Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
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Structural basis of cellular redox regulation by human TRP14Disulfide-Bond-Forming Pathways in Gram-Positive BacteriaOn the role of the cis-proline residue in the active site of DsbAStaphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative foldingProperties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid ResidueThe Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA EnzymesStructural and Mechanistic Insights into Unusual Thiol Disulfide OxidoreductaseRv2969c, 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 oxidasesComparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct ClassesThe Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide IsomeraseThe 1.2 Å resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin productionCrystal Structure of the Dithiol Oxidase DsbA Enzyme from Proteus Mirabilis Bound Non-covalently to an Active Site Peptide LigandStructural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising OxidoreductaseMutational analysis of the disulfide catalysts DsbA and DsbB.Electrostatics of cysteine residues in proteins: parameterization and validation of a simple model.Characterization of SrgA, a Salmonella enterica serovar Typhimurium virulence plasmid-encoded paralogue of the disulfide oxidoreductase DsbA, essential for biogenesis of plasmid-encoded fimbriae.Determination of ligand binding modes in weak protein-ligand complexes using sparse NMR data.Variation in the Subcellular Localization and Protein Folding Activity among Arabidopsis thaliana Homologs of Protein Disulfide Isomerase.Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member.IgG4 breaking the rules.Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF.Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.Key players involved in bacterial disulfide-bond formation.Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis.Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073.Increasing protein stability: importance of DeltaC(p) and the denatured state.Differences between the electronic environments of reduced and oxidized Escherichia coli DsbA inferred from heteronuclear magnetic resonance spectroscopyINHIBITION OF DIVERSE DsbA ENZYMES IN MULTI-DsbA ENCODING PATHOGENS.The CXXC motif is more than a redox rheostat.Mechanical architecture and folding of E. coli type 1 pilus domains.
P2860
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P2860
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Structural analysis of three H ...... le of His32 in DsbA stability.
@en
type
label
Structural analysis of three H ...... le of His32 in DsbA stability.
@en
prefLabel
Structural analysis of three H ...... le of His32 in DsbA stability.
@en
P2093
P2860
P356
P1433
P1476
Structural analysis of three H ...... ole of His32 in DsbA stability
@en
P2093
Bardwell JC
Glockshuber R
Huber-Wunderlich M
P2860
P304
P356
10.1002/PRO.5560060910
P577
1997-09-01T00:00:00Z