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Tau proteotasis in Alzheimer's disease
Subashchandrabose Chinnathambi. Advances in protein chemistry and structural biology, 2024-10-02
Topic: Disease mechanisms in lab and animal studies
Tau protein accumulation is one of the characteristic features of Alzheimer's disease (AD). Their accumulation is driven by the formation of intermediate toxic oligomers of Tau to the highly ordered neurofibrillary tangles. Cellular machineries engage different types of proteins such as, chaperone-co-chaperones complex, ubiquitin, kinases, proteases etc., to clear the aberrantly accumulated Tau protein which otherwise would cause neuronal death. In the milieu of proteotoxicity, it would be significant for the cell to follow a specific path for Tau clearance. Under this circumstance, cells express key proteins and other accessory proteins specific to the pathway. This is known to be dependent on the post-translational modifications and mutations associated with Tau. The processes involved maintenance of proteins homeostasis in cells collectively called proteostasis. The proteostasis involve the synthesis of proteins by ribosomes, protein folding mostly by chaperons and the degradation of improperly folded or unwanted proteins. Autophagy is the mechanism to eradicate unwanted, non-functional and toxic proteins from the cell. Proteostasis plays a pivotal role in maintaining the normal cellular environment in the expense of considerable amount of energy. AD is the prevalent type of dementia associated with aging, which is characterized by aggregation of Tau.
Key findings
- In the milieu of proteotoxicity, it would be significant for the cell to follow a specific path for Tau clearance.
- This is known to be dependent on the post-translational modifications and mutations associated with Tau.
- AD is the prevalent type of dementia associated with aging, which is characterized by aggregation of Tau.
Study details
- Evidence strengthLow
How this study scored 43/100
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. We have no data on journal's citation record, times cited, citations per year, impact for its field and year, cited by studies here, still being cited, senior author's track record, institution's track record, multi-centre collaboration and free to read, so those were left out: it earned 24 of the 56 points we could judge it on, which is 43 out of 100.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Advances in protein chemistry and structural biology) |
| Journal's citation record | — / 4 | No journal record from OpenAlex — left out of this score |
| 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 | — / 7 | No citation count (not found in OpenAlex) — left out of this score |
| Citations per year | — / 5 | No citation count or no year — left out of this score |
| Impact for its field and year | — / 6 | No field-weighted citation impact (OpenAlex has none yet) — left out of this score |
| Cited by studies here | — / 6 | Not yet checked against this library's citation graph — left out of this score |
| Still being cited | — / 4 | No yearly citation counts — left out of this score |
| Senior author's track record | — / 4 | Senior author's record not available — left out of this score |
| Institution's track record | — / 3 | No institution listed in OpenAlex — left out of this score |
| Multi-centre collaboration | — / 3 | Institutions not listed — left out of this score |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 40973404) |
| Free to read | — / 2 | Access not recorded — left out of this score |
| Points | 24 / 56 | Scored on 10 of 20 parts. We have no data for the rest, so they are left out: 24 of the 56 points we could judge it on is 43 out of 100. |
| Total | 43 / 100 | — |
What each of these 20 components measures, and what this score is not →
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Cite this study APA, Vancouver, BibTeX · download .bib or .ris
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APA 7th
Chinnathambi, S. (2025). Tau proteotasis in Alzheimer's disease. Advances in protein chemistry and structural biology. https://doi.org/10.1016/bs.apcsb.2024.09.003
Vancouver
Chinnathambi S. Tau proteotasis in Alzheimer's disease. Advances in protein chemistry and structural biology. 2025. doi:10.1016/bs.apcsb.2024.09.003. PMID: 40973404.
BibTeX
@article{chinnathambi2025-40973404,
author = {Chinnathambi, Subashchandrabose},
title = {{Tau proteotasis in Alzheimer's disease}},
journal = {Advances in protein chemistry and structural biology},
year = {2025},
doi = {10.1016/bs.apcsb.2024.09.003},
pmid = {40973404},
url = {https://doi.org/10.1016/bs.apcsb.2024.09.003}
}
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