Evidence map›Paper›PMID 42823417›Full record

ArticleNature communications2026

Identifying a broad-spectrum influenza inhibitor that blocks multiple functions of viral NS1 protein.

Yang Zhang, Yanan Luo, Wenrui Gai, Jinyu Wang, Lianghao Huang, Zihan Wang, Lishan Sun, Wanting Jiao, Wei Wang, Dehai Li

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Yang Zhang *Key Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China.
Yanan Luo *Key Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China.
Wenrui Gai *Key Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China.
Jinyu WangKey Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China.
Lianghao HuangKey Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China.
Zihan WangKey Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China.
Lishan SunKey Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China.
Wanting JiaoFerrier Research Institute, Victoria University of Wellington, Wellington, New Zealand.ORCID 0000-0002-0234-7206
Wei WangKey Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China. wwwakin@ouc.edu.cn.ORCID 0000-0002-6548-6422
Dehai LiKey Laboratory of Marine Drugs, Chinese Ministry of Education; School of Medicine and Pharmacy, Ocean University of China, Qingdao, PR China. dehaili@ouc.edu.cn.ORCID 0000-0002-7191-2002

Funding

National Natural Science Foundation of China (National Science Foundation of China) 81973234National Natural Science Foundation of China (National Science Foundation of China) 82173860National Natural Science Foundation of China (National Science Foundation of China) 82504874Natural Science Foundation of Shandong Province (Shandong Provincial Natural Science Foundation) ZR2025MS1301
6 · The paper itself

Abstract

Nonstructural protein 1 (NS1) is the key virulence factor of influenza A virus (IAV) that affects the replication and pathogenicity of IAV, which can be used as a promising anti-IAV target. Herein, we identify a marine derived NS1 inhibitor HDN2398 with broad-spectrum anti-IAV effects in different cell lines and female mice, superior to oseltamivir and baloxavir. HDN2398 attenuates the interferon antagonist function of NS1 by blocking NS1 dimerization and its binding to dsRNA. HDN2398 can block NS1 nucleolar localization, viral mRNA splicing and nuclear export through destroying the interaction between NS1 and nucleolin or NXF1. Phe9 and Trp187 may be required for the interaction between HDN2398 and NS1. In summary, our findings support the development of HDN2398 as a promising anti-IAV agent targeting NS1-host interaction.

Indexed as

Antiviral AgentsInfluenza A virusViral Nonstructural ProteinsAnimalsDibenzothiepinsDogsFemaleHumansInfluenza, HumanMadin Darby Canine Kidney CellsMiceMorpholinesOrthomyxoviridae InfectionsOseltamivirPyridinesPyridonesAntiviral AgentsbaloxavirDibenzothiepinsINS1 protein, influenza virusMorpholinesOseltamivirPyridinesPyridonesRNA-Binding ProteinsThiepinsTriazinesViral Nonstructural Proteins

Identifiers

PMID42823417
PMCPMC13631329

What OpenQuestion holds

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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.