V
Valentina Giorgio
Researcher at University of Padua
Publications - 71
Citations - 3179
Valentina Giorgio is an academic researcher from University of Padua. The author has contributed to research in topics: ATP synthase & Mitochondrion. The author has an hindex of 23, co-authored 48 publications receiving 2609 citations. Previous affiliations of Valentina Giorgio include University of Bologna & National Research Council.
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Journal ArticleDOI
Dimers of mitochondrial ATP synthase form the permeability transition pore
Valentina Giorgio,Sophia von Stockum,Manuela Antoniel,Astrid Fabbro,Federico Fogolari,Michael Forte,Gary D. Glick,Valeria Petronilli,Mario Zoratti,Ildikò Szabò,Giovanna Lippe,Paolo Bernardi +11 more
TL;DR: It is shown that CyPD binds the oligomycin sensitivity-conferring protein subunit of the enzyme at the same site as the ATP synthase inhibitor benzodiazepine 423 (Bz-423), which sensitizes the PTP to Ca2+.
Journal ArticleDOI
Cyclophilin D Modulates Mitochondrial F0F1-ATP Synthase by Interacting with the Lateral Stalk of the Complex
Valentina Giorgio,Elena Bisetto,Maria Eugenia Soriano,Federica Dabbeni-Sala,Emy Basso,Valeria Petronilli,Michael Forte,Paolo Bernardi,Giovanna Lippe +8 more
TL;DR: Blue native gel electrophoresis purification and immunoprecipitation of F0F1-ATP synthase from bovine heart mitochondria revealed that cyclophilin (CyP) D associates to the complex, demonstrating that CyPD association to the lateral stalk of ATP synthase modulates the activity of the complex.
Journal ArticleDOI
Cyclophilin D in Mitochondrial Pathophysiology
Valentina Giorgio,Maria Eugenia Soriano,Emy Basso,Elena Bisetto,Giovanna Lippe,Michael Forte,Paolo Bernardi +6 more
TL;DR: The best characterized functions of cyclophilin D in mitochondria are reviewed, i.e. regulation of the permeability transition pore, an inner membrane channel that plays an important role in the execution of cell death.
Journal ArticleDOI
Ca2+ binding to F-ATP synthase β subunit triggers the mitochondrial permeability transition
Valentina Giorgio,Victoria Burchell,Marco Schiavone,Claudio Bassot,Giovanni Minervini,Valeria Petronilli,Francesco Argenton,Michael Forte,Silvio C. E. Tosatto,Giovanna Lippe,Paolo Bernardi +10 more
TL;DR: The finding that T163S mutants of the β subunit confer resistance to Ca2+‐induced, PTP‐dependent death in cells and developing zebrafish embryos is a major advance in the molecular definition of the transition of F‐ATP synthase to a channel and of its role in cell death.
Journal ArticleDOI
Calcium and regulation of the mitochondrial permeability transition.
TL;DR: This review focuses on the hypothesis that the PTP forms from the F-ATP synthase and on the mechanisms through which Ca2+ can reversibly switch this energy-conserving nanomachine into an energy-dissipating device.