The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function. - Wikidata - wikimedia - TriplyDB

The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

http://www.wikidata.org/entity/Q34100678

about

A substrate-driven allosteric switch that enhances PDI catalytic activity The C-terminal CGHC motif of protein disulfide isomerase supports thrombosis.Vascular thiol isomerases.Platelet protein disulfide isomerase is required for thrombus formation but not for hemostasis in mice HPW-RX40 prevents human platelet activation by attenuating cell surface protein disulfide isomerases.Thiol isomerases in thrombus formation.Protein disulfide isomerase in thrombosis and vascular inflammation Defective PDI release from platelets and endothelial cells impairs thrombus formation in Hermansky-Pudlak syndrome 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 Quercetin-3-rutinoside Inhibits Protein Disulfide Isomerase by Binding to Its b'x Domain.Protein disulfide isomerase as an antithrombotic target Platelet-derived ERp57 mediates platelet incorporation into a growing thrombus by regulation of the αIIbβ3 integrin.Control of blood proteins by functional disulfide bonds.Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.Redox regulation of protein damage in plasma.An ERp57-mediated disulphide exchange promotes the interaction between Burkholderia cenocepacia and epithelial respiratory cells Extracellular Thiol Isomerases and Their Role in Thrombus Formation OX133, a monoclonal antibody recognizing protein-bound N-ethylmaleimide for the identification of reduced disulfide bonds in proteins.Probing for thiol isomerase activity in thrombi.A new antithrombotic strategy: inhibition of the C-terminal active site of protein disulfide isomerase.Intracellular Trafficking, Localization, and Mobilization of Platelet-Borne Thiol Isomerases.Dystroglycan is associated to the disulfide isomerase ERp57.Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy.Modulation of H(+),K(+)-ATPase activity by the molecular chaperone ERp57 highly expressed in gastric parietal cells.A humanized monoclonal antibody that inhibits platelet-surface ERp72 reveals a role for ERp72 in thrombosis.Distinct contributions of complement factors to platelet activation and fibrin formation in venous thrombus development.Redundancy of protein disulfide isomerases in the catalysis of the inactivating disulfide switch in A Disintegrin and Metalloprotease 17.Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates.Proteomic analysis of platelets treated with gamma irradiation versus a commercial photochemical pathogen reduction technology.An allosteric disulfide bond is involved in enhanced activation of factor XI by protein disulfide isomerase.Identification of allosteric disulfides from labile bonds in X-ray structures.Discovery of a Novel ERp57 Inhibitor as Antiplatelet Agent from Danshen (Salvia miltiorrhiza).Mechano-redox control of integrin de-adhesion

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

http://www.wikidata.org/entity/Q34100678

description

2012 nî lūn-bûn

@nan

2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի փետրվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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J.1538-7836.2011.04593.X

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Journal of Thrombosis and Haemostasis

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The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.

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P2093

A B Bicknell

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A D Simmonds

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J M Gibbins

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L-M Holbrook

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P Sasikumar

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R G Stanley

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P2860

A role for the thiol isomerase protein ERP5 in platelet function

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

N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin.

ERp57 is a multifunctional thiol-disulfide oxidoreductase

Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation

Characterization of Grb2-binding proteins in human platelets activated by Fc gamma RIIA cross-linking

The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules

Bacitracin reveals a role for multiple thiol isomerases in platelet function.

Platelet PECAM-1 inhibits thrombus formation in vivo.

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

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278-288

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10.1111/J.1538-7836.2011.04593.X

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2

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22168334

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3444690

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