Evidence map›Paper›PMID 41608866›Full record

ArticleMolecular nutrition & food research2026

Biflavonoids can Potentially Inhibit Amyloid Beta Internalization to Mitigate Its Cytotoxic Events.

Md Aminul Haque, Md Selim Hossain, Vijay Sankar Ramasamy, Il Seon Park

Abstract read
In one paragraph

Article in Molecular nutrition & food research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

Md Aminul HaqueSchool of Pharmacy, BRAC University, Merul Badda, Dhaka, Bangladesh.
Md Selim HossainDepartment of Biomedical Sciences, Chosun University, Dong-gu, Gwangju, South Korea.
Vijay Sankar RamasamyDepartment of Biomedical Sciences, Chosun University, Dong-gu, Gwangju, South Korea.
Il Seon ParkDepartment of Biomedical Sciences, Chosun University, Dong-gu, Gwangju, South Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid-β-42 (Aβ42) internalization plays a critical role in Alzheimer's disease (AD) pathology. We investigated whether biflavonoids, natural small molecules, could inhibit Aβ42 uptake and mitigate its cytotoxicity. Biochemical and imaging analyses revealed that biflavonoids dose-dependently blocked Aβ42 internalization, preventing lamin fragmentation and caspase activation which are considered as key steps in Aβ42-induced cell death. Confocal microscopy and Western blotting confirmed reduced Aβ42 entry, while aggregation assays in cell-free conditions demonstrated biflavonoids suppress Aβ42 fibril, oligomer, and β-sheet formation. These findings suggest biflavonoids exert cytoprotective effects by inhibiting both Aβ42 conformational changes and cellular uptake, positioning them as promising anti-amyloidogenic agents for AD therapy.

Indexed as

Amyloid beta-PeptidesBiflavonoidsPeptide FragmentsAlzheimer DiseaseAnimalsCaspasesHumansAmyloid beta-Peptidesamyloid beta-protein (1-42)BiflavonoidsCaspasesPeptide Fragmentsamyloid‐β‐42Aβ42 internalizationbiflavonoidscaspase activationcytoprotectionlamin B fragmentation

Identifiers

PMID41608866
PMCPMC12853324

What Socratic 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 Socratic graph.