Cited by 135Mitochondrial Function and PathologyCell death mechanisms and regulationAutophagy in Disease and Therapy

Physiopathology of the Permeability Transition Pore: Molecular Mechanisms in Human Pathology

Open access
Bonora, Massimo, Patergnani, Simone, Ramaccini, Daniela, Morciano, Giampaolo, Pedriali, Gaia, Kahsay, Asrat, Bouhamida, Esmaa, Giorgi, Carlotta +2 more·2020·Biomolecules

Abstract

Mitochondrial permeability transition (MPT) is the sudden loss in the permeability of the inner mitochondrial membrane (IMM) to low-molecular-weight solutes. Due to osmotic forces, MPT is paralleled by a massive influx of water into the mitochondrial matrix, eventually leading to the structural collapse of the organelle. Thus, MPT can initiate outer-mitochondrial-membrane permeabilization (MOMP), promoting the activation of the apoptotic caspase cascade and caspase-independent cell-death mechanisms. The induction of MPT is mostly dependent on mitochondrial reactive oxygen species (ROS) and Ca2+, but is also dependent on the metabolic stage of the affected cell and signaling events. Therefore, since its discovery in the late 1970s, the role of MPT in human pathology has been heavily investigated. Here, we summarize the most significant findings corroborating a role for MPT in the etiology of a spectrum of human diseases, including diseases characterized by acute or chronic loss of adult cells and those characterized by neoplastic initiation.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/biom10070998

Cites

22 of 22 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

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?

  • Glutamate-induced cell death is associated with mitochondrial dysfunction, Ca2+ accumulation, mitochondrial permeability transition pore opening, and functional collapse of mitochondria.

    “Glutamate-induced cell death is associated with mitochondrial dysfunction, associated with accumulation of Ca2+, activating mitochondrial permeability transition pore opening and causing functional collapse of mitochondria (for review, see Szabó and Zoratti, 1992; Bonora et al., 2020).”

    From Toxic Concentrations of Glutamate Induce Ferroptosis without Affecting Mitochondrial Respiration in Rodent Brain Slice Cultures (2026) · cites this paper as Bonora et al., 2020

    Section 1.1, “Mitochondrial Routes of Cell Death” (page not available), says pathological mitochondrial Ca2+ overload triggers permeability transition and pore opening, followed by collapse of mitochondrial potential and related activities that can lead to cell death. It does not connect this sequence specifically to glutamate-induced cell death. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

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

Flagged first, then by citations

Research works printed but not linked: 207

  1. [1]Dejean L.M. Martinez-Caballero S. Guo L. Hughes C. Teijido O. Ducret T. Ichas F. Korsmeyer S.J. Antonsson B. Jonas E.A. Oligomeric Bax is a component of the putative cytochrome c release channel MAC, mitochondrial apoptosis-induced channel Mol. Biol. Cell 2005 16 2424 2432 10.1091/mbc.e04-12-1111 15772159 PMC1087246 · DOI
  2. [2]Dejean L.M. Martinez-Caballero S. Manon S. Kinnally K.W. Regulation of the mitochondrial apoptosis-induced channel, MAC, by BCL-2 family proteins Biochim. Biophys. Acta 2006 1762 191 201 10.1016/j.bbadis.2005.07.002 16055309 · DOI
  3. [4]Kantrow S.P. Piantadosi C.A. Release of cytochrome c from liver mitochondria during permeability transition Biochem. Biophys. Res. Commun. 1997 232 669 671 10.1006/bbrc.1997.6353 9126333 · DOI
  4. [6]Bonora M. Pinton P. The mitochondrial permeability transition pore and cancer: Molecular mechanisms involved in cell death Front. Oncol. 2014 4 302 10.3389/fonc.2014.00302 25478322 PMC4235083 · DOI · Paper page
  5. [7]Giorgi C. Danese A. Missiroli S. Patergnani S. Pinton P. Calcium Dynamics as a Machine for Decoding Signals Trends Cell Biol. 2018 28 258 273 10.1016/j.tcb.2018.01.002 29409699 · DOI
  6. [8]Giorgi C. Marchi S. Pinton P. The machineries, regulation and cellular functions of mitochondrial calcium Nat. Rev. Mol. Cell Biol. 2018 19 713 730 10.1038/s41580-018-0052-8 30143745 · DOI · Paper page
  7. [11]Bonora M. Wieckowski M.R. Chinopoulos C. Kepp O. Kroemer G. Galluzzi L. Pinton P. Molecular mechanisms of cell death: Central implication of ATP synthase in mitochondrial permeability transition Oncogene 2015 34 1475 1486 10.1038/onc.2014.96 24727893 · DOI · Paper page
  8. [12]Schroers A. Kramer R. Wohlrab H. The reversible antiport-uniport conversion of the phosphate carrier from yeast mitochondria depends on the presence of a single cysteine J. Biol. Chem. 1997 272 10558 10564 10.1074/jbc.272.16.10558 9099701 · DOI
  9. [13]Petronilli V. Cola C. Bernardi P. Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore. II. The minimal requirements for pore induction underscore a key role for transmembrane electrical potential, matrix pH, and matrix Ca2+ J. Biol. Chem. 1993 268 1011 1016 7678245
  10. [14]Takeyama N. Matsuo N. Tanaka T. Oxidative damage to mitochondria is mediated by the Ca(2+)-dependent inner-membrane permeability transition Biochem. J. 1993 294 719 725 10.1042/bj2940719 7691056 PMC1134522 · DOI
  11. [15]Wieckowski M.R. Brdiczka D. Wojtczak L. Long-chain fatty acids promote opening of the reconstituted mitochondrial permeability transition pore FEBS Lett. 2000 484 61 64 10.1016/S0014-5793(00)02127-X 11068032 · DOI
  12. [16]Brenner C. Grimm S. The permeability transition pore complex in cancer cell death Oncogene 2006 25 4744 4756 10.1038/sj.onc.1209609 16892087 · DOI
  13. [17]Kowaltowski A.J. Castilho R.F. Vercesi A.E. Opening of the mitochondrial permeability transition pore by uncoupling or inorganic phosphate in the presence of Ca2+ is dependent on mitochondrial-generated reactive oxygen species FEBS Lett. 1996 378 150 152 10.1016/0014-5793(95)01449-7 8549822 · DOI
  14. [19]Baines C.P. Kaiser R.A. Sheiko T. Craigen W.J. Molkentin J.D. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death Nat. Cell Biol. 2007 9 550 555 10.1038/ncb1575 17417626 PMC2680246 · DOI · Paper page
  15. [21]Bonora M. Morganti C. Morciano G. Pedriali G. Lebiedzinska-Arciszewska M. Aquila G. Giorgi C. Rizzo P. Campo G. Ferrari R. Mitochondrial permeability transition involves dissociation of F1FO ATP synthase dimers and C-ring conformation EMBO Rep. 2017 18 1077 1089 10.15252/embr.201643602 28566520 PMC5494524 · DOI
  16. [22]Morciano G. Preti D. Pedriali G. Aquila G. Missiroli S. Fantinati A. Caroccia N. Pacifico S. Bonora M. Talarico A. Discovery of Novel 1,3,8-Triazaspiro[4.5]decane Derivatives That Target the c Subunit of F1/FO-Adenosine Triphosphate (ATP) Synthase for the Treatment of Reperfusion Damage in Myocardial Infarction J. Med. Chem. 2018 61 7131 7143 10.1021/acs.jmedchem.8b00278 30060655 · DOI
  17. [23]Giorgio V. von Stockum S. Antoniel M. Fabbro A. Fogolari F. Forte M. Glick G.D. Petronilli V. Zoratti M. Szabo I. Dimers of mitochondrial ATP synthase form the permeability transition pore Proc. Natl. Acad. Sci. USA 2013 110 5887 5892 10.1073/pnas.1217823110 23530243 PMC3625323 · DOI
  18. [24]Giorgio V. Burchell V. Schiavone M. Bassot C. Minervini G. Petronilli V. Argenton F. Forte M. Tosatto S. Lippe G. Ca(2+) binding to F-ATP synthase beta subunit triggers the mitochondrial permeability transition EMBO Rep. 2017 18 1065 1076 10.15252/embr.201643354 28507163 PMC5494526 · DOI
  19. [25]Antoniel M. Jones K. Antonucci S. Spolaore B. Fogolari F. Petronilli V. Giorgio V. Carraro M. Di Lisa F. Forte M. The unique histidine in OSCP subunit of F-ATP synthase mediates inhibition of the permeability transition pore by acidic pH EMBO Rep. 2018 19 257 268 10.15252/embr.201744705 29217657 PMC5797955 · DOI
  20. [26]Mnatsakanyan N. Llaguno M.C. Yang Y. Yan Y. Weber J. Sigworth F.J. Jonas E.A. A mitochondrial megachannel resides in monomeric F1FO ATP synthase Nat. Commun. 2019 10 5823 10.1038/s41467-019-13766-2 31862883 PMC6925261 · DOI
  21. [27]Urbani A. Giorgio V. Carrer A. Franchin C. Arrigoni G. Jiko C. Abe K. Maeda S. Shinzawa-Itoh K. Bogers J.F.M. Purified F-ATP synthase forms a Ca(2+)-dependent high-conductance channel matching the mitochondrial permeability transition pore Nat. Commun. 2019 10 4341 10.1038/s41467-019-12331-1 31554800 PMC6761146 · DOI
  22. [28]He J. Carroll J. Ding S. Fearnley I.M. Walker J.E. Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase Proc. Natl. Acad. Sci. USA 2017 114 9086 9091 10.1073/pnas.1711201114 28784775 PMC5576841 · DOI · Paper page
  23. [29]Carroll J. He J. Ding S. Fearnley I.M. Walker J.E. Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase Proc. Natl. Acad. Sci. USA 2019 116 12816 12821 10.1073/pnas.1904005116 31213546 PMC6601249 · DOI
  24. [30]Neginskaya M.A. Solesio M.E. Berezhnaya E.V. Amodeo G.F. Mnatsakanyan N. Jonas E.A. Pavlov E.V. ATP Synthase C-Subunit-Deficient Mitochondria Have a Small Cyclosporine A-Sensitive Channel, but Lack the Permeability Transition Pore Cell Rep. 2019 26 11 17 10.1016/j.celrep.2018.12.033 30605668 PMC6521848 · DOI
  25. [33]Li Y. Johnson N. Capano M. Edwards M. Crompton M. Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis Biochem. J. 2004 383 101 109 10.1042/BJ20040669 15233627 PMC1134048 · DOI
  26. [34]Zhang J. Han Y. Shi H. Chen J. Zhang X. Wang X. Zhou L. Liu J. Zhang J. Ji Z. Swine acute diarrhea syndrome coronavirus-induced apoptosis is caspase- and cyclophilin D- dependent Emerg. Microbes Infect. 2020 9 439 456 10.1080/22221751.2020.1722758 32090691 PMC7054944 · DOI
  27. [35]Garcia-Alvarado F. Govoni G. de Pascual R. Ruiz-Ruiz C. Munoz-Montero A. Gandia L. de Diego A.M.G. Garcia A.G. Otilonium and pinaverium trigger mitochondrial-mediated apoptosis in rat embryo cortical neurons in vitro Neurotoxicology 2019 70 99 111 10.1016/j.neuro.2018.11.003 30448301 · DOI
  28. [36]Lee Y.J. Lee C. Porcine deltacoronavirus induces caspase-dependent apoptosis through activation of the cytochrome c-mediated intrinsic mitochondrial pathway Virus Res. 2018 253 112 123 10.1016/j.virusres.2018.06.008 29940190 PMC7114866 · DOI
  29. [37]Wang H. Chen Y. Zhai N. Chen X. Gan F. Li H. Huang K. Ochratoxin A-Induced Apoptosis of IPEC-J2 Cells through ROS-Mediated Mitochondrial Permeability Transition Pore Opening Pathway J. Agric. Food. Chem. 2017 65 10630 10637 10.1021/acs.jafc.7b04434 29136370 · DOI
  30. [38]Naserzadeh P. Ansari Esfeh F. Kaviani M. Ashtari K. Kheirbakhsh R. Salimi A. Pourahmad J. Single-walled carbon nanotube, multi-walled carbon nanotube and Fe2O3 nanoparticles induced mitochondria mediated apoptosis in melanoma cells Cutan. Ocul. Toxicol. 2018 37 157 166 10.1080/15569527.2017.1363227 28768445 · DOI
  31. [39]Xie Z. Wang J. Liu M. Chen D. Qiu C. Sun K. CC-223 blocks mTORC1/C2 activation and inhibits human hepatocellular carcinoma cells in vitro and in vivo PLoS ONE 2017 12 e0173252 10.1371/journal.pone.0173252 28334043 PMC5363890 · DOI
  32. [40]Yang M. Wang B. Gao J. Zhang Y. Xu W. Tao L. Spinosad induces programmed cell death involves mitochondrial dysfunction and cytochrome C release in Spodoptera frugiperda Sf9 cells Chemosphere 2017 169 155 161 10.1016/j.chemosphere.2016.11.065 27870937 · DOI
  33. [41]Liu G. Zou H. Luo T. Long M. Bian J. Liu X. Gu J. Yuan Y. Song R. Wang Y. Caspase-Dependent and Caspase-Independent Pathways Are Involved in Cadmium-Induced Apoptosis in Primary Rat Proximal Tubular Cell Culture PLoS ONE 2016 11 e0166823 10.1371/journal.pone.0166823 27861627 PMC5115828 · DOI
  34. [42]Ottani F. Latini R. Staszewsky L. La Vecchia L. Locuratolo N. Sicuro M. Masson S. Barlera S. Milani V. Lombardi M. Cyclosporine A in Reperfused Myocardial Infarction: The Multicenter, Controlled, Open-Label CYCLE Trial J. Am. Coll. Cardiol. 2016 67 365 374 10.1016/j.jacc.2015.10.081 26821623 · DOI
  35. [43]Fakharnia F. Khodagholi F. Dargahi L. Ahmadiani A. Prevention of Cyclophilin D-Mediated mPTP Opening Using Cyclosporine-A Alleviates the Elevation of Necroptosis, Autophagy and Apoptosis-Related Markers Following Global Cerebral Ischemia-Reperfusion J. Mol. Neurosci. 2017 61 52 60 10.1007/s12031-016-0843-3 27664163 · DOI
  36. [44]Ou Z. Jiang T. Gao Q. Tian Y.Y. Zhou J.S. Wu L. Shi J.Q. Zhang Y.D. Mitochondrial-dependent mechanisms are involved in angiotensin II-induced apoptosis in dopaminergic neurons J. Renin. Angiotensin Aldosterone Syst. 2016 17 1470320316672349 10.1177/1470320316672349 27733642 PMC5843909 · DOI
  37. [45]Dong Y.Y. Zhuang Y.H. Cai W.J. Liu Y. Zou W.B. The mitochondrion interfering compound NPC-26 exerts potent anti-pancreatic cancer cell activity in vitro and in vivo Tumour Biol. 2016 37 15053 15063 10.1007/s13277-016-5403-5 27658776 · DOI
  38. [46]Chen Y. Li M. Li Z. Gao P. Zhou X. Zhang J. Bufalin induces apoptosis in the U2OS human osteosarcoma cell line via triggering the mitochondrial pathway Mol. Med. Rep. 2016 13 817 822 10.3892/mmr.2015.4583 26648158 · DOI
  39. [47]Borutaite V. Jekabsone A. Morkuniene R. Brown G.C. Inhibition of mitochondrial permeability transition prevents mitochondrial dysfunction, cytochrome c release and apoptosis induced by heart ischemia J. Mol. Cell. Cardiol. 2003 35 357 366 10.1016/S0022-2828(03)00005-1 12689815 · DOI
  40. [48]Precht T.A. Phelps R.A. Linseman D.A. Butts B.D. Le S.S. Laessig T.A. Bouchard R.J. Heidenreich K.A. The permeability transition pore triggers Bax translocation to mitochondria during neuronal apoptosis Cell Death Differ. 2005 12 255 265 10.1038/sj.cdd.4401552 15637643 · DOI
  41. [50]Narita M. Shimizu S. Ito T. Chittenden T. Lutz R.J. Matsuda H. Tsujimoto Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria Proc. Natl. Acad. Sci. USA 1998 95 14681 14686 10.1073/pnas.95.25.14681 9843949 PMC24509 · DOI
  42. [51]Scorrano L. Ashiya M. Buttle K. Weiler S. Oakes S.A. Mannella C.A. Korsmeyer S.J. A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis Dev. Cell 2002 2 55 67 10.1016/S1534-5807(01)00116-2 11782314 · DOI · Paper page
  43. [52]Vander Heiden M.G. Chandel N.S. Schumacker P.T. Thompson C.B. Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange Mol. Cell 1999 3 159 167 10.1016/S1097-2765(00)80307-X 10078199 · DOI · Paper page
  44. [53]Belzacq A.S. Vieira H.L. Verrier F. Vandecasteele G. Cohen I. Prevost M.C. Larquet E. Pariselli F. Petit P.X. Kahn A. Bcl-2 and Bax modulate adenine nucleotide translocase activity Cancer Res. 2003 63 541 546 12543814
  45. [54]Degterev A. Hitomi J. Germscheid M. Ch’en I.L. Korkina O. Teng X. Abbott D. Cuny G.D. Yuan C. Wagner G. Identification of RIP1 kinase as a specific cellular target of necrostatins Nat. Chem. Biol. 2008 4 313 321 10.1038/nchembio.83 18408713 PMC5434866 · DOI · Paper page
  46. [55]Sun X. Lee J. Navas T. Baldwin D.T. Stewart T.A. Dixit V.M. RIP3, a novel apoptosis-inducing kinase J. Biol. Chem. 1999 274 16871 16875 10.1074/jbc.274.24.16871 10358032 · DOI
  47. [57]Kokoszka J.E. Waymire K.G. Levy S.E. Sligh J.E. Cai J. Jones D.P. MacGregor G.R. Wallace D.C. The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore Nature 2004 427 461 465 10.1038/nature02229 14749836 PMC3049806 · DOI · Paper page
  48. [58]Temkin V. Huang Q. Liu H. Osada H. Pope R.M. Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis Mol. Cell. Biol. 2006 26 2215 2225 10.1128/MCB.26.6.2215-2225.2006 16507998 PMC1430284 · DOI
  49. [60]Irrinki K.M. Mallilankaraman K. Thapa R.J. Chandramoorthy H.C. Smith F.J. Jog N.R. Gandhirajan R.K. Kelsen S.G. Houser S.R. May M.J. Requirement of FADD, NEMO, and BAX/BAK for aberrant mitochondrial function in tumor necrosis factor alpha-induced necrosis Mol. Cell. Biol. 2011 31 3745 3758 10.1128/MCB.05303-11 21746883 PMC3165716 · DOI
  50. [61]Tischner D. Manzl C. Soratroi C. Villunger A. Krumschnabel G. Necrosis-like death can engage multiple pro-apoptotic Bcl-2 protein family members Apoptosis 2012 17 1197 1209 10.1007/s10495-012-0756-8 22971741 PMC4918797 · DOI
  51. [62]Weiner H. A medicine of human relationships Pharos. Alpha Omega Alpha Honor Med. Soc. 1989 52 2 6 2813500
  52. [63]Krawczak M. Bockel B. The formal analysis of multilocus DNA fingerprints EXS 1993 67 249 255 8400694
  53. [64]Bonora M. Wieckowski M.R. Sinclair D.A. Kroemer G. Pinton P. Galluzzi L. Targeting mitochondria for cardiovascular disorders: Therapeutic potential and obstacles Nat. Rev. Cardiol. 2019 16 33 55 10.1038/s41569-018-0074-0 30177752 PMC6349394 · DOI
  54. [66]Zahrebelski G. Nieminen A.L. al-Ghoul K. Qian T. Herman B. Lemasters J.J. Progression of subcellular changes during chemical hypoxia to cultured rat hepatocytes: A laser scanning confocal microscopic study Hepatology 1995 21 1361 1372 7737643
  55. [67]Fang Y.D. Xu X. Dang Y.M. Zhang Y.M. Zhang J.P. Hu J.Y. Zhang Q. Dai X. Teng M. Zhang D.X. MAP4 mechanism that stabilizes mitochondrial permeability transition in hypoxia: Microtubule enhancement and DYNLT1 interaction with VDAC1 PLoS ONE 2011 6 e28052 10.1371/journal.pone.0028052 22164227 PMC3229508 · DOI
  56. [68]Soares R.O.S. Losada D.M. Jordani M.C. Evora P. Castro E.S.O. Ischemia/Reperfusion Injury Revisited: An Overview of the Latest Pharmacological Strategies Int. J. Mol. Sci. 2019 20 5034 10.3390/ijms20205034 PMC6834141 31614478 · DOI
  57. [69]Liu R.R. Murphy T.H. Reversible cyclosporin A-sensitive mitochondrial depolarization occurs within minutes of stroke onset in mouse somatosensory cortex in vivo: A two-photon imaging study J. Biol. Chem. 2009 284 36109 36117 10.1074/jbc.M109.055301 19892710 PMC2794726 · DOI
  58. [70]Adachi M. Takahashi K. Nishikawa M. Miki H. Uyama M. High intraocular pressure-induced ischemia and reperfusion injury in the optic nerve and retina in rats Graefes Arch. Clin. Exp. Ophthalmol. 1996 234 445 451 10.1007/BF02539411 8817288 · DOI
  59. [71]Hwang J.H. Lee J.H. Lee K.H. Bae E.J. Sung D.K. Chang Y.S. Park W.S. Cyclosporine A attenuates hypoxic-ischemic brain injury in newborn rats Brain Res. 2010 1359 208 215 10.1016/j.brainres.2010.08.047 20735992 · DOI
  60. [72]Ong S.G. Lee W.H. Theodorou L. Kodo K. Lim S.Y. Shukla D.H. Briston T. Kiriakidis S. Ashcroft M. Davidson S.M. HIF-1 reduces ischaemia-reperfusion injury in the heart by targeting the mitochondrial permeability transition pore Cardiovasc. Res. 2014 104 24 36 10.1093/cvr/cvu172 25063991 · DOI
  61. [73]Chatterjee P.K. Brown P.A. Cuzzocrea S. Zacharowski K. Stewart K.N. Mota-Filipe H. McDonald M.C. Thiemermann C. Calpain inhibitor-1 reduces renal ischemia/reperfusion injury in the rat Kidney Int. 2001 59 2073 2083 10.1046/j.1523-1755.2001.00722.x 11380809 · DOI
  62. [74]Kalogeris T. Baines C.P. Krenz M. Korthuis R.J. Ischemia/Reperfusion Compr. Physiol. 2016 7 113 170 28135002 PMC5648017
  63. [75]Shintani-Ishida K. Yoshida K. Mitochondrial m-calpain opens the mitochondrial permeability transition pore in ischemia-reperfusion Int. J. Cardiol. 2015 197 26 32 10.1016/j.ijcard.2015.06.010 26113472 · DOI
  64. [76]Piper H.M. Meuter K. Schafer C. Cellular mechanisms of ischemia-reperfusion injury Ann. Thorac. Surg. 2003 75 S644 S648 10.1016/S0003-4975(02)04686-6 12607706 · DOI
  65. [77]Granger D.N. Kvietys P.R. Reperfusion injury and reactive oxygen species: The evolution of a concept Redox Biol. 2015 6 524 551 10.1016/j.redox.2015.08.020 26484802 PMC4625011 · DOI
  66. [79]Zorov D.B. Juhaszova M. Sollott S.J. Mitochondrial reactive oxygen species (ROS) and ROS-induced ROS release Physiol. Rev. 2014 94 909 950 10.1152/physrev.00026.2013 24987008 PMC4101632 · DOI · Paper page
  67. [80]Chen Y.R. Zweier J.L. Cardiac mitochondria and reactive oxygen species generation Circ. Res. 2014 114 524 537 10.1161/CIRCRESAHA.114.300559 24481843 PMC4118662 · DOI
  68. [81]Barzyc A. Lysik W. Slyk J. Kuszewski M. Zarebinski M. Wojciechowska M. Cudnoch-Jedrzejewska A. Reperfusion injury as a target for diminishing infarct size Med. Hypotheses 2020 137 109558 10.1016/j.mehy.2020.109558 31958650 · DOI
  69. [82]Griffiths E.J. Halestrap A.P. Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion Biochem. J. 1995 307 93 98 10.1042/bj3070093 7717999 PMC1136749 · DOI
  70. [83]Morciano G. Bonora M. Campo G. Aquila G. Rizzo P. Giorgi C. Wieckowski M.R. Pinton P. Mechanistic Role of mPTP in Ischemia-Reperfusion Injury Adv. Exp. Med. Biol. 2017 982 169 189 28551787
  71. [84]Upadhaya S. Madala S. Baniya R. Subedi S.K. Saginala K. Bachuwa G. Impact of cyclosporine A use in the prevention of reperfusion injury in acute myocardial infarction: A meta-analysis Cardiol. J. 2017 24 43 50 10.5603/CJ.a2016.0091 27734457 · DOI
  72. [85]Pottecher J. Kindo M. Chamaraux-Tran T.N. Charles A.L. Lejay A. Kemmel V. Vogel T. Chakfe N. Zoll J. Diemunsch P. Skeletal muscle ischemia-reperfusion injury and cyclosporine A in the aging rat Fundam. Clin. Pharmacol. 2016 30 216 225 10.1111/fcp.12180 26787364 · DOI
  73. [86]Uchino H. Minamikawa-Tachino R. Kristian T. Perkins G. Narazaki M. Siesjo B.K. Shibasaki F. Differential neuroprotection by cyclosporin A and FK506 following ischemia corresponds with differing abilities to inhibit calcineurin and the mitochondrial permeability transition Neurobiol. Dis. 2002 10 219 233 10.1006/nbdi.2002.0514 12270685 · DOI
  74. [87]Konukoglu D. Tasci I. Cetinkale O. Effects of cyclosporin A and ibuprofen on liver ischemia-reperfusion injury in the rat Clin. Chim. Acta 1998 275 1 8 10.1016/S0009-8981(97)00089-2 9706838 · DOI
  75. [88]Li J. Yan Z. Fang Q. A Mechanism Study Underlying the Protective Effects of Cyclosporine-A on Lung Ischemia-Reperfusion Injury Pharmacology 2017 100 83 90 10.1159/000458760 28501872 · DOI
  76. [89]Yazdani I. Majdani R. Ghasemnejad-Berenji M. Dehpour A.R. Comparison of multiple doses of cyclosporine A on germ cell apoptosis and epididymal sperm parameters after testicular ischemia/reperfusion in rats Exp. Mol. Pathol. 2019 110 104271 10.1016/j.yexmp.2019.104271 31251898 · DOI
  77. [90]Ruiz-Meana M. Inserte J. Fernandez-Sanz C. Hernando V. Miro-Casas E. Barba I. Garcia-Dorado D. The role of mitochondrial permeability transition in reperfusion-induced cardiomyocyte death depends on the duration of ischemia Basic Res. Cardiol. 2011 106 1259 1268 10.1007/s00395-011-0225-5 21959501 · DOI
  78. [91]Imahashi K. Pott C. Goldhaber J.I. Steenbergen C. Philipson K.D. Murphy E. Cardiac-specific ablation of the Na+-Ca2+ exchanger confers protection against ischemia/reperfusion injury Circ. Res. 2005 97 916 921 10.1161/01.RES.0000187456.06162.cb 16179590 · DOI
  79. [92]Imahashi K. Schneider M.D. Steenbergen C. Murphy E. Transgenic expression of Bcl-2 modulates energy metabolism, prevents cytosolic acidification during ischemia, and reduces ischemia/reperfusion injury Circ. Res. 2004 95 734 741 10.1161/01.RES.0000143898.67182.4c 15345651 · DOI
  80. [93]Luongo T.S. Lambert J.P. Gross P. Nwokedi M. Lombardi A.A. Shanmughapriya S. Carpenter A.C. Kolmetzky D. Gao E. van Berlo J.H. The mitochondrial Na+/Ca2+ exchanger is essential for Ca2+ homeostasis and viability Nature 2017 545 93 97 10.1038/nature22082 28445457 PMC5731245 · DOI · Paper page
  81. [94]Zhao Q. Wang S. Li Y. Wang P. Li S. Guo Y. Yao R. The role of the mitochondrial calcium uniporter in cerebral ischemia/reperfusion injury in rats involves regulation of mitochondrial energy metabolism Mol. Med. Rep. 2013 7 1073 1080 10.3892/mmr.2013.1321 23426506 · DOI
  82. [96]Campo G. Morciano G. Pavasini R. Bonora M. Sbano L. Biscaglia S. Bovolenta M. Pinotti M. Punzetti S. Rizzo P. Fo ATP synthase C subunit serum levels in patients with ST-segment Elevation Myocardial Infarction: Preliminary findings Int. J. Cardiol. 2016 221 993 997 10.1016/j.ijcard.2016.07.125 27441480 · DOI
  83. [97]Eirin A. Li Z. Zhang X. Krier J.D. Woollard J.R. Zhu X.Y. Tang H. Herrmann S.M. Lerman A. Textor S.C. A mitochondrial permeability transition pore inhibitor improves renal outcomes after revascularization in experimental atherosclerotic renal artery stenosis Hypertension 2012 60 1242 1249 10.1161/HYPERTENSIONAHA.112.199919 23045468 · DOI
  84. [98]Tanno M. Kuno A. Ishikawa S. Miki T. Kouzu H. Yano T. Murase H. Tobisawa T. Ogasawara M. Horio Y. Translocation of glycogen synthase kinase-3beta (GSK-3beta), a trigger of permeability transition, is kinase activity-dependent and mediated by interaction with voltage-dependent anion channel 2 (VDAC2) J. Biol. Chem. 2014 289 29285 29296 10.1074/jbc.M114.563924 25187518 PMC4200279 · DOI
  85. [99]Bao H. Ge Y. Zhuang S. Dworkin L.D. Liu Z. Gong R. Inhibition of glycogen synthase kinase-3beta prevents NSAID-induced acute kidney injury Kidney Int. 2012 81 662 673 10.1038/ki.2011.443 22258319 PMC3305839 · DOI
  86. [100]Wang Z. Ge Y. Bao H. Dworkin L. Peng A. Gong R. Redox-sensitive glycogen synthase kinase 3beta-directed control of mitochondrial permeability transition: Rheostatic regulation of acute kidney injury Free Radic. Biol. Med. 2013 65 849 858 10.1016/j.freeradbiomed.2013.08.169 23973862 PMC3859848 · DOI
  87. [101]Linkermann A. De Zen F. Weinberg J. Kunzendorf U. Krautwald S. Programmed necrosis in acute kidney injury Nephrol. Dial. Transplant. Off. Publ. Eur. Dial. Transpl. Assoc. Eur. Ren. Assoc. 2012 27 3412 3419 10.1093/ndt/gfs373 22942173 · DOI
  88. [102]Linkermann A. Brasen J.H. Darding M. Jin M.K. Sanz A.B. Heller J.O. De Zen F. Weinlich R. Ortiz A. Walczak H. Two independent pathways of regulated necrosis mediate ischemia-reperfusion injury Proc. Natl. Acad. Sci. USA 2013 110 12024 12029 10.1073/pnas.1305538110 23818611 PMC3718149 · DOI
  89. [103]Mulay S.R. Honarpisheh M.M. Foresto-Neto O. Shi C. Desai J. Zhao Z.B. Marschner J.A. Popper B. Buhl E.M. Boor P. Mitochondria Permeability Transition versus Necroptosis in Oxalate-Induced AKI J. Am. Soc. Nephrol. 2019 30 1857 1869 10.1681/ASN.2018121218 31296606 PMC6779355 · DOI
  90. [104]Du H. Guo L. Fang F. Chen D. Sosunov A.A. McKhann G.M. Yan Y. Wang C. Zhang H. Molkentin J.D. Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer’s disease Nat. Med. 2008 14 1097 1105 10.1038/nm.1868 18806802 PMC2789841 · DOI
  91. [105]Manczak M. Reddy P.H. Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer’s disease Hum. Mol. Genet. 2012 21 5131 5146 10.1093/hmg/dds360 22926141 PMC3490521 · DOI · Paper page
  92. [106]Devi L. Raghavendran V. Prabhu B.M. Avadhani N.G. Anandatheerthavarada H.K. Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain J. Biol. Chem. 2008 283 9089 9100 10.1074/jbc.M710012200 18245082 PMC2431021 · DOI
  93. [107]Yao J. Du H. Yan S. Fang F. Wang C. Lue L.F. Guo L. Chen D. Stern D.M. Gunn Moore F.J. Inhibition of amyloid-beta (Abeta) peptide-binding alcohol dehydrogenase-Abeta interaction reduces Abeta accumulation and improves mitochondrial function in a mouse model of Alzheimer’s disease J. Neurosci. 2011 31 2313 2320 10.1523/JNEUROSCI.4717-10.2011 21307267 PMC3381884 · DOI
  94. [108]Liu G. Zhang C. Yin J. Li X. Cheng F. Li Y. Yang H. Ueda K. Chan P. Yu S. alpha-Synuclein is differentially expressed in mitochondria from different rat brain regions and dose-dependently down-regulates complex I activity Neurosci. Lett. 2009 454 187 192 10.1016/j.neulet.2009.02.056 19429081 · DOI
  95. [109]Zhu Y. Duan C. Lu L. Gao H. Zhao C. Yu S. Ueda K. Chan P. Yang H. alpha-Synuclein overexpression impairs mitochondrial function by associating with adenylate translocator Int. J. Biochem. Cell Biol. 2011 43 732 741 10.1016/j.biocel.2011.01.014 21310263 · DOI
  96. [110]Tillement L. Lecanu L. Yao W. Greeson J. Papadopoulos V. The spirostenol (22R, 25R)-20alpha-spirost-5-en-3beta-yl hexanoate blocks mitochondrial uptake of Abeta in neuronal cells and prevents Abeta-induced impairment of mitochondrial function Steroids 2006 71 725 735 10.1016/j.steroids.2006.05.003 16787656 · DOI
  97. [111]Hou Y. Ghosh P. Wan R. Ouyang X. Cheng H. Mattson M.P. Cheng A. Permeability transition pore-mediated mitochondrial superoxide flashes mediate an early inhibitory effect of amyloid beta1-42 on neural progenitor cell proliferation Neurobiol. Aging 2014 35 975 989 10.1016/j.neurobiolaging.2013.11.002 24325797 PMC3946227 · DOI
  98. [113]Atlante A. Amadoro G. Bobba A. de Bari L. Corsetti V. Pappalardo G. Marra E. Calissano P. Passarella S. A peptide containing residues 26–44 of tau protein impairs mitochondrial oxidative phosphorylation acting at the level of the adenine nucleotide translocator Biochim. Biophys. Acta 2008 1777 1289 1300 10.1016/j.bbabio.2008.07.004 18725189 · DOI
  99. [114]Ludtmann M.H.R. Angelova P.R. Horrocks M.H. Choi M.L. Rodrigues M. Baev A.Y. Berezhnov A.V. Yao Z. Little D. Banushi B. Alpha-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease Nat. Commun. 2018 9 2293 10.1038/s41467-018-04422-2 29895861 PMC5997668 · DOI · Paper page
  100. [115]Martin L.J. Semenkow S. Hanaford A. Wong M. Mitochondrial permeability transition pore regulates Parkinson’s disease development in mutant alpha-synuclein transgenic mice Neurobiol. Aging 2014 35 1132 1152 10.1016/j.neurobiolaging.2013.11.008 24325796 PMC3948207 · DOI
  101. [116]Giaime E. Yamaguchi H. Gautier C.A. Kitada T. Shen J. Loss of DJ-1 does not affect mitochondrial respiration but increases ROS production and mitochondrial permeability transition pore opening PLoS ONE 2012 7 e40501 10.1371/journal.pone.0040501 22792356 PMC3392228 · DOI
  102. [117]Gandhi S. Wood-Kaczmar A. Yao Z. Plun-Favreau H. Deas E. Klupsch K. Downward J. Latchman D.S. Tabrizi S.J. Wood N.W. PINK1-associated Parkinson’s disease is caused by neuronal vulnerability to calcium-induced cell death Mol. Cell 2009 33 627 638 10.1016/j.molcel.2009.02.013 19285945 PMC2724101 · DOI · Paper page
  103. [118]Cui T. Fan C. Gu L. Gao H. Liu Q. Zhang T. Qi Z. Zhao C. Zhao H. Cai Q. Silencing of PINK1 induces mitophagy via mitochondrial permeability transition in dopaminergic MN9D cells Brain Res. 2011 1394 1 13 10.1016/j.brainres.2011.01.035 21262209 · DOI
  104. [119]Gautier C.A. Giaime E. Caballero E. Nunez L. Song Z. Chan D. Villalobos C. Shen J. Regulation of mitochondrial permeability transition pore by PINK1 Mol. Neurodegener. 2012 7 22 10.1186/1750-1326-7-22 22630785 PMC3405481 · DOI
  105. [120]Dagda R.K. Das Banerjee T. Janda E. How Parkinsonian toxins dysregulate the autophagy machinery Int. J. Mol. Sci. 2013 14 22163 22189 10.3390/ijms141122163 24217228 PMC3856058 · DOI
  106. [121]Rasheed M.Z. Tabassum H. Parvez S. Mitochondrial permeability transition pore: A promising target for the treatment of Parkinson’s disease Protoplasma 2017 254 33 42 10.1007/s00709-015-0930-2 26825389 · DOI
  107. [124]Castellazzi M. Patergnani S. Donadio M. Giorgi C. Bonora M. Bosi C. Brombo G. Pugliatti M. Seripa D. Zuliani G. Autophagy and mitophagy biomarkers are reduced in sera of patients with Alzheimer’s disease and mild cognitive impairment Sci. Rep. 2019 9 20009 10.1038/s41598-019-56614-5 31882960 PMC6934625 · DOI
  108. [125]Du F. Yu Q. Yan S. Hu G. Lue L.F. Walker D.G. Wu L. Yan S.F. Tieu K. Yan S.S. PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease Brain 2017 140 3233 3251 10.1093/brain/awx258 29077793 PMC5841141 · DOI
  109. [126]Fang E.F. Hou Y. Palikaras K. Adriaanse B.A. Kerr J.S. Yang B. Lautrup S. Hasan-Olive M.M. Caponio D. Dan X. Mitophagy inhibits amyloid-beta and tau pathology and reverses cognitive deficits in models of Alzheimer’s disease Nat. Neurosci. 2019 22 401 412 10.1038/s41593-018-0332-9 30742114 PMC6693625 · DOI · Paper page
  110. [127]Martin L.J. Gertz B. Pan Y. Price A.C. Molkentin J.D. Chang Q. The mitochondrial permeability transition pore in motor neurons: Involvement in the pathobiology of ALS mice Exp. Neurol. 2009 218 333 346 10.1016/j.expneurol.2009.02.015 19272377 PMC2710399 · DOI
  111. [128]Martin L.J. Fancelli D. Wong M. Niedzwiecki M. Ballarini M. Plyte S. Chang Q. GNX-4728, a novel small molecule drug inhibitor of mitochondrial permeability transition, is therapeutic in a mouse model of amyotrophic lateral sclerosis Front. Cell Neurosci. 2014 8 433 10.3389/fncel.2014.00433 25565966 PMC4271619 · DOI
  112. [129]Weber J.J. Clemensson L.E. Schioth H.B. Nguyen H.P. Olesoxime in neurodegenerative diseases: Scrutinising a promising drug candidate Biochem. Pharmacol. 2019 168 305 318 10.1016/j.bcp.2019.07.002 31283931 · DOI
  113. [130]Bordet T. Berna P. Abitbol J.L. Pruss R.M. Olesoxime (TRO19622): A Novel Mitochondrial-Targeted Neuroprotective Compound Pharmaceuticals. 2010 3 345 368 10.3390/ph3020345 27713255 PMC4033913 · DOI
  114. [132]Patergnani S. Fossati V. Bonora M. Giorgi C. Marchi S. Missiroli S. Rusielewicz T. Wieckowski M.R. Pinton P. Mitochondria in Multiple Sclerosis: Molecular Mechanisms of Pathogenesis Int. Rev. Cell Mol. Biol. 2017 328 49 103 28069137
  115. [133]Mahad D. Ziabreva I. Lassmann H. Turnbull D. Mitochondrial defects in acute multiple sclerosis lesions Brain 2008 131 1722 1735 10.1093/brain/awn105 18515320 PMC2442422 · DOI · Paper page
  116. [134]Inarrea P. Alarcia R. Alava M.A. Capablo J.L. Casanova A. Iniguez C. Iturralde M. Larrode P. Martin J. Mostacero E. Mitochondrial complex enzyme activities and cytochrome C expression changes in multiple sclerosis Mol. Neurobiol. 2014 49 1 9 10.1007/s12035-013-8481-z 23761047 · DOI
  117. [135]Bonora M. De Marchi E. Patergnani S. Suski J.M. Celsi F. Bononi A. Giorgi C. Marchi S. Rimessi A. Duszynski J. Tumor necrosis factor-alpha impairs oligodendroglial differentiation through a mitochondria-dependent process Cell Death Differ. 2014 21 1198 1208 10.1038/cdd.2014.35 24658399 PMC4085526 · DOI
  118. [136]Tranah G.J. Santaniello A. Caillier S.J. D’Alfonso S. Martinelli Boneschi F. Hauser S.L. Oksenberg J.R. Mitochondrial DNA sequence variation in multiple sclerosis Neurology 2015 85 325 330 10.1212/WNL.0000000000001744 26136518 PMC4520811 · DOI
  119. [137]Castellazzi M. Patergnani S. Donadio M. Giorgi C. Bonora M. Fainardi E. Casetta I. Granieri E. Pugliatti M. Pinton P. Correlation between auto/mitophagic processes and magnetic resonance imaging activity in multiple sclerosis patients J. Neuroinflammation 2019 16 131 10.1186/s12974-019-1526-0 31248423 PMC6598368 · DOI
  120. [138]Patergnani S. Castellazzi M. Bonora M. Marchi S. Casetta I. Pugliatti M. Giorgi C. Granieri E. Pinton P. Autophagy and mitophagy elements are increased in body fluids of multiple sclerosis-affected individuals J. Neurol. Neurosurg. Psychiatry 2018 89 439 441 10.1136/jnnp-2017-316234 28866627 · DOI
  121. [139]Barcelos I.P. Troxell R.M. Graves J.S. Mitochondrial Dysfunction and Multiple Sclerosis Biology 2019 8 37 10.3390/biology8020037 PMC6627385 31083577 · DOI
  122. [140]Su K. Bourdette D. Forte M. Mitochondrial dysfunction and neurodegeneration in multiple sclerosis Front. Physiol. 2013 4 169 10.3389/fphys.2013.00169 23898299 PMC3722885 · DOI
  123. [141]Forte M. Gold B.G. Marracci G. Chaudhary P. Basso E. Johnsen D. Yu X. Fowlkes J. Rahder M. Stem K. Cyclophilin D inactivation protects axons in experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis Proc. Natl. Acad. Sci. USA 2007 104 7558 7563 10.1073/pnas.0702228104 17463082 PMC1857227 · DOI
  124. [143]Pinton P. Rimessi A. Marchi S. Orsini F. Migliaccio E. Giorgio M. Contursi C. Minucci S. Mantovani F. Wieckowski M.R. Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial effects of the life-span determinant p66Shc Science 2007 315 659 663 10.1126/science.1135380 17272725 · DOI
  125. [144]Patergnani S. Marchi S. Rimessi A. Bonora M. Giorgi C. Mehta K.D. Pinton P. PRKCB/protein kinase C, beta and the mitochondrial axis as key regulators of autophagy Autophagy 2013 9 1367 1385 10.4161/auto.25239 23778835 · DOI
  126. [145]Su K.G. Savino C. Marracci G. Chaudhary P. Yu X. Morris B. Galipeau D. Giorgio M. Forte M. Bourdette D. Genetic inactivation of the p66 isoform of ShcA is neuroprotective in a murine model of multiple sclerosis Eur. J. Neurosci. 2012 35 562 571 10.1111/j.1460-9568.2011.07972.x 22277070 PMC3279590 · DOI
  127. [146]Savino C. Pelicci P. Giorgio M. The P66Shc/mitochondrial permeability transition pore pathway determines neurodegeneration Oxidative Med. Cell. Longev. 2013 2013 719407 10.1155/2013/719407 PMC3671270 23766859 · DOI · Paper page
  128. [147]Burr A.R. Molkentin J.D. Genetic evidence in the mouse solidifies the calcium hypothesis of myofiber death in muscular dystrophy Cell Death Differ. 2015 22 1402 1412 10.1038/cdd.2015.65 26088163 PMC4532779 · DOI
  129. [148]Emery A.E. The muscular dystrophies Lancet 2002 359 687 695 10.1016/S0140-6736(02)07815-7 11879882 · DOI · Paper page
  130. [150]Emery A.E. Population frequencies of inherited neuromuscular diseases--a world survey Neuromuscul. Disord. 1991 1 19 29 10.1016/0960-8966(91)90039-U 1822774 · DOI
  131. [151]Durbeej M. Campbell K.P. Muscular dystrophies involving the dystrophin-glycoprotein complex: An overview of current mouse models Curr. Opin. Genet. Dev. 2002 12 349 361 10.1016/S0959-437X(02)00309-X 12076680 · DOI
  132. [152]Ervasti J.M. Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin J. Cell Biol. 1993 122 809 823 10.1083/jcb.122.4.809 8349731 PMC2119587 · DOI
  133. [153]Jung C. Martins A.S. Niggli E. Shirokova N. Dystrophic cardiomyopathy: Amplification of cellular damage by Ca2+ signalling and reactive oxygen species-generating pathways Cardiovasc. Res. 2008 77 766 773 10.1093/cvr/cvm089 18056762 · DOI
  134. [154]Hoffman E.P. Monaco A.P. Feener C.C. Kunkel L.M. Conservation of the Duchenne muscular dystrophy gene in mice and humans Science 1987 238 347 350 10.1126/science.3659917 3659917 · DOI
  135. [155]Dubinin M.V. Talanov E.Y. Tenkov K.S. Starinets V.S. Mikheeva I.B. Sharapov M.G. Belosludtsev K.N. Duchenne muscular dystrophy is associated with the inhibition of calcium uniport in mitochondria and an increased sensitivity of the organelles to the calcium-induced permeability transition Biochim. Biophys. Acta Mol. Basis Dis. 2020 1866 165674 10.1016/j.bbadis.2020.165674 31926263 · DOI
  136. [156]Giacomotto J. Brouilly N. Walter L. Mariol M.C. Berger J. Segalat L. Becker T.S. Currie P.D. Gieseler K. Chemical genetics unveils a key role of mitochondrial dynamics, cytochrome c release and IP3R activity in muscular dystrophy Hum. Mol. Genet. 2013 22 4562 4578 10.1093/hmg/ddt302 23804750 · DOI
  137. [157]Stupka N. Gregorevic P. Plant D.R. Lynch G.S. The calcineurin signal transduction pathway is essential for successful muscle regeneration in mdx dystrophic mice Acta Neuropathol. 2004 107 299 310 10.1007/s00401-003-0807-x 14727129 · DOI
  138. [158]Chakkalakal J.V. Harrison M.A. Carbonetto S. Chin E. Michel R.N. Jasmin B.J. Stimulation of calcineurin signaling attenuates the dystrophic pathology in mdx mice Hum. Mol. Genet. 2004 13 379 388 10.1093/hmg/ddh037 14681302 · DOI
  139. [159]Reutenauer J. Dorchies O.M. Patthey-Vuadens O. Vuagniaux G. Ruegg U.T. Investigation of Debio 025, a cyclophilin inhibitor, in the dystrophic mdx mouse, a model for Duchenne muscular dystrophy Br. J. Pharmacol. 2008 155 574 584 10.1038/bjp.2008.285 18641676 PMC2579666 · DOI
  140. [160]Millay D.P. Sargent M.A. Osinska H. Baines C.P. Barton E.R. Vuagniaux G. Sweeney H.L. Robbins J. Molkentin J.D. Genetic and pharmacologic inhibition of mitochondrial-dependent necrosis attenuates muscular dystrophy Nat. Med. 2008 14 442 447 10.1038/nm1736 18345011 PMC2655270 · DOI
  141. [161]Palma E. Tiepolo T. Angelin A. Sabatelli P. Maraldi N.M. Basso E. Forte M.A. Bernardi P. Bonaldo P. Genetic ablation of cyclophilin D rescues mitochondrial defects and prevents muscle apoptosis in collagen VI myopathic mice Hum. Mol. Genet. 2009 18 2024 2031 10.1093/hmg/ddp126 19293339 · DOI
  142. [162]Lampe A.K. Bushby K.M. Collagen VI related muscle disorders J. Med Genet. 2005 42 673 685 10.1136/jmg.2002.002311 16141002 PMC1736127 · DOI
  143. [163]Merlini L. Martoni E. Grumati P. Sabatelli P. Squarzoni S. Urciuolo A. Ferlini A. Gualandi F. Bonaldo P. Autosomal recessive myosclerosis myopathy is a collagen VI disorder Neurology 2008 71 1245 1253 10.1212/01.wnl.0000327611.01687.5e 18852439 · DOI
  144. [164]Bernardi P. Krauskopf A. Basso E. Petronilli V. Blachly-Dyson E. Di Lisa F. Forte M.A. The mitochondrial permeability transition from in vitro artifact to disease target FEBS J. 2006 273 2077 2099 10.1111/j.1742-4658.2006.05213.x 16649987 · DOI · Paper page
  145. [165]Bonaldo P. Braghetta P. Zanetti M. Piccolo S. Volpin D. Bressan G.M. Collagen VI deficiency induces early onset myopathy in the mouse: An animal model for Bethlem myopathy Hum. Mol. Genet. 1998 7 2135 2140 10.1093/hmg/7.13.2135 9817932 · DOI
  146. [166]Irwin W.A. Bergamin N. Sabatelli P. Reggiani C. Megighian A. Merlini L. Braghetta P. Columbaro M. Volpin D. Bressan G.M. Mitochondrial dysfunction and apoptosis in myopathic mice with collagen VI deficiency Nat. Genet. 2003 35 367 371 10.1038/ng1270 14625552 · DOI
  147. [167]Angelin A. Tiepolo T. Sabatelli P. Grumati P. Bergamin N. Golfieri C. Mattioli E. Gualandi F. Ferlini A. Merlini L. Mitochondrial dysfunction in the pathogenesis of Ullrich congenital muscular dystrophy and prospective therapy with cyclosporins Proc. Natl. Acad. Sci. USA 2007 104 991 996 10.1073/pnas.0610270104 17215366 PMC1783427 · DOI
  148. [168]Tagliavini F. Sardone F. Squarzoni S. Maraldi N.M. Merlini L. Faldini C. Sabatelli P. Ultrastructural changes in muscle cells of patients with collagen VI-related myopathies Muscles Ligaments Tendons J. 2013 3 281 286 10.32098/mltj.04.2013.08 24596691 PMC3940501 · DOI
  149. [169]De Palma C. Morisi F. Cheli S. Pambianco S. Cappello V. Vezzoli M. Rovere-Querini P. Moggio M. Ripolone M. Francolini M. Autophagy as a new therapeutic target in Duchenne muscular dystrophy Cell Death Dis. 2012 3 e418 10.1038/cddis.2012.159 23152054 PMC3542595 · DOI · Paper page
  150. [170]Wong A. Cortopassi G. mtDNA mutations confer cellular sensitivity to oxidant stress that is partially rescued by calcium depletion and cyclosporin A Biochem. Biophys. Res. Commun. 1997 239 139 145 10.1006/bbrc.1997.7443 9345284 · DOI
  151. [171]Haroon M.F. Fatima A. Scholer S. Gieseler A. Horn T.F. Kirches E. Wolf G. Kreutzmann P. Minocycline, a possible neuroprotective agent in Leber’s hereditary optic neuropathy (LHON): Studies of cybrid cells bearing 11,778 mutation Neurobiol. Dis. 2007 28 237 250 10.1016/j.nbd.2007.07.021 17822909 · DOI
  152. [172]Cotan D. Cordero M.D. Garrido-Maraver J. Oropesa-Avila M. Rodriguez-Hernandez A. Gomez Izquierdo L. De la Mata M. De Miguel M. Lorite J.B. Infante E.R. Secondary coenzyme Q10 deficiency triggers mitochondria degradation by mitophagy in MELAS fibroblasts FASEB J. 2011 25 2669 2687 10.1096/fj.10-165340 21551238 · DOI
  153. [173]Cui J. Wang L. Ren X. Zhang Y. Zhang H. LRPPRC: A Multifunctional Protein Involved in Energy Metabolism and Human Disease Front. Physiol. 2019 10 595 10.3389/fphys.2019.00595 31178748 PMC6543908 · DOI
  154. [174]Burelle Y. Bemeur C. Rivard M.E. Thompson Legault J. Boucher G. Consortium L. Morin C. Coderre L. Des Rosiers C. Mitochondrial vulnerability and increased susceptibility to nutrient-induced cytotoxicity in fibroblasts from leigh syndrome French canadian patients PLoS ONE 2015 10 e0120767 10.1371/journal.pone.0120767 25835550 PMC4383560 · DOI
  155. [175]MacVicar T. Langer T. OPA1 processing in cell death and disease—The long and short of it J. Cell Sci. 2016 129 2297 2306 10.1242/jcs.159186 27189080 · DOI
  156. [176]Pfeffer G. Gorman G.S. Griffin H. Kurzawa-Akanbi M. Blakely E.L. Wilson I. Sitarz K. Moore D. Murphy J.L. Alston C.L. Mutations in the SPG7 gene cause chronic progressive external ophthalmoplegia through disordered mitochondrial DNA maintenance Brain 2014 137 1323 1336 10.1093/brain/awu060 24727571 PMC3999722 · DOI
  157. [177]Piquereau J. Caffin F. Novotova M. Prola A. Garnier A. Mateo P. Fortin D. Huynh le H. Nicolas V. Alavi M.V. Down-regulation of OPA1 alters mouse mitochondrial morphology, PTP function, and cardiac adaptation to pressure overload Cardiovasc. Res. 2012 94 408 417 10.1093/cvr/cvs117 22406748 PMC3863708 · DOI
  158. [179]Zhang D. Lu C. Whiteman M. Chance B. Armstrong J.S. The mitochondrial permeability transition regulates cytochrome c release for apoptosis during endoplasmic reticulum stress by remodeling the cristae junction J. Biol. Chem. 2008 283 3476 3486 10.1074/jbc.M707528200 18056990 · DOI
  159. [180]Hurst S. Baggett A. Csordas G. Sheu S.S. SPG7 targets the m-AAA protease complex to process MCU for uniporter assembly, Ca(2+) influx, and regulation of mitochondrial permeability transition pore opening J. Biol. Chem. 2019 294 10807 10818 10.1074/jbc.RA118.006443 31097542 PMC6635443 · DOI
  160. [181]Wong R.J. Cheung R. Ahmed A. Nonalcoholic steatohepatitis is the most rapidly growing indication for liver transplantation in patients with hepatocellular carcinoma in the U.S Hepatology 2014 59 2188 2195 10.1002/hep.26986 24375711 · DOI
  161. [182]Gastaldelli A. Kozakova M. Hojlund K. Flyvbjerg A. Favuzzi A. Mitrakou A. Balkau B. Investigators R. Fatty liver is associated with insulin resistance, risk of coronary heart disease, and early atherosclerosis in a large European population Hepatology 2009 49 1537 1544 10.1002/hep.22845 19291789 · DOI
  162. [183]Teodoro J.S. Rolo A.P. Duarte F.V. Simoes A.M. Palmeira C.M. Differential alterations in mitochondrial function induced by a choline-deficient diet: Understanding fatty liver disease progression Mitochondrion 2008 8 367 376 10.1016/j.mito.2008.07.008 18765303 · DOI
  163. [184]Chen D.F. Wang C.H. The relationship between the opening of mitochondrial permeability transition pores of cultured hepatocytes with their apoptoses in a non-alcoholic fatty liver disease model Chin. J. Hepatol. 2007 15 837 839 18073067
  164. [185]Kang M. Li S. Zhong D. Yang Z. Li P. Hepatocyte apoptosis and mitochondrial permeability transition pore opening in rats with nonalcoholic fatty liver J. South. Med Univ. 2013 33 1062 1066 23895854
  165. [186]Wang X. Du H. Shao S. Bo T. Yu C. Chen W. Zhao L. Li Q. Wang L. Liu X. Cyclophilin D deficiency attenuates mitochondrial perturbation and ameliorates hepatic steatosis Hepatology 2018 68 62 77 10.1002/hep.29788 29356058 · DOI
  166. [187]Lazarin Mde O. Ishii-Iwamoto E.L. Yamamoto N.S. Constantin R.P. Garcia R.F. da Costa C.E. Vitoriano Ade S. de Oliveira M.C. Salgueiro-Pagadigorria C.L. Liver mitochondrial function and redox status in an experimental model of non-alcoholic fatty liver disease induced by monosodium L-glutamate in rats Exp. Mol. Pathol. 2011 91 687 694 10.1016/j.yexmp.2011.07.003 21821020 · DOI
  167. [188]Rimessi A. Marchi S. Patergnani S. Pinton P. H-Ras-driven tumoral maintenance is sustained through caveolin-1-dependent alterations in calcium signaling Oncogene 2014 33 2329 2340 10.1038/onc.2013.192 23728347 · DOI
  168. [189]Arbel N. Ben-Hail D. Shoshan-Barmatz V. Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein J. Biol. Chem. 2012 287 23152 23161 10.1074/jbc.M112.345918 22589539 PMC3391160 · DOI · Paper page
  169. [190]Alavian K.N. Li H. Collis L. Bonanni L. Zeng L. Sacchetti S. Lazrove E. Nabili P. Flaherty B. Graham M. Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase Nat. Cell Biol. 2011 13 1224 1233 10.1038/ncb2330 21926988 PMC3186867 · DOI
  170. [191]Bittremieux M. Parys J.B. Pinton P. Bultynck G. ER functions of oncogenes and tumor suppressors: Modulators of intracellular Ca(2+) signaling Biochim. Biophys. Acta 2016 1863 1364 1378 10.1016/j.bbamcr.2016.01.002 26772784 · DOI
  171. [192]Marchi S. Marinello M. Bononi A. Bonora M. Giorgi C. Rimessi A. Pinton P. Selective modulation of subtype III IP(3)R by Akt regulates ER Ca(2)(+) release and apoptosis Cell Death Dis. 2012 3 e304 10.1038/cddis.2012.45 22552281 PMC3366079 · DOI
  172. [193]Marchi S. Rimessi A. Giorgi C. Baldini C. Ferroni L. Rizzuto R. Pinton P. Akt kinase reducing endoplasmic reticulum Ca2+ release protects cells from Ca2+-dependent apoptotic stimuli Biochem. Biophys. Res. Commun. 2008 375 501 505 10.1016/j.bbrc.2008.07.153 18723000 PMC2576286 · DOI
  173. [194]Papa A. Wan L. Bonora M. Salmena L. Song M.S. Hobbs R.M. Lunardi A. Webster K. Ng C. Newton R.H. Cancer-associated PTEN mutants act in a dominant-negative manner to suppress PTEN protein function Cell 2014 157 595 610 10.1016/j.cell.2014.03.027 24766807 PMC4098792 · DOI
  174. [195]Bononi A. Bonora M. Marchi S. Missiroli S. Poletti F. Giorgi C. Pandolfi P.P. Pinton P. Identification of PTEN at the ER and MAMs and its regulation of Ca(2+) signaling and apoptosis in a protein phosphatase-dependent manner Cell Death Differ. 2013 20 1631 1643 10.1038/cdd.2013.77 23811847 PMC3824603 · DOI
  175. [196]Bononi A. Agnoletto C. De Marchi E. Marchi S. Patergnani S. Bonora M. Giorgi C. Missiroli S. Poletti F. Rimessi A. Protein kinases and phosphatases in the control of cell fate Enzym. Res. 2011 2011 329098 10.4061/2011/329098 PMC3166778 21904669 · DOI
  176. [197]Missiroli S. Bonora M. Patergnani S. Giorgi C. Novel function of the tumor suppressor PML at ER-mitochondria sites in the control of autophagy Oncotarget 2017 8 81723 81724 10.18632/oncotarget.18974 29137212 PMC5669838 · DOI
  177. [198]Missiroli S. Bonora M. Patergnani S. Poletti F. Perrone M. Gafa R. Magri E. Raimondi A. Lanza G. Tacchetti C. PML at Mitochondria-Associated Membranes Is Critical for the Repression of Autophagy and Cancer Development Cell Rep. 2016 16 2415 2427 10.1016/j.celrep.2016.07.082 27545895 PMC5011426 · DOI
  178. [199]Giorgi C. Ito K. Lin H.K. Santangelo C. Wieckowski M.R. Lebiedzinska M. Bononi A. Bonora M. Duszynski J. Bernardi R. PML regulates apoptosis at endoplasmic reticulum by modulating calcium release Science 2010 330 1247 1251 10.1126/science.1189157 21030605 PMC3017677 · DOI
  179. [200]Luo J. Glycogen synthase kinase 3beta (GSK3beta) in tumorigenesis and cancer chemotherapy Cancer Lett. 2009 273 194 200 10.1016/j.canlet.2008.05.045 18606491 PMC4978950 · DOI
  180. [201]Giorgi C. Bonora M. Missiroli S. Morganti C. Morciano G. Wieckowski M.R. Pinton P. Alterations in Mitochondrial and Endoplasmic Reticulum Signaling by p53 Mutants Front. Oncol. 2016 6 42 10.3389/fonc.2016.00042 26942128 PMC4766755 · DOI
  181. [202]Giorgi C. Bonora M. Sorrentino G. Missiroli S. Poletti F. Suski J.M. Galindo Ramirez F. Rizzuto R. Di Virgilio F. Zito E. p53 at the endoplasmic reticulum regulates apoptosis in a Ca2+-dependent manner Proc. Natl. Acad. Sci. USA 2015 112 1779 1784 10.1073/pnas.1410723112 25624484 PMC4330769 · DOI
  182. [203]Bonora M. Giorgi C. Pinton P. Novel frontiers in calcium signaling: A possible target for chemotherapy Pharmacol. Res. 2015 99 82 85 10.1016/j.phrs.2015.05.008 26028552 · DOI
  183. [204]Giorgi C. Bonora M. Pinton P. Inside the tumor: p53 modulates calcium homeostasis Cell Cycle 2015 14 933 934 10.1080/15384101.2015.1010973 25715001 PMC4613355 · DOI
  184. [205]Giorgi C. Bonora M. Missiroli S. Poletti F. Ramirez F.G. Morciano G. Morganti C. Pandolfi P.P. Mammano F. Pinton P. Intravital imaging reveals p53-dependent cancer cell death induced by phototherapy via calcium signaling Oncotarget 2015 6 1435 1445 10.18632/oncotarget.2935 25544762 PMC4359305 · DOI
  185. [206]Kang B.H. Plescia J. Dohi T. Rosa J. Doxsey S.J. Altieri D.C. Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network Cell 2007 131 257 270 10.1016/j.cell.2007.08.028 17956728 · DOI
  186. [207]Ghosh J.C. Siegelin M.D. Dohi T. Altieri D.C. Heat shock protein 60 regulation of the mitochondrial permeability transition pore in tumor cells Cancer Res. 2010 70 8988 8993 10.1158/0008-5472.CAN-10-2225 20978188 PMC2982903 · DOI
  187. [208]Sinha D. D’Silva P. Chaperoning mitochondrial permeability transition: Regulation of transition pore complex by a J-protein, DnaJC15 Cell Death Dis. 2014 5 e1101 10.1038/cddis.2014.72 24603329 PMC3973195 · DOI
  188. [209]Aggarwal V. Tuli H.S. Varol A. Thakral F. Yerer M.B. Sak K. Varol M. Jain A. Khan M.A. Sethi G. Role of Reactive Oxygen Species in Cancer Progression: Molecular Mechanisms and Recent Advancements Biomolecules 2019 9 735 10.3390/biom9110735 PMC6920770 31766246 · DOI
  189. [210]Giorgi C. Marchi S. Simoes I.C.M. Ren Z. Morciano G. Perrone M. Patalas-Krawczyk P. Borchard S. Jedrak P. Pierzynowska K. Mitochondria and Reactive Oxygen Species in Aging and Age-Related Diseases Int. Rev. Cell Mol. Biol. 2018 340 209 344 30072092 PMC8127332
  190. [211]Fulda S. Galluzzi L. Kroemer G. Targeting mitochondria for cancer therapy Nat. Rev. Drug Discov. 2010 9 447 464 10.1038/nrd3137 20467424 · DOI
  191. [212]Shinohara Y. Ishida T. Hino M. Yamazaki N. Baba Y. Terada H. Characterization of porin isoforms expressed in tumor cells Eur. J. Biochem. 2000 267 6067 6073 10.1046/j.1432-1327.2000.01687.x 10998068 · DOI
  192. [213]Beinlich A. Strohmeier R. Kaufmann M. Kuhl H. Relation of cell proliferation to expression of peripheral benzodiazepine receptors in human breast cancer cell lines Biochem. Pharmacol. 2000 60 397 402 10.1016/S0006-2952(00)00325-7 10856435 · DOI
  193. [214]Maaser K. Hopfner M. Jansen A. Weisinger G. Gavish M. Kozikowski A.P. Weizman A. Carayon P. Riecken E.O. Zeitz M. Specific ligands of the peripheral benzodiazepine receptor induce apoptosis and cell cycle arrest in human colorectal cancer cells Br. J. Cancer 2001 85 1771 1780 10.1054/bjoc.2001.2181 11742501 PMC2363981 · DOI
  194. [215]Faure Vigny H. Heddi A. Giraud S. Chautard D. Stepien G. Expression of oxidative phosphorylation genes in renal tumors and tumoral cell lines Mol. Carcinog. 1996 16 165 172 10.1002/(SICI)1098-2744(199607)16:3<165::AID-MC7>3.0.CO;2-G 8688152 · DOI
  195. [216]Rempel A. Mathupala S.P. Griffin C.A. Hawkins A.L. Pedersen P.L. Glucose catabolism in cancer cells: Amplification of the gene encoding type II hexokinase Cancer Res. 1996 56 2468 2471 8653677
  196. [217]Gudnason V. Ingvarsson S. Jonasdottir A. Andresdottir V. Egilsson V. Isoenzyme pattern and subcellular localization of hexokinases in human breast cancer and nonpathological breast tissue Int. J. Cancer 1984 34 63 66 10.1002/ijc.2910340111 6746120 · DOI
  197. [219]Schaller S. Paradis S. Ngoh G.A. Assaly R. Buisson B. Drouot C. Ostuni M.A. Lacapere J.J. Bassissi F. Bordet T. TRO40303, a new cardioprotective compound, inhibits mitochondrial permeability transition J. Pharmacol. Exp. Ther. 2010 333 696 706 10.1124/jpet.110.167486 20215409 · DOI
  198. [220]Sileikyte J. Blachly-Dyson E. Sewell R. Carpi A. Menabo R. Di Lisa F. Ricchelli F. Bernardi P. Forte M. Regulation of the mitochondrial permeability transition pore by the outer membrane does not involve the peripheral benzodiazepine receptor (Translocator Protein of 18 kDa (TSPO)) J. Biol. Chem. 2014 289 13769 13781 10.1074/jbc.M114.549634 24692541 PMC4022851 · DOI
  199. [221]Atar D. Arheden H. Berdeaux A. Bonnet J.L. Carlsson M. Clemmensen P. Cuvier V. Danchin N. Dubois-Rande J.L. Engblom H. Effect of intravenous TRO40303 as an adjunct to primary percutaneous coronary intervention for acute ST-elevation myocardial infarction: MITOCARE study results Eur. Heart J. 2015 36 112 119 10.1093/eurheartj/ehu331 25179768 · DOI
  200. [222]Leruez S. Verny C. Bonneau D. Procaccio V. Lenaers G. Amati-Bonneau P. Reynier P. Scherer C. Prundean A. Orssaud C. Cyclosporine A does not prevent second-eye involvement in Leber’s hereditary optic neuropathy Orphanet J. Rare Dis. 2018 13 33 10.1186/s13023-018-0773-y 29454364 PMC5816422 · DOI

200 of 207 shown

Cited by

Sorted by citations

Authors
Bonora, M., Patergnani, S., Ramaccini, D., Morciano, G., Pedriali, G., Kahsay, A., Bouhamida, E., Giorgi, C., Wieckowski, M., & Pinton, P.
Affiliations
  • University of Ferrara (IT)
  • Instytut Biologii Doświadczalnej im. Marcelego Nenckiego (PL)
Corresponding author
  • Bonora, Massimo
  • Pinton, Paolo
Venue
Biomolecules
Publisher
MDPI AG
Published
2020-07-04
Volume
10
Issue
7
Pages
998
ISSN
2218-273X (ISSN-L)
OpenAlex
W3038384160
Cited by
135
References
22
Citations by year
2026: 13 · 2025: 23 · 2024: 18 · 2023: 20 · 2022: 27 · 2021: 25 · 2020: 9
FWCI
1.98
Type
journal article
Language
en
Open access
Locations
  • Biomolecules (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) (submittedVersion, other-oa)
  • Institutional Research Information System University of Ferrara (University of Ferrara) (submittedVersion, cc-by)
Funders
  • European Commission (HORIZON2020, 722619, 734719)
  • Ministero della Salute (GR2013-02356747)
  • Narodowym Centrum Nauki (UMO-2018/29/B/ NZ1 /00589)
  • Fondazione Umberto Veronesi
  • Associazione Italiana per la Ricerca sul Cancro (IG23670, AIRC, IG-23670, PRIN2017E5 L5P3, IG‐19803, 23670, 19803, PRIN20177E9EPY)
  • Università degli Studi di Ferrara (IG-23670, IG-19803, GGP11139B)
  • H2020 European Research Council (853057)
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
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords
mitochondrial permeability transition, mitochondrial permeability transition pore, inner mitochondrial membrane permeability, mitochondrial swelling, mitochondrial outer membrane permeabilization, apoptosis, caspase activation, reactive oxygen species, calcium, mitochondrial calcium uptake, cell death, human disease
MeSH terms
Mitochondrial Permeability Transition Pore, Calcium, Humans, Mitochondria, Signal Transduction, Cell Death, Reactive Oxygen Species, Membrane Potential, Mitochondrial

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