The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases.
about
Disulfide bond formation in the bacterial periplasm: major achievements and challenges aheadMany roles of the bacterial envelope reducing pathwaysReducing systems protecting the bacterial cell envelope from oxidative damageMolecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulenceBacterial thiol oxidoreductases - from basic research to new antibacterial strategiesA new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelopeCharacterization of DsbD in Neisseria meningitidis.Comparative Roles of the Two Helicobacter pylori Thioredoxins in Preventing Macromolecule DamagePneumococcal gene complex involved in resistance to extracellular oxidative stress.Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function.A low pKa cysteine at the active site of mouse methionine sulfoxide reductase AMisR/MisS two-component regulon in Neisseria meningitidis.A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis.Increased catalytic efficiency following gene fusion of bifunctional methionine sulfoxide reductase enzymes from Shewanella oneidensisA periplasmic thioredoxin-like protein plays a role in defense against oxidative stress in Neisseria gonorrhoeae.A new role for Escherichia coli DsbC protein in protection against oxidative stressOxidative stress, protein damage and repair in bacteria.Biochemical and functional characterization of a periplasmic disulfide oxidoreductase from Neisseria meningitidis essential for meningococcal viability.Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons.
P2860
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P2860
The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
The thioredoxin domain of Neis ...... thionine sulfoxide reductases.
@en
The thioredoxin domain of Neis ...... thionine sulfoxide reductases.
@nl
type
label
The thioredoxin domain of Neis ...... thionine sulfoxide reductases.
@en
The thioredoxin domain of Neis ...... thionine sulfoxide reductases.
@nl
prefLabel
The thioredoxin domain of Neis ...... thionine sulfoxide reductases.
@en
The thioredoxin domain of Neis ...... thionine sulfoxide reductases.
@nl
P2093
P2860
P356
P1476
The thioredoxin domain of Neis ...... thionine sulfoxide reductases.
@en
P2093
Herbert Weissbach
Lynnette C Johnson
Nathan Brot
Thomas J Jönsson
W Todd Lowther
P2860
P304
32668-32675
P356
10.1074/JBC.M604971200
P407
P577
2006-08-22T00:00:00Z