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Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease
Verdier Y, Zarándi M, Penke B.. Journal of peptide science : an official publication of the European Peptide Society, 2004-05-01
Topic: Amyloid, tau and blood-test diagnosis
The extracellular accumulation of amyloid-beta (Abeta) in neuritic plaques is one of the characteristic hallmarks of Alzheimer's disease (AD), a progressive dementing neurodegenerative disorder of the elderly. By virtue of its structure, Abeta is able to bind to a variety of biomolecules, including lipids, proteins and proteoglycans. The binding of the various forms of Abeta (soluble or fibrillar) to plasma membranes has been studied with regard to the direct toxicity of Abeta to neurons, and the activation of a local inflammation phase involving microglia.
Key findings
- By virtue of its structure, Abeta is able to bind to a variety of biomolecules, including lipids, proteins and proteoglycans.
- The binding of the various forms of Abeta (soluble or fibrillar) to plasma membranes has been studied with regard to the direct toxicity of Abeta to neurons, and the activation of a local inflammation phase involving microglia.
- The binding of Abeta to membrane lipids facilitates Abeta fibrillation, which in turn disturbs the structure and function of the membranes, such as membrane fluidity or the formation of ion channels.
- A subset of membrane proteins binds Abeta.
Why it matters
This review describes how beta-amyloid binds to lipids, proteins and proteoglycans on neuronal and glial membranes, which can promote amyloid fibrillation, damage membranes and trigger local inflammation. It is a summary of laboratory findings about binding and toxicity, not a study of a treatment or cure in patients.
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Study details
- Evidence strengthLow
How this study scored 41/100
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 (Journal of peptide science : an official publication of the European Peptide Society) |
| Journal's citation record | 1 / 4 | Journal of Peptide Science: journal h-index 84 (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) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 262 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 10.9 citations a year over 24 year(s) since 2004 |
| Impact for its field and year | 4 / 6 | Cited 9.0× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 3 other studies in this library |
| Still being cited | 1 / 4 | Cited 11 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) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 15160835) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 41 / 100 | — |
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Read the original
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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
Verdier, Y., Zarándi, M., & Penke, B. (2004). Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. Journal of peptide science : an official publication of the European Peptide Society. https://doi.org/10.1002/psc.573
Vancouver
Verdier Y, Zarándi M, Penke B. Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. Journal of peptide science : an official publication of the European Peptide Society. 2004. doi:10.1002/psc.573. PMID: 15160835.
BibTeX
@article{verdier2004-15160835,
author = {Verdier, Y. and Zarándi, M. and Penke, B.},
title = {{Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease}},
journal = {Journal of peptide science : an official publication of the European Peptide Society},
year = {2004},
doi = {10.1002/psc.573},
pmid = {15160835},
url = {https://doi.org/10.1002/psc.573}
}
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3 studies in the alzhub library list this one in their references.