Evidence map›Paper›PMID 30185465›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2018

TOM1 Regulates Neuronal Accumulation of Amyloid-β Oligomers by FcγRIIb2 Variant in Alzheimer's Disease.

Youngdae Gwon, Tae-In Kam, Seo-Hyun Kim, Sungmin Song, Hyejin Park, Bitna Lim, Haneul Lee, Weontae Lee, Dong-Gyu Jo, Yong-Keun Jung

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
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  6. Article
  7. Article
  8. Review
  9. Article
  10. 1-L Transcription in Alzheimer's Disease.Current issues in molecular biology · 2022
    Article
  11. Review
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  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Reply to Peng and Zhao: Loss of endocytic protein TOM1 in Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Amyloid-beta impairs TOM1-mediated IL-1R1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 3 countries.

Youngdae GwonSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.
Tae-In KamSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.
Seo-Hyun KimSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.ORCID 0000-0002-5112-0104
Sungmin SongSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.
Hyejin ParkSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.
Bitna LimSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.
Haneul LeeSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea.
Weontae LeeDepartment of Biochemistry, College of Life Sciences and Biotechnology, Yonsei University, Seoul 03722, Korea, and.
Dong-Gyu JoSchool of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Yong-Keun JungSchool of Biological Sciences, Seoul National University, Seoul 08826, Korea, ykjung@snu.ac.kr.ORCID 0000-0002-9686-3120
Seoul National University · KRSungkyunkwan University · KRYonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Emerging evidences suggest that intraneuronal Aβ correlates with the onset of Alzheimer's disease (AD) and highly contributes to neurodegeneration. However, critical mediator responsible for Aβ uptake in AD pathology needs to be clarified. Here, we report that FcγRIIb2, a variant of Fcγ-receptor IIb (FcγRIIb), functions in neuronal uptake of pathogenic Aβ. Cellular accumulation of oligomeric Aβ

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsAstrocytesCell LineDisease Models, AnimalFemaleHippocampusHumansIntracellular Signaling Peptides and ProteinsMaleMice, KnockoutMicroRNAsNeuronsPeptide FragmentsProteinsAmyloid beta-Peptidesamyloid beta-protein (1-40)amyloid beta-protein (1-42)FCGR2B protein, humanFcgr2b protein, mouseIntracellular Signaling Peptides and ProteinsMicroRNAsMIRN126 microRNA, humanPeptide FragmentsProteinsReceptors, IgGTOM1 protein, humanTOM1 protein, mouseAlzheimer's diseaseAmyloid beta (Aβ)Fcγ-receptor IIbIntraneuronal AβmiR-126TOM1

Identifiers

PMID30185465
PMCPMC6705977
OpenAlexW2892076417

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.