Evidence map›Paper›PMID 33809196›Full record

ArticleInternational journal of molecular sciences2021

Biflavonoid-Induced Disruption of Hydrogen Bonds Leads to Amyloid-β Disaggregation.

Peter K Windsor, Stephen P Plassmeyer, Dominic S Mattock, Jonathan C Bradfield, Erika Y Choi, Bill R Miller, Byung Hee Han

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Gas Tunnel Engineering of Prolyl Hydroxylase Reprograms Hypoxia Signaling in Cells.Angewandte Chemie (International ed. in English) · 2024
    Article
  6. Article
  7. Review
  8. Identification of Catechins' Binding Sites in Monomeric AInternational journal of molecular sciences · 2023
    Article
  9. Review
  10. Neuro-Nutraceutical Polyphenols: How Far Are We?Antioxidants (Basel, Switzerland) · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Molecular mechanisms of amyloid disaggregation.Journal of advanced research · 2022
    Review
  15. Article
  16. 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

7 authors at 2 institutions in 1 country.

Peter K WindsorDepartment of Chemistry, Truman State University, Kirksville, MO 63501, USA.ORCID 0000-0002-9490-7046
Stephen P PlassmeyerDepartment of Chemistry, Truman State University, Kirksville, MO 63501, USA.
Dominic S MattockDepartment of Chemistry, Truman State University, Kirksville, MO 63501, USA.ORCID 0000-0002-1346-0968
Jonathan C BradfieldDepartment of Chemistry, Truman State University, Kirksville, MO 63501, USA.
Erika Y ChoiDepartment of Pharmacology, A.T. Still University, Kirksville, MO 63501, USA.
Bill R MillerDepartment of Chemistry, Truman State University, Kirksville, MO 63501, USA.
Byung Hee HanDepartment of Pharmacology, A.T. Still University, Kirksville, MO 63501, USA.
Truman State University · USA.T. Still University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deposition of amyloid β (Aβ) fibrils in the brain is a key pathologic hallmark of Alzheimer's disease. A class of polyphenolic biflavonoids is known to have anti-amyloidogenic effects by inhibiting aggregation of Aβ and promoting disaggregation of Aβ fibrils. In the present study, we further sought to investigate the structural basis of the Aβ disaggregating activity of biflavonoids and their interactions at the atomic level. A thioflavin T (ThT) fluorescence assay revealed that amentoflavone-type biflavonoids promote disaggregation of Aβ fibrils with varying potency due to specific structural differences. The computational analysis herein provides the first atomistic details for the mechanism of Aβ disaggregation by biflavonoids. Molecular docking analysis showed that biflavonoids preferentially bind to the aromatic-rich, partially ordered N-termini of Aβ fibril via the π-π interactions. Moreover, docking scores correlate well with the ThT EC

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesBenzothiazolesBiflavonoidsBrainHumansHydrogen BondingMolecular Docking SimulationMolecular Dynamics SimulationProtein Aggregation, PathologicalamentoflavoneAmyloidAmyloid beta-PeptidesBenzothiazolesBiflavonoidsthioflavin TAlzheimer’s diseaseamentoflavoneamyloid aggregationanti-amyloid compoundsdrug discoverynaturally occurring flavonoidsneurodegenerative diseasepolyphenols

Identifiers

PMID33809196
PMCPMC8001082
OpenAlexW3139468163

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.