NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism
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The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-IStructural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coliThe crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species BThe tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteinsCrystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein3‘-Phosphoadenosine-5‘-phosphosulfate Reductase in Complex with Thioredoxin: A Structural Snapshot in the Catalytic Cycle † , ‡Structure-Function Relationship of the Chloroplastic Glutaredoxin S12 with an Atypical WCSYS Active SiteThe Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA EnzymesArabidopsis Chloroplastic Glutaredoxin C5 as a Model to Explore Molecular Determinants for Iron-Sulfur Cluster Binding into GlutaredoxinsMycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of MycobacteriaEnzyme structure captures four cysteines aligned for disulfide relayFormation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative StressCysteines under ROS attack in plants: a proteomics view.Electrostatics of cysteine residues in proteins: parameterization and validation of a simple model.Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli.Glutathionylation of trypanosomal thiol redox proteins.Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulationNeuronal Damage Induced by Perinatal Asphyxia Is Attenuated by Postinjury Glutaredoxin-2 AdministrationCharacterization of glutathione amide reductase from Chromatium gracile. Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling.S-Glutathionyl quantification in the attomole range using glutaredoxin-3-catalyzed cysteine derivatization and capillary gel electrophoresis with laser-induced fluorescence detection.Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.Thioredoxin 1-mediated post-translational modifications: reduction, transnitrosylation, denitrosylation, and related proteomics methodologies.Reversible silencing of CFTR chloride channels by glutathionylation.Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione.The reducing activity of glutaredoxin 3 toward cytoplasmic substrate proteins is restricted by methionine 43.Structure of Escherichia coli Grx2 in complex with glutathione: a dual-function hybrid of glutaredoxin and glutathione S-transferaseConferring specificity in redox pathways by enzymatic thiol/disulfide exchange reactions.Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling.Chaperone-like properties of tobacco plastid thioredoxins f and m.Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.Structure-function analysis of yeast Grx5 monothiol glutaredoxin defines essential amino acids for the function of the protein.A residue outside the active site CXXC motif regulates the catalytic efficiency of Glutaredoxin 3.Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase.Synthetic seleno-glutaredoxin 3 analogues are highly reducing oxidoreductases with enhanced catalytic efficiency.The dithiol glutaredoxins of african trypanosomes have distinct roles and are closely linked to the unique trypanothione metabolism.Crystallization and preliminary X-ray crystallographic studies of glutaredoxin 2 from Saccharomyces cerevisiae in different oxidation states.A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase.Determinants of activity in glutaredoxins: an in vitro evolved Grx1-like variant of Escherichia coli Grx3.GSTB1-1 from Proteus mirabilis: a snapshot of an enzyme in the evolutionary pathway from a redox enzyme to a conjugating enzyme.Mapping of a substrate binding site in the protein disulfide isomerase-related chaperone wind based on protein function and crystal structure.
P2860
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P2860
NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@ast
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@en
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@nl
type
label
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@ast
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@en
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@nl
prefLabel
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@ast
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@en
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@nl
P2093
P356
P1476
NMR structure of Escherichia c ...... ns for the enzymatic mechanism
@en
P2093
P304
P356
10.1006/JMBI.1998.2444
P407
P577
1999-02-01T00:00:00Z