Tau Promotes Neurodegeneration via DRP1 Mislocalization In Vivo
Open accessAbstract
Mitochondrial abnormalities have been documented in Alzheimer's disease and related neurodegenerative disorders, but the causal relationship between mitochondrial changes and neurodegeneration, and the specific mechanisms promoting mitochondrial dysfunction, are unclear. Here, we find that expression of human tau results in elongation of mitochondria in both Drosophila and mouse neurons. Elongation is accompanied by mitochondrial dysfunction and cell cycle-mediated cell death, which can be rescued in vivo by genetically restoring the proper balance of mitochondrial fission and fusion. We have previously demonstrated that stabilization of actin by tau is critical for neurotoxicity of the protein. Here, we demonstrate a conserved role for actin and myosin in regulating mitochondrial fission and show that excess actin stabilization inhibits association of the fission protein DRP1 with mitochondria, leading to mitochondrial elongation and subsequent neurotoxicity. Our results thus identify actin-mediated disruption of mitochondrial dynamics as a direct mechanism of tau toxicity in neurons in vivo.
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Pathologic tau causes an increase in actin stabilization that inhibits association of the fission protein Drp1 with mitochondria, leading to mitochondrial elongation and production of reactive oxygen species.
“Pathologic tau causes an increase in actin stabilization18 that inhibits association of the fission protein Drp1 with mitochondria, leading to mitochondrial elongation and the production of reactive oxygen species44.”
From Tau promotes neurodegeneration through global chromatin relaxation (2014) · cites this paper as [44]
No statistical methods were used to predetermine sample sizes but our sample sizes are similar to those reported in previous publications.
“No statistical methods were used to predetermine sample sizes but our sample sizes are similar to those reported in previous publications 7,16,44.”
From Tau promotes neurodegeneration through global chromatin relaxation (2014) · cites this paper as [44]
The Experimental Procedures (Immunoblotting; page unavailable) say immunoblots were repeated at least three times, but give no basis for comparing this paper’s sample sizes with those of the citing study. Searches for sample-size planning, sample counts, and comparisons with previous publications found no passage addressing that comparison. The statement about not predetermining sample sizes describes the citing authors’ own methods, not a claim this source can establish. (LLM, conf=0.70)
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510 · see citing works
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498 · see citing works
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · see citing works
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082 · see citing works
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Lee, T., & Luo, L. (1999) · Neuron · doi:10.1016/s0896-6273(00)80701-1 · Cited by 2,540 · see citing works
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works
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 · see citing works
Prevalence of Dementia in the United States: The Aging, Demographics, and Memory Study
Plassman, B. L., Langa, K. M., Fisher, G. G., Heeringa, S. G., Weir, D. R., Ofstedal, M. B., Burke, J. R., Hurd, M. D., Potter, G. G., Rodgers, W. L., et al. (2007) · Neuroepidemiology · doi:10.1159/000109998 · Cited by 1,932 · see citing works
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755 · see citing works
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572 · see citing works
Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474 · see citing works
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446 · see citing works
Tau is a candidate gene for chromosome 17 frontotemporal dementia
Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374 · see citing works
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367 · see citing works
Amyloid-β and tau — a toxic pas de deux in Alzheimer's disease
Ittner, L. M., & Götz, J. (2010) · Nature reviews. Neuroscience · doi:10.1038/nrn2967 · Cited by 1,357 · see citing works
Self-citationAlexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330 · see citing works
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300 · see citing works
Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria
Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129 · see citing works
S-Nitrosylation of Drp1 Mediates β-Amyloid-Related Mitochondrial Fission and Neuronal Injury
Cho, D.-H., Nakamura, T., Fang, J., Cieplak, P., Godzik, A., Gu, Z., & Lipton, S. A. (2009) · Science · doi:10.1126/science.1171091 · Cited by 1,092 · see citing works
Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012 · see citing works
Tauopathy in <i>Drosophila</i> : Neurodegeneration Without Neurofibrillary Tangles
Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939 · see citing works
Self-citationVerstreken, P., Ly, C. V., Venken, K. J. T., Koh, T.-W., Zhou, Y., & Bellen, H. J. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.018 · Cited by 841 · see citing works
Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., Mandelkow, E.-M., & Mandelkow, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.3.777 · Cited by 820 · see citing works
Spradling, A. C., Stern, D., Beaton, A., Rehm, E. J., Laverty, T., Mozden, N., Misra, S., & Rubin, G. M. (1999) · Genetics · doi:10.1093/genetics/153.1.135 · Cited by 780 · see citing works
Yin, H. L., & Stossel, T. P. (1979) · Nature · doi:10.1038/281583a0 · Cited by 779 · see citing works
Systematic generation of high-resolution deletion coverage of the Drosophila melanogaster genome
Parks, A. L., Cook, K. R., Belvin, M. P., Dompe, N., Fawcett, R., Huppert, K. A., Tan, L. R., Winter, C. G., Bogart, K. P., Deal, J. E., et al. (2004) · Nature Genetics · doi:10.1038/ng1312 · Cited by 755 · see citing works
A Lethal Defect of Mitochondrial and Peroxisomal Fission
Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa064436 · Cited by 749 · see citing works
Noble, W., Planel, E., Zehr, C., Olm, V., Meyerson, J., Suleman, F., Gaynor, K., Wang, L., LaFrancois, J., Feinstein, B., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500466102 · Cited by 709 · see citing works
Ramsden, M., Kotilinek, L., Forster, C., Paulson, J., McGowan, E., SantaCruz, K., Guimaraes, A., Yue, M., Lewis, J., Carlson, G., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.3279-05.2005 · Cited by 702 · see citing works
Glater, E. E., Megeath, L. J., Stowers, R. S., & Schwarz, T. L. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601067 · Cited by 667 · see citing works
Rhein, V., Song, X., Wiesner, A., Ittner, L. M., Baysang, G., Meier, F., Ozmen, L., Bluethmann, H., Dröse, S., Brandt, U., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905529106 · Cited by 655 · see citing works
Self-citationEctopic Cell Cycle Proteins Predict the Sites of Neuronal Cell Death in Alzheimer’s Disease Brain
Busser, J., Geldmacher, D. S., & Herrup, K. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-08-02801.1998 · Cited by 543 · see citing works
Hutchinson, E. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn2985 · Cited by 534 · see citing works
Jackson, G. R., Wiedau-Pazos, M., Sang, T.-K., Wagle, N., Brown, C. A., Massachi, S., & Geschwind, D. H. (2002) · Neuron · doi:10.1016/s0896-6273(02)00706-7 · Cited by 488 · see citing works
Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
Fulga, T. A., Elson-Schwab, I., Khurana, V., Steinhilb, M. L., Spires, T. L., Hyman, B. T., & Feany, M. B. (2007) · Nature Cell Biology · doi:10.1038/ncb1528 · Cited by 452 · see citing works
Self-citationProteomic and functional analyses reveal a mitochondrial dysfunction in P301L tau transgenic mice
David, D. C., Hauptmann, S., Scherping, I., Schuessel, K., Keil, U., Rizzu, P., Ravid, R., Dröse, S., Brandt, U., Müller, W. E., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500356200 · Cited by 447 · see citing works
Self-citationParone, P. A., Da Cruz, S., Tondera, D., Mattenberger, Y., James, D. I., Maechler, P., Barja, F., & Martinou, J.-C. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003257 · Cited by 415 · see citing works
Mitochondrial Function and Actin Regulate Dynamin-Related Protein 1-Dependent Mitochondrial Fission
Vos, K. J. D., Allan, V., Grierson, A. J., & Sheetz, M. P. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.064 · Cited by 345 · see citing works
Wang, X., Su, B., Fujioka, H., & Zhu, X. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.071208 · Cited by 341 · see citing works
Ahlijanian, M. K., Barrezueta, N. X., Williams, R. D., Jakowski, A. B., Kowsz, K. P., McCarthy, S. A., Coskran, T., Carlo, A. A., Seymour, P. A., Burkhardt, J. E., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040577797 · Cited by 339 · see citing works
Nishimura, I., Yang, Y., & Lu, B. (2004) · Cell · doi:10.1016/s0092-8674(04)00170-9 · Cited by 324 · see citing works
Oxidative stress mediates tau-induced neurodegeneration in Drosophila
Dias-Santagata, D., Fulga, T. A., Duttaroy, A., & Feany, M. B. (2007) · Journal of Clinical Investigation · doi:10.1172/jci28769 · Cited by 318 · see citing works
Self-citationNerve Growth Factor Signaling Regulates Motility and Docking of Axonal Mitochondria
Chada, S. R., & Hollenbeck, P. J. (2004) · Current Biology · doi:10.1016/j.cub.2004.07.027 · Cited by 296 · see citing works
Kopeikina, K. J., Carlson, G. A., Pitstick, R., Ludvigson, A. E., Peters, A., Luebke, J. I., Koffie, R. M., Frosch, M. P., Hyman, B. T., & Spires‐Jones, T. L. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.07.004 · Cited by 272 · see citing works
Mitochondrial energy metabolism and ageing
Bratic, I., & Trifunović, A. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.004 · Cited by 268 · see citing works
TOR-Mediated Cell-Cycle Activation Causes Neurodegeneration in a Drosophila Tauopathy Model
Khurana, V., Lu, Y., Steinhilb, M. L., Oldham, S., Shulman, J. M., & Feany, M. B. (2006) · Current Biology · doi:10.1016/j.cub.2005.12.042 · Cited by 266 · see citing works
Self-citationMolecular mechanisms and physiologic functions of mitochondrial dynamics
Otera, H., & Mihara, K. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr002 · Cited by 251 · see citing works
Perry, E. K., Perry, R. H., Tomlinson, B. E., Blessed, G., & Gibson, P. H. (1980) · Neuroscience Letters · doi:10.1016/0304-3940(80)90220-7 · Cited by 236 · see citing works
Myosin Light Chain–activating Phosphorylation Sites Are Required for Oogenesis in Drosophila
Jordan, P., & Karess, R. E. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.7.1805 · Cited by 225 · see citing works
Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia
Ittner, L. M., Fath, T., Ke, Y. D., Bi, M., van Eersel, J., Li, K. M., Gunning, P. W., & Götz, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808084105 · Cited by 219 · see citing works
Self-citationLinking molecular motors to membrane cargo
Akhmanova, A. S., & Hammer, J. A. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.008 · Cited by 218 · see citing works
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 209 · see citing works
Human Myo19 Is a Novel Myosin that Associates with Mitochondria
Quintero, O. A., DiVito, M. M., Adikes, R. C., Kortan, M. B., Case, L. B., Lier, A., Panaretos, N. S., Slater, S. Q., Rengarajan, M., Feliu, M., et al. (2009) · Current Biology · doi:10.1016/j.cub.2009.10.026 · Cited by 204 · see citing works
Tau Phosphorylation Sites Work in Concert to Promote Neurotoxicity In Vivo
Steinhilb, M. L., Dias-Santagata, D., Fulga, T. A., Felch, D. L., & Feany, M. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0327 · Cited by 187 · see citing works
Self-citationShapland, C., Hsuan, J. J., Totty, N. F., & Lawson, D. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.5.1065 · Cited by 171 · see citing works
Watanabe, T., Hosoya, H., & Yonemura, S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-07-0590 · Cited by 164 · see citing works
Ittner, L. M., Ke, Y. D., & Götz, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014472 · Cited by 156 · see citing works
Self-citationLysosomal Dysfunction Promotes Cleavage and Neurotoxicity of Tau In Vivo
Khurana, V., Elson‐Schwab, I., Fulga, T. A., Sharp, K. A., Loewen, C. A., Mulkearns-Hubert, E. E., Tyynelä, J., Scherzer, C. R., & Feany, M. Β. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001026 · Cited by 148 · see citing works
Self-citationPrevalence of Dementia in the United States
Plassman, B. L., Langa, K. M., Fisher, G. G., Heeringa, S. G., Weir, D. R., Ofstedal, M. B., Burke, J. R., Hurd, M. D., Potter, G. G., Rodgers, W. L., et al. (2007) · Cited by 139 · see citing works
Eckert, A., Hauptmann, S., Scherping, I., Meinhardt, J., Rhein, V. F., Dröse, S., Brandt, U., Fändrich, M., Müller, W. E., & Götz, J. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0391-6 · Cited by 129 · see citing works
Self-citationActin and myosin contribute to mammalian mitochondrial DNA maintenance
Reyes, A., He, J., Mao, C., Bailey, L., Re, M. D., Sembongi, H., Kazak, L., Dzionek, K., Holmes, J. B., Cluett, T. J., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr052 · Cited by 107 · see citing works
S/P and T/P phosphorylation is critical for tau neurotoxicity in <i>Drosophila</i>
Steinhilb, M. L., Dias‐Santagata, D., Mulkearns, E. E., Shulman, J. M., Biernat, J., Mandelkow, E., & Feany, M. B. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21232 · Cited by 107 · see citing works
Self-citationChang, K. T., & Min, K. (2005) · Nature Neuroscience · doi:10.1038/nn1564 · Cited by 96 · see citing works
WASP and SCAR have distinct roles in activating the Arp2/3 complex during myoblast fusion
Berger, S., Schäfer, G., Kesper, D. A., Holz, A., Eriksson, T., Palmer, R. H., Beck, L. A., Klämbt, C., Renkawitz‐Pohl, R., & Önel, S. (2008) · Journal of Cell Science · doi:10.1242/jcs.022269 · Cited by 92 · see citing works
Differential expression of the Drosophila mitofusin genes fuzzy onions (fzo) and dmfn
Hwa, J. J., Hiller, M. A., Fuller, M. T., & Santel, A. (2002) · Mechanisms of Development · doi:10.1016/s0925-4773(02)00141-7 · Cited by 89 · see citing works
The Unfolded Protein Response Protects from Tau Neurotoxicity In Vivo
Loewen, C. A., & Feany, M. Β. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013084 · Cited by 88 · see citing works
Self-citationCyclic AMP-dependent Protein Kinase Regulates the Alternative Splicing of Tau Exon 10
Shi, J., Qian, W., Yin, X., Iqbal, K., Grundke, I., Gu, X., Ding, F., Gong, C., & Liu, F. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.204453 · Cited by 87 · see citing works
Actin Dynamics Is Essential for Myosin-Based Transport of Membrane Organelles
Semenova, I., Burakov, A. V., Berardone, N., Zaliapin, I., Slepchenko, B. M., Svitkina, T., Kashina, A. S., & Rodionov, V. (2008) · Current Biology · doi:10.1016/j.cub.2008.08.070 · Cited by 72 · see citing works
Iijima-Ando, K., Zhao, L., Gatt, A., Shenton, C., & Iijima, K. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq068 · Cited by 72 · see citing works
Cook, C. N., Hejna, M. J., Magnuson, D. J., & Lee, J. M. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-8108 · Cited by 65 · see citing works
A neuroprotective role for the DNA damage checkpoint in tauopathy
Khurana, V., Merlo, P., DuBoff, B., Fulga, T. A., Sharp, K. A., Campbell, S. D., Götz, J., & Feany, M. Β. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00778.x · Cited by 57 · see citing works
Self-citationZhao, D. B., Côté, S., Jähnig, F., Haller, J., & Jäckle, H. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02920.x · Cited by 29 · see citing works
Grieshaber, S. S., Lankenau, D., Talbot, T., Holland, S., & Petersen, N. S. (2001) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.10007 · Cited by 9 · see citing works
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Wang, X., Wang, W., Li, L., Perry, G., Lee, H.-G., & Zhu, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.015 · Cited by 1,357 · see citing works
Mitochondria in oxidative stress, inflammation and aging: from mechanisms to therapeutic advances
Xu, X., Pang, Y., & Fan, X. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02253-4 · Cited by 939 · see citing works
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Kametani, F., & Hasegawa, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00025 · Cited by 836 · see citing works
An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817 · see citing works
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 · see citing works
Mitochondria at the neuronal presynapse in health and disease
Devine, M. J., & Kittler, J. T. (2018) · Nature reviews. Neuroscience · doi:10.1038/nrn.2017.170 · Cited by 615 · see citing works
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works
Asymmetric apportioning of aged mitochondria between daughter cells is required for stemness
Katajisto, P., Döhla, J., Chaffer, C. L., Pentinmikko, N., Marjanovic, N. D., Iqbal, S., Zoncu, R., Chen, W. W., Weinberg, R. A., & Sabatini, D. M. (2015) · Science · doi:10.1126/science.1260384 · Cited by 542 · see citing works
Tau promotes neurodegeneration through global chromatin relaxation
Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 519 · see citing works
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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 476 · see citing works
The role of mitochondrial dysfunction in Alzheimer's disease pathogenesis
Ashleigh, T., Swerdlow, R. H., & Beal, M. F. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12683 · Cited by 491 · see citing works
The importance of tau phosphorylation for neurodegenerative diseases
Noble, W., Hanger, D. P., Miller, C. C. J., & Lovestone, S. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00083 · Cited by 475 · see citing works
Drp1-dependent mitochondrial fission in cardiovascular disease
Jin, J., Wei, X., Zhi, X., Wang, X., & Meng, D. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-00518-y · Cited by 386 · see citing works
Chakrabarti, R., Ji, W.-K., Stan, R. V., de Juan Sanz, J., Ryan, T. A., & Higgs, H. N. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709111 · Cited by 349 · see citing works
Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration
Tracy, T. E., Madero‐Pérez, J., Swaney, D. L., Chang, T. S., Moritz, M., Konràd, C., Ward, M. E., Stevenson, E. J., Hüttenhain, R., Kauwe, G., et al. (2022) · Cell · doi:10.1016/j.cell.2021.12.041 · Cited by 347 · see citing works
Manor, U., Bartholomew, S. R., Golani, G., Christenson, E. T., Kozlov, M. M., Higgs, H. N., Spudich, J. A., & Lippincott‐Schwartz, J. (2015) · eLife · doi:10.7554/elife.08828 · Cited by 341 · see citing works
Ji, W.-K., Hatch, A. L., Merrill, R. A., Strack, S., & Higgs, H. N. (2015) · eLife · doi:10.7554/elife.11553 · Cited by 328 · see citing works
Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage
Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314 · see citing works
Rana, A., Oliveira, M. P., Khamoui, A. V., Aparicio, R., Rera, M., Rossiter, H. B., & Walker, D. W. (2017) · Nature Communications · doi:10.1038/s41467-017-00525-4 · Cited by 294 · see citing works
Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works
Mitochondrial Aspects of Synaptic Dysfunction in Alzheimer’s Disease
Cai, Q., & Tammineni, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160726 · Cited by 274 · see citing works
Tau-based therapies in neurodegeneration: opportunities and challenges
Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272 · see citing works
Self-citationDisease-associated tau impairs mitophagy by inhibiting Parkin translocation to mitochondria
Cummins, N., Tweedie, A., Zuryn, S., Bertran‐Gonzalez, J., & Götz, J. (2019) · The EMBO Journal · doi:10.15252/embj.201899360 · Cited by 267 · see citing works
Self-citationMitochondria as Potential Targets in Alzheimer Disease Therapy: An Update
Cenini, G., & Voos, W. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00902 · Cited by 257 · see citing works
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 254 · see citing works
A Role for Myosin II in Mammalian Mitochondrial Fission
Korobova, F. V., Gauvin, T. J., & Higgs, H. N. (2014) · Current Biology · doi:10.1016/j.cub.2013.12.032 · Cited by 244 · see citing works
Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases
Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250 · see citing works
Mitochondrial dynamics during cell cycling
Horbay, R., & Bilyy, R. O. (2016) · APOPTOSIS · doi:10.1007/s10495-016-1295-5 · Cited by 246 · see citing works
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 · see citing works
A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies
Orr, M. E., Sullivan, A. C., & Frost, B. E. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.011 · Cited by 232 · see citing works
Neuronal cell death mechanisms in Alzheimer’s disease: An insight
Goel, P., Chakrabarti, S., Goel, K., Bhutani, K., Chopra, T., & Bali, S. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.937133 · Cited by 235 · see citing works
α-synuclein Induces Mitochondrial Dysfunction through Spectrin and the Actin Cytoskeleton
Ordonez, D. G., Lee, M. K., & Feany, M. B. (2018) · Neuron · doi:10.1016/j.neuron.2017.11.036 · Cited by 227 · see citing works
Self-citationLamin Dysfunction Mediates Neurodegeneration in Tauopathies
Frost, B., Bardai, F. H., & Feany, M. B. (2016) · Current Biology · doi:10.1016/j.cub.2015.11.039 · Cited by 226 · see citing works
Self-citationOxidant/Antioxidant Imbalance in Alzheimer’s Disease: Therapeutic and Diagnostic Prospects
Wojsiat, J., Zoltowska, K. M., Laskowska-Kaszub, K., & Wojda, U. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6435861 · Cited by 221 · see citing works
Alterations in Mitochondrial Quality Control in Alzheimer’s Disease
Cai, Q., & Tammineni, P. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00024 · Cited by 215 · see citing works
Dysfunctional Mitochondria and Mitophagy as Drivers of Alzheimer’s Disease Pathogenesis
Chakravorty, A., Jetto, C. T., & Manjithaya, R. R. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00311 · Cited by 219 · see citing works
Mullane, K., & Williams, M. J. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.11.014 · Cited by 212 · see citing works
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 210 · see citing works
A role for tau at the synapse in Alzheimer’s disease pathogenesis
Pooler, A. M., Noble, W., & Hanger, D. P. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.09.018 · Cited by 203 · see citing works
Mitochondria-associated membranes as hubs for neurodegeneration
Krols, M., Isterdael, G. V., Asselbergh, B., Kremer, A., Lippens, S., Timmerman, V., & Janssens, S. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1528-7 · Cited by 200 · see citing works
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 184 · see citing works
Mechanisms Orchestrating Mitochondrial Dynamics for Energy Homeostasis
Yu, S. B., & Pekkurnaz, G. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.07.027 · Cited by 182 · see citing works
Mitochondrial dysfunction: the missing link between aging and sporadic Alzheimer’s disease
Grimm, A., Friedland, K., & Eckert, A. (2015) · Biogerontology · doi:10.1007/s10522-015-9618-4 · Cited by 182 · see citing works
Hu, Y., Li, X., Wang, Z.-H., Luo, Y., Zhang, X., Liu, X., Feng, Q., Wang, Q., Yue, Z., Chen, Z., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7861 · Cited by 171 · see citing works
Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160 · see citing works
Shulman, J. M., Imboywa, S., Giagtzoglou, N., Powers, M. P., Hu, Y., Devenport, D., Chipendo, P., Chibnik, L. B., Diamond, A., Perrimon, N., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt478 · Cited by 167 · see citing works
Self-citationp53 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 168 · see citing works
Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β
Vossel, K. A., Xu, J. C., Fomenko, V., Miyamoto, T., Suberbielle, E., Knox, J. A., Ho, K., Kim, D. H., Yu, G.-Q., & Mucke, L. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201407065 · Cited by 167 · see citing works
Defective mitochondrial fission augments NLRP3 inflammasome activation
Park, S., Won, J.-H., Hwang, I., Hong, S., Lee, H. K., & Yu, J. (2015) · Scientific Reports · doi:10.1038/srep15489 · Cited by 166 · see citing works
Why size matters – balancing mitochondrial dynamics in Alzheimer's disease
DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 164 · see citing works
Self-citationLi, X., Hu, Y., Wang, Z.-H., Luo, Y., Zhang, Y., Liu, X., Feng, Q., Wang, Q., Ye, K., Liu, G., et al. (2016) · Scientific Reports · doi:10.1038/srep24756 · Cited by 164 · see citing works
Pathak, D., Berthet, A., & Nakamura, K. (2013) · Annals of Neurology · doi:10.1002/ana.24014 · Cited by 157 · see citing works
Methylene blue upregulates Nrf2/ARE genes and prevents tau-related neurotoxicity
Stack, C., Jainuddin, S., Elipenahli, C., Gerges, M., Starkova, N. N., Starkov, A. A., Jové, M., Portero‐Otín, M., Launay, N., Pujol, A., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu080 · Cited by 159 · see citing works
Contribution of Tau Pathology to Mitochondrial Impairment in Neurodegeneration
Maria Jose Perez, J., Jara, C., & Quintanilla, R. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00441 · Cited by 153 · see citing works
Alzheimer’s Disease Pathogenesis: Role of Autophagy and Mitophagy Focusing in Microglia
Eshraghi, M., Adlimoghaddam, A., Mahmoodzadeh, A., Sharifzad, F., Yasavoli-Sharahi, H., Lorzadeh, S., Albensi, B. C., & Ghavami, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073330 · Cited by 158 · see citing works
Receptor-mediated Drp1 oligomerization on endoplasmic reticulum
Ji, W.-K., Chakrabarti, R., Fan, X., Schoenfeld, L. W., Strack, S., & Higgs, H. N. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201610057 · Cited by 151 · see citing works
Novel roles for actin in mitochondrial fission
Hatch, A. L., Gurel, P. S., & Higgs, H. N. (2014) · Journal of Cell Science · doi:10.1242/jcs.153791 · Cited by 150 · see citing works
Liu, C., Song, X., Nisbet, R. M., & Götz, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.641902 · Cited by 145 · see citing works
Self-citationRegulation of mitochondrial dynamics in astrocytes: Mechanisms, consequences, and unknowns
Jackson, J. G., & Robinson, M. B. (2017) · Glia · doi:10.1002/glia.23252 · Cited by 144 · see citing works
Ultrastructure and dynamics of the actin−myosin II cytoskeleton during mitochondrial fission
Yang, C., & Svitkina, T. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0313-6 · Cited by 139 · see citing works
Synapses: The Brain’s Energy-Demanding Sites
Faria‐Pereira, A., & Morais, V. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073627 · Cited by 145 · see citing works
Reddy, P. H. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132060 · Cited by 136 · see citing works
Yan, T., & Zhao, Y. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101381 · Cited by 137 · see citing works
Linking Oxidative Stress and Proteinopathy in Alzheimer’s Disease
Sharma, C., & Kim, S. R. (2021) · Antioxidants · doi:10.3390/antiox10081231 · Cited by 136 · see citing works
Mitochondrial fission‐fusion as an emerging key regulator of cell proliferation and differentiation
Mitra, K. (2013) · BioEssays · doi:10.1002/bies.201300011 · Cited by 132 · see citing works
Briston, T., & Hicks, A. R. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180025 · Cited by 129 · see citing works
Eckert, A., Nisbet, R. M., Grimm, A., & Götz, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.013 · Cited by 127 · see citing works
Self-citationGaignard, P., Lière, P., Thérond, P., Schumacher, M., Slama, A., & Guennoun, R. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00406 · Cited by 127 · see citing works
Barbero‐Camps, E., Fernández, A., Martínez-Gili, L., Fernández-Checa, J. C., & Colell, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt201 · Cited by 127 · see citing works
Mitochondrial dynamics, a key executioner in neurodegenerative diseases
Panchal, K., & Tiwari, A. K. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.11.002 · Cited by 127 · see citing works
Connecting the dots between tau dysfunction and neurodegeneration
Frost, B., Götz, J., & Feany, M. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.005 · Cited by 124 · see citing works
Self-citationActin filaments as dynamic reservoirs for Drp1 recruitment
Hatch, A. L., Ji, W.-K., Merrill, R. A., Strack, S., & Higgs, H. N. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-03-0193 · Cited by 122 · see citing works
Bamburg, J. R., Minamide, L. S., Wiggan, O., Tahtamouni, L. H., & Kuhn, T. B. (2021) · Cells · doi:10.3390/cells10102726 · Cited by 122 · see citing works
Motor proteins at the mitochondria–cytoskeleton interface
Kruppa, A. J., & Buß, F. (2021) · Journal of Cell Science · doi:10.1242/jcs.226084 · Cited by 121 · see citing works
Deconstructing Mitochondrial Dysfunction in Alzheimer Disease
García‐Escudero, V., Martín-Maestro, P., Perry, G. L., & Ávila, J. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/162152 · Cited by 118 · see citing works
Kang, T. (2020) · Antioxidants · doi:10.3390/antiox9070617 · Cited by 120 · see citing works
The multiple links between actin and mitochondria
Fung, T. S., Chakrabarti, R., & Higgs, H. N. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00613-y · Cited by 109 · see citing works
Lee, A., Kondapalli, C., Virga, D. M., Lewis, T. L., Koo, S. Y., Ashok, A., Mairet‐Coello, G., Herzig, S., Foretz, M., Viollet, B., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32130-5 · Cited by 113 · see citing works
Moore, A. S., & Holzbaur, E. (2018) · Current Opinion in Physiology · doi:10.1016/j.cophys.2018.03.003 · Cited by 106 · see citing works
Shields, L. Y., Kim, H., Zhu, L., Haddad, D., Berthet, A., Pathak, D., Lam, M., Ponnusamy, R., Diaz‐Ramirez, L. G., Gill, T. M., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.94 · Cited by 112 · see citing works
Yang, D., Ying, J., Wang, X., Zhao, T., Yoon, S., Yang, F., Zheng, Q., Liu, X., Yu, W., & Hua, F. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.654785 · Cited by 110 · see citing works
Alzheimer, mitochondria and gender
Grimm, A., Mensah‐Nyagan, A. G., & Eckert, A. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.04.012 · Cited by 107 · see citing works
Zádori, D., Veres, G., Szalárdy, L., Klivènyi, P., & Vécsei, L. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170929 · Cited by 107 · see citing works
Insights into Disease-Associated Tau Impact on Mitochondria
Szabo, L., Eckert, A., & Grimm, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176344 · Cited by 102 · see citing works
Salminen, A., Haapasalo, A., Kauppinen, A., Kaarniranta, K., Soininen, H. S., & Hiltunen, M. O. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.001 · Cited by 105 · see citing works
Tau physiology and pathomechanisms in frontotemporal lobar degeneration
Bodea, L., Eckert, A., Ittner, L. M., Piguet, O., & Götz, J. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13600 · Cited by 104 · see citing works
Self-citationInteraction of misfolded proteins and mitochondria in neurodegenerative disorders
Abramov, A. Y., Berezhnov, A. V., Fedotova, E. I., Зинченко, В. П., & Долгачева, Л. П. (2017) · Biochemical Society Transactions · doi:10.1042/bst20170024 · Cited by 105 · see citing works
Mitochondrial Stress Signaling Promotes Cellular Adaptations
Barbour, J. A., & Turner, N. A. (2014) · International Journal of Cell Biology · doi:10.1155/2014/156020 · Cited by 102 · see citing works
Fields, J. A., Serger, E., Campos, S., Divakaruni, A. S., Kim, C., Smith, K., Trejo, M., Adame, A., Spencer, B. J., Rockenstein, E. M., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.11.015 · Cited by 101 · see citing works
Focusing on mitochondria in the brain: from biology to therapeutics
Song, N., Mei, S., Wang, X.-X., Hu, G., & Lu, M. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00409-w · Cited by 102 · see citing works
Zhi, J., Yuan, X., Wei, J., Guo, X., Gong, Y., Li, J., Zhou, H., Zhang, L., & Liu, J. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c06687 · Cited by 97 · see citing works
Glucocorticoid impairs mitochondrial quality control in neurons
Choi, G. E., & Han, H. J. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105301 · Cited by 95 · see citing works
The Role of MAPT in Neurodegenerative Diseases: Genetics, Mechanisms and Therapy
Zhang, C., Xing, A., Tan, M., Tan, L., & Yu, J. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9415-8 · Cited by 91 · see citing works
Cerebrospinal fluid lactate is associated with multiple sclerosis disease progression
Albanese, M., Zagaglia, S., Landi, D., Boffa, L., Nicoletti, C. G., Marciani, M. G., Mandolesi, G., Marfia, G. A., Buttari, F., Mori, F., et al. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0502-1 · Cited by 88 · see citing works
Tau-induced neurodegeneration: mechanisms and targets
Beharry, C., Cohen, L. S., Di, J., Ibrahim, K., Briffa-Mirabella, S., & Alonso, A. D. C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1414-z · Cited by 88 · see citing works
Lee, D.-S., & Kim, J.-E. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0910-5 · Cited by 88 · see citing works
Leuner, K., Stockburger, C., Denzer, I., Eckert, G. P., & Müller, W. E. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00007-6 · Cited by 84 · see citing works
Götz, J., Xia, D., Leinenga, G., Chew, Y. L., & Nicholas, H. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00072 · Cited by 85 · see citing works
Self-citationGalvan, D. L., Long, J., Green, N., Chang, B. H., Lin, J. S., Schumacker, P. T., Truong, L. D., Overbeek, P. A., & Danesh, F. R. (2019) · Journal of Clinical Investigation · doi:10.1172/jci127277 · Cited by 85 · see citing works
Mitochondrial Dysfunction in Neurodegenerative Diseases
Yang, H. (2025) · Cells · doi:10.3390/cells14040276 · Cited by 92 · see citing works
- Authors
- DuBoff, B., Götz, J., & Feany, M. B.
- Affiliations
- Brigham and Women's Hospital (US)
- The University of Queensland (AU)
- ORCID
- Götz, Jürgen
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 75
- Issue
- 4
- Pages
- 618-632
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3428596
- OpenAlex
- W2082970812
- Cited by
- 377
- References
- 75
- Citations by year
- 2026: 15 · 2025: 25 · 2024: 24 · 2023: 30 · 2022: 24 · 2021: 43 · 2020: 26 · 2019: 25 · 2018: 28 · 2017: 30 · 2016: 24 · 2015: 24 · 2014: 29 · 2013: 27 · 2012: 3
- FWCI
- 17.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (F31AG032839, R21AG028074, R01AG033518, R01AG019790)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- tau protein, neurodegeneration, Drp1, mitochondrial fission, mitochondrial fusion, mitochondrial dynamics, mitochondrial elongation, actin filament stabilization, myosin, Alzheimer's disease, mitochondrial dysfunction, tau toxicity, Drosophila neurons, mouse neurons
- MeSH terms
- Actins, Analysis of Variance, Animals, Cytoplasm, Cytoskeletal Proteins, Disease Models, Animal, Drosophila, Gene Expression Regulation, Humans, Microtubule-Associated Proteins, Mitochondria, Mutation, Myosins, Nerve Degeneration, Neurons, tau Proteins, Cell Death, Gelsolin, Cell Cycle Proteins, GTP-Binding Proteins, In Situ Nick-End Labeling, GTP Phosphohydrolases, Mitochondrial Proteins, Tauopathies, ATP Synthetase Complexes, Drosophila Proteins, Animals, Genetically Modified, Dynamins, RNA Interference, MicroRNAs, Green Fluorescent Proteins, Voltage-Dependent Anion Channels, Mice
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