A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation.

By A. Delaunay, Delphine Pflieger, M. Barrault, J. Vinh, M. Tolédano. Cell, 2002

879 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/abb891e9fd8542e442db2b1e4739a99af7b8fd7d

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In Molecular Biology

Citations in the corpus

The Roles of Reactive Oxygen Metabolism in Drought: Not So Cut and Dried[1][C][W] (2014, background): “…H2O2 reduction to oxidation of a yeast activator protein1 transcription factor were described in yeast (Saccharomyces cerevisiae) several years ago (Delaunay et al., 2002), and a subsequent study reported that an Arabidopsis GPX can function in a similar manner to allow oxidation of components…”
Signaling Functions of Reactive Oxygen Species (2010, background): “Trx turns off the signaling pathway, by reducing both the sensor and the regulator (70).”
Hydrogen peroxide sensing, signaling and regulation of transcription factors (2014, background): “Gpx3/Orp1 becomes oxidized at Cys36 which forms a heterodimeric disulfide bond with Cys598 in Yap1 upon H2O2 exposure [256].”
ROS-dependent signal transduction (2014, background): “Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling.”
Two Enzymes in One: Two Yeast Peroxiredoxins Display Oxidative Stress-Dependent Switching from a Peroxidase to a Molecular Chaperone Function (2004, neutral): “exists in two forms that have two different functions (Delaunay et al., 2002).”
Stress response, cell death and signalling: the many faces of reactive oxygen species (2003, background): “In some cases, ROS oxidize target proteins directly, particularly peroxiredoxins and other peroxidases, but also including transcription factors (Aslund et al. 1999, Park et al. 2000, Delaunay et al. 2002, Goyer et al. 2002).”
Singlet oxygen and photo‐oxidative stress management in plants and algae (2005, background): “Interestingly, these cysteines are not directly oxidized by peroxide, but instead mediate interactions with Gpx3, a glutathione peroxidase that directly interacts with the redox-regulated domain to produce an intramolecular disulfide bond (Delaunay et al. 2002).”
Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway (2006, background): “It is unlikely that a disulfide bond is responsible for this modified form, although using a disulfide bond as a molecular switch is a very attractive model since disulfide linkage of Gpx3 and Yap1 has been used in yeast as a redox sensor (Delaunay et al., 2002).”
Reactive oxygen signalling: the latest news. (2004, background): “Perception of ROS in prokaryotes and fungi relies in part on two-component histidine kinase and thiol peroxidase systems [26].”