Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver - Test2 - elhamkhani - TriplyDB

Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver

Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver

http://www.wikidata.org/entity/Q28578397

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Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organization Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease 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 Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa. New insights into the specificity of thioredoxin function Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine Thioredoxin reductase Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Structures of tryparedoxins revealing interaction with trypanothione Crystal structure of the human thioredoxin reductase-thioredoxin complex Structural Analysis of Glutaredoxin Domain of Mus musculus Thioredoxin Glutathione Reductase Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity.Selenium and its supplementation in cardiovascular disease--what do we know?Distribution of protein disulphide isomerase in rat liver mitochondria Gene expression changes for antioxidants pathways in the mouse cochlea: relations to age-related hearing deficits.Mammalian thioredoxin reductase 1: roles in redox homoeostasis and characterization of cellular targets Expression of novel antioxidant thioredoxin-2 in the rat brain Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems Indolin-2-one compounds targeting thioredoxin reductase as potential anticancer drug leads Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide.Development of a human mitochondrial oligonucleotide microarray (h-MitoArray) and gene expression analysis of fibroblast cell lines from 13 patients with isolated F1Fo ATP synthase deficiency.Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells Pathogenic role of oxidative and nitrosative stress in primary biliary cirrhosis.News and views on thioredoxin reductases.Glutaredoxin 2 reduces both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal.Up-regulation of thioredoxin and thioredoxin reductase in human malignant pleural mesothelioma.Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.Thioredoxin reductase two modes of catalysis have evolved.Ebselen: a substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant Mitochondrial Thioredoxin-Glutathione Reductase from Larval Taenia crassiceps (Cysticerci).Selenium in biology: facts and medical perspectives.Trends in selenium biochemistry.Characterization of protein targets of mammalian thioredoxin reductases.Mammalian thioredoxin reductase: oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity.Thioredoxin reductase-2 is essential for keeping low levels of H(2)O(2) emission from isolated heart mitochondria.Manganese superoxide dismutase: guardian of the powerhouse.Mitochondrial peroxiredoxin III is a potential target for cancer therapy The subcellular location of selenoproteins and the impact on their function.

P2860

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P2860

Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver

http://www.wikidata.org/entity/Q28578397

description

1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

artículu científicu espublizáu en 1999

@ast

im Februar 1999 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 1999/02/19)

@sk

vědecký článek publikovaný v roce 1999

@cs

wetenschappelijk artikel (gepubliceerd op 1999/02/19)

@nl

наукова стаття, опублікована в лютому 1999

@uk

name

Molecular cloning and characte ...... doxin reductase from rat liver

@ast

Molecular cloning and characte ...... doxin reductase from rat liver

@en

Molecular cloning and characte ...... doxin reductase from rat liver

@nl

type

label

Molecular cloning and characte ...... doxin reductase from rat liver

@ast

Molecular cloning and characte ...... doxin reductase from rat liver

@en

Molecular cloning and characte ...... doxin reductase from rat liver

@nl

prefLabel

Molecular cloning and characte ...... doxin reductase from rat liver

@ast

Molecular cloning and characte ...... doxin reductase from rat liver

@en

Molecular cloning and characte ...... doxin reductase from rat liver

@nl

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Journal of Biological Chemistry

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Molecular cloning and characte ...... doxin reductase from rat liver

@en

P2093

A. Ginsburg

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

H. W. Yoon

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J. R. Kim

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K. S. Kwon

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R. L. Levine

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S. G. Rhee

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S. R. Lee

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P2860

Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation

Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked

A new human selenium-containing protein. Purification, characterization, and cDNA sequence

Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1.

Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes

The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin

Cloning and sequencing of mammalian glutathione reductase cDNA

Very long chain and long chain acyl-CoA thioesterases in rat liver mitochondria. Identification, purification, characterization, and induction by peroxisome proliferators

Cloning and expression of a novel mammalian thioredoxin

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scholarly article

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4820841

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10.1074/JBC.274.8.4722

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8

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P478

274

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1999-02-19T00:00:00Z

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9988709

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P921

L-selenocysteine