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45/100

✓ Peer-reviewed alzhub usefulness score 45 out of 100. Risk genes beyond APOE

Topic: Brain proteins, microglia and lab models

The neural protein FE65 contains two types of protein-protein interaction modules: one WW binding domain and two phosphotyrosine binding domains. The carboxyl-terminal phosphotyrosine binding domain of FE65 interacts in vivo with the beta-amyloid precursor protein, which is implicated in Alzheimer disease. To understand the function of this adapter protein, we identified binding partners for the FE65 WW domain.

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APA 7th

Ermekova, K. S., Zambrano, N., Linn, H., Minopoli, G., Gertler, F., Russo, T., et al. (1997). The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. The Journal of biological chemistry. https://doi.org/10.1074/jbc.272.52.32869

Vancouver

Ermekova KS, Zambrano N, Linn H, Minopoli G, Gertler F, Russo T, et al. The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled. The Journal of biological chemistry. 1997. doi:10.1074/jbc.272.52.32869. PMID: 9407065.

BibTeX

@article{ermekova1997-9407065,
  author  = {Ermekova, K. S. and Zambrano, N. and Linn, H. and Minopoli, G. and Gertler, F. and Russo, T. and Sudol, M.},
  title   = {{The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled}},
  journal = {The Journal of biological chemistry},
  year    = {1997},
  doi     = {10.1074/jbc.272.52.32869},
  pmid    = {9407065},
  url     = {https://doi.org/10.1074/jbc.272.52.32869}
}

Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record names 7 authors; APA and Vancouver show the first six, BibTeX and the downloads carry all of them. Check the citation against the original before you use it.

Key findings

The carboxyl-terminal phosphotyrosine binding domain of FE65 interacts in vivo with the beta-amyloid precursor protein, which is implicated in Alzheimer disease.
To understand the function of this adapter protein, we identified binding partners for the FE65 WW domain.
Proline-rich sequences sharing a proline-proline-leucine-proline core motif were recovered by screening expression libraries for ligands of the FE65 WW domain.
Five proteins of molecular masses 60, 75, 80, 140, and 200 kDa could be purified from mouse brain lysates by affinity to the FE65 WW domain.

Why it matters

This laboratory study identified proteins that bind to a specific domain of the neural protein FE65, which itself interacts with the amyloid precursor protein. It describes a basic protein interaction and does not test any treatment, prevention or cure for Alzheimer's disease.

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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 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	1997 — 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	Laboratory or animal study (title names “drosophila”) — scores zero
Randomized / blinded	0 / 2	No randomization or blinding stated — scores zero (not stated in the record — scored 0)
Times cited	5 / 7	Cited 238 times (OpenAlex, 2026-10-10)
Citations per year	2 / 5	7.7 citations a year over 31 year(s) since 1997
Impact for its field and year	4 / 6	Cited 9.4× the average for papers of its field and year (OpenAlex FWCI)
Cited by studies here	2 / 6	Cited by 4 other studies in this library
Still being cited	0 / 4	Cited 2 times in 2024–2026 (2026 still in progress; OpenAlex)
Senior author's track record	3 / 4	Last-listed author Marius Sudol: h-index 76 (OpenAlex, whole career)
Institution's track record	3 / 3	Massachusetts Institute of Technology: institution h-index 2,557 (OpenAlex)
Multicenter collaboration	1 / 3	OpenAlex lists 3 institution(s) in 2 countries
Indexed in PubMed	2 / 2	Indexed in PubMed (PMID 9407065)
Free to read	0 / 2	Behind a paywall — scores zero
Total	45 / 100	—

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