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Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease
Verdier Y, Penke B.. Current protein & peptide science, 2004-02-01
Topic: Amyloid, tau and blood-test diagnosis
The binding of amyloid beta peptides (Abeta) to plasma membranes appears to be a promising point of intervention in the events leading to the development of Alzheimer's disease (AD). This binding has been studied as regards the direct toxicity of Abeta on neurons, and the activation of a local inflammation phase involving microglia. By virtue of its structure, Abeta is able to bind to a variety of biomolecules, including lipids, proteoglycans and proteins.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Verdier, Y., & Penke, B. (2004). Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease. Current protein & peptide science. https://doi.org/10.2174/1389203043486937
Vancouver
Verdier Y, Penke B. Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease. Current protein & peptide science. 2004. doi:10.2174/1389203043486937. PMID: 14965318.
BibTeX
@article{verdier2004-14965318,
author = {Verdier, Y. and Penke, B.},
title = {{Binding sites of amyloid beta-peptide in cell plasma membrane and implications for Alzheimer's disease}},
journal = {Current protein \& peptide science},
year = {2004},
doi = {10.2174/1389203043486937},
pmid = {14965318},
url = {https://doi.org/10.2174/1389203043486937}
}
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Key findings
- This binding has been studied as regards the direct toxicity of Abeta on neurons, and the activation of a local inflammation phase involving microglia.
- By virtue of its structure, Abeta is able to bind to a variety of biomolecules, including lipids, proteoglycans and proteins.
- This review focuses on the membrane proteins that can mediate the interaction between Abeta and the plasma membranes in AD.
- On neurons, these are APP (amyloid precursor protein), the NMDA-R (N-methyl-D-aspartate receptor), integrins, the alpha7nicotinic acetylcholine receptor (alpha7nAChR), the P75 neurotrophin receptor (P75NTR) and the CLAC-P/collagen type XXV (collagen-like Alzheimer amyloid plaque component precursor/collagen XXV).
Why it matters
This review focuses on membrane proteins that can mediate the interaction between amyloid beta and the plasma membrane in Alzheimer's disease, including APP and the NMDA receptor. It discusses binding as a possible point of intervention but does not report a proven treatment, cure or prevention.
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Study details
- Evidence strengthLow
How this study scored 38/100
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 (Current protein & peptide science) |
| Journal's citation record | 1 / 4 | Current Protein and Peptide Science: journal h-index 112 (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 | 2004 — older than 20 years, still counted |
| 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 | 5 / 7 | Cited 114 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 4.8 citations a year over 24 year(s) since 2004 |
| Impact for its field and year | 3 / 6 | Cited 5.7× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 1 other studies in this library |
| Still being cited | 1 / 4 | Cited 3 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Botond Penke: h-index 60 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | Hungarian Academy of Sciences: institution h-index 608 (OpenAlex) |
| Multicenter collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 14965318) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 38 / 100 | — |
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