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
Cited by
Sorted by citations
Mitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002
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
During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735
Self-citationPINK1-dependent recruitment of Parkin to mitochondria in mitophagy
Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616
The cell biology of mitochondrial membrane dynamics
Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550
Self-citationMitochondrial Dynamics Controls T Cell Fate through Metabolic Programming
Buck, M. D., O’Sullivan, D., Geltink, R. I. K., Curtis, J. D., Chang, C., Sanin, D. E., Qiu, J., Kretz, O., Braas, D., van der Windt, G. J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.035 · Cited by 1,491
Self-citationMitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
Mitochondrial energetics in the kidney
Bhargava, P., & Schnellmann, R. G. (2017) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.107 · Cited by 1,391
Mitochondrial Dynamics in the Regulation of Nutrient Utilization and Energy Expenditure
Liesa, M., & Shirihai, O. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.002 · Cited by 1,341
Cogliati, S., Frezza, C., Soriano, M. E., Varanita, T., Quintana-Cabrera, R., Corrado, M., Cipolat, S., Costa, V., Casarin, A., Gomes, L. C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.032 · Cited by 1,265
Self-citationFis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224
Fusion and fission: interlinked processes critical for mitochondrial health
Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196
Rambold, A. S., Kostelecky, B., Elia, N., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107402108 · Cited by 1,188
Metabolic regulation of mitochondrial dynamics
Mishra, P., & Chan, D. C. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201511036 · Cited by 1,143
Mitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953
Mechanisms of Mitochondrial Fission and FusionPreprint
van der Bliek, A. M., Shen, Q., & Kawajiri, S. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011072 · Cited by 903
Pernas, L. F., & Scorrano, L. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105011 · Cited by 845
Self-citationMitochondrial fusion and fission: The fine‐tune balance for cellular homeostasis
Adebayo, M., Singh, S., Singh, A. P., & Dasgupta, S. (2021) · The FASEB Journal · doi:10.1096/fj.202100067r · Cited by 733
Mitochondrial Defects and Oxidative Stress in Alzheimer Disease and Parkinson Disease
Yan, M. H., Wang, X., & Zhu, X. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.014 · Cited by 718
Mitochondrial dysfunction in diabetic kidney disease
Forbes, J. M., & Thorburn, D. R. (2018) · Nature Reviews Nephrology · doi:10.1038/nrneph.2018.9 · Cited by 650
Mitochondrial dynamics, mitophagy and cardiovascular disease
Vásquez-Trincado, C., García‐Carvajal, I., Pennanen, C., Parra, V., Hill, J. A., Rothermel, B. A., & Lavandero, S. (2015) · The Journal of Physiology · doi:10.1113/jp271301 · Cited by 637
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
Benador, I. Y., Veliova, M., Mahdaviani, K., Petcherski, A., Wikström, J. D., Assali, E. A., Acín‐Pérez, R., Shum, M., de Oliveira, M. F., Cinti, S., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.003 · Cited by 640
miR-499 regulates mitochondrial dynamics by targeting calcineurin and dynamin-related protein-1
Wang, J., Jiao, J.-Q., Li, Q., Long, B., Wang, K., Liu, J., Li, Y.-R., & Li, P. (2010) · Nature Medicine · doi:10.1038/nm.2282 · Cited by 582
Bernardi, P., Rasola, A., Forte, M. A., & Lippe, G. (2015) · Physiological Reviews · doi:10.1152/physrev.00001.2015 · Cited by 598
Self-citationDynamic regulation of mitochondrial fission through modification of the dynamin‐related protein Drp1
Chang, C., & Blackstone, C. D. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05629.x · Cited by 602
Self-citationLaker, R. C., Drake, J. C., Wilson, R. J., Lira, V. A., Lewellen, B. M., Ryall, K. A., Fisher, C. C., Zhang, M., Saucerman, J. J., Goodyear, L. J., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00520-9 · Cited by 529
Mitochondrial Dysfunction in Cancer
Boland, M. L., Chourasia, A. H., & Macleod, K. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00292 · Cited by 521
Bernardi, P., & Lisa, F. D. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.023 · Cited by 503
Self-citationNew insights into the function and regulation of mitochondrial fission
Otera, H., Ishihara, N., & Mihara, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.002 · Cited by 501
Mishra, P., Carelli, V., Manfredi, G., & Chan, D. C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.011 · Cited by 473
Shirakabe, A., Zhai, P., Ikeda, Y., Saito, T., Maejima, Y., Hsu, C., Nomura, M., Egashira, K., Levine, B., & Sadoshima, J. (2016) · Circulation · doi:10.1161/circulationaha.115.020502 · Cited by 467
Varanita, T., Soriano, M. E., Romanello, V., Zaglia, T., Quintana-Cabrera, R., Semenzato, M., Menabò, R., Costa, V., Civiletto, G., Pesce, P., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.007 · Cited by 460
Self-citationFunction and regulation of the divisome for mitochondrial fission
Kraus, F., Roy, K., Pucadyil, T. J., & Ryan, M. T. (2021) · Nature · doi:10.1038/s41586-021-03214-x · Cited by 445
Raturi, A., & Simmen, T. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.04.013 · Cited by 470
Mitochondrial quality control and muscle mass maintenance.
Romanello, V., & Sandri, M. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2015.00422 · Cited by 434
Morais, V. A., Verstreken, P., Röthig, A. H. J., Smet, J., Snellinx, A., Vanbrabant, M., Haddad, D., Frezza, C., Mandemakers, W. J., Weisenhorn, D. M. V., et al. (2009) · EMBO Molecular Medicine · doi:10.1002/emmm.200900006 · Cited by 462
Self-citationMetformin Improves Mitochondrial Respiratory Activity through Activation of AMPK
Wang, Y., An, H., Liu, T., Qin, C., Sesaki, H., Guo, S., Radovick, S., Hussain, M., Maheshwari, A., Wondisford, F. E., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.070 · Cited by 432
“Because fission is associated with mitochondrial respiration (Cereghetti et al., 2008; Ishihara et al., 2006; Tanaka et al., 2010) and inhibition of fission by knocking out Drp1 impairs liver function (Yamada et al.”
BackgroundRole of Cardiolipin in Mitochondrial Signaling Pathways
Dudek, J. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00090 · Cited by 444
Mitochondria: from cell death executioners to regulators of cell differentiation
Kasahara, A., & Scorrano, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.08.005 · Cited by 433
Self-citationBøtker, H. E., Hausenloy, D. J., Andreadou, I., Antonucci, S., Boengler, K., Davidson, S. M., Deshwal, S., Devaux, Y., Lisa, F. D., Sante, M. D., et al. (2018) · Basic Research in Cardiology · doi:10.1007/s00395-018-0696-8 · Cited by 436
Wu, S., Zhou, F., Zhang, Z., & Xing, D. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08010.x · Cited by 423
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 445
Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology
Zhan, M., Brooks, C. R., Liu, F., Sun, L., & Dong, Z. (2013) · Kidney International · doi:10.1038/ki.2012.441 · Cited by 401
Mitochondrial Networking Protects β-Cells From Nutrient-Induced Apoptosis
Molina, A. J. A., Wikstrom, J. D., Stiles, L., Las, G., Mohamed, H., Elorza, A., Walzer, G., Twig, G., Katz, S., Corkey, B. E., et al. (2009) · Diabetes · doi:10.2337/db07-1781 · Cited by 381
Tau Promotes Neurodegeneration via DRP1 Mislocalization In Vivo
DuBoff, B., Götz, J., & Feany, M. B. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.026 · Cited by 377
mTOR Controls Mitochondrial Dynamics and Cell Survival via MTFP1
Morita, M., Prudent, J., Basu, K., Goyon, V., Katsumura, S., Hulea, L., Pearl, D., Siddiqui, N., Strack, S., McGuirk, S., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.013 · Cited by 381
Structural basis of mitochondrial receptor binding and constriction by DRP1
Kalia, R., Wang, R. Y., Yusuf, A., Thomas, P. V., Agard, D. A., Shaw, J. M., & Frost, A. S. (2018) · Nature · doi:10.1038/s41586-018-0211-2 · Cited by 385
Mitochondrial fusion/fission dynamics in neurodegeneration and neuronal plasticity
Bertholet, A. M., Delerue, T., Millet, A. M., Moulis, M. F., David, C., Daloyau, M., Arnauné-Pelloquin, L., Davezac, N., Mils, V., Miquel, M. C., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.10.011 · Cited by 363
Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H. H., Li, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593102 · Cited by 370
Mitochondrial Fusion Directs Cardiomyocyte Differentiation via Calcineurin and Notch Signaling
Kasahara, A., Cipolat, S., Chen, Y., Dorn, G. W., & Scorrano, L. (2013) · Science · doi:10.1126/science.1241359 · Cited by 354
Self-citationSharp, W. W., Fang, Y. H., Han, M., Zhang, H. J., Hong, Z., Banathy, A., Morrow, E., Ryan, J. J., & Archer, S. L. (2013) · The FASEB Journal · doi:10.1096/fj.12-226225 · Cited by 361
Mitochondrial fission requires DRP1 but not dynamins
Fonseca, T. B., Sánchez-Guerrero, Á., Milošević, I., & Raimundo, N. (2019) · Nature · doi:10.1038/s41586-019-1296-y · Cited by 353
Determinants and outcomes of mitochondrial dynamics
Quintana–Cabrera, R., & Scorrano, L. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.012 · Cited by 362
Self-citationBaker, M. J., Lampe, P., Stojanovski, D., Korwitz, A., Anand, R., Tatsuta, T., & Langer, T. (2014) · The EMBO Journal · doi:10.1002/embj.201386474 · Cited by 367
Mitochondrial ‘kiss‐and‐run’: interplay between mitochondrial motility and fusion–fission dynamics
Liu, X., Weaver, D., Shirihai, O. S., & Hajnóczky, G. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.255 · Cited by 360
Mitochondria in acute myocardial infarction and cardioprotection
Ramachandra, C. J. A., Hernández‐Reséndiz, S., Crespo-Avilan, G. E., Lin, Y., & Hausenloy, D. J. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.102884 · Cited by 348
Circadian Control of DRP1 Activity Regulates Mitochondrial Dynamics and Bioenergetics
Schmitt, K., Grimm, A., Dallmann, R., Oettinghaus, B., Restelli, L. M., Witzig, M., Ishihara, N., Mihara, K., Ripperger, J. A., Albrecht, U., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.01.011 · Cited by 346
Kim, D., Hwang, H., Ji, E. S., Kim, J. Y., Yoo, J. S., & Kwon, H. J. (2021) · Communications Biology · doi:10.1038/s42003-020-01566-0 · Cited by 333
MAPL SUMOylation of Drp1 Stabilizes an ER/Mitochondrial Platform Required for Cell Death
Prudent, J., Zunino, R., Sugiura, A., Mattie, S., Shore, G. C., & McBride, H. M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.08.001 · Cited by 335
Mitochondrial morphology and cardiovascular disease
Ong, S., & Hausenloy, D. J. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq237 · Cited by 331
Determinants and Functions of Mitochondrial Behavior
Labbè, K., Murley, A., & Nunnari, J. M. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155756 · Cited by 324
Regulation of Mitochondrial ATP Production: Ca2+ Signaling and Quality Control
Boyman, L., Karbowski, M., & Lederer, W. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.007 · Cited by 310
SR/ER–mitochondrial local communication: Calcium and ROS
Csordás, G., & Hajnóczky, G. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.06.004 · Cited by 316
The role of mitochondrial fission in cardiovascular health and disease
Quiles, J. M., & Gustafsson, Å. B. (2022) · Nature Reviews Cardiology · doi:10.1038/s41569-022-00703-y · Cited by 315
Molecular Strategies for Targeting Antioxidants to Mitochondria: Therapeutic Implications
Apostolova, N., & Víctor, V. M. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5952 · Cited by 311
Mitochondrial dynamics in cell death and neurodegeneration
Cho, D., Nakamura, T., & Lipton, S. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0435-2 · Cited by 306
Kim, S., Syed, G. H., Khan, M. A., Chiu, W.-W., Sohail, M. A., Gish, R. G., & Siddiqui, A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321114111 · Cited by 293
An intimate liaison: spatial organization of the endoplasmic reticulum–mitochondria relationship
de Brito, O. M., & Scorrano, L. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.177 · Cited by 310
Self-citationMitochondria–Lysosome Crosstalk: From Physiology to Neurodegeneration
Deus, C. M., Yambire, K. F., Oliveira, P. J., & Raimundo, N. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.009 · Cited by 299
Abnormal mitochondrial dynamics and neurodegenerative diseases
Su, B., Wang, X., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.013 · Cited by 301
Costa, V., Giacomello, M., Hudec, R., Lopreiato, R., Ermak, G., Lim, D., Malorni, W., Davies, K. J. A., Carafoli, E., & Scorrano, L. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000102 · Cited by 293
Self-citationYu, T., Jhun, B. S., & Yoon, Y. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3284 · Cited by 293
Hall, A. R., Burke, N., Dongworth, R. K., & Hausenloy, D. J. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12516 · Cited by 294
Vos, M. H. (2010) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2010.00139 · Cited by 307
Mitochondrial Dynamics: Coupling Mitochondrial Fitness with Healthy Aging
Sebastián, D., Palacı́n, M., & Antonio Zorzano, A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.01.003 · Cited by 292
The regulation of mitochondrial morphology: Intricate mechanisms and dynamic machinery
Palmer, C. S., Osellame, L. D., Stojanovski, D., & Ryan, M. T. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.021 · Cited by 300
Mitochondrial dynamics modulate the expression of pro‐inflammatory mediators in microglial cells
Park, J., Choi, H., Min, J., Park, S., Kim, J., Park, H., Kim, B., Chae, J., Yim, M., & Lee, D. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12361 · Cited by 270
Prieto, J., León, M., Ponsoda, X., Sendra, R., Bort, R., Ferrer‐Lorente, R., Raya, Á., López‐García, C., & Torres, J. (2016) · Nature Communications · doi:10.1038/ncomms11124 · Cited by 286
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
The Functional Impact of Mitochondrial Structure Across Subcellular Scales
Glancy, B. C., Kim, Y., Katti, P., & Willingham, T. B. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.541040 · Cited by 270
Stephan, T., Brüser, C., Deckers, M., Steyer, A. M., Balzarotti, F., Barbot, M., Behr, T. S., Heim, G., Hübner, W., Ilgen, P., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019104105 · Cited by 253
Recent advances into the understanding of mitochondrial fission
Elgass, K., Pakay, J. L., Ryan, M. T., & Palmer, C. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.002 · Cited by 274
Zhou, J., Li, G., Zheng, Y., Shen, H., Hu, X., Ming, Q., Huang, C., Li, P., & Gao, N. (2015) · Autophagy · doi:10.1080/15548627.2015.1056970 · Cited by 267
Wikström, J. D., Mahdaviani, K., Liesa, M., Sereda, S. B., Si, Y., Las, G., Twig, G., Petrovič, N., Zingaretti, C. M., Graham, A., et al. (2014) · The EMBO Journal · doi:10.1002/embj.201385014 · Cited by 267
Increased Drp1 Acetylation by Lipid Overload Induces Cardiomyocyte Death and Heart Dysfunction
Hu, Q., Zhang, H., Cortés, N. G., Wu, D., Wang, P., Zhang, J., Mattison, J. A., Smith, E., Bettcher, L., Wang, M., et al. (2020) · Circulation Research · doi:10.1161/circresaha.119.315252 · Cited by 265
Ribas, V., Drew, B. G., Zhou, Z., Phun, J., Kalajian, N. Y., Soleymani, T., Daraei, P., Widjaja, K., Wanagat, J., de Aguiar Vallim, T. Q., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad3815 · Cited by 259
Qi, X., Disatnik, M., Shen, N., Sobel, R. A., & Mochly‐Rosen, D. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-06-0551 · Cited by 264
Mitochondrial dynamics in neuronal injury, development and plasticity
Flippo, K. H., & Strack, S. (2017) · Journal of Cell Science · doi:10.1242/jcs.171017 · Cited by 263
Molecular mechanisms and physiologic functions of mitochondrial dynamics
Otera, H., & Mihara, K. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr002 · Cited by 265
Mitochondrial morphology in mitophagy and macroautophagy
Gomes, L. C., & Scorrano, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.012 · Cited by 259
Self-citationRole of mitochondrial quality surveillance in myocardial infarction: From bench to bedside
Zhou, H., Ren, J. T., Toan, S., & Mui, D. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101250 · Cited by 253
Calcium Transport and Signaling in Mitochondria
Bravo, R., Parra, V., López‐Crisosto, C., Díaz, P., Quest, A. F. G., & Lavandero, S. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160013 · Cited by 304
The constriction and scission machineries involved in mitochondrial fission
Kraus, F., & Ryan, M. T. (2017) · Journal of Cell Science · doi:10.1242/jcs.199562 · Cited by 244
Pyakurel, A., Savoia, C., Hess, D., & Scorrano, L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.021 · Cited by 244
Self-citationMitochondrial fission/fusion dynamics and apoptosis
Sheridan, C., & Martin, S. J. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.08.005 · Cited by 247
Mitochondrial dynamics in the adult cardiomyocytes: which roles for a highly specialized cell?
Piquereau, J., Caffin, F., Novotová, M., Lemaire, C., Veksler, V., Garnier, A., Ventura‐Clapier, R., & Joubert, F. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00102 · Cited by 251
Mitochondrial dynamics and their potential as a therapeutic target
Whitley, B. N., Engelhart, E. A., & Hoppins, S. C. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.002 · Cited by 228
Tolkovsky, A. M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.03.002 · Cited by 231
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
