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An unbiased approach to identifying tau kinases that phosphorylate tau at sites associated with Alzheimer disease
Cavallini A, Brewerton S, Bell A, Sargent S, Glover S, Hardy C, Moore R, Calley J et al.. The Journal of biological chemistry, 2013-06-24
Topic: Amyloid, tau and blood-test diagnosis
Neurofibrillary tangles, one of the hallmarks of Alzheimer disease (AD), are composed of paired helical filaments of abnormally hyperphosphorylated tau. The accumulation of these proteinaceous aggregates in AD correlates with synaptic loss and severity of dementia. Identifying the kinases involved in the pathological phosphorylation of tau may identify novel targets for AD.
Key findings
- The accumulation of these proteinaceous aggregates in AD correlates with synaptic loss and severity of dementia.
- Identifying the kinases involved in the pathological phosphorylation of tau may identify novel targets for AD.
- We used an unbiased approach to study the effect of 352 human kinases on their ability to phosphorylate tau at epitopes associated with AD.
- The kinases were overexpressed together with the longest form of human tau in human neuroblastoma cells.
Why it matters
This laboratory study used an unbiased approach to screen 352 human kinases for their ability to phosphorylate tau at sites associated with Alzheimer disease, in order to identify possible targets. It is early cell-based work and does not test any treatment, cure, or prevention in people.
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Study details
- Evidence strengthLow
How this study scored 44/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (The Journal of biological chemistry) |
| Journal's citation record | 4 / 4 | Journal of Biological Chemistry: journal h-index 780 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 1 / 5 | 2013 — within 20 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 133 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 8.9 citations a year over 15 year(s) since 2013 |
| Impact for its field and year | 3 / 6 | Cited 4.9× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 2 other studies in this library |
| Still being cited | 2 / 4 | Cited 36 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Suchira Bose: h-index 24 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | Albert Einstein College of Medicine: institution h-index 973 (OpenAlex) |
| Multi-centre collaboration | 2 / 3 | OpenAlex lists 5 institution(s) in 3 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 23798682) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 44 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m113.463984
- PubMed: 23798682
- Original source →
- Free full text: Journal of Biological Chemistry →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record's author list ends in “et al.”, so not every author is named. Check the citation against the original before you use it.
APA 7th
Cavallini, A., Brewerton, S., Bell, A., Sargent, S., Glover, S., Hardy, C., et al. (2013). An unbiased approach to identifying tau kinases that phosphorylate tau at sites associated with Alzheimer disease. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m113.463984
Vancouver
Cavallini A, Brewerton S, Bell A, Sargent S, Glover S, Hardy C, et al. An unbiased approach to identifying tau kinases that phosphorylate tau at sites associated with Alzheimer disease. The Journal of biological chemistry. 2013. doi:10.1074/jbc.m113.463984. PMID: 23798682.
BibTeX
@article{cavallini2013-23798682,
author = {Cavallini, A. and Brewerton, S. and Bell, A. and Sargent, S. and Glover, S. and Hardy, C. and Moore, R. and Calley, J. and others},
title = {{An unbiased approach to identifying tau kinases that phosphorylate tau at sites associated with Alzheimer disease}},
journal = {The Journal of biological chemistry},
year = {2013},
doi = {10.1074/jbc.m113.463984},
pmid = {23798682},
url = {https://doi.org/10.1074/jbc.m113.463984}
}
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