Intracellular Ca2+ signaling and Ca2+ microdomains in the control of cell survival, apoptosis and autophagy

AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1

Kim, J., Kundu, M., Viollet, B., & Guan, K.-L. (2011) · Nature Cell Biology · doi:10.1038/ncb2152 · Cited by 7,227

The versatility and universality of calcium signalling

Berridge, M. J., Lipp, P., & Bootman, M. D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036035 · Cited by 5,701

Calcium signalling: dynamics, homeostasis and remodelling

Berridge, M. J., Bootman, M. D., & Roderick, H. L. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1155 · Cited by 5,585

The unfolded protein response: controlling cell fate decisions under ER stress and beyond

Hetz, C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3270 · Cited by 4,093

TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival

Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914

AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint

Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849

Bcl-2 Antiapoptotic Proteins Inhibit Beclin 1-Dependent Autophagy

Pattingre, S., Tassa, A., Qu, X., Garuti, R., Liang, X. H., Mizushima, N., Packer, M., Schneider, M. D., & Levine, B. (2005) · Cell · doi:10.1016/j.cell.2005.07.002 · Cited by 3,536

Autophagy and the Integrated Stress Response

Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506

TFEB Links Autophagy to Lysosomal Biogenesis

Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365

A Gene Network Regulating Lysosomal Biogenesis and Function

Sardiello, M., Palmieri, M., di Ronza, A., Medina, D. L., Valenza, M., Gennarino, V. A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R. S., et al. (2009) · Science · doi:10.1126/science.1174447 · Cited by 2,543

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

mTOR regulation of autophagy

Jung, C. H., Ro, S.-H., Cao, J., Otto, N. M., & Kim, D.-H. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.017 · Cited by 2,090

ACIDIFICATION OF THE ENDOCYTIC AND EXOCYTIC PATHWAYS

Mellman, I., Fuchs, R., & Helenius, A. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.003311 · Cited by 2,032

ER stress-induced cell death mechanisms

Sano, R., & Reed, J. C. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.028 · Cited by 1,988

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

De Stefani, D., Raffaello, A., Teardo, E., Szabò, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,915

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

Baughman, J. M., Perocchi, F., Girgis, H. S., Plovanich, M., Belcher-Timme, C. A., Sancak, Y., Bao, X. R., Strittmatter, L., Goldberger, O., Bogorad, R. L., et al. (2011) · Nature · doi:10.1038/nature10234 · Cited by 1,906

Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum

Axe, E. L., Walker, S. A., Manifava, M., Chandra, P., Roderick, H. L., Habermann, A., Griffiths, G., & Ktistakis, N. T. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200803137 · Cited by 1,885

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

Mitochondria as sensors and regulators of calcium signalling

Rizzuto, R., De Stefani, D., Raffaello, A., & Mammucari, C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3412 · Cited by 1,781

Regulation of Mammalian Autophagy in Physiology and Pathophysiology

Ravikumar, B., Sarkar, S., Davies, J. E., Futter, M., Garcia-Arencibia, M., Green-Thompson, Z. W., Jimenez-Sanchez, M., Korolchuk, V. I., Lichtenberg, M., Luo, S., et al. (2010) · Physiological Reviews · doi:10.1152/physrev.00030.2009 · Cited by 1,727

Autophagosomes form at ER–mitochondria contact sites

Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,683

Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks

Alers, S., Löffler, A. S., Wesselborg, S., & Stork, B. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06159-11 · Cited by 1,483

Mitochondria Supply Membranes for Autophagosome Biogenesis during Starvation

Hailey, D. W., Rambold, A. S., Satpute-Krishnan, P., Mitra, K., Sougrat, R., Kim, P. K., & Lippincott-Schwartz, J. (2010) · Cell · doi:10.1016/j.cell.2010.04.009 · Cited by 1,429

Lysosomal calcium signalling regulates autophagy through calcineurin and TFEB

Medina, D. L., Di Paola, S., Peluso, I., Armani, A., De Stefani, D., Venditti, R., Montefusco, S., Scotto-Rosato, A., Prezioso, C., Forrester, A., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3114 · Cited by 1,413

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

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

Csordás, G., Renken, C., 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 1,373

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

Regulation of the mTOR Complex 1 Pathway by Nutrients, Growth Factors, and Stress

Sengupta, S., Peterson, T. R., & Sabatini, D. M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.026 · Cited by 1,241

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 1,205

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

Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis

Pinton, P., Giorgi, C., Siviero, R., Zecchini, E., & Rizzuto, R. (2008) · Oncogene · doi:10.1038/onc.2008.308 · Cited by 1,157

Range of Messenger Action of Calcium Ion and Inositol 1,4,5-Trisphosphate

Allbritton, N. L., Meyer, T., & Stryer, L. (1992) · Science · doi:10.1126/science.1465619 · Cited by 1,148

Ca 2+ -Induced Apoptosis Through Calcineurin Dephosphorylation of BAD

Wang, H.-G., Pathan, N., Ethell, I. M., Krajewski, S., Yamaguchi, Y., Shibasaki, F., McKeon, F., Bobo, T., Franke, T. F., & Reed, J. C. (1999) · Science · doi:10.1126/science.284.5412.339 · Cited by 1,132

Control of Macroautophagy by Calcium, Calmodulin-Dependent Kinase Kinase-β, and Bcl-2

Høyer-Hansen, M., Bastholm, L., Szyniarowski, P., Campanella, M., Szabadkai, G., Farkas, T., Bianchi, K., Fehrenbacher, N., Elling, F., Rizzuto, R., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.009 · Cited by 1,072

A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation

Hayashi-Nishino, M., Fujita, N., Noda, T., Yamaguchi, A., Yoshimori, T., & Yamamoto, A. (2009) · Nature Cell Biology · doi:10.1038/ncb1991 · Cited by 1,060

Essential Regulation of Cell Bioenergetics by Constitutive InsP3 Receptor Ca2+ Transfer to Mitochondria

Cárdenas, C., Miller, R. A., Smith, I., Bui, T., Molgó, J., Müller, M., Vais, H., Cheung, K.-H., Yang, J., Parker, I., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.007 · Cited by 1,026

Lithium induces autophagy by inhibiting inositol monophosphatase

Sarkar, S., Floto, R. A., Berger, Z., Imarisio, S., Cordenier, A., Pasco, M., Cook, L. J., & Rubinsztein, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504035 · Cited by 985

Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death

Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., & Molkentin, J. D. (2007) · Nature Cell Biology · doi:10.1038/ncb1575 · Cited by 971

The molecular machinery of autophagy: unanswered questions

Klionsky, D. J. (2005) · Journal of Cell Science · doi:10.1242/jcs.01620 · Cited by 933

Dimers of mitochondrial ATP synthase form the permeability transition pore

Giorgio, V., von Stockum, S., Antoniel, M., Fabbro, A., Fogolari, F., Forte, M., Glick, G. D., Petronilli, V., Zoratti, M., Szabó, I., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217823110 · Cited by 922

Plasma membrane contributes to the formation of pre-autophagosomal structures

Ravikumar, B., Moreau, K., Jahreiss, L., Puri, C., & Rubinsztein, D. C. (2010) · Nature Cell Biology · doi:10.1038/ncb2078 · Cited by 902

PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress

Verfaillie, T., Rubio, N., Garg, A. D., Bultynck, G., Rizzuto, R., Decuypere, J.-P., Piette, J., Linehan, C., Gupta, S., Samali, A., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2012.74 · Cited by 850

Bcl-2 family members: Dual regulators of apoptosis and autophagy

Levine, B., Sinha, S. C., & Kroemer, G. (2008) · Autophagy · doi:10.4161/auto.6260 · Cited by 834

Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D

Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808

MAM: more than just a housekeeper

Hayashi, T., Rizzuto, R., Hajnoczky, G., & Su, T.-P. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.12.002 · Cited by 787

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

Shoshan-Barmatz, V., De Pinto, V., Zweckstetter, M., Raviv, Z., Keinan, N., & Arbel, N. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.03.002 · Cited by 782

NAADP mobilizes calcium from acidic organelles through two-pore channels

Calcraft, P. J., Ruas, M., Pan, Z., Cheng, X., Arredouani, A., Hao, X., Tang, J., Rietdorf, K., Teboul, L., Chuang, K.-T., et al. (2009) · Nature · doi:10.1038/nature08030 · Cited by 760

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

Ca2+ signalling checkpoints in cancer: remodelling Ca2+ for cancer cell proliferation and survival

Roderick, H. L., & Cook, S. J. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2374 · Cited by 731

Transcriptional Activation of Lysosomal Exocytosis Promotes Cellular Clearance

Medina, D. L., Fraldi, A., Bouche, V., Annunziata, F., Mansueto, G., Spampanato, C., Puri, C., Pignata, A., Martina, J. A., Sardiello, M., et al. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.07.016 · Cited by 716

Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation

Polson, H. E. J., de Lartigue, J., Rigden, D. J., Reedijk, M., Urbé, S., Clague, M. J., & Tooze, S. A. (2010) · Autophagy · doi:10.4161/auto.6.4.11863 · Cited by 712

3D tomography reveals connections between the phagophore and endoplasmic reticulum

Ylä-Anttila, P., Vihinen, H., Jokitalo, E., & Eskelinen, E.-L. (2009) · Autophagy · doi:10.4161/auto.5.8.10274 · Cited by 675

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

Mallilankaraman, K., Doonan, P., Cárdenas, C., Chandramoorthy, H. C., 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

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

Pan, X., Liu, J., Nguyen, T., Liu, C., Sun, J., Teng, Y., Fergusson, M. M., Rovira, I. I., Allen, M., Springer, D. A., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2868 · Cited by 653

Bcl-2-mediated alterations in endoplasmic reticulum Ca 2+ analyzed with an improved genetically encoded fluorescent sensor

Palmer, A. E., Jin, C., Reed, J. C., & Tsien, R. Y. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408030101 · Cited by 625

Presenilins Form ER Ca2+ Leak Channels, a Function Disrupted by Familial Alzheimer's Disease-Linked Mutations

Tu, H., Nelson, O., Bezprozvanny, A., Wang, Z., Lee, S.-F., Hao, Y.-H., Serneels, L., De Strooper, B., Yu, G., & Bezprozvanny, I. (2006) · Cell · doi:10.1016/j.cell.2006.06.059 · Cited by 616

Ca2+ homeostasis and endoplasmic reticulum (ER) stress: An integrated view of calcium signaling

Krebs, J., Agellon, L. B., & Michalak, M. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.004 · Cited by 596

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

Alavian, K. N., Beutner, G., Lazrove, E., Sacchetti, S., Park, H.-A., Licznerski, P., Li, H., Nabili, P., Hockensmith, K., Graham, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401591111 · Cited by 592

Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis

Deniaud, A., Sharaf el dein, O., Maillier, E., Poncet, D., Kroemer, G., Lemaire, C., & Brenner, C. (2008) · Oncogene · doi:10.1038/sj.onc.1210638 · Cited by 586

The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology

Bernardi, P., Rasola, A., Forte, M., & Lippe, G. (2015) · Physiological Reviews · doi:10.1152/physrev.00001.2015 · Cited by 577

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 573

Mitochondrial permeability transition in Ca2+-dependent apoptosis and necrosis

Rasola, A., & Bernardi, P. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.04.007 · Cited by 563

Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria

Csordas, G. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.96 · Cited by 540

pH-dependent regulation of lysosomal calcium in macrophages

Christensen, K. A., Myers, J. T., & Swanson, J. A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.3.599 · Cited by 534

Calcium and cell death mechanisms: A perspective from the cell death community

Zhivotovsky, B., & Orrenius, S. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.03.003 · Cited by 525

MICU1 and MICU2 Finely Tune the Mitochondrial Ca2+ Uniporter by Exerting Opposite Effects on MCU Activity

Patron, M., Checchetto, V., Raffaello, A., Teardo, E., Vecellio Reane, D., Mantoan, M., Granatiero, V., Szabò, I., De Stefani, D., & Rizzuto, R. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.01.013 · Cited by 517

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

Bernardi, P., & Di Lisa, F. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.023 · Cited by 499

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

Raffaello, A., De Stefani, D., Sabbadin, D., Teardo, E., Merli, G., Picard, A., Checchetto, V., Moro, S., Szabò, I., & Rizzuto, R. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.157 · Cited by 490

MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism

Mallilankaraman, K., Cárdenas, C., Doonan, P. J., Chandramoorthy, H. C., Irrinki, K. M., Golenár, T., Csordás, G., Madireddi, P., Yang, J., Müller, M., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2622 · Cited by 489

Endoplasmic-Reticulum Calcium Depletion and Disease

Mekahli, D., Bultynck, G., Parys, J. B., De Smedt, H., & Missiaen, L. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004317 · Cited by 478

The endoplasmic reticulum–mitochondria connection: One touch, multiple functions

Marchi, S., Patergnani, S., & Pinton, P. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.015 · Cited by 475

Mitochondrial Ca2+ and apoptosis

Giorgi, C., Baldassari, F., Bononi, A., Bonora, M., De Marchi, E., Marchi, S., Missiroli, S., Patergnani, S., Rimessi, A., Suski, J. M., et al. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.02.008 · Cited by 474

Role of the c subunit of the F O ATP synthase in mitochondrial permeability transition

Bonora, M., Bononi, A., De Marchi, E., Giorgi, C., Lebiedzinska, M., Marchi, S., Patergnani, S., Rimessi, A., Suski, J. M., Wojtala, A., et al. (2013) · Cell Cycle · doi:10.4161/cc.23599 · Cited by 458

When ER stress reaches a dead end

Urra, H., Dufey, E., Lisbona, F., Rojas-Rivera, D., & Hetz, C. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.07.024 · Cited by 457

Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria

Rapizzi, E., Pinton, P., Szabadkai, G., Wieckowski, M. R., Vandecasteele, G., Baird, G., Tuft, R. A., Fogarty, K. E., & Rizzuto, R. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205091 · Cited by 452

Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM)

Raturi, A., & Simmen, T. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.04.013 · Cited by 447

BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death

Shimizu, S., Konishi, A., Kodama, T., & Tsujimoto, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3100 · Cited by 433

Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum

Oakes, S. A., Scorrano, L., Opferman, J. T., Bassik, M. C., Nishino, M., Pozzan, T., & Korsmeyer, S. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408352102 · Cited by 428

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

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

PML Regulates Apoptosis at Endoplasmic Reticulum by Modulating Calcium Release

Giorgi, C., Ito, K., Lin, H.-K., Santangelo, C., Wieckowski, M. R., Lebiedzinska, M., Bononi, A., Bonora, M., Duszynski, J., Bernardi, R., et al. (2010) · Science · doi:10.1126/science.1189157 · Cited by 420

Erratum: Corrigenda: MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism

Mallilankaraman, K., Cárdenas, C., Doonan, P. J., Chandramoorthy, H. C., Irrinki, K. M., Golenár, T., Csordás, G., Madireddi, P., Yang, J., Müller, M., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3202 · Cited by 418

Calcium signaling around Mitochondria Associated Membranes (MAMs)

Patergnani, S., Suski, J. M., Agnoletto, C., Bononi, A., Bonora, M., De Marchi, E., Giorgi, C., Marchi, S., Missiroli, S., Poletti, F., et al. (2011) · Cell Communication and Signaling · doi:10.1186/1478-811x-9-19 · Cited by 407

Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate

Chen, R., Valencia, I., Zhong, F., McColl, K. S., Roderick, H. L., Bootman, M. D., Berridge, M. J., Conway, S. J., Holmes, A. B., Mignery, G. A., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309146 · Cited by 404

Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling

Brailoiu, E., Churamani, D., Cai, X., Schrlau, M. G., Brailoiu, G. C., Gao, X., Hooper, R., Boulware, M. J., Dun, N. J., Marchant, J. S., et al. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200904073 · Cited by 401

Molecular mechanisms of endolysosomal Ca2+ signalling in health and disease

Morgan, A. J., Platt, F. M., Lloyd-Evans, E., & Galione, A. (2011) · Biochemical Journal · doi:10.1042/bj20110949 · Cited by 399

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

A molecular mechanism to regulate lysosome motility for lysosome positioning and tubulation

Li, X., Rydzewski, N., Hider, A., Zhang, X., Yang, J., Wang, W., Gao, Q., Cheng, X., & Xu, H. (2016) · Nature Cell Biology · doi:10.1038/ncb3324 · Cited by 387

The Mitochondrial Calcium Uniporter Matches Energetic Supply with Cardiac Workload during Stress and Modulates Permeability Transition

Luongo, T. S., Lambert, J. P., Yuan, A., Zhang, X., Gross, P., Song, J., Shanmughapriya, S., Gao, E., Jain, M., Houser, S. R., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.017 · Cited by 384

Coordination of agonist-induced Ca2+-signalling patterns by NAADP in pancreatic acinar cells

Cancela, J. M., Churchill, G. C., & Galione, A. (1999) · Nature · doi:10.1038/18032 · Cited by 376

Amino Acids Activate mTOR Complex 1 via Ca2+/CaM Signaling to hVps34

Gulati, P., Gaspers, L. D., Dann, S. G., Joaquin, M., Nobukuni, T., Natt, F., Kozma, S. C., Thomas, A. P., & Thomas, G. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.03.002 · Cited by 370

New functions of mitochondria associated membranes in cellular signaling

van Vliet, A. R., Verfaillie, T., & Agostinis, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.009 · Cited by 353

Remodeling of ryanodine receptor complex causes “leaky” channels: A molecular mechanism for decreased exercise capacity

Bellinger, A. M., Reiken, S., Dura, M., Murphy, P. W., Deng, S.-X., Landry, D. W., Nieman, D., Lehnart, S. E., Samaru, M., LaCampagne, A., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711074105 · Cited by 352

Chemical modulators of autophagy as biological probes and potential therapeutics

Fleming, A., Noda, T., Yoshimori, T., & Rubinsztein, D. C. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.500 · Cited by 349

Mitofusin 2-Containing Mitochondrial-Reticular Microdomains Direct Rapid Cardiomyocyte Bioenergetic Responses Via Interorganelle Ca 2+ Crosstalk

Chen, Y., Csordás, G., Jowdy, C., Schneider, T. G., Csordás, N., Wang, W., Liu, Y., Kohlhaas, M., Meiser, M., Bergem, S., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.266585 · Cited by 348

The mitochondrial permeability transition pore: a mystery solved?

Bernardi, P. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00095 · Cited by 335

Mitochondria-Associated Membranes: Composition, Molecular Mechanisms, and Physiopathological Implications

Giorgi, C., Missiroli, S., Patergnani, S., Duszynski, J., Wieckowski, M. R., & Pinton, P. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2014.6223 · Cited by 328

VDAC1 selectively transfers apoptotic Ca2+ signals to mitochondria

De Stefani, D., Bononi, A., Romagnoli, A., Messina, A., De Pinto, V, Pinton, P., & Rizzuto, R. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.92 · Cited by 321

Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP

Gómez-Suaga, P., Luzón-Toro, B., Churamani, D., Zhang, L., Bloor-Young, D., Patel, S., Woodman, P. G., Churchill, G. C., & Hilfiker, S. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr481 · Cited by 312

The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor

Rong, Y.-P., Bultynck, G., Aromolaran, A. S., Zhong, F., Parys, J. B., De Smedt, H., Mignery, G. A., Roderick, H. L., Bootman, M. D., & Distelhorst, C. W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907555106 · Cited by 307

MITOL Regulates Endoplasmic Reticulum-Mitochondria Contacts via Mitofusin2

Sugiura, A., Nagashima, S., Tokuyama, T., Amo, T., Matsuki, Y., Ishido, S., Kudo, Y., McBride, H. M., Fukuda, T., Matsushita, N., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.023 · Cited by 303

Calcium Elevation in Mitochondria Is the Main Ca2+ Requirement for Mitochondrial Permeability Transition Pore (mPTP) Opening

Baumgartner, H. K., Gerasimenko, J. V., Thorne, C., Ferdek, P., Pozzan, T., Tepikin, A. V., Petersen, O. H., Sutton, R., Watson, A. J. M., & Gerasimenko, O. V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.025353 · Cited by 276

The two-pore channel TPCN2 mediates NAADP-dependent Ca2+-release from lysosomal stores

Zong, X., Schieder, M., Cuny, H., Fenske, S., Gruner, C., Rötzer, K., Griesbeck, O., Harz, H., Biel, M., & Wahl-Schott, C. (2009) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0690-y · Cited by 275

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., Goes, T. S., Goes, A. M., Rodrigues, M. A., Gomez, M. V., Nathanson, M. H., & Leite, M. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506623200 · Cited by 270

MCUR1は細胞代謝を制御するミトコンドリアCa 2MCUR1+ 取込の必須成分である

Mallilankaraman, K. B., Cesar, C., Patrick, J., Harish, C. C., Krishna, M. I., Golenár, T., Gyoergy, C., Madireddi, P., Jun, Y., Müller, M., et al. (2012) · Nature Cell Biology · Cited by 270

Cytoprotective roles for autophagy

Moreau, K., Luo, S., & Rubinsztein, D. C. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.12.002 · Cited by 264

Targeting Bcl-2-IP3 Receptor Interaction to Reverse Bcl-2's Inhibition of Apoptotic Calcium Signals

Rong, Y.-P., Aromolaran, A. S., Bultynck, G., Zhong, F., Li, X., McColl, K., Matsuyama, S., Herlitze, S., Roderick, H. L., Bootman, M. D., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.014 · Cited by 263

Phosphorylation of inositol 1,4,5-trisphosphate receptors by protein kinase B/Akt inhibits Ca 2+ release and apoptosis

Szado, T., Vanderheyden, V., Parys, J. B., De Smedt, H., Rietdorf, K., Kotelevets, L., Chastre, E., Khan, F., Landegren, U., Söderberg, O., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711324105 · Cited by 262

Oncogene-induced senescence: the bright and dark side of the response

Gorgoulis, V. G., & Halazonetis, T. D. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.07.013 · Cited by 257

T Cells Deficient in Inositol 1,4,5-Trisphosphate Receptor Are Resistant to Apoptosis

Jayaraman, T., & Marks, A. R. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.6.3005 · Cited by 257

A dual role for Ca2+ in autophagy regulation

Decuypere, J.-P., Bultynck, G., & Parys, J. B. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.04.001 · Cited by 256

Up-regulation of lysosomal TRPML1 channels is essential for lysosomal adaptation to nutrient starvation

Wang, W., Gao, Q., Yang, M., Zhang, X., Yu, L., Lawas, M., Li, X., Bryant-Genevier, M., Southall, N. T., Marugan, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419669112 · Cited by 250

Regulation of the Autophagic Bcl-2/Beclin 1 Interaction

Decuypere, J.-P., Parys, J. B., & Bultynck, G. (2012) · Cells · doi:10.3390/cells1030284 · Cited by 249

VDAC, a multi-functional mitochondrial protein as a pharmacological target

Shoshan-Barmatz, V., & Ben-Hail, D. (2012) · Mitochondrion · doi:10.1016/j.mito.2011.04.001 · Cited by 248

Bcl-2 and Ca2+ homeostasis in the endoplasmic reticulum

Pinton, P., & Rizzuto, R. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401960 · Cited by 248

The mitochondrial voltage-dependent anion channel 1 in tumor cells

Shoshan-Barmatz, V., Ben-Hail, D., Admoni, L., Krelin, Y., & Tripathi, S. S. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.10.040 · Cited by 247

Selective Vulnerability of Cancer Cells by Inhibition of Ca2+ Transfer from Endoplasmic Reticulum to Mitochondria

Cárdenas, C., Müller, M., McNeal, A., Lovy, A., Jaňa, F., Bustos, G., Urra, F., Smith, N., Molgó, J., Diehl, J. A., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.02.030 · Cited by 247

Mitochondrial BCL‐2 inhibits AMBRA1‐induced autophagy

Strappazzon, F., Vietri‐Rudan, M., Campello, S., Nazio, F., Florenzano, F., Fimia, G. M., Piacentini, M., Levine, B., & Cecconi, F. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.49 · Cited by 246

Role of SERCA1 Truncated Isoform in the Proapoptotic Calcium Transfer from ER to Mitochondria during ER Stress

Chami, M., Oulès, B., Szabadkai, G., Tacine, R., Rizzuto, R., & Paterlini-Bréchot, P. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.014 · Cited by 239

Pharmacologic agents targeting autophagy

Vakifahmetoglu-Norberg, H., Xia, H.-G., & Yuan, J. (2015) · Journal of Clinical Investigation · doi:10.1172/jci73937 · Cited by 239

Identification of PTEN at the ER and MAMs and its regulation of Ca2+ signaling and apoptosis in a protein phosphatase-dependent manner

Bononi, A., Bonora, M., Marchi, S., Missiroli, S., Poletti, F., Giorgi, C., Pandolfi, P. P., & Pinton, P. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.77 · Cited by 237

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

Functional implications of calcium permeability of the channel formed by pannexin 1

Vanden Abeele, F., Bidaux, G., Gordienko, D., Beck, B., Panchin, Y. V., Baranova, A. V., Ivanov, D. V., Skryma, R., & Prevarskaya, N. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601115 · Cited by 231

Autophagy signal transduction by ATG proteins: from hierarchies to networks

Wesselborg, S., & Stork, B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2034-8 · Cited by 229

Downregulation of the Mitochondrial Calcium Uniporter by Cancer-Related miR-25

Marchi, S., Lupini, L., Patergnani, S., Rimessi, A., Missiroli, S., Bonora, M., Bononi, A., Corrà, F., Giorgi, C., De Marchi, E., et al. (2013) · Current Biology · doi:10.1016/j.cub.2012.11.026 · Cited by 228

Mitofusin-2 Independent Juxtaposition of Endoplasmic Reticulum and Mitochondria: An Ultrastructural Study

Cosson, P., Marchetti, A., Ravazzola, M., & Orci, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046293 · Cited by 227

The VDAC1 N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins

Abu-Hamad, S., Arbel, N., Calo, D., Arzoine, L., Israelson, A., Keinan, N., Ben-Romano, R., Friedman, O., & Shoshan-Barmatz, V. (2009) · Journal of Cell Science · doi:10.1242/jcs.040188 · Cited by 226

The Ca2+ Pumps of the Endoplasmic Reticulum and Golgi Apparatus

Vandecaetsbeek, I., Vangheluwe, P., Raeymaekers, L., Wuytack, F., & Vanoevelen, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004184 · Cited by 221

Mitochondrial ER Contacts Are Crucial for Mitophagy in Yeast

Böckler, S., & Westermann, B. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.01.012 · Cited by 216

Membrane dynamics in autophagosome biogenesis

Carlsson, S. R., & Simonsen, A. (2015) · Journal of Cell Science · doi:10.1242/jcs.141036 · Cited by 214

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

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

Structure and function of the mitochondrial calcium uniporter complex

De Stefani, D., Patron, M., & Rizzuto, R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.04.008 · Cited by 206

Prostate cell differentiation status determines transient receptor potential melastatin member 8 channel subcellular localization and function

Bidaux, G., Flourakis, M., Thebault, S., Zholos, A., Beck, B., Gkika, D., Roudbaraki, M., Bonnal, J.-L., Mauroy, B., Shuba, Y., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30168 · Cited by 195

Direct mobilisation of lysosomal Ca2+ triggers complex Ca2+ signals

Kilpatrick, B. S., Eden, E. R., Schapira, A. H., Futter, C. E., & Patel, S. (2013) · Journal of Cell Science · doi:10.1242/jcs.118836 · Cited by 192

The Mitochondrial Calcium Uniporter Controls Skeletal Muscle Trophism In Vivo

Mammucari, C., Gherardi, G., Zamparo, I., Raffaello, A., Boncompagni, S., Chemello, F., Cagnin, S., Braga, A., Zanin, S., Pallafacchina, G., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.056 · Cited by 190

Inositol 1,4,5-trisphosphate receptor-isoform diversity in cell death and survival

Ivanova, H., Vervliet, T., Missiaen, L., Parys, J. B., De Smedt, H., & Bultynck, G. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.007 · Cited by 186

Selective regulation of IP3-receptor-mediated Ca2+ signaling and apoptosis by the BH4 domain of Bcl-2 versus Bcl-Xl

Monaco, G., Decrock, E., Akl, H., Ponsaerts, R., Vervliet, T., Luyten, T., De Maeyer, M., Missiaen, L., Distelhorst, C. W., De Smedt, H., et al. (2012) · Cell Death & Differentiation · doi:10.1038/cdd.2011.97 · Cited by 183

Selective modulation of subtype III IP3R by Akt regulates ER Ca2+ release and apoptosis

Marchi, S., Marinello, M., Bononi, A., Bonora, M., Giorgi, C., Rimessi, A., & Pinton, P. (2012) · Cell Death & Disease · doi:10.1038/cddis.2012.45 · Cited by 182

Cyclophilin D in mitochondrial pathophysiology

Giorgio, V., Soriano, M. E., Basso, E., Bisetto, E., Lippe, G., Forte, M. A., & Bernardi, P. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.006 · Cited by 180

Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein

Arbel, N., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.345918 · Cited by 179

Post-Golgi Sec Proteins Are Required for Autophagy in Saccharomyces cerevisiae

Geng, J., Nair, U., Yasumura-Yorimitsu, K., & Klionsky, D. J. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-11-0969 · Cited by 179

At the right distance: ER-mitochondria juxtaposition in cell life and death

Naon, D., & Scorrano, L. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.05.011 · Cited by 178

Dependence of hepatocytic autophagy on intracellularly sequestered calcium.

Gordon, P. B., Holen, I., Fosse, M., Røtnes, J. S., & Seglen, P. O. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74287-2 · Cited by 176

Nicotinic acid adenine dinucleotide phosphate and cyclic ADP‐ribose regulate TRPM2 channels in T lymphocytes

Beck, A., Kolisek, M., Bagley, L. A., Fleig, A., Penner, R., Beck, A., Kolisek, M., Bagley, L. A., Fleig, A., & Penner, R. (2006) · The FASEB Journal · doi:10.1096/fj.05-5538fje · Cited by 176

Dysregulation of lysosomal morphology by pathogenic LRRK2 is corrected by two-pore channel 2 inhibition

Hockey, L. N., Kilpatrick, B. S., Eden, E. R., Lin-Moshier, Y., Brailoiu, G. C., Brailoiu, E., Futter, C. E., Schapira, A. H., Marchant, J. S., & Patel, S. (2014) · Journal of Cell Science · doi:10.1242/jcs.164152 · Cited by 174

NAADP induces Ca2+ oscillations via a two-pool mechanism by priming IP3- and cADPR-sensitive Ca2+ stores

Churchill, G. C. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2666 · Cited by 173

The IP3 receptor–mitochondria connection in apoptosis and autophagy

Decuypere, J.-P., Monaco, G., Bultynck, G., Missiaen, L., De Smedt, H., & Parys, J. B. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.11.023 · Cited by 173

Voltage-dependent Anion Channel 1-based Peptides Interact with Hexokinase to Prevent Its Anti-apoptotic Activity

Arzoine, L., Zilberberg, N., Ben-Romano, R., & Shoshan-Barmatz, V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m803614200 · Cited by 172

Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity

Arbel, N., & Shoshan-Barmatz, V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082990 · Cited by 168

Bcl-2 proteins and calcium signaling: complexity beneath the surface

Vervliet, T., Parys, J. B., & Bultynck, G. (2016) · Oncogene · doi:10.1038/onc.2016.31 · Cited by 166

Expression of Ca2+‐permeable two‐pore channels rescues NAADP signalling in TPC‐deficient cells

Ruas, M., Davis, L. C., Chen, C., Morgan, A. J., Chuang, K., Walseth, T. F., Grimm, C. M., Garnham, C., Powell, T., Platt, N., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490009 · Cited by 165

Ryanodine Receptors: Allosteric Ion Channel Giants

Van Petegem, F. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.08.004 · Cited by 163

An Interaction between Bcl-xL and the Voltage-dependent Anion Channel (VDAC) Promotes Mitochondrial Ca2+ Uptake

Huang, H., Hu, X., Eno, C. O., Zhao, G., Li, C., & White, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.448290 · Cited by 163

Mcl-1 promotes lung cancer cell migration by directly interacting with VDAC to increase mitochondrial Ca2+ uptake and reactive oxygen species generation

Huang, H., Shah, K., Bradbury, N. A., Li, C., & White, C. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.419 · Cited by 163

Role of Leaky Neuronal Ryanodine Receptors in Stress- Induced Cognitive Dysfunction

Liu, X., Betzenhauser, M. J., Reiken, S., Meli, A. C., Xie, W., Chen, B.-X., Arancio, O., & Marks, A. R. (2012) · Cell · doi:10.1016/j.cell.2012.06.052 · Cited by 162

Ins(1,4,5) P 3 receptor-mediated Ca 2+ signaling and autophagy induction are interrelated

Decuypere, J.-P., Welkenhuyzen, K., Luyten, T., Ponsaerts, R., Dewaele, M., Molgó, J., Agostinis, P., Missiaen, L., De Smedt, H., Parys, J. B., et al. (2011) · Autophagy · doi:10.4161/auto.7.12.17909 · Cited by 159

Bidirectional Ca2+ signaling occurs between the endoplasmic reticulum and acidic organelles

Morgan, A. J., Davis, L. C., Wagner, S. K., Lewis, A. M., Parrington, J., Churchill, G. C., & Galione, A. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201204078 · Cited by 155

Mitofusin 2: A Mitochondria-Shaping Protein with Signaling Roles Beyond Fusion

de Brito, O. M., & Scorrano, L. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1934 · Cited by 155

The SR/ER-mitochondria calcium crosstalk is regulated by GSK3β during reperfusion injury

Gomez, L., Thiébaut, P., Paillard, M., Ducreux, S., Abrial, M., Silva, C. C. D., Durand, A., Alam, M. R., Coppenolle, F. V., Sheu, S.-S., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.101 · Cited by 154

Organellar Calcium BuffersPreprint

Prins, D., & Michalak, M. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004069 · Cited by 154

Akt Kinase Phosphorylation of Inositol 1,4,5-Trisphosphate Receptors

Khan, M. T. M., Wagner, L. E., Yule, D. I., Bhanumathy, C. D., & Joseph, S. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509262200 · Cited by 154

EMRE Is a Matrix Ca2+ Sensor that Governs Gatekeeping of the Mitochondrial Ca2+ Uniporter

Vais, H., Mallilankaraman, K. B., Mak, D. D., Hoff, H. B., Payne, R. J., Tanis, J. E., & Foskett, J. K. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.054 · Cited by 154

Role of IP3 receptor signaling in cell functions and diseases

Mikoshiba, K. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.10.001 · Cited by 153

SLC25A23 augments mitochondrial Ca2+uptake, interacts with MCU, and induces oxidative stress–mediated cell death

Hoffman, N. E., Chandramoorthy, H. C. K., Shanmughapriya, S., Zhang, X. Q., Vallem, S., Doonan, P. J., Mallilankaraman, K. B., Guo, S., Rajan, S., Elrod, J. W., et al. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-08-0502 · Cited by 150

VDAC2 is required for truncated BID‐induced mitochondrial apoptosis by recruiting BAK to the mitochondria

Roy, S. S., Ehrlich, A. M., Craigen, W. J., & Hajnóczky, G. (2009) · EMBO Reports · doi:10.1038/embor.2009.219 · Cited by 150

ER functions of oncogenes and tumor suppressors: Modulators of intracellular Ca2+ signaling

Bittremieux, M., Parys, J. B., Pinton, P., & Bultynck, G. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.002 · Cited by 145

The BH4 Domain of Anti-apoptotic Bcl-XL, but Not That of the Related Bcl-2, Limits the Voltage-dependent Anion Channel 1 (VDAC1)-mediated Transfer of Pro-apoptotic Ca2+ Signals to Mitochondria

Monaco, G., Decrock, E., Arbel, N., van Vliet, A. R., Rovere, R. M. L. L., SMEDT, H. D., Parys, J. B., Agostinis, P., Leybaert, L., Shoshan‐Barmatz, V., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.622514 · Cited by 144

AMPK-independent induction of autophagy by cytosolic Ca2+ increase

Grotemeier, A., Alers, S., Pfisterer, S. G., Paasch, F., Daubrawa, M., Dieterle, A., Viollet, B., Wesselborg, S., Proikas-Cezanne, T., & Stork, B. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.01.015 · Cited by 143

Ribosome-translocon complex mediates calcium leakage from endoplasmic reticulum stores

Coppenolle, F. V., Abeele, F. V., Slomianny, C., Flourakis, M., Hesketh, J. E., Dewailly, E., & Prevarskaya, N. B. (2004) · Journal of Cell Science · doi:10.1242/jcs.01274 · Cited by 140

Lysosomes shape Ins(1,4,5)P3-evoked Ca2+ signals by selectively sequestering Ca2+ released from the endoplasmic reticulum

López-Sanjurjo, C. I., Tovey, S. C., Prole, D. L., & Taylor, C. W. (2012) · Journal of Cell Science · doi:10.1242/jcs.116103 · Cited by 139

Caspase-3-induced Truncation of Type 1 Inositol Trisphosphate Receptor Accelerates Apoptotic Cell Death and Induces Inositol Trisphosphate-independent Calcium Release during Apoptosis

Assefa, Z., Bultynck, G., Szlufcik, K., Kasri, N. N., Vermassen, E., Goris, J., Missiaen, L., Callewaert, G., Parys, J. B., & SMEDT, H. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403872200 · Cited by 137

Trichoplein/mitostatin regulates endoplasmic reticulum–mitochondria juxtaposition

Cerqua, C., Anesti, V., Pyakurel, A., Liu, D., Naón, D., Wiche, G., Baffa, R., Dimmer, K. S., & Scorrano, L. (2010) · EMBO Reports · doi:10.1038/embor.2010.151 · Cited by 136

MICU1 Motifs Define Mitochondrial Calcium Uniporter Binding and Activity

Hoffman, N. E., Chandramoorthy, H. C. K., Shanmughapriya, S., Zhang, X., Rajan, S., Mallilankaraman, K. B., Gandhirajan, R. K., Vagnozzi, R. J., Ferrer, L. M., Sreekrishnanilayam, K., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.11.026 · Cited by 136

Ca 2+ signals regulate mitochondrial metabolism by stimulating CREB-mediated expression of the mitochondrial Ca 2+ uniporter gene MCU

Shanmughapriya, S., Rajan, S., Hoffman, N. E., Zhang, X., Guo, S., Kolesar, J. E., Hines, K. J., Ragheb, J. G., Jog, N. R., Caricchio, R., et al. (2015) · Science Signaling · doi:10.1126/scisignal.2005673 · Cited by 132

Basal and Physiological Ca2+ Leak from the Endoplasmic Reticulum of Pancreatic Acinar Cells

Lomax, R. B., Camello‐Almaraz, C., Coppenolle, F. V., Petersen, O. H., & Tepikin, A. V. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201845200 · Cited by 130

Induction of Ca2+-driven apoptosis in chronic lymphocytic leukemia cells by peptide-mediated disruption of Bcl-2–IP3 receptor interaction

Zhong, F., Harr, M. W., Bultynck, G., Monaco, G., Parys, J. B., SMEDT, H. D., Rong, Y.-P., Molitoris, J. K., Lam, M. C., Ryder, C. B., et al. (2010) · Blood · doi:10.1182/blood-2010-09-307405 · Cited by 129

A primer of NAADP-mediated Ca2+ signalling: From sea urchin eggs to mammalian cells

Galione, A. (2014) · Cell Calcium · doi:10.1016/j.ceca.2014.09.010 · Cited by 128

Reconstitution and Characterization of a Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP)-sensitive Ca2+ Release Channel from Liver Lysosomes of Rats

Zhang, F., & Li, P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701614200 · Cited by 128

Nicotinic Acid Adenine Dinucleotide Phosphate (NAADP) Regulates Autophagy in Cultured Astrocytes

Pereira, G. J. S., Hirata, H., Fimia, G. M., do Carmo, L. G., Bincoletto, C., Han, S. W., Stilhano, R. S., Ureshino, R. P., Bloor-Young, D., Churchill, G. C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c110.216580 · Cited by 126

Akt kinase reducing endoplasmic reticulum Ca2+ release protects cells from Ca2+-dependent apoptotic stimuli

Marchi, S., Rimessi, A., Giorgi, C., Baldini, C., Ferroni, L., Rizzuto, R., & Pinton, P. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.07.153 · Cited by 125

Inositol 1,4,5-Trisphosphate and Its Receptors

Parys, J. B., & SMEDT, H. D. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2888-2_11 · Cited by 121

Ryanodine Receptor Physiology and Its Role in Disease

Lanner, J. T. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2888-2_9 · Cited by 121

Mitochondrial Ca2+ signals in autophagy

Cárdenas, C., & Foskett, J. K. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.03.001 · Cited by 120

Accumulation of Cytosolic Calcium Induces Necroptotic Cell Death in Human Neuroblastoma

Nomura, M., Ueno, A., Saga, K., Fukuzawa, M., & Kaneda, Y. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1283 · Cited by 119

ITPR1 Protects Renal Cancer Cells against Natural Killer Cells by Inducing Autophagy

Messai, Y., Noman, M. Z., Hasmim, M., Janji, B., Tittarelli, A., Boutet, M., Baud, V., Viry, E., Billot, K., Nanbakhsh, A., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0303 · Cited by 119

ER-to-mitochondria miscommunication and metabolic diseases

López‐Crisosto, C., Bravo, R., Rodriguez–Peña, M., Mera, C., Castro, P., Quest, A. F. G., Rothermel, B. A., Cifuentes, M., & Lavandero, S. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.07.011 · Cited by 118

TRPP2 channels regulate apoptosis through the Ca2+ concentration in the endoplasmic reticulum

Węgierski, T., Steffl, D., Kopp, C., Tauber, R., Buchholz, B., Nitschke, R., Kuehn, E. W., Walz, G., & Köttgen, M. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.307 · Cited by 118

Drosophila TRPML Is Required for TORC1 Activation

Wong, C., Li, R., Montell, C., & Venkatachalam, K. (2012) · Current Biology · doi:10.1016/j.cub.2012.06.055 · Cited by 115

IP3R2 levels dictate the apoptotic sensitivity of diffuse large B-cell lymphoma cells to an IP3R-derived peptide targeting the BH4 domain of Bcl-2

Akl, H., Monaco, G., Rovere, R. L., Welkenhuyzen, K., Kiviluoto, S., Vervliet, T., Molgó, J., Distelhorst, C., Missiaen, L., Mikoshiba, K., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.140 · Cited by 115

mTOR-Controlled Autophagy Requires Intracellular Ca2+ Signaling

Decuypere, J.-P., Kindt, D., Luyten, T., Welkenhuyzen, K., Missiaen, L., SMEDT, H. D., Bultynck, G., & Parys, J. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061020 · Cited by 115

TRPML1: An Ion Channel in the Lysosome

Wang, W., Zhang, X., Gao, Q., & Xu, H. (2014) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-54215-2_24 · Cited by 114

Characterization of Functional TRPV1 Channels in the Sarcoplasmic Reticulum of Mouse Skeletal Muscle

Lotteau, S. J., Ducreux, S., Romestaing, C., Legrand, C., & Coppenolle, F. V. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058673 · Cited by 112

Two‐pore channels ( TPC s): Current controversies

Morgan, A. J., & Galione, A. (2013) · BioEssays · doi:10.1002/bies.201300118 · Cited by 111

LETM1‐dependent mitochondrial Ca 2+ flux modulates cellular bioenergetics and proliferation

Doonan, P. J., Chandramoorthy, H. C. K., Hoffman, N. E., Zhang, X., Cárdenas, C., Shanmughapriya, S., Rajan, S., Vallem, S., Chen, X., Foskett, J. K., et al. (2014) · The FASEB Journal · doi:10.1096/fj.14-256453 · Cited by 111

Bax Inhibitor-1 Is a pH-dependent Regulator of Ca2+ Channel Activity in the Endoplasmic Reticulum

Kim, H., Lee, G., Ha, K. C., Ahn, T., Moon, J., Lee, B., Cho, S., Kim, S., Seo, Y. R., Shin, Y.-J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800075200 · Cited by 111

New Insights into the Role of Mitochondria-Associated Endoplasmic Reticulum Membrane

Fujimoto, M., & Hayashi, T. (2011) · International review of cytology · doi:10.1016/b978-0-12-386033-0.00002-5 · Cited by 108

The mitochondrial Ca2+ uniporter complex

Foskett, J. K., & Philipson, B. I. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.11.015 · Cited by 108

Interaction of calmodulin with Sec61α limits Ca2+ leakage from the endoplasmic reticulum

Erdmann, F., Schäuble, N., Lang, S., Jung, M., Honigmann, A., Ahmad, M., Dudek, J., Benedix, J., Harsman, A., Kopp, A., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.284 · Cited by 106

Structure-based analysis of VDAC1: N-terminus location, translocation, channel gating and association with anti-apoptotic proteins

Geula, S., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Biochemical Journal · doi:10.1042/bj20112079 · Cited by 105

Ca2+in quality control: An unresolved riddle critical to autophagy and mitophagy

East, D. A., & Campanella, M. (2013) · Autophagy · doi:10.4161/auto.25367 · Cited by 105

Physiology of Astroglia

Verkhratsky, A., & Nedergaard, M. (2018) · Physiological Reviews · doi:10.1152/physrev.00042.2016 · Cited by 1,678

Autophagy, Inflammation, and Immune Dysfunction in the Pathogenesis of Pancreatitis

Gukovskaya, A. S., Gukovsky, I., Algül, H., & Habtezion, A. (2017) · Gastroenterology · doi:10.1053/j.gastro.2017.08.071 · Cited by 357

Mitochondria‐associated endoplasmic reticulum membrane: Overview and inextricable link with cancer

Yang, X., Zhuang, J., Song, W., Shen, W., Wu, W., Shen, H., & Han, S. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17696 · Cited by 55

Impaired calcium signaling in muscle fibers from intercostal and foot skeletal muscle in a cigarette smoke-induced mouse model of COPD: E-C Coupling Dysfunction in COPD

Robison, P., Sussan, T. E., Chen, H., Biswal, S., Schneider, M. F., & Hernández-Ochoa, E. O. (2017) · Muscle & Nerve · doi:10.1002/mus.25466 · Cited by 14