Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

An exTREMe disruption in Alzheimer's cleanup.

The Journal of biological chemistry - 10 Aug 2018

Dodd Roger B

Abstract excerpt

Partial loss-of-function variants in the TREM2 immune receptor are associated with increased risk for Alzheimer's disease (AD) and other forms of neurodegenerative disease, but the molecular bases for these connections are unknown. Three new structures of WT and R47H mutant TREM2 immunoglobulin-like (Ig-like) domain now reveal that R47 functions to correctly position elements of the ligand-binding surface....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alzheimer Disease
Share to Brain
Share to Genetic Predisposition to Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genotype

Share to Membrane Glycoproteins

Share to Mutant Proteins

Share to Plaque, Amyloid

Share to Receptors, Immunologic

Source

Open in PubMed Open full text

Identifiers

PMID: 30097493
DOI: 10.1074/jbc.H118.004271
PMCID: PMC6093237

Genes

TREM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An exTREMe disruption in Alzheimer's cleanup.PMID 30097493Read ↗

Molecular basis for the loss-of-function effects of the Alzheimer's disease-associated R47H variant of the immune receptor TREM2.Semantic proximity Read ↗

Neurodegenerative disease mutations in TREM2 reveal a functional surface and distinct loss-of-function mechanisms.Semantic proximity Read ↗

Alzheimer disease: The involvement of TREM2 R47H variant in Alzheimer disease confirmed, but mechanisms remain elusive.Semantic proximity Read ↗

The Trem2 R47H variant confers loss-of-function-like phenotypes in Alzheimer's disease.Semantic proximity Read ↗

Humanized TREM2 mice reveal microglia-intrinsic and -extrinsic effects of R47H polymorphism.Semantic proximity Read ↗

TREM2 Alzheimer's variant R47H causes similar transcriptional dysregulation to knockout, yet only subtle functional phenotypes in human iPSC-derived macrophages.Semantic proximity Read ↗

TREM2 lipid sensing sustains the microglial response in an Alzheimer's disease model.Semantic proximity Read ↗

Functional insights from biophysical study of TREM2 interactions with ApoE and Aβ <sub>1-42</sub>Semantic proximity Read ↗

Wild-type sTREM2 blocks Aβ aggregation and neurotoxicity, but the Alzheimer's R47H mutant increases Aβ aggregation.Semantic proximity Read ↗

TREM2-H157Y Increases Soluble TREM2 Production and Reduces Amyloid PathologySemantic proximity Read ↗

TREM2-H157Y Increases Soluble TREM2 Production and Reduces Amyloid PathologySemantic proximity Read ↗

Wild-type sTREM2 blocks Aβ aggregation and neurotoxicity, while the Alzheimer’s R47H mutant does the oppositeSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.