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Tau Protein and Neurodegeneration
Michel Goedert. Alzheimer s & Dementia, 2025-12-01
Topic: Brain proteins, microglia and lab models
The different Alzheimer and Pick tau folds establish the existence of molecular conformers of assembled tau. Even though tau filaments from the brains of individuals with chronic traumatic encephalopathy (CTE) are also made of all six brain tau isoforms, the CTE fold is distinct from the Alzheimer fold. Sporadic four-repeat tauopathies can be divided into those with four-layered structures (corticobasal degeneration and argyrophilic grain disease) and those with three-layered structures (progressive supranuclear palsy and globular glial tauopathy). It is also possible to identify new disease entities (limbic-predominant neuronal inclusion body four-repeat tauopathy) through their distinct folds. Each sporadic tauopathy has a specific fold, but several diseases can share a given fold. To study mechanisms of disease, we are attempting to form the human disease folds in the test tube. Known structures of tau filaments assembled in vitro and in vivo are different from those found in the human brain. So far, we have managed to form the Alzheimer fold following the assembly of truncated or modified full-length human tau.
Key findings
- The different Alzheimer and Pick tau folds establish the existence of molecular conformers of assembled tau.
- Even though tau filaments from the brains of individuals with chronic traumatic encephalopathy (CTE) are also made of all six brain tau isoforms, the CTE fold is distinct from the Alzheimer fold.
- Sporadic four-repeat tauopathies can be divided into those with four-layered structures (corticobasal degeneration and argyrophilic grain disease) and those with three-layered structures (progressive supranuclear palsy and globular glial tauopathy).
- It is also possible to identify new disease entities (limbic-predominant neuronal inclusion body four-repeat tauopathy) through their distinct folds.
- Each sporadic tauopathy has a specific fold, but several diseases can share a given fold.
Why it matters
This work describes distinct molecular folds of assembled tau in different tauopathies, including Alzheimer's disease, Pick's disease and chronic traumatic encephalopathy. The authors report forming the Alzheimer fold in the test tube from truncated or modified human tau, which is laboratory structural work with no treatment or prevention tested.
Study details
- Evidence strengthLow
How this study scored 35/100
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 (Alzheimer s & Dementia) |
| Journal's citation record | 2 / 4 | Alzheimer s & Dementia: journal h-index 228 (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 | 4 / 5 | 2025 — within 3 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 | 1 / 7 | Cited 1 times (OpenAlex, 2026-10-10) |
| Citations per year | 0 / 5 | 0.3 citations a year over 3 year(s) since 2025 |
| Impact for its field and year | 1 / 6 | Cited 0.5× 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 1 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 4 / 4 | Last-listed author Michel Goedert: h-index 147 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | MRC Laboratory of Molecular Biology: institution h-index 816 (OpenAlex) |
| Multi-centre collaboration | 0 / 3 | OpenAlex lists 1 institution(s) in 1 country — scores zero (affiliation lists can be incomplete) |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 41435142) |
| Free to read | 2 / 2 | Free to read |
| Total | 35 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1002/alz70855_098415
- PubMed: 41435142
- Original source →
- Free full text: Alzheimer s & Dementia →
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. Check the citation against the original before you use it.
APA 7th
Goedert, M. (2025). Tau Protein and Neurodegeneration. Alzheimer s & Dementia. https://doi.org/10.1002/alz70855_098415
Vancouver
Goedert M. Tau Protein and Neurodegeneration. Alzheimer s & Dementia. 2025. doi:10.1002/alz70855_098415. PMID: 41435142.
BibTeX
@article{goedert2025-41435142,
author = {Goedert, Michel},
title = {{Tau Protein and Neurodegeneration}},
journal = {Alzheimer s \& Dementia},
year = {2025},
doi = {10.1002/alz70855_098415},
pmid = {41435142},
url = {https://doi.org/10.1002/alz70855_098415}
}
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