Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue. - Wikidata - wikimedia - TriplyDB

Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue.

Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue.

http://www.wikidata.org/entity/Q33287733

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The Measurement of Reversible Redox Dependent Post-translational Modifications and Their Regulation of Mitochondrial and Skeletal Muscle Function Ca(2+) signaling in the myocardium by (redox) regulation of PKA/CaMKII Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system 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 Formation and Reversibility of BiP Protein Cysteine Oxidation Facilitate Cell Survival during and post Oxidative Stress Redox regulation of soluble epoxide hydrolase by 15-deoxy-delta-prostaglandin J2 controls coronary hypoxic vasodilation Protein Oxidative Modifications: Beneficial Roles in Disease and Health Sulfenic acid chemistry, detection and cellular lifetime Biological Chemistry and Functionality of Protein Sulfenic Acids and Related Thiol Modifications 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.Methods for the determination and quantification of the reactive thiol proteome.Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding.Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins 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 Endosomal H2O2 production leads to localized cysteine sulfenic acid formation on proteins during lysophosphatidic acid-mediated cell signaling Postischemic deactivation of cardiac aldose reductase: role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids Proteomic approaches to the characterization of protein thiol modification.Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species.Antioxidant enzymes as redox-based biomarkers: a brief review The Expanding Landscape of the Thiol Redox Proteome.Overexpression of Catalase Diminishes Oxidative Cysteine Modifications of Cardiac Proteins.Interactions between mitochondrial reactive oxygen species and cellular glucose metabolism.Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes.Profiling the Reactivity of Cyclic C-Nucleophiles towards Electrophilic Sulfur in Cysteine Sulfenic Acid Activity of the tetrapyrrole regulator CrtJ is controlled by oxidation of a redox active cysteine located in the DNA binding domain.Methods to monitor classical protein-tyrosine phosphatase oxidation.Cardiovascular redox and ox stress proteomics.Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity.Deubiquitinases as a signaling target of oxidative stress.RegB kinase activity is repressed by oxidative formation of cysteine sulfenic acid.Highly efficient and selective enrichment of peptide subsets combining fluorous chemistry with reversed-phase chromatography Simple synthesis of 1,3-cyclopentanedione derived probes for labeling sulfenic acid proteins

P2860

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P2860

Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue.

http://www.wikidata.org/entity/Q33287733

description

2007 nî lūn-bûn

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2007 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2007年の論文

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Protein sulfenation as a redox ...... iotinylated dimedone analogue.

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Protein sulfenation as a redox ...... iotinylated dimedone analogue.

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Molecular & Cellular Proteomics

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Protein sulfenation as a redox ...... iotinylated dimedone analogue.

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Ewald Schröder

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Georgina May

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Piers R J Gaffney

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Rebecca L Charles

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Richard J Heads

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Robin Wait

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Shajna Begum

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P2860

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

Structural basis of the redox switch in the OxyR transcription factor

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

Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes

The utility of N,N-biotinyl glutathione disulfide in the study of protein S-glutathiolation

Simultaneous preparation of the three biotin-containing mitochondrial carboxylases from rat liver

Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple

Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison.

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10.1074/MCP.M700065-MCP200

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9

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