Evidence map›Paper›PMID 36574473›Full record

ArticleACS chemical neuroscience2023

A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ

Kevin N Baumann, Greta Šneiderienė, Michele Sanguanini, Matthias Schneider, Oded Rimon, Alicia González Díaz, Heather Greer, Dev Thacker, Sara Linse, Tuomas P J Knowles and 1 more

Open access · hybridAbstract read
In one paragraph

Article in ACS chemical neuroscience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 19% 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

8 citing papers in PubMed, 1 synthesis or guideline pooled it, 11 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Lipid-induced condensate formation from the Alzheimer's Aβ peptide triggers amyloid aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. 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

11 authors at 2 institutions in 3 countries.

Kevin N BaumannYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.ORCID 0000-0001-5613-6394
Greta ŠneiderienėYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.
Michele SanguaniniYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.
Matthias SchneiderYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.ORCID 0000-0002-1894-1859
Oded RimonYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.ORCID 0000-0002-5848-2968
Alicia González DíazYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.
Heather GreerYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.
Dev ThackerDepartment of Biochemistry and Structural Biology, Lund University, LundSE22100, Sweden.
Sara LinseDepartment of Biochemistry and Structural Biology, Lund University, LundSE22100, Sweden.ORCID 0000-0001-9629-7109
Tuomas P J KnowlesYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.ORCID 0000-0002-7879-0140
Michele VendruscoloYusuf Hamied Department of Chemistry, University of Cambridge, CambridgeCB2 1EW, U.K.ORCID 0000-0002-3616-1610
University of Cambridge · GBLund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aggregation of the amyloid β (Aβ) peptide is one of the molecular hallmarks of Alzheimer's disease (AD). Although Aβ deposits have mostly been observed extracellularly, various studies have also reported the presence of intracellular Aβ assemblies. Because these intracellular Aβ aggregates might play a role in the onset and progression of AD, it is important to investigate their possible origins at different locations of the cell along the secretory pathway of the amyloid precursor protein, from which Aβ is derived by proteolytic cleavage. Senile plaques found in AD are largely composed of the 42-residue form of Aβ (Aβ

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBiomimeticsHumansKineticsLipid BilayersPeptide FragmentsAmyloid beta-PeptidesLipid BilayersPeptide Fragmentsaggregation kineticsAlzheimer’s diseaseamyloid βcryo-electron microscopylipid membranesprotein aggregation

Identifiers

PMID36574473
PMCPMC9853501
OpenAlexW4313236105

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.