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GGA proteins mediate the recycling pathway of memapsin 2 (BACE)
He X, Li F, Chang WP, Tang J.. The Journal of biological chemistry, 2004-12-21
Topic: Brain proteins, microglia and lab models
Plain-language summary
Memapsin 2 (BACE, beta-secretase) is a membrane-associated aspartic protease that initiates the hydrolysis of beta-amyloid precursor protein (APP) leading to the production of amyloid-beta (A beta) and the progression of Alzheimer disease. Both memapsin 2 and APP are transported from the cell surface to endosomes where APP is cleaved by memapsin 2. We described previously that the cytosolic domain of memapsin 2 contains an acid cluster-dileucine motif (ACDL) that binds the VHS (Vps-27, Hrs, and STAM) domain of Golgi-localized gamma-ear-containing ARF-binding (GGA) proteins (He, X., Zhu, G., Koelsch, G., Rodgers, K.
What this study adds
Evidence grade: Low
This laboratory study found that GGA proteins colocalize with memapsin 2 (BACE) in the trans-Golgi network and endosomes and help mediate its recycling pathway. It describes basic cell biology of the beta-secretase and does not test any treatment for Alzheimer's disease.
Taken from this record’s own fields, not from reading the paper. The grade is assigned from the abstract’s wording; what that means.
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
APA 7th
He, X., Li, F., Chang, W. P., & Tang, J. (2005). GGA proteins mediate the recycling pathway of memapsin 2 (BACE). The Journal of biological chemistry. https://doi.org/10.1074/jbc.m411296200
Vancouver
He X, Li F, Chang WP, Tang J. GGA proteins mediate the recycling pathway of memapsin 2 (BACE). The Journal of biological chemistry. 2005. doi:10.1074/jbc.m411296200. PMID: 15615712.
BibTeX
@article{he2005-15615712,
author = {He, X. and Li, F. and Chang, W. P. and Tang, J.},
title = {{GGA proteins mediate the recycling pathway of memapsin 2 (BACE)}},
journal = {The Journal of biological chemistry},
year = {2005},
doi = {10.1074/jbc.m411296200},
pmid = {15615712},
url = {https://doi.org/10.1074/jbc.m411296200}
}
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
- Both memapsin 2 and APP are transported from the cell surface to endosomes where APP is cleaved by memapsin 2.
- We described previously that the cytosolic domain of memapsin 2 contains an acid cluster-dileucine motif (ACDL) that binds the VHS (Vps-27, Hrs, and STAM) domain of Golgi-localized gamma-ear-containing ARF-binding (GGA) proteins (He, X., Zhu, G., Koelsch, G., Rodgers, K.
- Here we report that GGA proteins colocalize in the trans-Golgi network and endosomes with memapsin 2 and a memapsin 2 chimera containing a cytosolic domain of a mannose-6-phosphate receptor.
- Depleting cellular GGA proteins with RNA interference or mutation of serine 498 to stop the phosphorylation of ACDL resulted in the accumulation of memapsin 2 in early endosomes.
Why it matters
This laboratory study found that GGA proteins colocalize with memapsin 2 (BACE) in the trans-Golgi network and endosomes and help mediate its recycling pathway. It describes basic cell biology of the beta-secretase and does not test any treatment for Alzheimer's disease.
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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 (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) |
| Randomized / blinded | 0 / 2 | No randomization or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 228 times (OpenAlex, 2026-10-10) |
| Citations per year | 3 / 5 | 9.9 citations a year over 23 year(s) since 2005 |
| Impact for its field and year | 3 / 6 | Cited 4.3× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 2 / 6 | Cited by 5 other studies in this library |
| Still being cited | 1 / 4 | Cited 4 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 3 / 4 | Last-listed author Jordan Tang: h-index 57 (OpenAlex, whole career) |
| Institution's track record | 1 / 3 | University of Oklahoma: institution h-index 716 (OpenAlex) |
| Multicenter collaboration | 1 / 3 | OpenAlex lists 3 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 15615712) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 44 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1074/jbc.m411296200
- PubMed: 15615712
- 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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