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
Items 601–700 of 997
Bonda, D., Smith, M. A., Perry, G. L., Lee, H., Wang, X., & Zhu, X. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072562 · Cited by 35
Fu, P., Epshtein, Y., Ramchandran, R., Mascarenhas, J. B., Cress, A. E., Jacobson, J. R., Garcia, J. G. N., & Natarajan, V. (2021) · Scientific Reports · doi:10.1038/s41598-021-97006-y · Cited by 34
Nan, J., Li, J., Lin, Y., Rahman, M. S. U., Li, Z., & Zhu, L. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16941 · Cited by 35
Brusco, J., & Haas, K. Z. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.282459 · Cited by 32
Mitochondrial Ca2+ transport and permeability transition in zebrafish (Danio rerio)
Azzolin, L., Basso, E., Argenton, F., & Bernardi, P. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.07.002 · Cited by 34
Self-citationAli, M. Z., & Dholaniya, P. S. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105344 · Cited by 33
Sun, Z., Ma, Z., Cao, W., Jiang, C., Guo, L., Liu, K., Gao, Y., Bai, J., Pi, J., Jiang, P., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1012872 · Cited by 34
Role of Presenilin in Mitochondrial Oxidative Stress and Neurodegeneration in Caenorhabditis elegans
Sarasija, S., & Norman, K. R. (2018) · Antioxidants · doi:10.3390/antiox7090111 · Cited by 31
Drp1 Phosphorylation Is Indispensable for Steroidogenesis in Leydig Cells
Park, J.-E., Kim, Y. J., Lee, S. G., Kim, J. Y., Chung, J.-Y., Jeong, S.-Y., Koh, H., Yun, J., Park, H. T., Yoo, Y. H., et al. (2019) · Endocrinology · doi:10.1210/en.2019-00029 · Cited by 34
Jackisch, L., Murphy, A. M., Kumar, S., Randeva, H. S., Tripathi, G., & McTernan, P. G. (2020) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaa258 · Cited by 36
Calcineurin in the heart: New horizons for an old friend
Chaklader, M., & Rothermel, B. A. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110134 · Cited by 34
Mofatteh, M., Iturra, F. E., Alamban, A., Ricca, F. D., Bakshi, A., & Aydogan, M. G. (2021) · eLife · doi:10.7554/elife.72104 · Cited by 32
Mitochondrial fission and bioenergetics mediate human lung fibroblast durotaxis
Guo, T., Jiang, C., Yang, S., Zhu, Y., He, C., Carter, A. B., Antony, V. B., Peng, H., & Zhou, Y. (2022) · JCI Insight · doi:10.1172/jci.insight.157348 · Cited by 35
Fluid Mechanical Forces and Endothelial Mitochondria: A Bioengineering Perspective
Scheitlin, C. G., Nair, D. M., Crestanello, J. A., Zweier, J. L., & Alevriadou, B. R. (2014) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-014-0357-4 · Cited by 34
Giacomo, G. D., Rizza, S., Montagna, C., & Filomeni, G. (2012) · International Journal of Cell Biology · doi:10.1155/2012/361872 · Cited by 33
Alzheimer disease as a vascular disorder: Where do mitochondria fit?
Correia, S. C., Santos, R. X., Cardoso, S., Carvalho, C., Candeias, E., Duarte, A. I., Plácido, A. I., Santos, M. S., & Moreira, P. I. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.07.006 · Cited by 32
(Neuro)degenerated Mitochondria-ER contacts
Mario, A. D., Quintana–Cabrera, R., Martinvalet, D., & Giacomello, M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.056 · Cited by 35
Intracellular calcium is a rheostat for the STING signaling pathway
Kwon, D., Sesaki, H., & Kang, S. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.117 · Cited by 32
Suresh, K. S., Servinsky, L. E., Jiang, H., Bigham, Z., Zaldumbide, J., Huetsch, J., Kliment, C. R., Acoba, M. G., Kirsch, B. J., Claypool, S. M., et al. (2019) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00396.2018 · Cited by 32
Yu, M., Yang, J., Gao, X., Sun, W., Liu, S., Han, Y., Lu, X., Jin, C., Wu, S., & Cai, Y. (2020) · Metallomics · doi:10.1039/c9mt00291j · Cited by 32
Melatonin Treatment Improves Renal Fibrosis via miR-4516/SIAH3/PINK1 Axis
Yoon, Y. M., Go, G., Yoon, S., Lim, J. H., Lee, G., Lee, J. H., & Lee, S. H. (2021) · Cells · doi:10.3390/cells10071682 · Cited by 33
Sirtuin 5 depletion impairs mitochondrial function in human proximal tubular epithelial cells
Haschler, T. N., Horsley, H., Bałys, M., Anderson, G. W., Taanman, J., Unwin, R. J., & Norman, J. T. (2021) · Scientific Reports · doi:10.1038/s41598-021-94185-6 · Cited by 33
Corrado, M., Mariotti, F. R., Trapani, L., Taraborrelli, L., Nazio, F., Cianfanelli, V., Soriano, M. E., Schrepfer, E., Cecconi, F., Scorrano, L., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593727 · Cited by 31
Self-citationDubois, M., Boulghobra, D., Rochebloine, G., Pallot, F., Yehya, M., Bornard, I., Gayrard, S., Coste, F., Walther, G., Meyer, G., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103044 · Cited by 33
Tak, H., Eun, J. W., Kim, J., Park, S. J., Kim, C., Ji, E., Lee, H., Kang, H., Cho, D., Lee, K., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.90 · Cited by 31
Song, Y., Li, T., Liu, Z., Xu, Z., Zhang, Z., Chi, L., & Liu, Y. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.03.013 · Cited by 32
Ahmed, M. E., Selvakumar, G. P., Kempuraj, D., Thangavel, R., Mentor, S., Dubova, I., Raikwar, S. P., Zaheer, S. A., Iyer, S. S., & Zaheer, A. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1544-z · Cited by 36
Dynamic Control of Mitochondrial Ca2+ Levels as a Survival Strategy of Cancer Cells
Madreiter‐Sokolowski, C. T., Gottschalk, B., Sokolowski, A., Malli, R., & Graier, W. F. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.614668 · Cited by 30
Compartmentalized Signaling in Aging and Neurodegeneration
Benedetto, G. D., Iannucci, L. F., Surdo, N. C., Zanin, S., Conca, F., Grisan, F., Gerbino, A., & Lefkimmiatis, K. (2021) · Cells · doi:10.3390/cells10020464 · Cited by 30
Yuan, Y., Chen, J., Ge, X., Deng, J., Xu, X., Zhao, Y., & Wang, H. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13273 · Cited by 32
Dysfunctional Mitochondrial Dynamics in the Pathophysiology of Neurodegenerative Diseases
Haun, F., Nakamura, T., & Lipton, S. A. (2013) · Journal of Cell Death · doi:10.4137/jcd.s10847 · Cited by 34
The role of circadian clock-controlled mitochondrial dynamics in diabetic cardiomyopathy
Jin, Z., Ji, Y., Su, W., Zhou, L., Wu, X., Gao, L., Guo, J., Liu, Y., Zhang, Y., Wen, X., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1142512 · Cited by 34
New therapeutic directions in type II diabetes and its complications: mitochondrial dynamics
Wang, S., Zhao, H., Lin, S., Lv, Y., Lin, Y. N., Liu, Y., Peng, R., & Jin, H. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1230168 · Cited by 33
SAMM 50 Affects Mitochondrial Morphology through the Association of Drp1 in Mammalian Cells
Liu, S., Gao, Y., Zhang, C., Li, H., Pan, S., Wang, X., Du, S., Deng, Z., Wang, L., Song, Z., et al. (2016) · FEBS Letters · doi:10.1002/1873-3468.12170 · Cited by 29
Cooper, H. A., & Eguchi, S. (2018) · Clinical Science · doi:10.1042/cs20180671 · Cited by 30
RetractedSong, S. B., Park, J., Jang, S. Y., & Hwang, E. S. (2021) · Cells · doi:10.3390/cells10030612 · Cited by 31
Barbosa, D. J., Serrat, R., Mirra, S., Quevedo, M., de Barreda, E. G., Ávila, J., Ferreira, L. M., Branco, P. S., Fernandes, E. G. R., Bastos, M. D. L., et al. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu042 · Cited by 31
Banerjee, K., Munshi, S., Xu, H., Frank, D. E., Chen, H., Chu, C. T., Yang, J., Cho, S., Kagan, V. E., Denton, T. T., et al. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.02.011 · Cited by 30
The ER-mitochondria couple: In life and death from steroidogenesis to tumorigenesis
Doghman, M., & Lalli, E. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.08.050 · Cited by 35
Wang, H., Zheng, S., Liu, M., Jia, C., Wang, S., Wang, X., Xue, S., & Guo, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165052 · Cited by 30
The mechanisms and roles of mitochondrial dynamics in C. elegans
Campbell, D., & Zuryn, S. (2023) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2023.10.006 · Cited by 28
Tang, Y., Liu, X., Zhao, J., Tan, X., Liu, B., Zhang, G., Sun, L., Han, D., Chen, H., & Wang, M. (2016) · Brain Research · doi:10.1016/j.brainres.2016.05.042 · Cited by 28
Tumour microenvironment on mitochondrial dynamics and chemoresistance in cancer
Han, Y., Cho, U., Kim, S., Park, I. S., Cho, J., Dhanasekaran, D. N., & Song, Y. S. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1459594 · Cited by 28
JNK1 and ERK1/2 modulate lymphocyte homeostasis via BIM and DRP1 upon AICD induction
Simula, L., Corrado, M., Accordi, B., Rita, A. D., Nazio, F., Antonucci, Y., Daniele, A. D., Caicci, F., Caruana, I., Soriano, M. E., et al. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0540-1 · Cited by 29
Cid‐Castro, C., & Morán, J. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8832863 · Cited by 29
Chaanine, A. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910579 · Cited by 31
Mitochondrial phosphoproteomes are functionally specialized across tissues
Hansen, F. M., Kremer, L. S., Karayel, O., Bludau, I., Larsson, N.-G., Kühl, I., & Mann, M. (2024) · Life Science Alliance · doi:10.26508/lsa.202302147 · Cited by 29
Mitochondrial fission augments capsaicin-induced axonal degeneration
Chiang, H., Ohno, N., Hsieh, Y.-L., Mahad, D., Kikuchi, S., Komuro, H., Hsieh, S., & Trapp, B. D. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1354-3 · Cited by 28
Mitochondrial dynamic changes in health and genetic diseases
Chen, L., Winger, A. J., & Knowlton, A. A. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3663-y · Cited by 31
Lee, D. G., Min, J., Lee, H., & Lee, D. (2018) · NeuroToxicology · doi:10.1016/j.neuro.2018.07.011 · Cited by 29
Zhang, L., Xie, X., Tao, J., Wang, S., Hu, M., Wang, X., Yu, Z., Xu, L., Lin, Y., Wu, W., et al. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.166831 · Cited by 28
Mitochondrial Dynamics: In Cell Reprogramming as It Is in Cancer
Prieto, J., & Torres, J. (2017) · Stem Cells International · doi:10.1155/2017/8073721 · Cited by 26
Zhao, Q., Lu, D., Wang, J., Liu, B., Cheng, H., Mattson, M. P., & Cheng, A. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0230-4 · Cited by 30
Darwesh, A. M., Keshavarz-Bahaghighat, H., Jamieson, K. L., & Seubert, J. M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143502 · Cited by 27
BDE-47 induces nephrotoxicity through ROS-dependent pathways of mitochondrial dynamics in PK15 cells
Sun, S., Zhao, Z., Rao, Q., Li, X., Ruan, Z., & Yang, J. (2021) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2021.112549 · Cited by 28
Monroy-Ramírez, H. C., Basurto‐Islas, G., Mena, R., Cisneros, B., Binder, L. I., Ávila, J., & García‐Sierra, F. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122401 · Cited by 32
Piilgaard, H., Witgen, B. M., Rasmussen, P. V., & Lauritzen, M. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2011.28 · Cited by 28
Histone deacetylase inhibitors induce mitochondrial elongation
Lee, J. S., Yoon, Y. G., Yoo, S. H., Jeong, N. Y., Jeong, S. H., Lee, S. Y., Jung, D., Jeong, S., & Yoo, Y. H. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.23027 · Cited by 29
Mitochondrial Dynamics in the Heart as a Novel Therapeutic Target for Cardioprotection
Hwang, S. J., & Kim, W. (2013) · Chonnam Medical Journal · doi:10.4068/cmj.2013.49.3.101 · Cited by 29
Ca2+–Sensor Proteins in the Autophagic and Endocytic Traffic
Ghislat, G., & Knecht, E. (2013) · Current Protein and Peptide Science · doi:10.2174/13892037112139990033 · Cited by 28
Malena, A., Pantic, B., Borgia, D., Sgarbi, G., Solaini, G., Holt, I. J., Spinazzola, A., Perissinotto, E., Sandri, M., Baracca, A., et al. (2016) · Autophagy · doi:10.1080/15548627.2016.1226734 · Cited by 31
Mukherjee, A., Patra, U., Bhowmick, R., & Chawla‐Sarkar, M. (2018) · Cellular Microbiology · doi:10.1111/cmi.12831 · Cited by 29
Dynamin‐like protein 1 cleavage by calpain in Alzheimer’s disease
Jiang, S., Shao, C., Tang, F., Wang, W., & Zhu, X. (2019) · Aging Cell · doi:10.1111/acel.12912 · Cited by 27
Cheng, W., Yang, S., Li, X., Liang, F., Zhou, R., Wang, H., Feng, Y., & Wang, Y. (2019) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2019.114850 · Cited by 29
Liu, X., Guo, C., & Zhang, Q. (2023) · Cell Stress and Chaperones · doi:10.1007/s12192-023-01321-4 · Cited by 27
Ren, C., Hu, C., Hu, M., Wu, Y., Yang, Y., & Lu, F. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.156088 · Cited by 27
A novel role for kynurenine 3-monooxygenase in mitochondrial dynamics
Maddison, D. C., Alfonso-Núñez, M., Swaih, A. M., Breda, C., Campesan, S., Allcock, N., Straatman-Iwanowska, A. A., Kyriacou, C. P., & Giorgini, F. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009129 · Cited by 30
Bonekamp, N. A., Vormund, K., Jacob, R., & Schrader, M. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.07.020 · Cited by 27
Subcellular Distribution of HDAC1 in Neurotoxic Conditions Is Dependent on Serine Phosphorylation
Zhu, Y., Vidaurre, Ó. G., Adula, K. P., Kezunovic, N., Wentling, M., Huntley, G. W., & Casaccia, P. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3000-16.2017 · Cited by 28
Chae, U., Min, J., Lee, H., Song, K., Lee, H., Lee, H. J., Lee, S., & Lee, D. (2017) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2017.1344988 · Cited by 28
Propofol-Induced Developmental Neurotoxicity: From Mechanisms to Therapeutic Strategies
Zhang, J., & Li, Y. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00755 · Cited by 30
Liu, J. S., Bao, X., Huang, J., Chen, R., Tan, Y., Zhang, Z., Xiao, B., Kong, F., Gu, C., Du, J., et al. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155767 · Cited by 27
Okada, M., Morioka, S., Kanazawa, H., & Yamawaki, H. (2016) · APOPTOSIS · doi:10.1007/s10495-016-1262-1 · Cited by 26
Mui, D., & Zhang, Y. (2020) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2020.1784938 · Cited by 27
Zhao, J., Dong, L., Huo, T., Cheng, J., Li, X., Huangfu, X., Sun, S., Wang, H., & Li, L. (2021) · NeuroMolecular Medicine · doi:10.1007/s12017-021-08688-6 · Cited by 26
Decoding the Phosphatase Code: Regulation of Cell Proliferation by Calcineurin
Masaki, T., & Shimada, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031122 · Cited by 26
Impact of Drp1-Mediated Mitochondrial Dynamics on T Cell Immune Modulation
Song, J., Yi, X., Gao, R.-L., Sun, L., Wu, Z., Zhang, S., Huang, L., Han, C., & Ma, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.873834 · Cited by 29
Mitochondrial chaperone DnaJA3 induces Drp1-dependent mitochondrial fragmentation
Elwi, A. N., Lee, B., Meijndert, H. C., Braun, J. E. A., & Kim, S.-W. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.05.004 · Cited by 31
Shu, S., Cui, H., Liu, Z., Zhang, H., Yang, Y., Chen, X., Zeng, Z., Du, L., Fu, M., Yang, Z., et al. (2024) · Metabolism · doi:10.1016/j.metabol.2024.155977 · Cited by 26
Wang, W., Yang, X., Chen, Y., Ye, X., Jiang, K., Xiong, A., Yang, L., & Wang, Z. (2020) · Journal of Applied Toxicology · doi:10.1002/jat.4004 · Cited by 25
Low‐glucose‐sensitive TRPC6 dysfunction drives hypoglycemia‐induced cognitive impairment in diabetes
He, C., Gao, P., Cui, Y., Li, Q., Li, Y., Lu, Z., Ma, H., Zhao, Y., Li, L., Sun, F., et al. (2020) · Clinical and Translational Medicine · doi:10.1002/ctm2.205 · Cited by 25
Yang, D., Rong, R., Yang, R., You, M., Wang, M., Li, H., & Ji, D. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.04.082 · Cited by 23
Semenzato, M., Kohr, M. J., Quirin, C., Menabò, R., Alánová, P., Alán, L., Pellattiero, A., Murphy, E., Lisa, F. D., & Scorrano, L. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102755 · Cited by 24
Self-citationCharacterization of TNF-induced caspase-independent necroptosis
Sawai, H. (2014) · Leukemia Research · doi:10.1016/j.leukres.2014.02.002 · Cited by 25
Sakamoto, A., Saotome, M., Hasan, P., Satoh, T., Ohtani, H., Urushida, T., Katoh, H., Satoh, H., & Hayashi, H. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.01.004 · Cited by 25
Morphological Pathways of Mitochondrial Division
Tandler, B., Hoppel, C. L., & Mears, J. A. (2018) · Antioxidants · doi:10.3390/antiox7020030 · Cited by 26
Swine Influenza Virus Induces RIPK1/DRP1-Mediated Interleukin-1 Beta Production
Park, H.-S., Liu, G., Liu, Q., & Zhou, Y. (2018) · Viruses · doi:10.3390/v10080419 · Cited by 24
Kaushal, J., Popli, P., Sankhwar, P., Shukla, V., & Dwivedi, A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.427 · Cited by 25
Kim, M. H., Lee, H. J., Lee, S., Lee, H., Huh, J., Bae, Y. C., & Lee, D. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00148-19 · Cited by 25
Zuo, W., Yan, F., Liu, Z., & Zhang, B. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173143 · Cited by 24
SAM50, a side door to the mitochondria: The case of cytotoxic proteases
Lionello, S., Marzaro, G., & Martinvalet, D. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105196 · Cited by 24
Marchesan, E., Nardin, A., Mauri, S., Bernardo, G., Chander, V., Paola, S. D., Chinellato, M., von Stockum, S., Chakraborty, J., Herkenne, S., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-023-01251-9 · Cited by 29
Self-citationHoly, J. M., Kolomitsyna, O., Krasutsky, D., Oliveira, P. J., Perkins, E. L., & Krasutsky, P. A. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.06.075 · Cited by 24
Enhancement of mitochondrial ATP production by the Escherichia coli cytotoxic necrotizing factor 1
Travaglione, S., Loizzo, S., Rizza, T., Brocco, A. D., Ballan, G., Guidotti, M., Vona, R., Nottia, M. D., Torraco, A., Carrozzo, R., et al. (2014) · FEBS Journal · doi:10.1111/febs.12874 · Cited by 25
CaMKIV regulates mitochondrial dynamics during sepsis
Zhang, X., Griepentrog, J. E., Zou, B., Xu, L., Cyr, A. R., Chambers, L., Zuckerbraun, B. S., Shiva, S., & Rosengart, M. R. (2020) · Cell Calcium · doi:10.1016/j.ceca.2020.102286 · Cited by 23
Tan, Y., Xia, F., Li, L., Peng, X., Liu, W., Zhang, Y., Fang, H., Zeng, Z., & Chen, Z. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6669075 · Cited by 23
RetractedRole of Mitochondrial Dynamics in Cocaine’s Neurotoxicity
Wen, S., Aki, T., Funakoshi, T., Unuma, K., & Uemura, K. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105418 · Cited by 25
Fajardo, G., Coronado, M. J., Matthews, M. D., & Bernstein, D. (2022) · Biomedicines · doi:10.3390/biomedicines10061375 · Cited by 23
MDMA impairs mitochondrial neuronal trafficking in a Tau- and Mitofusin2/Drp1-dependent manner
Barbosa, D. J., Serrat, R., Mirra, S., Quevedo, M., de Barreda, E. G., Ávila, J., Fernandes, E. G. R., Bastos, M. D. L., Capela, J. P., Carvalho, F. D., et al. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1209-7 · Cited by 24
Relationship Between β-Amyloid and Mitochondrial Dynamics
Kim, D. I., Lee, K. H., Oh, J. Y., Kim, J. S., & Han, H. J. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0434-4 · Cited by 23
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
