Evidence map›Paper›PMID 39941148›Full record

ArticleInternational journal of molecular sciences2025

Molecular Simulation of the Binding of Amyloid Beta to Apolipoprotein A-I in High-Density Lipoproteins.

Chris J Malajczuk, Ricardo L Mancera

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2025. 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. Review
  4. 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

2 authors.

Chris J MalajczukCurtin Medical School and Curtin Medical Research Institute, Curtin University, GPO Box U1987, Perth, WA 6845, Australia.ORCID 0000-0002-8865-090X
Ricardo L ManceraCurtin Medical School and Curtin Medical Research Institute, Curtin University, GPO Box U1987, Perth, WA 6845, Australia.ORCID 0000-0002-9191-5622

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Disrupted clearance of amyloid beta (Aβ) from the brain enhances its aggregation and formation of amyloid plaques in Alzheimer's disease. The most abundant protein constituent of circulating high-density lipoprotein (HDL) particles, apoA-I, readily crosses the blood-brain barrier from periphery circulation, exhibits low-micromolar binding affinity for soluble, neurotoxic forms of Aβ, and modulates Aβ aggregation and toxicity in vitro. Its highly conserved N-terminal sequence,

Indexed as

Amyloid beta-PeptidesApolipoprotein A-ILipoproteins, HDLMolecular Dynamics SimulationAlzheimer DiseaseBinding SitesHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsProtein BindingAmyloid beta-PeptidesApolipoprotein A-ILipoproteins, HDLAlzheimer’s diseaseamyloid betaapoA-IHDLmolecular dynamics simulation

Identifiers

PMID39941148
PMCPMC11818119

What OpenQuestion holds

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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.