Journal ArticleDOI
Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple.
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TLDR
Estimates can be used to more fully understand the redox biochemistry that results from oxidative stress, which hopefully will provide a rationale and understanding of the cellular mechanisms associated with cell growth and development, signaling, and reductive or oxidative stress.About:
This article is published in Free Radical Biology and Medicine.The article was published on 2001-06-01. It has received 4274 citations till now. The article focuses on the topics: RoGFP & Redox.read more
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Xanthophyll cycle – a mechanism protecting plants against oxidative stress
TL;DR: Four, mainly hypothetical, mechanisms explaining the protective role of xanthophyll cycles in oxidative stress are presented, one of them is the direct quenching of overexcitation by products of the light phase of xAnthophyll cycle carotenoids in the process of photoprotection.
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Searching for a photocycle of the cryptochrome photoreceptors
TL;DR: The initial photochemistry of plant cryptochromes has been extensively investigated in recent years and it is hypothesized that cryptochrome photoexcitation involves a Trp-triad-dependent photoreduction, leading to conformational changes, signal propagation, and physiological responses.
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Redox regulation of human ogg1 activity in response to cellular oxidative stress
Anne Bravard,Anne Bravard,Monique Vacher,Monique Vacher,Barbara Gouget,Alexandre Coutant,Florence Hillairet de Boisferon,Florence Hillairet de Boisferon,Stéphanie Marsin,Stéphanie Marsin,Sylvie Chevillard,J. Pablo Radicella,J. Pablo Radicella +12 more
TL;DR: It is suggested that cadmium inhibits hOGG1 activity mainly by indirect oxidation of critical cysteine residues and that excretion of the metal from the cells leads to normalization of the redox cell status and restoration of an active hOGg1.
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Detection of Reactive Oxygen Species-sensitive Thiol Proteins by Redox Difference Gel Electrophoresis IMPLICATIONS FOR MITOCHONDRIAL REDOX SIGNALING
TL;DR: Thiol redox modification affected enzyme activity, suggesting that the reversible modification of enzyme activity by ROS from the respiratory chain may be an important and unexplored mode of mitochondrial redox signaling.
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Evidence for the Role of a Peroxidase Compound I-type Intermediate in the Oxidation of Glutathione, NADH, Ascorbate, and Dichlorofluorescin by Cytochrome c/H2O2: IMPLICATIONS FOR OXIDATIVE STRESS DURING APOPTOSIS *
TL;DR: The findings suggest the formation of a peroxidase compound I-type intermediate, in which one oxidizing equivalent is present as an oxoferryl heme species and the other as the protein tyrosyl radical previously identified.
References
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Induction of apoptotic program in cell-free extracts : requirement for datp and cytochrome c
TL;DR: Cells undergoing apoptosis in vivo showed increased release of cy tochrome c to their cytosol, suggesting that mitochondria may function in apoptosis by releasing cytochrome c.
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The Pecking Order of Free Radicals and Antioxidants: Lipid Peroxidation, α-Tocopherol, and Ascorbate
TL;DR: In this article, the authors used one-electron reduction potentials to predict a pecking order, or hierarchy, for free radical reactions, which is in agreement with experimentally observed free radical electron (hydrogen atom) transfer reactions.
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Oxidative stress as a mediator of apoptosis
Thomas M. Buttke,Paul Sandstrom +1 more
TL;DR: Thomas Buttke and Paul Sandstrom suggest that eukaryotic cells may benefit from this perilous existence by invoking oxidative stress as a common mediator of apoptosis.
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Antioxidant and Redox Regulation of Gene Transcription
Chandan K. Sen,Lester Packer +1 more
TL;DR: The efficacy of different antioxidants to favorably influence the molecular mechanisms implicated in human disease should be a critical determinant of its selection for clinical studies.
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Oxidized redox state of glutathione in the endoplasmic reticulum
TL;DR: Results suggest that the demonstrated preferential transport of GSSG compared to GSH into the ER lumen may contribute to this redox compartmentation.