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Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein
Rossjohn J, Cappai R, Feil SC, Henry A, McKinstry WJ, Galatis D, Hesse L, Multhaup G et al.. Nature structural biology, 1999-04-01
Topic: Amyloid, tau and blood-test diagnosis
Amyloid precursor protein (APP) plays a central role in Alzheimer disease. A proteolytic-breakdown product of APP, called beta-amyloid, is a major component of the diffuse and fibrillar deposits found in Alzheimer diseased brains. The normal physiological role of APP remains largely unknown despite much work.
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APA 7th
Rossjohn, J., Cappai, R., Feil, S. C., Henry, A., McKinstry, W. J., Galatis, D., et al. (1999). Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein. Nature structural biology. https://doi.org/10.1038/7562
Vancouver
Rossjohn J, Cappai R, Feil SC, Henry A, McKinstry WJ, Galatis D, et al. Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein. Nature structural biology. 1999. doi:10.1038/7562. PMID: 10201399.
BibTeX
@article{rossjohn1999-10201399,
author = {Rossjohn, J. and Cappai, R. and Feil, S. C. and Henry, A. and McKinstry, W. J. and Galatis, D. and Hesse, L. and Multhaup, G. and others},
title = {{Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein}},
journal = {Nature structural biology},
year = {1999},
doi = {10.1038/7562},
pmid = {10201399},
url = {https://doi.org/10.1038/7562}
}
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Key findings
- A proteolytic-breakdown product of APP, called beta-amyloid, is a major component of the diffuse and fibrillar deposits found in Alzheimer diseased brains.
- The normal physiological role of APP remains largely unknown despite much work.
- A knowledge of its function will not only provide insights into the genesis of the disease but may also prove vital in the development of an effective therapy.
- Here we describe the 1.8 A resolution crystal structure of the N-terminal, heparin-binding domain of APP (residues 28-123), which is responsible, among other things, for stimulation of neurite outgrowth.
Why it matters
This study describes the crystal structure of a part of the amyloid precursor protein, noting that the protein's normal function is still largely unknown. It provides structural information only and does not test any treatment, cure, or prevention.
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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 randomized / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Nature structural biology) |
| Journal's citation record | 2 / 4 | Nature Structural Biology: journal h-index 231 (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 | 1999 — 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 244 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 8.4 citations a year over 29 year(s) since 1999 |
| Impact for its field and year | 3 / 6 | Cited 4.0× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 9 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 | 4 / 4 | Last-listed author Colin Louis Masters: h-index 175 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | Heidelberg University: institution h-index 1,344 (OpenAlex) |
| Multicenter collaboration | 2 / 3 | OpenAlex lists 5 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 10201399) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 44 / 100 | — |
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