Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidases that function as antioxidants, molecular chaperones, and signal modulators. - Wikidata - wikimedia - TriplyDB

Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidases that function as antioxidants, molecular chaperones, and signal modulators.

Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidases that function as antioxidants, molecular chaperones, and signal modulators.

http://www.wikidata.org/entity/Q35721861

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Utilizing Natural and Engineered Peroxiredoxins As Intracellular Peroxide Reporters Thiol-Based Peroxidases and Ascorbate Peroxidases: Why Plants Rely on Multiple Peroxidase Systems in the Photosynthesizing Chloroplast?Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling The sulfiredoxin-peroxiredoxin (Srx-Prx) axis in cell signal transduction and cancer development Protein Oxidative Modifications: Beneficial Roles in Disease and Health Mitochondrial peroxiredoxin 3 regulates sensory cell survival in the cochlea Biological Chemistry and Functionality of Protein Sulfenic Acids and Related Thiol Modifications Proteomic analysis of bladder cancer indicates Prx-I as a key molecule in BI-TK/GCV treatment system.Nitrosative stress induces peroxiredoxin 1 ubiquitination during ischemic insult via E6AP activation in endothelial cells both in vitro and in vivo.Peroxiredoxin 1 (Prx1) is a dual-function enzyme by possessing Cys-independent catalase-like activity Identification of O-GlcNAc modification targets in mouse retinal pericytes: implication of p53 in pathogenesis of diabetic retinopathy.Cold Atmospheric Plasma Treatment Induces Anti-Proliferative Effects in Prostate Cancer Cells by Redox and Apoptotic Signaling Pathways.Cysteine-independent Catalase-like Activity of Vertebrate Peroxiredoxin 1 (Prx1).Redox reactions in mammalian spermatogenesis and the potential targets of reactive oxygen species under oxidative stress Repeated Superovulation via PMSG/hCG Administration Induces 2-Cys Peroxiredoxins Expression and Overoxidation in the Reproductive Tracts of Female Mice Roles for cytosolic NADPH redox in regulating pulmonary artery relaxation by thiol oxidation-elicited subunit dimerization of protein kinase G1α Involvement of redox state in the aging of Drosophila melanogaster.Identification of DUOX1-dependent redox signaling through protein S-glutathionylation in airway epithelial cells.Peroxiredoxin 2 is associated with colorectal cancer progression and poor survival of patients.Cell stress proteins in atherothrombosis Molecular biology of atherosclerosis.The impact of thiol peroxidases on redox regulation.Sulfonation of the resolving cysteine in human peroxiredoxin 1: A comprehensive analysis by mass spectrometry.Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling.Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling.Protein S-mycothiolation functions as redox-switch and thiol protection mechanism in Corynebacterium glutamicum under hypochlorite stress.The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone.Purification and Characterization of an ATPase GsiA from Salmonella enterica Hyperglycemia decreases preoxiredoxin-2 expression in a middle cerebral artery occlusion model Phosphoribulokinase from Chlamydomonas reinhardtii: a Benson-Calvin cycle enzyme enslaved to its cysteine residues.Peroxiredoxin 1 interacts with and blocks the redox factor APE1 from activating interleukin-8 expression.Glutathionylation of Pea Chloroplast 2-Cys Prx and Mitochondrial Prx IIF Affects Their Structure and Peroxidase Activity and Sulfiredoxin Deglutathionylates Only the 2-Cys Prx.Posttranslational modification of cysteine in redox signaling and oxidative stress: Focus on s-glutathionylation.Prognostic significance of mammalian sterile 20-like kinase 1 in breast cancer.Thioredoxin system-mediated regulation of mutant Kras associated pancreatic neoplasia and cancer.THE MULTI-FACETED IMPACT OF PEROXIREDOXINS ON AGING AND DISEASE.Role of Dietary Antioxidants in the Preservation of Vascular Function and the Modulation of Health and Disease.Prx II and CKBB proteins interaction under physiologic al and thermal stress conditions in A549 and HeLa cells.Mitochondrial uncoupling proteins: subtle regulators of cellular redox signaling.The intriguing CP12-like tail of adenylate kinase 3 from Chlamydomonas reinhardtii.

P2860

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P2860

Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidases that function as antioxidants, molecular chaperones, and signal modulators.

http://www.wikidata.org/entity/Q35721861

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Protein glutathionylation in t ...... erones, and signal modulators.

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Protein glutathionylation in t ...... erones, and signal modulators.

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type

label

Protein glutathionylation in t ...... erones, and signal modulators.

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Protein glutathionylation in t ...... erones, and signal modulators.

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prefLabel

Protein glutathionylation in t ...... erones, and signal modulators.

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Protein glutathionylation in t ...... erones, and signal modulators.

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P1433

Antioxidants & Redox Signaling

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Protein glutathionylation in t ...... erones, and signal modulators.

@en

P2093

Hammou Oubrahim

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

Ho Zoon Chae

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Ji Won Park

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P Boon Chock

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

Sue Goo Rhee

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P2860

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

1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities

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

Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation

Oligomeric peroxiredoxin-I is an essential intermediate for p53 to activate MST1 kinase and apoptosis

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

HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation

Prdx1 inhibits tumorigenesis via regulating PTEN/AKT activity

Characterization of a mammalian peroxiredoxin that contains one conserved cysteine

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506-523

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10.1089/ARS.2011.4260

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6

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16

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51828230

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22114845

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molecular chaperones

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3270059

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