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BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein
Elliott E, Tsvetkov P, Ginzburg I.. The Journal of biological chemistry, 2007-10-22
Topic: Brain proteins, microglia and lab models
Intraneuronal accumulation of phosphorylated Tau protein is a molecular pathology found in many forms of dementia, including Alzheimer disease. Research into possible mechanisms leading to the accumulation of modified Tau protein and the possibility of removing Tau protein from the system have revealed that the chaperone protein system can interact with Tau and mediate its degradation. Hsp70/Hsc70, a member of the chaperone protein family, interacts with Tau protein and mediates proper folding of Tau and can promote degradation of Tau protein under certain circumstances.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Elliott, E., Tsvetkov, P., & Ginzburg, I. (2007). BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m706379200
Vancouver
Elliott E, Tsvetkov P, Ginzburg I. BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein. The Journal of biological chemistry. 2007. doi:10.1074/jbc.m706379200. PMID: 17954934.
BibTeX
@article{elliott2007-17954934,
author = {Elliott, E. and Tsvetkov, P. and Ginzburg, I.},
title = {{BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein}},
journal = {The Journal of biological chemistry},
year = {2007},
doi = {10.1074/jbc.m706379200},
pmid = {17954934},
url = {https://doi.org/10.1074/jbc.m706379200}
}
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
- Research into possible mechanisms leading to the accumulation of modified Tau protein and the possibility of removing Tau protein from the system have revealed that the chaperone protein system can interact with Tau and mediate its degradation.
- Hsp70/Hsc70, a member of the chaperone protein family, interacts with Tau protein and mediates proper folding of Tau and can promote degradation of Tau protein under certain circumstances.
- However, because Hsp70/Hsc70 has many binding partners that can mediate its activity, there is still much to discover about how Hsp70 acts in vivo to regulate Tau protein.
- BAG-1, an Hsp70/Hsc70 binding partner, has been implicated as a mediator of neuronal function.
Why it matters
This laboratory study examined how BAG-1 associates with the Hsc70.Tau complex and regulates proteasomal degradation of Tau protein. It is basic molecular research and does not test any treatment, cure, or prevention in people.
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Study details
- Evidence strengthLow
How this study scored 40/100
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 | 2007 — 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 114 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 5.4 citations a year over 21 year(s) since 2007 |
| Impact for its field and year | 3 / 6 | Cited 5.5× 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 | 1 / 4 | Cited 9 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Irith Ginzburg: h-index 35 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | Weizmann Institute of Science: institution h-index 1,080 (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 17954934) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 40 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m706379200
- PubMed: 17954934
- 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).
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