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
Items 501–600 of 1,001
Cerebrospinal Fluid Biomarkers in Alzheimer’s Disease—From Brain Starch to Bench and Bedside
Pawlowski, M., Meuth, S., & Duning, T. (2017) · Diagnostics · doi:10.3390/diagnostics7030042 · Cited by 25
Local Translation in Nervous System Pathologies
Gamarra, M., de la Cruz, A., Blanco‐Urrejola, M., & Baleriola, J. (2021) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2021.689208 · Cited by 30
Plectin in the Central Nervous System and a Putative Role in Brain Astrocytes
Potokar, M., & Jorgačevski, J. (2021) · Cells · doi:10.3390/cells10092353 · Cited by 22
Radical pairs may play a role in microtubule reorganization
Zadeh‐Haghighi, H., & Simon, C. (2022) · Scientific Reports · doi:10.1038/s41598-022-10068-4 · Cited by 24
Dityrosine cross-linking and its potential roles in Alzheimer’s disease
Maina, M. B., Al‐Hilaly, Y. K., & Serpell, L. C. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1132670 · Cited by 27
Pike, A. F., Kramer, N. I., Blaauboer, B. J., Seinen, W., & Brands, R. (2014) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2014.12.006 · Cited by 26
Chen, X., Fang, F., Florio, J. B., Rockenstein, E. M., Masliah, E., Mobley, W. C., Rissman, R. A., & Wu, C. (2018) · Traffic · doi:10.1111/tra.12610 · Cited by 25
Calcium channel blockers and Alzheimer's disease.
Tan, Y., Deng, Y., & Qing, H. (2012) · Europe PMC (PubMed Central) · doi:10.3969/j.issn.1673-5374.2012.02.010 · Cited by 23
Manavalan, A., Feng, L., Sze, S. K., Hu, J., & Heese, K. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.02.029 · Cited by 25
Tau Phosphorylation and Aggregation as a Therapeutic Target in Tauopathies
Badiola, N., Suárez‐Calvet, M., & Lleó, A. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710793237403 · Cited by 26
Super-Accuracy and Super-Resolution
Toprak, E., Kural, C., & Selvin, P. R. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)75001-1 · Cited by 24
Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease
Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23
Targeting Mitophagy in Alzheimer’s Disease
Jayatunga, D. P. W., Hone, E., Bharadwaj, P., Garg, M. L., Verdile, G., Guillemin, G. J., & Martins, R. N. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191258 · Cited by 25
Bovyn, M. J., Narayanareddy, B. R. J., Gross, S. P., & Allard, J. F. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e20-10-0658 · Cited by 24
Zhang, X., Lin, L., Li, H., Xia, W., Liu, Q., Zhou, X., Lin, D., & Fu, X. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.07.158 · Cited by 25
Elastic Coupling Effects in Cooperative Transport by a Pair of Molecular Motors
Berger, F., Keller, C., Lipowsky, R., & Klumpp, S. (2012) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-012-0258-3 · Cited by 23
Modulating motility of intracellular vesicles in cortical neurons with nanomagnetic forces on-chip
Kunze, A., Murray, C., Godzich, C., Lin, J., Owsley, K., Tay, A. K. P., & Carlo, D. D. (2017) · Lab on a Chip · doi:10.1039/c6lc01349j · Cited by 24
Hochmair, J., van den Oetelaar, M. C. M., Ravatt, L. M., Diez, L., Lemmens, L. J. M., Ponce-Lina, R., Sankar, R., Franck, M., Nolte, G., Semenova, E., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08548-0 · Cited by 26
Mechanisms Underlying Aluminum Neurotoxicity Related to 14-3-3ζ Protein
Wang, X., Cheng, D., Jiang, W., & Ma, Y. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy021 · Cited by 23
Intraneuronal Tau Misfolding Induced by Extracellular Amyloid-β Oligomers
Rudenko, L. K., Wallrabe, H. K., Periasamy, A., Siller, K. H., Švindrych, Z., Seward, M. E., Best, M. N., & Bloom, G. S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190226 · Cited by 24
The ubiquitin proteoform problem
Deol, K. K., & Strieter, E. R. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.02.015 · Cited by 22
A Review on the Mechanism of Tuina Promoting the Recovery of Peripheral Nerve Injury
Liu, Z., Wang, H., Yu, T., Jiao, Y., Zhang, Y., Liu, D., Xu, Y., Guan, Q., & Lu, M. (2021) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2021/6652099 · Cited by 23
p38 Inhibition Decreases Tau Toxicity in Microglia and Improves Their Phagocytic Function
Perea, J. R., Bolós, M., Cuadros, R., García, E., García‐Escudero, V., Hernández, F., McManus, R. M., Heneka, M. T., & Ávila, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02715-0 · Cited by 24
Gut Microbiota as a Hidden Player in the Pathogenesis of Alzheimer’s Disease
Choi, H., Lee, D., & Mook‐Jung, I. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215235 · Cited by 24
Steenbergen, V. V., Lavoie‐Cardinal, F., Kazwiny, Y., Decet, M., Martens, T., Verstreken, P., Boesmans, W., Koninck, P. D., & Berghe, P. V. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2203499119 · Cited by 24
Heparan Sulfate Proteoglycans in Tauopathy
Zhu, Y., Gandy, L. A., Zhang, F., Liu, J., Wang, C., Blair, L. J., Linhardt, R. J., & Wang, L. (2022) · Biomolecules · doi:10.3390/biom12121792 · Cited by 27
Kukuruzinska, M. A. (2009) · Cell Health and Cytoskeleton · doi:10.2147/chc.s5965 · Cited by 23
Thompson, A. R., Hoeprich, G. J., & Berger, C. L. (2013) · Biophysical Journal · doi:10.1016/j.bpj.2013.05.022 · Cited by 22
Selective impact of Tau loss on nociceptive primary afferents and pain sensation
Sotiropoulos, I., Lopes, A. T., Pinto, V., Lopes, S., Carlos, S., Duarte-Silva, S., Neves-Carvalho, A., Pinto-Ribeiro, F., Pinheiro, S., Fernandes, R., et al. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.07.008 · Cited by 23
GRK5 influences the phosphorylation of tau via GSK3β and contributes to Alzheimer's disease
Zhao, J., Li, X., Chen, X., Cai, Y., Wang, Y., Sun, W., Mai, H., Yang, J., Fan, W., Tang, P., et al. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27709 · Cited by 22
Navigating the cell: how motors overcome roadblocks and traffic jams to efficiently transport cargo
Lakadamyali, M. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp55271c · Cited by 25
11 A Stochastic Compartmental Model for Fast Axonal TransportPreprint
McKinley, S. A., Popovic, L., & Reed, M. C. (2011) · Cited by 23
Transport by Molecular Motors in the Presence of Static DefectsPreprint
Chai, Y., Lipowsky, R., & Klumpp, S. (2009) · Cited by 23
Crowe, A., Henderson, M. J., Anderson, J. D., Titus, S. A., Zakharov, A. V., Simeonov, A. M., Buist, A., Delay, C., Moechars, D., Trojanowski, J. Q., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010532 · Cited by 23
Venkatramani, A., Mukherjee, S., Kumari, A. R., & Panda, D. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.01.172 · Cited by 22
Pal, S., & Melnik, R. (2022) · Scientific Reports · doi:10.1038/s41598-022-11242-4 · Cited by 22
Blessing, E., Parekh, A., Betensky, R. A., Babb, J. S., Saba, N., Debure, L., Varga, A. W., Ayappa, I. A., Rapoport, D. M., Butler, T., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105748 · Cited by 22
Aboud, O., Parcon, P. A., DeWall, K. M., Liu, L., Mrak, R. E., & Griffin, W. S. T. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00103 · Cited by 23
"MEMORY BYTES" — MOLECULAR MATCH FOR CaMKII PHOSPHORYLATION ENCODING OF MICROTUBULE LATTICES
Hameroff, S. R., Craddock, T. J. A., & Tuszyński, J. A. (2010) · Journal of Integrative Neuroscience · doi:10.1142/s0219635210002482 · Cited by 23
Afreen, S., Methner, D. N. R., & Ferreira, A. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.08.026 · Cited by 22
Correlation Imaging Reveals Specific Crowding Dynamics of Kinesin Motor Proteins
Miedema, D. M., Kushwaha, V. S., Denisov, D. V., Açar, Ş., Nienhuis, B., Peterman, E. J. G., & Schall, P. (2017) · Physical Review X · doi:10.1103/physrevx.7.041037 · Cited by 23
Modulating Protein Phosphatase 2A Rescues Disease Phenotype in Neurodegenerative Tauopathies
McKenzie-Nickson, S., Chan, J., Perez, K. A., Hung, L. W., Cheng, L., Sedjahtera, A., Gunawan, L., Adlard, P. A., Hayne, D. J., McInnes, L. E., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00161 · Cited by 22
Liu, G., Thangavel, R., Rysted, J., Kim, Y., Francis, M. B., Adams, E., Lin, Z., Taugher, R. J., Wemmie, J. A., Usachev, Y. M., et al. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24517 · Cited by 22
Thomas, V. (2021) · Routledge eBooks · doi:10.4324/9781003134404-1 · Cited by 22
Microtubules Gate Tau Condensation to Spatially Regulate Microtubule FunctionsPreprint
Tan, R., Lam, A. J., Tan, T. C., Han, J. S., Nowakowski, D. W., Vershinin, M. D., Simó, S., Ori-McKenney, K. M., & McKenney, R. J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/423376 · Cited by 22
DYRK1A Regulates the Bidirectional Axonal Transport of APP in Human-Derived Neurons
Fernandez Bessone, I., Navarro, J., Martinez, E., Karmirian, K., Holubiec, M., Alloatti, M., Goto-Silva, L., Arnaiz Yepez, C., Martins-de-Souza, D., Minardi Nascimento, J., et al. (2022) · The Journal of Neuroscience · doi:10.1523/jneurosci.2551-21.2022 · Cited by 21
Williams, A. E., Hammer, N. I., Fortenberry, R. C., & Reinemann, D. N. (2021) · Molecules · doi:10.3390/molecules26164790 · Cited by 21
Choreographing the motor-driven endosomal dance
Jongsma, M. L. M., Bakker, N., & Neefjes, J. (2022) · Journal of Cell Science · doi:10.1242/jcs.259689 · Cited by 23
Mitochondrial trafficking in neuropsychiatric diseases
Deheshi, S., Pasqualotto, B. A., & Rintoul, G. L. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.06.015 · Cited by 21
HIV-associated neurodegeneration: exploitation of the neuronal cytoskeleton
Wenzel, E. D., Avdoshina, V., & Mocchetti, I. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-019-00737-y · Cited by 21
Charafeddine, R. A., Cortopassi, W. A., Lak, P., Tan, R., McKenney, R. J., Jacobson, M. P., Barber, D. L., & Wittmann, T. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007004 · Cited by 24
Phosphoregulation of Kinesins Involved in Long-Range Intracellular Transport
Kumari, D., & Ray, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.873164 · Cited by 21
Ávila, J. (2009) · Frontiers in Aging Neuroscience · doi:10.3389/neuro.24.001.2009 · Cited by 23
Pacheco, C. D., Elrick, M. J., & Lieberman, A. P. (2009) · Autophagy · doi:10.4161/auto.5.4.8364 · Cited by 20
Pisani, F., Pisani, V., Arcangeli, F., Harding, A., & Singhrao, S. K. (2023) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph20116049 · Cited by 21
PM2.5 triggers tau aggregation in a mouse model of tauopathy
Liu, C., Meng, L., Gao, Y., Chen, J., Zhu, M., Xiong, M., Xiao, T., Gu, X., Liu, C., Li, T., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.176703 · Cited by 22
Non-Canonical Roles of Tau and Their Contribution to Synaptic Dysfunction
Siano, G., Falcicchia, C., Origlia, N., Cattaneo, A., & Primio, C. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810145 · Cited by 22
MINFLUX reveals dynein stepping in live neurons
Schleske, J. M., Hubrich, J., Wirth, J. O., D’Este, E., Engelhardt, J., & Hell, S. W. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2412241121 · Cited by 17
Statistical challenges in microrheology
Didier, G., McKinley, S. A., Hill, D. B., & Fricks, J. (2012) · Journal of Time Series Analysis · doi:10.1111/j.1467-9892.2012.00792.x · Cited by 20
Tarhan, M. C., Orazov, Y., Yokokawa, R., Karsten, S. L., & Fujita, H. (2013) · Lab on a Chip · doi:10.1039/c3lc50151e · Cited by 20
The impacts of molecular motor traffic jams
Ross, J. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203542109 · Cited by 20
Self-citationActivation of conventional kinesin motors in clusters by shaw voltage-gated potassium channels
Barry, J., Xu, M., Gu, Y., Dangel, A. W., Jukkola, P. I., Shrestha, C. L., & Gu, C. (2013) · Journal of Cell Science · doi:10.1242/jcs.122234 · Cited by 21
Vesicular Axonal Transport is Modified In Vivo by Tau Deletion or Overexpression in Drosophila
Talmat-Amar, Y., Arribat, Y., & Parmentier, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030744 · Cited by 20
Transport by Molecular Motors in the Presence of Static Defects
Chai, Y., Lipowsky, R., & Klumpp, S. (2009) · Journal of Statistical Physics · doi:10.1007/s10955-009-9715-3 · Cited by 20
The Role of Tau in Neuronal Function and Neurodegeneration
Aranda-Abreu, G. E., Rojas-Durán, F., Hernández‐Aguilar, M. E., Herrera‐Covarrubias, D., García, L. I., Toledo‐Cárdenas, M. R., & Chi-Castañeda, D. (2025) · Neurology International · doi:10.3390/neurolint17050075 · Cited by 20
Differential Maturation of the Two Regulated Secretory Pathways in Human iPSC-Derived Neurons
Emperador-Melero, J., Nadadhur, A. G., Schut, D., van Weering, J. R. T., Heine, V. M., Toonen, R. F. G., & Verhage, M. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.01.019 · Cited by 19
Cario, A., Savastano, A., Wood, N. B., Liu, Z., Previs, M. J., Hendricks, A. G., Zweckstetter, M., & Berger, C. L. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114215119 · Cited by 19
Romano, L. E. L., Aw, W. Y., Hixson, K. M., Novoselova, T. V., Havener, T. M., Howell, S., Taylor‐Blake, B., Hall, C. L., Xing, L., Beri, J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111580 · Cited by 19
Limorenko, G., Tatlı, M., Rajasekhar, K., Nazarov, S., Weil, M., Schöndorf, D. C., Geist, D., Reinhardt, P., Ehrnhoefer, D. E., Stahlberg, H., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39314-7 · Cited by 22
Rescue of tau-induced synaptic transmission pathology by paclitaxel
Erez, H., Shemesh, O. A., & Spira, M. E. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00034 · Cited by 22
Papegaey, A., Eddarkaoui, S., Deramecourt, V., Fernández-Gómez, F.-J., Pantano, P., Obriot, H., Machala, C., Anquetil, V., Camuzat, A., Brice, A., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0345-0 · Cited by 24
Phosphorylated nucleolar Tau protein is related to the neuronal in vitro differentiation
Federico, C., Gil, L., Bruno, F., D’Amico, A. G., D’Agata, V., & Saccone, S. (2018) · Gene · doi:10.1016/j.gene.2018.04.051 · Cited by 19
An Introduction to Ultrasensitive Assays for Plasma Tau Detection
Ding, X., Tuo, Q., & Lei, P. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201499 · Cited by 20
Lee, S., Jung, C., Lee, G. S., & Hall, G. F. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0954 · Cited by 19
MAP9/MAPH-9 supports axonemal microtubule doublets and modulates motor movement
Tran, M. V., Khuntsariya, D., Fetter, R. D., Ferguson, J. W., Wang, J. T., Long, A. F., Cote, L. E., Wellard, S. R., Vázquez-Martínez, N., Sallee, M. D., et al. (2024) · Developmental Cell · doi:10.1016/j.devcel.2023.12.001 · Cited by 18
Durairajan, S. S. K., Selvarasu, K., Singh, A. K., Patnaik, S., Iyaswamy, A., Jaiswal, Y., Williams, L. L., & Huang, J. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1432002 · Cited by 18
Kinesin passing permanent blockages along its protofilament track
Dreblow, K., Kalchishkova, N., & Böhm, K. J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.04.035 · Cited by 18
Zhang, X., Zou, L. B., Meng, L., Xiong, M., Pan, L., Chen, G., Zheng, Y., Xiong, J., Wang, Z., Duong, D. M., et al. (2021) · eLife · doi:10.7554/elife.65301 · Cited by 17
Navarro‐Hortal, M. D., Romero‐Márquez, J. M., Osta, S., Jiménez-Trigo, V., Muñoz-Ollero, P., & Varela‐López, A. (2022) · Diseases · doi:10.3390/diseases10020028 · Cited by 18
Nabti, I., Reddy, B. J. N., Rezgui, R., Wang, W., Gross, S. P., & Shubeita, G. T. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2206677119 · Cited by 18
Numb regulates Tau levels and prevents neurodegeneration in tauopathy mouse models
Lacomme, M., Hales, S. C., Brown, T. W., Stevanovic, K., Jolicoeur, C., Cai, J., Bois, T., Desrosiers, M., Dalkara, D., & Cayouette, M. (2022) · Science Advances · doi:10.1126/sciadv.abm4295 · Cited by 18
Alzheimer’s disease: an axonal injury disease?
Liang, D., & Zhang, Z. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1264448 · Cited by 21
Printed Biosensors for the Detection of Alzheimer’s Disease Based on Blood Biomarkers
Zeng, Y., Huang, Z., Liu, Y., & Xu, T. (2023) · Journal of Analysis and Testing · doi:10.1007/s41664-023-00277-9 · Cited by 18
Das, V., Sim, D. A., & Miller, J. H. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23394 · Cited by 18
Mattiuzzo, N. R., Toulza, È., Jonca, N., Serre, G., & Guerrin, M. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2010.01188.x · Cited by 18
Twelvetrees, A. E., Hendricks, A. G., & Holzbaur, E. L. F. (2012) · Cell · doi:10.1016/j.cell.2012.05.001 · Cited by 18
Self-citationSuzuki, M., & Kimura, T. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.05.056 · Cited by 18
Intrinsically disordered proteins (IDPs) studied by EPR and in-cell EPR
Weickert, S., Cattani, J., & Drescher, M. (2018) · Royal Society of Chemistry eBooks · doi:10.1039/9781788013888-00001 · Cited by 18
Early-onset cognitive deficits and axonal transport dysfunction in P301S mutant tau transgenic mice
Onishi, T., Matsumoto, Y., Hattori, M., Obayashi, Y., Nakamura, K., Yano, T., Horiguchi, T., & Iwashita, H. (2014) · Neuroscience Research · doi:10.1016/j.neures.2013.12.006 · Cited by 18
KIF18A's neck linker permits navigation of microtubule-bound obstacles within the mitotic spindle
Malaby, H. L. H., Lessard, D. V., Berger, C. L., & Stumpff, J. K. (2019) · Life Science Alliance · doi:10.26508/lsa.201800169 · Cited by 18
Improving Mouse Models for Dementia. Are All the Effects in Tau Mouse Models Due to Overexpression?Preprint
Joel, Z., Izquierdo, P., Salih, D. A. M., Richardson, J. C., Cummings, D. M., & Edwards, F. A. (2018) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2018.83.037531 · Cited by 18
Morphology and Transport in Eukaryotic Cells
Agrawal, A., Scott, Z. C., & Koslover, E. F. (2022) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-111121-103956 · Cited by 18
Needs, H. I., Wilkinson, K. A., Henley, J. M., & Collinson, I. R. (2023) · Journal of Cell Science · doi:10.1242/jcs.260993 · Cited by 19
Age-dependent changes in synaptic plasticity enhance tau oligomerization in the mouse hippocampus
Kimura, T., Suzuki, M., & Akagi, T. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0469-x · Cited by 17
Memorcise and Alzheimer’s disease
Loprinzi, P. D., Frith, E., & Ponce, P. (2018) · The Physician and Sportsmedicine · doi:10.1080/00913847.2018.1445932 · Cited by 17
3D rotational motion of an endocytic vesicle on a complex microtubule network in a living cell
Lee, S., & Higuchi, H. (2019) · Biomedical Optics Express · doi:10.1364/boe.10.006611 · Cited by 17
Monzon, G. A., Scharrel, L., D’Souza, A. I., Henrichs, V., Santen, L., & Diez, S. (2020) · Journal of Cell Science · doi:10.1242/jcs.249938 · Cited by 19
Emergence of directional bias in tau deposition from axonal transport dynamics
Torok, J., Maia, P. D., Verma, P., Mezias, C., & Raj, A. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009258 · Cited by 18
Aging in the nervous system ofCaenorhabditis elegans
Chew, Y. L., Fan, X., Götz, J., & Nicholas, H. (2013) · Communicative & Integrative Biology · doi:10.4161/cib.25288 · Cited by 20
Identification of Stk25 as a Genetic Modifier of Tau Phosphorylation in Dab1-Mutant Mice
Matsuki, T., Zaka, M., Guerreiro, R. J., van der Brug, M. P., Cooper, J. A., Cookson, M., Hardy, J., & Howell, B. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031152 · Cited by 17
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
