Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and saccharomyces cerevisiae responses to oxidative stress.
By O. Carmel-Harel, G. Storz. Annual Review of Microbiology, 2000
727 citations recorded by the source corpus.
Subfields: Insect Science, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/adf9c9827ddcea15e6f3d922dadc23ec616b4dfb
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Citations in the corpus
- Antibacterial Activity of Ti₃C₂Tx MXene. (2016, methodology): “of glutathione by adsorption, or binding.(47) In this study glutathione was exposed to increasing”
- Stress Physiology of Lactic Acid Bacteria (2016, background): “as well as the thioredoxin systems is crucial (260).”
- Unravelling the biology of macrophage infection by gene expression profiling of intracellular Salmonella enterica (2002, background): “The inducible systems that protect against oxidative stress are either OxyR or SoxRS regulated and can be switched on by hydrogen peroxide and superoxide respectively (Carmel-Harel and Storz, 2000).”
- Antibacterial activity of graphite, graphite oxide, graphene oxide, and reduced graphene oxide: membrane and oxidative stress. (2011, methodology): “GSH has been used as an oxidative stress indicator in cells.(13,29,36) The Ellman's assay is able to quantify the concentration of thiol groups in GSH.”
- The extracytoplasmic function (ECF) sigma factors. (2002, background): “Together, these proteins allow reducing equivalents, in the form of NADPH, to be efficiently used to reduce oxidized thiols (Carmel-Harel and Storz, 2000).”
- Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System (2004, unknown): “Furthermore, Grx1 (as well as Trx2 and GR) has been shown to be regulated by the transcription factor OxyR, which is known to activate the expression of several antioxidant defensive genes in response to elevated levels of hydrogen peroxide (13).”