The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Tubulin requires tau for growth onto microtubule initiating sites.
Open accessAbstract
Tubulin purified by phosphocellulose chromatography and free of accessory proteins will not form microtubules in the absence or presence of microtubule initiating sites (flagellar microtubules). The capacity for growth onto pre-existing "seeds" can be restored by the addition of small quantities of partially purified tau protein. Larger quantities restore the capacity for spontaneous assembly. These results suggest that tubulin requires tau for both initiation and growth of microtubules and that tau is incorporated into the microtubule throughout its length.
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
“Therefore, inappropriate phosphorylation of tau at these regions can lower its affinity for tubulin and inhibit its ability to promote microtubule assembly [15].”
From Glial contributions to neurodegeneration in tauopathies (2017) · cites this paper as [15]
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
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
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
Self-citationMicrotubule Assembly in the Absence of Added Nucleotides
Shelanski, M. L., Gaskin, F., & Cantor, C. R. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.3.765 · Cited by 2,053
Microtubule Formation in vitro in Solutions Containing Low Calcium Concentrations
Weisenberg, R. C. (1972) · Science · doi:10.1126/science.177.4054.1104 · Cited by 1,216
Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules
Gaskin, F., Cantor, C. R., & Shelanski, M. L. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90048-5 · Cited by 823
Murphy, D. B., & Borisy, G. G. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.7.2696 · Cited by 539
Witman, G. B., Carlson, K., Berliner, J. A., & Rosenbaum, J. L. (1972) · The Journal of Cell Biology · doi:10.1083/jcb.54.3.507 · Cited by 512
Self-citationNucleated Assembly of Microtubules in Porcine Brain Extracts
Borisy, G. G., & Olmsted, J. B. (1972) · Science · doi:10.1126/science.177.4055.1196 · Cited by 322
Cited by
Sorted by citations
Items 101–200 of 239
Characterisation of male meiotic-sterile mutations in Drosophila melanogaster
Lifschytz, E., & Meyer, G. F. (1977) · Chromosoma · doi:10.1007/bf00294944 · Cited by 43
Rate for nucleotide release from tubulin.
Brylawski, B. P., & Caplow, M. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33113-2 · Cited by 42
Pseudohyperphosphorylation Has Differential Effects on Polymerization and Function of Tau Isoforms
Combs, B., Voss, K., & Gamblin, T. C. (2011) · Biochemistry · doi:10.1021/bi2010569 · Cited by 41
Miller, N., Feng, Z., Edens, B. M., Yang, B., Shi, H., Sze, C. C., Hong, B. T., Su, S. C., Cantú, J. A., Topczewski, J., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.3716-14.2015 · Cited by 41
Seed-competent tau monomer initiates pathology in a tauopathy mouse model
Mirbaha, H., Chen, D., Mullapudi, V., Terpack, S. J., White, C. L., Joachimiak, Ł. A., & Diamond, M. I. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102163 · Cited by 39
Bai, Q., & Burton, E. A. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.09.004 · Cited by 42
Identification of tau protein regions required for process formation in PC12 cells
Léger, J. G., Brandt, R., & Lee, G. S. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.12.3403 · Cited by 41
Selective digestion of mouse metaphase chromosomes
Rattner, J. B., Krystal, G., & Hamkalo, B. A. (1978) · Chromosoma · doi:10.1007/bf00330554 · Cited by 39
M�ller, W. G., Bernd, A., & Schr�der, H. C. (1983) · Molecular and Cellular Biochemistry · doi:10.1007/bf00225254 · Cited by 38
Lung endothelium, tau, and amyloids in health and disease
Balczon, R., Lin, M. T., Voth, S. B., Nelson, A. R., Schupp, J. C., Wagener, B. M., Pittet, J., & Stevens, T. (2023) · Physiological Reviews · doi:10.1152/physrev.00006.2023 · Cited by 40
Aillaud, I., Kaniyappan, S., Chandupatla, R., Ramirez, L. M., Alkhashrom, S., Eichler, J., Horn, A. H. C., Zweckstetter, M., Mandelkow�, E., Sticht, H., et al. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-00959-z · Cited by 33
Altered Levels and Isoforms of Tau and Nuclear Membrane Invaginations in Huntington’s Disease
Fernández‐Nogales, M., & Lucas, J. J. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00574 · Cited by 32
Cyclin-dependent kinase 5, a node protein in diminished tauopathy: a systems biology approach
Castro-Álvarez, J. F., Uribe‐Arias, A., MejÃa-Raigosa, D., & Cardona‐Gómez, G. P. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00232 · Cited by 34
Luna‐Muñoz, J., Charles, R., Claude, M., Flores-Rodríguez, P., Ávila, J., Sergio, R., de la Cruz, F., Mena, R., Meraz‐Ríos, M. A., & Florán, B. (2013) · InTech eBooks · doi:10.5772/54228 · Cited by 43
New insights into tau–microtubules interaction revealed by isothermal titration calorimetry
Tsvetkov, P. O., Makarov, A. А., Malesinski, S., Peyrot, V., & Devred, F. (2011) · Biochimie · doi:10.1016/j.biochi.2011.09.011 · Cited by 30
Abdel-Rafei, M. K., & Thabet, N. M. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118410 · Cited by 30
Reassessment of Neuronal Tau Distribution in Adult Human Brain and Implications for Tau Pathobiology
Paterno, G., Bell, B. M., Gorion, K.-M. M., Prokop, S., & Giasson, B. I. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01394-9 · Cited by 30
In vitro assembly of tubulin from nonneural cells (Ehrlich ascites tumor cells)
Doenges, K. H., Nagle, B. W., Uhlmann, A., & Bryan, J. (1977) · Biochemistry · doi:10.1021/bi00634a025 · Cited by 29
Black, M. M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.21.7783 · Cited by 28
Luk, C. Y., Giovannoni, G., Williams, D. R., Lees, A. J., & de Silva, R. (2009) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2009.02.015 · Cited by 25
Franklin, R. M., & Martin, M. (1981) · Histochemistry and Cell Biology · doi:10.1007/bf00517131 · Cited by 24
On the Mechanism of Turnover of the Carboxy-Terminal Tyrosine of the Alpha Chain of Tubulin
Deanin, G. G., Preston, S. F., Hanson, R. K., & Gordon, M. W. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04786.x · Cited by 24
Tau PET Imaging for Staging of Alzheimer's Disease in Down Syndrome
Rafii, M. S. (2018) · Developmental Neurobiology · doi:10.1002/dneu.22658 · Cited by 23
Detecting tau in serum of transgenic animal models after tau immunotherapy treatment
d’Abramo, C., Acker, C. M., Schachter, J. B., Terracina, G., Wang, X., Forest, S. K., & Davies, P. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.09.017 · Cited by 22
Schröder, H. C., Bernd, A., Zahn, R. K., & Müller, W. E. G. (1984) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(84)90178-7 · Cited by 22
Concerning the efficiency of the treadmilling phenomenon with microtubules.
Caplow, M., Langford, G. M., & Zeebèrg, B. R. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33385-4 · Cited by 22
Safinya, C. R., Raviv, U., Needleman, D. J., Zidovska, A., Choi, M. C., Ojeda-López, M. A., Ewert, K. K., Li, Y., Miller, H. P., Quispe, J. D., et al. (2011) · Advanced Materials · doi:10.1002/adma.201004647 · Cited by 21
Jouroukhin, Y., Ostritsky, R., & Gozes, I. (2012) · Journal of Molecular Neuroscience · doi:10.1007/s12031-012-9882-6 · Cited by 20
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
Control of spindle form and function in grasshopper spermatocytes
Marek, L. F. (1978) · Chromosoma · doi:10.1007/bf00327171 · Cited by 20
Tau interacts with SHP2 in neuronal systems and in Alzheimer's disease brains
Kim, Y., Liu, G., Leugers, C. J., Mueller, J. D., Francis, M. B., Hefti, M. M., Schneider, J. A., & Lee, G. S. (2019) · Journal of Cell Science · doi:10.1242/jcs.229054 · 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
Kanagasingam, S., von Ruhland, C. J., Welbury, R. R., & Singhrao, S. K. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220486 · Cited by 17
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
Compartments of tubulin and tubulin-like proteins in differentiating neuroblastoma cells
Chan, K. Y., & Baxter, C. F. (1979) · Brain Research · doi:10.1016/0006-8993(79)90809-6 · Cited by 17
Ijezie, E. C., Miller, M. J., Hardy, C., Jarvis, A. R., Czajka, T. F., D’Brant, L., Rugenstein, N., Waickman, A. T., Murphy, E. A., & Butler, D. C. (2025) · Brain Pathology · doi:10.1111/bpa.70006 · Cited by 20
Recent studies of atomic‐resolution structures of tau protein and structure‐based inhibitors
Zhu, L., & Qian, Z. (2021) · Quantitative Biology · doi:10.15302/j-qb-021-0271 · Cited by 16
Tau in the gut, does it really matter?
Derkinderen, P., Rolli‐Derkinderen, M., Chapelet, G., Neunlist, M., & Noble, W. J. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15320 · Cited by 16
Human Induced Pluripotent Stem Cell Models of Frontotemporal Dementia With Tau Pathology
Kühn, R., Mahajan, A., Canoll, P., & Hargus, G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.766773 · Cited by 18
Structural genomic variations and Parkinson's disease
Bandrés‐Ciga, S., Ruz, C., Barrero, F. J., Sevilla, F. E., Pelegrina, J., Vives, F., & Durán, R. (2017) · Minerva Medica · doi:10.23736/s0026-4806.17.05246-6 · Cited by 16
Carlier, M., Simon, C., & Pantaloni, D. (1984) · Biochemistry · doi:10.1021/bi00302a037 · Cited by 16
Tau here, tau there, tau almost everywhere: Clarifying the distribution of tau in the adult CNS
Kanaan, N. M. (2024) · Cytoskeleton · doi:10.1002/cm.21820 · Cited by 15
Tubulin:tyrosine ligase in oocytes and embryos of Xenopus laevis
Preston, S. F., Deanin, G. G., Hanson, R. K., & Gordon, M. W. (1981) · Developmental Biology · doi:10.1016/0012-1606(81)90345-6 · Cited by 15
Equilibrium components of tubulin preparations
Gethner, J. S., Flynn, G. W., Berne, B. J., & Gaskin, F. (1977) · Biochemistry · doi:10.1021/bi00645a021 · Cited by 15
Microtubule-Tau Interaction as a Therapeutic Target for Alzheimer’s Disease
Ivashko‐Pachima, Y., Zhou, L.-Y., Lei, P., & Gozes, I. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0715-x · Cited by 15
Expression, phosphorylation, localization, and microtubule binding of tau in colorectal cell lines
Huda, M. N., Kim, D. H., Erdene-Ochir, E., Kim, Y. S., & Pan, C. (2016) · Applied Biological Chemistry · doi:10.1007/s13765-016-0228-x · Cited by 14
Sandoval, I. V., & Cuatrecasas, P. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb20947.x · Cited by 13
LaCroix, M., Artikis, E., Hitt, B. D., Beaver, J. D., Estill, S. J., Gleason, K., Tamminga, C. A., Evers, B. M., White, C. L., Caughey, B. W., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105545 · Cited by 11
The C-Terminus of Tau Protein Plays an Important Role in Its Stability and Toxicity
Geng, J., Xia, L., Li, W., & Dou, F. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0314-7 · Cited by 11
Huda, M. N., Erdene-Ochir, E., & Pan, C. (2017) · Journal of Visualized Experiments · doi:10.3791/55932 · Cited by 11
Fellous, A., Prasad, V., Ohayon, R., Jordan, M. A., & Ludueña, R. F. (1994) · Journal of Protein Chemistry · doi:10.1007/bf01901694 · Cited by 11
Application of Immunofluorescence in Studies of Cytoskeletal Antigens
Kalnins, V. I., & Connolly, J. A. (1981) · Advances in cellular neurobiology · doi:10.1016/b978-0-12-008302-2.50015-8 · Cited by 11
Multifactorial etiology of progressive supranuclear palsy (PSP): the genetic component
Müller, U., Höglinger, G. U., & Dickson, D. W. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02898-z · Cited by 10
S, H. S. G. N., Prasanna, V. L., Satish, K. S., Yergolkar, A. V., Krishnamurthy, M., Rajalekshmi, S. G., Radhika, K., & Burri, R. R. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101421 · Cited by 10
Green, L. H., Raff, E. C., & Raff, R. A. (1979) · Insect Biochemistry · doi:10.1016/0020-1790(79)90068-4 · Cited by 10
The Implication of Glial Metabotropic Glutamate Receptors in Alzheimer’s Disease
de Lima, I. B. Q., & Ribeiro, F. M. (2021) · Current Neuropharmacology · doi:10.2174/1570159x20666211223140303 · Cited by 9
Tubulin and the Microtubule System in Cellular Growth and Development
Biswas, B., Banerjee, A. C., & Bhattacharyya, B. (1981) · Springer eBooks · doi:10.1007/978-1-4615-7951-9_3 · Cited by 9
Gaudreault, R., Hervé, V., van de Ven, T. G. M., Mousseau, N., & Ramassamy, C. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201549 · Cited by 8
Mechanism for nucleotide incorporation into steady-state microtubules
Caplow, M., Brylawski, B. P., & Reid, R. C. (1984) · Biochemistry · doi:10.1021/bi00321a071 · Cited by 8
Regulation of Neurodegeneration-associated Protein Fragments by the N-degron Pathways
Eldeeb, M. A., Ragheb, M. A., Soliman, M. H., & Fahlman, R. P. (2022) · Neurotoxicity Research · doi:10.1007/s12640-021-00396-0 · Cited by 9
Gozes, I. (2010) · The EPMA Journal · doi:10.1007/s13167-010-0029-y · Cited by 7
Baas, P. W., & Black, M. M. (1989) · Neuroscience · doi:10.1016/0306-4522(89)90170-x · Cited by 7
Myocardial colchicine-binding proteins: Possible relation to DNA synthesis initiation
Limas, C. (1979) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(79)80001-2 · Cited by 7
Jamison, D., Kadamangudi, S., Tumurbaatar, B., Zhang, W.-R., Palmer, L. K., Kunkel, S., Kayed, R., Limón, A., & Taglialatela, G. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251352382 · Cited by 5
Akbari, V., Bahramikia, S., Jalalvand, A. R., Mehrabi, M., Ezati, M., & Khodarahmi, R. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2273433 · Cited by 6
E3 ligase Praja1 mediates ubiquitination and degradation of microtubule‐associated protein tau
Aoki, S., Onodera, W., Takashima, A., Kawasaki, K., Imadegawa, K., Kurahashi, H., Oishi, M., Asahi, T., & Soeda, Y. (2025) · FEBS Journal · doi:10.1111/febs.70303 · Cited by 6
Traveling the tau pathway: A personal account
Kosik, K. S. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s327 · Cited by 6
Yu, D., Feinstein, S. C., & Valentine, M. T. (2015) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2015.09.043 · Cited by 6
Cook, B. M., Proctor, D. A., Bromberg, R., LaPointe, N. E., Feinstein, S. C., & Wilson, L. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.003 · Cited by 5
Fosket, D. E., Morejohn, L. C., & Westerling, K. E. (1981) · Proceedings in life sciences · doi:10.1007/978-3-642-68035-9_18 · Cited by 5
The contribution of N-terminally modified amyloid beta to the etiology of Alzheimer's disease
Wittnam, J. L. (2012) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3182 · Cited by 5
R ole of Tau, a microtubule associated protein, in Drosophila photoreceptor morphogenesis
Nam, S. (2016) · genesis · doi:10.1002/dvg.22966 · Cited by 4
Sun, Y., Li, C., Wang, J., & Shi, H. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202300868 · Cited by 4
Müller, W. E. G., Bernd, A., & Schröder, H. C. (1983) · Springer eBooks · doi:10.1007/978-1-4613-3879-6_12 · Cited by 4
Microtubules in the Nervous System
Soifer, D., & Mack, K. (1984) · Springer eBooks · doi:10.1007/978-1-4684-4586-2_10 · Cited by 4
Russotto, A., Longobardi, A., Ciullini, A., Cazzaniga, F. A., Bacınoğlu, M. B., Borroni, B., Ghidoni, R., Moda, F., & Saraceno, C. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-07471-6 · Cited by 5
Polymerization of recombinant tau core fragments in vitro and seeding studies in cultured cells
Paterno, G., Bell, B. M., Riley-DiPaolo, A., LaVoie, M. J., & Giasson, B. I. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1268360 · Cited by 3
Relave, E. T., Hedna, R., Maio, A. D., Devred, F., Kovacic, H., Robin, M., & Breuzard, G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111785 · Cited by 3
Optimization and Biodistribution of [11C]-TKF, An Analog of Tau Protein Imaging Agent [18F]-THK523
Kong, Y., Guan, Y., Hua, F., Zhang, Z., Lu, X., Zhu, T., Zhao, B., Zhu, J., Li, C., & Chen, J. (2016) · Molecules · doi:10.3390/molecules21081019 · Cited by 3
THE BIOLOGICAL REGULATION OF MICROTUBULE ASSEMBLY AND FUNCTION
Lockwood, A. H. (1978) · Elsevier eBooks · doi:10.1016/b978-0-12-217850-4.50029-0 · Cited by 3
Dependence on the order of addition of MAPs and GTP for microtubule assembly
Dhalla, S. S., Sharma, R. K., & Wang, J. H.-C. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80614-x · Cited by 3
A strongly basic protein of the MAP2 family copolymerizes with tubulin and induces polymerization
Nguyen, M., & Fasold, H. (1991) · Journal of Protein Chemistry · doi:10.1007/bf01025479 · Cited by 3
Tubulin Synthesis during the Cell Cycle
Bird, R. C., Zimmerman, S. B., & Zimmerman, A. M. (1980) · Elsevier eBooks · doi:10.1016/b978-0-12-747750-3.50013-2 · Cited by 3
Seed-competent tau monomer initiates pathology in PS19 tauopathy micePreprint
Mirbaha, H., Chen, D., Mullapudi, V., Terpack, S. J., White, C. L., Joachimiak, Ł. A., & Diamond, M. I. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.03.474806 · Cited by 3
Rierola, M., Trushina, N. I., Monteiro-Abreu, N., Conze, C., Holtmannspötter, M., Kurre, R., Holzer, M., Arendt, T., Heinisch, J. J., Brandt, R., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.09.495530 · Cited by 4
Rahman, M., Sharma, P., Chattopadhyay, T., & Saroja, S. R. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108396 · Cited by 2
Regulation of Tubulin Expression in Brain
Morrison, M. R., & Griffin, W. S. T. (1986) · Springer eBooks · doi:10.1007/978-1-4613-2151-4_10 · Cited by 2
Chlamydomonas ciliary central apparatus
Witman, G. B., & Mitchell, D. R. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-822508-0.00016-2 · Cited by 2
Self-citationASPECTS OF THE IN VITRO TUBULIN POLYMERIZATION
Maccioni, R. B., Vera, J. C., & Slebe, J. C. (1981) · Elsevier eBooks · doi:10.1016/b978-0-12-641820-0.50016-9 · Cited by 2
Bachmann, S., Bell, M., Klimek, J., & Zempel, H. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.16.154757 · Cited by 2
Needs, H. I., Wilkinson, K. A., Henley, J. M., & Collinson, I. R. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.30.518502 · Cited by 2
Murthy, M. N., & Shyamala, B. V. (2023) · Journal of Complementary and Alternative Medical Research · doi:10.9734/jocamr/2023/v22i3461 · Cited by 1
Phospho-Tau Signature During Mitosis: AT8, p-T217 and p-S422 as Key Phospho-Epitopes
Goussard, M., Zarka, K., Denus, M., Curel, T., Claeysen, S., Lefebvre, B., Hamdane, M., Marin, P., Villeneuve, J., & Parmentier, M. (2025) · Cells · doi:10.3390/cells14201638 · Cited by 1
Tau and amyloid-β imaging with proteomics and genomics
Chinnathambi, S., Baisya, U., & Ananthanarayana, V. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.02.009 · Cited by 1
Pathogenesis of neurodegenerative diseases via templated recruitment
Guo, J. (2013) · ScholarlyCommons (University of Pennsylvania) · Cited by 1
The Tau-Induced Reduction of mRNA Levels of Kv Channels in Human Neuroblastoma SK-N-SH Cells
Hu, X.-M., Li, X., & Li, X. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0683-6 · Cited by 1
Tau in Tauopathies That Leads to Cognitive Disorders and in Cancer
Huda, M. N., & Pan, C. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.74025 · Cited by 1
Bioelectrochemistry for various facets of tau protein biochemistry
Lewis, T., Vargas, A., & Martić, S. (2021) · Current Opinion in Electrochemistry · doi:10.1016/j.coelec.2021.100915 · Cited by 1
Genetic Characterisation of Neurodegenerative disorders
Fung, H. (2007) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 1
Pelvat, P. B., & de Haller, G. (1984) · Archiv für Protistenkunde · doi:10.1016/s0003-9365(84)80009-3 · Cited by 1
Metadata
- Authors
- Witman, G. B., Cleveland, D. W., Weingarten, M. D., & Kirschner, M. W.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1976-11
- Volume
- 73
- Issue
- 11
- Pages
- 4070-4074
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC431332
- OpenAlex
- W1996731829
- Cited by
- 238
- References
- 27
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 4 · 2023: 11 · 2022: 11 · 2021: 18 · 2020: 8 · 2019: 10 · 2018: 10 · 2017: 8 · 2016: 12 · 2015: 10 · 2014: 10 · 2013: 10 · 2012: 6
- FWCI
- 7.58
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Keywords
- tubulin, tau protein, microtubule growth, flagellar microtubules, microtubule assembly, microtubule-associated proteins
- MeSH terms
- Animals, Flagella, Glycoproteins, Kinetics, Microscopy, Electron, Microtubules, Molecular Weight, Proteins, Tubulin
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