Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution - Test2 - elhamkhani - TriplyDB

Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

http://www.wikidata.org/entity/Q27626603

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Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism Atomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti Native and inhibited structure of a Mu class-related glutathione S-transferase from Plasmodium falciparum NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerization Thioredoxin A Active-Site Mutants Form Mixed Disulfide Dimers That Resemble Enzyme–Substrate Reaction Intermediates An atypical catalytic mechanism involving three cysteines of thioredoxin Structure of the thioredoxin-fold domain of human phosducin-like protein 2 Expression, purification, crystallization and X-ray crystallographic studies of different redox states of the active site of thioredoxin 1 from the whiteleg shrimpLitopenaeus vannamei Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure Intramolecularly hydrogen-bonded peptide conformations Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling Molecular 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 thioredoxin Escherichia 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 resolution Direct 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 mutant Folding subdomains of thioredoxin characterized by native-state hydrogen exchange The 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 assembly Glutathione-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

http://www.wikidata.org/entity/Q27626603

description

1975 nî lūn-bûn

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1975 թուականի Յունիսին հրատարակուած գիտական յօդուած

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1975 թվականի հունիսին հրատարակված գիտական հոդված

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1975年の論文

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1975年論文

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1975年論文

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1975年論文

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1975年論文

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1975年論文

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1975年论文

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name

Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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type

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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Proceedings of the National Academy of Sciences of the United States of America

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Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8 A resolution

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A Holmgren

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B O Söderberg

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C I Brändén

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H Eklund

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P2860

Structure of liver alcohol dehydrogenase at 2.9-angstrom resolution

Chemical and biological evolution of nucleotide-binding protein

Comparison of super-secondary structures in proteins

Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units

The matching of physical models to three-dimensional electron-density maps: a simple optical device

D-glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance.

The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin at 2.0-Angstrom resolution

Crystallization and preliminary crystallographic data for thioredoxin from Escherichia coli B.

An immunologic approach to the conformational equilibria of polypeptides.

Thioredoxin. A localized conformational change accompanying reduction of the protein to the sulfhydryl form.

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2305-9

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10.1073/PNAS.72.6.2305

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6

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72

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1975-06-01T00:00:00Z

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242904205

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1094461

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Escherichia coli

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432746

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