Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. - Wikidata - awgldk - TriplyDB

Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.

Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.

http://www.wikidata.org/entity/Q40652199

about

Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine Defective mitochondrial peroxiredoxin-3 results in sensitivity to oxidative stress in Fanconi anemia Nuclear and cytoplasmic peroxiredoxin-1 differentially regulate NF-kappaB activities The NAD(P)H oxidase homolog Nox4 modulates insulin-stimulated generation of H2O2 and plays an integral role in insulin signal transduction Chemistry and biology of reactive oxygen species in signaling or stress responses H2O2-dependent hyperoxidation of peroxiredoxin 6 (Prdx6) plays a role in cellular toxicity via up-regulation of iPLA2 activity The peroxiredoxin repair proteins A conserved mechanism for sulfonucleotide reduction Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles Reciprocal Control of the Circadian Clock and Cellular Redox State - a Critical Appraisal The redox biology of schistosome parasites and applications for drug development The function of the NADPH thioredoxin reductase C-2-Cys peroxiredoxin system in plastid redox regulation and signalling The basics of thiols and cysteines in redox biology and chemistry Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling A primer on peroxiredoxin biochemistry Crystallographic and Mutational Studies of Mycobacterium tuberculosis recA Mini-inteins Suggest a Pivotal Role for a Highly Conserved Aspartate Residue Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate Cysteine S-Nitrosylation Protects Protein-tyrosine Phosphatase 1B against Oxidation-induced Permanent Inactivation Protein Engineering of the Quaternary Sulfiredoxin{middle dot}Peroxiredoxin Enzyme{middle dot}Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation Loss of yeast peroxiredoxin Tsa1p induces genome instability through activation of the DNA damage checkpoint and elevation of dNTP levels Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable.ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin.Proteomic profile of reversible protein oxidation using PROP, purification of reversibly oxidized proteins.Identification and characterization of alternatively transcribed form of peroxiredoxin IV gene that is specifically expressed in spermatids of postpubertal mouse testis Circadian redox signaling in plant immunity and abiotic stress Formation, Reactivity, and Detection of Protein Sulfenic Acids Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death.Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions.Prediction of reversibly oxidized protein cysteine thiols using protein structure properties The extraordinary catalytic ability of peroxiredoxins: a combined experimental and QM/MM study on the fast thiol oxidation step Cofactor binding protects flavodoxin against oxidative stress.Proteomic analysis of bladder cancer indicates Prx-I as a key molecule in BI-TK/GCV treatment system.A proteomic approach to identify early molecular targets of oxidative stress in human epithelial lens cells.Protein disulfide bond formation in the cytoplasm during oxidative stress.Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue.The redox sensor TXNL1 plays a regulatory role in fluid phase endocytosis.Tumor cell phenotype is sustained by selective MAPK oxidation in mitochondria.Specific expression profile and prognostic significance of peroxiredoxins in grade II-IV astrocytic brain tumors.Mitochondrial-targeted fluorescent probes for reactive oxygen species.

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P2860

Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.

http://www.wikidata.org/entity/Q40652199

description

2003 nî lūn-bûn

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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2003年论文

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2003年论文

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name

Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.

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Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.

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Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.

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Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.

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Ho Zoon Chae

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Hyun Ae Woo

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Kanghwa Kim

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Kap-Seok Yang

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Sang Won Kang

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Sue Goo Rhee

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Sung Chul Hwang

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