The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
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Flux analysis uncovers key role of functional redundancy in formaldehyde metabolismStructures of gram-negative cell walls and their derived membrane vesiclesThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaEfficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasmShedding light on disulfide bond formation: engineering a redox switch in green fluorescent proteinCrystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITEFunctional differences in yeast protein disulfide isomerases.NF-κB, JNK, and TLR Signaling Pathways in HepatocarcinogenesisFunctional studies of multiple thioredoxins from Mycobacterium tuberculosisStrategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Characterization of an HPr kinase mutant of Staphylococcus xylosus.Pathogenicity of Salmonella enterica in Caenorhabditis elegans relies on disseminated oxidative stress in the infected hostSalmonella enterica serovar typhimurium trxA mutants are protective against virulent challenge and induce less inflammation than the live-attenuated vaccine strain SL3261.Thiol-based redox switchesCharacterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin.Catalase-peroxidases of Legionella pneumophila: cloning of the katA gene and studies of KatA function.Functional specialization of Chlamydomonas reinhardtii cytosolic thioredoxin h1 in the response to alkylation-induced DNA damageIdentification of genes in an extraintestinal isolate of Escherichia coli with increased expression after exposure to human urine.Escherichia coli and Salmonella 2000: the view from here.Link between the membrane-bound pyridine nucleotide transhydrogenase and glutathione-dependent processes in Rhodobacter sphaeroidesDefenses against oxidative stress in Neisseria gonorrhoeae: a system tailored for a challenging environmentThioredoxin 1 promotes intracellular replication and virulence of Salmonella enterica serovar Typhimurium.Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD.Comparative genomics of enterococci: variation in Enterococcus faecalis, clade structure in E. faecium, and defining characteristics of E. gallinarum and E. casseliflavus.Escherichia coli FtnA acts as an iron buffer for re-assembly of iron-sulfur clusters in response to hydrogen peroxide stressThioredoxin 1 participates in the activity of the Salmonella enterica serovar Typhimurium pathogenicity island 2 type III secretion system.trans-acting mutations in loci other than kdpDE that affect kdp operon regulation in Escherichia coli: effects of cytoplasmic thiol oxidation status and nucleoid protein H-NS on kdp expression.Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD.DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis.Spx is a global effector impacting stress tolerance and biofilm formation in Staphylococcus aureus.Human Tissue Plasminogen Activator Expression in Escherichia coli using Cytoplasmic and Periplasmic Cumulative Power.Effects of oxygen on biofilm formation and the AtlA autolysin of Streptococcus mutans.Secretion of human serum albumin by Kluyveromyces lactis overexpressing KlPDI1 and KlERO1.Re-engineering redox-sensitive green fluorescent protein for improved response rate.Prediction of pKa and redox properties in the thioredoxin superfamily.
P2860
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P2860
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին 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
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@ast
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@en
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@nl
type
label
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@ast
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@en
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@nl
prefLabel
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@ast
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@en
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@nl
P2860
P1476
The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.
@en
P2093
P2860
P304
P407
P577
1999-03-01T00:00:00Z