Evidence map›Paper›PMID 39283364›Full record

ArticleJournal of natural medicines2025

Azamollugin, a mollugin derivative, has inhibitory activity on MyD88- and TRIF-dependent pathways.

Yuki Nakajima, Hitomi Nishino, Kazunori Takahashi, Alfarius Eko Nugroho, Yusuke Hirasawa, Toshio Kaneda, Hiroshi Morita

Abstract read
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In one paragraph

Article in Journal of natural medicines, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

7 authors.

Yuki NakajimaSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41 Shinagawa-Ku, Tokyo, 142-8501, Japan.
Hitomi NishinoSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41 Shinagawa-Ku, Tokyo, 142-8501, Japan.
Kazunori TakahashiSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41 Shinagawa-Ku, Tokyo, 142-8501, Japan.
Alfarius Eko NugrohoSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41 Shinagawa-Ku, Tokyo, 142-8501, Japan.
Yusuke HirasawaSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41 Shinagawa-Ku, Tokyo, 142-8501, Japan.
Toshio KanedaSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41 Shinagawa-Ku, Tokyo, 142-8501, Japan. kaneda@hoshi.ac.jp.
Hiroshi MoritaSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41 Shinagawa-Ku, Tokyo, 142-8501, Japan. moritah@hoshi.ac.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previously, we reported that azamollugin, an aza-derivative of mollugin, exhibited potent inhibitory activity on NO production in LPS-stimulated RAW 264.7 cells. Further investigations in this study revealed that azamollugin not only suppressed iNOS gene expression regulated by NF-κB, but also inhibited LPS-induced IFN-β expression, which is known to be regulated by IRF3. Azamollugin exhibited an inhibitory activity on LPS-induced IRAK1 activation, suggesting inhibitory effect on the MyD88-dependent pathway. Furthermore, azamollugin inhibited LPS-induced phosphorylation of IRF3 and its upstream factor, TBK1/IKKε, suggesting an inhibitory effect on the TRIF-dependent pathway via TLR4. In addition, azamollugin also suppressed poly(I:C)-induced phosphorylation of TBK1 and IRF3, suggesting an inhibitory effect on the TRIF-dependent pathway via TLR3. These results suggest that azamollugin has inhibitory activity against both the MyD88-dependent and TRIF-dependent pathways, respectively.

Indexed as

Adaptor Proteins, Vesicular TransportMyeloid Differentiation Factor 88Signal TransductionAnimalsInterferon-betaInterferon Regulatory Factor-3Interleukin-1 Receptor-Associated KinasesLipopolysaccharidesMiceNF-kappa BNitric Oxide Synthase Type IIPhosphorylationProtein Serine-Threonine KinasesRAW 264.7 CellsAdaptor Proteins, Vesicular TransportInterferon-betaInterferon Regulatory Factor-3Interleukin-1 Receptor-Associated KinasesLipopolysaccharidesMyd88 protein, mouseMyeloid Differentiation Factor 88NF-kappa BNitric Oxide Synthase Type IIProtein Serine-Threonine KinasesTbk1 protein, mouseTicam1 protein, mouseAnti-inflammatoryAzamolluginIFN-βIKKεIRAK1IRF3MolluginNF-κBOxomolluginTBK1

Identifiers

PMID39283364

What OpenQuestion holds

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Registered trials

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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.