The mitochondrial permeability transition pore: Is it formed by the ATP synthase.; adenine nucleotide translocators or both?
Open accessThe claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Some combination of mitochondrial proteins (CypD, ANT, ATP synthase, VDAC, PiC, SPG-7) is necessary to fully exhibit the properties of mPTP.
“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 [21]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,120 · see citing works
Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280 · see citing works
Self-citationDimers of mitochondrial ATP synthase form the permeability transition pore
Giorgio, V., von Stockum, S., Antoniel, M., Fabbro, A., Fogolari, F., Forte, M. A., Glick, G. D., Petronilli, V., Zoratti, M., Szabó, I., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217823110 · Cited by 924 · see citing works
Alavian, K. N., Beutner, G., Lazrove, E., Sacchetti, S., Park, H., Licznerski, P., Li, H., Nabili, P., Hockensmith, K., Graham, M. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401591111 · Cited by 595 · see citing works
Giorgio, V., Bisetto, E., Soriano, M. E., Dabbeni‐Sala, F., Basso, E., Petronilli, V., Forte, M. A., Bernardi, P., & Lippe, G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.020115 · Cited by 306 · see citing works
He, J., Ford, H. C., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702357114 · Cited by 251 · see citing works
Inhibition of mitochondrial permeability transition by deletion of the ANT family and CypD
Karch, J., Bround, M. J., Khalil, H., Sargent, M. A., Latchman, N., Terada, N., Peixoto, P. M., & Molkentin, J. D. (2019) · Science Advances · doi:10.1126/sciadv.aaw4597 · Cited by 250 · see citing works
Modulation of the mitochondrial megachannel by divalent cations and protons.
Szabó, I., Bernardi, P., & Zoratti, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50677-9 · Cited by 241 · see citing works
Neginskaya, M. A., Solesio, M. E., Berezhnaya, E. V., Amodeo, G. F., Mnatsakanyan, N., Jonas, E. A., & Pavlov, E. V. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.033 · Cited by 187 · see citing works
Mitochondrial Permeability Transition: A Molecular Lesion with Multiple Drug Targets
Briston, T., Selwood, D. L., Szabadkai, G., & Duchen, M. R. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.11.004 · Cited by 185 · see citing works
Urbani, A., Giorgio, V., Carrer, A., Franchin, C., Arrigoni, G., Jiko, C., Abe, K., Maeda, S., Shinzawa‐Itoh, K., Bogers, J. F. M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12331-1 · Cited by 183 · see citing works
A mitochondrial megachannel resides in monomeric F1FO ATP synthase
Mnatsakanyan, N., Llaguno, M. C., Yang, Y., Yan, Y., Weber, J., Sigworth, F. J., & Jonas, E. A. (2019) · Nature Communications · doi:10.1038/s41467-019-13766-2 · Cited by 152 · see citing works
Carroll, J., He, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904005116 · Cited by 128 · see citing works
Baines, C. P., & Gutiérrez‐Aguilar, M. (2018) · Cell Calcium · doi:10.1016/j.ceca.2018.05.003 · Cited by 70 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
The mitochondrial permeability transition: Nexus of aging, disease and longevity
Rottenberg, H., & Hoek, J. B. (2021) · Cells · doi:10.3390/cells10010079 · Cited by 94 · see citing works
“Because experiments with ATP synthase and ANT provided the strongest evidence for participation in the mPTP channel, it was recently suggested that both ATP synthase and ANT are required for the formation of a fully functional mPTP channel, although the nature of this composite channel remains elusive [1,20,21].”
Background
- Authors
- Baines, C. P., & Gutiérrez-Aguilar, M.
- Affiliations
- University of Missouri (US)
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2020-10
- Volume
- 1861
- Issue
- 10
- Pages
- 148249
- ISSN
- 0005-2728 (ISSN-L)
- PMC
- PMC9121818
- OpenAlex
- W3036164356
- Cited by
- 7
- References
- 14
- Citations by year
- 2023: 1 · 2022: 3 · 2021: 1 · 2020: 2
- FWCI
- 0.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Dirección General de Asuntos del Personal Académico, Universidad Nacional Autónoma de México
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- mitochondrial permeability transition pore, ATP synthase, adenine nucleotide translocase, mitochondrial permeability transition, cell death, pore formation mechanism, mitochondrial membrane permeability
- MeSH terms
- Mitochondrial Permeability Transition Pore, Mitochondrial ADP, ATP Translocases, Kinetics, ATP Synthetase Complexes, Mitochondrial Membrane Transport Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
