Evidence map›Paper›PMID 34544868›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane.

Hebah Fatafta, Mohammed Khaled, Michael C Owen, Abdallah Sayyed-Ahmad, Birgit Strodel

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
10.2field-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

42 citing papers in PubMed, 106 citations in OpenAlex.

  1. Membrane Complexity and Phase Behavior Dictate the Stability of Membrane-Inserted AβChemphyschem : a European journal of chemical physics and physical chemistry · 2026
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  13. Membrane-assisted Aβ40 aggregation pathways.Cell reports. Physical science · 2025
    Article
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  18. Membrane-assisted Aβ40 aggregation pathways.bioRxiv : the preprint server for biology · 2024
    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

5 authors at 3 institutions in 4 countries.

Hebah FataftaInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0002-6646-767X
Mohammed KhaledInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0003-2611-1836
Michael C OwenCentral European Institute of Technology, Masaryk University, Brno 625 00, Czech Republic.ORCID 0000-0001-9076-7114
Abdallah Sayyed-AhmadDepartment of Physics, Birzeit University, 71939 Birzeit, Palestine.ORCID 0000-0003-2415-8403
Birgit StrodelInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, 52425 Jülich, Germany; b.strodel@fz-juelich.de.ORCID 0000-0002-8734-7765
Forschungszentrum Jülich · DEBirzeit University · PSCentral European Institute of Technology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed understanding of the mutual interference of amyloid-β oligomers and the neuronal membrane, we carried out microseconds of all-atom molecular dynamics (MD) simulations on the dimerization of amyloid-β (Aβ)42 in the aqueous phase and in the presence of a lipid bilayer mimicking the in vivo composition of neuronal membranes. The dimerization in solution is characterized by a random coil to β-sheet transition that seems on pathway to amyloid aggregation, while the interactions with the neuronal membrane decrease the order of the Aβ42 dimer by attenuating its propensity to form a β-sheet structure. The main lipid interaction partners of Aβ42 are the surface-exposed sugar groups of the gangliosides GM1. As the neurotoxic activity of amyloid oligomers increases with oligomer order, these results suggest that GM1 is neuroprotective against Aβ-mediated toxicity.

Indexed as

Protein MultimerizationAmyloidAmyloid beta-PeptidesCell MembraneG(M1) GangliosideHumansLipid BilayersMolecular Dynamics SimulationNeuronsProtein BindingProtein ConformationAmyloidAmyloid beta-PeptidesG(M1) GangliosideLipid BilayersAlzheimer’s diseaseamyloid-βmolecular dynamicsneuronal membranetransition network

Identifiers

PMID34544868
PMCPMC8488611
OpenAlexW3200190491

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.