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46/100

✓ Peer-reviewed alzhub usefulness score 46 out of 100. TREM2 and immune genetics

Topic: Brain proteins, microglia and lab models

Triggering receptor expressed on myeloid cells 2 (TREM2) is an immune receptor expressed on the surface of microglia, macrophages, dendritic cells, and osteoclasts. The R47H TREM2 variant is a significant risk factor for late-onset Alzheimer's disease (AD), and the molecular basis of R47H TREM2 loss of function is an emerging area of TREM2 biology. Here, we report three high-resolution structures of the extracellular ligand-binding domains (ECDs) of R47H TREM2, apo-WT, and phosphatidylserine (PS)-bound WT TREM2 at 1.8, 2.2, and 2.2 Å, respectively.

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APA 7th

Sudom, A., Talreja, S., Danao, J., Bragg, E., Kegel, R., Min, X., et al. (2018). Molecular basis for the loss-of-function effects of the Alzheimer's disease-associated R47H variant of the immune receptor TREM2. The Journal of biological chemistry. https://doi.org/10.1074/jbc.ra118.002352

Vancouver

Sudom A, Talreja S, Danao J, Bragg E, Kegel R, Min X, et al. Molecular basis for the loss-of-function effects of the Alzheimer's disease-associated R47H variant of the immune receptor TREM2. The Journal of biological chemistry. 2018. doi:10.1074/jbc.ra118.002352. PMID: 29794134.

BibTeX

@article{sudom2018-29794134,
  author  = {Sudom, A. and Talreja, S. and Danao, J. and Bragg, E. and Kegel, R. and Min, X. and Richardson, J. and Zhang, Z. and others},
  title   = {{Molecular basis for the loss-of-function effects of the Alzheimer's disease-associated R47H variant of the immune receptor TREM2}},
  journal = {The Journal of biological chemistry},
  year    = {2018},
  doi     = {10.1074/jbc.ra118.002352},
  pmid    = {29794134},
  url     = {https://doi.org/10.1074/jbc.ra118.002352}
}

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Key findings

The R47H TREM2 variant is a significant risk factor for late-onset Alzheimer's disease (AD), and the molecular basis of R47H TREM2 loss of function is an emerging area of TREM2 biology.
Here, we report three high-resolution structures of the extracellular ligand-binding domains (ECDs) of R47H TREM2, apo-WT, and phosphatidylserine (PS)-bound WT TREM2 at 1.8, 2.2, and 2.2 Å, respectively.
The structures reveal that Arg 47 plays a critical role in maintaining the structural features of the complementarity-determining region 2 (CDR2) loop and the putative positive ligand-interacting surface (PLIS), stabilizing conformations capable of ligand interaction.
This is exemplified in the PS-bound structure, in which the CDR2 loop and PLIS drive critical interactions with PS via surfaces that are disrupted in the variant.

Why it matters

This structural biology study describes how the R47H TREM2 variant changes the shape of the receptor, helping explain its loss of function. It is laboratory-based molecular work and does not test any treatment or prevention in people.

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Study details

Evidence strengthLow

How this study scored 46/100

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	2 / 5	2018 — 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 150 times (OpenAlex, 2026-10-10)
Citations per year	3 / 5	15.0 citations a year over 10 year(s) since 2018
Impact for its field and year	3 / 6	Cited 4.7× the average for papers of its field and year (OpenAlex FWCI)
Cited by studies here	3 / 6	Cited by 19 other studies in this library
Still being cited	3 / 4	Cited 64 times in 2024–2026 (2026 still in progress; OpenAlex)
Senior author's track record	2 / 4	Last-listed author Zhulun Wang: h-index 41 (OpenAlex, whole career)
Institution's track record	1 / 3	Amgen (United States): institution h-index 779 (OpenAlex)
Multicenter collaboration	0 / 3	OpenAlex lists 1 institution(s) in 1 country — scores zero (affiliation lists can be incomplete)
Indexed in PubMed	2 / 2	Indexed in PubMed (PMID 29794134)
Free to read	0 / 2	Behind a paywall — scores zero
Total	46 / 100	—

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