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Cyclophilin D controls mitochondrial pore–dependent Ca2+ exchange, metabolic flexibility, and propensity for heart failure in mice
Open accessAbstract
Cyclophilin D (which is encoded by the Ppif gene) is a mitochondrial matrix peptidyl-prolyl isomerase known to modulate opening of the mitochondrial permeability transition pore (MPTP). Apart from regulating necrotic cell death, the physiologic function of the MPTP is largely unknown. Here we have shown that Ppif(-/-) mice exhibit substantially greater cardiac hypertrophy, fibrosis, and reduction in myocardial function in response to pressure overload stimulation than control mice. In addition, Ppif(-/-) mice showed greater hypertrophy and lung edema as well as reduced survival in response to sustained exercise stimulation. Cardiomyocyte-specific transgene expression of cyclophilin D in Ppif(-/-) mice rescued the enhanced hypertrophy, reduction in cardiac function, and rapid onset of heart failure following pressure overload stimulation. Mechanistically, the maladaptive phenotype in the hearts of Ppif(-/-) mice was associated with an alteration in MPTP-mediated Ca(2+) efflux resulting in elevated levels of mitochondrial matrix Ca(2+) and enhanced activation of Ca(2+)-dependent dehydrogenases. Elevated matrix Ca(2+) led to increased glucose oxidation relative to fatty acids, thereby limiting the metabolic flexibility of the heart that is critically involved in compensation during stress. These findings suggest that the MPTP maintains homeostatic mitochondrial Ca(2+) levels to match metabolism with alterations in myocardial workload, thereby suggesting a physiologic function for the MPTP.
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“however, lack of cyclophilin D in cardiac cells may be detrimental under certain conditions, as this deficiency compromises Ca2+ handling in mitochondria, decreasing the ability of mitochondria to efflux Ca2+ after alterations in myocardial workload due to lack of beneficial (perhaps transient) MPT pore formation (123).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [123]
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Cites
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,131
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
Huang, D. W., Sherman, B. T., Tan, Q., Collins, J., Alvord, W. G., Roayaei, J., Stephens, R. D., Baseler, M., Lane, H. C., & Lempicki, R. A. (2007) · Genome biology · doi:10.1186/gb-2007-8-9-r183 · Cited by 2,482
Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280
Self-citationNakagawa, T., Shimizu, S., Watanabe, T., Yamaguchi, O., Otsu, K., Yamagata, H., Inohara, H., Kubo, T., & Tsujimoto, Y. (2005) · Nature · doi:10.1038/nature03317 · Cited by 1,635
Circularly permuted green fluorescent proteins engineered to sense Ca 2+
Nagai, T., Sakaue-Sawano, A., Park, E. S., & Miyawaki, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051636098 · Cited by 969
Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 950
Self-citationLeone, T. C., Weinheimer, C. J., & Kelly, D. P. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7473 · Cited by 943
Regulation of mitochondrial dehydrogenases by calcium ions
Denton, R. M. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.01.005 · Cited by 885
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Items 201–300 of 383
Garbincius, J. F., Luongo, T. S., Jadiya, P., Hildebrand, A. N., Kolmetzky, D. W., Mangold, A. S., Roy, R., Ibetti, J., Nwokedi, M., Koch, W. J., et al. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.03.001 · Cited by 37
Self-citationChinopoulos, C., & Ádám‐Vizi, V. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.04.007 · Cited by 32
Cyclophilin D regulates mitochondrial flashes and metabolism in cardiac myocytes
Shang, W. H., Gao, H., Lu, F., Ma, Q., Fang, H., Sun, T., Xu, J., Ding, Y., Lin, Y., Wang, Y., et al. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.10.036 · Cited by 31
Role of mitochondrial Ca2+ homeostasis in cardiac muscles
Cao, J. L., Adaniya, S. M., Cypress, M. W., Suzuki, Y., Kusakari, Y., Jhun, B. S., & O‐Uchi, J. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.01.027 · Cited by 33
Lv, Y., Cheng, L., & Peng, F. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.910452 · Cited by 37
Zhang, Y., Yao, J., Zhang, M., Wang, Y., & Shi, X. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1083935 · Cited by 31
Mitochondrial calcium signaling and redox homeostasis in cardiac health and disease
Popoiu, T.-A., Maack, C., & Bertero, E. (2023) · Frontiers in Molecular Medicine · doi:10.3389/fmmed.2023.1235188 · Cited by 36
Rohrbach, S., Aslam, M., Niemann, B., & Schulz, R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12650 · Cited by 31
LRRC10 is required to maintain cardiac function in response to pressure overload
Brody, M. J., Feng, L., Grimes, A. C., Hacker, T. A., Olson, T. M., Kamp, T. J., Balijepalli, R. C., & Lee, Y.-S. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00717.2014 · Cited by 30
Heart failure—potential new targets for therapy
Nabeebaccus, A., Zheng, S. L., & Shah, A. M. (2016) · British Medical Bulletin · doi:10.1093/bmb/ldw025 · Cited by 30
Yun, B., Lee, H.-J., Ghosh, M., Cravatt, B. F., Hsu, K., Bonventre, J. V., Ewing, H., Gelb, M. H., & Leslie, C. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.497651 · Cited by 29
Cyclophilin inhibition as a potential treatment for nonalcoholic steatohepatitis (NASH)
Ure, D., Trepanier, D. J., Mayo, P., & Foster, R. T. (2019) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2020.1703948 · Cited by 30
Li, A., Yi, J., Li, X., & Zhou, J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.595800 · Cited by 27
The molecular mosaic of regulated cell death in the cardiovascular system
Martens, M. D., Karch, J. M., & Gordon, J. W. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166297 · Cited by 31
Self-citationHormonal orchestra: mastering mitochondria's role in health and disease
Al-Suhaimi, E. A., Alquwaie, R., AlSaqabi, R., Winarni, D., Dewi, F. R. P., Rubaish, A. A., Shehzad, A., & Elaı̈ssari, A. (2024) · Endocrine · doi:10.1007/s12020-024-03967-1 · Cited by 32
Behera, R., Sharma, V., Grewal, A. K., Kumar, A., Arora, B., Najda, A., Albadrani, G. M., Altyar, A. E., Abdel‐Daim, M. M., & Singh, T. G. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114599 · Cited by 31
Xiong, X., Yang, X., Duan, L., Liu, W., Zhang, Y., Liu, Y., Wang, P., Li, S., & Li, X. (2017) · Scientific Reports · doi:10.1038/srep42965 · Cited by 28
Inhibition of the mitochondrial permeability transition improves bone fracture repair
Shares, B. H., Smith, C. O., Sheu, T., Sautchuk, R., Schilling, K. J., Shum, L. C., Paine, A., Huber, A., Gira, E., Brown, E. B., et al. (2020) · Bone · doi:10.1016/j.bone.2020.115391 · Cited by 28
Cyclophilin D-mediated Mitochondrial Permeability Transition Regulates Mitochondrial Function
Zhou, S., Yu, Q., Zhang, L., & Jiang, Z. (2023) · Current Pharmaceutical Design · doi:10.2174/1381612829666230313111314 · Cited by 27
Ren, C., Hu, C., Hu, M., Wu, Y., Yang, Y., & Lu, F. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.156088 · Cited by 27
Belosludtsev, K. N., Starinets, V. S., Talanov, E. Y., Mikheeva, I. B., Dubinin, M. V., & Belosludtseva, N. V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179524 · Cited by 27
Zeng, J., Chen, B., Lv, X., Sun, L., Zeng, X., Zheng, H., Du, Y., Wang, G., Ma, M., & Guan, Y. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14432 · Cited by 26
Dabkowski, E. R., O’Connell, K. A., Xu, W., Ribeiro, E. H., Hecker, P. I., Shekar, K. C., Daneault, C., Rosiers, C. D., & Stanley, W. C. (2013) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-013-6487-4 · Cited by 27
Cyclophilin inhibition as a strategy for the treatment of human disease
Stauffer, W. T., Goodman, A. Z., & Gallay, P. A. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1417945 · Cited by 27
Cyclophilin‐D: a resident regulator of mitochondrial gene expression
Radhakrishnan, J., Bazarek, S. F., Chandran, B., & Gazmuri, R. J. (2015) · The FASEB Journal · doi:10.1096/fj.14-263855 · Cited by 25
Control of Cell Differentiation by Mitochondria, Typically Evidenced in Dictyostelium Development
Maeda, Y., & Chida, J. (2013) · Biomolecules · doi:10.3390/biom3040943 · Cited by 26
Hiemstra, J. A., Gutiérrez‐Aguilar, M., Marshall, K. D., McCommis, K. S., Zgoda, P. J., Cruz-Rivera, N., Jenkins, N. T., Krenz, M., Domeier, T. L., Baines, C. P., et al. (2014) · Physiological Reports · doi:10.14814/phy2.12050 · Cited by 28
Mohammadi‐Bardbori, A., Najibi, A., Amirzadegan, N., Gharibi, R., Dashti, A., Omidi, M., Saeedi, A., Ghaffarian‐Bahraman, A., & Niknahad, H. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.05.041 · Cited by 26
Shiomi, M., Miyamae, M., Takemura, G., Kaneda, K., Inamura, Y., Onishi, A., Koshinuma, S., Momota, Y., Minami, T., & Figueredo, V. M. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.12.027 · Cited by 25
Lingan, J. V., Alanzalon, R. E., & Porter, G. A. (2017) · Pediatric Research · doi:10.1038/pr.2017.19 · Cited by 24
Postconditioning signalling in the heart: mechanisms and translatability
Bice, J. S., & Baxter, G. F. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12976 · Cited by 24
Therapeutic implications of novel peptides targeting ER–mitochondria Ca2+-flux systems
Kerkhofs, M., Bultynck, G., Vervliet, T., & Monaco, G. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2019.03.020 · Cited by 25
Gainutdinov, T. M., Molkentin, J. D., Siemen, D., Ziemer, M., Dębska–Vielhaber, G., Vielhaber, S., Gizatullina, Z. Z., Orynbayeva, Z., & Gellerich, F. N. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.05.009 · Cited by 24
Self-citationMitochondrial contributions to neuronal development and function
Princz, A., Kounakis, K., & Tavernarakis, N. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0333 · Cited by 25
Endoplasmic reticulum stress contributes to heart protection induced by cyclophilin D inhibition
Belaïdi, E., Décorps, J., Augeul, L., Durand, A., & Ovize, M. (2013) · Basic Research in Cardiology · doi:10.1007/s00395-013-0363-z · Cited by 23
Disease Outcome and Brain Metabolomics of Cyclophilin-D Knockout Mice in Sepsis
Kobayashi, T., Uchino, H., Elmér, E., Ogihara, Y., Fujita, H., Sekine, S., Ishida, Y., Saiki, I., Shibata, S., & Kawachi, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020961 · Cited by 22
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BackgroundMitochondrial Cardiomyopathy and Related Arrhythmias
Montaigne, D., & Pentiah, A. D. (2015) · Cardiac Electrophysiology Clinics · doi:10.1016/j.ccep.2015.03.008 · Cited by 22
The Role of Peptidyl Prolyl Isomerases in Aging and Vascular Diseases
McClements, L., Annett, S., Yakkundi, A., & Robson, T. (2015) · Current Molecular Pharmacology · doi:10.2174/1874467208666150519115729 · Cited by 22
Li, X., Ma, W., Wang, X., Ci, Y., & Zhao, Y. (2018) · Cancer Biomarkers · doi:10.3233/cbm-171040 · Cited by 22
Kwon, J., Schumacher, S. M., Gao, E., Chuprun, J. K., Ibetti, J., Roy, R., Khan, M., Kishore, R., & Koch, W. J. (2021) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00571.2020 · Cited by 20
The Haves and Have-Nots: The Mitochondrial Permeability Transition Pore across Species
Frigo, E., Tommasin, L., Lippe, G., Carraro, M., & Bernardi, P. (2023) · Cells · doi:10.3390/cells12101409 · Cited by 23
RCAN 1 regulates vesicle recycling and quantal release kinetics via effects on calcineurin activity
Zanin, M., Mackenzie, K. D., Peiris, H. S., Pritchard, M. A., & Keating, D. J. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12086 · Cited by 21
CaMKII and stress mix it up in mitochondria
Joiner, M.-L. A., & Koval, O. M. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00067 · Cited by 21
A Mitochondrial Basis for Heart Failure Progression
Watson, W. D., Arvidsson, P. M., Miller, J. J. J. J., Lewis, A. J., & Rider, O. J. (2024) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-024-07582-0 · Cited by 21
Tamrakar, P., Ibrahim, B. A., Gujar, A. D., & Briski, K. P. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23481 · Cited by 20
Rogers, C., Davis, B., Neufer, P. D., Murphy, M. P., Anderson, E. J., & Robidoux, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.11.012 · Cited by 21
Mitochondrial calcium in command of juggling myriads of cellular functions
Singh, S., & Mabalirajan, U. (2021) · Mitochondrion · doi:10.1016/j.mito.2020.12.011 · Cited by 20
Genetic deletion of p66shc and/or cyclophilin D results in decreased pulmonary vascular tone
Gierhardt, M., Pak, O., Sydykov, A. S., Kraut, S., Schäffer, J., Garcia, C., Veith, C., Zeidan, E. M., Brosien, M., Quanz, K., et al. (2020) · Cardiovascular Research · doi:10.1093/cvr/cvaa310 · Cited by 19
The effect of chronic alcohol consumption on mitochondrial calcium handling in hepatocytes
Wang, G., Mémin, E., Murali, I., & Gaspers, L. D. (2016) · Biochemical Journal · doi:10.1042/bcj20160255 · Cited by 19
Sui, S., Tian, J., Gauba, E., Wang, Q., Guo, L., & Du, H. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14484 · Cited by 19
Blockade of cyclophilin D rescues dexamethasone-induced oxidative stress in gingival tissue
He, Y., Zhang, L., Zhu, Z., Xiao, A., Yu, H., & Gan, X. (2017) · PLoS ONE · doi:10.1371/journal.pone.0173270 · Cited by 19
Progression of herpesvirus infection remodels mitochondrial organization and metabolism
Leclerc, S., Gupta, A., Ruokolainen, V., Chen, J.-H., Kunnas, K., Ekman, A. A., Niskanen, H., Belevich, I. N., Vihinen, H., Turkki, P., et al. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1011829 · Cited by 18
Marcu, R., Neeley, C. K., Karamanlidis, G., & Hawkins, B. J. (2012) · Journal of Visualized Experiments · doi:10.3791/4131 · Cited by 18
Kamei, Y., Koushi, M., Aoyama, Y., & Asakai, R. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.07.004 · Cited by 19
Agyapong, E. D., Pedriali, G., Ramaccini, D., Bouhamida, E., Tremoli, E., Giorgi, C., Pinton, P., & Morciano, G. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05240-5 · Cited by 17
Garvin, A. M., Strock, N. C. A., Hackenberger, J. L., & Korzick, D. H. (2017) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-017-2034-7 · Cited by 17
Dubinin, M. V., Starinets, V. S., Talanov, E. Y., Mikheeva, I. B., Belosludtseva, N. V., Serov, D. A., Tenkov, K. S., Belosludtseva, E. V., & Belosludtsev, K. N. (2021) · Biomedicines · doi:10.3390/biomedicines9091232 · Cited by 17
Drahota, Z., Milerová, M., Endlicher, R., Rychtrmoc, D., Červinková, Z., & Ošťádal, B. (2012) · Physiological Research · doi:10.33549/physiolres.932377 · Cited by 17
Wu, W., Zheng, J., & Jia, Z. (2021) · iScience · doi:10.1016/j.isci.2021.102895 · Cited by 16
Involvement of Cyclophilin D and Calcium in Isoflurane-induced Preconditioning
Teixeira, G., Chiari, P. C., Fauconnier, J., Abrial, M., Couture-Lepetit, E., Harisseh, R., Pillot, B., Lacampagne, A., Tourneur, Y., Gharib, A., et al. (2015) · Anesthesiology · doi:10.1097/aln.0000000000000876 · Cited by 16
Effect of hydrogen sulfide on isolated rat heart reaction under volume load and ischemia-reperfusion
Tv, S., Hoshovs'ka, I., Semenikhina, O., & Sahach, V. (2012) · Fìzìologìčnij žurnal · doi:10.15407/fz58.06.057 · Cited by 16
Kashlov, Y., Donev, I. S., Doneva, J. G., Valkov, V., Kirkorova, A., Ghenev, P., Conev, N. V., Radeva, T. R., Ivanov, B., & Georgieva, Z. T. (2016) · BioScience Trends · doi:10.5582/bst.2016.01077 · Cited by 16
Changes in Myocardial Metabolism Preceding Sudden Cardiac Death
Snyder, J. E., Zhai, R., Lackey, A. I., & Sato, P. Y. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00640 · Cited by 16
The shape of things to come: mitochondrial fusion and fission in the adult heart
Hall, A. R., & Hausenloy, D. J. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs150 · Cited by 16
Klawitter, J., Pennington, A. T., Klawitter, J., Thurman, J. M., & Christians, U. (2017) · Scientific Reports · doi:10.1038/s41598-017-10076-9 · Cited by 14
Cyclophilin D knockout protects the mouse kidney against cyclosporin A-induced oxidative stress
Klawitter, J., Klawitter, J., Pennington, A. T., Kirkpatrick, B. E., Roda, G. F., Kotecha, N. C., Thurman, J. M., & Christians, U. (2019) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00417.2018 · Cited by 14
Sun, J., & Jacobs, K. M. (2016) · Frontiers in Systems Neuroscience · doi:10.3389/fnsys.2016.00063 · Cited by 13
Acute inhibition of GSK causes mitochondrial remodeling
Nguyen, T. T. M., Wong, R. P., Wang, G., Guček, M., Steenbergen, C., & Murphy, E. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00033.2012 · Cited by 14
Self-citationProximal tubule cyclophilin D mediates kidney fibrogenesis in obstructive nephropathy
Jang, H., Noh, M. R., Ha, L., Kim, J., & Padanilam, B. J. (2021) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00171.2021 · Cited by 13
Harvey, K. L., Hussain, A., & Maddock, H. L. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu001 · Cited by 13
Ethanol Consumption Affects Neuronal Function: Role of the Mitochondria
Tapia‐Rojas, C., Maria Jose Perez, J., Jara, C., Vergara, E. H., & Quintanilla, R. A. (2018) · InTech eBooks · doi:10.5772/intechopen.71611 · Cited by 15
Zhang, B., Jia, K., Tian, J., & Du, H. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.05.204 · Cited by 13
Carrer, A., Laquatra, C., Tommasin, L., & Carraro, M. (2021) · Molecules · doi:10.3390/molecules26216463 · Cited by 14
Cyclophilin D regulates lifespan and protein expression of aging markers in the brain of mice
Vereczki, V., Mansour, J. J., Pour‐Ghaz, I., Bodnár, I., Pintér, O., Zelena, D., Oszwald, E., Ádám‐Vizi, V., & Chinopoulos, C. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.03.003 · Cited by 12
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Schenkl, C., Heyne, E., Doenst, T., Schulze, P. C., & Nguyễn, T. D. (2023) · Life · doi:10.3390/life13041027 · Cited by 12
Samartsev, V. N., Khoroshavina, E. I., Pavlova, E. K., Dubinin, M. V., & Semenova, A. A. (2023) · Membranes · doi:10.3390/membranes13050472 · Cited by 11
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Stevens, T. L., Cohen, H. M., Garbincius, J. F., & Elrod, J. W. (2024) · Nature Cardiovascular Research · doi:10.1038/s44161-024-00463-7 · Cited by 12
Self-citationZhu, X., Qin, Z., Zhou, M., Li, C., Jing, J., Ye, W., & Gan, X. (2024) · Biomolecules · doi:10.3390/biom14101318 · Cited by 12
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Park, H., Hu, S., Kim, S. Y., Yoon, S., Yoon, N. G., Lee, J. H., Choi, W., Kong, S., Kim, J. H., Nam, D., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02314-8 · Cited by 16
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Shao, R., Li, J., Qu, T., Liao, Y., & Chen, M. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2849985 · Cited by 11
Deb, A., Tow, B. D., Qing, Y., Walker, M., Hodges, E. R., Stewart, J. A., Knollmann, B. C., Zheng, Y., Wang, Y., & Liu, B. (2023) · Cells · doi:10.3390/cells12020204 · Cited by 10
Dikalova, A., Ao, M., Lantier, L., Gutor, S. S., & Dikalov, S. (2025) · Function · doi:10.1093/function/zqaf006 · Cited by 10
Kumar, A., Mello, J. D. F. R. E., Wu, Y., Morris, D., Mezghani, I., Smith, E., Rombauts, S., Bossier, P., Krahn, J. M., Sigworth, F. J., et al. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01476-w · Cited by 10
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Lewno, M. T., Cui, T., & Wang, X. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.690423 · Cited by 10
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Metadata
- Authors
- Elrod, J. W., Wong, R., Mishra, S., Vagnozzi, R. J., Sakthievel, B., Goonasekera, S. A., Karch, J., Gabel, S., Farber, J., Force, T., Heller Brown, J., Murphy, E., & Molkentin, J. D.
- Affiliations
- Cincinnati Children's Hospital Medical Center (US)
- National Institutes of Health (US)
- University of California San Diego (US)
- Thomas Jefferson University (US)
- Corresponding author
- Molkentin, Jeffery D.
- ORCID
- Venue
- Journal of Clinical Investigation
- Published
- 2010-10-01
- Volume
- 120
- Issue
- 10
- Pages
- 3680-3687
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC2947235
- OpenAlex
- W1966536813
- Cited by
- 384
- References
- 47
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 13 · 2023: 21 · 2022: 20 · 2021: 29 · 2020: 29 · 2019: 23 · 2018: 24 · 2017: 25 · 2016: 34 · 2015: 36 · 2014: 32 · 2013: 21 · 2012: 31
- FWCI
- 10.68
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- Fondation Leducq
- National Institutes of Health (HL80101)
- National Heart, Lung, and Blood Institute (HL-62927, HL80101, R01HL081104, P01HL080101, F32HL092737, R37HL028143, HL81104, R01HL062927)
- National Institute of General Medical Sciences (T32GM007752)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Fibrosis and Remodeling
- Keywords
- cyclophilin D, mitochondrial permeability transition pore, mitochondrial calcium, cardiac hypertrophy, heart failure, pressure overload, metabolic flexibility, glucose oxidation, fatty acid oxidation, cardiomyocyte-specific overexpression, myocardial fibrosis, pulmonary edema
- MeSH terms
- Peptidyl-Prolyl Isomerase F, Mitochondrial Permeability Transition Pore, Aging, Animals, Calcium, Cardiomegaly, Heart Failure, Mice, Transgenic, Mitochondria, Heart, Myocardial Contraction, Cyclophilins, Mitochondrial Membrane Transport Proteins, Mice
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