Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin. - Wikidata - awgldk - TriplyDB

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

http://www.wikidata.org/entity/Q37358101

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Mechanisms of altered redox regulation in neurodegenerative diseases--focus on S--glutathionylation Thiol redox chemistry: role of protein cysteine oxidation and altered redox homeostasis in allergic inflammation and asthma The sulfiredoxin-peroxiredoxin (Srx-Prx) axis in cell signal transduction and cancer development Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling Non-additive hepatic gene expression elicited by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and 2,2',4,4',5,5'-hexachlorobiphenyl (PCB153) co-treatment in C57BL/6 mice Oxidative stress and glutathione in TGF-beta-mediated fibrogenesis S-glutathionylation: from molecular mechanisms to health outcomes Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation Peroxiredoxin 1 (Prx1) is a dual-function enzyme by possessing Cys-independent catalase-like activity Redox regulation of lipopolysaccharide-mediated sulfiredoxin induction, which depends on both AP-1 and Nrf2.Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-Cys peroxiredoxin Prx3.Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin.Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity.Protein S-glutathiolation: redox-sensitive regulation of protein function.Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidases that function as antioxidants, molecular chaperones, and signal modulators.Aberrant sumoylation signaling evoked by reactive oxygen species impairs protective function of Prdx6 by destabilization and repression of its transcription.Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides.Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1).Strategies to decrease ongoing oxidant burden in chronic obstructive pulmonary disease.A comparison of reversible versus irreversible protein glutathionylation.Glutathione synthesis and its role in redox signaling.Genetic ablation of glutaredoxin-1 causes enhanced resolution of airways hyperresponsiveness and mucus metaplasia in mice with allergic airways disease Sulfiredoxin redox-sensitive interaction with S100A4 and non-muscle myosin IIA regulates cancer cell motility.Sulfiredoxin Promotes Colorectal Cancer Cell Invasion and Metastasis through a Novel Mechanism of Enhancing EGFR Signaling In vivo tagging and characterization of S-glutathionylated proteins by a chemoenzymatic method.Glutathionylation of the Active Site Cysteines of Peroxiredoxin 2 and Recycling by Glutaredoxin.Cysteine-based redox regulation and signaling in plants Loss of sulfiredoxin renders mice resistant to azoxymethane/dextran sulfate sodium-induced colon carcinogenesis.Involvement of redox state in the aging of Drosophila melanogaster.Pleiotropic functions of glutathione S-transferase P Regulation by glutathionylation of isocitrate lyase from Chlamydomonas reinhardtii.Localized redox relays as a privileged mode of cytoplasmic hydrogen peroxide signaling.Tumor promoter-induced sulfiredoxin is required for mouse skin tumorigenesis.S-glutathiolation in life and death decisions of the cell.S-glutathionylation of ion channels: insights into the regulation of channel functions, thiol modification crosstalk, and mechanosensing Glutathionylspermidine in the modification of protein SH groups: the enzymology and its application to study protein glutathionylation.Sulfhydryl-mediated redox signaling in inflammation: role in neurodegenerative diseases.Protein S-mycothiolation functions as redox-switch and thiol protection mechanism in Corynebacterium glutamicum under hypochlorite stress.

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P2860

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

http://www.wikidata.org/entity/Q37358101

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 27 June 2009

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

@en

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

@nl

type

label

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

@en

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

@nl

prefLabel

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

@en

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

@nl

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JBC.M109.021394

P1433

Journal of Biological Chemistry

P1476

Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

@en

P2093

Ji Won Park

http://www.w3.org/2001/XMLSchema#string

John J Mieyal

http://www.w3.org/2001/XMLSchema#string

P Boon Chock

http://www.w3.org/2001/XMLSchema#string

Sue Goo Rhee

http://www.w3.org/2001/XMLSchema#string

P2860

Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site

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

Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin

Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product

Mutagenesis and modeling of the peroxiredoxin (Prx) complex with the NMR structure of ATP-bound human sulfiredoxin implicate aspartate 187 of Prx I as the catalytic residue in ATP hydrolysis

Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerization

Structure of the sulphiredoxin–peroxiredoxin complex reveals an essential repair embrace

Thioredoxin-dependent peroxide reductase from yeast.

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

Human peroxiredoxin 1 and 2 are not duplicate proteins: the unique presence of CYS83 in Prx1 underscores the structural and functional differences between Prx1 and Prx2

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23364-23374

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scholarly article

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10.1074/JBC.M109.021394

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35

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284

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2009-06-27T00:00:00Z

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19561357

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2749110

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