Evidence map›Paper›PMID 31234523›Full record

ReviewMolecules (Basel, Switzerland)2019

Inhibition of the Self-Assembly of Aβ and of Tau by Polyphenols: Mechanistic Studies.

Qiuchen Zheng, Micheal T Kebede, Merc M Kemeh, Saadman Islam, Bethany Lee, Stuart D Bleck, Liliana A Wurfl, Noel D Lazo

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
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  15. Review
  16. Highly toxic Aβ begets more Aβ.Neural regeneration research · 2024
    Article
  17. Article
  18. Rationally Designed Peptoid Inhibitors of Amyloid-β Oligomerization.Chembiochem : a European journal of chemical biology · 2024
    Article
  19. Review
  20. 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

8 authors at 1 institution in 1 country.

Qiuchen ZhengCarlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, USA. qzheng@clarku.edu.
Micheal T KebedeCarlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, USA. mkebede@clarku.edu.
Merc M KemehCarlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, USA. mkemeh@clarku.edu.
Saadman IslamCarlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, USA. sislam@clarku.edu.
Bethany LeeCarlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, USA. blee@clarku.edu.
Stuart D BleckCarlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, USA. sbleck@clarku.edu.
Liliana A WurflCarlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, USA. lwurfl@clarku.edu.
Noel D LazoCarlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610, USA. nlazo@clarku.edu.ORCID 0000-0003-1769-7572
Clark University · US

Funding

Determinants of the Proteolytic Degradation of Soluble Amyloid-betaR15AG055043 · NIA · CLARK UNIVERSITY (WORCESTER, MA) · PI LAZO, NOEL D. · 2018 to 2018
$376k
NIA NIH HHS R15 AG055043NIA NIH HHS R15AG055043
6 · The paper itself

Abstract

The amyloid-β (Aβ) peptide and tau protein are thought to play key neuropathogenic roles in Alzheimer's disease (AD). Both Aβ and tau self-assemble to form the two major pathological hallmarks of AD: amyloid plaques and neurofibrillary tangles, respectively. In this review, we show that naturally occurring polyphenols abundant in fruits, vegetables, red wine, and tea possess the ability to target pathways associated with the formation of assemblies of Aβ and tau. Polyphenols modulate the enzymatic processing of the amyloid-β precursor protein and inhibit toxic Aβ oligomerization by enhancing the clearance of Aβ42 monomer, modulating monomer-monomer interactions and remodeling oligomers to non-toxic forms. Additionally, polyphenols modulate tau hyperphosphorylation and inhibit tau β-sheet formation. The anti-Aβ-self-assembly and anti-tau-self-assembly effects of polyphenols increase their potential as preventive or therapeutic agents against AD, a complex disease that involves many pathological mechanisms.

Indexed as

Amyloid beta-PeptidesAnimalsHumansModels, MolecularMolecular StructurePhosphorylationPolyphenolsProtein AggregatesProtein Aggregation, PathologicalProtein BindingProtein MultimerizationStructure-Activity Relationshiptau ProteinsAmyloid beta-PeptidesPolyphenolsProtein Aggregatestau ProteinsAlzheimer′s diseaseamyloid assembliesamyloid-β self-assemblyneurofibrillary tanglespolyphenolstau hyperphosphorylationtau self-assembly

Identifiers

PMID31234523
PMCPMC6630797
OpenAlexW2950603038

What OpenQuestion 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 OpenQuestion graph.