about
Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoaMitochondrial Redox Signaling and Tumor ProgressionAdvanced glycation end-products: modifiable environmental factors profoundly mediate insulin resistanceCharacterization of human thioredoxin-like-1: potential involvement in the cellular response against glucose deprivationArsenic binding to proteinsc-Myc and AMPK Control Cellular Energy Levels by Cooperatively Regulating Mitochondrial Structure and FunctionStructural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparumHuman spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity.The characterization of the Caenorhabditis elegans mitochondrial thioredoxin system uncovers an unexpected protective role of thioredoxin reductase 2 in β-amyloid peptide toxicity.Control of mitochondrial outer membrane permeabilization and Bcl-xL levels by thioredoxin 2 in DT40 cells.DNA damage related crosstalk between the nucleus and mitochondria.Thioredoxin-2 (TRX-2) is an essential gene regulating mitochondria-dependent apoptosisSptrx-2, a fusion protein composed of one thioredoxin and three tandemly repeated NDP-kinase domains is expressed in human testis germ cells.Regulatory roles of thioredoxin in oxidative stress-induced cellular responses.The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice.Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space.Mitochondrial peroxiredoxin III is a potential target for cancer therapyMitochondrial thiols in the regulation of cell death pathways.Two subpopulations of mitochondria in the aging rat heart display heterogenous levels of oxidative stress.Crystal structures of oxidized and reduced forms of human mitochondrial thioredoxin 2.In vitro susceptibility of thioredoxins and glutathione to redox modification and aging-related changes in skeletal muscle.Exercise training induces a cardioprotective phenotype and alterations in cardiac subsarcolemmal and intermyofibrillar mitochondrial proteins.Alterations of cellular redox state during NNK-induced malignant transformation and resistance to radiation.Alternative start sites in the Saccharomyces cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductaseMitochondrial energy metabolism and redox signaling in brain aging and neurodegenerationThe energy-redox axis in aging and age-related neurodegeneration.The role of peroxiredoxins in cancer.The functional role of peroxiredoxin 3 in reactive oxygen species, apoptosis, and chemoresistance of cancer cells.Energy metabolism and inflammation in brain aging and Alzheimer's disease.The expression and activity of thioredoxin reductase 1 splice variants v1 and v2 regulate the expression of genes associated with differentiation and adhesionInteraction of mitochondrial thioredoxin with glucocorticoid receptor and NF-kappaB modulates glucocorticoid receptor and NF-kappaB signalling in HEK-293 cells.Overexpression of thioredoxin reductase 1 inhibits migration of HEK-293 cells.Overexpression of enzymatically active human cytosolic and mitochondrial thioredoxin reductase in HEK-293 cells. Effect on cell growth and differentiation.Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity.The thioredoxin system in aging muscle: key role of mitochondrial thioredoxin reductase in the protective effects of caloric restriction?Mitochondrial protection by the thioredoxin-2 and glutathione systems in an in vitro endothelial model of sepsis.Loss of Trx-2 enhances oxidative stress-dependent phenotypes in Drosophila.Mutational analysis of human thioredoxin reductase 1. Effects on p53-mediated gene expression and interferon and retinoic acid-induced cell death.Alternative mRNAs arising from trans-splicing code for mitochondrial and cytosolic variants of Echinococcus granulosus thioredoxin Glutathione reductase.A putative glutathione peroxidase of Drosophila encodes a thioredoxin peroxidase that provides resistance against oxidative stress but fails to complement a lack of catalase activity.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
name
The mitochondrial thioredoxin system.
@ast
The mitochondrial thioredoxin system.
@en
The mitochondrial thioredoxin system.
@nl
type
label
The mitochondrial thioredoxin system.
@ast
The mitochondrial thioredoxin system.
@en
The mitochondrial thioredoxin system.
@nl
prefLabel
The mitochondrial thioredoxin system.
@ast
The mitochondrial thioredoxin system.
@en
The mitochondrial thioredoxin system.
@nl
P2093
P356
P1476
The mitochondrial thioredoxin system.
@en
P2093
Damdimopoulos AE
Miranda-Vizuete A
P304
P356
10.1089/ARS.2000.2.4-801
P577
2000-01-01T00:00:00Z