Metal and redox modulation of cysteine protein function.
Niroshini M. Giles,Aaron B. Watts,Gregory I. Giles,Fiona H. Fry,Jennifer A. Littlechild,Claus Jacob +5 more
TLDR
The diversity of cysteine's multiple roles in vivo is equally as fascinating as it is promising for future biochemical and pharmacological research.About:
This article is published in Chemistry & Biology.The article was published on 2003-08-01 and is currently open access. It has received 407 citations till now. The article focuses on the topics: Non-innocent ligand & Cysteine.read more
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Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
TL;DR: The role of reactive oxygen species (ROS) as signaling molecules in starvation‐induced autophagy is described and a cysteine residue located near the HsAtg4 catalytic site is specified as a critical for this regulation.
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Protein posttranslational modifications: the chemistry of proteome diversifications.
TL;DR: An understanding of the scope and pattern of the many posttranslational modifications in eukaryotic cells provides insight into the function and dynamics of proteome compositions.
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Multifaceted roles of disulfide bonds. Peptides as therapeutics.
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Antioxidant activity of sulfur and selenium: a review of reactive oxygen species scavenging, glutathione peroxidase, and metal-binding antioxidant mechanisms.
TL;DR: The antioxidant activities of sulfur and selenium compounds are discussed, focusing on several antioxidant mechanisms, including ROS scavenging, glutathione peroxidase, and metal-binding antioxidant mechanisms.
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Accumulation of Free ADP-ribose from Mitochondria Mediates Oxidative Stress-induced Gating of TRPM2 Cation Channels
Anne-Laure Perraud,Christina L. Takanishi,Betty W. Shen,Shin Kang,Megan K. Smith,Carsten Schmitz,Heather Knowles,Dana Ferraris,Weixing Li,Jie Zhang,Barry L. Stoddard,Andrew M. Scharenberg +11 more
TL;DR: The data are most consistent with a model of oxidative and nitrosative stress-induced TRPM2 activation in which mitochondria are induced to produce free ADP-ribose and release it to the cytosol, where its subsequent accumulation inducesTRPM2 gating via interaction within a binding cleft in the C-terminal NUDT9-H domain of TR PM2.
References
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Journal ArticleDOI
Oxidants, oxidative stress and the biology of ageing.
Toren Finkel,Nikki J. Holbrook +1 more
TL;DR: Evidence that the appropriate and inappropriate production of oxidants, together with the ability of organisms to respond to oxidative stress, is intricately connected to ageing and life span is reviewed.
Journal ArticleDOI
Physiological functions of thioredoxin and thioredoxin reductase.
Elias S.J. Arnér,Arne Holmgren +1 more
TL;DR: All mammalian thioredoxin reduct enzyme isozymes are homologous to glutathione reductase and contain a conserved C-terminal elongation with a cysteine-selenocysteine sequence forming a redox-active selenenylsulfide/selenolthiol active site and are inhibited by goldthioglucose and other clinically used drugs.
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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.
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X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution.
TL;DR: A three-dimensional structure for the monomeric iron-containing hydrogenase (CpI) from Clostridium pasteurianum was determined, providing insights into the mechanism of biological hydrogen activation and has broader implications for [Fe-S] cluster structure and function in biological systems.
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Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
TL;DR: Results of these studies indicate that the most common pathway for the oxidation of simple aliphatic amino acids involves the hydroxyl radical-mediated abstraction of a hydrogen atom to form a carbon-centered radical at the alpha-position of the amino acid or amino acid residue in the polypeptide chain.