Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase
Open accessAbstract
Significance: Cellular powerhouses called mitochondria generate fuel known as adenosine triphosphate, or ATP, to sustain complex life. The capacity of mitochondria to do so depends on a supply of energy from oxidation of energy-rich compounds in foodstuffs to generate a chemical potential difference for hydrogen ions, called the proton motive force (pmf), across the inner mitochondrial membrane. Disruption of this membrane dissipates the pmf, and the cells die for lack of fuel. This event happens, for example, when the concentration of calcium ions inside human mitochondria is increased. The mitochondria respond by opening a pore, water enters, and the mitochondria swell and burst. The molecular identity of the pore is disputed, and we have disproved one proposal.
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.
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?
Very recent findings seem to exclude possibility that F1FO ATPase constitutes pore-forming component of PTPC.
“However, very recent findings seem to exclude the possibility that the F1FO ATPase constitutes the pore-forming component of the PTPC [402–405].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [403]
Mitochondria from human cells lacking all genes coding for c subunit of F1FO ATP synthase retain ability to undergo MPT in response to Ca2+ overload.
“Second, mitochondria from human cells lacking all the genes coding for the c subunit of the F1FO ATP synthase, i.e., ATP synthase, H+ transporting, mitochondrial Fo complex subunit C1 (subunit 9; ATP5G1), subunit C2 (subunit 9; ATP5G2), and subunit C3 (subunit 9; ATP5G3), reportedly retain the ability to undergo MPT in response to Ca2+ overload [403].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [403]
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
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works
Genome engineering using the CRISPR-Cas9 system
Ran, F. A., Hsu, P. D., Wright, J., Agarwala, V., Scott, D. A., & Zhang, F. (2013) · Nature Protocols · doi:10.1038/nprot.2013.143 · Cited by 11,133 · see citing works
New Colorimetric Cytotoxicity Assay for Anticancer-Drug Screening
Skehan, P., Storeng, R., Scudiero, D. A., Monks, A. P., McMahon, J., Vistica, D. T., Warren, J. T., Bokesch, H. R., Kenney, S., & Boyd, M. R. (1990) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/82.13.1107 · Cited by 9,801 · see citing works
The Perseus computational platform for comprehensive analysis of (prote)omics data
Tyanova, S., Temu, T., Sinitcyn, P. G., Carlson, A., Hein, M. Y., Geiger, T., Mann, M., & Cox, J. (2016) · Nature Methods · doi:10.1038/nmeth.3901 · Cited by 7,977 · see citing works
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574 · see citing works
Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A., Olsen, J. V., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr101065j · Cited by 5,349 · see citing works
Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
Abrahams, J. P., Leslie, A. G. W., Lutter, R., & Walker, J. E. (1994) · Nature · doi:10.1038/370621a0 · Cited by 3,004 · see citing works
Self-citationThe mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway
Lieber, M. R. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.093131 · Cited by 2,882 · see citing works
The mitochondrial permeability transition
Zoratti, M., & Szabó, I. (1995) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(95)00003-a · Cited by 2,395 · see citing works
Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., & Mann, M. (1996) · Nature · doi:10.1038/379466a0 · Cited by 1,674 · see citing works
Ebola virus entry requires the cholesterol transporter Niemann–Pick C1
Carette, J. E., Raaben, M., Wong, A., Herbert, A. S., Obernosterer, G., Mulherkar, N., Kuehne, A. I., Kranzusch, P. J., Griffin, A. M., Ruthel, G. T., et al. (2011) · Nature · doi:10.1038/nature10348 · Cited by 1,309 · see citing works
The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086 · see citing works
Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., & Molkentin, J. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1575 · Cited by 971 · see citing works
Dimers 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
Crompton, M., Ellinger, H., & COSTI, A. (1988) · PubMed Central · Cited by 841 · see citing works
The Ca2+-induced membrane transition in mitochondria
Haworth, R. A., & Hunter, D. R. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90372-2 · Cited by 793 · see citing works
Quantitative, High-Resolution Proteomics for Data-Driven Systems Biology
Cox, J., & Mann, M. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061308-093216 · Cited by 685 · see citing works
Petronilli, V., Miotto, G., Canton, M., Brini, M., Colonna, R., Bernardi, P., & Lisa, F. D. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77239-5 · Cited by 677 · see citing works
Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
Strauss, M., Hofhaus, G., Schröder, R. R., & Kühlbrandt, W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.35 · Cited by 677 · see citing works
The ATP synthase: the understood, the uncertain and the unknown
Walker, J. E. (2013) · Biochemical Society Transactions · doi:10.1042/bst20110773 · Cited by 614 · see citing works
Self-citationAlavian, 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
Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
Watt, I. N., Montgomery, M. G., Runswick, M. J., Leslie, A. G. W., & Walker, J. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011099107 · Cited by 513 · see citing works
Self-citationRasola, A., & Bernardi, P. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0723-y · Cited by 507 · see citing works
Disassembly and Reassembly of the Yeast Vacuolar H+-ATPase in Vivo
Kane, P. M. (1995) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46944-4 · Cited by 462 · see citing works
Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition
Bonora, M., Bononi, A., Marchi, E. D., Giorgi, C., Lebiedzińska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., et al. (2013) · Cell Cycle · doi:10.4161/cc.23599 · Cited by 454 · see citing works
Bcl-2 potentiates the maximal calcium uptake capacity of neural cell mitochondria.
Murphy, A. N., Bredesen, D. E., Cortopassi, G. A., Wang, E., & Fiskum, G. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9893 · Cited by 403 · see citing works
Mitochondrial ATP synthase subunit c storage in the ceroid‐lipofuscinoses (Batten disease)
Palmer, D. N., Fearnley, I. M., Walker, J. E., Hall, N. A., Lake, B. D., Wolfe, L. S., Haltia, M., Martinus, R. D., & Jolly, R. D. (1992) · American Journal of Medical Genetics · doi:10.1002/ajmg.1320420428 · Cited by 360 · see citing works
Self-citationRegulation of Plasma Membrane V-ATPase Activity by Dissociation of Peripheral Subunits
Sumner, J.-P., Dow, J. A. T., Earley, F. G. P., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5649 · Cited by 335 · see citing works
Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
Zhou, A., Rohou, A. L., Schep, D. G., Bason, J. V., Montgomery, M. G., Walker, J. E., Grigorieff, N., & Rubinstein, J. L. (2015) · eLife · doi:10.7554/elife.10180 · Cited by 298 · see citing works
Self-citationHahn, A. S., Parey, K., Bublitz, M., Mills, D. J., Zickermann, V., Vonck, J., Kühlbrandt, W., & Meier, T. W. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.037 · Cited by 272 · see citing works
Physiologic Functions of Cyclophilin D and the Mitochondrial Permeability Transition Pore
Elrod, J. W., & Molkentin, J. D. (2013) · Circulation Journal · doi:10.1253/circj.cj-13-0321 · Cited by 266 · see citing works
Megabase-scale deletion using CRISPR/Cas9 to generate a fully haploid human cell linePreprint
Essletzbichler, P., Konopka, T., Santoro, F., Chen, D., Gapp, B. V., Královics, R., Brummelkamp, T. R., Nijman, S. M. B., & Bürckstümmer, T. (2014) · Genome Research · doi:10.1101/gr.177220.114 · Cited by 266 · see citing works
Griffiths, E. J., & Halestrap, A. P. (1991) · Biochemical Journal · doi:10.1042/bj2740611 · Cited by 220 · see citing works
How the regulatory protein, IF 1 , inhibits F 1 -ATPase from bovine mitochondria
Gledhill, J. R., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707326104 · Cited by 205 · see citing works
Self-citationIdentification of the subunits of F1F0-ATPase from bovine heart mitochondria
Walker, J. E., Lutter, R., Dupuis, A., & Runswick, M. J. (1991) · Biochemistry · doi:10.1021/bi00236a007 · Cited by 193 · see citing works
Self-citationDudkina, N. V., Heinemeyer, J., Keegstra, W., Boekema, E. J., & Braun, H. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.09.065 · Cited by 193 · see citing works
On the structure of the stator of the mitochondrial ATP synthase
Dickson, V. K., Silvester, J. A., Fearnley, I. M., Leslie, A. G. W., & Walker, J. E. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601177 · Cited by 187 · see citing works
Self-citationThe structure of the membrane extrinsic region of bovine ATP synthase
Rees, D. M., Leslie, A. G. W., & Walker, J. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910365106 · Cited by 177 · see citing works
Self-citationCollinson, I. R., Runswick, M. J., Buchanan, S. K., Fearnley, I. M., Skehel, M. J., van Raaij, M. J., Griffiths, D. E., & Walker, J. E. (1994) · Biochemistry · doi:10.1021/bi00191a026 · Cited by 167 · see citing works
Self-citationCarraro, M., Giorgio, V., Šileikytė, J., Sartori, G., Forte, M. A., Lippe, G., Zoratti, M., Szabó, I., & Bernardi, P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.c114.559633 · Cited by 160 · see citing works
Two overlapping genes in bovine mitochondrial DNA encode membrane components of ATP synthase.
Fearnley, I. M., & Walker, J. E. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04456.x · Cited by 158 · see citing works
Self-citationMorales‐Ríos, E., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517542112 · Cited by 142 · see citing works
Self-citationSchmidt, C., Zhou, M., Marriott, H., Morgner, N., Politis, A., & Robinson, C. V. (2013) · Nature Communications · doi:10.1038/ncomms2985 · Cited by 136 · see citing works
Duncan, A. L., Robinson, A. J., & Walker, J. E. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608396113 · Cited by 129 · see citing works
Self-citationATP Synthase from Bovine Heart Mitochondria
Collinson, I. R., van Raaij, M. J., Runswick, M. J., Fearnley, I. M., Skehel, M. J., Orriss, G. L., Miroux, B., & Walker, J. E. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1591 · Cited by 114 · see citing works
Self-citationIdentification of Two Proteins Associated with Mammalian ATP Synthase
Meyer, B., Wittig, I., Trifilieff, É., Karas, M., & Schägger, H. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700097-mcp200 · Cited by 112 · see citing works
Assembly and oligomerization of human ATP synthase lacking mitochondrial subunits a and A6L
Wittig, I., Meyer, B., Heide, H., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.021 · Cited by 105 · see citing works
Azarashvili, T., Odinokova, I. V., Bakunts, A. G., Ternovsky, V. I., Krestinina, O. V., Tyynelä, J., & Saris, N.-E. L. (2013) · Cell Calcium · doi:10.1016/j.ceca.2013.12.002 · Cited by 104 · see citing works
Abramov, A. Y. (2003) · Cell Calcium · doi:10.1016/s0143-4160(02)00203-8 · Cited by 104 · see citing works
NDUFAF7 Methylates Arginine 85 in the NDUFS2 Subunit of Human Complex I
Rhein, V. F., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.518803 · Cited by 100 · see citing works
Self-citationGlobal profiling of protease cleavage sites by chemoselective labeling of protein N-termini
Xu, G., Shin, S. B. Y., & Jaffrey, S. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908958106 · Cited by 99 · see citing works
He, J., Cooper, H. M., Reyes, A., Re, M. D., Kazak, L., Wood, S. R., Mao, C. C., Fearnley, I. M., Walker, J. E., & Holt, I. J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks257 · Cited by 89 · see citing works
Self-citationN‐terminome analysis of the human mitochondrial proteome
Jácome, A. S. V., Rabilloud, T., Schaeffer‐Reiss, C., Rompais, M., Ayoub, D., Lane, L., Bairoch, A., DORSSELAER, A. V., & Carapito, C. (2015) · PROTEOMICS · doi:10.1002/pmic.201400617 · Cited by 74 · see citing works
Sequences of members of the human gene family for the c subunit of mitochondrial ATP synthase
Dyer, M. R., & Walker, J. E. (1993) · Biochemical Journal · doi:10.1042/bj2930051 · Cited by 70 · see citing works
Self-citationEzaki, J., Takeda‐Ezaki, M., & Kominami, E. (2000) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022781 · Cited by 69 · see citing works
Vinothkumar, K. R., Montgomery, M. G., Liu, S., & Walker, J. E. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615902113 · Cited by 61 · see citing works
Self-citationThapsigargin directly induces the mitochondrial permeability transition
Kôrge, P., & Weiss, J. N. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00724.x · Cited by 59 · see citing works
Induction of the permeability transition pore in cells depleted of mitochondrial DNA
Masgras, I., Rasola, A., & Bernardi, P. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.02.022 · Cited by 57 · see citing works
How release of phosphate from mammalian F 1 -ATPase generates a rotary substep
Bason, J. V., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1506465112 · Cited by 55 · see citing works
Self-citationAssociation of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria
Chen, R., Runswick, M. J., Carroll, J., Fearnley, I. M., & Walker, J. E. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.05.079 · Cited by 53 · see citing works
Self-citationDissociation of NAD(P)+-stimulated mitochondrial Ca2+ efflux from swelling and membrane damage
Vercesi, A. E. (1984) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(84)90523-x · Cited by 51 · see citing works
Sequence Analysis and Mapping of a Novel Human Mitochondrial ATP Synthase Subunit 9 cDNA (ATP5G3)
Yan, W., Lerner, T. J., Haines, J. L., et al. (1994) · Genomics · doi:10.1006/geno.1994.1631 · Cited by 50 · see citing works
Collinson, I. R., VANRAAIJ, M., Runswick, M. J., et al. (1994) · Journal of Molecular Biology · doi:10.1016/s0022-2836(84)71591-9 · Cited by 49 · see citing works
Phospholipids Occupy the Internal Lumen of the c Ring of the ATP Synthase ofEscherichia coli
Oberfeld, B., Brunner, J., & Dimroth, P. (2006) · Biochemistry · doi:10.1021/bi052304+ · Cited by 44 · see citing works
Lee, J., Ding, S., Walpole, T. B., Holding, A. N., Montgomery, M. G., Fearnley, I. M., & Walker, J. E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645283 · Cited by 43 · see citing works
Self-citationWoollacott, A. J., & Simpson, P. B. (2001) · SLAS DISCOVERY · doi:10.1177/108705710100600607 · Cited by 32 · see citing works
Collinson, I. R., Fearnley, I. M., Skehel, M. J., et al. (1994) · Biochemical Journal · doi:10.1042/bj3030639 · Cited by 31 · see citing works
Self-citationWalpole, T. B., Palmer, D. N., Jiang, H., Ding, S., Fearnley, I. M., & Walker, J. E. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.047456 · Cited by 27 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- Gledhill JR, Montgomery MG, Leslie AGW, Walker JE (2007) How the regulatory protein, IF1, inhibits F1-ATPase from bovine mitochondria. Proc Natl Acad Sci USA 104(40):15671-15676.
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · 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
He, J., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711201114 · Cited by 182 · see citing works
Self-citationBriston, T., Roberts, M., Lewis, S., Powney, B., M. Staddon, J., Szabadkai, G., & Duchen, M. R. (2017) · Scientific Reports · doi:10.1038/s41598-017-10673-8 · Cited by 152 · see citing works
Mitochondrial calcium cycling in neuronal function and neurodegeneration
Walters, G. C., & Usachev, Y. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094356 · Cited by 105 · see citing works
A 20/20 view of ANT function in mitochondrial biology and necrotic cell death
Bround, M. J., Bers, D. M., & Molkentin, J. D. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.05.012 · Cited by 83 · see citing works
Carraro, M., Carrer, A., Urbani, A., & Bernardi, P. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.05.014 · Cited by 71 · see citing works
Dynamics of the mitochondrial permeability transition pore: Transient and permanent opening events
Boyman, L., Coleman, A. K., Zhao, G., Wescott, A. P., Joca, H. C., Greiser, B. M., Karbowski, M., Ward, C. W., & Lederer, W. J. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.03.016 · Cited by 68 · see citing works
Carroll, J., He, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2100558118 · Cited by 46 · see citing works
Self-citationPost-translational modifications of the mitochondrial F 1 F O -ATPase
Nesci, S., Trombetti, F., Ventrella, V., & Pagliarani, A. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.08.007 · Cited by 21 · see citing works
Baines, C. P., & Gutiérrez-Aguilar, M. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148249 · Cited by 7 · see citing works
- Authors
- He, J., Ford, H. C., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Walker, John E.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-03-13
- Volume
- 114
- Issue
- 13
- Pages
- 3409-3414
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5380099
- OpenAlex
- W2596115537
- Cited by
- 251
- References
- 68
- Citations by year
- 2026: 10 · 2025: 11 · 2024: 13 · 2023: 22 · 2022: 15 · 2021: 33 · 2020: 47 · 2019: 36 · 2018: 41 · 2017: 23
- FWCI
- 16.41
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Apollo (University of Cambridge) (submittedVersion)
- Apollo
- Funders
- Medical Research Council (MC_U1065663150, MR/M009858/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitochondrial permeability transition, mitochondrial membrane permeability, proton motive force, mitochondrial swelling, mitochondrial calcium, ATP production, mitochondrial membrane potential
- MeSH terms
- Adenosine Triphosphate, Biological Transport, Humans, Isoenzymes, Mitochondria, Permeability, Mitochondrial Proton-Translocating ATPases
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
