Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins. - Test2 - elhamkhani - TriplyDB

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

http://www.wikidata.org/entity/Q33983693

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The peroxiredoxin repair proteins A conserved mechanism for sulfonucleotide reduction Hydrogen peroxide - production, fate and role in redox signaling of tumor cells Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system Abnormal Ca(2+) cycling in failing ventricular myocytes: role of NOS1-mediated nitroso-redox balance Hydrogen peroxide sensing, signaling and regulation of transcription factors Structure of the sulphiredoxin–peroxiredoxin complex reveals an essential repair embrace Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate Protein Engineering of the Quaternary Sulfiredoxin{middle dot}Peroxiredoxin Enzyme{middle dot}Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation The sulfiredoxin-peroxiredoxin (Srx-Prx) axis in cell signal transduction and cancer development Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta Emerging roles of Nrf2 and phase II antioxidant enzymes in neuroprotection Dual role of peroxiredoxin I in macrophage-derived foam cells Identification and characterization of alternatively transcribed form of peroxiredoxin IV gene that is specifically expressed in spermatids of postpubertal mouse testis DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-like peroxidase Inactivation of cytosolic aldehyde dehydrogenase via S-nitrosylation in ethanol-exposed rat liver Effects of thioredoxin reductase-1 deletion on embryogenesis and transcriptome The antioxidant protein alkylhydroperoxide reductase of Helicobacter pylori switches from a peroxide reductase to a molecular chaperone function.Peroxiredoxins and Redox Signaling in Plants.Increased oxidation and degradation of cytosolic proteins in alcohol-exposed mouse liver and hepatoma cells.Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue.ATP-dependent modulation and autophosphorylation of rapeseed 2-Cys peroxiredoxin.Peroxiredoxin 6 fails to limit phospholipid peroxidation in lung from Cftr-knockout mice subjected to oxidative challenge.Human cell toxicogenomic analysis linking reactive oxygen species to the toxicity of monohaloacetic acid drinking water disinfection byproducts.Redox control of liver function in health and disease Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin II by H2O2 in red blood cells.Reactive oxygen and nitrogen species in steatotic hepatocytes: a molecular perspective on the pathophysiology of ischemia-reperfusion injury in the fatty liver.Circadian rhythm of hyperoxidized peroxiredoxin II is determined by hemoglobin autoxidation and the 20S proteasome in red blood cells.Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia Redox regulation of lipopolysaccharide-mediated sulfiredoxin induction, which depends on both AP-1 and Nrf2.Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide-mediated S-nitrosylation.Structural basis for the retroreduction of inactivated peroxiredoxins by human sulfiredoxin Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin.Novel oxidative modifications in redox-active cysteine residues.Cysteine oxidation within N-terminal mutant huntingtin promotes oligomerization and delays clearance of soluble protein.Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin.Post-translational modifications of mitochondrial aldehyde dehydrogenase and biomedical implications.Nuclear factor E2-related factor 2 dependent overexpression of sulfiredoxin and peroxiredoxin III in human lung cancer.Oxidative stress as a potential causal factor for autoimmune hemolytic anemia and systemic lupus erythematosus Sulfiredoxin protein is critical for redox balance and survival of cells exposed to low steady-state levels of H2O2.

P2860

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P2860

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

http://www.wikidata.org/entity/Q33983693

description

2004 nî lūn-bûn

@nan

2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

@ast

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

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type

label

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

@ast

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

@en

prefLabel

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

@ast

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

@en

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P1433

Journal of Biological Chemistry

P1476

Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

@en

P2093

Hyun Ae Woo

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Jeong Soo Yang

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Kwang Joo Park

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Sue Goo Rhee

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Sung Jun Park

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Tong-Shin Chang

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Woojin Jeong

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P2860

Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate

Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine

Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation

Characterization of a mammalian peroxiredoxin that contains one conserved cysteine

Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes

Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling

ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.

Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD

Peroxiredoxin, a novel family of peroxidases

Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid

P304

3125-3128

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scholarly article

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10.1074/JBC.C400496200

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5

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P478

280

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2004-12-08T00:00:00Z

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P698

15590625

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