Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery. - Wikidata - awgldk - TriplyDB

Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery.

Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery.

http://www.wikidata.org/entity/Q36119402

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H2O2-dependent hyperoxidation of peroxiredoxin 6 (Prdx6) plays a role in cellular toxicity via up-regulation of iPLA2 activity Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles The thioredoxin/peroxiredoxin/sulfiredoxin system: current overview on its redox function in plants and regulation by reactive oxygen and nitrogen species Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling A primer on peroxiredoxin biochemistry Structure of the sulphiredoxin–peroxiredoxin complex reveals an essential repair embrace Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate Protein Engineering of the Quaternary Sulfiredoxin{middle dot}Peroxiredoxin Enzyme{middle dot}Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4 Crystal Structure of Reduced and of Oxidized Peroxiredoxin IV Enzyme Reveals a Stable Oxidized Decamer and a Non-disulfide-bonded Intermediate in the Catalytic Cycle Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys Peroxiredoxin Structural Snapshots of Yeast Alkyl Hydroperoxide Reductase Ahp1 Peroxiredoxin Reveal a Novel Two-cysteine Mechanism of Electron Transfer to Eliminate Reactive Oxygen Species Peroxiredoxin 3 is a redox-dependent target of thiostrepton in malignant mesothelioma cells Crystallization and preliminary crystallographic analysis of mouse peroxiredoxin II with significant pseudosymmetry.Downstream targets and intracellular compartmentalization in Nox signaling.Resistance of Biomphalaria glabrata 13-16-R1 snails to Schistosoma mansoni PR1 is a function of haemocyte abundance and constitutive levels of specific transcripts in haemocytes Signaling functions of reactive oxygen species.Cysteine-based redox switches in enzymes Analysis of the peroxiredoxin family: using active-site structure and sequence information for global classification and residue analysis.Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin.Overview of peroxiredoxins in oxidant defense and redox regulation.Proteomics of Fusarium oxysporum race 1 and race 4 reveals enzymes involved in carbohydrate metabolism and ion transport that might play important roles in banana Fusarium wilt.Oxidative stress modulates heme synthesis and induces peroxiredoxin-2 as a novel cytoprotective response in β-thalassemic erythropoiesis.Activation of hypoxia-inducible factor-1 protects airway epithelium against oxidant-induced barrier dysfunction.Peroxiredoxins in parasites.Peroxiredoxin-2 expression is increased in beta-thalassemic mouse red cells but is displaced from the membrane as a marker of oxidative stress.S-nitrosylation of peroxiredoxin 2 promotes oxidative stress-induced neuronal cell death in Parkinson's disease Protein kinase A-mediated CREB phosphorylation is an oxidant-induced survival pathway in alveolar type II cells Discovering mechanisms of signaling-mediated cysteine oxidation.Redox-based regulation of signal transduction: principles, pitfalls, and promises Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase system Increasing extracellular H2O2 produces a bi-phasic response in intracellular H2O2, with peroxiredoxin hyperoxidation only triggered once the cellular H2O2-buffering capacity is overwhelmed.A redox-sensitive peroxiredoxin that is important for longevity has tissue- and stress-specific roles in stress resistance.Decreasing peroxiredoxin II expression decreases glutathione, alters cell cycle distribution, and sensitizes glioma cells to ionizing radiation and H(2)O(2).Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins.Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity Natural Killer cell-dependent and non-dependent anti-viral activity of 2-Cys Peroxiredoxin against HIV.A direct and continuous assay for the determination of thioredoxin reductase activity in cell lysates.Typical 2-Cys peroxiredoxins--structures, mechanisms and functions.Comparative proteomic analysis of cysteine oxidation in colorectal cancer patients.

P2860

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P2860

Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery.

http://www.wikidata.org/entity/Q36119402

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2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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Oxidation state governs struct ...... ell cycle arrest and recovery.

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Oxidation state governs struct ...... ell cycle arrest and recovery.

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Oxidation state governs struct ...... ell cycle arrest and recovery.

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Oxidation state governs struct ...... ell cycle arrest and recovery.

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Oxidation state governs struct ...... ell cycle arrest and recovery.

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Oxidation state governs struct ...... ell cycle arrest and recovery.

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Oxidation state governs struct ...... ell cycle arrest and recovery.

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Alan K Howe

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Albert van der Vliet

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Kelly Weirather

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Leslie B Poole

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Nicholas H Heintz

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Paula B Deming

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Thomas J Jönsson

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Timothy J Phalen

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Vikas Anathy

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P2860

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

Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation

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

The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity

Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling

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

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

Structure, mechanism and regulation of peroxiredoxins

Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography

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779-789

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10.1083/JCB.200606005

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5

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175

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Albert van der Vliet

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2006-12-01T00:00:00Z

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6653084

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