The roles of mitochondria in global and local intracellular calcium signalling

A new generation of Ca2+ indicators with greatly improved fluorescence properties.

Grynkiewicz, G., Poenie, M., & Tsien, R. Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83641-4 · Cited by 21,722 · see citing works

Calcium's Role in Mechanotransduction during Muscle Development

Damm, T. B., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,548 · see citing works

Copper-Zinc Superoxide Dismutase (SOD1) Is Released by Microglial Cells and Confers Neuroprotection against 6-OHDA Neurotoxicity

Polazzi, E., Mengoni, I., Caprini, M., Peña‐Altamira, E., Kurtys, E., & Monti, B. (2012) · Neurosignals · doi:10.1159/000337115 · Cited by 9,023 · see citing works

Calcium signalling: dynamics, homeostasis and remodelling

Berridge, M., Bootman, M., & Roderick, H. (2003) · Nature reviews. Molecular cell biology · doi:10.1038/nrm1155 · Cited by 5,747 · see citing works

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 5,120 · see citing works

Calcium Signaling

Clapham, D. E. (2007) · Cell · doi:10.1016/j.cell.2007.11.028 · Cited by 4,175 · see citing works

Mitofusin 2 tethers endoplasmic reticulum to mitochondria

de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works

Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca ²⁺ Responses

Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257 · see citing works

Calcium homeostasis in intact lymphocytes: cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator.

Tsien, R. Y., Pozzan, T., & RINK, T. J. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.94.2.325 · Cited by 2,251 · see citing works

New calcium indicators and buffers with high selectivity against magnesium and protons: design, synthesis, and properties of prototype structures

Tsien, R. Y. (1980) · Biochemistry · doi:10.1021/bi00552a018 · Cited by 2,243 · see citing works

Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter

Baughman, J. M., Perocchi, F., Girgis, H. S., Plovanich, M. E., Belcher-Timme, C. A., Sancak, Y., Bao, X., Strittmatter, L., Goldberger, O., Bogorad, R., et al. (2011) · Nature · doi:10.1038/nature10234 · Cited by 1,926 · see citing works

Sigma-1 Receptor Chaperones at the ER- Mitochondrion Interface Regulate Ca2+ Signaling and Cell Survival

Hayashi, T., & Su, T.-P. (2007) · Cell · doi:10.1016/j.cell.2007.08.036 · Cited by 1,826 · 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

Voltage-Gated Calcium Channels

Catterall, W. A. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003947 · Cited by 1,628 · see citing works

Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores

Minta, A., Kao, J. P. Y., & Tsien, R. Y. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83165-9 · Cited by 1,621 · see citing works

A high signal-to-noise Ca2+ probe composed of a single green fluorescent protein

Nakai, J., Ohkura, M., & Imoto, K. (2001) · Nature Biotechnology · doi:10.1038/84397 · Cited by 1,619 · see citing works

A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter

Stefani, D. D., Raffaello, A., Teardo, E., Szabò, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,431 · see citing works

Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels

Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413 · see citing works

The mitochondrial calcium uniporter is a highly selective ion channel

Kirichok, Y., Krapivinsky, G., & Clapham, D. E. (2004) · Nature · doi:10.1038/nature02246 · Cited by 1,409 · see citing works

Structural and functional features and significance of the physical linkage between ER and mitochondria

Csordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377 · see citing works

An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen

Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275 · see citing works

Microdomains with High Ca 2+ Close to IP 3 -Sensitive Channels that Are Sensed by Neighboring Mitochondria

Rizzuto, R., Brini, M., Murgia, M., & Pozzan, T. (1993) · Science · doi:10.1126/science.8235595 · Cited by 1,207 · see citing works

Microdomains of Intracellular Ca2+: Molecular Determinants and Functional Consequences

Rizzuto, R., & Pozzan, T. (2005) · Physiological Reviews · doi:10.1152/physrev.00004.2005 · Cited by 1,201 · see citing works

Inositol Trisphosphate Receptor Ca²⁺Release Channels

Foskett, J. K., White, C., Cheung, K.-H., & Mak, D.-O. D. (2007) · Physiological Reviews · doi:10.1152/physrev.00035.2006 · Cited by 1,188 · 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

Decoding of cytosolic calcium oscillations in the mitochondria

Hajnóczky, G., Gaspers, L. D., Seitz, M. B., & Thomas, A. P. (1995) · Cell · doi:10.1016/0092-8674(95)90430-1 · Cited by 1,110 · see citing works

Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin

Rizzuto, R., Simpson, A. W. M., Brini, M., & Pozzan, T. (1992) · Nature · doi:10.1038/358325a0 · Cited by 931 · see citing works

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 · see citing works

MICU1 encodes a mitochondrial EF hand protein required for Ca2+ uptake

Perocchi, F., Gohil, V. M., Girgis, H. S., Bao, X. R., McCombs, J. E., Palmer, A. E., & Mootha, V. K. (2010) · Nature · doi:10.1038/nature09358 · Cited by 881 · see citing works

The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility

Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871 · see citing works

Dynamic and quantitative Ca 2+ measurements using improved cameleons

Miyawaki, A., Griesbeck, O., Heim, R., & Tsien, R. Y. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2135 · Cited by 822 · see citing works

Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming

Jouaville, L. S., Pinton, P., Bastianutto, C., Rutter, G. A., & Rizzuto, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13807 · Cited by 814 · see citing works

NCLX is an essential component of mitochondrial Na + /Ca 2+ exchange

Palty, R., Silverman, W. F., Hershfinkel, M., Caporale, T., Sensi, S. L., Parnis, J., Nolte, C., Fishman, D., Shoshan‐Barmatz, V., Herrmann, S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908099107 · Cited by 789 · see citing works

Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface

Csordás, G., Várnai, P., Golenár, T., Roy, S., Purkins, G., Schneider, T. G., Balla, T., & Hajnóczky, G. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.029 · Cited by 750 · see citing works

The Inositol Trisphosphate/Calcium Signaling Pathway in Health and Disease

Berridge, M. J. (2016) · Physiological Reviews · doi:10.1152/physrev.00006.2016 · Cited by 748 · see citing works

Coming together to define membrane contact sites

Scorrano, L., Matteis, M. A. D., Emr, S. D., Giordano, F., Hajnóczky, G., Kornmann, B., Lackner, L. L., Levine, T. P., Pellegrini, L., Reinisch, K. M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09253-3 · Cited by 726 · see citing works

Chronic enrichment of hepatic endoplasmic reticulum–mitochondria contact leads to mitochondrial dysfunction in obesity

Arruda, A. P., Pers, B. M., Parlakgül, G., Güney, E., Inouye, K., & Hotamışlıgil, G. S. (2014) · Nature Medicine · doi:10.1038/nm.3735 · Cited by 716 · see citing works

Genetically encoded calcium indicators for multi-color neural activity imaging and combination with optogenetics

Akerboom, J., Calderón, N. C., Tian, L., Wabnig, S., Prigge, M., Tolö, J., Gordus, A. G., Orger, M. B., Severi, K. E., Macklin, J. J., et al. (2013) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2013.00002 · Cited by 710 · see citing works

Critical Stability Constants

Smith, R. M., & Martell, A. E. (1989) · Springer eBooks · doi:10.1007/978-1-4615-6764-6 · Cited by 694 · see citing works

Miro1 Is a Calcium Sensor for Glutamate Receptor-Dependent Localization of Mitochondria at Synapses

MacAskill, A. F., Rinholm, J. E., Twelvetrees, A. E., Arancibia‐Cárcamo, I. L., Muir, J., Fransson, Å., Aspenström, P., Attwell, D., & Kittler, J. T. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.030 · Cited by 677 · see citing works

EMRE Is an Essential Component of the Mitochondrial Calcium Uniporter Complex

Sancak, Y., Markhard, A. L., Kitami, T., Kovács-Bogdán, E., Kamer, K. J., Udeshi, N. D., Carr, S. A., Chaudhuri, D., Clapham, D. E., Li, A. A., et al. (2013) · Science · doi:10.1126/science.1242993 · Cited by 666 · see citing works

MICU1 Is an Essential Gatekeeper for MCU-Mediated Mitochondrial Ca2+ Uptake that Regulates Cell Survival

Mallilankaraman, K. B., Doonan, P. J., Cárdenas, C., Chandramoorthy, H. C. K., Müller, M., Miller, R., Hoffman, N. E., Gandhirajan, R. K., Molgó, J., Birnbaum, M. J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.011 · Cited by 661 · see citing works

The physiological role of mitochondrial calcium revealed by mice lacking the mitochondrial calcium uniporter

Pan, X., Liu, J., Nguyen, T. T. M., Liu, C., Sun, J., Teng, Y., Fergusson, M. M., Rovira, I. I., Allen, M. D., Springer, D., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2868 · Cited by 645 · see citing works

The elementary unit of store-operated Ca2+ entry: local activation of CRAC channels by STIM1 at ER–plasma membrane junctions

Luik, R. M., Wu, M. M., Buchanan, J., & Lewis, R. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604015 · Cited by 639 · see citing works

Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions

Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625 · 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

Relationship between configuration, function, and permeability in calcium-treated mitochondria.

Hunter, D. R., Haworth, R. A., & Southard, J. H. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33220-9 · Cited by 619 · see citing works

PACS‐2 controls endoplasmic reticulum–mitochondria communication and Bid‐mediated apoptosis

Simmen, T., Aslan, J. E., Blagoveshchenskaya, A. D., Thomas, L., Wan, L., Xiang, Y. K., Feliciangeli, S. F., Hung, C., Crump, C. M., & Thomas, G. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600559 · Cited by 593 · see citing works

Mitofusin 2 ablation increases endoplasmic reticulum–mitochondria coupling

Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504880112 · Cited by 578 · see citing works

VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis

Vos, K. J. D., Mórotz, G. M., Stoica, R., Tudor, E. L., Lau, K., Ackerley, S., Warley, A., Shaw, C. E., & Miller, C. C. J. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr559 · Cited by 573 · see citing works

Mitochondrial calcium overload is a key determinant in heart failure

Santulli, G., Xie, W., Reiken, S. R., & Marks, A. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1513047112 · Cited by 561 · see citing works

Mitochondrial Participation in the Intracellular Ca2+ Network

Babcock, D. F., Herrington, J. B., Goodwin, P. C., Park, Y. B., & Hille, B. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.4.833 · Cited by 548 · see citing works

Calcium at the Center of Cell Signaling: Interplay between Endoplasmic Reticulum, Mitochondria, and Lysosomes

Raffaello, A., Mammucari, C., Gherardi, G., & Rizzuto, R. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.001 · Cited by 542 · see citing works

Bidirectional Ca ²⁺ -dependent control of mitochondrial dynamics by the Miro GTPase

Saotome, M., Safiulina, D., Szabadkai, G., Das, S., Fransson, Å., Aspenstrom, P., Rizzuto, R., & Hajnóczky, G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808953105 · Cited by 538 · see citing works

Quasi‐synaptic calcium signal transmission between endoplasmic reticulum and mitochondria

Csordás, G., Thomas, A. P., & Hajnóczky, G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.96 · Cited by 536 · see citing works

The endoplasmic reticulum Ca2+ store: a view from the lumen

Meldolesi, J., & Pozzan, T. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01143-2 · Cited by 528 · see citing works

Mitochondrial Regulation of Store-operated Calcium Signaling in T Lymphocytes

Hoth, M., Fanger, C. M., & Lewis, R. S. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.3.633 · Cited by 505 · see citing works

Apoptosis driven by IP3‐linked mitochondrial calcium signals

Szalai, G., Krishnamurthy, R., & Hajnóczky, G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6349 · Cited by 495 · see citing works

ER-mitochondria tethering by PDZD8 regulates Ca 2+ dynamics in mammalian neurons

Hirabayashi, Y., Kwon, S., Paek, H., Pernice, W. M., Paul, M. A., Lee, J., Erfani, P., Raczkowski, A. M., Petrey, D. S., Pon, L. A., et al. (2017) · Science · doi:10.1126/science.aan6009 · Cited by 495 · see citing works

MICU1 Controls Both the Threshold and Cooperative Activation of the Mitochondrial Ca2+ Uniporter

Csordás, G., Golenár, T., Seifert, E. L., Kamer, K. J., Sancak, Y., Perocchi, F., Moffat, C., Weaver, D., de la Fuente, S., Bogorad, R. L., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.020 · Cited by 491 · see citing works

The mitochondrial calcium uniporter is a multimer that can include a dominant‐negative pore‐forming subunit

Raffaello, A., Stefani, D. D., Sabbadin, D., Teardo, E., Merli, G., Picard, A., Checchetto, V., Moro, S., Szabó, I., & Rizzuto, R. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.157 · Cited by 489 · see citing works

Imaging intraorganellar Ca2+ at subcellular resolution using CEPIA

Suzuki, J., Kanemaru, K., Ishii, K., Ohkura, M., Okubo, Y., & Iino, M. (2014) · Nature Communications · doi:10.1038/ncomms5153 · Cited by 483 · see citing works

Identity, structure, and function of the mitochondrial permeability transition pore: controversies, consensus, recent advances, and future directions

Bernardi, P., Gerle, C., Halestrap, A. P., Jonas, E. A., Karch, J. M., Mnatsakanyan, N., Pavlov, E. V., Sheu, S., & Soukas, A. A. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01187-0 · Cited by 482 · see citing works

Spatial and temporal aspects of cellular calcium signaling

Thomas, A. P., Bird, G. S. J., Hajnóczky, G., Gaspers, L. D., & Putney, J. W. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.13.8940296 · Cited by 480 · see citing works

Control of mitochondrial motility and distribution by the calcium signal

Yi, M., Weaver, D., & Hajnóczky, G. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406038 · Cited by 476 · see citing works

Calcium Channels, Synaptic Plasticity, and Neuropsychiatric Disease

Nanou, E., & Catterall, W. A. (2018) · Neuron · doi:10.1016/j.neuron.2018.03.017 · Cited by 476 · see citing works

A unique mitochondria-associated membrane fraction from rat liver has a high capacity for lipid synthesis and contains pre-Golgi secretory proteins including nascent lipoproteins.

Rusiñol, A. E., Cui, Z., Chen, M. H., & Vance, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47012-3 · Cited by 469 · see citing works

MICU2, a Paralog of MICU1, Resides within the Mitochondrial Uniporter Complex to Regulate Calcium Handling

Plovanich, M., Bogorad, R. L., Sancak, Y., Kamer, K. J., Strittmatter, L., Li, A. A., Girgis, H. S., Kuchimanchi, S., Groot, J. D., Speciner, L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055785 · Cited by 463 · see citing works

A Quantitative Proteome Map of the Human Body

Jiang, L., Wang, M., Lin, S., Jian, R., Li, X., Chan, J., Dong, G., Fang, H., Robinson, A. E., Aguet, F., et al. (2020) · Cell · doi:10.1016/j.cell.2020.08.036 · Cited by 458 · see citing works

CALCIUM UPTAKE BY RAT KIDNEY MITOCHONDRIA

DeLuca, H. F., & Engstrom, G. W. (1961) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.47.11.1744 · Cited by 454 · 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

There's Something Wrong with my MAM; the ER–Mitochondria Axis and Neurodegenerative Diseases

Paillusson, S., Stoica, R., Gomez-Suaga, P., Lau, D. H. W., Mueller, S., Miller, T., & Miller, C. C. J. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.01.008 · Cited by 439 · see citing works

Increased mitochondrial calcium levels associated with neuronal death in a mouse model of Alzheimer’s disease

Calvo-Rodríguez, M., Hou, S. S., Snyder, A. C., Kharitonova, E. K., Russ, A., Das, S., Fan, Z., Muzikansky, A., Garcı́a-Alloza, M., Serrano‐Pozo, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16074-2 · Cited by 432 · see citing works

Molecular mechanisms of mitochondrial dynamics

Tábara, L. C., Segawa, M., & Prudent, J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00785-1 · Cited by 431 · see citing works

Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes

Jouaville, L. S., Ichas, F., Holmuhamedov, E., Camacho, P., & Lechleiter, J. D. (1995) · Nature · doi:10.1038/377438a0 · Cited by 427 · see citing works

Presynaptic Mitochondrial Calcium Sequestration Influences Transmission at Mammalian Central Synapses

Billups, B., & Forsythe, I. D. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-14-05840.2002 · Cited by 414 · see citing works

The ER-Mitochondria Tethering Complex VAPB-PTPIP51 Regulates Autophagy

Gómez‐Suaga, P., Paillusson, S., Stoica, R., Noble, W. J., Hanger, D. P., & Miller, C. C. J. (2017) · Current Biology · doi:10.1016/j.cub.2016.12.038 · Cited by 413 · see citing works

Mitochondrial calcium exchange in physiology and disease

Garbincius, J. F., & Elrod, J. W. (2021) · Physiological Reviews · doi:10.1152/physrev.00041.2020 · Cited by 413 · see citing works

Deficient Endoplasmic Reticulum-Mitochondrial Phosphatidylserine Transfer Causes Liver Disease

Hernández‐Álvarez, M. I., Sebastián, D., Vives, S., Ivanova, S., Bartoccioni, P., Kakimoto, P. A., Plana, N., Veiga, S. R., Hernandez, V. A., Vasconcelos, N., et al. (2019) · Cell · doi:10.1016/j.cell.2019.04.010 · Cited by 400 · see citing works

Ca2+ Hot Spots on the Mitochondrial Surface Are Generated by Ca2+ Mobilization from Stores, but Not by Activation of Store-Operated Ca2+ Channels

Giacomello, M., Drago, I., Bortolozzi, M., Scorzeto, M., Gianelle, A., Pizzo, P., & Pozzan, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.04.003 · Cited by 399 · see citing works

The mitochondrial Na+/Ca2+ exchanger is essential for Ca2+ homeostasis and viability

Luongo, T. S., Lambert, J. P., Gross, P., Nwokedi, M., Lombardi, A. A., Shanmughapriya, S., Carpenter, A. C., Kolmetzky, D., Gao, E., van Berlo, J. H., et al. (2017) · Nature · doi:10.1038/nature22082 · Cited by 396 · see citing works

EFFECT OF ACTIVE ACCUMULATION OF CALCIUM AND PHOSPHATE IONS ON THE STRUCTURE OF RAT LIVER MITOCHONDRIA

Greenawalt, J. W., Rossi, C. S., & Lehninger, A. L. (1964) · The Journal of Cell Biology · doi:10.1083/jcb.23.1.21 · Cited by 378 · see citing works

Loss-of-function mutations in MICU1 cause a brain and muscle disorder linked to primary alterations in mitochondrial calcium signaling

Logan, C. V., Szabadkai, G., Sharpe, J. A., Parry, D. A., Torelli, S., Childs, A., Kriek, M., Phadke, R., Johnson, C. A., Roberts, N. Y., et al. (2013) · Nature Genetics · doi:10.1038/ng.2851 · Cited by 369 · see citing works

α-Synuclein binds to the ER–mitochondria tethering protein VAPB to disrupt Ca2+ homeostasis and mitochondrial ATP production

Paillusson, S., Gómez‐Suaga, P., Stoica, R., Little, D., Gissen, P., Devine, M. J., Noble, W. J., Hanger, D. P., & Miller, C. C. J. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1704-z · Cited by 369 · see citing works

Active mitochondria surrounding the pancreatic acinar granule region prevent spreading of inositol trisphosphate‐evoked local cytosolic Ca2+ signals

Tinel, H., Cancela, J., Mogami, H., Gerasimenko, J. V., Gerasimenko, O. V., Tepikin, A. V., & Petersen, O. H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.4999 · Cited by 361 · see citing works

Calcium content of mitochondria and endoplasmic reticulum in liver frozen rapidly in vivo

Somlyo, A. P., Bond, M., & Somlyo, A. V. (1985) · Nature · doi:10.1038/314622a0 · Cited by 360 · see citing works

Mitochondria-lysosome contacts regulate mitochondrial Ca 2+ dynamics via lysosomal TRPML1

Peng, W., Wong, Y. C., & Krainc, D. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2003236117 · Cited by 342 · see citing works

A survey of the interaction of calcium ions with mitochondria from different tissues and species

Carafoli, E., & Lehninger, A. L. (1971) · Biochemical Journal · doi:10.1042/bj1220681 · Cited by 340 · see citing works

Enhanced Ryanodine Receptor Recruitment Contributes to Ca2+Disruptions in Young, Adult, and Aged Alzheimer's Disease Mice

Stutzmann, G. E., Smith, I. F., Caccamo, A., Oddo, S., LaFerla, F. M., & Parker, I. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0739-06.2006 · Cited by 327 · see citing works

Cloning and sequence analysis of cDNA for the luminescent protein aequorin.

Inouye, S., Noguchi, M., Sakaki, Y., Takagi, Y., Miyata, T., Iwanaga, S., Miyata, T., & Tsuji, F. I. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.10.3154 · Cited by 326 · see citing works

Impaired mitochondrial calcium efflux contributes to disease progression in models of Alzheimer’s disease

Jadiya, P., Kolmetzky, D. W., Tomar, D., Di Meco, A., Lombardi, A. A., Lambert, J. P., Luongo, T. S., Ludtmann, M. H., Praticò, D., & Elrod, J. W. (2019) · Nature Communications · doi:10.1038/s41467-019-11813-6 · Cited by 323 · 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

Presenilin-1 Mutations Increase Levels of Ryanodine Receptors and Calcium Release in PC12 Cells and Cortical Neurons

Chan, S. L., Mayne, M. B., Holden, C. P., Geiger, J. D., & Mattson, M. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000040200 · Cited by 314 · see citing works

Redox Nanodomains Are Induced by and Control Calcium Signaling at the ER-Mitochondrial Interface

Booth, D. M., Enyedi, B., Geiszt, M., Várnai, P., & Hajnóczky, G. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.040 · Cited by 310 · see citing works

Mitochondrial calcium transport

Nicholls, D. G., & Crompton, M. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)80806-4 · Cited by 308 · see citing works

Structure and mechanism of the mitochondrial Ca2+ uniporter holocomplex

Fan, M., Zhang, J., Tsai, C.-W., Orlando, B. J., Rodriguez, M. X., Xu, Y., Liao, M., Tsai, M.-F., & Feng, L. (2020) · Nature · doi:10.1038/s41586-020-2309-6 · Cited by 307 · see citing works

DJ-1 regulates the integrity and function of ER-mitochondria association through interaction with IP3R3-Grp75-VDAC1

Liu, Y., Ma, X., Fujioka, H., Liu, J., Chen, S., & Zhu, X. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1906565116 · Cited by 299 · see citing works

Mitochondria Exert a Negative Feedback on the Propagation of Intracellular Ca2+ Waves in Rat Cortical Astrocytes

Boitier, E., Rea, R., & Duchen, M. R. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.4.795 · Cited by 298 · see citing works

IP3 receptor isoforms differently regulate ER-mitochondrial contacts and local calcium transfer

Bartók, Á., Weaver, D., Golenár, T., Nichtová, Z., Katona, M., Bánsághi, S., Alzayady, K. J., Thomas, V. K., Ando, H., Mikoshiba, K., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11646-3 · Cited by 294 · see citing works

CaV1 and CaV2 Channels Engage Distinct Modes of Ca2+ Signaling to Control CREB-Dependent Gene Expression

Wheeler, D. G., Groth, R. D., Ma, H., Barrett, C. F., Owen, S. F., Safa, P., & Tsien, R. W. (2012) · Cell · doi:10.1016/j.cell.2012.03.041 · Cited by 287 · see citing works

Non-canonical function of IRE1α determines mitochondria-associated endoplasmic reticulum composition to control calcium transfer and bioenergetics

Carreras‐Sureda, A., Jaña, F., Urra, H., Durand, S., Mortenson, D. E., Sagredo, A. I., Bustos, G., Hazari, Y., Ramos‐Fernández, E., Sassano, M. L., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0329-y · Cited by 286 · see citing works

Presenilin 2 modulates endoplasmic reticulum (ER)–mitochondria interactions and Ca 2+ cross-talk

Zampese, E., Fasolato, C., Kipanyula, M. J., Bortolozzi, M., Pozzan, T., & Pizzo, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100735108 · Cited by 285 · see citing works

VDAC closure increases calcium ion flux

Tan, W., & Colombini, M. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.06.002 · Cited by 281 · see citing works

Dysregulated IP3Signaling in Cortical Neurons of Knock-In Mice Expressing an Alzheimer's-Linked Mutation inPresenilin1Results in Exaggerated Ca2+Signals and Altered Membrane Excitability

Stutzmann, G. E., Caccamo, A., LaFerla, F. M., & Parker, I. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4386-03.2004 · Cited by 278 · see citing works

Presynaptic calcium channels: specialized control of synaptic neurotransmitter release

DOLPHIN, A. C., & Lee, A. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-020-0278-2 · Cited by 274 · see citing works

The Type III Inositol 1,4,5-Trisphosphate Receptor Preferentially Transmits Apoptotic Ca2+ Signals into Mitochondria

Mendes, C. C. P., Gomes, D. A., Thompson, M., Souto, N. C., Góes, T. S., Goes, A. M., Rodrigues, M. Â., Gomez, M. V., Nathanson, M. H., & Leite, M. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506623200 · Cited by 270 · see citing works

Mitochondria Recycle Ca2+ to the Endoplasmic Reticulum and Prevent the Depletion of Neighboring Endoplasmic Reticulum Regions

Arnaudeau, S., Kelley, W. L., Walsh, J. V., & Demaurex, N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103274200 · Cited by 269 · see citing works

Mitochondrial control of calcium-channel gating: A mechanism for sustained signaling and transcriptional activation in T lymphocytes

Hoth, M., Button, D. C., & Lewis, R. S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.180143997 · Cited by 269 · see citing works

Mitochondria Suppress Local Feedback Activation of Inositol 1,4,5-Trisphosphate Receptors by Ca2+

Hajnóczky, G., Hager, R., & Thomas, A. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.20.14157 · Cited by 263 · see citing works

MFF-dependent mitochondrial fission regulates presynaptic release and axon branching by limiting axonal mitochondria size

Lewis, T. L., Kwon, S.-K., Lee, A., Shaw, R., & Polleux, F. (2018) · Nature Communications · doi:10.1038/s41467-018-07416-2 · Cited by 260 · see citing works

The mitochondrial calcium uniporter regulates breast cancer progression via HIF‐1α

Tosatto, A., Sommaggio, R., Kummerow, C., Bentham, R. B., Blacker, T. S., Berecz, T., Duchen, M. R., Rosato, A., Bogeski, I., Szabadkai, G., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606255 · Cited by 258 · see citing works

Visualization and Manipulation of Plasma Membrane-Endoplasmic Reticulum Contact Sites Indicates the Presence of Additional Molecular Components within the STIM1-Orai1 Complex

Várnai, P., Tóth, B. I., Tóth, D. J., Hunyady, L., & Balla, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704339200 · Cited by 247 · see citing works

Transient Mitochondrial Depolarizations Reflect Focal Sarcoplasmic Reticular Calcium Release in Single Rat Cardiomyocytes

Duchen, M. R., Leyssens, A., & Crompton, M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.4.975 · Cited by 246 · see citing works

Propagation of the apoptotic signal by mitochondrial waves

Pacher, P., & Hajnóczky, G. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4107 · Cited by 240 · see citing works

Calcium-release channels: structure and function of IP3 receptors and ryanodine receptors

Woll, K. A., & Petegem, F. V. (2021) · Physiological Reviews · doi:10.1152/physrev.00033.2020 · Cited by 237 · see citing works

Three-dimensional architecture of extended synaptotagmin-mediated endoplasmic reticulum–plasma membrane contact sites

Fernández‐Busnadiego, R., Saheki, Y., & Camilli, P. V. D. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1503191112 · Cited by 235 · see citing works

A key role for MAM in mediating mitochondrial dysfunction in Alzheimer disease

Area-Gomez, E., de Groof, A., Bonilla, E., Montesinos, J., Tanji, K., Boldogh, I., Pon, L., & Schon, E. A. (2018) · Cell Death & Disease · doi:10.1038/s41419-017-0215-0 · Cited by 235 · see citing works

Elementary events of InsP3-induced Ca2+ liberation in Xenopus oocytes: hot spots, puffs and blips

Parker, I., Choi, J., & Yao, Y. (1996) · Cell Calcium · doi:10.1016/s0143-4160(96)90100-1 · Cited by 233 · see citing works

Altered ER–mitochondria contact impacts mitochondria calcium homeostasis and contributes to neurodegeneration in vivo in disease models

Lee, K., Huh, S., Lee, S., Wu, Z., Kim, A., Kang, H., & Lu, B. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1721136115 · Cited by 233 · see citing works

Respiring mitochondria determine the pattern of activation and inactivation of the store‐operated Ca2+ current ICRAC

Gilabert, J., & Parekh, A. B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.23.6401 · Cited by 231 · see citing works

Endoplasmic reticulum calcium release through ITPR2 channels leads to mitochondrial calcium accumulation and senescence

Wiel, C., Lallet-Daher, H., Gitenay, D., Gras, B., Le Calvé, B., Augert, A., Ferrand, M., Prevarskaya, N., Simonnet, H., Vindrieux, D., et al. (2014) · Nature Communications · doi:10.1038/ncomms4792 · Cited by 231 · see citing works

Making the connection: How membrane contact sites have changed our view of organelle biology

Voeltz, G. K., Sawyer, E. M., Hajnóczky, G., & Prinz, W. A. (2024) · Cell · doi:10.1016/j.cell.2023.11.040 · Cited by 230 · see citing works

Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein

Prasher, D. C., McCann, R. O., & Cormier, M. J. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)90321-3 · Cited by 227 · see citing works

Anti-immunoglobulin, cytoplasmic free calcium, and capping in B lymphocytes.

Pozzan, T., Arslan, P., Tsien, R. Y., & RINK, T. J. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.94.2.335 · Cited by 225 · see citing works

Ca2+-dependent Control of the Permeability Properties of the Mitochondrial Outer Membrane and Voltage-dependent Anion-selective Channel (VDAC)

Báthori, G., Csordás, G., Garcı́a-Pérez, C., Davies, E., & Hajnóczky, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600906200 · Cited by 224 · 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

MICU3 is a tissue-specific enhancer of mitochondrial calcium uptake

Patrón, M., Granatiero, V., Espino, J., Rizzuto, R., & Stefani, D. D. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0113-8 · Cited by 220 · see citing works

Calcium Signal Transmission between Ryanodine Receptors and Mitochondria

Szalai, G., Csordás, G., Hantash, B. M., Thomas, A. P., & Hajnóczky, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.15305 · Cited by 218 · see citing works

MICU1 and MICU2 play nonredundant roles in the regulation of the mitochondrial calcium uniporter

Kamer, K. J., & Mootha, V. K. (2014) · EMBO Reports · doi:10.1002/embr.201337946 · Cited by 218 · see citing works

Interactions between sarco-endoplasmic reticulum and mitochondria in cardiac and skeletal muscle – pivotal roles in Ca2+ and reactive oxygen species signaling

Eisner, V., Csordás, G., & Hajnóczky, G. (2013) · Journal of Cell Science · doi:10.1242/jcs.093609 · Cited by 215 · see citing works

Mechanisms underlying the loss of mitochondrial membrane potential in glutamate excitotoxicity

Abramov, A. Y., & Duchen, M. R. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.017 · Cited by 213 · see citing works

Calcium microdomains at the immunological synapse: how ORAI channels, mitochondria and calcium pumps generate local calcium signals for efficient T‐cell activation

Quintana, A., Pasche, M., Junker, C., Alansary, D., Rieger, H., Kummerow, C., Núñez, L., Villalobos, C., Meraner, P., Becherer, U., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.289 · Cited by 210 · 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

Calcium channel ITPR2 and mitochondria–ER contacts promote cellular senescence and aging

Ziegler, D. V., Vindrieux, D., Goehrig, D., Jaber, S., Collin, G., Griveau, A., Wiel, C., Bendridi, N., Djebali, S., Farfariello, V., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-20993-z · Cited by 195 · see citing works

LKB1 Regulates Mitochondria-Dependent Presynaptic Calcium Clearance and Neurotransmitter Release Properties at Excitatory Synapses along Cortical Axons

Kwon, S., Sando, R. C., Lewis, T. L., Hirabayashi, Y., Maximov, A., & Polleux, F. (2016) · PLoS Biology · doi:10.1371/journal.pbio.1002516 · Cited by 194 · 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

Hearts deficient in both Mfn1 and Mfn2 are protected against acute myocardial infarction

Hall, A. R., Burke, N., Dongworth, R. K., Kalkhoran, S. B., Dyson, A., Vicencio, J. M., Dorn, G. W., Yellon, D. M., & Hausenloy, D. J. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.139 · Cited by 190 · see citing works

Transport of Ca2+ from Sarcoplasmic Reticulum to Mitochondria in Rat Ventricular Myocytes

Sharma, V. K., Ramesh, V., Franzini‐Armstrong, C., & Sheu, S. S. (2000) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005520714221 · Cited by 186 · see citing works

Prevention by chlorpromazine of ischemic liver cell death.

Chien, K. R., Abrams, J., Pfau, R. G., & Farber, J. L. (1977) · PubMed Central · Cited by 186 · see citing works

Dynamic pacing of cell metabolism by intracellular Ca2+ transients.

Pralong, W. F., Spät, A., & Wollheim, C. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46986-4 · Cited by 185 · see citing works

Transglutaminase Type 2 Regulates ER-Mitochondria Contact Sites by Interacting with GRP75

D’Eletto, M., Rossin, F., Occhigrossi, L., Farrace, M. G., Faccenda, D., Desai, R., Marchi, S., Refolo, G., Falasca, L., Antonioli, M., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.094 · Cited by 185 · see citing works

Calcium regulates cell death in cancer: Roles of the mitochondria and mitochondria-associated membranes (MAMs)

Danese, A., Patergnani, S., Bonora, M., Wieckowski, M. R., Previati, M., Giorgi, C., & Pinton, P. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.01.003 · Cited by 184 · see citing works

Structure and Function of IP 3 ReceptorsPreprint

Prole, D. L., & Taylor, C. W. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a035063 · Cited by 184 · see citing works

Mitochondrial fusion is frequent in skeletal muscle and supports excitation–contraction coupling

Eisner, V., Lenaers, G., & Hajnóczky, G. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201312066 · Cited by 177 · see citing works

Sustained Ca2+ Transfer across Mitochondria Is Essential for Mitochondrial Ca2+ Buffering, Store-operated Ca2+ Entry, and Ca2+ Store Refilling

Malli, R., Frieden, M., Osibow, K., Zoratti, C., Mayer, M., Demaurex, N., & Graier, W. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302511200 · Cited by 175 · see citing works

Power Grid Protection of the Muscle Mitochondrial Reticulum

Glancy, B., Hartnell, L. M., Combs, C. A., Femnou, A., Sun, J., Murphy, E., Subramaniam, S., & Balaban, R. S. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.063 · Cited by 172 · see citing works

Mitochondria, OxPhos, and neurodegeneration: cells are not just running out of gas

Área-Gómez, E., Guardia‐Laguarta, C., Schon, E. A., & Przedborski, S. (2019) · Journal of Clinical Investigation · doi:10.1172/jci120848 · Cited by 169 · see citing works

Evidence that mitochondria buffer physiological Ca2+ loads in lizard motor nerve terminals

David, G., Barrett, J. N., & Barrett, E. F. (1998) · The Journal of Physiology · doi:10.1111/j.1469-7793.1998.059bo.x · Cited by 168 · see citing works

Balancing ER-Mitochondrial Ca2+ Fluxes in Health and Disease

Loncke, J., Kaasik, A., Борисович, Б. И., Parys, J. B., Kerkhofs, M., & Bultynck, G. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.02.003 · Cited by 168 · see citing works

Model of Sarcomeric Ca2+ Movements, Including ATP Ca2+ Binding and Diffusion, during Activation of Frog Skeletal Muscle

Baylor, S. M., & Hollingworth, S. (1998) · The Journal of General Physiology · doi:10.1085/jgp.112.3.297 · Cited by 167 · see citing works

Enhanced caffeine‐induced Ca2+release in the 3xTg‐AD mouse model of Alzheimer's disease

Smith, I. F., Hitt, B. D., Green, K. N., Oddo, S., & LaFerla, F. M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03332.x · Cited by 164 · see citing works

The Integration of Mitochondrial Calcium Transport and Storage

Nicholls, D. G., & Chalmers, S. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041753.52832.f3 · Cited by 162 · see citing works

Mitochondrial fusion dynamics is robust in the heart and depends on calcium oscillations and contractile activity

Eisner, V., Cupo, R. R., Gao, E., Csordás, G., Slovinsky, W. S., Paillard, M., Cheng, L., Ibetti, J., Chen, S. R. W., Chuprun, J. K., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617288114 · Cited by 161 · see citing works

VPS13D bridges the ER to mitochondria and peroxisomes via Miro

Guillén-Samander, A., Leonzino, M., Hanna, M. G., Tang, N., Shen, H., & Camilli, P. V. D. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202010004 · Cited by 159 · see citing works

Splice variants of mitofusin 2 shape the endoplasmic reticulum and tether it to mitochondria

Naón, D., Hernández‐Álvarez, M. I., Shinjo, S., Wieczór, M., Ivanova, S., de Brito, O. M., Quintana, A., Hidalgo, J., Palacı́n, M., Aparicio, P., et al. (2023) · Science · doi:10.1126/science.adh9351 · Cited by 158 · see citing works

TOM70 Sustains Cell Bioenergetics by Promoting IP3R3-Mediated ER to Mitochondria Ca2+ Transfer

Filadi, R., Leal, N. S., Schreiner, B., Rossi, A., Dentoni, G., Pinho, C. M., Wiehager, B., Cieri, D., Calí, T., Pizzo, P., et al. (2018) · Current Biology · doi:10.1016/j.cub.2017.12.047 · Cited by 158 · see citing works

Physiology of intracellular calcium buffering

Eisner, D. A., Neher, E., Taschenberger, H., & Smith, G. L. (2023) · Physiological Reviews · doi:10.1152/physrev.00042.2022 · Cited by 158 · see citing works

Ca 2+ marks: Miniature calcium signals in single mitochondria driven by ryanodine receptors

Pacher, P., Thomas, A. P., & Hajnóczky, G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032423699 · Cited by 152 · see citing works

ER-mitochondria cross-talk is regulated by the Ca 2+ sensor NCS1 and is impaired in Wolfram syndrome

Angebault, C., Fauconnier, J., Patergnani, S., Rieusset, J., Danese, A., Affortit, C., Jagodzinska, J., Piro-Mégy, C., Quilès, M., Cazevieille, C., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aaq1380 · Cited by 149 · see citing works

Ca2+ signals initiate at immobile IP3 receptors adjacent to ER-plasma membrane junctions

Thillaiappan, N. B., Chavda, A. P., Tovey, S. C., Prole, D. L., & Taylor, C. W. (2017) · Nature Communications · doi:10.1038/s41467-017-01644-8 · Cited by 149 · see citing works

Ca2+ signalling in the Golgi apparatus

Pizzo, P., Lissandron, V., Capitanio, P., & Pozzan, T. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.01.006 · Cited by 148 · see citing works

The Role of Mitochondria for Ca2+ Refilling of the Endoplasmic Reticulum

Malli, R., Frieden, M., Trenker, M., & Graier, W. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409353200 · Cited by 147 · see citing works

Endoplasmic reticulum-mitochondria miscommunication is an early and causal trigger of hepatic insulin resistance and steatosis

Beaulant, A., Dia, M., Pillot, B., Chauvin, M., Ji-cao, J., Durand, C., Bendridi, N., Chanon, S., Vieille‐Marchiset, A., Silva, C. C. D., et al. (2022) · Journal of Hepatology · doi:10.1016/j.jhep.2022.03.017 · Cited by 147 · see citing works

Inositol 1,4,5‐trisphosphate receptors and their protein partners as signalling hubs

Prole, D. L., & Taylor, C. W. (2016) · The Journal of Physiology · doi:10.1113/jp271139 · Cited by 146 · see citing works

FATE1 antagonizes calcium‐ and drug‐induced apoptosis by uncoupling ER and mitochondria

Doghman, M., Granatiero, V., Sbiera, S., Sbiera, I., Lacas‐Gervais, S., Brau, F., Faßnacht, M., Rizzuto, R., & Lalli, E. (2016) · EMBO Reports · doi:10.15252/embr.201541504 · Cited by 144 · see citing works

High‐affinity cooperative Ca2+ binding by MICU1–MICU2 serves as an on–off switch for the uniporter

Kamer, K. J., Grabarek, Z., & Mootha, V. K. (2017) · EMBO Reports · doi:10.15252/embr.201643748 · Cited by 144 · see citing works

Functional reconstitution of the mitochondrial Ca2+/H+ antiporter Letm1

Tsai, M.-F., Jiang, D., Zhao, L., Clapham, D. E., & Miller, C. (2013) · The Journal of General Physiology · doi:10.1085/jgp.201311096 · Cited by 142 · see citing works

VDAC regulation of mitochondrial calcium flux: From channel biophysics to disease

Rosencrans, W. M., Rajendran, M., Bezrukov, S. M., & Rostovtseva, T. K. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102356 · Cited by 142 · see citing works

Phospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes

Yeo, H. K., Park, T. H., Kim, H. Y., Jang, H., Lee, J., Hwang, G., Ryu, S. E., Park, S. H., Song, H. K., Ban, H. S., et al. (2021) · EMBO Reports · doi:10.15252/embr.202051323 · Cited by 142 · see citing works

Mitochondrial calcium transport and the redox nature of the calcium-induced membrane permeability transition

Vercesi, A. E., Castilho, R. F., Kowaltowski, A. J., Oliveira, H. C. F., de Souza-Pinto, N. C., Figueira, T. R., & Busanello, E. N. B. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.034 · Cited by 141 · see citing works

Regulation of NAD+-linked isocitrate dehydrogenase and 2-oxoglutarate dehydrogenase by Ca2+ ions within toluene-permeabilized rat heart mitochondria. Interactions with regulation by adenine nucleotides and NADH/NAD+ ratios

Rutter, G. A., & Denton, R. M. (1988) · Biochemical Journal · doi:10.1042/bj2520181 · Cited by 138 · see citing works

MICU1 controls cristae junction and spatially anchors mitochondrial Ca2+ uniporter complex

Gottschalk, B., Klec, C., Leitinger, G., Bernhart, E. M., Rost, R., Bischof, H., Madreiter‐Sokolowski, C. T., Radulović, S., Eroğlu, E., Sattler, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11692-x · Cited by 136 · see citing works

Systematic Identification of MCU Modulators by Orthogonal Interspecies Chemical Screening

Arduíno, D. M., Wettmarshausen, J., Vais, H., Navas-Navarro, P., Cheng, Y., Leimpek, A., Ma, Z., Delrio-Lorenzo, A., Giordano, A., Garcı́a-Pérez, C., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.07.019 · Cited by 134 · see citing works

High- and low-calcium-dependent mechanisms of mitochondrial calcium signalling

Spät, A., Szanda, G., Csordás, G., & Hajnóczky, G. (2008) · Cell Calcium · doi:10.1016/j.ceca.2007.11.015 · Cited by 131 · see citing works

Physiological Functions of CRAC Channels

Emrich, S. M., Yoast, R. E., & Trebak, M. (2021) · Annual Review of Physiology · doi:10.1146/annurev-physiol-052521-013426 · Cited by 129 · see citing works

Miro1‐dependent mitochondrial positioning drives the rescaling of presynaptic Ca2+ signals during homeostatic plasticity

Vaccaro, V., Devine, M. J., Higgs, N., & Kittler, J. T. (2016) · EMBO Reports · doi:10.15252/embr.201642710 · Cited by 127 · see citing works

Long-Term Potentiation Requires a Rapid Burst of Dendritic Mitochondrial Fission during Induction

Divakaruni, S. S., Dyke, A. M. V., Chandra, R., LeGates, T. A., Contreras, M., Dharmasri, P. A., Higgs, H. N., Lobo, M. K., Thompson, S. M., & Blanpied, T. A. (2018) · Neuron · doi:10.1016/j.neuron.2018.09.025 · Cited by 126 · see citing works

NCLX Protein, but Not LETM1, Mediates Mitochondrial Ca2+ Extrusion, Thereby Limiting Ca2+-induced NAD(P)H Production and Modulating Matrix Redox State

Marchi, U. D., Domingo, J. S., Castelbou, C., Sekler, I., Wiederkehr, A., & Demaurex, N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.540898 · Cited by 120 · see citing works

A turquoise fluorescence lifetime-based biosensor for quantitative imaging of intracellular calcium

van der Linden, F. H., Mahlandt, E. K., Arts, J. J. G., Beumer, J., Puschhof, J., de Man, S. M. A., Chertkova, A. O., Ponsioen, B., Clevers, H. C., van Buul, J. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27249-w · Cited by 120 · see citing works

VDAC2-specific cellular functions and the underlying structure

Naghdi, S., & Hajnóczky, G. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.04.020 · Cited by 117 · see citing works

MICU1 Interacts with the D-Ring of the MCU Pore to Control Its Ca2+ Flux and Sensitivity to Ru360

Paillard, M., Csordás, G., Huang, K., Várnai, P., Joseph, S. K., & Hajnóczky, G. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.09.008 · Cited by 117 · see citing works

ER–Mitochondria contact sites: A new regulator of cellular calcium flux comes into play

Krols, M., Bultynck, G., & Janssens, S. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201607124 · Cited by 111 · see citing works

MFN2 mutations in Charcot–Marie–Tooth disease alter mitochondria-associated ER membrane function but do not impair bioenergetics

Larrea, D., Pera, M., Gonnelli, A., Quintana–Cabrera, R., Akman, H. O., Guardia‐Laguarta, C., VELASCO, K. R., Área-Gómez, E., Bello, F. D., Stefani, D. D., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz008 · Cited by 110 · see citing works

Mitochondria Positioning Controls Local Calcium Influx in T Cells

Schwindling, C., Quintana, A., Krause, E., & Hoth, M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0902872 · Cited by 110 · see citing works

Individual Cardiac Mitochondria Undergo Rare Transient Permeability Transition Pore Openings

Lu, X., Kwong, J. Q., Molkentin, J. D., & Bers, D. M. (2015) · Circulation Research · doi:10.1161/circresaha.115.308093 · Cited by 109 · see citing works

Mitochondria control store‐operated Ca2+ entry through Na+ and redox signals

Nissim, T. B. K., Zhang, X., Elazar, A., Roy, S., Stolwijk, J. A., Zhou, Y., Motiani, R. K., Guéguinou, M., Hempel, N., Hershfinkel, M., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201592481 · Cited by 109 · see citing works

ER-Mitochondria Communication. How Privileged?

Franzini-Armstrong, C. (2007) · Physiology · doi:10.1152/physiol.00017.2007 · Cited by 109 · see citing works

Stable Golgi-Mitochondria Complexes and Formation of Golgi Ca2+ Gradients in Pancreatic Acinar Cells

Dolman, N. J., Gerasimenko, J. V., Gerasimenko, O. V., Voronina, S. G., Petersen, O. H., & Tepikin, A. V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412694200 · Cited by 108 · see citing works

Calcium-induced conformational changes of the regulatory domain of human mitochondrial aspartate/glutamate carriers

Thangaratnarajah, C., Ruprecht, J. J., & Kunji, E. R. S. (2014) · Nature Communications · doi:10.1038/ncomms6491 · Cited by 107 · see citing works

The mitochondrial permeability transition pore is a dispensable element for mitochondrial calcium efflux

Marchi, E. D., Bonora, M., Giorgi, C., & Pinton, P. (2014) · Cell Calcium · doi:10.1016/j.ceca.2014.03.004 · Cited by 103 · see citing works

Homozygous deletion in MICU1 presenting with fatigue and lethargy in childhood

Lewis‐Smith, D., Kamer, K. J., Griffin, H. R., Childs, A., Pysden, K., Titov, D. V., Duff, J., Pyle, A., Taylor, R. W., Yu‐Wai‐Man, P., et al. (2016) · Neurology Genetics · doi:10.1212/nxg.0000000000000059 · Cited by 103 · see citing works

A High-Throughput Screening Identifies MICU1 Targeting Compounds

Marco, G. D., Vallese, F., Jourde, B., Bergsdorf, C., Sturlese, M., Mario, A. D., Techer-Etienne, V., Haasen, D., Oberhauser, B., Schleeger, S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.01.081 · Cited by 103 · see citing works

Amyloid β Oligomers Increase ER-Mitochondria Ca2+ Cross Talk in Young Hippocampal Neurons and Exacerbate Aging-Induced Intracellular Ca2+ Remodeling

Calvo-Rodríguez, M., Hernando-Pérez, E., Núñez, L., & Villalobos, C. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00022 · Cited by 101 · see citing works

OPA1 promotes pH flashes that spread between contiguous mitochondria without matrix protein exchange

Domingo, J. S., Giacomello, M., Poburko, D., Scorrano, L., & Demaurex, N. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.124 · Cited by 100 · see citing works

Dysregulation of Mitochondrial Ca2+ Uptake and Sarcolemma Repair Underlie Muscle Weakness and Wasting in Patients and Mice Lacking MICU1

Debattisti, V., Horn, A. J., Singh, R. P., Seifert, E. L., Hogarth, M. W., Mázala, D. A. G., Huang, K. T., Horváth, R., Jaiswal, J. K., & Hajnóczky, G. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.063 · Cited by 100 · see citing works

The contribution of the SPCA1 Ca2+ pump to the Ca2+ accumulation in the Golgi apparatus of HeLa cells assessed via RNA-mediated interference

Baelen, K. V., Vanoevelen, J. M., Callewaert, G., Parys, J. B., SMEDT, H. D., Raeymaekers, L., Rizzuto, R., Missiaen, L., & Wuytack, F. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00977-x · Cited by 95 · see citing works

Polycystin 2 regulates mitochondrial Ca 2+ signaling, bioenergetics, and dynamics through mitofusin 2

Kuo, I. Y., Brill, A. L., Lemos, F. O., Jiang, J., Falcone, J. L., Kimmerling, E. P., Cai, Y., Dong, K., Kaplan, D. L., Wallace, D. P., et al. (2019) · Science Signaling · doi:10.1126/scisignal.aat7397 · Cited by 95 · see citing works

The role of calcium in the regulation of mitochondrial metabolism

Denton, R. M., & McCormack, J. G. (1980) · Biochemical Society Transactions · doi:10.1042/bst0080266 · Cited by 95 · see citing works

Capture at the ER-mitochondrial contacts licenses IP3 receptors to stimulate local Ca2+ transfer and oxidative metabolism

Katona, M., Bartók, Á., Nichtová, Z., Csordás, G., Berezhnaya, E. V., Weaver, D., Ghosh, A., Várnai, P., Yule, D. I., & Hajnóczky, G. (2022) · Nature Communications · doi:10.1038/s41467-022-34365-8 · Cited by 94 · see citing works

The mitochondrial phosphate carrier: Role in oxidative metabolism, calcium handling and mitochondrial disease

Seifert, E. L., Ligeti, E., Mayr, J. A., Sondheimer, N., & Hajnóczky, G. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.06.031 · Cited by 90 · see citing works

Mitochondria-organelle crosstalk in establishing compartmentalized metabolic homeostasis

Chen, B., Lyssiotis, C. A., & Shah, Y. M. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.03.003 · Cited by 78 · see citing works

Super mitochondria-enriched extracellular vesicles enable enhanced mitochondria transfer

Wang, Y., Yu, H., Yi, Z.-J., Qi, L., Yang, J.-S., Xie, H.-X., Zhao, M., Liu, N.-H., Chen, J., Zhou, T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64486-9 · Cited by 71 · see citing works

Mitochondrial dysfunction in diabetic ulcers: pathophysiological mechanisms and targeted therapeutic strategies

Yu, P., Chen, L. Y., Chen, Y., Thomas, E. R., Zhou, S., Yang, Y., Liu, K., Wu, J., & Li, X. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1625474 · Cited by 32 · see citing works

Urolithin Α modulates inter-organellar communication via calcium-dependent mitophagy to promote healthy ageing

Roussos, A., Kitopoulou, K., Borbolis, F., Ploumi, C., Gianniou, D. D., Li, Z., He, H., Tsakiri, E. N., Madsen, H. B., Kostakis, I. K., et al. (2025) · Autophagy · doi:10.1080/15548627.2025.2561073 · Cited by 31 · see citing works

Recent advances in the mitochondria-targeting small molecule fluorescent probes: from the principal design to biological applications

Zhang, D., Ding, Y., Zhang, Z., Zhang, L., Huang, Z., Shen, Q., Wu, Q., Li, L., & Yu, C. (2025) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2025.217229 · Cited by 29 · see citing works

Impact of reactive oxygen species on bone regeneration in diabetes: Mechanisms and therapeutic strategies

Tian, K., Xiong, T., Zeng, D., Huang, Z., Liu, R., & Luo, F. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103941 · Cited by 19 · see citing works

Impaired Atrial Mitochondrial Calcium Handling in Patients With Atrial Fibrillation

Pronto, J. R. D., Mason, F. E., Rog‐Zielinska, E. A., Fakuade, F. E., Bülow, D., Tóth, M., Machwart, K., Brandes, P., Wiedmann, F., Kohlhaas, M., et al. (2025) · Circulation Research · doi:10.1161/circresaha.124.325658 · Cited by 12 · see citing works

Mitochondrial homeostasis dysregulation: Potential mechanisms of Alzheimer's disease mediated by TDP-43

Huang, W., Huang, J., Kuang, N., Wu, J., Feng, F., Luo, Y., & Huang, N. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103290 · Cited by 12 · see citing works

VBIT-4 Rescues Mitochondrial Dysfunction and Reduces Skeletal Muscle Degeneration in a Severe Model of Duchenne Muscular Dystrophy

Dubinin, M. V., Stepanova, A. E., Mikheeva, I. B., Igoshkina, A. D., Kraeva, E. N., Cherepanova, A. A., Talanov, E. Y., Polikarpova, A. V., Astashev, M. E., Loginov, V. A., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26188845 · Cited by 12 · see citing works

Targeting mitochondrial homeostasis as a cancer treatment strategy: current status and future prospects

Zhong, H., Pan, R., Ouyang, Y., Xiao, T., Gu, W., Yang, H., Wang, H., Li, H., Peng, T., & Chen, P. (2026) · Molecular Cancer · doi:10.1186/s12943-026-02571-3 · Cited by 13 · see citing works

Magnetically Stimulated Myogenesis Recruits a CRY2-TRPC1 Photosensitive Signaling Axis

Iversen, J. N., Tai, Y. K., Wu, K. Y., Wong, C. J. K., Lim, H. Y., & Franco‐Obregón, A. (2025) · Cells · doi:10.3390/cells14030231 · Cited by 8 · see citing works

Calcium Regulation of Mitochondrial Metabolism

Mannella, C. A., Swietach, P., & Boyman, L. (2025) · Annual Review of Physiology · doi:10.1146/annurev-physiol-052424-082740 · Cited by 8 · see citing works

Mitochondrial specialization and signaling shape neuronal function

Tong, B. C., Gubinelli, F., Burbulla, L. F., & Harbauer, A. B. (2026) · Trends in Neurosciences · doi:10.1016/j.tins.2025.12.006 · Cited by 9 · see citing works

The Multifaceted Role of Calcium Signaling in Regulated Necrosis

Pérez-Rivera, E., Plasencia, C., & Ros, U. (2025) · Biomolecules · doi:10.3390/biom15060854 · Cited by 7 · see citing works

Mitochondrial Dysfunction: The Cellular Bridge from Emotional Stress to Disease Onset: A Narrative Review

Venkatesan, S., Comi, C., Marchi, F. D., Esposito, T., Gramaglia, C. M., Smirne, C., Pour, M. M. O., Pirisi, M., Vaschetto, R., Zeppegno, P., et al. (2026) · Biomolecules · doi:10.3390/biom16010117 · Cited by 10 · see citing works

Matrix mechanical remodeled carrier-free nanosystem for programmable closed-loop reversal of liver fibrosis via STING alkylation

Han, H., Yu, D., Liu, Y., Jia, H., & Liu, W. (2025) · Science Advances · doi:10.1126/sciadv.adz4126 · Cited by 7 · see citing works

The cGAS-STING pathway in aging and neurological diseases: From mechanisms to treatment

Li, Y., Chen, Y., Liu, Y., Wang, C., Fu, X., & Ren, M. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111978 · Cited by 5 · see citing works

Mitochondrial homeostasis: A key regulator in endometrial physiology and pathology

Zhang, K.-K., Zhang, E., Wu, K., Cheng, W., & Wei, S. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104519 · Cited by 5 · see citing works

Mitochondria as key targets underlying hypomagnetic field-induced biological effects

Ren, J., Wang, M., Zhao, C., Luo, Y., & Tian, L. (2025) · iScience · doi:10.1016/j.isci.2025.114389 · Cited by 5 · see citing works

A Mesoporous Calcium Peroxide Nanocuboid with High Tumor Accumulation Across Biological Barriers for High Efficacy Tumor Therapy

Fan, Q., Wang, M., Lin, J., Huang, Y., Yang, H. J., Zhu, J., Ren, B. W., Sun, L. X., Li, Z., Liu, A., et al. (2025) · Advanced Science · doi:10.1002/advs.202510778 · Cited by 5 · see citing works

Mechanical stress facilitates calcium influx and growth of alveolar epithelial cells via activation of the BDKRB1/Ca2+/CaMKII/MEK1/ERK axis

Zhang, Y., Zhang, Q., Li, Q., Shi, Z.-Y., Pan, C., Yan, R., Fei, D., Xu, S., & Luo, Y. (2025) · Respiratory Research · doi:10.1186/s12931-025-03240-7 · Cited by 4 · see citing works

Mitochondrial Calcium Overload Drives mtDNA-cGAS-STING Activation via VDAC1 and MCU Upregulation in Periodontitis

Cheng, X., Cai, Y., Geng, Y., 臧小英, Liu, J., & Qingxian, L. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27104317 · Cited by 4 · see citing works

Exploring the interplay between mitochondria and endoplasmic reticulum in pulmonary arterial hypertension

Liao, Z., & He, Y. (2025) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2025.1623775 · Cited by 3 · see citing works

Non-canonical roles of lysosomes in neurons

Spencer, J. I., Sudarikova, Y., & Devine, M. J. (2025) · Trends in Neurosciences · doi:10.1016/j.tins.2025.10.009 · Cited by 4 · see citing works

Emerging roles of the ciliary-mitochondrial axis in cellular homeostasis and neuroprotection

Miller, E., Bambakidis, P., Templin, P., Paul, B. D., & Pieper, A. A. (2025) · Molecular Neurodegeneration Advances · doi:10.1186/s44477-025-00005-w · Cited by 3 · see citing works

Mitochondria-associated endoplasmic reticulum membranes and calcium ion exchange: A novel direction for aging and neurodegenerative diseases

Yang, Y., Chen, M., Ding, L., Liu, J., Luo, J., Yan, R., Ning, J., Xie, S., Li, X., Ren, Z., et al. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-25-00857 · Cited by 3 · see citing works

Mitochondrial protein-enriched artificial nanovesicles: mitochondrial recovery and antioxidation for diabetic wound treatment

Xia, J., Wang, L., Song, Y., Zhu, M., Xu, Y., Liu, J., Guan, X., Zhang, Q., 赫克曼, Wang, F., et al. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04100-2 · Cited by 3 · see citing works

Role of mitochondrial dysfunction in muscle wasting in cancer cachexia: a narrative review

Su, X., Wang, S., Qu, Y., Wang, Y., Tian, Z., Chao, X., Li, Z., & Ma, D. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07906-8 · Cited by 3 · see citing works

Silicon rhodamine-based fluorescent probes for monitoring mitochondrial viscosity dynamics during mitophagy

Zhao, Z., Li, H., Li, L., Li, Z., Ai, Q., Wen, X., & Gao, B. (2026) · Chemical Communications · doi:10.1039/d6cc00586a · Cited by 3 · see citing works

Piezo-metastructured arrays enhance osteoblast mitochondrial quality control to promote osseointegration under osteoporotic conditions

Peng, S., Wang, K., Ning, X., Li, B., Zhang, M., Hu, D., Lei, Y., Wang, Y., Zhou, J., & Han, Y. (2026) · Biomaterials · doi:10.1016/j.biomaterials.2026.124248 · Cited by 3 · see citing works

Crosstalk between UPR and mitochondria: The triad of ER–mitochondria contacts, Ca²⁺, and ROS

Zito, E., & Hajnóczky, G. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108428 · Cited by 3 · see citing works

Asymmetric distribution of mitochondrial Ca 2+ regulators specifies compartment-specific mitochondrial function and neuronal developmentPreprint

Jang, D. C., Kim, S. Y., Kim, W., Jung, H., Chung, C., Bang, S., Kim, H. N., Choi, H. W., Han, K., Cho, Y., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.23.660978 · Cited by 3 · see citing works

Calcium-dependent regulation of physiological vs pathological cardiomyocyte hypertrophy

Chung, J., Isles, N., Johnston, S. T., Collins, D. J., McMullen, J. R., Roderick, H. L., & Rajagopal, V. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.120046 · Cited by 2 · see citing works

Mitochondrial Transport Proteins in Cardiovascular Diseases: Metabolic Gatekeepers, Pathogenic Mediators and Therapeutic Targets

Pei, Y., Wan, S., Qi, J., Xi, X., Zhu, Y., An, P., Luo, J., & Luo, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178475 · Cited by 3 · see citing works

ER morphological analysis associated with interstitial cells of Cajal and smooth muscle cells in the murine stomach

Tamada, H., & Iino, S. (2025) · Cell and Tissue Research · doi:10.1007/s00441-025-04016-7 · Cited by 2 · see citing works

Presenilin mutations disrupt iron homeostasis to promote ferroptosis mediated neurodegeneration in Caenorhabditis elegans

Ryan, K. C., Laboy, J. T., Ashraf, R., Ashkavand, Z., Jayasinghe, I., & Norman, K. R. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103910 · Cited by 2 · see citing works

Non-canonical role of natural quinones in mitochondrial nucleoid organization for maintaining respiration and protecting cardiac function

Pal, S., Ishihara, T., Setoyama, D., Chen, C.-L., Onoue, K., Yonemura, S., Ogasawara, E., & Ishihara, N. (2025) · The Journal of Biochemistry · doi:10.1093/jb/mvaf062 · Cited by 2 · see citing works

Integrating network toxicology and molecular docking to uncover mechanisms of novel herbicide-induced neurodegeneration

Wu, G., Chen, Y., Yao, Y., Huang, W., & Wu, K. (2025) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2025.106821 · Cited by 2 · see citing works

Micropeptides in the oncological dark matter: decoding their roles in tumor progression and therapy resistance

Zhang, Q., Yang, H., Wang, C., Ousmane, D., Liu, J., Liu, Z., Liu, W., Yan, Y., Xu, Z., & Wang, J. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07310-8 · Cited by 2 · see citing works

CISD2 ensures adequate ER-mitochondrial coupling, critically supporting mitochondrial function in neurons

Loncke, J., de Ridder, I., Rovere, R. L., Vaarmann, A., Fan, G., Ahuja, K., Serysheva, I. I., Verfaillie, C. M., Kerkhofs, M., Parys, J. B., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02132-7 · Cited by 2 · see citing works

AI-Resolved Protein Energy Landscapes, Electrodynamics, and Fluidic Microcircuits as a Unified Framework for Predicting Neurodegeneration

Panţu, C., Breazu, A., Oprea, Ș., Șerban, M., Covache-Busuioc, R.-A., Munteanu, O., Dobrin, N., Costea, D., & Eva, L. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020676 · Cited by 2 · see citing works

MitoCommun: a database for decoding mitochondrial communication networks

Wu, X., Chen, D., Feng, J., Bu, X., Wu, S., & Qiao, J. (2026) · BMC Genomics · doi:10.1186/s12864-026-12549-6 · Cited by 2 · see citing works

Calcium Signaling Pathways in Head and Neck Squamous Cell Carcinoma Therapy: A Review

Yu, Q., & Jiang, X. (2026) · Journal of Cellular Physiology · doi:10.1002/jcp.70142 · Cited by 2 · see citing works

Advances in the designing endoplasmic reticulum-targeted fluorescent probes

İnel, M., Yildirim, A. E., Ozturk, B., & Yilmaz, M. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.109619 · Cited by 2 · see citing works

Neutrophil membrane-coated and MMP2-responsive nanoparticles deliver PIM1 inhibitor to alleviate inflammatory arthritis through inhibiting Th17 cell differentiation

Su, Z., Chen, Z., Lin, J., Yu, W., Zeng, Y., Zhang, W., Li, Q., Lin, Y., Liu, Z., Zheng, G., et al. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04280-x · Cited by 2 · see citing works

Precise control of metal–ligand interactions: advanced chelation strategies for next-generation theranostic nanomedicine

Li, K., Li, Z., Gao, Y., Zhang, B., Zhang, X., Xin, H., Wang, Q., He, Q., Cui, P., Xu, H., et al. (2026) · Materials Horizons · doi:10.1039/d5mh02450a · Cited by 2 · see citing works

Field-effect transistor biosensors for monitoring cellular physiological activities: A comprehensive review

Xiao, L., Yu, S., Dai, W., Zhou, J., Li, Y.-T., & Zhang, G.-J. (2026) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2026.118902 · Cited by 2 · see citing works

Distinct Mitochondrial Central Dogma Gene Expression in the Buffalo Brain: A Comparative Transcriptomic Study with Metabolically Active Organs

Sadeesh, E. M., Lahamge, M. S., Ampadi, A. N., Kumari, S., & Mohiddin, R. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06134-x · Cited by 2 · see citing works

Membranes arrest the coarsening of mitochondrial condensates in human cells

(2026) · doi:10.1038/s42003-026-10085-3 · Cited by 2 · see citing works

Migrasome-driven mitocytosis relieves mitochondrial damage induced by chikungunya virus TF and 6K

Wang, S., Zhang, D., & Zhang, L. (2026) · hLife · doi:10.1016/j.hlife.2025.12.002 · Cited by 1 · see citing works

Mitochondrial dynamics and neuronal death in neurodegenerative diseases

Chowdhury, S., Dutta, R., Khan, N., Chakraborty, P., & Kar, K. (2024) · Neurophysiology · doi:10.1007/s11062-025-09985-7 · Cited by 1 · see citing works

Cu(OH)2 nanopesticide induced adolescent social behavior deficits via long noncoding RNA-mediated synaptic network dysfunction

Ren, Z., Duan, Y., Ren, M., Cai, Y., Liang, J., Wang, X., Sun, J., Ren, D., Ku, T., Ning, X., et al. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.141294 · Cited by 1 · see citing works

Nanomedicine as core enablers: Mechanisms of mitophagy and theranostic strategies in ischemia-reperfusion injury

Zhou, S., Wang, X., Zhu, J., Zheng, J., Song, X., Huang, B., & Chen, Y. (2026) · Nano Today · doi:10.1016/j.nantod.2026.103005 · Cited by 1 · see citing works

TRPC6 governs brown adipose thermogenesis via a BMPR2-p38 MAPK signaling axis

Xie, D., Peng, Y., Zhang, S., Mai, X., Wen, W., Wang, M., Wang, Q.-P., & Sun, J. (2026) · Molecular Metabolism · doi:10.1016/j.molmet.2026.102341 · Cited by 1 · see citing works

The impact of dendritic mitochondrial heterogeneity on synapse function

Cawley, M. L., & Farris, S. (2026) · Trends in Neurosciences · doi:10.1016/j.tins.2026.01.011 · Cited by 1 · see citing works

Mitochondrial homeostasis: the central hub governing the progression of atherosclerosis

Liu, H., Zhao, S., Gao, H., Wang, Y., Gao, J., Guo, P., Yang, Y., Cui, W., Zhang, S. M., Shi, Y., et al. (2026) · Precision Clinical Medicine · doi:10.1093/pcmedi/pbag010 · Cited by 1 · see citing works

The roles and interrelationship of the three redox-inert ions of magnesium, calcium, and zinc in redox biochemistry

Maret, W. (2026) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2026.100082 · Cited by 1 · see citing works

Ryanodine Receptor Ca 2+ Leak‐Induced Redistribution of Ca 2+ in Dystrophic mdx Mouse Muscle

Gaglianone, R. B., Lamboley, C. R. H., Dick, T. J. M., Meizoso‐Huesca, A., Singh, D. P., & Launikonis, B. S. (2026) · Acta Physiologica · doi:10.1111/apha.70251 · Cited by 1 · see citing works

An INF2-dependent actin-mediated step in inositol 1,4,5-trisphosphate receptor cluster formation and activity

Zavala, M., Ghosh, A., Joseph, S. K., & Chakrabarti, R. (2026) · Current Biology · doi:10.1016/j.cub.2026.05.022 · Cited by 1 · see citing works

Autism as a brain energy disorder: How impairments in brain glucose metabolism give rise to autism symptoms

Blagojevic-Stokic, N., Whiteley, P., Marlow, B. P., & Wills, J. (2026) · Brain Network Disorders · doi:10.1016/j.bnd.2026.04.002 · Cited by 1 · see citing works

Fibroblast Mitochondrial Ca 2+ Overload Drives Skin Fibrosis via Mitochondrial DNA Leakage and Cyclic GMP ‐ AMP Synthase–Stimulator of Interferon Genes Activation in Systemic Sclerosis

Zhang, X., Wang, Y., Huang, H., Guo, X., Ye, W., Cao, L., Wang, Z., Hou, Y., Wang, Y., Yang, J., et al. (2026) · Arthritis & Rheumatology · doi:10.1002/art.70261 · Cited by 1 · see citing works

The Mitochondrion: A Redox-Centric Mediator of Postmortem Meat Quality

Li, C.-Y., Guo, Z.-B., Wang, Y.-L., & Zhang, Y. (2026) · Food Reviews International · doi:10.1080/87559129.2026.2718279 · Cited by 1 · see citing works

Mitochondrial NCLX couples glucagon- and PDE2A-Dependent signals to regulate hepatic lipid metabolism

Assali, E. A., Taha, M., Salhab, A., Amer, J., Krishnan, K. C., Kostić, M., Veliova, M., Brownstein, A. J., Shirihai, O. S., Safadi, R., et al. (2026) · Molecular Metabolism · doi:10.1016/j.molmet.2026.102433 · Cited by 1 · see citing works

Mitochondrial alterations induced by Macrovipera lebetina venom

Doltchinkova, V. R., Vitkova, V., Shkodrova, M., Kitanova, M., Lozanova, V. V., Lozanova, S. V., Ivanov, A. J., & Roumenin, C. S. (2025) · European Biophysics Journal · doi:10.1007/s00249-025-01796-2 · Cited by 1 · see citing works

Hydrogen-Induced Calcium Influx via the TRPC4-TRPC4AP AxisPreprint

Zhao, P., Li, H., Cai, Z., Zhang, X., Wen, X., Liu, Z., Jiang, S., Dang, Z., Jiang, X. D., Wang, J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.19.644243 · Cited by 1 · see citing works

Cisd2 ensures adequate ER-mitochondrial coupling, thereby critically supporting mitochondrial function in neuronsPreprint

Loncke, J., de Ridder, I., Rovere, R. L., Vaarmann, A., Fan, G., Ahuja, K., Serysheva, I. I., Verfaillie, C. M., Kerkhofs, M., Parys, J. B., et al. (2025) · Research Square · doi:10.21203/rs.3.rs-6298090/v1

Shaping the waves: Mitochondrial regulation of calcium oscillations in smooth muscle

Coleman, H. A., & Parkington, H. C. (2025) · The Journal of Physiology · doi:10.1113/jp288974

In vivo imaging of neuronal mitochondrial Ca2+ transients with two-photon microscopy in awake mice

Qiu, S., Zhang, H., Zhou, F., Huang, H., He, C., & Wang, X. (2025) · Mitochondrial Communications · doi:10.1016/j.mitoco.2025.08.002

Aging-driven organelle miscommunication in the failing heart

Ortega, A., Bascuñan-Ortiz, E., Troncoso, M. F., Muñoz-Rodríguez, C., Navarrete-Gallegos, L., Yero-Haber, R., Becerra, B., Mora, A., Lopez‐Gallardo, E., Chiong, M., et al. (2025) · The Journal of Cardiovascular Aging · doi:10.20517/jca.2025.08

Calcium dynamics unplugged: NCLX in disease and therapeutic frontiers

Majumder, D. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-11188-6

Special Issue “Mitochondrial Remodeling and the Targeting Strategies for Disease Treatment”

Teng, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311370

Autism as a Disorder of Brain Energy: How Impairments in Brain Glucose Metabolism Give Rise to Autism SymptomsPreprint

Blagojevic-Stokic, N., Whiteley, P., Marlow, B. P., & Wills, J. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6043194

The Participation of Acetyl Phosphate, a Microbial and Host Metabolite, in the Regulation of the Calcium Balance in Mitochondria and Cells

Nv, B., Berezhnov, A. V., & Fedotcheva, N. I. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27021007

Piezo1 signaling facilitates capillarization of LSECs and contributes to liver fibrosis progressionPreprint

Xiang, Y., Gao, L., Han, Y., Zhang, Y., Chang, X., Zhu, L., Meng, Y., Ju, Y., Zheng, Y., Yang, T., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-8630916/v1

The Electromechanical Connectome: Integrating Voltage, Mechanical Nano-Forces, and Subcellular Fluid Phase Dynamics in Human Neural Computation

Filipoiu, F. M., Tătaru, C.-I., Dobrin, N., Șerban, M., Covache-Busuioc, R.-A., Toader, C., Rădoi, M. P., Munteanu, O., & Enyedi, M. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27042074

Cytosol alkalization induces cytosolic and mitochondrial calcium elevation in human cells

Vlasova, A., Bukhalovich, S. M., Kravtsunova, D. I., Gromova, A., Bagaeva, D. F., Zhilinskaya, A. P., Bogorodskiy, A., Ilyinsky, N., Vlasov, A., Kuklin, A. I., et al. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.153551

An integrated cartilage-on-a-chip recapitulating the bio-chemo-mechanical microenvironment in osteoarthritic joints

Jia, H., Yang, S., Du, L., Gao, H., Sun, K., Kong, F., Tang, T., Zhang, Q., Weng, T., & Xu, Y. (2026) · Bio-Design and Manufacturing · doi:10.1631/bdm.2500348

Mitochondrial Calcium Dysregulation and Targeted Therapies in Heart Failure

Liu, M., & Jin, Y. (2026) · Reviews in Cardiovascular Medicine · doi:10.31083/rcm46211

Unveiling Epigenetic Molecular Mechanisms in Bone Fracture Risk: Insights From 731 Immune Cells, 1400 Metabolites, and Critical Genetic Pathways

Wan, X., Lu, W.-C., Xue, J., Huang, J., Qian, W.-H., Hu, Z.-Y., You, W.-L., & Zhang, Y.-F. (2026) · Mediators of Inflammation · doi:10.1155/mi/3846184

TRPA1 channel activation by synthetic lipid nanoparticlesPreprint

Milici, A., Startek, J. B., Bultynck, G., & Talavera, K. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.03.722497

Chemotaxis of ATPase-Powered Nanoparticles up Extra- and Intracellular ATP Gradients

Shandilya, E., Lu, X., Sen, A., & Butler, P. J. (2026) · Nano Letters · doi:10.1021/acs.nanolett.5c06514

Viscosity-responsive AIEgen with mitochondrial/endoplasmic reticulum dual targeting for fatty liver fluorescence imaging and tumor photodynamic therapy

Liu, C., Li, Y., Chen, X., Yang, L., Xie, X., & Qi, Z. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.109965

RNA-binding protein RCAN1.1L modulates ATF2 mRNA stability to promote mitochondrial fission in acute ischemic stroke

Ji, Y., Ma, X., Wang, L., Liu, F., Tang, Y., Yang, X., Zhan, Z., Liu, S., Zhao, J., Wang, T., et al. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-08809-8

A Step Beyond pH: Electrochemical Network Deregulation in Cancer, Mechanisms, Consequences, and Therapeutic Implications: A Narrative ReviewPreprint

Koltai, T. (2026) · Qeios · doi:10.32388/4ellu7

Quantum-Resolved Photonic Editing of Endothelial Gene Regulation

Chamkouri, H. (2026) · Journal of Bio-X Research · doi:10.34133/jbioxresearch.0088

非光遗传双光子光调控细胞钙信号研究进展(特邀)

Bingyi, 李. L., Haipeng, 王. W., Qiao, 于. Y., Zichuan, 唐. T., & Hao, 贺. H. (2026) · Infrared and Laser Engineering · doi:10.3788/irla20260039

Activity-Dependent Postsynaptic Mitochondrial ROS Signaling Drives Avoidance Plasticity in C. elegansPreprint

Knight, K. M., Lenninger, Z., Deihl, E. W., Doser, R. L., & Hoerndli, F. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.05.730457

Translating Mitochondrial Complexity into Drug Delivery Design

Tsichlis, I., Protopapa, C., Vlachou, M., & Demetzos, C. (2026) · Springer proceedings in complexity · doi:10.1007/978-3-032-09101-7_39

Nitrate-Sialin2 axis couples ER-mitochondrial calcium signaling with fatty acid metabolism to drive white adipose browning

Jiang, O., Cao, Z., Kong, S., Wu, Q., Zhang, T., Chen, X., Zhou, B., Feng, Y., Wu, S., Wang, J., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74256-w

Supramolecular nanomedicine reprogramming calcium ions metabolism for cancer cell PANoptosis and immunotherapy

Li, Y., Shen, D., Zong, X., Gong, F., Zhu, X., Wu, J., Xue, H., Yao, H., & Li, R. (2026) · 中国科学通报：英文版 · doi:10.1016/j.scib.2026.06.037

Targeting Mitochondria–Endoplasmic Reticulum Crosstalk as a Promising Therapy for Uremia-Accelerated Atherosclerosis

Ruli, Z., Xiong, Q., & Shi, Y. (2026) · Integrative Medicine in Nephrology and Andrology · doi:10.1097/imna-d-25-00065

Mt1–Ca 2+ –Mitochondrial Metabolic Axis Maintains Temporomandibular Joint Condylar Cartilage Homeostasis Under Low Oxygen and Hypoxic Condition

Yan, Y., Jia, F., Gao, Z., Liang, C., & Geng, W. (2026) · Journal of Cellular Physiology · doi:10.1002/jcp.70203

ROS-mitochondrial nexus in stem cell growth and differentiation and implications in cancer and degenerative diseases

Akhtar, M. J., & Panwar, S. (2026) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2026.189663

Exercise-induced mitochondrial remodeling in energy-demanding organs during aging

Zhou, Z., Gao, J., Wang, M., & Zhang, H. (2026) · iScience · doi:10.1016/j.isci.2026.116791

Mitochondrial dysfunction in energy metabolism: Unraveling cardiometabolic diseases

Gao, J., & Yao, M. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-34186-1.00011-6

A Conserved Flexible N-Terminal Domain Tunes the Calcium Sensitivity of Sorcin by Stabilizing Its Active ConformationPreprint

Ye, Q., Wu, A., Carillo, K. J., Boyenle, I. D., Hemesath, H. R., He, Y., Delaeter, N., Jeon, J., Orban, J. P., Zhang, L., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.29.741579

Asymmetric distribution of mitochondrial Ca2+ regulators specifies compartment-specific mitochondrial function and neuronal development

Jang, D. C., Kim, S. Y., Kim, W. S., Choi, I. Y., Jang, E., Jung, H., Chung, C., Bang, S., Kim, H. N., Choi, H. W., et al. (2026) · Experimental & Molecular Medicine · doi:10.1038/s12276-026-01803-2 · Cited by 3 · see citing works

Hippocampal TRAP1 overexpression mitigates hypoxia-evoked learning and memory impairments via MERCS

Lu, G., Chengxiao, H., Rui, C., Yanrong, G., Ma, S., & Rili, G. (2026) · Scientific Reports · doi:10.1038/s41598-026-56389-6

Hypertensive mt. tRNAIle4263A>G mutation orchestrates vascular senescence and apoptosis by activation of mitochondria-ER interplay

Cao, N., Zhao, H., Wu, Z., Li, S., Tong, W., Jin, L., Wu, M., Liu, J., Liu, A., Wang, M., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104360

Mitochondrial Ca2+ Influx via MCU-1 Contributes to Oxidative Mitochondrial Defects in PDR-1/Parkin-Deficient Caenorhabditis elegans Body-Wall Muscle

Kawasumi, M., & Teranishi, M. (2026) · Antioxidants · doi:10.3390/antiox15081043

Mitochondria and calcium: from cell signalling to cell death

Duchen, M. R. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00057.x · Cited by 1,261 · see citing works

Mitochondrial organization and Ca2+ uptake

Olson, M. L., Chalmers, S., & McCarron, J. G. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110705 · Cited by 41 · see citing works

Interplay between mitochondria and cellular calcium signalling

Jacobson, J., & Duchen, M. R. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000009869.29827.df · Cited by 122 · see citing works

Ca2+ signalling in mitochondria: mechanism and role in physiology and pathology

Brini, M. (2003) · Cell Calcium · doi:10.1016/s0143-4160(03)00145-3 · Cited by 108 · see citing works

Mitochondrial Calcium Handling in Physiology and Disease

Granatiero, V., Stefani, D. D., & Rizzuto, R. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_2 · Cited by 77 · see citing works