Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution.
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Structure of the Type III Pantothenate Kinase from Bacillus anthracis at 2.0 Å Resolution: Implications for Coenzyme A-Dependent Redox Biology † , ‡Pyridine Nucleotide Complexes with Bacillus anthracis Coenzyme A-Disulfide Reductase: A Structural Analysis of Dual NAD(P)H Specificity † ‡Crystal Structure and Catalytic Properties of Bacillus anthracis CoADR-RHD: Implications for Flavin-Linked Sulfur TraffickingTurnover-Dependent Covalent Inactivation of Staphylococcus aureus Coenzyme A-Disulfide Reductase by Coenzyme A-Mimetics: Mechanistic and Structural InsightsReal-Time Imaging of the Bacillithiol Redox Potential in the Human Pathogen Staphylococcus aureus Using a Genetically Encoded Bacilliredoxin-Fused Redox BiosensorBroad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum.Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis .A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR.Bacillithiol, a new player in bacterial redox homeostasis.The coenzyme A disulphide reductase of Borrelia burgdorferi is important for rapid growth throughout the enzootic cycle and essential for infection of the mammalian hostThe antibiotic CJ-15,801 is an antimetabolite that hijacks and then inhibits CoA biosynthesis.The orphan protein bis-γ-glutamylcystine reductase joins the pyridine nucleotide disulfide reductase family.Characterization of NADH oxidase/NADPH polysulfide oxidoreductase and its unexpected participation in oxygen sensitivity in an anaerobic hyperthermophilic archaeonProtein S-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap in Staphylococcus aureus Under Hypochlorite Stress.NADPH-dependent and -independent Disulfide Reductase Systems.Hydrogen Sulfide Sensing through Reactive Sulfur Species (RSS) and Nitroxyl (HNO) in Enterococcus faecalis.A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry.Deletion of BmoR affects the expression of genes related to thiol/disulfide balance in Bacteroides fragilis
P2860
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P2860
Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
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2006年论文
@zh-cn
name
Structure of coenzyme A-disulf ...... s aureus at 1.54 A resolution.
@en
type
label
Structure of coenzyme A-disulf ...... s aureus at 1.54 A resolution.
@en
prefLabel
Structure of coenzyme A-disulf ...... s aureus at 1.54 A resolution.
@en
P2093
P2860
P356
P1433
P1476
Structure of coenzyme A-disulf ...... us aureus at 1.54 A resolution
@en
P2093
Al Claiborne
Hiroaki Sakai
Jamie R Wallen
T Conn Mallett
Tomitake Tsukihara
P2860
P304
11278-11289
P356
10.1021/BI061139A
P407
P50
P577
2006-09-01T00:00:00Z