The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.
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.
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 cited source says what the claim attributes to it.
In the citing paper
“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]
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“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]
Experimental — accuracy not yet measured
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
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
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
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
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273
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
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
Lee, T., & Luo, L. (1999) · Neuron · doi:10.1016/s0896-6273(00)80701-1 · Cited by 2,540
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
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
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
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
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
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
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
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
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
Alexander, 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
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
Amyloid-β and tau--a toxic pas de deux in Alzheimer’s disease
Ittner, L. M., & Götz, J. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2967 · Cited by 1,269
Self-citationDephosphorylation 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
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
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
Tauopathy in Drosophila : 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
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
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
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 781
Yin, H. L., & Stossel, T. P. (1979) · Nature · doi:10.1038/281583a0 · Cited by 779
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
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
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
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
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
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
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
Hutchinson, E. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn2985 · Cited by 534
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
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
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
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
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
Wang, X., Su, B., Fujioka, H., & Zhu, X. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.071208 · Cited by 341
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
Nishimura, I., Yang, Y., & Lu, B. (2004) · Cell · doi:10.1016/s0092-8674(04)00170-9 · Cited by 324
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
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
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 281
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 276
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
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 265
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
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 230
Self-citationMyosin 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
Linking 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
Mechanism of Neuroprotective Mitochondrial Remodeling by PKA/AKAP1
Merrill, R. A., Dagda, R. K., Dickey, A. S., Cribbs, J. T., Green, S. H., Usachev, Y. M., & Strack, S. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000612 · Cited by 212
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
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
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
Watanabe, T., Hosoya, H., & Yonemura, S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-07-0590 · Cited by 164
Ittner, L. M., Ke, Y. D., & Götz, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014472 · Cited by 156
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 152
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
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 132
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
S/P and T/P phosphorylation is critical for tau neurotoxicity in Drosophila
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
Self-citationChang, K. T., & Min, K. (2005) · Nature Neuroscience · doi:10.1038/nn1564 · Cited by 96
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
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 91
Self-citationDifferential 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
Cyclic 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
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
Iijima-Ando, K., Zhao, L., Gatt, A., Shenton, C., & Iijima, K. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq068 · Cited by 72
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
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 58
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
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
Flagged first, then by citations
Cited by
Sorted by citations
Oxidative stress and mitochondrial dysfunction in Alzheimer’s disease
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
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 1,016
Reconsideration of Amyloid Hypothesis and Tau Hypothesis in Alzheimer's Disease
Kametani, F., & Hasegawa, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00025 · Cited by 836
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
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
Metadata
- 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
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- 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
- 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
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
