Evidence map›Paper›PMID 33339319›Full record

ArticleMolecules (Basel, Switzerland)2020

Chalcones Display Anti-NLRP3 Inflammasome Activity in Macrophages through Inhibition of Both Priming and Activation Steps-Structure-Activity-Relationship and Mechanism Studies.

Wohn-Jenn Leu, Jung-Chun Chu, Jui-Ling Hsu, Chi-Min Du, Yi-Huei Jiang, Lih-Ching Hsu, Wei-Jan Huang, Jih-Hwa Guh

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

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

13 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Chalcone: A potential scaffold for NLRP3 inflammasome inhibitors.European journal of medicinal chemistry reports · 2023
    Article
  10. Review
  11. Review
  12. Article
  13. Inflammasome Inhibitors.Molecules (Basel, Switzerland) · 2021
    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

8 authors at 2 institutions in 1 country.

Wohn-Jenn LeuSchool of Pharmacy, College of Medicine, National Taiwan University, No. 33, Linsen S. Rd, Taipei 100, Taiwan.
Jung-Chun ChuGraduate Institute of Pharmacognosy, Taipei Medical University, No. 250, Wuxing St., Taipei 110, Taiwan.
Jui-Ling HsuSchool of Pharmacy, College of Medicine, National Taiwan University, No. 33, Linsen S. Rd, Taipei 100, Taiwan.
Chi-Min DuSchool of Pharmacy, College of Medicine, National Taiwan University, No. 33, Linsen S. Rd, Taipei 100, Taiwan.
Yi-Huei JiangSchool of Pharmacy, College of Medicine, National Taiwan University, No. 33, Linsen S. Rd, Taipei 100, Taiwan.
Lih-Ching HsuSchool of Pharmacy, College of Medicine, National Taiwan University, No. 33, Linsen S. Rd, Taipei 100, Taiwan.
Wei-Jan HuangGraduate Institute of Pharmacognosy, Taipei Medical University, No. 250, Wuxing St., Taipei 110, Taiwan.
Jih-Hwa GuhSchool of Pharmacy, College of Medicine, National Taiwan University, No. 33, Linsen S. Rd, Taipei 100, Taiwan.ORCID 0000-0002-6738-6054
National Taiwan University · TWTaipei Medical University · TW

Funding

Ministry of Science and Technology, Taiwan MOST 107-2320-B-002-018-MY3 and MOST 106-2320-B-002 -005 -MY3
6 · The paper itself

Abstract

Chalcones are responsible for biological activity throughout fruits, vegetables, and medicinal plants in preventing and treating a variety of inflammation-related diseases. However, their structure-activity relationship (SAR) in inhibiting inflammasome activation has not been explored. We synthesized numerous chalcones and determined their SAR on lipopolysaccharide (LPS)-primed ATP-induced NLRP3 inflammasome activation. 11Cha1 displayed good inhibitory activity on release reaction of caspase-1, IL-1β, and IL-18. It significantly inhibited LPS-induced phosphorylation and proteolytic degradation of IĸB-α and nuclear translocation of NF-ĸB, but had little effect on mitogen-activated protein kinases (MAPKs) activities. Furthermore, 11Cha1 blocked LPS-induced up-regulation of NLRP3, pro-caspase-1, ASC, IL-18, and IL-1β, indicating the suppression on priming step of inflammasome activation. ASC dimerization and oligomerization are considered to be direct evidence for inflammasome activation. 11Cha1 profoundly inhibited ATP-induced formation of ASC dimers, trimers, and oligomers, and the assembly of ASC, pro-caspase-1, and NLRP3 in inflammasome formation. Decrease of intracellular K

Indexed as

Adenosine TriphosphateCaspase 1Cell LineChalconesDimerizationHumansInflammasomesInterleukin-1betaLipopolysaccharidesMacrophagesNF-kappa BNF-KappaB Inhibitor alphaNLR Family, Pyrin Domain-Containing 3 ProteinPhosphorylationPyroptosisStructure-Activity RelationshipAdenosine TriphosphateCaspase 1ChalconesInflammasomesInterleukin-1betaLipopolysaccharidesNF-kappa BNF-KappaB Inhibitor alphaNLR Family, Pyrin Domain-Containing 3 ProteinATPchalconeK+ effluxNF-ĸBNLRP3 inflammasomestructure-activity relationship

Identifiers

PMID33339319
PMCPMC7767297
OpenAlexW3111967981

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.