ArticleRSC chemical biology2026
Affinity-based protein profiling of the antiviral natural product nanchangmycin.
Article in RSC chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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.
Who cites it
1 citing paper in PubMed.
- A high throughput assay to identify modulators of Death Receptor 3 (DR3).SLAS discovery : advancing life sciences R & D · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nanchangmycin is a natural product with broad-spectrum activity against various organisms, exhibiting antibiotic, antiviral, anticancer, and antifibrotic effects. Nanchangmycin belongs to the family of polyether ionophores and is proposed to exert its therapeutic effects by altering ion gradients across biological membranes. Although this therapeutic mechanism has been well characterised in cancer models, it does not fully explain how nanchangmycin inhibits Zika virus infection, as recently reported. The specific molecular targets responsible for mediating nanchangmycin's antiviral activity remain unknown. Here, we designed a photoreactive clickable nanchangmycin probe and employed chemical proteomics to identify protein targets of nanchangmycin related to Zika virus infection in human cells. Among the most prominent targets was the protein SEC11A, a key component of the signal peptidase complex, which is essential for cleaving and processing Zika virus proteins. We showed that nanchangmycin blocks the cleavage of a Zika virus polyprotein, suggesting a novel mechanism for nanchangmycin-mediated inhibition of Zika virus infection.
Identifiers
What OpenQuestion holds
Registered trials
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.