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Physiological functions of APP family proteins
Müller UC, Zheng H.. Cold Spring Harbor perspectives in medicine, 2012-02-01
Topic: Brain proteins, microglia and lab models
Biochemical and genetic evidence establishes a central role of the amyloid precursor protein (APP) in Alzheimer disease (AD) pathogenesis. Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically, both point mutations and duplications of wild-type APP are linked to a subset of early onset of familial AD (FAD) and cerebral amyloid angiopathy. As such, the biological functions of APP and its processing products have been the subject of intense investigation, and the past 20+ years of research have met with both excitement and challenges.
Key findings
- Biochemically, deposition of the β-amyloid (Aβ) peptides produced from proteolytic processing of APP forms the defining pathological hallmark of AD; genetically, both point mutations and duplications of wild-type APP are linked to a subset of early onset of familial AD (FAD) and cerebral amyloid angiopathy.
- As such, the biological functions of APP and its processing products have been the subject of intense investigation, and the past 20+ years of research have met with both excitement and challenges.
- This article will review the current understanding of the physiological functions of APP in the context of APP family members.
Why it matters
This review summarizes evidence that amyloid precursor protein and its processing products are central to Alzheimer's disease pathogenesis and that APP mutations and duplications cause some early-onset familial cases. It is a review of existing knowledge and does not report a new treatment, cure or prevention.
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Study details
- Evidence strengthLow
How this study scored 45/100
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. We have no data on impact for its field and year, so that was left out: it earned 42 of the 94 points we could judge it on, which is 45 out of 100.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Cold Spring Harbor perspectives in medicine) |
| Journal's citation record | 2 / 4 | Cold Spring Harbor Perspectives in Medicine: journal h-index 197 (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 | 2012 — within 20 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) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 6 / 7 | Cited 311 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 19.4 citations a year over 16 year(s) since 2012 |
| Impact for its field and year | — / 6 | No field-weighted citation impact (OpenAlex has none yet) — left out of this score |
| Cited by studies here | 2 / 6 | Cited by 6 other studies in this library |
| Still being cited | 2 / 4 | Cited 36 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Hui Zheng: h-index 77 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | Baylor College of Medicine: institution h-index 1,607 (OpenAlex) |
| Multi-centre collaboration | 1 / 3 | OpenAlex lists 2 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 22355794) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Points | 42 / 94 | Scored on 19 of 20 parts. We have no data for the rest, so they are left out: 42 of the 94 points we could judge it on is 45 out of 100. |
| Total | 45 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1101/cshperspect.a006288
- PubMed: 22355794
- Original source →
- Free full text: Cold Spring Harbor Perspectives in Medicine →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
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.
APA 7th
Müller, U. C., & Zheng, H. (2012). Physiological functions of APP family proteins. Cold Spring Harbor perspectives in medicine. https://doi.org/10.1101/cshperspect.a006288
Vancouver
Müller UC, Zheng H. Physiological functions of APP family proteins. Cold Spring Harbor perspectives in medicine. 2012. doi:10.1101/cshperspect.a006288. PMID: 22355794.
BibTeX
@article{muller2012-22355794,
author = {Müller, U. C. and Zheng, H.},
title = {{Physiological functions of APP family proteins}},
journal = {Cold Spring Harbor perspectives in medicine},
year = {2012},
doi = {10.1101/cshperspect.a006288},
pmid = {22355794},
url = {https://doi.org/10.1101/cshperspect.a006288}
}
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