Evidence map›Paper›PMID 38351005›Full record

ArticleNature communications2024

Cryo-EM structures of lipidic fibrils of amyloid-β (1-40).

Benedikt Frieg, Mookyoung Han, Karin Giller, Christian Dienemann, Dietmar Riedel, Stefan Becker, Loren B Andreas, Christian Griesinger, Gunnar F Schröder

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
18.6field-weighted citation impact, top 1% 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

39 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
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  8. Polymorphic structures of rapidly twisting 40-residue amyloid-β fibrils.bioRxiv : the preprint server for biology · 2026
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Amyloid-beta (1-40) peptide is associated with systemic metabolic health.European journal of clinical investigation · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

9 authors at 3 institutions in 1 country.

Benedikt Frieg *Institute of Biological Information Processing (IBI-7: Structural Biochemistry) and JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-7877-0262
Mookyoung Han *Department of NMR-Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID 0009-0004-8007-5711
Karin GillerDepartment of NMR-Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Christian DienemannDepartment of Molecular Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID 0000-0002-2172-5110
Dietmar RiedelLaboratory of Electron Microscopy, Max-Planck-Institute for Multidisciplinary Sciences, Göttingen, Germany.
Stefan BeckerDepartment of NMR-Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. sabe@mpinat.mpg.de.ORCID 0000-0003-2041-5740
Loren B AndreasDepartment of NMR-Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. land@mpinat.mpg.de.ORCID 0000-0003-3216-9065
Christian GriesingerDepartment of NMR-Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. cigr@mpinat.mpg.de.
Gunnar F SchröderInstitute of Biological Information Processing (IBI-7: Structural Biochemistry) and JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, Germany. gu.schroeder@fz-juelich.de.ORCID 0000-0003-1803-5431
Max Planck Institute for Multidisciplinary SciencesMax Planck Institute for the Study of Religious and Ethnic Diversity · DEForschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is a progressive and incurable neurodegenerative disease characterized by the extracellular deposition of amyloid plaques. Investigation into the composition of these plaques revealed a high amount of amyloid-β (Aβ) fibrils and a high concentration of lipids, suggesting that fibril-lipid interactions may also be relevant for the pathogenesis of AD. Therefore, we grew Aβ40 fibrils in the presence of lipid vesicles and determined their structure by cryo-electron microscopy (cryo-EM) to high resolution. The fold of the major polymorph is similar to the structure of brain-seeded fibrils reported previously. The majority of the lipids are bound to the fibrils, as we show by cryo-EM and NMR spectroscopy. This apparent lipid extraction from vesicles observed here in vitro provides structural insights into potentially disease-relevant fibril-lipid interactions.

Indexed as

Alzheimer DiseaseNeurodegenerative DiseasesAmyloidAmyloid beta-PeptidesCryoelectron MicroscopyHumansLipidsPeptide FragmentsAmyloidAmyloid beta-PeptidesLipidsPeptide Fragments

Identifiers

PMID38351005
PMCPMC10864299
OpenAlexW4391779573

What OpenQuestion holds

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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.