Evidence map›Paper›PMID 38564154›Full record

ArticleJournal of natural medicines2024

Oxomollugin, an oxidized substance in mollugin, inhibited LPS-induced NF-κB activation via the suppressive effects on essential activation factors of TLR4 signaling.

Yuki Nakajima, Naohide Tsuboi, Kumiko Katori, Maigunuer Waili, Alfarius Eko Nugroho, Kazunori Takahashi, Hitomi Nishino, Yusuke Hirasawa, Yoko Kawasaki, Yukihiro Goda and 2 more

Abstract read
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In one paragraph

Article in Journal of natural medicines, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.9field-weighted citation impact, top 11% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
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  3. Review
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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

12 authors at 3 institutions in 1 country.

Yuki NakajimaSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41, Shinagawa-ku, Tokyo, 142-8501, Japan.
Naohide TsuboiSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41, Shinagawa-ku, Tokyo, 142-8501, Japan.
Kumiko KatoriSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41, Shinagawa-ku, Tokyo, 142-8501, Japan.
Maigunuer WailiSchool 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.
Kazunori TakahashiSchool 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.
Yusuke HirasawaSchool of Pharmacy and Pharmaceutical Sciences, Hoshi University, Ebara 2-4-41, Shinagawa-ku, Tokyo, 142-8501, Japan.
Yoko KawasakiNational Institute of Health Sciences, 3-25-26 Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa, 210-9501, Japan.
Yukihiro GodaNational Institute of Health Sciences, 3-25-26 Tonomachi, Kawasaki-ku, Kawasaki, Kanagawa, 210-9501, 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.
Ebara (Japan) · JPHoshi University · JPNational Institute of Health Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxomollugin is a degraded product of mollugin and was found to be an active compound that inhibits LPS-induced NF-κB activation. In this study, we investigated the inhibitory activity of oxomollugin, focusing on TLR4 signaling pathway, resulting in NF-κB activation. Oxomollugin inhibited the LPS-induced association of essential factors for initial activation of TLR4 signaling, MyD88, IRAK4 and TRAF6. Furthermore, oxomollugin showed suppressive effects on LPS-induced modification of IRAK1, IRAK2 and TRAF6, LPS-induced association of TRAF6-TAK1/TAB2, and followed by IKKα/β phosphorylation, which critical in signal transduction leading to LPS-induced NF-κB activation. The consistent results suggested that oxomollugin inhibits LPS-induced NF-κB activation via the suppression against signal transduction in TLR4 signaling pathway.The activities of oxomollugin reported in this study provides a deeper understanding on biological activity of mollugin derivatives as anti-inflammatory compounds.

Indexed as

LipopolysaccharidesNF-kappa BSignal TransductionToll-Like Receptor 4AnimalsHumansLactonesMiceMyeloid Differentiation Factor 88PhosphorylationRAW 264.7 CellsResorcinolsZearalenone7-oxozeanolLactonesLipopolysaccharidesMyeloid Differentiation Factor 88NF-kappa BResorcinolsTLR4 protein, humanToll-Like Receptor 4ZearalenoneAnti-inflammatoryIRAKMolluginMyD88NF-κBOxomolluginTLR4TRAF6

Identifiers

PMID38564154
OpenAlexW4393512828

What OpenQuestion holds

Textmetadata
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.