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The Alzheimer amyloid precursor protein. Identification of a stable intermediate in the biosynthetic/degradative pathway
Oltersdorf T, Ward PJ, Henriksson T, Beattie EC, Neve R, Lieberburg I, Fritz LC.. The Journal of biological chemistry, 1990-03-01
Topic: Amyloid, tau and blood-test diagnosis
The amyloid forming beta-peptide of Alzheimer's disease is synthesized as part of a larger integral membrane precursor protein (beta APP) of which three alternatively spliced versions of 695, 751, and 770 amino acids have been described. A fourth beta APP form of 563 amino acids does not contain the beta-peptide region. Recent experiments using transient expression in HeLa cells (Weidemann, A., Konig, G., Bunke, D., Fischer, P., Salbaum, J.M., Masters, C.L., and Beyreuther, K.
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APA 7th
Oltersdorf, T., Ward, P. J., Henriksson, T., Beattie, E. C., Neve, R., Lieberburg, I., et al. (1990). The Alzheimer amyloid precursor protein. Identification of a stable intermediate in the biosynthetic/degradative pathway. The Journal of biological chemistry. https://doi.org/10.1016/s0021-9258(19)39590-0
Vancouver
Oltersdorf T, Ward PJ, Henriksson T, Beattie EC, Neve R, Lieberburg I, et al. The Alzheimer amyloid precursor protein. Identification of a stable intermediate in the biosynthetic/degradative pathway. The Journal of biological chemistry. 1990. doi:10.1016/s0021-9258(19)39590-0. PMID: 1968460.
BibTeX
@article{oltersdorf1990-1968460,
author = {Oltersdorf, T. and Ward, P. J. and Henriksson, T. and Beattie, E. C. and Neve, R. and Lieberburg, I. and Fritz, L. C.},
title = {{The Alzheimer amyloid precursor protein. Identification of a stable intermediate in the biosynthetic/degradative pathway}},
journal = {The Journal of biological chemistry},
year = {1990},
doi = {10.1016/s0021-9258(19)39590-0},
pmid = {1968460},
url = {https://doi.org/10.1016/s0021-9258(19)39590-0}
}
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.
Key findings
- A fourth beta APP form of 563 amino acids does not contain the beta-peptide region.
- Recent experiments using transient expression in HeLa cells (Weidemann, A., Konig, G., Bunke, D., Fischer, P., Salbaum, J.M., Masters, C.L., and Beyreuther, K.
- (1989) Cell 57, 115-126) indicate that the beta APP undergoes several posttranslational modifications including the cleavage and secretion of a large portion of its extracellular domain.
- The nature and fate of the fragment that remains cell-associated following this cleavage has not heretofore been described.
Why it matters
This laboratory work describes how the amyloid precursor protein is processed and identifies a stable intermediate fragment that remains in cells. It does not test any treatment or show how to prevent or cure Alzheimer's disease.
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Study details
- Evidence strengthLow
How this study scored 44/100
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 (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 | 1990 — 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 282 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 7.4 citations a year over 38 year(s) since 1990 |
| Impact for its field and year | 5 / 6 | Cited 22.5× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 3 / 6 | Cited by 19 other studies in this library |
| Still being cited | 0 / 4 | Cited 2 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 1 / 4 | Last-listed author L C Fritz: h-index 15 (OpenAlex, whole career) |
| Institution's track record | 3 / 3 | Harvard University: institution h-index 3,235 (OpenAlex) |
| Multi-centre 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 1968460) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 44 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1016/s0021-9258(19)39590-0
- PubMed: 1968460
- Original source →
- Free full text: Journal of Biological Chemistry →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
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