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Phosphorylation affects the ability of tau protein to promote microtubule assembly.
Open accessAbstract
Tau is a family of closely related proteins known for its ability to copolymerize with tubulin, inducing the formation of microtubules. When tau was stripped of phosphate by treatment with alkaline phosphatase it underwent a pronounced change in electrophoretic mobility, probably reflecting a conformational change. The dephosphorylated tau promoted significantly more rapid and more extensive polymerization of microtubules though there was no obvious difference in the microtubules formed. Partially purified microtubule protein contains a kinase that can rephosphorylate tau.
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In the citing paper
“Tau hyperphosphorylation reduces its ability to stabilize microtubules [3–5]”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [3]
In the citing paper
“In addition, phosphorylation of Tau reduces its ability to bind and stabilize microtubules [3–5].”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [3]
In the citing paper
“Tau’s function and microtubule affinity are modulated by alternative splicing (Kellogg et al., 2018; McVicker et al., 2014) and phosphorylation, both of which play key roles in normal development and pathology”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Lindwall and Cole, 1984
In the citing paper
“Tau is phosphorylated at numerous residues and at different developmental stages, and individual tau molecules often exhibit heterogeneous phosphorylation patterns”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Lindwall and Cole, 1984
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
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
Microtubule 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
Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915
Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881
Vallee, R. B. (1982) · The Journal of cell biology · doi:10.1083/jcb.92.2.435 · Cited by 551
Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein.
Sloboda, R. D., Rudolph, S. A., Rosenbaum, J. L., & Greengard, P. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.177 · Cited by 547
Theurkauf, W. E., & Vallee, R. B. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81107-9 · Cited by 333
Nucleated 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
Research works printed but not linked: 1
- Walter, 1978, J. Cyclic Nucleotide Res., 4, 437
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Gozes, I. (2010) · The EPMA Journal · doi:10.1007/s13167-010-0029-y · Cited by 7
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Ko, L., Liu, W.-K., Georgieff, I. S., & Yen, S.-H. C. (1996) · Brain Research · doi:10.1016/0006-8993(95)01268-0 · Cited by 7
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Ferreira, J. D. S., Guilhermino, M. M., Leite, J. H. G. M., Chaves, D. F., do Vale, A., Silveira, R. M. F., Costa, W. P., Facó, O., & Façanha, D. A. E. (2019) · Biological Rhythm Research · doi:10.1080/09291016.2019.1628393 · Cited by 5
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Shea, T. B. (1996) · Neuroscience Research Communications · doi:10.1002/(sici)1520-6769(199607)19:1 · Cited by 5
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Dickson, D. W., Ksiȩżak-Reding, H., Crowe, A., & Yen, S.-H. C. (1987) · Advances in behavioral biology · doi:10.1007/978-1-4613-1657-2_12 · Cited by 5
Haque, N., Denman, R. B., Merz, G., Grundke, I., & Iqbal, K. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00089-r · Cited by 5
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Willer, B. S., Haider, M. N., Wilber, C., Esopenko, C., Turner, M., & Leddy, J. J. (2020) · Clinics in Sports Medicine · doi:10.1016/j.csm.2020.08.012 · Cited by 4
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Baudier, J., & Cole, R. D. (1987) · Advances in behavioral biology · doi:10.1007/978-1-4613-1657-2_2 · Cited by 4
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Olesen, M. A., Ancía, A., & Quintanilla, R. A. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.168059 · Cited by 3
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Weeks, R. D., Banack, S. A., Howell, S., Thunga, P., Metcalf, J. S., Green, A. J., Cox, P. A., & Planchart, A. (2023) · Neurotoxicity Research · doi:10.1007/s12640-023-00658-z · Cited by 3
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Yang, Z. W., & Babitch, J. A. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb02860.x · Cited by 3
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Harris, R. A. (2017) · Scholarship@Western (Western University) · Cited by 3
Nagaratnam, N., Nagaratnam, K., & Cheuk, G. (2017) · Springer eBooks · doi:10.1007/978-3-319-32700-6_71-1 · Cited by 3
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Riederer, B. M. (1995) · Advances in molecular and cell biology · doi:10.1016/s1569-2558(08)60261-1 · Cited by 3
Bershadsky, A. D., & Vasiliev, J. M. (1988) · Springer eBooks · doi:10.1007/978-1-4684-5278-5_3 · Cited by 3
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Ávila, J., Correas, I., de Ancos, J. G., Ledesma, D., Ulloa, L., de Garcini, E. M., & Díaz‐Nido, J. (1993) · Elsevier eBooks · doi:10.1016/b978-0-444-81470-8.50010-7 · Cited by 3
Microtubule dynamics and morphogenesis in Paramecium
Laurent, M., & Fleury‐Aubusson, A. (1996) · European Journal of Protistology · doi:10.1016/s0932-4739(96)80049-6 · Cited by 3
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Sajeevan, B., Gopika, M. G., Sreelekshmi, S., Rejithamol, R., Antherjanam, S., & Saraswathyamma, B. (2023) · Wiley eBooks · doi:10.1002/9781394167135.ch11 · Cited by 3
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Price, T. M., Tucker, A. E., & Funk, K. E. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103223 · Cited by 2
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Beheshti, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815854-8.00035-5 · Cited by 2
Wu, G., Luo, Y., Guo, Q., Yang, M., Mahaman, Y. A. R., Liu, Y., Wang, J., Liu, R., Gao, X., & Wang, X. (2024) · Journal of Alzheimer s Disease · doi:10.1177/13872877241307341 · Cited by 2
Shahwan, M. J., Yadav, D. K., Khan, M. S., Choudhury, A., Shamsi, A., Hassan, M. I., & Anwar, S. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142812 · Cited by 2
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Tam, J. H. K., & Pasternak, S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801942-9.00004-5 · Cited by 2
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Raxworthy, M. J. (1988) · Biochemical Education · doi:10.1016/0307-4412(88)90003-9 · Cited by 2
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Iqbal, K. (1986) · Neurobiology of Aging · doi:10.1016/0197-4580(86)90057-6 · Cited by 2
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Brisch, E., Ahrens, D. P., & Suprenant, K. A. (1999) · Journal of Experimental Zoology · doi:10.1002/(sici)1097-010x(19990215)283:3 · Cited by 2
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Sadananda, A., & Ray, K. (2012) · Journal of Neurogenetics · doi:10.3109/01677063.2012.699564 · Cited by 2
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Sahu, K. K., Chaudhary, R., Farooqi, M. A., & Kaurav, M. (2024) · Drug Delivery Letters · doi:10.2174/0122103031331346241122152643 · Cited by 1
Riemann, K., von Ahsen, J., Böhm, T., Schlegel, M., Kreuzer, M., Fenzl, T., Russ, H., Parsons, C. G., & Rammes, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094167 · Cited by 1
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Donison, N. S., Palik, J., Hintermayer, M. A., Volkening, K., & Strong, M. J. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02170-1 · Cited by 1
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Yi, M. (2009) · Cited by 1
The Conformations of Tau Protein and its Aggregation into Alzheimer Paired Helical Filaments
Mandelkow�, E., Friedhoff, P., Biernat, J., & Mandelkow, E. (1998) · Advances in behavioral biology · doi:10.1007/978-1-4615-5337-3_32 · Cited by 1
Cerebrospinal Fluid Based Diagnosis in Alzheimer’s Disease
Zerr, I., Kaerst, L., Gawinecka, J., & Varges, D. (2011) · InTech eBooks · doi:10.5772/16684 · Cited by 1
A dynamic view to the modulation of phosphorylation and O-GlcNAcylation by inhibition of O-GlcNAcase
Tang, C., & Welty, D. F. (2013) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2013.03.001 · Cited by 1
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Iqbal, K., & Grundke, I. (2007) · Springer eBooks · doi:10.1007/978-0-387-71522-3_14 · Cited by 1
Relation between schizophrenia and Alzheimer's disease: the reelin signaling pathway
Aoki, T., Mizuki, Y., & Terashima, T. (2005) · Psychogeriatrics · doi:10.1111/j.1479-8301.2005.00091.x · Cited by 1
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Lü, J., & He, R. (2017) · Springer eBooks · doi:10.1007/978-94-024-1177-5_9 · Cited by 1
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Radiographic interpretation of unilocular radiolucent mandibular lesions.
Raitz, R., Côrrea, L., & Fenyo-Pereira, M. (2009) · PubMed · Cited by 1
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Wolfe, M. S. (2016) · Topics in medicinal chemistry · doi:10.1007/7355_2016_14 · Cited by 2
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Huda, M. N., & Pan, C. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.74025 · Cited by 1
Tau, Tangles and Tauopathies: Insights from Drosophila Disease Models
Nisha, N., Pragati, Tandon, S., Aqsa, A., Aggarwal, P., & Sarkar, S. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_8 · 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
Delacourte, A., Sergeant, N., & Buée, L. (2009) · Humana Press eBooks · doi:10.1007/978-1-59745-336-3_20 · Cited by 1
The Expression of Microtubule Proteins During the Development of the Nervous System
Ginzburg, I., & Littauer, U. Z. (1986) · Topics in the neurosciences · doi:10.1007/978-1-4613-2321-1_8 · Cited by 1
Kincaid, R. L. (1995) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-79423-0_9 · Cited by 1
Sparkman, D. R. (1992) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(92)90042-c · Cited by 1
Lovestone, S. (1996) · International Journal of Geriatric Psychiatry · doi:10.1002/(sici)1099-1166(199604)11:4 · Cited by 1
Tau and α-Synuclein in Neurodegenerative Diseases
Giasson, B. I., Wilson, C., Trojanowski, J. Q., & Lee, V. M. ‐. (2001) · Humana Press eBooks · doi:10.1007/978-1-59259-006-3_7 · Cited by 1
Lövestam, S., Wagstaff, J. L., Katsinelos, T., Shi, J., Freund, S. M. V., Goedert, M., & Scheres, S. H. W. (2025) · eLife · doi:10.7554/elife.104778.3 · Cited by 1
Neurodegenerative Disorders with Tauopathies: Mad Tau Diseases?
Buée, L., Vanbesien-Mailliot, C., Bussière, T., Sergeant, N., Buée‐Scherrer, V., Hof, P. R., Flament, S., & Delacourte, A. (2000) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-662-04056-0_8 · Cited by 1
Metadata
- Authors
- Lindwall, G., & Cole, R. D.
- Affiliations
- University of California, Berkeley (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1984-04
- Volume
- 259
- Issue
- 8
- Pages
- 5301-5305
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1481130297
- Cited by
- 901
- References
- 33
- Citations by year
- 2026: 8 · 2025: 27 · 2024: 19 · 2023: 28 · 2022: 38 · 2021: 41 · 2020: 40 · 2019: 39 · 2018: 25 · 2017: 25 · 2016: 31 · 2015: 18 · 2014: 18 · 2013: 23 · 2012: 26
- FWCI
- 13.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tau protein, phosphorylation, microtubule assembly, dephosphorylation, alkaline phosphatase, protein conformational change, electrophoretic mobility
- MeSH terms
- Alkaline Phosphatase, Animals, Brain, Cattle, Kinetics, Microscopy, Electron, Microtubules, Nerve Tissue Proteins, Phosphorylation, Proteins, Tubulin, tau Proteins, Macromolecular Substances
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