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
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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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