platelet incorporation into a growing thrombus by regulation of the αIIbβ3 integrin.Protein disulfide isomerase inhibition blocks thrombin generation in humans by interfering with platelet factor V activation.Control of blood proteins by functional disulfide bonds.S-nitrosothiols as selective antithrombotic agents - possible mechanisms Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells.Extracellular Thiol Isomerases and Their Role in Thrombus Formation Cell surface thiol isomerases may explain the platelet-selective action of S-nitrosoglutathione Posttranslational forms of beta 2-glycoprotein I in the pathogenesis of the antiphospholipid syndrome Novel antiplatelet role for a protein disulfide isomerase-targeted peptide: evidence of covalent binding to the C-terminal CGHC redox motif.

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P2860

Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1.

http://www.wikidata.org/entity/Q42600965

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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name

Enzymatically catalyzed disulf ...... agen via integrin alpha2beta1.

@en

Enzymatically catalyzed disulf ...... agen via integrin alpha2beta1.

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type

label

Enzymatically catalyzed disulf ...... agen via integrin alpha2beta1.

@en

Enzymatically catalyzed disulf ...... agen via integrin alpha2beta1.

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prefLabel

Enzymatically catalyzed disulf ...... agen via integrin alpha2beta1.

@en

Enzymatically catalyzed disulf ...... agen via integrin alpha2beta1.

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BLOOD-2002-06-1646

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Enzymatically catalyzed disulf ...... agen via integrin alpha2beta1.

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C Graham Knight

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David W Essex

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Delia Griffiths

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Eveline M Wijnen

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Judith Lahav

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Michael Makris

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Oded Hess

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Richard W Farndale

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Samir W Hamaia

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2085-2092

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scholarly article

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10.1182/BLOOD-2002-06-1646

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6

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102

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