Evidence map›Paper›PMID 38836448›Full record

ArticleThe journal of physical chemistry. B2024

Modulation of Lipid Dynamics in the β-Amyloid Aggregates Induced Membrane Fragmentation.

Wei Qiang, Maurine K Kengewerere, June M Kenyaga

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Review
  3. Membrane-assisted Aβ40 aggregation pathways.Cell reports. Physical science · 2025
    Article
  4. Membrane-assisted Aβ40 aggregation pathways.bioRxiv : the preprint server for biology · 2024
    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

3 authors.

Wei QiangDepartment of Chemistry, Binghamton University, State University of New York, Binghamton, New York 13902, United States.ORCID 0000-0002-0044-810X
Maurine K KengewerereDepartment of Chemistry, Binghamton University, State University of New York, Binghamton, New York 13902, United States.
June M KenyagaDepartment of Chemistry, Binghamton University, State University of New York, Binghamton, New York 13902, United States.

Funding

Molecular Structural Basis of Non-specific Neuronal Membrane Disruption Induced by Early-Stage Beta-Amyloid Peptide AggregationR01GM125853 · NIGMS · STATE UNIVERSITY OF NY,BINGHAMTON · PI Wei Qiang · 2018 to 2026
$2.5M
NIGMS NIH HHS R01 GM125853
6 · The paper itself

Abstract

Nonspecific membrane disruption is considered a plausible mechanism for the cytotoxicity induced by β-amyloid (Aβ) aggregates. In scenarios of high local Aβ concentrations, a two-step membrane fragmentation model has been proposed. Initially, membrane-embedded Aβ oligomeric aggregates form, followed by membrane fragmentation. However, the key molecular-level interactions between Aβ oligomeric aggregates and lipids that drive the second-stage membrane fragmentation remain unclear. This study monitors the time-dependent changes in lipid dynamics and water accessibility of model liposomes during Aβ-induced membrane fragmentation. Our results indicate that lipid dynamics on the nanosecond to microsecond time scale undergo rapid acceleration upon initial incubation with membrane-incorporated Aβ oligomeric aggregates, followed by a slow deceleration process. Concurrently, lipid headgroups become less accessible to water. Both observations suggest a carpet-like mechanism of membrane disruption for the Aβ-induced membrane fragmentation process.

Indexed as

Amyloid beta-PeptidesCell MembraneLiposomesProtein AggregatesWaterAmyloid beta-PeptidesLiposomesProtein AggregatesWater

Identifiers

PMID38836448
PMCPMC11811819

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.