Evidence map›Paper›PMID 33662414›Full record

ArticleInternational journal of biological macromolecules2021

Fisetin inhibits tau aggregation by interacting with the protein and preventing the formation of β-strands.

Shifeng Xiao, Yafei Lu, Qiuping Wu, Jiaying Yang, Jierui Chen, Suyue Zhong, David Eliezer, Qiulong Tan, Chengchen Wu

Open access · greenAbstract read
In one paragraph

Article in International journal of biological macromolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 2 pooled it
5.0field-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

21 citing papers in PubMed, 2 syntheses or guidelines pooled it, 52 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  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

9 authors at 2 institutions in 2 countries.

Shifeng XiaoShenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, Guangdong 518060, China; Shenzhen-Hong Kong Institute of Brain Science-Shenzhen Fundamental Research Institutions, Shenzhen, Guangdong 518055, China.
Yafei LuShenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, Guangdong 518060, China.
Qiuping WuShenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, Guangdong 518060, China.
Jiaying YangShenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, Guangdong 518060, China.
Jierui ChenShenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, Guangdong 518060, China.
Suyue ZhongShenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, Guangdong 518060, China.
David EliezerDepartment of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
Qiulong TanShenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, Guangdong 518060, China. Electronic address: tanqiulong@qq.com.
Chengchen WuShenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, Guangdong 518060, China. Electronic address: chengchenwu2020@szu.edu.cn.
Shenzhen University · CNCornell University · US

Funding

Structure and Function of Alpha-SynucleinR37AG019391 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI ELIEZER, DAVID · 2010 to 2019
$3.4M
Structure and Function of TauRF1AG066493 · NIA · WEILL MEDICAL COLL OF CORNELL UNIV · PI ELIEZER, DAVID · 2020 to 2020
$2.4M
NIA NIH HHS R37 AG019391NIA NIH HHS RF1 AG066493
6 · The paper itself

Abstract

Alzheimer's disease is a neurodegenerative disease which severely impacts the health of the elderly. Current treatments are only able to alleviate symptoms, but not prevent or cure the disease. The neurofibrillary tangles formed by tau protein aggregation are one of the defining characteristics of Alzheimer's disease, so tau protein has become a key target for the drug design. In this study, we show that fisetin, a plant-derived polyphenol compound, can inhibit aggregation of the tau fragment, K18, and can disaggregate tau K18 filaments in vitro. Meanwhile it is able to prevent the formation of tau aggregates in cells. Both experimental and computational studies indicate that fisetin could directly interact with tau K18 protein. The binding is mainly created by hydrogen bond and van der Waal force, prevents the formation of β-strands at the two hexapeptide motifs, and does not perturb the secondary structure or the tubulin binding ability of tau protein. In summary, fisetin might be a candidate for further development as a potential preventive or therapeutic drug for Alzheimer's disease.

Indexed as

Alzheimer DiseaseAmino Acid MotifsFlavonolsHumansProtein AggregatesRecombinant Proteinstau ProteinsfisetinFlavonolsMAPT protein, humanProtein AggregatesRecombinant Proteinstau ProteinsAlzheimer's diseaseCompound-protein interactionFisetinMolecular dynamic simulationProtein aggregationTau protein

Identifiers

PMID33662414
PMCPMC9022726
OpenAlexW3134703482

What OpenQuestion holds

Textmetadata
LicenceTDM
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.