Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay.
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A substrate-driven allosteric switch that enhances PDI catalytic activityThe C-terminal CGHC motif of protein disulfide isomerase supports thrombosis.The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activityComparative Analysis of the Interaction between Different Flavonoids and PDIA3Protein disulfide isomerase inhibitors constitute a new class of antithrombotic agents.Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1.Effect of pharmaceutical potential endocrine disruptor compounds on protein disulfide isomerase reductase activity using di-eosin-oxidized-glutathione.HPW-RX40 prevents human platelet activation by attenuating cell surface protein disulfide isomerases.The platelet-surface thiol isomerase enzyme ERp57 modulates platelet function.Structure-function analysis of the endoplasmic reticulum oxidoreductase TMX3 reveals interdomain stabilization of the N-terminal redox-active domain.Defective PDI release from platelets and endothelial cells impairs thrombus formation in Hermansky-Pudlak syndromeBoth 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 thrombosisIdentification of the thiol isomerase-binding peptide, mastoparan, as a novel inhibitor of shear-induced transforming growth factor β1 (TGF-β1) activation.Protein disulfide isomerase as a novel target for cyclopentenone prostaglandins: implications for hypoxic ischemic injuryEndothelin-1 receptor antagonists regulate cell surface-associated protein disulfide isomerase in sickle cell disease.Platelet-derived ERp57 mediates platelet incorporation into a growing thrombus by regulation of the αIIbβ3 integrin.Protein disulfide isomerase secretion following vascular injury initiates a regulatory pathway for thrombus formation.Redox-sensitive probes for the measurement of redox chemistries within phagosomes of macrophages and dendritic cells.Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.Methods of measuring protein disulfide isomerase activity: a critical overview.Alkylating Agent-Induced NRF2 Blocks Endoplasmic Reticulum Stress-Mediated Apoptosis via Control of Glutathione Pools and Protein Thiol Homeostasis.Cell surface thiol isomerases may explain the platelet-selective action of S-nitrosoglutathioneA di-arginine motif contributes to the ER localization of the type I transmembrane ER oxidoreductase TMX4.Succination of Protein Disulfide Isomerase Links Mitochondrial Stress and Endoplasmic Reticulum Stress in the Adipocyte During Diabetes.TMX1 determines cancer cell metabolism as a thiol-based modulator of ER-mitochondria Ca2+ flux.Thiol redox sensitivity of two key enzymes of heme biosynthesis and pentose phosphate pathways: uroporphyrinogen decarboxylase and transketolase.The dehydrogenase region of the NADPH oxidase component Nox2 acts as a protein disulfide isomerase (PDI) resembling PDIA3 with a role in the binding of the activator protein p67 (phox.).A humanized monoclonal antibody that inhibits platelet-surface ERp72 reveals a role for ERp72 in thrombosis.Mechanistic insights on the reduction of glutathione disulfide by protein disulfide isomerase.Challenges in the evaluation of thiol-reactive inhibitors of human protein disulfide Isomerase.Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates.Conserved Residues Lys57 and Lys401 of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation.Geraniol as a novel antivirulence agent against bacillary dysentery-causing Shigella sonnei.
P2860
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P2860
Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay.
description
2007 nî lūn-bûn
@nan
2007 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մարտին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Characterization of redox stat ...... a sensitive fluorescent assay.
@ast
Characterization of redox stat ...... a sensitive fluorescent assay.
@en
Characterization of redox stat ...... a sensitive fluorescent assay.
@nl
type
label
Characterization of redox stat ...... a sensitive fluorescent assay.
@ast
Characterization of redox stat ...... a sensitive fluorescent assay.
@en
Characterization of redox stat ...... a sensitive fluorescent assay.
@nl
prefLabel
Characterization of redox stat ...... a sensitive fluorescent assay.
@ast
Characterization of redox stat ...... a sensitive fluorescent assay.
@en
Characterization of redox stat ...... a sensitive fluorescent assay.
@nl
P1476
Characterization of redox stat ...... a sensitive fluorescent assay.
@en
P2093
Arun Raturi
Bulent Mutus
P356
10.1016/J.FREERADBIOMED.2007.03.025
P577
2007-03-31T00:00:00Z