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Phosphatidylinositol and inositol involvement in Alzheimer amyloid-beta fibril growth and arrest
McLaurin J, Franklin T, Chakrabartty A, Fraser PE.. Journal of molecular biology, 1998-04-01
Topic: Amyloid, tau and blood-test diagnosis
Plain-language summary
A key pathological feature of Alzheimer's disease is the formation and accumulation of amyloid fibres. The major component is the 39 to 42 residue amyloid-beta peptide (Abeta) which is an internal proteolytic fragment of the integral membrane amyloid precursor protein. Aggregation of Abeta into insoluble amyloid fibres is a nucleation-dependent event that may be modulated by the presence of amyloid-associated molecules.
What this study adds
Evidence grade: Low
This laboratory study examined how phosphatidylinositol and inositol affect the growth and stopping of amyloid-beta fibrils. It is basic chemistry work and does not show any treatment, cure or prevention for Alzheimer's disease.
Taken from this record’s own fields, not from reading the paper. The grade is assigned from the abstract’s wording; what that means.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
McLaurin, J., Franklin, T., Chakrabartty, A., & Fraser, P. E. (1998). Phosphatidylinositol and inositol involvement in Alzheimer amyloid-beta fibril growth and arrest. Journal of molecular biology. https://doi.org/10.1006/jmbi.1998.1677
Vancouver
McLaurin J, Franklin T, Chakrabartty A, Fraser PE. Phosphatidylinositol and inositol involvement in Alzheimer amyloid-beta fibril growth and arrest. Journal of molecular biology. 1998. doi:10.1006/jmbi.1998.1677. PMID: 9571042.
BibTeX
@article{mclaurin1998-9571042,
author = {McLaurin, J. and Franklin, T. and Chakrabartty, A. and Fraser, P. E.},
title = {{Phosphatidylinositol and inositol involvement in Alzheimer amyloid-beta fibril growth and arrest}},
journal = {Journal of molecular biology},
year = {1998},
doi = {10.1006/jmbi.1998.1677},
pmid = {9571042},
url = {https://doi.org/10.1006/jmbi.1998.1677}
}
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Key findings
- The major component is the 39 to 42 residue amyloid-beta peptide (Abeta) which is an internal proteolytic fragment of the integral membrane amyloid precursor protein.
- Aggregation of Abeta into insoluble amyloid fibres is a nucleation-dependent event that may be modulated by the presence of amyloid-associated molecules.
- Fibril formation is also associated with neurotoxicity which may be the result of specific Abeta interactions with membrane proteins and/or lipids.
- Using circular dichroism spectroscopy, tyrosine fluorescence spectroscopy and electron microscopy, we have examined the binding of Abeta peptides 1-40 (Abeta40) and 1-42 (Abeta42) to the glycolipid, phosphatidylinositol (PI), and different inositol headgroups.
Why it matters
This laboratory study examined how phosphatidylinositol and inositol affect the growth and stopping of amyloid-beta fibrils. It is basic chemistry work and does not show any treatment, cure or prevention for Alzheimer's disease.
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Study details
- Evidence strengthLow
How this study scored 42/100
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 (Journal of molecular biology) |
| Journal's citation record | 3 / 4 | Journal of Molecular Biology: journal h-index 484 (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 | 1998 — 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 140 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 4.7 citations a year over 30 year(s) since 1998 |
| Impact for its field and year | 3 / 6 | Cited 4.4× 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 3 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Paul E. Fraser: h-index 76 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | University of Toronto: institution h-index 1,923 (OpenAlex) |
| Multicenter 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 9571042) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 42 / 100 | — |
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