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Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductaseKinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathwaysStructural and Mechanistic Insights into Unusual Thiol Disulfide OxidoreductaseNrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum Dimerizes at High Protein Concentration and Exclusively Receives Electrons from Thioredoxin ReductaseTuning of thioredoxin redox properties by intramolecular hydrogen bondsThiol redox biochemistry: insights from computer simulationsThiol-based redox switchesThioredoxin 1-mediated post-translational modifications: reduction, transnitrosylation, denitrosylation, and related proteomics methodologies.Analysis and functional prediction of reactive cysteine residues.Methylation of arsenic by recombinant human wild-type arsenic (+3 oxidation state) methyltransferase and its methionine 287 threonine (M287T) polymorph: Role of glutathione.Probing the active site tryptophan of Staphylococcus aureus thioredoxin with an analog.Oxidant sensing by reversible disulfide bond formationEnzymatic control of cysteinyl thiol switches in proteins.Conferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.(1)H, (13)C and (15)N chemical shift assignments of Saccharomyces cerevisiae type 1 thioredoxin in the oxidized state by solution NMR spectroscopy.The conserved active site tryptophan of thioredoxin has no effect on its redox properties.Electron capture by the thiyl radical and disulfide bond: ligand effects on the reduction potential.Revealing unexpected mechanisms for nucleophilic attack on S-S and Se-Se bridges.The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of Mycobacterium tuberculosis.Cy-preds: An algorithm and a web service for the analysis and prediction of cysteine reactivity.Protein flexibility and cysteine reactivity: influence of mobility on the H-bond network and effects on pKa prediction.Conserved Residues Lys57 and Lys401 of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation.Repurposing Auranofin, Ebselen, and PX-12 as Antimicrobial Agents Targeting the Thioredoxin System.Dramatic substituent effects on the mechanisms of nucleophilic attack on Se-S bridges.Intra- and inter-protein couplings of backbone motions underlie protein thiol-disulfide exchange cascade
P2860
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P2860
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
How thioredoxin dissociates its mixed disulfide
@ast
How thioredoxin dissociates its mixed disulfide
@en
How thioredoxin dissociates its mixed disulfide
@nl
type
label
How thioredoxin dissociates its mixed disulfide
@ast
How thioredoxin dissociates its mixed disulfide
@en
How thioredoxin dissociates its mixed disulfide
@nl
prefLabel
How thioredoxin dissociates its mixed disulfide
@ast
How thioredoxin dissociates its mixed disulfide
@en
How thioredoxin dissociates its mixed disulfide
@nl
P2093
P2860
P50
P1476
How thioredoxin dissociates its mixed disulfide
@en
P2093
Koen Van Laer
Paul Geerlings
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000461
P407
P577
2009-08-13T00:00:00Z