The path from mitochondrial ROS to aging runs through the mitochondrial permeability transition pore

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works

Aging: a theory based on free radical and radiation chemistry

Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567 · see citing works

Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release

Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works

The Free Radical Theory of Aging Matures

BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879 · see citing works

Oxidative Stress

Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520 · see citing works

The Biologic Clock: The Mitochondria?

Harman, D. (1972) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1972.tb00787.x · Cited by 1,991 · see citing works

NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus

Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648 · see citing works

Declining NAD+ Induces a Pseudohypoxic State Disrupting Nuclear-Mitochondrial Communication during Aging

Gomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482 · see citing works

NAD+ and sirtuins in aging and disease

Imai, S.-I., & Guarente, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.002 · Cited by 1,481 · see citing works

The mitochondrial basis of aging

Sun, N., Youle, R. J., & Finkel, T. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.028 · Cited by 1,441 · see citing works

NAD ⁺ repletion improves mitochondrial and stem cell function and enhances life span in mice

Zhang, H., Ryu, D., Wu, Y., Gariani, K., Wang, X., Luan, P., D’Amico, D., Ropelle, E. R., Lutolf, M. P., Aebersold, R., et al. (2016) · Science · doi:10.1126/science.aaf2693 · Cited by 1,255 · cited 1× · see citing works

The NAD+/Sirtuin Pathway Modulates Longevity through Activation of Mitochondrial UPR and FOXO Signaling

Mouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210 · see citing works

Reactive oxygen species and mitochondria: A nexus of cellular homeostasis

Dunn, J. D., Álvarez, L., Zhang, X., & Soldati, T. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.005 · Cited by 1,199 · see citing works

Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling

Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063 · see citing works

Diversity of ageing across the tree of life

Jones, O. R., Scheuerlein, A., Salguero‐Gómez, R., Camarda, C. G., Schaible, R., Casper, B. B., Dahlgren, J. P., Ehrlén, J., Garcia, M. B., Menges, E. S., et al. (2013) · Nature · doi:10.1038/nature12789 · Cited by 1,033 · 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

Mitochondrial Cardiolipin Is Required for Nlrp3 Inflammasome Activation

Iyer, S. S., He, Q., Janczy, J. R., Elliott, E. I., Zhong, Z., Olivier, A. K., Sadler, J. J., Knepper-Adrian, V., Han, R., Qiao, L., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.001 · Cited by 938 · see citing works

Critical role for calcium mobilization in activation of the NLRP3 inflammasome

Murakami, T., Öckinger, J., Yu, J., Byles, V., McColl, A., Hofer, A. M., & Horng, T. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117765109 · Cited by 925 · see citing works

CD38 Dictates Age-Related NAD Decline and Mitochondrial Dysfunction through an SIRT3-Dependent Mechanism

Camacho-Pereira, J., Tarragó, M. G., Chini, C. C. S., Nin, V., Escande, C., Warner, G. M., Puranik, A. S., Schoon, R. A., Reid, J. M., Galina, A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.006 · Cited by 901 · see citing works

ROS-dependent signal transduction

Reczek, C. R., & Chandel, N. S. (2014) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.09.010 · Cited by 850 · see citing works

Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress.

Crompton, M., Ellinger, H., & COSTI, A. (1988) · PubMed Central · Cited by 841 · see citing works

VDAC, a multi-functional mitochondrial protein regulating cell life and death

Shoshan‐Barmatz, V., Pinto, V. D., Zweckstetter, M., Raviv, Z., Keinan, N., & Arbel, N. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.03.002 · Cited by 792 · see citing works

Mitochondrial permeability transition: a common pathway to necrosis and apoptosis

Js, K., He, L., & Lemasters, J. J. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00618-1 · Cited by 756 · see citing works

Calcium and neurodegeneration

Mattson, M. P. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00275.x · Cited by 751 · see citing works

p53 Opens the Mitochondrial Permeability Transition Pore to Trigger Necrosis

Vaseva, A. V., Marchenko, N. D., Ji, K., Tsirka, S. E., Holzmann, S., & Moll, U. M. (2012) · Cell · doi:10.1016/j.cell.2012.05.014 · Cited by 740 · see citing works

Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide

Bienert, G. P., & Chaumont, F. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.09.017 · Cited by 736 · see citing works

Superoxide flashes in single mitochondria

Wang, W., Fang, H., Groom, L., Cheng, A., Zhang, W., Liu, J., Wang, X., Li, K., Han, P., Zheng, M., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.017 · Cited by 715 · see citing works

Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol

Han, D., Antunes, F., Canali, R., Rettori, D., & Cadenas, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210269200 · Cited by 711 · see citing works

Opening of the mitochondrial permeability transition pore causes depletion of mitochondrial and cytosolic NAD+ and is a causative event in the death of myocytes in postischemic reperfusion of the heart

Di Lisa, F., Menabò, R., Canton, M., Barile, M., & Bernardi, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006825200 · Cited by 678 · see citing works

The mitochondrial permeability transition from<i>in vitro</i>artifact to disease target

Bernardi, P., Krauskopf, A., Basso, E., Petronilli, V., Blalchy‐Dyson, E., Di Lisa, F., & Forte, M. A. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05213.x · Cited by 627 · see citing works

PGC1α and mitochondrial metabolism – emerging concepts and relevance in ageing and neurodegenerative disorders

Austin, S., & St‐Pierre, J. (2012) · Journal of Cell Science · doi:10.1242/jcs.113662 · Cited by 606 · see citing works

An uncoupling channel within the c-subunit ring of the F 1 F O ATP synthase is the mitochondrial permeability transition pore

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

Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy

Hafner, A. V., Dai, J., Gomes, A. P., Xiao, C., Palmeira, C. M., Rosenzweig, A., & Sinclair, D. A. (2010) · Aging · doi:10.18632/aging.100252 · Cited by 547 · see citing works

The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents

Petronilli, V., Costantini, P., Scorrano, L., Colonna, R., Passamonti, S., & Bernardi, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89437-1 · Cited by 531 · see citing works

The mitochondrial permeability transition pore: Molecular nature and role as a target in cardioprotection

Bernardi, P., & Lisa, F. D. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.023 · Cited by 499 · see citing works

Cyclophilin‐D binds strongly to complexes of the voltage‐dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore

Crompton, M., Virji, S., & Ward, J. M. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2580729.x · Cited by 492 · see citing works

Inflamm‐ageing and lifelong antigenic load as major determinants of ageing rate and longevity

Martinis, M. D., Franceschi, C., Monti, D., & Ginaldi, L. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.02.055 · Cited by 488 · see citing works

Mitochondrial oxidative stress in aging and healthspan

Dai, D., Chiao, Y. A., Marcinek, D. J., Szeto, H. H., & Rabinovitch, P. S. (2014) · Longevity & Healthspan · doi:10.1186/2046-2395-3-6 · Cited by 481 · see citing works

The Mitochondrial Permeability Transition, Release of Cytochrome c and Cell Death

Petronilli, V., Penzo, D., Scorrano, L., Bernardi, P., & Di Lisa, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010604200 · Cited by 472 · see citing works

The mitochondrial permeability transition: A current perspective on its identity and role in ischaemia/reperfusion injury

Halestrap, A. P., & Richardson, A. P. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.08.018 · Cited by 466 · see citing works

Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization.

Bernardi, P. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50355-6 · Cited by 449 · see citing works

SIRT3 Reverses Aging-Associated Degeneration

Brown, K., Xie, S., Qiu, X., Mohrin, M., Shin, J., Liu, Y., Zhang, D., Scadden, D. T., & Chen, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.005 · Cited by 436 · see citing works

Ryanodine receptor oxidation causes intracellular calcium leak and muscle weakness in aging

Andersson, D. C., Betzenhauser, M. J., Reiken, S., Meli, A. C., Umanskaya, A., Xie, W., Shiomi, T., Zalk, R., Lacampagne, A., & Marks, A. R. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.05.014 · Cited by 424 · see citing works

Mitochondria as a Source of Reactive Oxygen and Nitrogen Species: From Molecular Mechanisms to Human Health

Figueira, T. R., de Barros, M. H., Camargo, A. A., Castilho, R. F., Ferreira, J. C. B., Kowaltowski, A. J., Sluse, F. E., de Souza-Pinto, N. C., & Vercesi, A. E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4729 · Cited by 417 · see citing works

The three ‘P’s of mitophagy: PARKIN.; PINK1.; and post-translational modifications

Durcan, T. M., & Fon, E. A. (2015) · Genes &amp; Development · doi:10.1101/gad.262758.115 · Cited by 400 · see citing works

Membrane phospholipids, lipoxidative damage and molecular integrity: A causal role in aging and longevity

Pamplona, R. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.07.003 · Cited by 387 · see citing works

Nuclear DNA damage signalling to mitochondria in ageing

Fang, E. F., Scheibye-Knudsen, M., Chua, K. F., Mattson, M. P., Croteau, D. L., & Bohr, V. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.14 · Cited by 387 · see citing works

Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition

Woodfield, K., Rück, A., Brdiczka, D. G., & Halestrap, A. P. (1998) · Biochemical Journal · doi:10.1042/bj3360287 · Cited by 386 · see citing works

Mitochondrial stress induces chromatin reorganization to promote longevity and UPR(mt)

Tian, Y., Garcia, G., Bian, Q., Steffen, K. K., Joe, L., Wolff, S., Meyer, B. J., & Dillin, A. (2016) · Cell · doi:10.1016/j.cell.2016.04.011 · Cited by 370 · see citing works

Two conserved histone demethylases regulate mitochondrial stress-induced longevity

Merkwirth, C., Jovaisaite, V., Durieux, J., Matilainen, O., Jordan, S. D., Quiros, P. M., Steffen, K. K., Williams, E. G., Mouchiroud, L., Tronnes, S. U., et al. (2016) · Cell · doi:10.1016/j.cell.2016.04.012 · Cited by 363 · see citing works

Reactive oxygen species and the mitochondrial signaling pathway of cell death.

Bras, M. L., Clément, M.-V., Pervaiz, S., & Brenner, C. (2005) · PubMed · doi:10.14670/hh-20.205 · Cited by 359 · see citing works

Signaling the mitochondrial unfolded protein response

Pellegrino, M. W., Nargund, A. M., & Haynes, C. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.019 · Cited by 359 · see citing works

The overexpression of major antioxidant enzymes does not extend the lifespan of mice

Pérez, V. I., Van Remmen, H., Bokov, A., Epstein, C. J., Vijg, J., & Richardson, A. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2008.00449.x · Cited by 353 · see citing works

Mitochondrial effectors of cellular senescence: beyond the free radical theory of aging

Ziegler, D. V., Wiley, C. D., & Velarde, M. C. (2014) · Aging Cell · doi:10.1111/acel.12287 · Cited by 353 · see citing works

Stem cells and healthy aging

Goodell, M. A., & Rando, T. A. (2015) · Science · doi:10.1126/science.aab3388 · Cited by 347 · see citing works

Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition

Bonora, M., Wieckowski, M. R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., & Pinton, P. (2015) · Oncogene · doi:10.1038/onc.2014.96 · Cited by 330 · see citing works

Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise

Goncalves, R. L. S., Quinlan, C. L., Perevoshchikova, I. V., Hey-Mogensen, M., & Brand, M. D. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.619072 · Cited by 329 · cited 1× · see citing works

Loss of cardioprotection with ageing

Boengler, K., Schulz, R., & Heusch, G. (2009) · Cardiovascular Research · doi:10.1093/cvr/cvp033 · Cited by 328 · see citing works

Mitochondria—Judges and Executioners of Cell Death Sentences

Bhola, P. D., & Letai, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.019 · Cited by 326 · see citing works

Differential expression of adenine nucleotide translocator isoforms in mammalian tissues and during muscle cell differentiation.

Stepien, G., Torroni, A., Chung, A. B., Hodge, J. A., & Wallace, D. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42082-0 · Cited by 325 · see citing works

Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration

Kincaid, B., & Bossy‐Wetzel, E. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00048 · Cited by 314 · see citing works

Function of the SIRT 3 mitochondrial deacetylase in cellular physiology, cancer, and neurodegenerative disease

Ansari, A., Rahman, M. S., Saha, S. K., Saikot, F. K., Deep, A., & Kim, K. (2016) · Aging Cell · doi:10.1111/acel.12538 · Cited by 307 · see citing works

Synaptic Mitochondria Are More Susceptible to Ca2+Overload than Nonsynaptic Mitochondria

Brown, M. R., Sullivan, P. G., & Geddes, J. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510303200 · Cited by 303 · see citing works

Age-dependent cardiomyopathy in mitochondrial mutator mice is attenuated by overexpression of catalase targeted to mitochondria

Dai, D., Chen, T., Wanagat, J., Laflamme, M., Marcinek, D. J., Emond, M. J., Ngo, C. P., Prolla, T. A., & Rabinovitch, P. S. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00581.x · Cited by 280 · see citing works

The sirtuins, oxidative stress and aging: an emerging link

Merksamer, P. I., Liu, Y., He, W., Hirschey, M. D., Chen, D., & Verdin, E. (2013) · Aging · doi:10.18632/aging.100544 · Cited by 275 · 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

Opening of the Mitochondrial Permeability Transition Pore Induces Reactive Oxygen Species Production at the Level of the Respiratory Chain Complex I

Batandier, C., Leverve, X., & Fontaine, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310329200 · Cited by 264 · see citing works

Low rates of hydrogen peroxide production by isolated heart mitochondria associate with long maximum lifespan in vertebrate homeotherms

Lambert, A. J., Boysen, H. M., Buckingham, J. A., Yang, T., Podlutsky, A. J., Austad, S. N., Kunz, T., Buffenstein, R., & Brand, M. D. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00312.x · Cited by 264 · see citing works

When a theory of aging ages badly

Lapointe, J., & Hekimi, S. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0138-8 · Cited by 261 · see citing works

The Mitochondrial Permeability Transition

Halestrap, A. P. (2002) · Springer eBooks · doi:10.1007/978-3-642-58268-4_12 · Cited by 260 · see citing works

Mitochondrial dysfunction and longevity in animals: Untangling the knot

Wang, Y., & Hekimi, S. (2015) · Science · doi:10.1126/science.aac4357 · Cited by 248 · see citing works

Cell Senescence: Role in Aging and Age-Related Diseases

Campisi, J., & Robert, L. (2014) · Interdisciplinary Topics in Gerontology and Geriatrics · doi:10.1159/000358899 · Cited by 240 · see citing works

Mitochondrial permeability transition pore in Alzheimer's disease: Cyclophilin D and amyloid beta

Du, H., & Yan, S. S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.005 · Cited by 235 · see citing works

The Mitochondrial Permeability Transition Pore is Modulated by Oxidative Agents Through Both Pyridine Nucleotides and Glutathione at Two Separate Sites

Chernyak, B. V., & Bernardi, P. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0623w.x · Cited by 233 · see citing works

Mitochondrial Ca2+ Uniporter Is a Mitochondrial Luminal Redox Sensor that Augments MCU Channel Activity

Dong, Z., Shanmughapriya, S., Tomar, D., Siddiqui, N., Lynch, S., Nemani, N., Breves, S. L., Zhang, X., Tripathi, A., Palaniappan, P., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.01.032 · Cited by 233 · see citing works

MICU1 Serves as a Molecular Gatekeeper to Prevent In Vivo Mitochondrial Calcium Overload

Liu, J. C., Liu, J., Holmström, K. M., Menazza, S., Parks, R. J., Fergusson, M. M., Yu, Z., Springer, D., Halsey, C., Liu, C., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.011 · Cited by 222 · see citing works

Mitochondrial Ca2+ and regulation of the permeability transition pore

Hurst, S., Hoek, J. B., & Sheu, S. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9672-x · Cited by 220 · see citing works

Increased sensitivity to mitochondrial permeability transition and myonuclear translocation of endonuclease G in atrophied muscle of physically active older humans

Gouspillou, G., Sgarioto, N., Kapchinsky, S., Purves‐Smith, F., Norris, B., Pion, C. H., Barbat‐Artigas, S., Lemieux, F., Taivassalo, T., Morais, J. A., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-242750 · Cited by 217 · see citing works

Mitochondrial reactive oxygen species and inflammation: Molecular mechanisms, diseases and promising therapies

Rimessi, A., Previati, M., Nigro, F., Wieckowski, M. R., & Pinton, P. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.06.015 · Cited by 210 · see citing works

The Mitochondrial Permeability Transition Pore and Cancer: Molecular Mechanisms Involved in Cell Death

Bonora, M., & Pinton, P. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00302 · Cited by 208 · see citing works

Metformin protects the ischemic heart by the Akt-mediated inhibition of mitochondrial permeability transition pore opening

Bhamra, G. S., Hausenloy, D. J., Davidson, S. M., Carr, R. D., Paiva, M. S. A., Wynne, A. M., Mocanu, M. M., & Yellon, D. M. (2007) · Basic Research in Cardiology · doi:10.1007/s00395-007-0691-y · Cited by 207 · see citing works

MICU1 regulation of mitochondrial Ca2+ uptake dictates survival and tissue regeneration

Antony, A. N., Paillard, M., Moffat, C., Juskeviciute, E., Correnti, J., Bolon, B., Rubin, E., Csordás, G., Seifert, E. L., Hoek, J. B., et al. (2016) · Nature Communications · doi:10.1038/ncomms10955 · Cited by 206 · see citing works

Mitochondrial Permeability Transition: New Findings and Persisting Uncertainties

Izzo, V., Bravo-San Pedro, J. M., Sica, V., Kroemer, G., & Galluzzi, L. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.04.006 · Cited by 205 · see citing works

Mitochondrial and Cytoplasmic ROS Have Opposing Effects on Lifespan

Schaar, C. E., Dues, D. J., Spielbauer, K. K., Machiela, E., Cooper, J. F., Senchuk, M., Hekimi, S., & Van Raamsdonk, J. M. (2015) · PLOS Genetics · doi:10.1371/journal.pgen.1004972 · Cited by 203 · see citing works

Tissue-Specific Mitochondrial Decoding of Cytoplasmic Ca2+ Signals Is Controlled by the Stoichiometry of MICU1/2 and MCU

Paillard, M., Csordás, G., Szanda, G., Golenár, T., Debattisti, V., Bartók, Á., Wang, N., Moffat, C., Seifert, E. L., Spät, A., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.032 · Cited by 194 · see citing works

The Mitochondrial Free Radical Theory of Aging

Barja, G. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00001-5 · Cited by 193 · see citing works

Cysteine 203 of Cyclophilin D Is Critical for Cyclophilin D Activation of the Mitochondrial Permeability Transition Pore

Nguyen, T. T. M., Stevens, M. V., Kohr, M. J., Steenbergen, C., Sack, M. N., & Murphy, E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243469 · Cited by 189 · see citing works

A new role for oxidative stress in aging: The accelerated aging phenotype in Sod1-/- mice is correlated to increased cellular senescence

Zhang, Y., Unnikrishnan, A., Deepa, S. S., Liu, Y., Li, Y., Ikeno, Y., Sosnowska, D., Van Remmen, H., & Richardson, A. (2017) · Redox Biology · doi:10.1016/j.redox.2016.10.014 · Cited by 185 · see citing works

Mitochondrial dysfunction and intracellular calcium dysregulation in ALS

Kawamata, H., & Manfredi, G. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.05.003 · Cited by 173 · see citing works

Age-related activation of mitochondrial caspase-independent apoptotic signaling in rat gastrocnemius muscle

Marzetti, E., Wohlgemuth, S. E., Lees, H. A., Chung, H.-Y., Giovannini, S., & Leeuwenburgh, C. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2008.05.005 · Cited by 172 · see citing works

Phosphate Is Essential for Inhibition of the Mitochondrial Permeability Transition Pore by Cyclosporin A and by Cyclophilin D Ablation

Basso, E., Petronilli, V., Forte, M. A., & Bernardi, P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800132200 · Cited by 167 · see citing works

Biology of Mitochondria in Neurodegenerative Diseases

Martin, L. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00005-9 · Cited by 162 · see citing works

Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis

Tomasello, F., Messina, A., Lartigue, L., Schembri, L., Medina, C., Reina, S., Thoraval, D., Crouzet, M., Ichas, F., De Pinto, V., et al. (2009) · Cell Research · doi:10.1038/cr.2009.98 · Cited by 161 · see citing works

Low levels of lipid oxidation radically increase the passive permeability of lipid bilayers

Runas, K. A., & Malmstadt, N. (2014) · Soft Matter · doi:10.1039/c4sm01478b · Cited by 161 · see citing works

Signaling networks determining life span

Riera, C. E., Merkwirth, C., De Magalhaes Filho, C. D., & Dillin, A. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014451 · Cited by 161 · see citing works

Oxidative damage to mitochondria is mediated by the Ca2+-dependent inner-membrane permeability transition

Takeyama, N., Matsuo, N., & Tanaka, T. (1993) · Biochemical Journal · doi:10.1042/bj2940719 · Cited by 149 · see citing works

Metformin inhibits mitochondrial permeability transition and cell death: a pharmacological in vitro study

Guigas, B., Détaille, D., Chauvin, C., Batandier, C., Oliveira, F. D., Fontaine, E. M., & Leverve, X. M. (2004) · Biochemical Journal · doi:10.1042/bj20040885 · Cited by 148 · see citing works

Alterations in intrinsic mitochondrial function with aging are fiber type‐specific and do not explain differential atrophy between muscles

Picard, M. A., Ritchie, D., Thomas, M. M., Wright, K. J., & Hepple, R. T. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00745.x · Cited by 145 · see citing works

The permeability transition in heart mitochondria is regulated synergistically by ADP and cyclosporin A.

Novgorodov, S. A., Gudz, T. I., Milgrom, Y. M., & Brierley, G. P. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41996-5 · Cited by 144 · see citing works

Mitoflash frequency in early adulthood predicts lifespan in Caenorhabditis elegans

Shen, E.-Z., Song, C.-Q., Lin, Y., Zhang, W.-H., Su, P.-F., Liu, W.-Y., Zhang, P., Xu, J., Lin, N., Zhan, C., et al. (2014) · Nature · doi:10.1038/nature13012 · Cited by 139 · see citing works

Mitochondrial function and myocardial aging. A critical analysis of the role of permeability transition

DILISA, F., & BERNARDI, P. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.02.009 · Cited by 139 · see citing works

Interaction of peroxidized cardiolipin with rat‐heart mitochondrial membranes: Induction of permeability transition and cytochrome <i>c</i> release

Petrosillo, G., Casanova, G., Matera, M., Ruggiero, F. M., & Paradies, G. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.036 · Cited by 137 · see citing works

Aging Enhances the Activation of the Permeability Transition Pore in Mitochondria

Mather, M. W., & Rottenberg, H. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2994 · Cited by 134 · see citing works

Roles for ROS and hydrogen sulfide in the longevity response to germline loss in Caenorhabditis elegans

Wei, Y., & Kenyon, C. J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1524727113 · Cited by 131 · see citing works

Relationship between Metabolic Rate, Free Radicals, Differentiation and Aging: A Unified Theory

Sohal, R. S., & Allen, R. G. (1985) · Springer eBooks · doi:10.1007/978-1-4899-2218-2_4 · Cited by 129 · see citing works

Effect of Cytochrome c on the Generation and Elimination of O<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" altimg="si1.gif"><mml:msubsup><mml:mrow/><mml:mrow><mml:mn>2</mml:mn></mml:mrow><mml:mrow><mml:mo>⨪</mml:mo></mml:mrow></mml:msubsup></mml:math> and H2O2 in Mitochondria

Zhao, Y., Wang, Z.-B., & Xu, J.-X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209681200 · Cited by 129 · see citing works

The mitochondrial permeability transition pore in AD 2016: An update

Biasutto, L., Azzolini, M., Szabó, I., & Zoratti, M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.02.012 · Cited by 128 · see citing works

Inhibition of myocardial reperfusion injury by ischemic postconditioning requires sirtuin 3-mediated deacetylation of cyclophilin D

Bochaton, T., Silva, C. C. D., Pillot, B., Villedieu, C., Ferreras, L., Alam, M. R., Thibault, H., Strina, M., Gharib, A., Ovize, M., et al. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.03.017 · Cited by 126 · see citing works

The ‘mitoflash’ probe cpYFP does not respond to superoxide

Schwarzländer, M., Wagner, S., Ermakova, Y. G., Belousov, V. V., Radí, R., Beckman, J. S., Buettner, G. R., Demaurex, N., Duchen, M. R., Forman, H. J., et al. (2014) · Nature · doi:10.1038/nature13858 · Cited by 125 · see citing works

Redox modification of ryanodine receptors by mitochondria‐derived reactive oxygen species contributes to aberrant Ca2+ handling in ageing rabbit hearts

Cooper, L. L., Li, W., Lu, Y., Centracchio, J. N., Terentyeva, R., Koren, G., & Terentyev, D. A. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.260521 · Cited by 125 · see citing works

Erastin Disrupts Mitochondrial Permeability Transition Pore (mPTP) and Induces Apoptotic Death of Colorectal Cancer Cells

Huo, H., Zhou, Z., Qin, J., Liu, W., Wang, B., & Gu, Y. (2016) · PLOS ONE · doi:10.1371/journal.pone.0154605 · Cited by 125 · see citing works

Nrf2 protects mitochondrial decay by oxidative stress

Strom, J. G., Xu, B., Tian, X., & Chen, Q. M. (2015) · The FASEB Journal · doi:10.1096/fj.14-268904 · Cited by 124 · see citing works

The mitochondrial permeability transition pore regulates Parkinson's disease development in mutant α-synuclein transgenic mice

Martin, L. J., Semenkow, S., Hanaford, A. R., & Wong, M. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.11.008 · Cited by 123 · see citing works

Defective sarcoplasmic reticulum–mitochondria calcium exchange in aged mouse myocardium

Fernández‐Sanz, C., Ruiz‐Meana, M., Miró‐Casas, E., Núñez, E., Castellano, J., Loureiro, M., Barba, I., Poncelas, M., Rodríguez‐Sinovas, A., Vázquez, J., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.526 · Cited by 118 · see citing works

DNA repair and aging: The impact of the p53 family

Nicolai, S., Rossi, A., Di Daniele, N., Melino, G., Annicchiarico-Petruzzelli, M., & Raschellà, G. (2015) · Aging · doi:10.18632/aging.100858 · Cited by 118 · see citing works

Opening of the mitochondrial permeability transition pore links mitochondrial dysfunction to insulin resistance in skeletal muscle

Taddeo, E. P., Laker, R. C., Breen, D. S., Akhtar, Y., Kenwood, B. M., Liao, J. A., Zhang, M., Fazakerley, D. J., Tomsig, J. L., Harris, T. E., et al. (2013) · Molecular Metabolism · doi:10.1016/j.molmet.2013.11.003 · Cited by 116 · see citing works

P53 Dependent Mitochondrial Permeability Transition Pore Opening Is Required for Dexamethasone‐Induced Death of Osteoblasts

Zhen, Y.-F., Wang, G., Zhu, L., Tan, S., Zhang, F., Zhou, X., & Wang, X. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24589 · Cited by 116 · see citing works

Mitochondrial permeability transition pore induces mitochondria injury in Huntington disease

Quintanilla, R. A., Jin, Y. N., Rommy von Bernhardi, M., & Johnson, G. V. W. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-45 · Cited by 114 · see citing works

From ATP to PTP and Back

Bernardi, P., Lisa, F. D., Fogolari, F., & Lippe, G. (2015) · Circulation Research · doi:10.1161/circresaha.115.306557 · Cited by 113 · see citing works

Complex IV-deficient Surf1−/− mice initiate mitochondrial stress responses

Pulliam, D. A., Deepa, S. S., Liu, Y., Hill, S., Lin, A., Bhattacharya, A., Shi, Y., Sloane, L. B., Viscomi, C. F., Zeviani, M., et al. (2014) · Biochemical Journal · doi:10.1042/bj20140291 · Cited by 108 · see citing works

Sirt3, Mitochondrial ROS, Ageing, and Carcinogenesis

Park, S., Özden, Ö., Jiang, H., Cha, Y. I., Pennington, J. D., Aykin‐Burns, N., Spitz, D. R., Gius, D. R., & Kim, H. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12096226 · Cited by 107 · see citing works

A cardiac mitochondrial cAMP signaling pathway regulates calcium accumulation, permeability transition and cell death

Wang, Z., Liu, D., Varin, A., Nicolas, V, Courilleau, D., Mateo, P., Caubere, C., Rouet, P., Gomez, A.-M., Vandecasteele, G., et al. (2016) · Cell Death &amp; Disease · doi:10.1038/cddis.2016.106 · Cited by 106 · see citing works

ROS‐Mediated PARP Activity Undermines Mitochondrial Function After Permeability Transition Pore Opening During Myocardial Ischemia–Reperfusion

Schriewer, J. M., Peek, C. B., Bass, J. T., & Schumacker, P. T. (2013) · Journal of the American Heart Association · doi:10.1161/jaha.113.000159 · Cited by 103 · see citing works

Mitochondrial aquaporin-8 knockdown in human hepatoma HepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability

Marchissio, M. J., Francés, D. E., Carnovale, C. E., & Marinelli, R. A. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.08.005 · Cited by 102 · see citing works

Mitochondrial calcium uniporter regulator 1 (MCUR1) regulates the calcium threshold for the mitochondrial permeability transition

Chaudhuri, D., Artiga, D. J., Abiria, S. A., & Clapham, D. E. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1602264113 · Cited by 102 · see citing works

Age‐Dependent Changes in the Calcium Sensitivity of Striatal Mitochondria in Mouse Models of Huntington's Disease

Brustovetsky, N., LaFrance, R., Purl, K. J., Brustovetsky, T., Keene, C. D., Low, W. C., & Dubinsky, J. M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03036.x · Cited by 101 · see citing works

Mitochondria and aging: A role for the permeability transition?

Crompton, M. (2004) · Aging Cell · doi:10.1046/j.1474-9728.2003.00073.x · Cited by 101 · see citing works

How do reactive oxygen species and calcium trigger mitochondrial membrane permeabilisation?

Tajeddine, N. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.02.013 · Cited by 101 · see citing works

Increased calcium vulnerability of senescent cardiac mitochondria: protective role for a mitochondrial potassium channel opener

Jahangir, A., Özcan, C., Holmuhamedov, E., & Terzic, A. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00242-1 · Cited by 100 · see citing works

Selective Inhibition of the Mitochondrial Permeability Transition Pore Protects against Neurodegeneration in Experimental Multiple Sclerosis

Warne, J., Pryce, G., Hill, J. M., Shi, X., Lennerås, F., Puentes, F., Kip, M., Hilditch, L., Walker, P., Simone, M. I., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.700385 · Cited by 99 · see citing works

Stress Regulates Aquaporin-8 Permeability to Impact Cell Growth and Survival

Medraño-Fernández, I., Bestetti, S., Bertolotti, M., Bienert, G. P., Bottino, C., Laforenza, U., Rubartelli, A., & Sitia, R. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6636 · Cited by 97 · see citing works

Caloric restriction increases brain mitochondrial calcium retention capacity and protects against excitotoxicity

Amigo, I., Menezes‐Filho, S. L., Luévano‐Martínez, L. A., Chausse, B., & Kowaltowski, A. J. (2017) · Aging Cell · doi:10.1111/acel.12527 · Cited by 95 · see citing works

Antioxidants reveal an inverted U‐shaped dose‐response relationship between reactive oxygen species levels and the rate of aging in Caenorhabditis elegans

Desjardins, D., Cacho‐Valadez, B., Liu, J., Wang, Y., Yee, C. S., Bernard, K., Khaki, A., Breton, L., & Hekimi, S. (2016) · Aging Cell · doi:10.1111/acel.12528 · Cited by 94 · see citing works

The mitochondrial permeability transition pore and its adaptive responses in tumor cells

Rasola, A., & Bernardi, P. (2014) · Cell Calcium · doi:10.1016/j.ceca.2014.10.003 · Cited by 91 · see citing works

Mitochondrial aquaporin-8-mediated hydrogen peroxide transport is essential for teleost spermatozoon motility

Chauvigné, F., Boj, M., Finn, R. N., et al. (2015) · Scientific Reports · doi:10.1038/srep07789 · Cited by 90 · see citing works

Cell culture-based profiling across mammals reveals DNA repair and metabolism as determinants of species longevity

Ma, S., Upneja, A., Galecki, A., Tsai, Y.-M., Burant, C. F., Raskind, S., Zhang, Q., Zhang, Z. D., Seluanov, A., Gorbunova, V., et al. (2016) · eLife · doi:10.7554/elife.19130 · Cited by 89 · see citing works

Mitochondria-targeted ROS scavenger improves post-ischemic recovery of cardiac function and attenuates mitochondrial abnormalities in aged rats

Escobales, N., Nuñez, R. E., Jang, S., Parodi‐Rullán, R. M., Ayala‐Peña, S., Sacher, J. R., Skoda, E. M., Wipf, P., Frontera, W. R., & Javadov, S. A. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.10.009 · Cited by 88 · see citing works

Bioenergetics and permeability transition pore opening in heart subsarcolemmal and interfibrillar mitochondria: Effects of aging and lifelong calorie restriction

Hofer, T., Servais, S., Seo, A. Y., Marzetti, E., Hiona, A., Upadhyay, S. J., Wohlgemuth, S. E., & Leeuwenburgh, C. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.01.004 · Cited by 87 · see citing works

Cyclophilin D Knock-Out Mice Show Enhanced Resistance to Osteoporosis and to Metabolic Changes Observed in Aging Bone

Shum, L. C., White, N., Nadtochiy, S. M., Bentley, K. L. D. M., Brookes, P. S., Jonason, J. H., & Eliseev, R. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155709 · Cited by 85 · see citing works

A midlife crisis for the mitochondrial free radical theory of aging

Stuart, J. A., Maddalena, L. A., Merilovich, M., & Robb, E. L. (2014) · Longevity & Healthspan · doi:10.1186/2046-2395-3-4 · Cited by 84 · see citing works

Exercise mitigates mitochondrial permeability transition pore and quality control mechanisms alterations in nonalcoholic steatohepatitis

Gonçalves, I. O., Passos, E., Diogo, C. V., Rocha‐Rodrigues, S., Alves, E. S., Oliveira, P. J., Ascensão, A. A. M. R., & Magalhães, J. (2015) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2015-0470 · Cited by 84 · see citing works

Brain Region-Specific, Age-Related, Alterations in Mitochondrial Responses to Elevated Calcium

Brown, M. R., Geddes, J. W., & Sullivan, P. G. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041775.10388.23 · Cited by 82 · see citing works

Complex I generated, mitochondrial matrix-directed superoxide is released from the mitochondria through voltage dependent anion channels

Lustgarten, M. S., Bhattacharya, A., Müller, F. L., Jang, Y. C., Shimizu, T., Shirasawa, T., Richardson, A. G., & Remmen, H. V. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.05.055 · Cited by 82 · see citing works

Brain cortex mitochondrial bioenergetics in synaptosomes and non-synaptic mitochondria during aging

Lores‐Arnaiz, S., Lombardi, P., Karadayian, A. G., Orgambide, F., Cicerchia, D., & Bustamante, J. (2016) · Neurochemical Research · doi:10.1007/s11064-015-1817-5 · Cited by 81 · see citing works

Complex I and complex III inhibition specifically increase cytosolic hydrogen peroxide levels without inducing oxidative stress in HEK293 cells

Forkink, M., Basit, F., Teixeira, J., Swarts, H. G. P., Koopman, W. J. H., & Willems, P. H. G. M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.09.003 · Cited by 80 · see citing works

HAX-1 regulates cyclophilin-D levels and mitochondria permeability transition pore in the heart

Lam, C. K., Zhao, W., Liu, G.-S., Cai, W.-F., Gardner, G., Adly, G., & Kranias, E. G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1508760112 · Cited by 80 · see citing works

Mitochondrial Dysfunction in Lymphocytes from Old Mice: Enhanced Activation of the Permeability Transition

Rottenberg, H., & Wu, S. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7605 · Cited by 79 · see citing works

Mitochondrial permeability transition pore: a promising target for the treatment of Parkinson’s disease

Rasheed, M. Z., Tabassum, H., & Parvez, S. (2016) · PROTOPLASMA · doi:10.1007/s00709-015-0930-2 · Cited by 79 · see citing works

Comprehensive analysis of mitochondrial permeability transition pore activity in living cells using fluorescence-imaging-based techniques

Bonora, M., Morganti, C., Morciano, G., Giorgi, C., Wieckowski, M. R., & Pinton, P. (2016) · Nature Protocols · doi:10.1038/nprot.2016.064 · Cited by 79 · see citing works

In vitro aging promotes endoplasmic reticulum (ER)-mitochondria Ca 2+ cross talk and loss of store-operated Ca 2+ entry (SOCE) in rat hippocampal neurons

Calvo-Rodríguez, M., García-Durillo, M., Villalobos, C., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.08.001 · Cited by 78 · see citing works

Increased susceptibility to Ca 2+ ‐induced permeability transition and to cytochrome c release in rat heart mitochondria with aging: effect of melatonin

Petrosillo, G., Moro, N., Paradies, V., Ruggiero, F. M., & Paradies, G. (2010) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2010.00758.x · Cited by 73 · see citing works

Cyclophilin D Promotes Brain Mitochondrial F1FO ATP Synthase Dysfunction in Aging Mice

Gauba, E., Guo, L., & Du, H. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160822 · Cited by 73 · see citing works

Exercise training induces respiratory substrate-specific decrease in Ca²⁺-induced permeability transition pore opening in heart mitochondria

Marcil, M., Bourduas, K., Ascah, A., & Burelle, Y. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00913.2005 · Cited by 71 · see citing works

Decreased mitochondrial bioenergetics and calcium buffering capacity in the basal ganglia correlates with motor deficits in a nonhuman primate model of aging

Pandya, J. D., Grondin, R., Yonutas, H. M., Haghnazar, H., Gash, D. M., Zhang, Z., & Sullivan, P. G. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.01.018 · Cited by 70 · see citing works

Mitochondrial Flash: Integrative Reactive Oxygen Species and pH Signals in Cell and Organelle Biology

Wang, W., Gong, G., Wang, X., Wei‐LaPierre, L., Cheng, H., Dirksen, R. T., & Sheu, S. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6739 · Cited by 70 · see citing works

Influence of aging on membrane permeability transition in brain mitochondria

Toman, J., & Fiskum, G. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9337-8 · Cited by 69 · see citing works

Mitochondrial flashes: new insights into mitochondrial ROS signalling and beyond

Hou, T., Wang, X., Ma, Q., & Cheng, H. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.275735 · Cited by 68 · see citing works

Endurance training reverts heart mitochondrial dysfunction.; permeability transition and apoptotic signaling in long-term severe hyperglycemia

Lumini-Oliveira, J., Magalhães, J., Pereira, C. V., Moreira, A. C., Oliveira, P. J., & Ascensão, A. (2011) · Mitochondrion · doi:10.1016/j.mito.2010.07.005 · Cited by 66 · see citing works

A respiratory chain controlled signal transduction cascade in the mitochondrial intermembrane space mediates hydrogen peroxide signaling

Patterson, H. C., Gerbeth, C., Thiru, P., Vögtle, F. ‐., Knoll, M., Shahsafaei, A., Samocha, K. E., Huang, C. X., Harden, M. M., Song, R., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517932112 · Cited by 66 · see citing works

New aspects of p66Shc in ischaemia reperfusion injury and other cardiovascular diseases

Lisa, F. D., Giorgio, M., Ferdinándy, P., & Schulz, R. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13478 · Cited by 66 · see citing works

Mitochondrial Membrane Potential in Aging Cells

Sugrue, M. M., & Tatton, W. G. (2001) · Neurosignals · doi:10.1159/000046886 · Cited by 65 · see citing works

Permeability transition pore-mediated mitochondrial superoxide flashes mediate an early inhibitory effect of amyloid beta1−42 on neural progenitor cell proliferation

Hou, Y., Ghosh, P., Wan, R., Ouyang, X., Cheng, H., Mattson, M. P., & Cheng, A. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.11.002 · Cited by 65 · see citing works

GNX-4728, a novel small molecule drug inhibitor of mitochondrial permeability transition, is therapeutic in a mouse model of amyotrophic lateral sclerosis

Martin, L. J., Fancelli, D., Wong, M., Niedzwiecki, M. V., Ballarini, M., Plyte, S. E., & Chang, Q. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00433 · Cited by 63 · see citing works

Redox Sensitivities of Global Cellular Cysteine Residues under Reductive and Oxidative Stress

Araki, K., Kusano, H., Sasaki, N., Tanaka, R., Hatta, T., Fukui, K., & Natsume, T. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00087 · Cited by 63 · see citing works

Mitochondrial-Targeted Catalase

Dai, D., Chiao, Y. A., Martin, G. M., Marcinek, D. J., Basisty, N., Quarles, E. K., & Rabinovitch, P. S. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2016.12.015 · Cited by 62 · see citing works

The mitochondrial unfolded protein response and increased longevity: Cause, consequence, or correlation?

Bennett, C. F., & Kaeberlein, M. R. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.02.002 · Cited by 61 · see citing works

Reversal of Aging-Related Neuronal Ca2+ Dysregulation and Cognitive Impairment by Delivery of a Transgene Encoding FK506-Binding Protein 12.6/1b to the Hippocampus

Gant, J. C., Chen, K.-C., Kadish, I., Blalock, E. M., Thibault, O., Porter, N. M., & Landfield, P. W. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1248-15.2015 · Cited by 60 · see citing works

Analysis of oxygen consumption and mitochondrial permeability with age in mice

Goodell, S., & Cortopassi, G. A. (1998) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(97)00182-6 · Cited by 59 · see citing works

Mitochondrial Permeability Transition Pore Component Cyclophilin D Distinguishes Nigrostriatal Dopaminergic Death Paradigms in the MPTP Mouse Model of Parkinson's Disease

Thomas, B., Banerjee, R., Starkova, N. N., Zhang, S. F., Calingasan, N. Y., Yang, L., Wille, E. J., Lorenzo, B. J., Ho, D. J., Beal, M. F., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3849 · Cited by 57 · see citing works

Regulation of Ca2+ transport in brain mitochondria. II. The mechanism of the adenine nucleotides enhancement of Ca2+ uptake and retention

Rottenberg, H., & Marbach, M. (1990) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(90)90010-2 · Cited by 56 · see citing works

Changes in the mitochondrial permeability transition pore in aging and age-associated diseases

Paradies, G., Paradies, V., Ruggiero, F. M., & Petrosillo, G. (2012) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2012.12.006 · Cited by 56 · see citing works

Cyclophilin D links programmed cell death and organismal aging in Podospora anserina

Brust, D., Daum, B., Breunig, C., Hamann, A., Kühlbrandt, W., & Osiewacz, H. D. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00609.x · Cited by 54 · see citing works

Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State

Folda, A., Citta, A., Scalcon, V., Calí, T., Zonta, F., Scutari, G., Bindoli, A., & Rigobello, M. P. (2016) · Scientific Reports · doi:10.1038/srep23071 · Cited by 54 · see citing works

F1F0 ATP Synthase–Cyclophilin D Interaction Contributes to Diabetes-Induced Synaptic Dysfunction and Cognitive Decline

Yan, S., Wu, L., Wu, L., Zhong, C., Zhong, C., Yu, Q., Wang, Y., Lue, L., Douglas, J. T., Douglas, J. T., et al. (2016) · Diabetes · doi:10.2337/db16-0556 · Cited by 54 · see citing works

Altered FoF1 ATP synthase and susceptibility to mitochondrial permeability transition pore during ischaemia and reperfusion in aging cardiomyocytes

Fernández‐Sanz, C., Castellano, J. M., Miró‐Casas, E., Núñez, E., Inserte, J., Vázquez, J., David Garcia-dorado, A., & Ruiz‐Meana, M. (2015) · Thrombosis and Haemostasis · doi:10.1160/th14-10-0901 · Cited by 53 · see citing works

Age‐related changes in regional brain mitochondria from Fischer 344 rats

LaFrance, R., Brustovetsky, N., Sherburne, C., DeLong, D., & Dubinsky, J. M. (2005) · Aging Cell · doi:10.1111/j.1474-9726.2005.00156.x · Cited by 51 · see citing works

Cyclosporin a Increases Mitochondrial Calcium Uptake Capacity in Cortical Astrocytes but not Cerebellar Granule Neurons

Bambrick, L. L., Chandrasekaran, K., Mehrabian, Z., Wright, C. L., Krueger, B. K., & Fiskum, G. M. (2006) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9004-7 · Cited by 51 · see citing works

In aging, the vulnerability of rat brain mitochondria is enhanced due to reduced level of 2′,3′-cyclic nucleotide-3′-phosphodiesterase (CNP) and subsequently increased permeability transition in brain mitochondria in old animals

Krestinina, O. V., Azarashvili, T., Baburina, Y. L., Galvita, A., Grachev, D., Stricker, R., & Reiser, G. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.09.008 · Cited by 48 · see citing works

Expression of SIRT1 and SIRT3 varies according to age in mice

Kwon, Y.-H., Kim, J., Lee, C.-Y., & Kim, H. (2015) · Anatomy & Cell Biology · doi:10.5115/acb.2015.48.1.54 · Cited by 48 · see citing works

Bcl-xL in neuroprotection and plasticity

Jonas, E. A., Porter, G. A., Jr., & Alavian, K. N. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00355 · Cited by 48 · see citing works

A Novel In Vitro CypD-Mediated p53 Aggregation Assay Suggests a Model for Mitochondrial Permeability Transition by Chaperone Systems

Lebedev, I., Nemajerová, A., Foda, Z. H., Kornaj, M., Tong, M., Moll, U. M., & Seeliger, M. A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.001 · Cited by 47 · see citing works

The P66Shc/mitochondrial permeability transition pore pathway determines neurodegeneration

Savino, C., Pelicci, P., & Giorgio, M. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/719407 · Cited by 46 · see citing works

Hsp90 regulation of mitochondrial protein folding: from organelle integrity to cellular homeostasis

Altieri, D. C. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1177-0 · Cited by 46 · see citing works

Identification of a Small Molecule Cyclophilin D Inhibitor for Rescuing Aβ-Mediated Mitochondrial Dysfunction

Valasani, K. R., Sun, Q., Du, F., Zhang, Z., Yu, Q., Guo, Y., Li, J., Roy, A., & Yan, S. S. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00451 · Cited by 45 · see citing works

Enhanced oxidative stress sensitizes the mitochondrial permeability transition pore to opening in heart from Zucker Fa/fa rats with type 2 diabetes

Riojas-Hernández, A., Bernal‐Ramírez, J., Rodríguez-Mier, D., Morales, E., Domínguez-Barragán, E. M., Borja-Villa, C., Rivera-Álvarez, I., García‐Rivas, G., Altamirano, J., & Garcı́a, N. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.09.018 · Cited by 43 · see citing works

Age-Associated Differences in Activation of Akt/GSK-3 Signaling Pathways and Inhibition of Mitochondrial Permeability Transition Pore Opening in the Rat Heart

Zhu, J., Rebecchi, M. J., Tan, M., Glass, P. S. A., Brink, P. R., & Liu, L. (2010) · The Journals of Gerontology Series A · doi:10.1093/gerona/glq035 · Cited by 42 · see citing works

Possible role of mitochondrial permeability transition pore in the pathogenesis of Huntington disease

Quintanilla, R. A., Tapia‐Rojas, C., & Maria Jose Perez, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.054 · Cited by 42 · see citing works

Mitochondrial 2′, 3′-cyclic nucleotide 3′-phosphodiesterase (CNP) interacts with mPTP modulators and functional complexes (I–V) coupled with release of apoptotic factors

Baburina, Y. L., Azarashvili, T., Grachev, D., Krestinina, O. V., Galvita, A., Stricker, R., & Reiser, G. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2015.07.012 · Cited by 39 · see citing works

The inhibition of calcium signaling in T lymphocytes from old mice results from enhanced activation of the mitochondrial permeability transition pore

Mather, M. W., & Rottenberg, H. (2002) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00416-x · Cited by 39 · see citing works

Permeability Transition Pore-Mediated Mitochondrial Superoxide Flashes Regulate Cortical Neural Progenitor Differentiation

Hou, Y., Mattson, M. P., & Cheng, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076721 · Cited by 39 · see citing works

Exogenous hydrogen sulfide restores cardioprotection of ischemic post-conditioning via inhibition of mPTP opening in the aging cardiomyocytes

Li, H., Zhang, C., Sun, W., Li, L., Wu, B., 白淑芝, Li, H., Zhong, X., Wang, R., Wu, L., et al. (2015) · Cell & Bioscience · doi:10.1186/s13578-015-0035-9 · Cited by 39 · see citing works

Involvement of mitochondrial permeability transition pore (mPTP) in cardiac arrhythmias: Evidence from cyclophilin D knockout mice

Gordan, R., Fefelova, N., Gwathmey, J. K., & Xie, L. (2016) · Cell Calcium · doi:10.1016/j.ceca.2016.09.001 · Cited by 37 · see citing works

Forty years later: Mitochondria as therapeutic targets in muscle diseases

Zulian, A., Schiavone, M., Giorgio, V., & Bernardi, P. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.09.043 · Cited by 37 · see citing works

Alterations in voltage-sensing of the mitochondrial permeability transition pore in ANT1-deficient cells

Dóczi, J., Törőcsik, B., Echaniz‐Laguna, A., de Camaret, B. M., Starkov, A. A., Starkova, N. N., Gál, A., Molnár, M. J., Kawamata, H., Manfredi, G., et al. (2016) · Scientific Reports · doi:10.1038/srep26700 · Cited by 36 · see citing works

Dietary Restriction Augments Protection Against Induction of the Mitochondrial Permeability Transition

Kristal, B. S., & Yu, B. P. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00444-9 · Cited by 35 · see citing works

Modulation of mitochondrial ion transport by inorganic polyphosphate - essential role in mitochondrial permeability transition pore

Baev, A. Y., Negoda, A. E., & Abramov, A. Y. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9650-3 · Cited by 35 · see citing works

Transgenic overexpression of adenine nucleotide translocase 1 protects ischemic hearts against oxidative stress

Klumpe, I., Savvatis, K., Westermann, D., Tschöpe, C., Rauch, U., Landmesser, U., Schultheiss, H.-P., & Dörner, A. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1413-4 · Cited by 35 · see citing works

Cyclophilin D is expressed predominantly in mitochondria of γ‐aminobutyric acidergic interneurons

Hazelton, J. L., Petrasheuskaya, M., Fiskum, G. M., & Kristián, T. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21921 · Cited by 34 · see citing works

Age-associated differences in the inhibition of mitochondrial permeability transition pore opening by cyclosporine A

Liu, L., ZHU, J., Brink, P. R., Glass, P. S. A., & Rebecchi, M. J. (2011) · Acta Anaesthesiologica Scandinavica · doi:10.1111/j.1399-6576.2011.02421.x · Cited by 32 · see citing works

Lipopolysaccharide Induces CD38 Expression and Solubilization in J774 Macrophage Cells

Lee, C.-U., Song, E., Yoo, C.-H., Kwak, Y.-K., & Han, M. (2012) · Molecules and Cells · doi:10.1007/s10059-012-0263-3 · Cited by 32 · see citing works

Mitochondrial dysfunction in cell senescence and aging

Miwa, S., Kashyap, S., Chini, E., & von Zglinicki, T. (2022) · Journal of Clinical Investigation · doi:10.1172/jci158447 · Cited by 1,061 · see citing works

Targeting mitochondria-located circrna scar alleviates nash via reducing mros output

Zhao, Q., Liu, J., Deng, H., Ma, R., Liao, J.-Y., Liang, H., Hu, J., Li, J., Guo, Z., Cai, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.009 · Cited by 469 · see citing works

Mitochondrial Permeability Uncouples Elevated Autophagy and Lifespan Extension

Zhou, B., Kreuzer, J., Kumsta, C., Wu, L., Kamer, K. J., Cedillo, L., Zhang, Y., Li, S., Kacergis, M. C., Webster, C. M., et al. (2019) · Cell · doi:10.1016/j.cell.2019.02.013 · Cited by 220 · see citing works

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

Advanced oxidation protein products induce pre‐osteoblast apoptosis through a nicotinamide adenine dinucleotide phosphate oxidase‐dependent, mitogen‐activated protein kinases‐mediated intrinsic apoptosis pathway

Zhu, S., Zhuang, J., Wu, Q., Liu, Z., Liao, C., Luo, S., Chen, J., & Zhong, Z. (2018) · Aging Cell · doi:10.1111/acel.12764 · Cited by 55 · see citing works

Sanglifehrin A inhibits opening of mitochondrial permeability transition pore (MPTP) during ischemia/reperfusion in the adult but not in the immature heart

Chvojkova, Z., Skarka, L., Ošťádalová, I., et al. (2006) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2006.03.111

Mitochondrial permeability transition pore-dependent necrosis

Robichaux, D. J., Harata, M., Murphy, E., & Karch, J. M. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.11.003 · Cited by 192 · see citing works

Ischaemic Preconditioning Inhibits Opening of Mitochondrial Permeability Transition Pores in the Reperfused Rat Heart

Javadov, S. A., Clarke, S. J., Das, M., Griffiths, E. J., Lim, K. H. H., & Halestrap, A. P. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.034231 · Cited by 350 · see citing works

Physiological and Pathological Roles of the Mitochondrial Permeability Transition Pore in the Heart

Kwong, J. Q., & Molkentin, J. D. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.001 · Cited by 463 · see citing works

Inhibition of Bcl-2 Sensitizes Mitochondrial Permeability Transition Pore (MPTP) Opening in Ischemia-Damaged Mitochondria

Chen, Q., Xu, H., Xu, A., Ross, T., Bowler, E., Hu, Y., & Lesnefsky, E. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118834 · Cited by 63 · see citing works