The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Open accessAbstract
Dynein and kinesin motor proteins transport cellular cargoes toward opposite ends of microtubule tracks. In neurons, microtubules are abundantly decorated with microtubule-associated proteins (MAPs) such as tau. Motor proteins thus encounter MAPs frequently along their path. To determine the effects of tau on dynein and kinesin motility, we conducted single-molecule studies of motor proteins moving along tau-decorated microtubules. Dynein tended to reverse direction, whereas kinesin tended to detach at patches of bound tau. Kinesin was inhibited at about a tenth of the tau concentration that inhibited dynein, and the microtubule-binding domain of tau was sufficient to inhibit motor activity. The differential modulation of dynein and kinesin motility suggests that MAPs can spatially regulate the balance of microtubule-dependent axonal transport.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Tau impedes kinesin and dynein motors on microtubules via competition for microtubule binding (198); thus tau may also block proper trafficking and fusion of autophagosomes to lysosomes, causing impaired autophagy.”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [198]
In the citing paper
“While some motors, such as kinesin-1 and kinesin-3, are strongly inhibited by tau in an isoform- and lattice-dependent manner, others, like kinesin-2 and dynein, can more effectively navigate tau-decorated regions”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau envelopes act as selective, reversible barriers along microtubules, regulating the access of motor proteins and other MAPs to the microtubule.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“The extent of tau’s influence on motor proteins depends on several factors including (1) the tau isoform and PTMs, (2) the underlying microtubule lattice, and (3) the intrinsic properties of the motors themselves.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Envelope formation is sensitive to the intramolecular lattice spacing between α and β tubulin.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau exhibits both diffusive and cooperative interactions with microtubules.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau does not form envelopes on GMPCPP-polymerized microtubules, which are irreversibly expanded, mimicking the GTP-state, but readily forms envelopes on compacted GDP-lattices or reversibly expanded taxol-lattices”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau regulates the axonal cytoskeleton (Kanai et al., 1992; Chen et al., 1992; Panda et al., 2003; Rosenberg et al., 2008; Chung et al., 2015; Biswas and Kalil, 2018), and acts as a selective barrier on microtubules to direct intracellular transport”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Cooperativity leads to cohesive envelope-like structures (Dixit et al., 2008; Hinrichs et al., 2012; McVicker et al., 2014; Siahaan et al., 2019; Tan et al., 2019; Siahaan et al., 2022).”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Axonal cargoes are transported by teams of motors with differing sensitivities to tau, as we observed for kinesin-1 (KIF5C) and kinesin-3 (KIF1A) (Figure 3) and as shown previously”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Previous studies showed that tau differentially regulates motor proteins, with kinesin-1 and kinesin-3 being more sensitive to tau-mediated inhibition than kinesin-2 and dynein”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Overexpression of either Tau WT, 3A, or 3D reduced anterograde movement of mitochondria in PC12 cells and cortical neurons, as reported (Mandelkow et al., 2004;Hollenbeck and Saxton, 2005;Dixit et al., 2008).”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau is highly expressed in neurons in the mammalian brain, and normally localizes predominantly to axons as an important regulator of axonal transport [124–126].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [124]
Citations
Cites
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174
The Molecular Motor Toolbox for Intracellular Transport
Vale, R. D. (2003) · Cell · doi:10.1016/s0092-8674(03)00111-9 · Cited by 1,982
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
Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 769
Direct observation of single kinesin molecules moving along microtubules
Vale, R. D., Funatsu, T., Pierce, D. W., Romberg, L., Harada, Y., & Yanagida, T. (1996) · Nature · doi:10.1038/380451a0 · Cited by 711
Dynactin increases the processivity of the cytoplasmic dynein motor
King, S. J., & Schroer, T. A. (1999) · Nature Cell Biology · doi:10.1038/71338 · Cited by 661
Domains of tau Protein and Interactions with Microtubules
Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655
Cytoplasmic dynein functions as a gear in response to load
Mallik, R., Carter, B. C., Lex, S. A., King, S. J., & Gross, S. P. (2004) · Nature · doi:10.1038/nature02293 · Cited by 494
Multiple-motor based transport and its regulation by Tau
Vershinin, M., Carter, B. C., Razafsky, D. S., King, S. J., & Gross, S. P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607919104 · Cited by 457
Axonal transport and neurodegenerative disease
Chevalier-Larsen, E. S., & Holzbaur, E. L. F. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.04.002 · Cited by 453
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Alzheimer Disease: An Update on Pathobiology and Treatment Strategies
Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821
Fang, E. F., Hou, Y., Palikaras, K., Adriaanse, B. A., Kerr, J. S., Yang, B., Lautrup, S., Hasan-Olive, M. M., Caponio, D., Dan, X., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0332-9 · Cited by 1,740
Mitochondria dysfunction in the pathogenesis of Alzheimer’s disease: Recent advances.
Wang, W., Zhao, F., Ma, X., Perry, G., & Zhu, X. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00376-6 · Cited by 1,274
The axonal transport of mitochondria
Saxton, W. M., & Hollenbeck, P. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.053850 · Cited by 1,218
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201
Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118
Tau-targeting therapies for Alzheimer disease
Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994
Mitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration
Sheng, Z., & Cai, Q. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3156 · Cited by 940
Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899
Biochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint
Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 897
Axonal transport deficits and neurodegenerative diseases
Millecamps, S., & Julien, J.-P. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3380 · Cited by 755
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723
Axonal transport: cargo-specific mechanisms of motility and regulation
Maday, S., Twelvetrees, A. E., Moughamian, A. J., & Holzbaur, E. L. F. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.019 · Cited by 683
Self-citationStochastic models of intracellular transport
Bressloff, P. C., & Newby, J. (2013) · Reviews of Modern Physics · doi:10.1103/revmodphys.85.135 · Cited by 637
Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609
Regulators of the cytoplasmic dynein motor
Kardon, J. R., & Vale, R. D. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2804 · Cited by 603
Microtubules and Microtubule-Associated ProteinsPreprint
Goodson, H. V., & Jonasson, E. M. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022608 · Cited by 627
Animal models of Alzheimer's disease and frontotemporal dementia
Götz, J., & Ittner, L. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2420 · Cited by 676
Dejanovic, B., Huntley, M. A., De Mazière, A., Meilandt, W. J., Wu, T., Srinivasan, K., Jiang, Z., Gandham, V., Friedman, B. A., Ngu, H., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.014 · Cited by 517
Traffic control: regulation of kinesin motors
Verhey, K. J., & Hammond, J. W. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2782 · Cited by 546
Lee, W., Loo, C., Bebawy, M., Luk, F., Mason, R. S., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 552
Copper in the brain and Alzheimer’s disease
Hung, Y. H., Bush, A. I., & Cherny, R. A. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0600-y · Cited by 503
Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494
Tau Reduction Prevents Aβ-Induced Defects in Axonal Transport
Vossel, K. A., Zhang, K., Brodbeck, J., Daub, A. C., Sharma, P., Finkbeiner, S., Cui, B., & Mucke, L. (2010) · Science · doi:10.1126/science.1194653 · Cited by 486
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
Kent, S. A., Spires-Jones, T. L., & Durrant, C. S. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02196-w · Cited by 446
Synapses and Alzheimer's Disease
Sheng, M., Sabatini, B. L., & Sudhof, T. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005777 · Cited by 436
The Role of Tau in Alzheimer's Disease and Related Disorders
Medeiros, R., Baglietto‐Vargas, D., & LaFerla, F. M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00177.x · Cited by 484
Bidirectional cargo transport: moving beyond tug of war
Hancock, W. O. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3853 · Cited by 447
Motor coordination via a tug-of-war mechanism drives bidirectional vesicle transport
Hendricks, A. G., Perlson, E., Ross, J. L., Schroeder, H. W., Tokito, M., & Holzbaur, E. L. F. (2010) · Current Biology · doi:10.1016/j.cub.2010.02.058 · Cited by 423
Self-citationTau Protein Modifications and Interactions: Their Role in Function and Dysfunction
Mietelska‐Porowska, A., Wasik, U., Goras, M., Filipek, A., & Niewiadomska, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15034671 · Cited by 431
Zhang, B., Carroll, J., Trojanowski, J. Q., Yao, Y., Iba, M., Potuzak, J. S., Hogan, A.-M. L., Xie, S. X., Ballatore, C., Smith, A. B., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4922-11.2012 · Cited by 401
Tau Promotes Neurodegeneration via DRP1 Mislocalization In Vivo
DuBoff, B., Götz, J., & Feany, M. B. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.026 · Cited by 377
Control of mitochondrial transport and localization in neurons
MacAskill, A. F., & Kittler, J. T. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.11.002 · Cited by 372
Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367
Microtubule-Associated Proteins: Structuring the Cytoskeleton
Bodakuntla, S., Jijumon, A. S., Villablanca, C., González-Billault, C. E., & Janke, C. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.07.004 · Cited by 377
Axonal transport: Driving synaptic function
Guedes-Dias, P., & Holzbaur, E. L. F. (2019) · Science · doi:10.1126/science.aaw9997 · Cited by 355
Self-citationLiquid-liquid phase separation in biology: mechanisms, physiological functions and human diseases
Zhang, H., Ji, X., Li, P., Liu, C., Lou, J., Wang, Z., Wen, W., Xiao, Y., Zhang, M., & Zhu, X. (2020) · Science China Life Sciences · doi:10.1007/s11427-020-1702-x · Cited by 355
Mummery, C. J., Börjesson-Hanson, A., Blackburn, D. J., Vijverberg, E. G. B., De Deyn, P. P., Ducharme, S., Jonsson, M., Schneider, A., Rinne, J. O., Ludolph, A. C., et al. (2023) · Nature Medicine · doi:10.1038/s41591-023-02326-3 · Cited by 347
New Insights Into the Pathogenesis of Alzheimer's Disease
Fan, L., Mao, C., Hu, X., Zhang, S., Yang, Z., Hu, Z., Sun, H., Fan, Y., Dong, Y., Yang, J., et al. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2019.01312 · Cited by 362
Retrograde axonal transport: pathways to cell death?
Perlson, E., Maday, S., Fu, M., Moughamian, A. J., & Holzbaur, E. L. F. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.03.006 · Cited by 340
Self-citationNaini, S. M. A., & Soussi‐Yanicostas, N. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/151979 · Cited by 329
Tau pathophysiology in neurodegeneration: a tangled issue
Spires‐Jones, T. L., Stoothoff, W. H., de Calignon, A., Jones, P., & Hyman, B. T. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2008.11.007 · Cited by 321
Intramolecular Strain Coordinates Kinesin Stepping Behavior along Microtubules
Yildiz, A., Tomishige, M., Gennerich, A., & Vale, R. D. (2008) · Cell · doi:10.1016/j.cell.2008.07.018 · Cited by 313
Walking the walk: how kinesin and dynein coordinate their steps
Gennerich, A., & Vale, R. D. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.12.002 · Cited by 318
Diabetes mellitus and Alzheimer's disease: GSK-3β as a potential link
Zhang, Y., Huang, N.-Q., Yan, F., Jin, H., Zhou, S.-Y., Shi, J.-S., & Jin, F. (2018) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.11.015 · Cited by 301
Biochemistry of Tau in Alzheimer’s disease and related neurological disorders
Sergeant, N., Bretteville, A., Hamdane, M., Caillet-Boudin, M.-L., Grognet, P., Bombois, S., Blum, D., Delacourte, A., Pasquier, F., Vanmechelen, E., et al. (2008) · Expert Review of Proteomics · doi:10.1586/14789450.5.2.207 · Cited by 300
Iron in Neurodegeneration – Cause or Consequence?
Ndayisaba, A., Kaindlstorfer, C., & Wenning, G. K. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00180 · Cited by 305
Glaucoma: the retina and beyond
Davis, B. M., Crawley, L. A., Pahlitzsch, M., Javaid, F. Z., & Cordeiro, M. F. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1609-2 · Cited by 291
JIP1 regulates the directionality of APP axonal transport by coordinating kinesin and dynein motors
Fu, M., & Holzbaur, E. L. F. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302078 · Cited by 277
Self-citationKopeikina, 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 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 281
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
Integrated regulation of motor-driven organelle transport by scaffolding proteins
Fu, M., & Holzbaur, E. L. F. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.002 · Cited by 266
Self-citationMicrotubule-Based Transport and the Distribution, Tethering, and Organization of OrganellesPreprint
Barlan, K., & Gelfand, V. I. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a025817 · Cited by 284
Synaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258
Diabetes and Alzheimer’s disease crosstalk
Baglietto‐Vargas, D., Shi, J. J., Yaeger, D. M., Ager, R. R., & LaFerla, F. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.03.005 · Cited by 263
Microtubules gate tau condensation to spatially regulate microtubule functions
Tan, R., Lam, A. J., Tan, T., Han, J., Nowakowski, D. W., Vershinin, M., Simó, S., Ori-McKenney, K. M., & McKenney, R. J. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0375-5 · Cited by 231
The paradox of paclitaxel neurotoxicity: Mechanisms and unanswered questions
Gornstein, E. L., & Schwarz, T. L. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.016 · Cited by 255
von Delius, M., & Leigh, D. A. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15005g · Cited by 256
Autophagy, aging, and age-related neurodegeneration
Palmer, J. E., Wilson, N., Son, S. M., Obrocki, P., Wróbel, L., Rob, M., Takla, M., Korolchuk, V. I., & Rubinsztein, D. C. (2024) · Neuron · doi:10.1016/j.neuron.2024.09.015 · Cited by 277
Ageing and neurodegenerative diseases
Hung, C.-W., Chen, Y., Hsieh, W.-L., Chiou, S., & Kao, C.-L. (2010) · Ageing Research Reviews · doi:10.1016/j.arr.2010.08.006 · Cited by 257
Which way to go? Cytoskeletal organization and polarized transport in neurons
Kapitein, L. C., & Hoogenraad, C. C. (2010) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.08.015 · Cited by 255
Cellular and pathological functions of tau
Bravo, C. P., Naguib, S. A., & Gan, L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00753-9 · Cited by 271
Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction
Deniston, C. K., Salogiannis, J., Mathea, S., Snead, D., Lahiri, I., Matyszewski, M., Donosa, O., Watanabe, R., Böhning, J., Shiau, A. K., et al. (2020) · Nature · doi:10.1038/s41586-020-2673-2 · Cited by 253
The role of pathological tau in synaptic dysfunction in Alzheimer’s diseases
Wu, M., Zhang, M., Yin, X., Chen, K., Hu, Z., Zhou, Q., Cao, X., Chen, Z., & Liu, D. (2021) · Translational Neurodegeneration · doi:10.1186/s40035-021-00270-1 · Cited by 241
Pratt, W. B., Gestwicki, J. E., Osawa, Y., & Lieberman, A. P. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124332 · Cited by 244
The Key Roles of GSK-3β in Regulating Mitochondrial Activity
Yang, K. H., Chen, Z., Gao, J., Shi, W., Li, L., Jiang, S., Hu, H., Liu, Z., Xu, D., & Wu, L. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000485580 · Cited by 241
Wilson, C., & González-Billault, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00381 · Cited by 238
Holth, J. K., Bomben, V. C., Reed, J. G., Inoue, T., Younkin, L., Younkin, S. G., Pautler, R. G., Botas, J., & Noebels, J. L. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.3191-12.2013 · Cited by 238
On and Around Microtubules: An Overview
Wade, R. H. (2009) · Molecular Biotechnology · doi:10.1007/s12033-009-9193-5 · Cited by 256
Soluble forms of tau are toxic in Alzheimer's disease
Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232
Kinesin Assembly and Movement in Cells
Verhey, K. J., Kaul, N., & Soppina, V. (2011) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-042910-155310 · Cited by 231
Cellular and pathological heterogeneity of primary tauopathies
Chung, D. C., Roemer, S. F., Petrucelli, L., & Dickson, D. W. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00476-x · Cited by 232
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
Tau in neurodegenerative disease
Gao, Y.-L., Wang, N., Sun, F.-R., Cao, X.-P., Zhang, W., & Yu, J.-T. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.04.23 · Cited by 222
Radtke, K., Kieneke, D., Wolfstein, A., Michael, K., Steffen, W., Scholz, T., Karger, A., & Sodeik, B. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000991 · Cited by 221
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220
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 226
Xia, Y., Prokop, S., & Giasson, B. I. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00460-5 · Cited by 227
Loss of Miro1-directed mitochondrial movement results in a novel murine model for neuron disease
Nguyen, T., Oh, S. S., Weaver, D., Lewandowska, A., Maxfield, D., Schuler, M.-H., Smith, N. K., Macfarlane, J. L., Saunders, G. W., Palmer, C. A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402449111 · Cited by 223
Motor ProteinsPreprint
Sweeney, H. L., & Holzbaur, E. L. F. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021931 · Cited by 233
Self-citationProts, I., Grosch, J., Brazdis, R.-M., Simmnacher, K., Veber, V., Havlicek, S., Hannappel, C., Krach, F., Krumbiegel, M., Schütz, O., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713129115 · Cited by 223
Molecular crowding creates traffic jams of kinesin motors on microtubules
Leduc, C., Padberg‐Gehle, K., Varga, V., Helbing, D., Diez, S., & Howard, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107281109 · Cited by 219
Microtubule-based transport – basic mechanisms, traffic rules and role in neurological pathogenesis
Franker, M. A. M., & Hoogenraad, C. C. (2013) · Journal of Cell Science · doi:10.1242/jcs.115030 · Cited by 216
Competition between microtubule-associated proteins directs motor transport
Monroy, B. Y., Sawyer, D. L., Ackermann, B. E., Borden, M. M., Tan, T. C., & Ori-McKenney, K. M. (2018) · Nature Communications · doi:10.1038/s41467-018-03909-2 · Cited by 213
Kanaan, N. M., Pigino, G. F., Brady, S. T., Lazarov, O., Binder, L. I., & Morfini, G. A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.003 · Cited by 215
Richetin, K., Steullet, P., Pachoud, M., Perbet, R., Parietti, E., Maheswaran, M., Eddarkaoui, S., Bégard, S., Pythoud, C., Rey, M. J., et al. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-00728-x · Cited by 214
Zhang, W., Xu, C., Sun, J., Shen, H., Wang, J., & Yang, C. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.008 · Cited by 221
Stable kinesin and dynein assemblies drive the axonal transport of mammalian prion protein vesicles
Encalada, S. E., Szpankowski, L., Xia, C.-H., & Goldstein, L. S. B. (2011) · Cell · doi:10.1016/j.cell.2011.01.021 · Cited by 206
Shahpasand, K., Uemura, I., Saito, T., Asano, T., Hata, K., Shibata, K., Toyoshima, Y., Hasegawa, M., & Hisanaga, S.-I. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5927-11.2012 · Cited by 206
Tau deletion promotes brain insulin resistance
Marciniak, E., Leboucher, A., Caron, E., Ahmed, T., Tailleux, A., Dumont, J., Issad, T., Gerhardt, E., Pagesy, P., Vileno, M., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20161731 · Cited by 205
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
Dynein achieves processive motion using both stochastic and coordinated stepping
Qiu, W., Derr, N. D., Goodman, B. S., Villa, E., Wu, D., Shih, W. M., & Reck‐Peterson, S. L. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2205 · Cited by 202
Ramkumar, A., Jong, B. Y., & Ori-McKenney, K. M. (2017) · Developmental Dynamics · doi:10.1002/dvdy.24599 · Cited by 208
Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 207
Metadata
- Authors
- Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Ross, Jennifer L.
- Holzbaur, Erika L. F.
- Venue
- Science
- Published
- 2008-02-22
- Volume
- 319
- Issue
- 5866
- Pages
- 1086-1089
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2866193
- OpenAlex
- W1981662243
- Cited by
- 1,012
- References
- 20
- Citations by year
- 2026: 32 · 2025: 35 · 2024: 39 · 2023: 52 · 2022: 68 · 2021: 80 · 2020: 76 · 2019: 59 · 2018: 58 · 2017: 62 · 2016: 52 · 2015: 44 · 2014: 63 · 2013: 42 · 2012: 83
- FWCI
- 24.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5p01ar051174-05)
- National Institute of General Medical Sciences (GM-48661, R01GM048661)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (P01-AR-051174)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tau protein, dynein, kinesin, motor proteins, microtubule-associated proteins, axonal transport, microtubule-binding domain, motor protein motility, single-molecule tracking
- MeSH terms
- Alzheimer Disease, Animals, Axonal Transport, Dyneins, Mice, Transgenic, Microscopy, Fluorescence, Microtubules, Models, Neurological, Neurons, Protein Binding, Recombinant Fusion Proteins, Kinesins, tau Proteins, Protein Isoforms, 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
