Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis.
By M. Giorgio, E. Migliaccio, F. Orsini, Demis Paolucci, M. Moroni, C. Contursi, Giovanni Pelliccia, L. Luzi, S. Minucci, M. Marcaccio and 5 more. Cell, 2005
1,163 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/7634bea52f3394192ab4d688c721798e2e788030
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Citations in the corpus
- ROS and p53: a versatile partnership. (2008, background): “Confronted in the mitochondria with pro-apoptotic stimulation, p66shc oxidizes cytochrome c, producing H2O2, which promotes the opening of the mitochondrial permeability transition pore and triggers apoptosis [31].”
- Chemistry and biology of reactive oxygen species in signaling or stress responses (2011, background): “In addition, the Src homology and collagen homolog protein (p66shc) is an adaptor protein for receptor protein tyrosine kinase signaling but also has a redox signaling and stress role by catalyzing electron transfer from cytochrome c to reduce O 2 to [O 2 ] •− and H 2 O 2 (ref”
- Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release. (2014, background): “In mitochondria, this adapter molecule has been suggested to function as a redox enzyme possibly oxidizing cytochrome c and generating H2O2 in the amino-terminal portion of p66 shc containing sequence similar to that of certain redox enzymes (156).”
- Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases (2014, background): “Upon oxidative stress, p66Shc translocates to mitochondrial intermembrane space, where it associates with cytochromec, thus inducing ROS generation [65].”
- Signal transduction by reactive oxygen species (2011, background): “Although one-electron reactions predominate, two-electron reactions that allow the direct reduction of molecular oxygen to hydrogen peroxide do exist within the mitochondria (Giorgio et al., 2005).”
- Mitochondria-Ros Crosstalk in the Control of Cell Death and Aging (2011, background): “On the contrary, overexpression of p66shc causes alterations of mitochondrial Ca2+ responses (which is an early event of mitochondrial damage) and fragmentation of mitochondrial network [161], leading to cytochrome c release and apoptosis [162].”
- Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis (2008, background): “Intriguingly, upon phosphorylation by PKCb and peptidyl–prolyl cis/trans isomerase (Pin1) recognition, p66shc translocates to mitochondria (Pinton et al., 2007a) where it exerts its own oxidoreductase activity (Giorgio et al., 2005).”
- Reperfusion injury and reactive oxygen species: The evolution of a concept (2015, background): “There appear to be cytoplasmic, ER, and mitochondrial pools of inactive p66 [355,356].”