The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Open accessAbstract
Changes in mitochondrial morphology that occur during cell cycle, differentiation, and death are tightly regulated by the balance between fusion and fission processes. Excessive fragmentation can be caused by inhibition of the fusion machinery and is a common consequence of dysfunction of the organelle. Here, we show a role for calcineurin-dependent translocation of the profission dynamin related protein 1 (Drp1) to mitochondria in dysfunction-induced fragmentation. When mitochondrial depolarization is associated with sustained cytosolic Ca 2+ rise, it activates the cytosolic phosphatase calcineurin that normally interacts with Drp1. Calcineurin-dependent dephosphorylation of Drp1, and in particular of its conserved serine 637, regulates its translocation to mitochondria as substantiated by site directed mutagenesis. Thus, fragmentation of depolarized mitochondria depends on a loop involving sustained Ca 2+ rise, activation of calcineurin, and dephosphorylation of Drp1 and its translocation to the organelle.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Interestingly, the downstream ROCK target calcineurin can dephosphorylate Drp1 and cause mitochondrial fission [135,136].”
From RhoA Signaling in Neurodegenerative Diseases (2022) · cites this paper as [135]
Experimental — accuracy not yet measuredIn the citing paper
“The activation of cAMP/PKA upon nutrient starvation leads to phosphorylation of Drp1, preventing its stable docking on the mitochondrial surface and therefore mitochondrial fission (Cereghetti et al, 2008) (Fig 2A).”
From Mitochondrial response to nutrient availability and its role in metabolic disease (2014) · cites this paper as Cereghetti et al, 2008
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Mitochondria: More Than Just a Powerhouse
McBride, H. M., Neuspiel, M., & Wasiak, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.054 · Cited by 1,985
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion
Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673
Self-citationMitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,546
Self-citationBAX and BAK Regulation of Endoplasmic Reticulum Ca 2+ : A Control Point for Apoptosis
Scorrano, L., Oakes, S. A., Opferman, J. T., Cheng, E. H. Y., Sorcinelli, M. D., Pozzan, T., & Korsmeyer, S. J. (2003) · Science · doi:10.1126/science.1081208 · Cited by 1,387
Self-citationMitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission.
Taguchi, N., Ishihara, N., Jofuku, A., Oka, T., & Mihara, K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607279200 · Cited by 1,226
Organelle isolation: functional mitochondria from mouse liver, muscle and cultured filroblasts
Frezza, C., Cipolat, S., & Scorrano, L. (2007) · Nature Protocols · doi:10.1038/nprot.2006.478 · Cited by 1,188
Self-citationCribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,061
Chang, C., & Blackstone, C. D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700083200 · Cited by 824
Self-citationCipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 756
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 997
Mitochondrial dynamics as regulators of cancer biology
Trotta, A. P., & Chipuk, J. E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2451-3 · Cited by 226
CaMKII induces permeability transition through Drp1 phosphorylation during chronic β-AR stimulation
Xu, S., Wang, P., Zhang, H., Gong, G., Gutierrez Cortes, N., Zhu, W., Yoon, Y., Tian, R., & Wang, W. (2016) · Nature Communications · doi:10.1038/ncomms13189 · Cited by 218
Li, S., Xu, S., Roelofs, B. A., Boyman, L., Lederer, W. J., Sesaki, H., & Karbowski, M. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201404050 · Cited by 214
SPG7 Is an Essential and Conserved Component of the Mitochondrial Permeability Transition Pore
Shanmughapriya, S., Rajan, S., Hoffman, N. E., Higgins, A. M., Tomar, D., Nemani, N., Hines, K. J., Smith, D. J., Eguchi, A., Vallem, S., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.009 · Cited by 209
Mechanism of Neuroprotective Mitochondrial Remodeling by PKA/AKAP1
Merrill, R. A., Dagda, R. K., Dickey, A. S., Cribbs, J. T., Green, S. H., Usachev, Y. M., & Strack, S. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000612 · Cited by 212
Mitochondrial Dynamics in Cardiovascular Health and Disease
Ong, S., Hall, A. R., & Hausenloy, D. J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4777 · Cited by 213
Gawlowski, T., Suárez, J., Scott, B. T., Torres‐Gonzalez, M., Wang, H., Schwappacher, R., Han, X., Yates, J. R., Hoshijima, M., & DILLMANN, W. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.390682 · Cited by 214
Resistance to Caspase-Independent Cell Death Requires Persistence of Intact Mitochondria
Tait, S. W. G., Parsons, M. J., Llambi, F., Bouchier‐Hayes, L., Connell, S., Muñoz‐Pinedo, C., & Green, D. R. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.03.014 · Cited by 204
Dany, M., Gencer, S., Nganga, R., Thomas, R. J., Oleinik, N. V., Baron, K. D., Szulc, Z. M., Ruvolo, P. P., Kornblau, S. M., Andreeff, M., et al. (2016) · Blood · doi:10.1182/blood-2016-04-708750 · Cited by 211
Mitochondrial Dynamics in Stem Cells and Differentiation
Seo, B. J., Yoon, S. H., & Tae, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123893 · Cited by 208
The role of Drp1 in mitophagy and cell death in the heart
Tong, M., Zablocki, D., & Sadoshima, J. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.04.015 · Cited by 202
Ottolini, D., Calí, T., Negro, A., & Brini, M. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt068 · Cited by 210
Mitochondria in the maintenance of hematopoietic stem cells: new perspectives and opportunities
Filippi, M., & Ghaffari, S. (2019) · Blood · doi:10.1182/blood-2018-10-808873 · Cited by 209
Dickey, A. S., & Strack, S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3159-11.2011 · Cited by 206
Figueroa‐Romero, C., Iñiguez-Lluhí, J. A., Stadler, J., Chang, C., Arnoult, D., Keller, P. J., Hong, Y. H., Blackstone, C. D., & Feldman, E. L. (2009) · The FASEB Journal · doi:10.1096/fj.09-136630 · Cited by 207
Self-citationFerreira-da-Silva, A., Valacca, C., Rios, E., Pópulo, H., Soares, P., Sobrinho-Simões, M. A., Scorrano, L., Máximo, V., & Campello, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122308 · Cited by 200
Self-citationRomanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197
Mitochondrial fusion proteins: Dual regulators of morphology and metabolism
Antonio Zorzano, A., Liesa, M., Sebastián, D., Segalés, J., & Palacín, M. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.01.002 · Cited by 204
Mitochondrial dynamics and viral infections: A close nexus
Khan, M. A., Syed, G. H., Kim, S., & Siddiqui, A. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.040 · Cited by 195
Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission
Koirala, S., Guo, Q., Kalia, R., Bui, H., Eckert, D. M., Frost, A. S., & Shaw, J. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300855110 · Cited by 201
Dysregulated Mitochondrial Dynamics and Metabolism in Obesity, Diabetes, and Cancer
Dai, W., & Jiang, L. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00570 · Cited by 186
Baixauli, F., Martin-Cofreces, N. B., Morlino, G., Carrasco, Y. R., Calabia-Linares, C., Veiga, E., Serrador, J. M., & Sánchez‐Madrid, F. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.25 · Cited by 191
Pink1 disables the anti-fission machinery to segregate damaged mitochondria for mitophagy
Pryde, K. R., Smith, H. L., Chau, K.-Y., & Schapira, A. H. V. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201509003 · Cited by 185
The ever-growing complexity of the mitochondrial fission machinery
Pagliuso, A., Cossart, P., & Stavru, F. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2603-0 · Cited by 192
Mitochondrial Dynamics in Basal and Stressful Conditions
Zemirli, N., Morel, É., & Molino, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020564 · Cited by 196
Mitochondrial network structure homeostasis and cell death
Xie, L., Shi, F., Tan, Z., Li, Y., Bode, A. M., & Cao, Y. (2018) · Cancer Science · doi:10.1111/cas.13830 · Cited by 179
Neurodegeneration as a consequence of failed mitochondrial maintenance
Karbowski, M., & Neutzner, A. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0921-0 · Cited by 187
Mitochondrial alterations in apoptosis
Cosentino, K., & García‐Sáez, A. J. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2014.04.001 · Cited by 199
Morphological dynamics of mitochondria — A special emphasis on cardiac muscle cells
Hom, J., & Sheu, S. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.02.023 · Cited by 189
Cyclophilin D in mitochondrial pathophysiology
Giorgio, V., Soriano, M. E., Basso, E., Bisetto, E., Lippe, G., Forte, M. A., & Bernardi, P. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.12.006 · Cited by 179
Self-citationAt 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
Self-citationConstriction of the mitochondrial inner compartment is a priming event for mitochondrial division
Cho, B., Cho, H. M., Jo, Y., Kim, H. D., Song, M., Moon, C., Kim, H., Kim, K., Sesaki, H., Rhyu, I. J., et al. (2017) · Nature Communications · doi:10.1038/ncomms15754 · Cited by 179
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
Mitochondrial quality control in human health and disease
Liu, B., Xu, C.-Z., Liu, Y., Lu, Z., Fu, T.-L., Li, G., Deng, Y., Luo, G., Ding, S. Z., Li, N., et al. (2024) · Military Medical Research · doi:10.1186/s40779-024-00536-5 · Cited by 211
Matton, A., Craig, K. J. T., Beilina, A. G., van der Brug, M., Harwig, M. C., Ahmad, R., Miller, D. W., Zambrano, I., Cowburn, R. F., Behbahani, H., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005701 · Cited by 181
Jain, P., Luo, Z., & Blanke, S. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105175108 · Cited by 173
H2O2-induced mitochondrial fragmentation in C2C12 myocytes
Fan, X., Hussien, R., & Brooks, G. A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.08.024 · Cited by 175
Caspase-cleaved Tau Expression Induces Mitochondrial Dysfunction in Immortalized Cortical Neurons
Quintanilla, R. A., Matthews-Roberson, T. A., Dolan, P. J., & Johnson, G. V. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808908200 · Cited by 170
The permeability transition pore as a Ca2+ release channel: New answers to an old question
Bernardi, P., & von Stockum, S. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.03.004 · Cited by 183
Self-citationDynamics of Dynamin-Related Protein 1 in Alzheimer’s Disease and Other Neurodegenerative Diseases
Oliver, D., & Reddy, P. H. (2019) · Cells · doi:10.3390/cells8090961 · Cited by 172
p53 and mitochondrial function in neurons
Wang, D. B., Kinoshita, C., Kinoshita, Y., & Morrison, R. S. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.12.015 · Cited by 174
Cell Death Pathways in Acute Ischemia/Reperfusion Injury
Gottlieb, R. A. (2011) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248411409581 · Cited by 171
Bonello, F., Hassoun, S.-M., Mouton-Liger, F., Shin, Y. S., Muscat, A., Tesson, C., Lesage, S., Beart, P. M., Brice, A., Krupp, J., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz004 · Cited by 163
Staying cool in difficult times: Mitochondrial dynamics, quality control and the stress response
Shutt, T. E., & McBride, H. M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.024 · Cited by 167
Low-level laser therapy for beta amyloid toxicity in rat hippocampus
Lu, Y., Wang, R., Dong, Y., Tucker, D., Zhao, N., Ahmed, M. E., Zhu, L., Liu, T. C., Cohen, R. M., & Zhang, Q. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.10.003 · Cited by 165
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 162
Specific Interaction with Cardiolipin Triggers Functional Activation of Dynamin-Related Protein 1
Bustillo-Zabalbeitia, I., Montessuit, S., Raemy, E., Basañez, G., Terrones, O., & Martinou, J.-C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102738 · Cited by 162
Zunino, R., Braschi, E., Xu, L., & McBride, H. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901902200 · Cited by 166
Bossy, B., Petrilli, A. M., Klinglmayr, E., Chen, J., Lütz‐Meindl, U., Knott, A. B., Masliah, E., Schwarzenbacher, R., & Bossy‐Wetzel, E. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100552 · Cited by 165
Shaping the role of mitochondria in the pathogenesis of Huntington's disease
Costa, V., & Scorrano, L. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.65 · Cited by 162
Self-citationA novel autophagy enhancer as a therapeutic agent against metabolic syndrome and diabetes
Lim, H. J., Lim, Y.-M., Kim, K. H., Jeon, Y. E., Park, K., Kim, J., Hwang, H., Lee, D., Pagire, H. S., Kwon, H. J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03939-w · Cited by 164
Altered Mitochondrial Dynamics and TBI Pathophysiology
Fischer, T. D., Hylin, M. J., Zhao, J., Moore, A. N., Waxham, M. N., & Dash, P. K. (2016) · Frontiers in Systems Neuroscience · doi:10.3389/fnsys.2016.00029 · Cited by 160
Xu, S., Pi, H., Chen, Y., Zhang, N., Guo, P., Lu, Y., He, M., Xie, J., Zhong, M., Zhang, Y., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.7 · Cited by 159
Mitochondrial dynamics and mitophagy in lung disorders
Sharma, A. K., Ahmad, S., Ahmad, T., Ali, S., & Syed, M. A. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119876 · Cited by 161
Mitophagy in Cerebral Ischemia and Ischemia/Reperfusion Injury
Shen, L., Gan, Q., Yang, Y., Reis, C., Zhang, Z., Xu, S., Zhang, T., & Sun, C. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.687246 · Cited by 162
Pennanen, C., Parra, V., López‐Crisosto, C., Morales, P. E., del Campo, A., Gutiérrez, T., Rivera-Mejías, P., Kuzmicic, J., Chiong, M., Antonio Zorzano, A., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.139394 · Cited by 166
Mitophagy: the latest problem for Parkinson's disease
Vives-Bauzá, C., & Przedborski, S. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.11.002 · Cited by 161
Mitochondrial dynamics and cell death in heart failure
Marín-García, J., & Akhmedov, A. T. (2016) · Heart Failure Reviews · doi:10.1007/s10741-016-9530-2 · Cited by 160
Mul1 restrains Parkin-mediated mitophagy in mature neurons by maintaining ER-mitochondrial contacts
Puri, R., Cheng, X., Lin, M.-Y., Huang, N., & Sheng, Z. (2019) · Nature Communications · doi:10.1038/s41467-019-11636-5 · Cited by 160
Valsecchi, F., Ramos-Espiritu, L. S., Buck, J., Levin, L. R., & Manfredi, G. (2013) · Physiology · doi:10.1152/physiol.00004.2013 · Cited by 155
Roles of mitochondrial dynamics modulators in cardiac ischaemia/reperfusion injury
Maneechote, C., Palee, S., Chattipakorn, S. C., & Chattipakorn, N. (2017) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13330 · Cited by 154
Cell death in the myocardium: My heart won't go on
Orogo, A. M., & Gustafsson, Å. B. (2013) · IUBMB Life · doi:10.1002/iub.1180 · Cited by 152
Mitochondrial morphology—emerging role in bioenergetics
Galloway, C. A., Lee, H., & Yoon, Y. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.035 · Cited by 159
Mitochondrial response to nutrient availability and its role in metabolic disease
Gao, A. W., Cantó, C., & Houtkooper, R. H. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201303782 · Cited by 148
Molecular regulation of mitochondrial dynamics in cardiac disease
Nan, J., Zhu, W. M., Rahman, M. S. U., Liu, M., Li, D. X., Su, S., Zhang, N., Hu, X., Yu, H., Gupta, M. P., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.03.006 · Cited by 150
Mitochondrial cAMP-PKA signaling: What do we really know?
Amer, Y. O., & Hébert-Chatelain, É. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.04.005 · Cited by 146
Ju, W., Perkins, G. A., Keun-young Kim, A., Bastola, T., Choi, W.-Y., & Choi, S. (2022) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2022.101136 · Cited by 152
Kang, Y. J., Bang, B., Han, K. H., Hong, L., Shim, E.-J., Ma, J., Lerner, R. A., & Otsuka, M. (2015) · Nature Communications · doi:10.1038/ncomms9371 · Cited by 146
Mitochondrial dynamics controls anti-tumour innate immunity by regulating CHIP-IRF1 axis stability
Gao, Z., Li, Y., Wang, F., Huang, T., Fan, K.-Q., Zhang, Y., Zhong, J.-Y., Cao, Q., Tong, C., Jia, J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01919-0 · Cited by 149
Ong, S., Kalkhoran, S. B., Cabrera-Fuentes, H. A., & Hausenloy, D. J. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.04.056 · Cited by 145
Fundamentals of T Cell Metabolism and Strategies to Enhance Cancer Immunotherapy
Rivera, G. O. R., Knochelmann, H. M., Dwyer, C. J., Smith, A. S., Wyatt, M. M., Rivera-Reyes, A. M., Thaxton, J. E., & Paulos, C. M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.645242 · Cited by 154
A neuron–glia lipid metabolic cycle couples daily sleep to mitochondrial homeostasis
Haynes, P. R., Pyfrom, E. S., Li, Y., Stein, C., Cuddapah, V. A., Jacobs, J. A., Yue, Z., & Sehgal, A. (2024) · Nature Neuroscience · doi:10.1038/s41593-023-01568-1 · Cited by 149
Zhang, B., Alysandratos, K., Angelidou, A., Asadi, S., Sismanopoulos, N., Delivanis, D.-A., Weng, Z., Miniati, A., Vasiadi, M., Katsarou‐Katsari, A., et al. (2011) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2011.02.005 · Cited by 144
Dagda, R. K., Gusdon, A. M., Pien, I., Strack, S., Green, S., Li, C., Houten, B. V., Cherra, S. J., & Chu, C. T. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.74 · Cited by 146
New insights into the role of mitochondrial calcium homeostasis in cell migration
Paupe, V., & Prudent, J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.05.039 · Cited by 146
SR and mitochondria: Calcium cross-talk between kissing cousins
Dorn, G. W., & Maack, C. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.07.015 · Cited by 146
Loss of OMA1 delays neurodegeneration by preventing stress-induced OPA1 processing in mitochondria
Korwitz, A., Merkwirth, C., Richter‐Dennerlein, R., Tröder, S. E., Sprenger, H., Quirós, P. M., López-Otı́n, C., Rugarli, E. I., & Langer, T. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201507022 · Cited by 138
Mechanisms and roles of mitochondrial localisation and dynamics in neuronal function
Seager, R., Lee, L. J., Henley, J. M., & Wilkinson, K. A. (2020) · Neuronal Signaling · doi:10.1042/ns20200008 · Cited by 152
Xu, S., Pi, H., Zhang, L., Zhang, N.-X., Li, Y., Zhang, H., Tang, J., Li, H., Feng, M., Deng, P., et al. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12310 · Cited by 139
Virus Control of Cell Metabolism for Replication and Evasion of Host Immune Responses
Moreno‐Altamirano, M. M. B., Kolstoe, S. E., & Sánchez-García, F. J. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00095 · Cited by 136
AKAP1 Protects from Cerebral Ischemic Stroke by Inhibiting Drp1-Dependent Mitochondrial Fission
Flippo, K. H., Gnanasekaran, A., Perkins, G. A., Ahmad, A., Merrill, R. A., Dickey, A. S., Taylor, S. S., McKnight, G. S., Chauhan, A. K., Usachev, Y. M., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.0649-18.2018 · Cited by 142
Park, H., Yoon, N. G., Lee, J., Hu, S., Yoon, S., Kim, S. Y., Hong, J.-H., Nam, D., Chae, Y. C., Park, J. B., et al. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0360-x · Cited by 139
Physiological Mitochondrial Fragmentation Is a Normal Cardiac Adaptation to Increased Energy Demand
Coronado, M. J., Fajardo, G., Nguyen, K., Zhao, M., Kooiker, K. B., Jung, G., Hu, D., Reddy, S., Sandoval, E., Stotland, A. B., et al. (2017) · Circulation Research · doi:10.1161/circresaha.117.310725 · Cited by 136
Mitochondrial Dynamics in Diabetic Cardiomyopathy
Galloway, C. A., & Yoon, Y. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6293 · Cited by 135
Pim-1 preserves mitochondrial morphology by inhibiting dynamin-related protein 1 translocation
Din, S., Mason, M., Völkers, M., Johnson, B., Cottage, C. T., Wang, Z., Joyo, A. Y., Quijada, P. J., Erhardt, P., Magnuson, N. S., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213294110 · Cited by 139
Silva, D. F., Selfridge, J. E., Lu, J., E, L., Roy, N., Hutfles, L., Burns, J. M., Michaelis, E. K., Yan, S., Cardoso, S. M., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt247 · Cited by 133
The molecular mechanism and cellular functions of mitochondrial division
Lackner, L. L., & Nunnari, J. M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.11.011 · Cited by 136
Moore, T. M., Zhou, Z., Cohn, W., Norheim, F., Lin, A. J., Kalajian, N., Strumwasser, A. R., Cory, K., Whitney, K., Ho, T., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2018.11.012 · Cited by 131
The changing shape of mitochondrial apoptosis
Wasilewski, M., & Scorrano, L. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.03.007 · Cited by 135
Self-citationBrain iron overload following intracranial haemorrhage
Garton, T. P., Keep, R. F., Hua, Y., & Xi, G. (2016) · Stroke and Vascular Neurology · doi:10.1136/svn-2016-000042 · Cited by 131
Oettinghaus, B., Schulz, J. M., Restelli, L. M., Licci, M., Savoia, C., Schmidt, A., Schmitt, K., Grimm, A., Morè, L., Hench, J., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.39 · Cited by 130
Self-citationAtypical mitochondrial fission upon bacterial infection
Stavru, F., Palmer, A. E., Wang, C., Youle, R. J., & Cossart, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315784110 · Cited by 129
The mitochondrial permeability transition pore and cyclophilin D in cardioprotection
Lisa, F. D., Carpi, A., Giorgio, V., & Bernardi, P. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.01.031 · Cited by 132
Self-citationCeramide induced mitophagy and tumor suppression
Dany, M., & Öğretmen, B. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.12.039 · Cited by 130
Wang, X., Su, B., Liu, W., He, X., Gao, Y., Castellani, R. J., Perry, G. L., Smith, M. A., & Zhu, X. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00721.x · Cited by 134
Mitochondrial Dynamics: Functional Link with Apoptosis
Otera, H., & Mihara, K. (2012) · International Journal of Cell Biology · doi:10.1155/2012/821676 · Cited by 131
Deng, X., Liu, J., Liu, L., Sun, X., Huang, J., & Dong, J. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.41768 · Cited by 128
Palma, E., Tiepolo, T., Angelin, A., Sabatelli, P., Maraldi, N. M., Basso, E., Forte, M. A., Bernardi, P., & Bonaldo, P. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp126 · Cited by 128
Self-citationMitochondrial outer-membrane permeabilization and remodelling in apoptosis
Jourdain, A. A., & Martinou, J. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.05.001 · Cited by 133
Mitochondrial Morphofunction in Mammalian Cells
Bulthuis, E. P., Adjobo-Hermans, M. J. W., Willems, P. H. G. M., & Koopman, W. J. H. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7534 · Cited by 133
Metadata
- Authors
- Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L.
- Affiliations
- Veneto Institute of Molecular Medicine (IT)
- *Dulbecco-Telethon Institute;
- National Institutes of Health (US)
- University of Padua (IT)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-10-14
- Volume
- 105
- Issue
- 41
- Pages
- 15803-15808
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2572940
- OpenAlex
- W2023283007
- Cited by
- 1,129
- References
- 35
- Citations by year
- 2026: 40 · 2025: 51 · 2024: 54 · 2023: 79 · 2022: 67 · 2021: 79 · 2020: 92 · 2019: 60 · 2018: 86 · 2017: 78 · 2016: 80 · 2015: 59 · 2014: 68 · 2013: 58 · 2012: 54
- FWCI
- 16.44
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (acceptedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Padua Research Archive (University of Padova) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- calcineurin, Drp1, mitochondrial fission, mitochondrial depolarization, mitochondrial fragmentation, intracellular calcium, mitochondrial morphology, mitochondrial fusion
- MeSH terms
- Calcium, HeLa Cells, Humans, Microtubule-Associated Proteins, Mitochondria, Phosphorylation, Serine, Mutagenesis, Site-Directed, Calcineurin, GTP Phosphohydrolases, Protein Transport, Mitochondrial Proteins, Dynamins, Membrane Potential, Mitochondrial
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
