G
Giuseppe Rotilio
Researcher at University of Rome Tor Vergata
Publications - 292
Citations - 15041
Giuseppe Rotilio is an academic researcher from University of Rome Tor Vergata. The author has contributed to research in topics: Superoxide dismutase & Copper. The author has an hindex of 62, co-authored 292 publications receiving 14424 citations. Previous affiliations of Giuseppe Rotilio include University of Udine & University of Messina.
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Aspects of the structure, function, and applications of superoxide dismutase
TL;DR: After consideration of the question of superoxide toxicity and superoxide pathology, several areas in which SOD has been investigated or used as a tool in a biochemical, pharmacological, or clinical context are discussed.
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Reduction and inactivation of superoxide dismutase by hydrogen peroxide
Robert C. Bray,Stephen A. Cockle,E. Martin Fielden,Peter B. Roberts,Giuseppe Rotilio,Lilia Calabrese +5 more
TL;DR: Reactions of H( 2)O(2) with superoxide dismutase were studied by e.p.r. (electron paramagnetic resonance) spectroscopy and other methods and it is suggested that this histidine is close to the metal in the native enzyme and essential for its enzymic activity.
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Cell signalling and the glutathione redox system.
TL;DR: Recent knowledge on the role played by several redox modulators in inducing signalling events that finally regulate cell cycle progression is summarised.
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Rescue of cells from apoptosis by inhibition of active GSH extrusion
Lina Ghibelli,C. Fanelli,Giuseppe Rotilio,E. Lafavia,Simona Coppola,C. Colussi,Patrizia Civitareale,M.R. Ciriolo +7 more
TL;DR: Evidence indicates that extrusion of reduced glutathione precedes and is responsible for the irreversible morphofunctional changes of apoptosis, probably by altering the intracellular redox state without intervention of reactive oxygen species, thus giving a rationale for the development of redox‐dependent apoptosis under anaerobic conditions.
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The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis
E. Martin Fielden,Peter B. Roberts,Robert C. Bray,David J. Lowe,Gillian N. Mautner,Giuseppe Rotilio,Lilia Calabrese +6 more
TL;DR: Pre-steady-state rates of reduction and reoxidation of copper in the enzyme are consistent with these processes being rate-limiting in enzyme turnover, and it is suggested that the results may be best interpreted in terms of an allosteric type of mechanism, with two initially indistinguishable copper atoms in the enzymes.