Mitochondria as sensors and regulators of calcium signalling

Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death

Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280 · see citing works

Mechanisms by which mitochondria transport calcium

Gunter, T. E., & Pfeiffer, D. R. (1990) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1990.258.5.c755 · Cited by 1,640 · see citing works

Role of calcium ions in regulation of mammalian intramitochondrial metabolism

McCormack, J. G., Halestrap, A. P., & Denton, R. M. (1990) · Physiological Reviews · doi:10.1152/physrev.1990.70.2.391 · Cited by 1,398 · see citing works

Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria

Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129 · see citing works

Novel targets for Huntington's disease in an mTOR-independent autophagy pathway

Williams, A., Sarkar, S., Cuddon, P., Ttofi, E. K., Saiki, S., Siddiqi, F. H., Jahreiss, L., Fleming, A., Pask, D., Goldsmith, P., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.79 · Cited by 800 · see citing works

The Golgi apparatus is an inositol 1,4,5‐trisphosphate‐sensitive Ca2+ store, with functional properties distinct from those of the endoplasmic reticulum

Pinton, P., Pozzan, T., & Rizzuto, R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.18.5298 · Cited by 435 · see citing works

Cyclophilin D controls mitochondrial pore–dependent Ca2+ exchange, metabolic flexibility, and propensity for heart failure in mice

Elrod, J. W., Wong, R., Mishra, S., Vagnozzi, R. J., Sakthievel, B., Goonasekera, S. A., Karch, J., Gabel, S., Farber, J., Force, T., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci43171 · Cited by 384 · see citing works

The inositol 1,4,5-trisphosphate receptor regulates autophagy through its interaction with Beclin 1

Vicencio, J. M., Ortiz, C., Criollo, A., Jones, A. W. E., Kepp, O., Galluzzi, L., Joza, N., Vitale, I., Morselli, E., Tailler, M., et al. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2009.34 · Cited by 289 · see citing works

Respiration-dependent accumulation of inorganic phosphate and Ca++ by rat liver mitochondria

Lehninger, A. L., Rossi, C. S., & Greenawalt, J. W. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90377-2 · Cited by 188 · see citing works

Mitochondrial matrix Ca ² ⁺ as an intrinsic signal regulating mitochondrial motility in axons

Chang, K. T., Niescier, R. F., & Min, K.-T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106862108 · Cited by 153 · see citing works

The Proapoptotic Factors Bax and Bak Regulate T Cell Proliferation through Control of Endoplasmic Reticulum Ca2+ Homeostasis

Jones, R. G., Bui, T., White, C., Madesh, M., Krawczyk, C. M., Lindsten, T., Hawkins, B. J., Kubek, S., Frauwirth, K. A., Wang, Y. L., et al. (2007) · Immunity · doi:10.1016/j.immuni.2007.05.023 · Cited by 109 · see citing works

The cell biology of mitochondrial membrane dynamics

Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550 · see citing works

Calcium and ROS: A mutual interplay

Görlach, A., Bertram, K., Hudecova, S., & Krizanova, O. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.010 · Cited by 1,546 · see citing works

13 reasons why the brain is susceptible to oxidative stress

Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works

Endoplasmic reticulum-mitochondria contacts: Function of the junction

Rowland, A. A., & Voeltz, G. K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3440 · Cited by 1,018 · see citing works

Mitochondria in the Regulation of Innate and Adaptive Immunity

Weinberg, S. E., Sena, L. A., & Chandel, N. S. (2015) · Immunity · doi:10.1016/j.immuni.2015.02.002 · Cited by 960 · see citing works

The Tumor Microenvironment Represses T Cell Mitochondrial Biogenesis to Drive Intratumoral T Cell Metabolic Insufficiency and Dysfunction

Scharping, N. E., Menk, A. V., Moreci, R. S., Whetstone, R. D., Dadey, R. E., Watkins, S. C., Ferris, R. L., & Delgoffe, G. M. (2016) · Immunity · doi:10.1016/j.immuni.2016.07.009 · Cited by 848 · see citing works

Initiation and perpetuation of <scp>NLRP</scp> 3 inflammasome activation and assembly

Elliott, E. I., & Sutterwala, F. S. (2015) · Immunological Reviews · doi:10.1111/imr.12286 · Cited by 821 · see citing works

Mitonuclear communication in homeostasis and stress

Quirós, P. M., Mottis, A., & Auwerx, J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.23 · Cited by 787 · see citing works

Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease

Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654 · see citing works

Mitochondrial dynamics in adaptive and maladaptive cellular stress responses

Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622 · see citing works

Transient Opening of the Mitochondrial Permeability Transition Pore Induces Microdomain Calcium Transients in Astrocyte Processes

Agarwal, A., Wu, P.-H., Hughes, E. G., Fukaya, M., Tischfield, M. A., Langseth, A. J., Wirtz, D., & Bergles, D. E. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.034 · Cited by 441 · see citing works

Oxidative stress and calcium dysregulation by palmitate in type 2 diabetes

Ly, L. D., Xu, S., Choi, S.-K., Ha, C.-M., Thoudam, T., Cha, S.-K., Wiederkehr, A., Wollheim, C. B., Lee, I.-K., & Park, K.-S. (2017) · Experimental &amp; Molecular Medicine · doi:10.1038/emm.2016.157 · Cited by 378 · see citing works

Binding of FUN14 domain containing 1 with inositol 1,4,5-trisphosphate receptor in mitochondria-associated endoplasmic reticulum membranes maintains mitochondrial dynamics and function in hearts in vivo

Wu, S., Lu, Q., Wang, Q., Ding, Y., Ma, Z., Mao, X., Huang, K., Xie, Z., & Zou, M.-H. (2017) · Circulation · doi:10.1161/circulationaha.117.030235 · Cited by 320 · see citing works

Hyperglycemia-Driven Inhibition of AMP-Activated Protein Kinase α2 Induces Diabetic Cardiomyopathy by Promoting Mitochondria-Associated Endoplasmic Reticulum Membranes In Vivo

Wu, S., Lu, Q., Ding, Y., Wu, Y., Qiu, Y., Wang, P., Mao, X., Huang, K., Xie, Z., & Zou, M.-H. (2019) · Circulation · doi:10.1161/circulationaha.118.033552 · Cited by 298 · see citing works

BCL-2 family: integrating stress responses at the ER to control cell demise

Pihán, P., Carreras-Sureda, A., & Hetz, C. (2017) · Cell Death &amp; Differentiation · doi:10.1038/cdd.2017.82 · Cited by 274 · see citing works

Omega-3 Fatty Acids and Insulin Resistance: Focus on the Regulation of Mitochondria and Endoplasmic Reticulum Stress

Lepretti, M., Martucciello, S., Burgos Aceves, M., Putti, R., & Lionetti, L. (2018) · Nutrients · doi:10.3390/nu10030350 · Cited by 232 · 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 dynamics maintain muscle stem cell regenerative competence throughout adult life by regulating metabolism and mitophagy

Hong, X., Isern, J., Campanario, S., Perdiguero, E., Ramírez-Pardo, I., Segalés, J., Hernansanz-Agustín, P., Curtabbi, A., Deryagin, O., Pollán, A., et al. (2022) · Cell stem cell · doi:10.1016/j.stem.2022.07.009 · Cited by 213 · see citing works

The Involvement of Mg²⁺ in Regulation of Cellular and Mitochondrial Functions

Pilchova, I., Klacanova, K., Tatarkova, Z., Kaplan, P., & Racay, P. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6797460 · Cited by 198 · see citing works

Inhibition of mitochondrial fragmentation protects against Alzheimer’s disease in rodent model

Wang, W., Yin, J., Ma, X., Zhao, F., Siedlak, S. L., Wang, Z., Torres, S., Fujioka, H., Xu, Y., Perry, G., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx299 · Cited by 175 · see citing works

VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress

Shoshan-Barmatz, V., N. Maldonado, E., & Krelin, Y. (2017) · Cell Stress · doi:10.15698/cst2017.10.104 · Cited by 170 · see citing works

Emerging concepts in smooth muscle contributions to airway structure and function: implications for health and disease

Prakash, Y. S. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00370.2016 · Cited by 136 · see citing works

Mitochondrial metabolites: undercover signalling molecules

Frezza, C. (2017) · Interface Focus · doi:10.1098/rsfs.2016.0100 · Cited by 136 · see citing works

Mitochondrial damage-associated molecular patterns and vascular function

Wenceslau, C. F., McCarthy, C. G., Szasz, T., Spitler, K., Goulopoulou, S., Webb, R. C., & Working Group on DAMPs in Cardiovascular Disease (2014) · European Heart Journal · doi:10.1093/eurheartj/ehu047 · Cited by 135 · see citing works

Mitochondria as a centrally positioned hub in the innate immune response

Sandhir, R., Halder, A., & Sunkaria, A. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.10.020 · Cited by 135 · see citing works

Mitochondrial calcium cycling in neuronal function and neurodegeneration

Walters, G. C., & Usachev, Y. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094356 · Cited by 105 · see citing works

PINK1 Is Dispensable for Mitochondrial Recruitment of Parkin and Activation of Mitophagy in Cardiac Myocytes

Kubli, D. A., Cortez, M. Q., Moyzis, A. G., Najor, R. H., Lee, Y., & Gustafsson, Å. B. (2015) · PLOS ONE · doi:10.1371/journal.pone.0130707 · Cited by 102 · see citing works

Reduced mitochondrial calcium uptake in macrophages is a major driver of inflammaging

Seegren, P. V., Harper, L. R., Downs, T. K., Zhao, X.-Y., Viswanathan, S. B., Stremska, M. E., Olson, R. J., Kennedy, J., Ewald, S. E., Kumar, P., et al. (2023) · Nature Aging · doi:10.1038/s43587-023-00436-8 · Cited by 88 · see citing works

Calcium, Bioenergetics, and Parkinson’s Disease

Zampese, E., & Surmeier, D. J. (2020) · Cells · doi:10.3390/cells9092045 · Cited by 79 · see citing works

Mitoprotective Effects of Centella asiatica (L.) Urb.: Anti-Inflammatory and Neuroprotective Opportunities in Neurodegenerative Disease

Wong, J. H., Barron, A. M., & Abdullah, J. M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.687935 · Cited by 79 · see citing works

The cellular basis of dendrite pathology in neurodegenerative diseases

Kweon, J. H., Kim, S., & Lee, S. B. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.1.131 · Cited by 73 · see citing works

A Neurotoxic Ménage-à-trois: Glutamate, Calcium, and Zinc in the Excitotoxic Cascade

Granzotto, A., Canzoniero, L. M. T., & Sensi, S. L. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.600089 · Cited by 67 · see citing works

Mitochondrial Matrix Ca²⁺ Accumulation Regulates Cytosolic NAD⁺/NADH Metabolism, Protein Acetylation, and Sirtuin Expression

Marcu, R., Wiczer, B. M., Neeley, C. K., & Hawkins, B. J. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00068-14 · Cited by 62 · see citing works

A little goes a long way: Neurobiological effects of low intensity rTMS and implications for mechanisms of rTMS

Moretti, J., & Rodger, J. (2022) · Current Research in Neurobiology · doi:10.1016/j.crneur.2022.100033 · Cited by 60 · see citing works

Parathyroid Hormone Causes Endothelial Dysfunction by Inducing Mitochondrial ROS and Specific Oxidative Signal Transduction Modifications

Gambardella, J., De Rosa, M., Sorriento, D., Prevete, N., Fiordelisi, A., Ciccarelli, M., Trimarco, B., De Luca, N., & Iaccarino, G. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9582319 · Cited by 58 · see citing works

Remodeling of Ca2+ signaling in cancer: Regulation of inositol 1,4,5-trisphosphate receptors through oncogenes and tumor suppressors

Ando, H., Kawaai, K., Bonneau, B., & Mikoshiba, K. (2018) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.12.001 · Cited by 55 · see citing works

Mitochondrial turnover and homeostasis in ageing and neurodegeneration

Markaki, M., & Tavernarakis, N. (2020) · FEBS Letters · doi:10.1002/1873-3468.13802 · Cited by 50 · see citing works

Naringin‐generated <scp>ROS</scp> promotes mitochondria‐mediated apoptosis in <scp><i>Candida albicans</i></scp>

Kim, H., & Lee, D. G. (2021) · IUBMB Life · doi:10.1002/iub.2476 · Cited by 44 · see citing works

The role of suboptimal mitochondrial function in vulnerability to post‐traumatic stress disorder

Preston, G., Kirdar, F., & Kozicz, T. (2018) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-018-0168-1 · Cited by 36 · see citing works

Ultraviolet B irradiation induced Nrf2 degradation occurs via activation of TRPV1 channels in human dermal fibroblasts

Huang, K.-F., Ma, K.-H., Jhap, T.-Y., Liu, P.-S., & Chueh, S.-H. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.06.020 · Cited by 27 · see citing works

Cyclophilin D, a target for counteracting skeletal muscle dysfunction in mitochondrial myopathy

Gineste, C., Hernandez, A., Ivarsson, N., Cheng, A. J., Naess, K., Wibom, R., Lesko, N., Bruhn, H., Wedell, A., Freyer, C., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv361 · Cited by 21 · see citing works

CYFIP1 governs the development of cortical axons by modulating calcium availability

Ricci, C., Midroit, M. J., Caicci, F., Achsel, T., Domínguez-Iturza, N., & Bagni, C. (2025) · Nature Communications · doi:10.1038/s41467-025-65801-0 · Cited by 1 · see citing works