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2005, Methods in enzymology, ISBN 0121828069, Volume 401., xxxvii, 560, [6]
Book
Free Radical Biology and Medicine, ISSN 0891-5849, 05/2016, Volume 94, pp. 55 - 65
Glutathione is an abundant, low-molecular-weight tripeptide whose biological importance is dependent upon its redox-active free sulphydryl moiety. Its role as... 
Mitochondria | Yeast | Thioredoxin | Glutathione reductase | Glutathione | OXIDATIVE STRESS | PROTECTION | ANCILLARY ROLE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ATYPICAL 2-CYS PEROXIREDOXIN | REDOX REGULATION | ENDOCRINOLOGY & METABOLISM | REDUCTASE | HYDROGEN-PEROXIDE | TARGET GENE | OXIDIZED GLUTATHIONE | INTERMEMBRANE SPACE | Cytoplasm - enzymology | Oxidation-Reduction | Glutathione - metabolism | Glutathione Reductase - metabolism | Saccharomyces cerevisiae - genetics | Antioxidants - metabolism | Mitochondria - metabolism | Glutathione Reductase - genetics | Saccharomyces cerevisiae - metabolism | Cytosol - enzymology | Glutathione - genetics | Sulfhydryl Compounds - metabolism | Thioredoxins - genetics | Mitochondria - genetics | Thioredoxins - metabolism | Iron-Sulfur Proteins - metabolism | Mutation | Glutathione Disulfide | Antioxidants | Thiols | roGFP2, redox-responsive fluorescent protein | GSH, reduced glutathione | CLS, chronological life span | OxD, degree of probe oxidation | dNTP, deoxynucleotide | Gpx, glutathione reductase 1, glutathione peroxidases | SD, standard deviation | ROS, reactive oxygen species | red, reduced | GSSG, oxidized glutathione | Cys, cysteine | ox, oxidized | OD600, optical density at 600 nm | Original Contribution | MetO, methionine sulphoxide | AMS, 4-acetamido-4′maleimidyldystilbene-2,2′-disulphonic acid | ONPG, o-nitrophenyl-β-D-galactopyranoside | Trx, thioredoxin | Prx, peroxiredoxin | Glr1, glutathione reductase 1 | Fe–S, iron–sulphur | ER, endoplasmic reticulum
Journal Article
Journal Article
Free Radical Research, ISSN 1029-2470, 2011, Volume 45, Issue 11-12, pp. 1245 - 1266
Abstract The intestinal tract, known for its capability for self-renew, represents the first barrier of defence between the organism and its luminal... 
cellular glutathione/glutathione disulfide (GSH/GSSG) redox state | redox control of intestinal cell phenotypic transitions | intestinal microbiota | intestinal disorders and tissue redox state | mucosal GSH and GSH-dependent enzymes | extracellular cysteine/cystine (Cys/CySS) redox state | intestinal NFκB redox signalling | GSH and intestinal oxidative stress | intestinal redox status and control of redox balance | Intestinal disorders and tissue redox state | Mucosal GSH and GSH-dependent enzymes | Cellular glutathione/glutathione disulfide (GSH/GSSG) redox state | Intestinal microbiota | Intestinal redox status and control of redox balance | Redox control of intestinal cell phenotypic transitions | Extracellular cysteine/cystine (Cys/CySS) redox state | Intestinal NFκB redox signalling | EXTRACELLULAR THIOL/DISULFIDE REDOX | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROPEROXIDE-INDUCED APOPTOSIS | RAT SMALL-INTESTINE | PEROXIDIZED LIPIDS | intestinal NF kappa B redox signalling | INFLAMMATORY-BOWEL-DISEASE | MOUSE SMALL INTESTINE | cellular glutathione/glutathione disulfi de (GSH/GSSG) redox state | GLUTATHIONE-S-TRANSFERASE | EPITHELIAL-CELL TYPES | NF-KAPPA-B | MITOCHONDRIAL GLUTATHIONE | Oxidation-Reduction | Oxidative Stress | Signal Transduction | Glutathione - metabolism | Cystine - metabolism | Humans | Thioredoxins - metabolism | Cysteine - metabolism | Glutathione Disulfide - metabolism | Intestines - metabolism | Intestines - enzymology | cellular glutathione | cystine (Cys | GSSG) redox state | intestinal NFκB redox signaling | CySS) redox state | extracellular cysteine | glutathione disulfide (GSH
Journal Article