Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis
about
Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coliEssential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin.Proteomics analysis of Thermoplasma acidophilum with a focus on protein complexes.Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF.Structure based development of phenylimidazole-derived inhibitors of indoleamine 2,3-dioxygenase.Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpCThe origami of thioredoxin-like folds.The selectivity, voltage-dependence and acid sensitivity of the tandem pore potassium channel TASK-1: contributions of the pore domains.Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution.Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase systemMeasurement of peroxiredoxin activity.Mechanism of SN2 disulfide bond cleavage by phosphorus nucleophiles. Implications for biochemical disulfide reducing agentsNTRC new ways of using NADPH in the chloroplast.Overexpression of chloroplast NADPH-dependent thioredoxin reductase in Arabidopsis enhances leaf growth and elucidates in vivo function of reductase and thioredoxin domains.Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds.Crystallization and preliminary X-ray studies of ferredoxin-NAD(P)+ reductase from Chlorobium tepidumFlavoprotein-Mediated Tellurite Reduction: Structural Basis and Applications to the Synthesis of Tellurium-Containing Nanostructures.NADH oxidase and alkyl hydroperoxide reductase subunit C (peroxiredoxin) from Amphibacillus xylanus form an oligomeric assembly.NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2-Cys peroxiredoxin machinery.
P2860
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P2860
Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis
description
2001 nî lūn-bûn
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2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2001 թվականի ապրիլին հրատարակված գիտական հոդված
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2001年の論文
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2001年論文
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2001年論文
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2001年論文
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2001年論文
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2001年论文
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name
Structure of intact AhpF revea ...... ain rotations during catalysis
@ast
Structure of intact AhpF revea ...... ain rotations during catalysis
@en
Structure of intact AhpF revea ...... ain rotations during catalysis
@nl
type
label
Structure of intact AhpF revea ...... ain rotations during catalysis
@ast
Structure of intact AhpF revea ...... ain rotations during catalysis
@en
Structure of intact AhpF revea ...... ain rotations during catalysis
@nl
prefLabel
Structure of intact AhpF revea ...... ain rotations during catalysis
@ast
Structure of intact AhpF revea ...... ain rotations during catalysis
@en
Structure of intact AhpF revea ...... ain rotations during catalysis
@nl
P2093
P3181
P356
P1433
P1476
Structure of intact AhpF revea ...... ain rotations during catalysis
@en
P2093
P304
P3181
P356
10.1021/BI002765P
P407
P577
2001-04-03T00:00:00Z