Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis
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Structure ofHordeum vulgareNADPH-dependent thioredoxin reductase 2. Unwinding the reaction mechanismThioredoxin System from Deinococcus radioduransMapping Conformational Transitions in Cyclic AMP Receptor Protein: Crystal Structure and Normal-Mode Analysis of Mycobacterium tuberculosis apo-cAMP Receptor ProteinSolution structures of Mycobacterium tuberculosis thioredoxin C and models of intact thioredoxin system suggest new approaches to inhibitor and drug designNrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum Dimerizes at High Protein Concentration and Exclusively Receives Electrons from Thioredoxin ReductaseRv2969c, essential for optimal growth inMycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidasesThe structural basis of an NADP+-independent dithiol oxidase in FK228 biosynthesisFunctional studies of multiple thioredoxins from Mycobacterium tuberculosisMycobacterium tuberculosis Thioredoxin Reductase Is Essential for Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant DefenseDocking into Mycobacterium tuberculosis Thioredoxin Reductase Protein Yields Pyrazolone Lead Molecules for Methicillin-Resistant Staphylococcus aureusX-ray structures of thioredoxin and thioredoxin reductase from Entamoeba histolytica and prevailing hypothesis of the mechanism of Auranofin action.Crystallization and preliminary X-ray studies of ferredoxin-NAD(P)+ reductase from Chlorobium tepidumDealing with structural variability in molecular replacement and crystallographic refinement through normal-mode analysis.Crystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor.Domain motions of glucosamine-6P synthase: comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation.Protein-protein interactions at an enzyme-substrate interface: characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase.Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase.A novel twist on molecular interactions between thioredoxin and nicotinamide adenine dinucleotide phosphate-dependent thioredoxin reductase.
P2860
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P2860
Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis
description
2005 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2005
@ast
im Dezember 2005 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2005/12/01)
@sk
vědecký článek publikovaný v roce 2005
@cs
wetenschappelijk artikel (gepubliceerd op 2005/12/01)
@nl
наукова стаття, опублікована в грудні 2005
@uk
مقالة علمية (نشرت في ديسمبر 2005)
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name
Conformational flexibility of ...... cture and normal-mode analysis
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Conformational flexibility of ...... cture and normal-mode analysis
@en
Conformational flexibility of ...... cture and normal-mode analysis
@nl
type
label
Conformational flexibility of ...... cture and normal-mode analysis
@ast
Conformational flexibility of ...... cture and normal-mode analysis
@en
Conformational flexibility of ...... cture and normal-mode analysis
@nl
prefLabel
Conformational flexibility of ...... cture and normal-mode analysis
@ast
Conformational flexibility of ...... cture and normal-mode analysis
@en
Conformational flexibility of ...... cture and normal-mode analysis
@nl
P2093
P3181
P1476
Conformational flexibility of ...... cture and normal-mode analysis
@en
P2093
Chandra Verma
Shekhar C. Mande
P304
P3181
P356
10.1107/S0907444905030519
P577
2005-12-01T00:00:00Z