Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure. - Wikidata - awgldk - TriplyDB

Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure.

Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure.

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Thiol-Based Peroxidases and Ascorbate Peroxidases: Why Plants Rely on Multiple Peroxidase Systems in the Photosynthesizing Chloroplast?The role of peroxiredoxin II in chemoresistance of breast cancer cells Dimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerization Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide: a kinetic and computational study Dual role of peroxiredoxin I in macrophage-derived foam cells Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.Peroxiredoxins and Redox Signaling in Plants.ATP-dependent modulation and autophosphorylation of rapeseed 2-Cys peroxiredoxin.A Proteome Translocation Response to Complex Desert Stress Environments in Perennial Phragmites Sympatric Ecotypes with Contrasting Water Availability Comparison of the chloroplast peroxidase system in the chlorophyte Chlamydomonas reinhardtii, the bryophyte Physcomitrella patens, the lycophyte Selaginella moellendorffii and the seed plant Arabidopsis thaliana.Natural genetic variation in the expression regulation of the chloroplast antioxidant system among Arabidopsis thaliana accessions.Chloroplast NADPH-dependent thioredoxin reductase from Chlorella vulgaris alleviates environmental stresses in yeast together with 2-Cys peroxiredoxin.Peroxiredoxins in plants and cyanobacteria.Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC The hydrogen peroxide-sensitive proteome of the chloroplast in vitro and in vivo.Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin Seleno-independent glutathione peroxidases. More than simple antioxidant scavengers.Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation NTRC new ways of using NADPH in the chloroplast.Redox signal integration: from stimulus to networks and genes.The peroxiredoxin and glutathione peroxidase families in Chlamydomonas reinhardtii Dissecting the integrative antioxidant and redox systems in plant mitochondria. Effect of stress and S-nitrosylation The oligomeric conformation of peroxiredoxins links redox state to function.First report of a peroxiredoxin homologue in jellyfish: molecular cloning, expression and functional characterization of CcPrx4 from Cyanea capillata.Generation of superoxide anion in chloroplasts of Arabidopsis thaliana during active photosynthesis: a focus on rapidly induced genes.Molecular characterization and expression analysis of a peroxiredoxin 1 cDNA from Korean rose bitterling (Rhodeus uyekii).Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2.2-Cys peroxiredoxin responds to low temperature and other cues in Caragana jubata, a plant species of cold desert of Himalaya.Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms.The conformational bases for the two functionalities of 2-cysteine peroxiredoxins as peroxidase and chaperone.Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus.In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation.Structural and biochemical characterization of peroxiredoxin Qbeta from Xylella fastidiosa: catalytic mechanism and high reactivity.Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions.Specificity versus redundancy in the RAP2.4 transcription factor family of Arabidopsis thaliana: transcriptional regulation of genes for chloroplast peroxidases.Antitumor quinol PMX464 is a cytocidal anti-trypanosomal inhibitor targeting trypanothione metabolism.A comparative study of type I and type II tryparedoxin peroxidases in Leishmania major.Functional analysis of the pathways for 2-Cys peroxiredoxin reduction in Arabidopsis thaliana chloroplasts.Regulatory subunit B'gamma of protein phosphatase 2A prevents unnecessary defense reactions under low light in Arabidopsis.Cloning, overexpression, purification and preliminary crystallographic studies of a mitochondrial type II peroxiredoxin from Pisum sativum.

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P2860

Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure.

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2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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Reaction mechanism of plant 2- ...... and the quaternary structure.

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Reaction mechanism of plant 2- ...... and the quaternary structure.

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Reaction mechanism of plant 2- ...... and the quaternary structure.

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Reaction mechanism of plant 2- ...... and the quaternary structure.

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Reaction mechanism of plant 2- ...... and the quaternary structure.

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Reaction mechanism of plant 2- ...... and the quaternary structure.

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Reaction mechanism of plant 2- ...... and the quaternary structure.

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Andreas Brockhinke

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Janine König

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Karl-Josef Dietz

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Kirsten Lotte

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Margarete Baier

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Regina Plessow

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P2860

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

Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli

Protective function of chloroplast 2-cysteine peroxiredoxin in photosynthesis. Evidence from transgenic Arabidopsis

Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product

Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution

The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins

Structures of tryparedoxins revealing interaction with trypanothione

Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution

Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution

Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae.

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24409-24420

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10.1074/JBC.M301145200

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27

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12702727

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