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BACE1 cytoplasmic domain interacts with the copper chaperone for superoxide dismutase-1 and binds copper
Angeletti B, Waldron KJ, Freeman KB, Bawagan H, Hussain I, Miller CC, Lau KF, Tennant ME et al.. The Journal of biological chemistry, 2005-02-18
Topic: Brain proteins, microglia and lab models
The amyloidogenic pathway leading to the production and deposition of Abeta peptides, major constituents of Alzheimer disease senile plaques, is linked to neuronal metal homeostasis. The amyloid precursor protein binds copper and zinc in its extracellular domain, and the Abeta peptides also bind copper, zinc, and iron. The first step in the generation of Abeta is cleavage of amyloid precursor protein by the aspartic protease BACE1.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
Angeletti, B., Waldron, K. J., Freeman, K. B., Bawagan, H., Hussain, I., Miller, C. C., et al. (2005). BACE1 cytoplasmic domain interacts with the copper chaperone for superoxide dismutase-1 and binds copper. The Journal of biological chemistry. https://doi.org/10.1074/jbc.m412034200
Vancouver
Angeletti B, Waldron KJ, Freeman KB, Bawagan H, Hussain I, Miller CC, et al. BACE1 cytoplasmic domain interacts with the copper chaperone for superoxide dismutase-1 and binds copper. The Journal of biological chemistry. 2005. doi:10.1074/jbc.m412034200. PMID: 15722349.
BibTeX
@article{angeletti2005-15722349,
author = {Angeletti, B. and Waldron, K. J. and Freeman, K. B. and Bawagan, H. and Hussain, I. and Miller, C. C. and Lau, K. F. and Tennant, M. E. and others},
title = {{BACE1 cytoplasmic domain interacts with the copper chaperone for superoxide dismutase-1 and binds copper}},
journal = {The Journal of biological chemistry},
year = {2005},
doi = {10.1074/jbc.m412034200},
pmid = {15722349},
url = {https://doi.org/10.1074/jbc.m412034200}
}
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Key findings
- The amyloid precursor protein binds copper and zinc in its extracellular domain, and the Abeta peptides also bind copper, zinc, and iron.
- The first step in the generation of Abeta is cleavage of amyloid precursor protein by the aspartic protease BACE1.
- Here we show that BACE1 interacts with CCS (the copper chaperone for superoxide dismutase-1 (SOD1)) through domain I and the proteins co-immunoprecipitate from rat brain extracts.
- We have also been able to visualize the co-transport of membranous BACE1 and soluble CCS through axons.
Why it matters
This laboratory study showed that BACE1 interacts with the copper chaperone for superoxide dismutase-1 and binds copper. It describes a molecular interaction related to metal handling and does not test any treatment, cure, or prevention.
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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 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 | 2005 — 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 124 times (OpenAlex, 2026-10-10) |
| Citations per year | 2 / 5 | 5.4 citations a year over 23 year(s) since 2005 |
| Impact for its field and year | 3 / 6 | Cited 5.7× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 3 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 | 2 / 4 | Last-listed author Colin Dingwall: h-index 46 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | Newcastle University: institution h-index 932 (OpenAlex) |
| Multi-centre collaboration | 2 / 3 | OpenAlex lists 4 institution(s) in 2 countries |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 15722349) |
| 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: 10.1074/jbc.m412034200
- PubMed: 15722349
- 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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