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Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path
Buxbaum JD, Thinakaran G, Koliatsos V, O'Callahan J, Slunt HH, Price DL, Sisodia SS.. The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998-12-01
Topic: Amyloid, tau and blood-test diagnosis
Amyloid deposition is a neuropathological hallmark of Alzheimer's disease. The principal component of amyloid deposits is beta amyloid peptide (Abeta), a peptide derived by proteolytic processing of the amyloid precursor protein (APP). APP is axonally transported by the fast anterograde component.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Buxbaum, J. D., Thinakaran, G., Koliatsos, V., O'Callahan, J., Slunt, H. H., Price, D. L., et al. (1998). Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path. The Journal of neuroscience : the official journal of the Society for Neuroscience. https://doi.org/10.1523/jneurosci.18-23-09629.1998
Vancouver
Buxbaum JD, Thinakaran G, Koliatsos V, O'Callahan J, Slunt HH, Price DL, et al. Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path. The Journal of neuroscience : the official journal of the Society for Neuroscience. 1998. doi:10.1523/jneurosci.18-23-09629.1998. PMID: 9822724.
BibTeX
@article{buxbaum1998-9822724,
author = {Buxbaum, J. D. and Thinakaran, G. and Koliatsos, V. and O'Callahan, J. and Slunt, H. H. and Price, D. L. and Sisodia, S. S.},
title = {{Alzheimer amyloid protein precursor in the rat hippocampus: transport and processing through the perforant path}},
journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience},
year = {1998},
doi = {10.1523/jneurosci.18-23-09629.1998},
pmid = {9822724},
url = {https://doi.org/10.1523/jneurosci.18-23-09629.1998}
}
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
- The principal component of amyloid deposits is beta amyloid peptide (Abeta), a peptide derived by proteolytic processing of the amyloid precursor protein (APP).
- APP is axonally transported by the fast anterograde component.
- Several studies have indicated that Abeta deposits occur in proximity to neuritic and synaptic profiles.
- Taken together, these latter observations have suggested that APP, axonally transported to nerve terminals, may be processed to Abeta at those sites.
Why it matters
In rats, the amyloid precursor protein is transported along axons to nerve terminals, where it may be processed into amyloid beta. This describes a possible site of amyloid formation but tests no treatment and shows no effect on disease.
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Study details
- Evidence strengthLow
How this study scored 47/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported 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 neuroscience : the official journal of the Society for Neuroscience) |
| Journal's citation record | 4 / 4 | Journal of Neuroscience: journal h-index 651 (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 | Laboratory or animal study (title names “rat”) — scores zero |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 267 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 8.9 citations a year over 30 year(s) since 1998 |
| Impact for its field and year | 3 / 6 | Cited 3.4× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 8 other studies in this library |
| Still being cited | 1 / 4 | Cited 7 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 4 / 4 | Last-listed author Sangram S. Sisodia: h-index 101 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | Johns Hopkins University: institution h-index 2,306 (OpenAlex) |
| Multicenter collaboration | 2 / 3 | OpenAlex lists 5 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 9822724) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 47 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1523/jneurosci.18-23-09629.1998
- PubMed: 9822724
- Original source →
- Free full text: Journal of Neuroscience →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
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