Evidence map›Paper›PMID 38888760›Full record

ReviewThe Journal of membrane biology2024

Aggregation Behavior of Amyloid Beta Peptide Depends Upon the Membrane Lipid Composition.

Lipika Mirdha

Abstract readReview
PubMed Publisher
In one paragraph

Review in The Journal of membrane biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Neuroinflammation in Alzheimer disease.Nature reviews. Immunology · 2025
    Review
  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

1 author.

Lipika MirdhaSchool of Chemistry, Sambalpur University, Jyoti Vihar, Burla, Odisha, 768 019, India. lipika@suniv.ac.in.

Funding

Science and Engineering Research Board File No. CRG/2023/000386
6 · The paper itself

Abstract

Protein aggregation plays a crucial role in the development of several neurodegenerative diseases. It is important to understand the aggregation process for the detection of the onset of these diseases. Alzheimer's Disease (AD) is one of the most prevalent neurodegenerative diseases caused by the aggregation of Aβ-40 and Aβ-42 peptides. The smaller oligomers lead to the formation of protein plaque at the neural membranes leading to memory loss and other disorders. Interestingly, aggregation takes place at the neural membranes, therefore the membrane composition seems to play an important role in the aggregation process. Despite a large number of literatures on the effect of lipid composition on protein aggregation, there are very few concise reviews that highlight the role of membrane composition in protein aggregation. In this review, we have discussed the implication of membrane composition on the aggregation of amyloid beta peptide with a special emphasis on cholesterol. We have further discussed the role of the degree of unsaturation of fatty acids and the participation of apolipoprotein E4 (ApoE4) in the onset of AD.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesMembrane LipidsAnimalsCell MembraneCholesterolHumansPeptide FragmentsProtein AggregatesProtein Aggregation, PathologicalAmyloid beta-PeptidesCholesterolMembrane LipidsPeptide FragmentsProtein AggregatesAggregationAmyloid peptidesApolipoprotein ECholesterolFatty acidsLipid composition

Identifiers

What OpenQuestion holds

Textmetadata
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.