The distribution of tau in the mammalian central nervous system.
Open accessAbstract
We have determined the biochemical and immunocytochemical localization of the heterogeneous microtubule-associated protein tau using a monoclonal antibody that binds to all of the tau polypeptides in both bovine and rat brain. Using immunoblot assays and competitive enzyme-linked immunosorbent assays, we have shown tau to be more abundant in bovine white matter extracts and microtubules than in extracts and microtubules from an enriched gray matter region of the brain. On a per mole basis, twice-cycled microtubules from white matter contained three times more tau than did twice-cycled microtubules from gray matter. Immunohistochemical studies that compared the localization of tau with that of MAP2 and tubulin demonstrated that tau was restricted to axons, extending the results of the biochemical studies. Tau localization was not observed in glia, which indicated that, at least in brain, tau is neuron specific. These observations indicate that tau may help define a subpopulation of microtubules that is restricted to axons. Furthermore, the monoclonal antibody described in this report should prove very useful to investigators studying axonal sprouting and growth because it is an exclusive axonal marker.
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
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?
Tau is predominantly expressed in cortical and hippocampal neurons, with expression also in oligodendrocytes and astrocytes.
“Tau is predominantly expressed in cortical and hippocampal neurons [5–7], although there is also expression in other cell types such as oligodendrocytes and astrocytes [8, 9].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [7]
The Results (p. 1374) locate tau mainly in neuronal axons, supporting the neuronal part of the claim. The paper examines the medulla, substantia nigra, and cerebellum, but does not establish predominant expression in cortical or hippocampal neurons. The glial-cell clause has separate citations [8, 9] and is not attributed to this source. (LLM, conf=0.84)
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.
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Phosphorylation affects the ability of tau protein to promote microtubule assembly.
Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works
De Camilli, P., Miller, P. E., Navone, F., Theurkauf, W. E., & Vallee, R. B. (1984) · Neuroscience · doi:10.1016/0306-4522(84)90194-5 · Cited by 381 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works
Bloom (2014) · doi:10.1001/jamaneurol.2013.5847 · Cited by 2,194 · see citing works
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 · see citing works
Pathology of Neurodegenerative Diseases
Dugger, B. N., & Dickson, D. W. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028035 · Cited by 1,665 · see citing works
Tau pathology and neurodegeneration
Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133 · see citing works
Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., & Crowther, R. A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03390.x · Cited by 1,037 · see citing works
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929 · see citing works
Hiesberger, T., Trommsdorff, M., Howell, B. W., Goffinet, A., Mumby, M. C., Cooper, J. A., & Herz, J. (1999) · Neuron · doi:10.1016/s0896-6273(00)80861-2 · Cited by 916 · see citing works
Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works
Self-citationKöpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779 · see citing works
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 · 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
Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633 · see citing works
Tau protein kinases: Involvement in Alzheimer's disease
Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631 · see citing works
The Role of NMDA Receptors in Alzheimer’s Disease
Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00043 · Cited by 535 · see citing works
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 · see citing works
The microtubule binding domain of tau protein
Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500 · see citing works
Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies
Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2959 · Cited by 440 · see citing works
Phosphorylation determines two distinct species of tau in the central nervous system
Papasozomenos, S. C., & Binder, L. I. (1987) · Cell Motility · doi:10.1002/cm.970080303 · Cited by 420 · see citing works
Self-citationNuclear Tau, a Key Player in Neuronal DNA Protection
Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421 · see citing works
Liquid-liquid phase separation induces pathogenic tau conformations in vitro
Kanaan, N. M., Hamel, C., Grabinski, T., & Combs, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16580-3 · Cited by 397 · see citing works
LoPresti, P., Szuchet, S., Papasozomenos, S. C., Zinkowski, R. P., & Binder, L. I. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.22.10369 · Cited by 388 · see citing works
Self-citationKosik, K., & Finch, E. (1987) · The Journal of Neuroscience · doi:10.1523/jneurosci.07-10-03142.1987 · Cited by 368 · see citing works
Zhao, J., Fu, Y., Yasvoina, M., Shao, P., Hitt, B., O'Connor, T., Logan, S., Maus, E., Citron, M., Berry, R., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4396-06.2007 · Cited by 365 · see citing works
Self-citationTau and neuroinflammation: what impact for Alzheimer's disease and tauopathies?
Laurent, C., Buée, L., & Blum, D. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.01.003 · Cited by 348 · see citing works
Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.t01-1-01061.x · Cited by 313 · see citing works
Alexander, A. G., Marfil, V., & Li, C. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00279 · Cited by 310 · see citing works
Role of tau protein in Alzheimer’s disease: The prime pathological player
Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278 · see citing works
Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B
Wang, J.-Z., Gong, C.-X., Zaidi, T., Grundke-Iqbal, I., & Iqbal, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.9.4854 · Cited by 269 · see citing works
Klein, C., Krämer, E.-M., Cardine, A.-M., Schraven, B., Brandt, R., & Trotter, J. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-03-00698.2002 · Cited by 250 · see citing works
The Association of Tau With Mitochondrial Dysfunction in Alzheimer’s Disease
Cheng, Y., & Bai, F. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00163 · Cited by 239 · see citing works
Maas, T., Eidenmüller, J., & Brandt, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000389200 · Cited by 226 · see citing works
Tau Does Not Stabilize Axonal Microtubules but Rather Enables Them to Have Long Labile Domains
Qiang, L., Sun, X., Austin, T. O., Muralidharan, H., Jean, D. C., Liu, M., Yu, W., & Baas, P. W. (2018) · Current Biology · doi:10.1016/j.cub.2018.05.045 · Cited by 222 · see citing works
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 · 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
Tau co-organizes dynamic microtubule and actin networks
Elie, A., Prezel, E., Guérin, C., Denarier, E., Ramirez-Rios, S., Serre, L., Andrieux, A., Fourest-Lieuvin, A., Blanchoin, L., & Arnal, I. (2015) · Scientific Reports · doi:10.1038/srep09964 · Cited by 200 · see citing works
Hirokawa, N., Funakoshi, T., Sato-Harada, R., & Kanai, Y. (1996) · The Journal of cell biology · doi:10.1083/jcb.132.4.667 · Cited by 179 · see citing works
Tau Proteins and Neurofibrillary Degeneration
Goedert, M., Spillantini, M. G., & Crowther, R. A. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00671.x · Cited by 178 · 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
Intraneuronal Aβ detection in 5xFAD mice by a new Aβ-specific antibody
Youmans, K. L., Tai, L. M., Kanekiyo, T., Stine Jr, W. B., Michon, S.-C., Nwabuisi-Heath, E., Manelli, A. M., Fu, Y., Riordan, S., Eimer, W. A., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-8 · Cited by 164 · see citing works
Self-citationNuclear Tau and Its Potential Role in Alzheimer’s Disease
Bukar Maina, M., Al-Hilaly, Y., & Serpell, L. (2016) · Biomolecules · doi:10.3390/biom6010009 · Cited by 161 · see citing works
Fukami, S., Watanabe, K., Iwata, N., Haraoka, J., Lu, B., Gerard, N. P., Gerard, C., Fraser, P., Westaway, D., George-Hyslop, P. S., et al. (2002) · Neuroscience Research · doi:10.1016/s0168-0102(02)00015-9 · Cited by 157 · see citing works
Gourmaud, S., Shou, H., Irwin, D. J., Sansalone, K., Jacobs, L. M., Lucas, T. H., Marsh, E. D., Davis, K. A., Jensen, F. E., & Talos, D. M. (2020) · Brain · doi:10.1093/brain/awz381 · Cited by 155 · see citing works
Kanai, Y., & Hirokawa, N. (1995) · Neuron · doi:10.1016/0896-6273(95)90298-8 · Cited by 144 · see citing works
Hartigan, J. A., & Johnson, G. V. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21395 · Cited by 141 · see citing works
Kontaxi, C., Piccardo, P., & Gill, A. C. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00056 · Cited by 138 · see citing works
Cognitive defects are reversible in inducible mice expressing pro-aggregant full-length human Tau
Van der Jeugd, A., Hochgräfe, K., Ahmed, T., Decker, J. M., Sydow, A., Hofmann, A., Wu, D., Messing, L., Balschun, D., D’Hooge, R., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0987-3 · Cited by 135 · see citing works
Bancher, C., Jellinger, K., Lassmann, H., Fischer, P., & Leblhuber, F. (1996) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/bf02189115 · Cited by 130 · see citing works
Differential Incorporation of Tau Isoforms in Alzheimer's Disease
Espinoza, M., de Silva, R., Dickson, D. W., & Davies, P. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-14101 · Cited by 119 · see citing works
Depletion of a microtubule-associated motor protein induces the loss of dendritic identity
Yu, W., Cook, C., Sauter, C., Kuriyama, R., Kaplan, P. L., & Baas, P. W. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-15-05782.2000 · Cited by 116 · see citing works
Ambegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113 · see citing works
Rat tau proteome consists of six tau isoforms: implication for animal models of human tauopathies
Hanes, J., Zilka, N., Bartkova, M., Caletkova, M., Dobrota, D., & Novak, M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05869.x · Cited by 109 · see citing works
Bernardo, T. C., Marques‐Aleixo, I., Beleza, J., Oliveira, P. J., Ascensão, A., & Magalhães, J. (2016) · Brain Pathology · doi:10.1111/bpa.12403 · Cited by 108 · see citing works
Desale, S. E., Chidambaram, H., & Chinnathambi, S. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00036-1 · Cited by 99 · see citing works
Tau‐66: evidence for a novel tau conformation in Alzheimer's disease
Ghoshal, N., García‐Sierra, F., Fu, Y., Beckett, L. A., Mufson, E. J., Kuret, J., Berry, R. W., & Binder, L. I. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00346.x · Cited by 97 · see citing works
Self-citationSottejeau, Y., Bretteville, A., Cantrelle, F.-X., Malmanche, N., Demiaute, F., Mendes, T., Delay, C., Alves Dos Alves, H., Flaig, A., Davies, P., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0237-8 · Cited by 98 · see citing works
“In contrast to other antibodies, the Tau-1 antibody binds to various non-phosphorylated Tau sites; the signal thus decreases when Tau is hyperphosphorylated [31].”
Hypothesis: microtubules, a key to Alzheimer disease
Matsuyama, S. S., & Jarvik, L. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.8152 · Cited by 95 · see citing works
Tang, A.-H., Karson, M. A., Nagode, D. A., McIntosh, J. M., Uebele, V. N., Renger, J. J., Klugmann, M., Milner, T. A., & Alger, B. E. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2781-11.2011 · Cited by 92 · see citing works
Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles
Prezel, E., Elie, A., Delaroche, J., Stoppin-Mellet, V., Bosc, C., Serre, L., Fourest-Lieuvin, A., Andrieux, A., Vantard, M., & Arnal, I. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0429 · Cited by 83 · see citing works
Tsujio, I., Zaidi, T., Xu, J., Kotula, L., Grundke-Iqbal, I., & Iqbal, K. (2005) · FEBS Letters · doi:10.1016/j.febslet.2004.11.097 · Cited by 80 · see citing works
Schnurra, I., Bernstein, H.-G., Riederer, P., & Braunewell, K.-H. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0432 · Cited by 76 · see citing works
Yoshiyama, Y., Zhang, B., Bruce, J., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-33-10662.2003 · Cited by 72 · see citing works
Tau hyperphosphorylation and deregulation of calcineurin in mouse models of Huntington’s disease
Gratuze, M., Noël, A., Julien, C., Cisbani, G., Milot-Rousseau, P., Morin, F., Dickler, M., Goupil, C., Bezeau, F., Poitras, I., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddu456 · Cited by 65 · see citing works
Skein-like inclusions in the anterior horn cells in motor neuron disease
Mizusawa, H., Nakamura, H., Wakayama, I., Yen, S.-H. C., & Hirano, A. (1991) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(91)90112-k · Cited by 63 · see citing works
Centonze, D., Rossi, S., Napoli, I., Mercaldo, V., Lacoux, C., Ferrari, F., Ciotti, M. T., De Chiara, V., Prosperetti, C., Maccarrone, M., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0548-07.2007 · Cited by 59 · see citing works
Expression of Tau40 Induces Activation of Cultured Rat Microglial Cells
Wang, L., Jiang, Q., Chu, J., Lin, L., Li, X.-G., Chai, G.-S., Wang, Q., Wang, J.-Z., & Tian, Q. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076057 · Cited by 47 · see citing works
Faulty splicing and cytoskeleton abnormalities in <scp>H</scp> untington's disease
Fernández‐Nogales, M., Santos‐Galindo, M., Hernández, I. H., Cabrera, J. R., & Lucas, J. J. (2016) · Brain Pathology · doi:10.1111/bpa.12430 · Cited by 41 · see citing works
Polis, B., & Samson, A. O. (2024) · Journal of Alzheimer's Disease · doi:10.3233/jad-240058 · Cited by 43 · see citing works
Peng, Y., Tao, H., Wang, S., Xiao, J., Wang, Y., & Su, H. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104463 · Cited by 31 · see citing works
Preserved autophagy in cognitively intact non‐demented individuals with Alzheimer's neuropathology
Tumurbaatar, B., Fracassi, A., Scaduto, P., Guptarak, J., Woltjer, R., Jupiter, D., & Taglialatela, G. (2023) · Alzheimer's & Dementia · doi:10.1002/alz.13074 · Cited by 32 · see citing works
Along the way to a neurofibrillary tangle: a look at the structure of tau
Kosik, K. S., Kowall, N. W., & McKee, A. (1989) · Annals of Medicine · doi:10.3109/07853898909149195 · Cited by 31 · see citing works
Protein-Protein Interactions and Aggregation Inhibitors in Alzheimer’s Disease
Ganeshpurkar, A., Swetha, R., Kumar, D., Gangaram, G. P., Singh, R., Gutti, G., Jana, S., Kumar, D., Kumar, A., & Singh, S. K. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190304153353 · Cited by 30 · see citing works
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 · see citing works
Helgager, J., Liu, G., & McNamara, J. O. (2013) · Journal of Comparative Neurology · doi:10.1002/cne.23225 · Cited by 17 · see citing works
Dickson, J. R., Yoon, H., Frosch, M. P., & Hyman, B. T. (2021) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlab040 · Cited by 13 · see citing works
Nakata, R., Torii, T., Miyasaka, T., & Misonou, H. (2026) · Neuroscience Research · doi:10.1016/j.neures.2025.104987 · Cited by 3 · see citing works
Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease
Chimal-Juárez, E., Patel, H., Jury-Garfe, N., Dabin, L. C., Vidal, R., Kim, J., & Lasagna-Reeves, C. A. (2026) · bioRxiv · doi:10.64898/2026.05.12.724684
Beaudet, D., Berger, C. L., & Hendricks, A. G. (2026) · eLife · doi:10.7554/elife.110011
- Authors
- Binder, L. I., Frankfurter, A., & Rebhun, L. I.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1985-10-01
- Volume
- 101
- Issue
- 4
- Pages
- 1371-1378
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2113928
- OpenAlex
- W1994030229
- Cited by
- 1,588
- References
- 3
- Citations by year
- 2026: 27 · 2025: 36 · 2024: 46 · 2023: 46 · 2022: 59 · 2021: 59 · 2020: 55 · 2019: 48 · 2018: 41 · 2017: 30 · 2016: 31 · 2015: 31 · 2014: 40 · 2013: 27 · 2012: 37
- FWCI
- 30.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (NS 17588)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- tau protein, microtubule-associated proteins, axons, white matter, gray matter, microtubules, neuron-specific proteins, MAP2, tubulin, monoclonal antibodies, axonal sprouting, central nervous system
- MeSH terms
- Animals, Antibodies, Monoclonal, Axons, Brain Chemistry, Cattle, Immunologic Techniques, Mice, Inbred BALB C, Microtubule-Associated Proteins, Microtubules, Nerve Tissue Proteins, Neuroglia, Tubulin, tau Proteins, Mice, Rats
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