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Raffaele Colonna

Researcher at University of Padua

Publications -  50
Citations -  5755

Raffaele Colonna 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 28, co-authored 50 publications receiving 5612 citations. Previous affiliations of Raffaele Colonna include National Institutes of Health.

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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.
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The Voltage Sensor of the Mitochondrial Permeability Transition Pore Is Tuned by the Oxidation-Reduction State of Vicinal Thiols INCREASE OF THE GATING POTENTIAL BY OXIDANTS AND ITS REVERSAL BY REDUCING AGENTS*

TL;DR: It is concluded that the oxidation-reduction state of vicinal thiols in cysteinyl residues plays a critical role in tuning the voltage sensor of the transition pore, with an increase of gating potential as the couple is poised to a more oxidized state.
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Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations.

TL;DR: The PTP and the mitochondrial megachannel are the same molecular structures and the same factors affect both the process of pore induction and its open-closed orientation, which indicates that PTP induction is directly related to matrix pH.