The DOI matches its Crossref record; 210 of the 215 references it cites were found in a registry or an index.
Molecular nature and regulation of the mitochondrial permeability transition pore(s), drug target(s) in cardioprotection
Abstract
The mitochondrial permeability transition, an established mechanism for heart diseases, is a long-standing mystery of mitochondrial biology and a prime drug target for cardioprotection. Several hypotheses about its molecular nature have been put forward over the years, and the prevailing view is that permeabilization of the inner mitochondrial membrane follows opening of a high-conductance channel, the permeability transition pore, which is also called mitochondrial megachannel or multiconductance channel. The permeability transition strictly requires matrix Ca 2+ and is favored by the matrix protein cyclophilin D, which mediates the inhibitory effects of cyclosporin A. Here we provide a review of the field, with specific emphasis on the possible role of the adenine nucleotide translocator and of the F-ATP synthase in channel formation, and on currently available small molecule inhibitors. While the possible mechanisms through which the adenine nucleotide translocator and the F-ATP synthase might form high-conductance channels remain unknown, reconstitution experiments and site-directed mutagenesis combined to electrophysiology have provided important clues. The hypothesis that more than one protein may act as a permeability transition pore provides a reasonable explanation for current controversies in the field, and holds great promise for the solution of the mystery of the permeability transition.
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“The inescapable conclusion from these studies is that some combination of these proteins is necessary to fully exhibit the properties of mPTP [1,18,20,21].”
From The mitochondrial permeability transition: Nexus of aging, disease and longevity (2021) · cites this paper as [1]
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Items 201–210 of 210
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Channel formation by F-ATP synthase and the permeability transition pore: an update
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Genetic manipulation of SPG7 or NipSnap2 does not affect mitochondrial permeability transition
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Fondation Leducq Transatlantic Network of Excellence Targeting Mitochondria to Treat Heart Disease
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5 of the 215 references couldn’t be matched to a known paper.
Research works printed but not linked: 4
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Bernardi, P., Gerle, C., Halestrap, A. P., Jonas, E. A., Karch, J. M., Mnatsakanyan, N., Pavlov, E. V., Sheu, S., & Soukas, A. A. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01187-0 · Cited by 504
Self-citationMitochondrial pores at the crossroad between cell death and inflammatory signaling
Flores‐Romero, H., Dadsena, S., & García‐Sáez, A. J. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.021 · Cited by 131
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Ca2+ handling at the mitochondria-ER contact sites in neurodegeneration
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The mitochondrial permeability transition: Nexus of aging, disease and longevity
Rottenberg, H., & Hoek, J. B. (2021) · Cells · doi:10.3390/cells10010079 · Cited by 94
“5 nS) that is activated by calcium, oxidative stress and membrane depolarization [1,2].”
BackgroundInfluential
Metadata
- Authors
- Carraro, M., Carrer, A., Urbani, A., & Bernardi, P.
- Affiliations
- University of Padua (IT)
- Corresponding author
- Bernardi, Paolo
- Venue
- Journal of Molecular and Cellular Cardiology
- Publisher
- Elsevier BV
- Published
- 2020-07
- Volume
- 144
- Pages
- 76-86
- ISSN
- 0022-2828 (ISSN-L)
- OpenAlex
- W3028471616
- Cited by
- 71
- References
- 215
- Citations by year
- 2026: 4 · 2025: 10 · 2024: 3 · 2023: 8 · 2022: 11 · 2021: 20 · 2020: 15
- FWCI
- 4.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular and Cellular Cardiology (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- Fondazione Telethon
- Ministero dell’Istruzione, dell’Università e della Ricerca
- Fondation Leducq
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- mitochondrial permeability transition, mitochondrial permeability transition pore, cardioprotection, cyclophilin D, cyclosporine, adenine nucleotide translocase, F-ATP synthase, mitochondrial matrix calcium, small molecule inhibitors, heart disease
- MeSH terms
- Mitochondrial Permeability Transition Pore, Animals, Cardiotonic Agents, Mitochondria, Heart, Permeability, Protein Binding, Biomarkers, Mice, Knockout, Mitochondrial Proton-Translocating ATPases, Organic Anion Transporters, Mice, Protein Interaction Domains and Motifs, Protein Multimerization, Drug Discovery
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