Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
about
Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same geneCrystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanismAtomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter acetiNative and inhibited structure of a Mu class-related glutathione S-transferase from Plasmodium falciparumNMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteinsDimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerizationThioredoxin A Active-Site Mutants Form Mixed Disulfide Dimers That Resemble Enzyme–Substrate Reaction IntermediatesAn atypical catalytic mechanism involving three cysteines of thioredoxinStructure of the thioredoxin-fold domain of human phosducin-like protein 2Expression, purification, crystallization and X-ray crystallographic studies of different redox states of the active site of thioredoxin 1 from the whiteleg shrimpLitopenaeus vannameiMycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of MycobacteriaSelenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structureIntramolecularly hydrogen-bonded peptide conformationsThioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingMolecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli.The protein disulphide-isomerase family: unravelling a string of folds.Redox regulation of cell survival by the thioredoxin superfamily: an implication of redox gene therapy in the heart.13C NMR and fluorescence analysis of tryptophan dynamics in wild-type and two single-Trp variants of Escherichia coli thioredoxinEscherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase.Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione.Handedness of crossover connections in beta sheets.Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker.TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance.The Eps1p protein disulfide isomerase conserves classic thioredoxin superfamily amino acid motifs but not their functional geometries.Crystal structure of thioltransferase at 2.2 A resolutionDirect cloning of the trxB gene that encodes thioredoxin reductase.Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12.The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutantFolding subdomains of thioredoxin characterized by native-state hydrogen exchangeThe origami of thioredoxin-like folds.Thioredoxin and thioredoxin target proteins: from molecular mechanisms to functional significance.Vicinal cysteines in the prosequence play a role in von Willebrand factor multimer assemblyGlutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase.Rescue of bacteriophage T7 DNA polymerase of low processivity by suppressor mutations affecting gene 3 endonuclease.Comprehensively Characterizing the Thioredoxin Interactome In Vivo Highlights the Central Role Played by This Ubiquitous Oxidoreductase in Redox Control.Three-dimensional structure of thioredoxin induced by bacteriophage T4.Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein.Deuterium labelling in NMR structural analysis of larger proteins.Interacting with thioredoxin-1--disease or no disease?Description of the topographical changes associated to the different stages of the DsbA catalytic cycle.
P2860
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P2860
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
description
1975 nî lūn-bûn
@nan
1975 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1975 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1975年の論文
@ja
1975年論文
@yue
1975年論文
@zh-hant
1975年論文
@zh-hk
1975年論文
@zh-mo
1975年論文
@zh-tw
1975年论文
@wuu
name
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@ast
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@en
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@nl
type
label
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@ast
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@en
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@nl
prefLabel
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@ast
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@en
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@nl
P2093
P2860
P356
P1476
Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution
@en
P2093
A Holmgren
B O Söderberg
C I Brändén
P2860
P304
P356
10.1073/PNAS.72.6.2305
P407
P577
1975-06-01T00:00:00Z