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Valeria Petronilli

Researcher at University of Padua

Publications -  95
Citations -  13479

Valeria Petronilli is an academic researcher from University of Padua. The author has contributed to research in topics: Mitochondrial permeability transition pore & Mitochondrion. The author has an hindex of 47, co-authored 95 publications receiving 12860 citations. Previous affiliations of Valeria Petronilli include Université de Namur.

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Dimers of mitochondrial ATP synthase form the permeability transition pore

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+.
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Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D

TL;DR: The experiments demonstrate that the PTP can form and open, that CyP-D represents the target for PTP inhibition by CsA, and that Cyp-D modulates the sensitivity of the P TP to Ca2+ but not its regulation by the proton electrochemical gradient, adenine nucleotides, and oxidative stress.
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The mitochondrial permeability transition

TL;DR: This review summarizes recent work on the regulation of the permeability transition pore, a cyclosporin A‐sensitive mitochondrial channel that may play a role in intracellular calcium homeostasis and in a variety of forms of cell death.
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Mitochondria and cell death. Mechanistic aspects and methodological issues.

TL;DR: This work tries to identify the mechanistic aspects of mitochondrial involvement in cell death as can be derived from current understanding of mitochondrial physiology, with special emphasis on the permeability transition and its consequences (like onset of swelling, cytochrome c release and respiratory inhibition).
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Transient and Long-Lasting Openings of the Mitochondrial Permeability Transition Pore Can Be Monitored Directly in Intact Cells by Changes in Mitochondrial Calcein Fluorescence

TL;DR: In hepatocytes and MH1C1 cells coloaded with Co2+ and calcein AM, treatment with MTP inducers caused a rapid, though limited, decrease in mitochondrial calce in fluorescence, which was significantly reduced by CsA, and MTP likely fluctuates rapidly between open and closed states in intact cells.