The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
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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Iqbal, K., & Grundke, I. (1994) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4615-8149-9_5
Nordmeyer, P. J. (2015) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-5124
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Behrendt, M. G. (2012) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.14767
Geddes, J. W., & Matus, A. I. (1997) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60052-8
Murtishaw, A. S. (2020) · Digital Scholarship - UNLV (University of Nevada Reno) · doi:10.34917/6456429
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Kanai, Y., Takemura, R., & Hirokawa, N. (1990) · Neuroscience Research Supplements · doi:10.1016/0921-8696(90)90688-y
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Rothenberg, K. G., Siedlak, S. L., Lee, H., Zhu, X., Perry, G. L., & Smith, M. A. (2011) · Future Neurology · doi:10.2217/fnl.10.81
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Orr, M. E. (2012) · Montana State University ScholarWorks (Montana State University)
Kosik, K. S., & Selkoe, D. J. (1989) · Springer eBooks · doi:10.1007/978-3-642-46690-8_4
depression in the hippocampus Microtubule-associated protein tau is essential for long-term
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Hua, Q., He, R., Haque, N., & Iqbal, K. (2003)
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Monplaisir, K. M. (2016) · Human Biology
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May, S. E. (2018) · Digital Commons - URI (University of Rhode Island) · doi:10.23860/diss-may-shannon-2018
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Moussa, C. (2019) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-030-05067-2_10
Alves, S. S. (2019) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.17.2019.tde-30052019-164627
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Sandberg, A. (2019) · Linköping studies in science and technology. Dissertations · doi:10.3384/diss.diva-161659
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Wang, S., Jiang, Y. X., Liu, Y., Liu, Q., Sun, H., Mei, M., & Liao, X. (2021) · Research Square · doi:10.21203/rs.3.rs-1062929/v1
Obrenovich, M. E., Raina, A. K., Ogawa, O., Atwood, C., Morelli, L., & Smith, M. A. (2007) · Springer eBooks · doi:10.1007/0-387-29390-6_6
Siman, R., & Greenberg, B. (1996) · Humana Press eBooks · doi:10.1007/978-1-59259-466-5_10
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Zampar, S. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9004
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Nielsen, J. E. (2021) · VBN Forskningsportal (Aalborg Universitet) · doi:10.54337/aau455017331
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Paul, B. D. (2022) · Wiley eBooks · doi:10.1002/9781119799900.ch18
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Beaudet, D., Berger, C. L., & Hendricks, A. G. (2026) · eLife · doi:10.7554/elife.110011.3
Amyloid β Deposition, Tau Phosphorylation, ApoE4 Dysfunction, and Formaldehyde
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Criado‐Marrero, M., Gebru, N. T., Blazier, D. M., Gould, L. A., Baker, J. D., Beaulieu‐Abdelahad, D., & Blair, L. J. (2021) · Figshare · doi:10.6084/m9.figshare.14391487
Chang, Y.-L., Yang, C.-C., Huang, Y.-Y., Chen, Y.-A., Yang, C.-W., Liao, C.-Y., Li, H., Wu, C.-S., Lin, C.-H., & Teng, S.-C. (2024) · Figshare · doi:10.6084/m9.figshare.24864323
Beaudet, D., Berger, C. L., & Hendricks, A. G. (2026) · eLife · doi:10.7554/elife.110011
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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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