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43/100

✓ Peer-reviewed alzhub usefulness score 43 out of 100. Risk genes beyond APOE

Topic: Amyloid, tau and blood-test diagnosis

Plain-language summary

A peptide corresponding to the amino acid sequence of A beta 17-42 (LVFFAEDVGSNKGAIIGLMVGGVVIA) was isolated from Alzheimer Disease patient brains containing large deposits of diffuse-type amyloid. Brain homogenates were lysed in SDS and submitted to high speed centrifugations. A beta peptides were purified by size exclusion chromatography on Superose 12 and TSK 3000 SW columns.

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APA 7th

Gowing, E., Roher, A. E., Woods, A. S., Cotter, R. J., Chaney, M., Little, S. P., et al. (1994). Chemical characterization of A beta 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease. The Journal of biological chemistry. https://doi.org/10.1016/s0021-9258(19)78080-6

Vancouver

Gowing E, Roher AE, Woods AS, Cotter RJ, Chaney M, Little SP, et al. Chemical characterization of A beta 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease. The Journal of biological chemistry. 1994. doi:10.1016/s0021-9258(19)78080-6. PMID: 8157623.

BibTeX

@article{gowing1994-8157623,
  author  = {Gowing, E. and Roher, A. E. and Woods, A. S. and Cotter, R. J. and Chaney, M. and Little, S. P. and Ball, M. J.},
  title   = {{Chemical characterization of A beta 17-42 peptide, a component of diffuse amyloid deposits of Alzheimer disease}},
  journal = {The Journal of biological chemistry},
  year    = {1994},
  doi     = {10.1016/s0021-9258(19)78080-6},
  pmid    = {8157623},
  url     = {https://doi.org/10.1016/s0021-9258(19)78080-6}
}

Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record names 7 authors; APA and Vancouver show the first six, BibTeX and the downloads carry all of them. Check the citation against the original before you use it.

How to read this study

Design: our record does not state a study design, so check the methods section of the original before weighing the result.
Size: the record gives no participant count. Look for one in the original before trusting a pattern.
Effect: the record gives no effect size, so the summary above cannot say how large any difference was.

What the evidence grade means here

This page is graded low. alzhub.org assigns the grade automatically from keywords in the abstract, not from reading the paper. Low means the abstract matched neither pattern. It is the default label, and it does not mean the work is poor; many sound lab and imaging papers land here. It can add at most 5 of the 100 points in the study score, and it is a label about design, not a verdict on whether the findings are true.

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Key findings

Brain homogenates were lysed in SDS and submitted to high speed centrifugations.
A beta peptides were purified by size exclusion chromatography on Superose 12 and TSK 3000 SW columns.
An A beta peptide with M(r) of 3,000 was recovered that on automatic gas-phase Edman degradation yielded the amino acid sequence of A beta starting at residue 17 (Leu).
The 3-kDa peptide was subsequently hydrolyzed with trypsin and reacted with CNBr, and the resulting peptides were separated by reverse phase high pressure liquid chromatography and characterized by amino acid analyses, peptide microsequencing, and mass spectrometry.

Why it matters

This chemical study isolated and identified a specific amyloid beta fragment, Aβ17-42, from the brains of Alzheimer's disease patients who had large amounts of diffuse amyloid deposits. It describes the composition of these deposits but provides no information about treating, curing, or preventing the disease.

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Study details

Evidence strengthLow

How this study scored 43/100

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 (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	1994 — 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 223 times (OpenAlex, 2026-10-10)
Citations per year	2 / 5	6.6 citations a year over 34 year(s) since 1994
Impact for its field and year	4 / 6	Cited 10.7× the average for papers of its field and year (OpenAlex FWCI)
Cited by studies here	3 / 6	Cited by 10 other studies in this library
Still being cited	1 / 4	Cited 6 times in 2024–2026 (2026 still in progress; OpenAlex)
Senior author's track record	2 / 4	Last-listed author Melvyn J. Ball: h-index 43 (OpenAlex, whole career)
Institution's track record	1 / 3	Wayne State University: institution h-index 864 (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 8157623)
Free to read	0 / 2	Behind a paywall — scores zero
Total	43 / 100	—

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