Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member
about
Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediateProteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active siteRegulation of peroxiredoxin I activity by Cdc2-mediated phosphorylationA method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stressDimer-oligomer interconversion of wild-type and mutant rat 2-Cys peroxiredoxin: disulfide formation at dimer-dimer interfaces is not essential for decamerizationInactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acidIdentification and characterization of alternatively transcribed form of peroxiredoxin IV gene that is specifically expressed in spermatids of postpubertal mouse testisMice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stressAugmented expression of peroxiredoxin VI in rat lung and kidney after birth implies an antioxidative role.Down regulation of superoxide dismutases and glutathione peroxidase by reactive oxygen and nitrogen species.Hydrogen peroxide in the human body.Redox control systems in the nucleus: mechanisms and functions.Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.Identification of oxidative stress related proteins as biomarkers for lung cancer and chronic obstructive pulmonary disease in bronchoalveolar lavage.Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein.Overexpression of Peroxiredoxin 4 Affects Intestinal Function in a Dietary Mouse Model of Nonalcoholic Fatty Liver Disease.Expression of cyclooxygenase-2, peroxiredoxin I, peroxiredoxin 6 and nuclear factor-κB in oral squamous cell carcinomaAdipocyte-derived PAMM suppresses macrophage inflammation by inhibiting MAPK signallingThe effect of peroxiredoxin 4 on fly physiology is a complex interplay of antioxidant and signaling functionsDecreasing peroxiredoxin II expression decreases glutathione, alters cell cycle distribution, and sensitizes glioma cells to ionizing radiation and H(2)O(2).Redox regulation of fertilisation and the spermatogenic process.Destroy and exploit: catalyzed removal of hydroperoxides from the endoplasmic reticulumPeroxiredoxin 4 protects against nonalcoholic steatohepatitis and type 2 diabetes in a nongenetic mouse model.JNK/FOXO-mediated neuronal expression of fly homologue of peroxiredoxin II reduces oxidative stress and extends life span.Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis?The Relevance of Mammalian Peroxiredoxins to the Gametogenesis, Embryogenesis, and Pregnancy Outcomes.Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells.Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence.Induction of peroxiredoxin gene expression by oxygen in lungs of newborn primates.Molecular cloning and characterization of peroxiredoxin 4 involved in protection against oxidative stress in the silkworm Bombyx mori.Overexpression of peroxiredoxin 4 attenuates atherosclerosis in apolipoprotein E knockout mice.Peroxiredoxin distribution in the mouse brain with emphasis on neuronal populations affected in neurodegenerative disorders.Oxidative stress and antioxidants in hepatic pathogenesis.Alteration of gene expressions by the overexpression of mitochondrial phospholipid hydroperoxide glutathione peroxidase (mtPHGPx).Peroxiredoxins, a novel protein family in lung cancer.Peroxiredoxin 4 (PRDX4): Its critical in vivo roles in animal models of metabolic syndrome ranging from atherosclerosis to nonalcoholic fatty liver disease.Hydrogen peroxide produced by superoxide dismutase SOD-2 activates sperm in Caenorhabditis elegans.Peroxiredoxin genes are not induced in myeloid leukemia cells exposed to ionizing radiation.Mutual interaction between oxidative stress and endoplasmic reticulum stress in the pathogenesis of diseases specifically focusing on non-alcoholic fatty liver disease
P2860
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P2860
Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member
description
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1999
@ast
im Januar 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1999/01/29)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/01/29)
@nl
наукова стаття, опублікована в січні 1999
@uk
مقالة علمية (نشرت في 29-1-1999)
@ar
name
Cloning of the peroxiredoxin g ...... erization of the fourth member
@ast
Cloning of the peroxiredoxin g ...... erization of the fourth member
@en
Cloning of the peroxiredoxin g ...... erization of the fourth member
@nl
type
label
Cloning of the peroxiredoxin g ...... erization of the fourth member
@ast
Cloning of the peroxiredoxin g ...... erization of the fourth member
@en
Cloning of the peroxiredoxin g ...... erization of the fourth member
@nl
prefLabel
Cloning of the peroxiredoxin g ...... erization of the fourth member
@ast
Cloning of the peroxiredoxin g ...... erization of the fourth member
@en
Cloning of the peroxiredoxin g ...... erization of the fourth member
@nl
P2093
P2860
P3181
P1433
P1476
Cloning of the peroxiredoxin g ...... erization of the fourth member
@en
P2093
A. Matsumoto
M. Egashira
N. Niikawa
N. Taniguchi
P2860
P304
P3181
P356
10.1016/S0014-5793(98)01736-0
P407
P577
1999-01-29T00:00:00Z