The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments.
Open accessAbstract
Brain proline-directed protein kinase (BPDK), which contains a catalytic subunit homologous to and displaying site-specific phosphorylation similar to p34cdc2 kinase (Lew, J., Winkfein, R. J., Paudel, H. K., and Wang, J. H. (1992) J. Biol. Chem. 267, 25922-25926), has been examined for possible involvement in tau phosphorylation. Immunoblot analyses using peptide antibodies specific for BPDK have revealed the presence of the kinase in bovine brain microtubules purified extensively by repeated polymerization and depolymerization cycles. When the microtubule proteins are separated into the tubulin and microtubule-associated protein fractions, BPDK is found exclusively in the latter fraction. BPDK phosphorylates both tau and MAP2, the former protein being phosphorylated to a stoichiometry of 3.8 mol of phosphate/mol of tau. Analysis of the phosphopeptides isolated from the tryptic digest of the phosphorylated bovine tau has revealed seven phosphorylation sites. Based on the sequence alignment between bovine and human tau proteins, these sites correspond to Ser-195, Ser-202, Thr-205, Thr-231, Ser-235, Ser-396, and Ser-404 of human tau. Mass spectrometric analysis of the tau protein isolated from Alzheimer's paired helical filaments (PHFs) has determined three abnormal phosphorylation sites and two phosphopeptides containing a total of five abnormal phosphates (Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., and Ihara, Y. (1992) J. Biol. Chem. 267, 17047-…
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In the citing paper
“However, without exception, these studies have been carried out in vitro.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]
In the citing paper
“They extend results obtained in vitro [7,12,14] to an in vivo model system, and indicate that GSK3fl may be involved in the phosphorylation of tau in vivo.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]
In the citing paper
“Mitogen-activated protein kinase, glycogen synthase kinase-3 (GSK3) and neuronal cdc2-1ike kinase have been shown to phosphorylate tau protein in vitro at a number of sites that are phosphorylated in PHFs.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]
In the citing paper
“However, since in vitro studies [7,12,14] have demonstrated that tau can be directly phosphorylated by GSK3fl at many of the sites we observed in transfected cells, GSK3fl probably was directly responsible for the increased immunoreactivities and mobility shifts observed here.”
From Glycogen synthase kinase-3β phosphorylates tau protein at multiple sites in intact cells (1995) · cites this paper as [14]
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Patrick, G. N., Zukerberg, L. R., Nikolić, M., de la Monte, S. M., Dikkes, P., & Tsai, L. (1999) · Nature · doi:10.1038/45159 · Cited by 1,541
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Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965
Ohshima, T., Ward, J. M., Huh, C. G., Longenecker, G., Veeranna, Pant, H. C., Brady, R. O., Martin, L. J., & Kulkarni, A. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.11173 · Cited by 897
Tau protein and the neurofibrillary pathology of Alzheimer's disease
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Metadata
- Authors
- Paudel, H. K., Lew, J., Ali, Z., & Wang, J. H.
- Affiliations
- University of Calgary (CA)
- ORCID
- Ali, Z
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-11
- Volume
- 268
- Issue
- 31
- Pages
- 23512-23518
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1568595238
- Cited by
- 285
- References
- 49
- Citations by year
- 2023: 4 · 2022: 3 · 2021: 2 · 2020: 1 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 2 · 2014: 5 · 2013: 7 · 2012: 6
- FWCI
- 12.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau phosphorylation, paired helical filaments, Alzheimer's disease, MAP2, microtubule-associated proteins, phosphorylation sites
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Brain, Cattle, Humans, Microtubule-Associated Proteins, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Phosphoserine, Phosphothreonine, tau Proteins, Protein Serine-Threonine Kinases, Calcium-Calmodulin-Dependent Protein Kinases, Proline-Directed Protein Kinases
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