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The physiological role of the amyloid precursor protein as an adhesion molecule in the developing nervous system
Sosa LJ, Cáceres A, Dupraz S, Oksdath M, Quiroga S, Lorenzo A.. Journal of neurochemistry, 2017-08-15
Topic: Brain proteins, microglia and lab models
The amyloid precursor protein (APP) is a type I transmembrane glycoprotein better known for its participation in the physiopathology of Alzheimer disease as the source of the beta amyloid fragment. However, the physiological functions of the full length protein and its proteolytic fragments have remained elusive. APP was first described as a cell-surface receptor; nevertheless, increasing evidence highlighted APP as a cell adhesion molecule. In this review, we will focus on the current knowledge of the physiological role of APP as a cell adhesion molecule and its involvement in key events of neuronal development, such as migration, neurite outgrowth, growth cone pathfinding, and synaptogenesis. Finally, since APP is over-expressed in Down syndrome individuals because of the extra copy of chromosome 21, in the last section of the review, we discuss the potential contribution of APP to the neuronal and synaptic defects described in this genetic condition. Read the Editorial Highlight for this article on page 9. Cover Image for this issue: doi. 10.1111/jnc.13817.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Sosa, L. J., Cáceres, A., Dupraz, S., Oksdath, M., Quiroga, S., & Lorenzo, A. (2017). The physiological role of the amyloid precursor protein as an adhesion molecule in the developing nervous system. Journal of neurochemistry. https://doi.org/10.1111/jnc.14122
Vancouver
Sosa LJ, Cáceres A, Dupraz S, Oksdath M, Quiroga S, Lorenzo A. The physiological role of the amyloid precursor protein as an adhesion molecule in the developing nervous system. Journal of neurochemistry. 2017. doi:10.1111/jnc.14122. PMID: 28677143.
BibTeX
@article{sosa2017-28677143,
author = {Sosa, L. J. and Cáceres, A. and Dupraz, S. and Oksdath, M. and Quiroga, S. and Lorenzo, A.},
title = {{The physiological role of the amyloid precursor protein as an adhesion molecule in the developing nervous system}},
journal = {Journal of neurochemistry},
year = {2017},
doi = {10.1111/jnc.14122},
pmid = {28677143},
url = {https://doi.org/10.1111/jnc.14122}
}
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
- APP was first described as a cell-surface receptor; nevertheless, increasing evidence highlighted APP as a cell adhesion molecule.
- In this review, we will focus on the current knowledge of the physiological role of APP as a cell adhesion molecule and its involvement in key events of neuronal development, such as migration, neurite outgrowth, growth cone pathfinding, and synaptogenesis.
- Finally, since APP is over-expressed in Down syndrome individuals because of the extra copy of chromosome 21, in the last section of the review, we discuss the potential contribution of APP to the neuronal and synaptic defects described in this genetic condition.
- Read the Editorial Highlight for this article on page 9.
- Cover Image for this issue: doi. 10.1111/jnc.13817.
Why it matters
This review focuses on the normal physiological role of amyloid precursor protein as a cell adhesion molecule in neuronal development, including migration, neurite outgrowth, and synaptogenesis. It discusses how APP overexpression in Down syndrome might contribute to neuronal and synaptic defects, but it reports no treatment, cure, or prevention.
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 (Journal of neurochemistry) |
| Journal's citation record | 3 / 4 | Journal of Neurochemistry: journal h-index 349 (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 | 2 / 5 | 2017 — within 10 year(s) of the newest study here |
| 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 104 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 9.5 citations a year over 11 year(s) since 2017 |
| Impact for its field and year | 3 / 6 | Cited 7.9× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 1 other studies in this library |
| Still being cited | 2 / 4 | Cited 27 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Alfredo Lorenzo: h-index 23 (OpenAlex, whole career) |
| Institution's track record | 0 / 3 | Consejo Nacional de Investigaciones Científicas y Técnicas: institution h-index 639 (OpenAlex) |
| Multicenter collaboration | 2 / 3 | OpenAlex lists 6 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 28677143) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 43 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1111/jnc.14122
- PubMed: 28677143
- Original source →
- Free full text: Journal of Neurochemistry →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
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