Evidence map›Paper›PMID 36221865›Full record

ReviewCurrent neuropharmacology2023

Unveiling the Potential of Polyphenols as Anti-Amyloid Molecules in Alzheimer's Disease.

Eva Rahman Kabir, Namara Mariam Chowdhury, Hasina Yasmin, Md Tanvir Kabir, Rokeya Akter, Asma Perveen, Ghulam Md Ashraf, Shamima Akter, Md Habibur Rahman, Sherouk Hussein Sweilam

Open access · greenAbstract readReview
In one paragraph

Review in Current neuropharmacology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
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

10 authors at 7 institutions in 6 countries.

Eva Rahman KabirSchool of Pharmacy, BRAC University, 66 Mohakhali, Dhaka 1212, Bangladesh.
Namara Mariam ChowdhurySchool of Pharmacy, BRAC University, 66 Mohakhali, Dhaka 1212, Bangladesh.
Hasina YasminDepartment of Pharmacy, Brac University, 66 Mohakhali, Dhaka 1212, Bangladesh.
Md Tanvir KabirSchool of Pharmacy, BRAC University, 66 Mohakhali, Dhaka 1212, Bangladesh.
Rokeya AkterDepartment of Pharmacy, Jagannath University, Dhaka, Bangladesh.
Asma PerveenGlocal School of Life Sciences, Glocal University, Mirzapur Pole, Saharanpur, Uttar Pradesh, India.
Ghulam Md AshrafDepartment of Medical Laboratory Sciences, College of Health Sciences, University of Sharjah, Sharjah 27272, United Arab Emirates.
Shamima AkterDepartment of Bioinformatics and Computational Biology, George Mason University, Fairfax, Virginia 22030, USA.
Md Habibur RahmanDepartment of Pharmacy, Southeast University, Dhaka, Bangladesh.
Sherouk Hussein SweilamDepartment of Pharmacognosy, College of Pharmacy, Prince Sattam Bin Abdulaziz University, Al-Kharj 11942, Saudi Arabia.
BRAC University · BDEgyptian Russian University · EGGeorge Mason University · USGlocal University · INJagannath University · BDSoutheast University · BDUniversity of Sharjah · AE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is a devastating neurodegenerative disease that mostly affects the elderly population. Mechanisms underlying AD pathogenesis are yet to be fully revealed, but there are several hypotheses regarding AD. Even though free radicals and inflammation are likely to be linked with AD pathogenesis, still amyloid-beta (Aβ) cascade is the dominant hypothesis. According to the Aβ hypothesis, a progressive buildup of extracellular and intracellular Aβ aggregates has a significant contribution to the AD-linked neurodegeneration process. Since Aβ plays an important role in the etiology of AD, therefore Aβ-linked pathways are mainly targeted in order to develop potential AD therapies. Accumulation of Aβ plaques in the brains of AD individuals is an important hallmark of AD. These plaques are mainly composed of Aβ (a peptide of 39-42 amino acids) aggregates produced via the proteolytic cleavage of the amyloid precursor protein. Numerous studies have demonstrated that various polyphenols (PPHs), including cyanidins, anthocyanins, curcumin, catechins and their gallate esters were found to markedly suppress Aβ aggregation and prevent the formation of Aβ oligomers and toxicity, which is further suggesting that these PPHs might be regarded as effective therapeutic agents for the AD treatment. This review summarizes the roles of Aβ in AD pathogenesis, the Aβ aggregation pathway, types of PPHs, and distribution of PPHs in dietary sources. Furthermore, we have predominantly focused on the potential of food-derived PPHs as putative anti-amyloid drugs.

Indexed as

Alzheimer DiseaseNeurodegenerative DiseasesAgedAmyloidAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnthocyaninsHumansPlaque, AmyloidAmyloidAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnthocyaninsAlzheimer’s diseaseamyloid precursor proteinAβneurodegenerative diseaseneuroprotectionpolyphenols

Identifiers

PMID36221865
PMCPMC10227919
OpenAlexW4304631631

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.