ArticleFrontiers in pharmacology2025
Emodin mitigates rheumatoid arthritis through direct binding to TNF-α.
Article in Frontiers in pharmacology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers, 1 of them a synthesis that pooled it.
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Who cites it
4 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The role of TNF signaling pathway in post-stroke cognitive impairment: a systematic review.Annals of medicine · 2025Pooled it
- Integrated network pharmacology and experimental validation to elucidate the mechanism of Lysimachia paridiformis var. stenophylla Franch. in rheumatoid arthritis.Scientific reports · 2026Article
- STAT1 transcriptionally activates CXCL13 to promote cell inflammation and proliferation and inhibit cell apoptosis in rheumatoid arthritis fibroblast-like synoviocytes.Journal of orthopaedic surgery and research · 2026Article
- The Therapeutic Potential of Phytochemicals Unlocks New Avenues in the Management of Rheumatoid Arthritis.International journal of molecular sciences · 2025Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Emodin has shown certain anti-rheumatoid arthritis (RA) activity in preliminary studies. However, the precise mechanisms of emodin's anti-RA effects, particularly its direct targets, remain unclear. This study aimed to evaluate the anti-RA activity of emodin and elucidate its potential mechanisms, with a specific focus on identifying its molecular targets. Employing a collagen-induced arthritis (CIA) rat model, along with transcriptomic analysis, thermal proteome profiling (TPP) and TNF-α-induced L929 cell model, the anti-RA activity of emodin was confirmed, identifying TNF-α as a potential target. Techniques such as drug affinity responsive target stability (DARTS), cellular thermal shift assay (CETSA), Affinity ultrafiltration-liquid chromatography/mass spectrometry (AUF-LC/MS), surface plasmon resonance (SPR) and bio-layer interferometry (BLI) validated the direct binding of emodin to TNF-α. Molecular dynamics simulation, ELISA and BLI further revealed that emodin stabilizes the asymmetric trimeric structure of TNF-α, disrupting the TNF-α-TNFR1 interaction.
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Registered trials
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