Evidence map›Paper›PMID 30018137›Full record

ArticleThe Journal of biological chemistry2018

Amyloid-β fibrils assembled on ganglioside-enriched membranes contain both parallel β-sheets and turns.

Teruhiko Matsubara, Hanaki Yasumori, Koichiro Ito, Takafumi Shimoaka, Takeshi Hasegawa, Toshinori Sato

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Imaging and Characterization of Ganglioside-Induced Amyloid Fibril Formation.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Polymer sailing on rafts within lipid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Ganglioside GM1 produces stable, short, and cytotoxic AβChemical communications (Cambridge, England) · 2023
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. β-Amyloid aggregation and heterogeneous nucleation.Protein science : a publication of the Protein Society · 2019
    Review
  19. Review
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

6 authors at 2 institutions in 1 country.

Teruhiko MatsubaraFrom the Department of Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Kouhoku-ku, Yokohama 223-8522, Japan and.ORCID 0000-0002-8006-4324
Hanaki YasumoriFrom the Department of Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Kouhoku-ku, Yokohama 223-8522, Japan and.
Koichiro ItoFrom the Department of Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Kouhoku-ku, Yokohama 223-8522, Japan and.
Takafumi Shimoakathe Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Takeshi Hasegawathe Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Toshinori SatoFrom the Department of Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Kouhoku-ku, Yokohama 223-8522, Japan and sato@bio.keio.ac.jp.
Keio University · JPKyoto University Institute for Chemical Research

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Some protein and peptide aggregates, such as those of amyloid-β protein (Aβ), are neurotoxic and have been implicated in several neurodegenerative diseases. Aβ accumulates at nanoclusters enriched in neuronal lipids called gangliosides in the presynaptic neuronal membrane, and the resulting oligomeric and/or fibrous forms accelerate the development of Alzheimer's disease. Although the presence of Aβ deposits at such nanoclusters is known, the mechanism of their assembly and the relationship between Aβ secondary structure and topography are still unclear. Here, we first confirmed by atomic force microscopy that Aβ

Indexed as

AmyloidAmyloid beta-PeptidesCholesterolGangliosidesG(M1) GangliosideHumansMembranes, ArtificialMicroscopy, Atomic ForceProtein Structure, SecondarySphingomyelinsAmyloidAmyloid beta-PeptidesCholesterolGangliosidesG(M1) GangliosideMembranes, ArtificialSphingomyelinsAlzheimer's diseaseamyloid β (Aβ)atomic force microscopy (AFM)fibrilFourier transform IR (FTIR)gangliosidelipid bilayerneurodegenerationneuronal membraneparallel β-structure

Identifiers

PMID30018137
PMCPMC6130953
OpenAlexW2883076286

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.