Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. - Wikidata - awgldk - TriplyDB

Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

http://www.wikidata.org/entity/Q33580845

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Differential alkylation-based redox proteomics--Lessons learnt Cellular biochemistry methods for investigating protein tyrosine phosphatases Mass spectrometry in studies of protein thiol chemistry and signaling: opportunities and caveats Chemical approaches to detect and analyze protein sulfenic acids Redox modification of cell signaling in the cardiovascular system The redox biochemistry of protein sulfenylation and sulfinylation Protein Oxidative Modifications: Beneficial Roles in Disease and Health Purification of reversibly oxidized proteins (PROP) reveals a redox switch controlling p38 MAP kinase activity.Redox activation of aldose reductase in the ischemic heart Sulfenic acid chemistry, detection and cellular lifetime Formation, Reactivity, and Detection of Protein Sulfenic Acids Measurement of Reactive Oxygen Species, Reactive Nitrogen Species, and Redox-Dependent Signaling in the Cardiovascular System: A Scientific Statement From the American Heart Association.Cysteines under ROS attack in plants: a proteomics view.Proteomic approaches to quantify cysteine reversible modifications in aging and neurodegenerative diseases.Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding.Cofactor binding protects flavodoxin against oxidative stress.Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways.Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue.Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation Possibilities and pitfalls in quantifying the extent of cysteine sulfenic acid modification of specific proteins within complex biofluids.Protein redox modification as a cellular defense mechanism against tissue ischemic injury.Effects of ionizing radiation on biological molecules--mechanisms of damage and emerging methods of detection Metabolic profiling reveals that PNPLA3 induces widespread effects on metabolism beyond triacylglycerol remodeling in Huh-7 hepatoma cells.Biochemical methods for monitoring protein thiol redox states in biological systems Effect of cysteic acid position on the negative ion fragmentation of proteolytic derived peptides.Caloric restriction and the aging process: a critique Postischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids Posttranslational glutathiolation of aldose reductase (AKR1B1): a possible mechanism of protein recovery from S-nitrosylation.The redoxome: Proteomic analysis of cellular redox networks.Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Chemical methods for the proteome-wide identification of posttranslationally modified proteins Association between life-span extension by caloric restriction and thiol redox state in two different strains of mice.The redox stress hypothesis of aging Cell signalling by reactive lipid species: new concepts and molecular mechanisms.Identification of a redox-sensitive switch within the JAK2 catalytic domain.Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes.Chemical methods for the direct detection and labeling of S-nitrosothiols.Activity of the tetrapyrrole regulator CrtJ is controlled by oxidation of a redox active cysteine located in the DNA binding domain.

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P2860

Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

http://www.wikidata.org/entity/Q33580845

description

2004 nî lūn-bûn

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2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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name

Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Proceedings of the National Academy of Sciences of the United States of America

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Widespread sulfenic acid formation in tissues in response to hydrogen peroxide.

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Hendrik Neubert

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Jonathan P Brennan

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P2860

Cell transformation by the superoxide-generating oxidase Mox1

Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1

Apoptosis repressor with caspase recruitment domain protects against cell death by interfering with Bax activation

Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore

MEKK1 suppresses oxidative stress-induced apoptosis of embryonic stem cell-derived cardiac myocytes

Structural basis of the redox switch in the OxyR transcription factor

Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

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

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

Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation

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