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.
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“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]
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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
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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. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.16.618683 · Cited by 1
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Gozes, I. (2012) · Advances in predictive, preventive and personalised medicine · doi:10.1007/978-94-007-5866-7_5
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Hargreaves, A. J. (2016) · Liverpool John Moores University · doi:10.24377/ljmu.t.00005128
Bryan, J., & Nagle, B. W. (1978) · Elsevier eBooks · doi:10.1016/b978-0-12-217850-4.50026-5
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Yakubu, A. O., Atafo, G. I., Nwaze, C. E., Bakare, T. Y., Adeniyi, T. O., Alare, K., Oladele, A. B., & Solagbade, O. S. (2026) · NeuroMarkers. · doi:10.1016/j.neumar.2026.100167 · Cited by 1
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Barbereau, C. (2020) · theses.fr (ABES) · doi:10.70675/dfe1802ez70f2z4da6zb3e5z63d1de7a429c
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Danis, C. (2018) · theses.fr (ABES) · doi:10.70675/c783a062zb57bz4024z85d0z509baaed8a1b
Lipka, J., Shan, X., Zhang, Q., Dutka, P., Phu, L., Johnson, M. C., Wendorff, T. J., Adrian, M., Biton, A., Sun, D., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.07.749799
Modifications of the tau protein and their varied effects on aggregation and function
Combs, B. (2013) · KU ScholarWorks (The University of Kansas)
DNA Replication and the Cell Cycle
Herman, R. H. (1980) · Springer eBooks · doi:10.1007/978-1-4613-3006-6_7
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
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