Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
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The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancerDisulfide-Bond-Forming Pathways in Gram-Positive BacteriaThe crystal structure of Mycobacterium tuberculosis alkylhydroperoxidase AhpD, a potential target for antitubercular drug designGram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosisAn Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression AnalysisMitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity.The evolutionarily conserved Dim1 protein defines a novel branch of the thioredoxin fold superfamilyThioredoxin peroxidases of the malarial parasite Plasmodium falciparumCrystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry.Identification of S-nitrosylation of proteins of Helicobacter pylori in response to nitric oxide stress.Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization.Reactive sulfur species: an emerging concept in oxidative stress.Glutathione--functions and metabolism in the malarial parasite Plasmodium falciparum.A comparative proteomic strategy for subcellular proteome research: ICAT approach coupled with bioinformatics prediction to ascertain rat liver mitochondrial proteins and indication of mitochondrial localization for catalase.Redox paradox: insulin action is facilitated by insulin-stimulated reactive oxygen species with multiple potential signaling targetsBiochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion.Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxinSeleno-independent glutathione peroxidases. More than simple antioxidant scavengers.Actinobacterial peroxidases: an unexplored resource for biocatalysis.Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. strain PCC 6803.Genome-wide analysis of thioredoxin fold superfamily peroxiredoxins in Arabidopsis and rice.Comparative phenotypic and physiological characteristics of spotted leaf 6 (spl6) and brown leaf spot2 (bl2) lesion mimic mutants (LMM) in rice.Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus.Antioxidant system within yeast peroxisome. Biochemical and physiological characterization of CbPmp20 in the methylotrophic yeast Candida boidinii.Evaluation of a new antigen for diagnosis of Helicobacter pylori infection in stool of adult and children.Characterization of novel hexadecameric thioredoxin peroxidase from Aeropyrum pernix K1.The Peroxiredoxin Family: An Unfolding Story.Peroxiredoxin genes are not induced in myeloid leukemia cells exposed to ionizing radiation.
P2860
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P2860
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
@en
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
@nl
type
label
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
@en
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
@nl
prefLabel
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
@en
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
@nl
P2860
P356
P1433
P1476
Evidence that peroxiredoxins are novel members of the thioredoxin fold superfamily.
@en
P2093
Schröder E
P2860
P304
P356
10.1002/PRO.5560071125
P577
1998-11-01T00:00:00Z