Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress.

By P. Klatt, S. Lamas. European Journal of Biochemistry, 2000

762 citations recorded by the source corpus.

Subfields: Biochemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/03e71404af11a477aa81de4b9ed5a1eac626474d

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Citations in the corpus

Glutathione Is a Key Player in Metal-Induced Oxidative Stress Defenses (2012, background): “A second mechanism is glutathionylation of regulatory proteins with direct conjugation of GSH to target cysteine residues, another function of GRx [187].”
Advances in Photosynthesis and Respiration: Focus on Plant Respiration (2005, background): “…in the literature of how such alteration of function could occur include the oxidation of specific reactive cysteine residues in proteins (Zheng et al., 1998), modification of particular protein-protein interactions (Saitoh et al., 1998) and protein S-glutathiolation (Klatt and Lamas, 2000).”
Metabolic endophenotype and related genotypes are associated with oxidative stress in children with autism (2006, background): “…range of functions that include nitrogen and oxygen free radical scavenger [Dickinson et al., 2003], protein redox status and enzyme activity [Klatt and Lamas, 2000], cell membrane integrity and signal transduction [Dickinson and Forman, 2002; Sagristá et al., 2002], transcription factor…”
Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System (2004, positive): “Furthermore, these types of posttranslational modification are involved in the regulation of specific transcriptional events vital to the adaptation seen in cells during oxidative stress (53).”
Free radicals and antioxidants in normal physiological functions and human disease. (2007, background): “Overproduction of reactive nitrogen species is called nitrosative stress (Klatt & Lamas, 2000; Ridnour et al., 2004).”
Oxidative stress, mitochondrial dysfunction and neurodegenerative diseases; a mechanistic insight. (2015, background): “Overproduction of reactive nitrogen species is called nitrosative stress [27,28].”
Radical-free biology of oxidative stress. (2008, background): “5a) Several proteins are regulated by GS-ylation, and many others undergo GS-ylation under oxidative stress conditions (44, 93).”
Endothelial cell superoxide generation: regulation and relevance for cardiovascular pathophysiology. (2004, background): “Alternatively, the reversible covalent addition of GSH to cysteine residues (or S-glutathiolation) may be involved in activating tyrosine kinases (79).”
Biochemistry of Free Radicals and Antioxidants (2010, neutral): “Overproduction of reactive nitrogen species is called nitrosative stress [22].”