On the role of the cis-proline residue in the active site of DsbA
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The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-IThe structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolismProperties 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 EnzymesCrystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITECrystal Structure of the Human Ubiquitin-activating Enzyme 5 (UBA5) Bound to ATP: MECHANISTIC INSIGHTS INTO A MINIMALISTIC E1 ENZYMEThe Multidrug Resistance IncA/C Transferable Plasmid Encodes a Novel Domain-swapped Dimeric Protein-disulfide IsomeraseConservation of cis prolyl bonds in proteins during evolution.Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.The acidic nature of the CcmG redox-active center is important for cytochrome c maturation in Escherichia coli.Structural basis for heterogeneous phenotype of ERG11 dependent Azole resistance in C.albicans clinical isolatesFunctional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.On the non-respect of the thermodynamic cycle by DsbA variants.Force-dependent isomerization kinetics of a highly conserved proline switch modulates the mechanosensing region of filamin.Mechanisms of oxidative protein folding in the bacterial cell envelope.F-like type IV secretion systems encode proteins with thioredoxin folds that are putative DsbC homologues.Acceleration of protein folding by four orders of magnitude through a single amino acid substitution.Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily.The role of an evolutionarily conserved cis-proline in the thioredoxin-like domain of human class Alpha glutathione transferase A1-1.The thiol-disulfide oxidoreductase system in the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC 125: discovery of a novel disulfide oxidoreductase enzyme.Prediction of pKa and redox properties in the thioredoxin superfamily.A novel method of analyzing proline synonymous codons in E. coli.The SAAPdb web resource: a large-scale structural analysis of mutant proteins.Structural role of a conserved active site cis proline in the Thermotoga maritima acetyl esterase from the carbohydrate esterase family 7.Crystal structures of E. coli CcmG and its mutants reveal key roles of the N-terminal beta-sheet and the fingerprint region.Evidence that the substrate backbone conformation is critical to phosphorylation by p42 MAP kinase
P2860
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P2860
On the role of the cis-proline residue in the active site of DsbA
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին 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
On the role of the cis-proline residue in the active site of DsbA
@ast
On the role of the cis-proline residue in the active site of DsbA
@en
On the role of the cis-proline residue in the active site of DsbA
@nl
type
label
On the role of the cis-proline residue in the active site of DsbA
@ast
On the role of the cis-proline residue in the active site of DsbA
@en
On the role of the cis-proline residue in the active site of DsbA
@nl
prefLabel
On the role of the cis-proline residue in the active site of DsbA
@ast
On the role of the cis-proline residue in the active site of DsbA
@en
On the role of the cis-proline residue in the active site of DsbA
@nl
P2093
P2860
P356
P1433
P1476
On the role of the cis-proline residue in the active site of DsbA
@en
P2093
P2860
P304
P356
10.1110/PS.8.1.96
P577
1999-01-01T00:00:00Z