Evidence map›Paper›PMID 33652858›Full record

ReviewInternational journal of molecular sciences2021

Natural Products Targeting Amyloid Beta in Alzheimer's Disease.

Joo-Hee Lee, Na-Hyun Ahn, Su-Bin Choi, Youngeun Kwon, Seung-Hoon Yang

Open access · goldAbstract readReview
In one paragraph

Review 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 17 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 2 pooled it
2.4field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 2 syntheses or guidelines pooled it, 40 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Basic and clinical neuroscience · 2025
    Article
  5. Novel Emerging Targets Identification in Reducing Risk of Alzheimer's Disease.Central nervous system agents in medicinal chemistry · 2025
    Review
  6. Phytoactive drugs used in the treatment of Alzheimer's disease and dementia.Naunyn-Schmiedeberg's archives of pharmacology · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Nobiletin prevents amyloid βMetabolic brain disease · 2022
    Article
  15. Article
  16. Review
  17. 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

5 authors at 1 institution in 1 country.

Joo-Hee LeeDepartment of Medical Biotechnology, College of Life Science and Biotechnology, Dongguk University, Seoul 04620, Korea.
Na-Hyun AhnDepartment of Medical Biotechnology, College of Life Science and Biotechnology, Dongguk University, Seoul 04620, Korea.
Su-Bin ChoiDepartment of Medical Biotechnology, College of Life Science and Biotechnology, Dongguk University, Seoul 04620, Korea.
Youngeun KwonDepartment of Medical Biotechnology, College of Life Science and Biotechnology, Dongguk University, Seoul 04620, Korea.
Seung-Hoon YangDepartment of Medical Biotechnology, College of Life Science and Biotechnology, Dongguk University, Seoul 04620, Korea.ORCID 0000-0002-6880-8861
Dongguk University · KR

Funding

National Research Foundation of Korea 2015R1A6A3A04058568National Research Foundation of Korea 2020R1F1A1076240
6 · The paper itself

Abstract

Alzheimer's disease (AD) is a neurodegenerative disease characterized by severe brain damage and dementia. There are currently few therapeutics to treat this disease, and they can only temporarily alleviate some of the symptoms. The pathogenesis of AD is mainly preceded by accumulation of abnormal amyloid beta (Aβ) aggregates, which are toxic to neurons. Therefore, modulation of the formation of these abnormal aggregates is strongly suggested as the most effective approach to treat AD. In particular, numerous studies on natural products associated with AD, aiming to downregulate Aβ peptides and suppress the formation of abnormal Aβ aggregates, thus reducing neural cell death, are being conducted. Generation of Aβ peptides can be prevented by targeting the secretases involved in Aβ-peptide formation (secretase-dependent). Additionally, blocking the intra- and intermolecular interactions of Aβ peptides can induce conformational changes in abnormal Aβ aggregates, whereby the toxicity can be ameliorated (structure-dependent). In this review, AD-associated natural products which can reduce the accumulation of Aβ peptides via secretase- or structure-dependent pathways, and the current clinical trial states of these products are discussed.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesAnimalsBiological ProductsDrug DiscoveryHumansMolecular Targeted TherapyProtein AggregatesProtein ConformationSignal TransductionAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesBiological ProductsProtein AggregatesAlzheimer’s diseaseamyloid betanatural productssecretase-dependentstructure-dependent

Identifiers

PMID33652858
PMCPMC7956407
OpenAlexW3134449768

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.