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Amyloid plaque core protein in Alzheimer disease and Down syndrome
Masters CL, Simms G, Weinman NA, Multhaup G, McDonald BL, Beyreuther K.. Proceedings of the National Academy of Sciences of the United States of America, 1985-06-01
Topic: Amyloid, tau and blood-test diagnosis
Plain-language summary
We have purified and characterized the cerebral amyloid protein that forms the plaque core in Alzheimer disease and in aged individuals with Down syndrome. The protein consists of multimeric aggregates of a polypeptide of about 40 residues (4 kDa). The amino acid composition, molecular mass, and NH2-terminal sequence of this amyloid protein are almost identical to those described for the amyloid deposited in the congophilic angiopathy of Alzheimer disease and Down syndrome, but the plaque core proteins have ragged NH2 termini. The shared 4-kDa subunit indicates a common origin for the amyloids of the plaque core and of the congophilic angiopathy. There are superficial resemblances between the solubility characteristics of the plaque core and some of the properties of scrapie infectivity, but there are no similarities in amino acid sequences between the plaque core and scrapie polypeptides.
What this study adds
Evidence grade: Low
This 1985 laboratory study purified the protein at the core of the amyloid plaques found in the brains of people with Alzheimer disease and older people with Down syndrome, and found it is made of clumps of a small protein of "about 40 residues (4 kDa)". It reported that this protein is "almost identical" to the amyloid deposited in brain blood-vessel walls, apart from "ragged" starting ends, which the authors say "indicates a common origin" for the two, and it found "no similarities in amino acid sequences" with scrapie.
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
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985). Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proceedings of the National Academy of Sciences of the United States of America. https://doi.org/10.1073/pnas.82.12.4245
Vancouver
Masters CL, Simms G, Weinman NA, Multhaup G, McDonald BL, Beyreuther K. Amyloid plaque core protein in Alzheimer disease and Down syndrome. Proceedings of the National Academy of Sciences of the United States of America. 1985. doi:10.1073/pnas.82.12.4245. PMID: 3159021.
BibTeX
@article{masters1985-3159021,
author = {Masters, C. L. and Simms, G. and Weinman, N. A. and Multhaup, G. and McDonald, B. L. and Beyreuther, K.},
title = {{Amyloid plaque core protein in Alzheimer disease and Down syndrome}},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {1985},
doi = {10.1073/pnas.82.12.4245},
pmid = {3159021},
url = {https://doi.org/10.1073/pnas.82.12.4245}
}
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
- We have purified and characterized the cerebral amyloid protein that forms the plaque core in Alzheimer disease and in aged individuals with Down syndrome.
- The protein consists of multimeric aggregates of a polypeptide of about 40 residues (4 kDa).
- The amino acid composition, molecular mass, and NH2-terminal sequence of this amyloid protein are almost identical to those described for the amyloid deposited in the congophilic angiopathy of Alzheimer disease and Down syndrome, but the plaque core proteins have ragged NH2 termini.
- The shared 4-kDa subunit indicates a common origin for the amyloids of the plaque core and of the congophilic angiopathy.
- There are superficial resemblances between the solubility characteristics of the plaque core and some of the properties of scrapie infectivity, but there are no similarities in amino acid sequences between the plaque core and scrapie polypeptides.
Why it matters
This 1985 laboratory study purified the protein at the core of the amyloid plaques found in the brains of people with Alzheimer disease and older people with Down syndrome, and found it is made of clumps of a small protein of "about 40 residues (4 kDa)". It reported that this protein is "almost identical" to the amyloid deposited in brain blood-vessel walls, apart from "ragged" starting ends, which the authors say "indicates a common origin" for the two, and it found "no similarities in amino acid sequences" with scrapie. It describes what plaques are made of, gives no number of brains studied, and does not test whether amyloid causes dementia or how to treat it.
Study details
- Evidence strengthLow
How this study scored 56/100
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. We have no data on senior author's track record and institution's track record, so those were left out: it earned 52 of the 93 points we could judge it on, which is 56 out of 100.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Proceedings of the National Academy of Sciences of the United States of America) |
| Journal's citation record | 4 / 4 | Proceedings of the National Academy of Sciences: journal h-index 1,167 (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 | 1985 — 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 | 7 / 7 | Cited 4,435 times (OpenAlex, 2026-10-10) |
| Citations per year | 5 / 5 | 103.1 citations a year over 43 year(s) since 1985 |
| Impact for its field and year | 6 / 6 | Cited 65.9× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 5 / 6 | Cited by 144 other studies in this library |
| Still being cited | 4 / 4 | Cited 265 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | — / 4 | OpenAlex's profile for last-listed author K Beyreuther holds only 9 work(s), too few to judge a track record — left out of this score |
| Institution's track record | — / 3 | No institution listed in OpenAlex — left out of this score |
| Multicenter collaboration | 0 / 3 | OpenAlex lists 0 institution(s) in 0 countries — scores zero (affiliation lists can be incomplete) |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 3159021) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Points | 52 / 93 | Scored on 18 of 20 parts. We have no data for the rest, so they are left out: 52 of the 93 points we could judge it on is 56 out of 100. |
| Total | 56 / 100 | — |
What each of these 20 components measures, and what this score is not →
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