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Is Tau Acetylation a Key to Frontotemporal Lobar Degeneration Diagnosis?
Diana Piotrowska, Irena Matečko‐Burmann, Laia Montoliu‐Gaya, Gunnar Brinkmalm, Henrik Zetterberg. Clinical Chemistry, 2026-07-27
Topic: Brain proteins, microglia and lab models
Tau protein misfolding and deposition in the brain is a common factor across many neurodegenerative diseases, grouped under the term tauopathies. These can be divided into primary tauopathies, where tau is the sole aggregating protein, and secondary tauopathies, in which tau aggregates in response to other disease processes, e.g., amyloid β aggregation. In physiological conditions, tau acts as a stabilizing agent for microtubules; the poly-tubulin cylindrical structures that serve as both part of the cytoskeleton and internal transport tracks inside axons. However, in some conditions, tau detaches from the microtubules and may bind to other strands of tau protein and its fragments, forming oligomers and larger aggregates. This can be the result of a mutation in the microtubule-associated protein tau (MAPT) gene, hyperphosphorylation, or other, not yet known, reasons. Tau fragments are known to be released from neurons and move from the brain interstitial fluid into cerebrospinal fluid (CSF) and across the blood–brain barrier into plasma, where they can be measured as biomarkers. Total-tau (t-tau) and brain-derived-tau are indicators of axonal degeneration, and their high levels in biofluids, in the absence of phosphorylated tau (p-tau) biomarkers, suggest acute neuronal injury, as, for example, in stroke, brain trauma, or Creutzfeldt–Jakob disease. P-tau peptides, such as p-tau181, p-tau217, and p-tau231, are characteristic of Alzheimer disease (AD) pathology. The availability of blood-based biomarkers has changed the field of AD research immensely, enabling ante-mortem diagnosis and classification of patients for involvement into clinical trials of disease-modifying treatments. This, however, is not the case with primary tauopathies, which still lack validated biomarkers.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Piotrowska, D., Matečko‐Burmann, I., Montoliu‐Gaya, L., Brinkmalm, G., & Zetterberg, H. (2026). Is Tau Acetylation a Key to Frontotemporal Lobar Degeneration Diagnosis? Clinical Chemistry. https://doi.org/10.1093/clinchem/hvag090
Vancouver
Piotrowska D, Matečko‐Burmann I, Montoliu‐Gaya L, Brinkmalm G, Zetterberg H. Is Tau Acetylation a Key to Frontotemporal Lobar Degeneration Diagnosis? Clinical Chemistry. 2026. doi:10.1093/clinchem/hvag090. PMID: 42504910.
BibTeX
@article{piotrowska2026-42504910,
author = {Piotrowska, Diana and Matečko‐Burmann, Irena and Montoliu‐Gaya, Laia and Brinkmalm, Gunnar and Zetterberg, Henrik},
title = {{Is Tau Acetylation a Key to Frontotemporal Lobar Degeneration Diagnosis?}},
journal = {Clinical Chemistry},
year = {2026},
doi = {10.1093/clinchem/hvag090},
pmid = {42504910},
url = {https://doi.org/10.1093/clinchem/hvag090}
}
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. Check the citation against the original before you use it.
Key findings
- This can be the result of a mutation in the microtubule-associated protein tau (MAPT) gene, hyperphosphorylation, or other, not yet known, reasons.
Why it matters
This paper discusses how tau protein misfolds and aggregates in tauopathies, including frontotemporal lobar degeneration, and how tau fragments released from neurons can be measured in cerebrospinal fluid and plasma as biomarkers. It raises the question of whether tau acetylation could be key to diagnosing frontotemporal lobar degeneration, but the text provided does not report a study result or a new treatment for Alzheimer's disease.
New to this subject? Start with our plain-English guide: Blood tests & biomarkers →
Study details
- Evidence strengthLow
How this study scored 37/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomized / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Clinical Chemistry) |
| Journal's citation record | 3 / 4 | Clinical Chemistry: journal h-index 323 (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 | 5 / 5 | 2026 — within 1 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) |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 0 / 7 | Cited 0 times (OpenAlex, 2026-10-10) |
| Citations per year | 0 / 5 | 0.0 citations a year over 2 year(s) since 2026 |
| Impact for its field and year | 0 / 6 | Cited 0.0× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 0 / 6 | No other study in this library cites it |
| Still being cited | 0 / 4 | Cited 0 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 4 / 4 | Last-listed author Henrik Zetterberg: h-index 196 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | University College London: institution h-index 2,029 (OpenAlex) |
| Multicenter collaboration | 3 / 3 | OpenAlex lists 11 institution(s) in 5 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 42504910) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 37 / 100 | — |
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