Evidence map›Paper›PMID 41104677›Full record

ArticleACS nano2025

RNA Binding Sensitivity of Nonstructural Protein 8 Revealed by Small-Angle Neutron Scattering and Alphafold2 Prediction.

Xin Jiang, Jinxin Xu, Zhenyu Liao, Na Wang, Taisen Zuo, Changli Ma, Hanqiu Jiang, Yubin Ke, He Cheng, Howard Wang and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS nano, 2025. 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

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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

14 authors.

Xin JiangDepartment of Physics, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong 999077, China.
Jinxin XuState Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China.
Zhenyu LiaoDepartment of Materials Science and Engineering, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong 999077, China.
Na WangState Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China.
Taisen ZuoSpallation Neutron Source Science Center, Dongguan, Guangdong 523803, China.ORCID 0000-0001-6741-5399
Changli MaSpallation Neutron Source Science Center, Dongguan, Guangdong 523803, China.
Hanqiu JiangSpallation Neutron Source Science Center, Dongguan, Guangdong 523803, China.
Yubin KeSpallation Neutron Source Science Center, Dongguan, Guangdong 523803, China.
He ChengSpallation Neutron Source Science Center, Dongguan, Guangdong 523803, China.ORCID 0000-0001-8718-4110
Howard WangNeutron Science Platform, Songshan Lake Materials Laboratory, Dongguan, Guangdong 523808, China.ORCID 0000-0001-9905-4049
Jinkui ZhaoNeutron Science Platform, Songshan Lake Materials Laboratory, Dongguan, Guangdong 523808, China.
Jun FanDepartment of Materials Science and Engineering, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong 999077, China.ORCID 0000-0001-8227-9671
Jinsong LiuState Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China.ORCID 0000-0003-2317-0558
Xiangqiang ChuDepartment of Physics, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong 999077, China.ORCID 0000-0003-4320-5316

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The flexible structure enables nonstructural protein 8 (nsp8) to respond quickly to environmental changes, which are essential for RNA replication and transcription of SARS-CoV-2. In this work, small-angle neutron scattering and AlphaFold2 prediction were applied to characterize the structural change of SARS-CoV-2 nsp8 dimers and tetramers. The results demonstrated that the nsp8 tetramer with a more exposed core domain shows a low thermal stability. The exposed core domain increases its sensitivity to RNA and adapts its structure to interact with RNA. Our work reveals the structural difference between the two forms of SARS-CoV-2 nsp8s in the RNA synthesis process, which partly elucidates the molecular mechanism behind RNA replication of the RNA virus.

Indexed as

RNA, ViralSARS-CoV-2Viral Nonstructural ProteinsModels, MolecularNeutron DiffractionProtein BindingScattering, Small AngleRNA, ViralViral Nonstructural ProteinsNonstructural protein 8 (Nsp8)RNA-protein complexSmall angle neutron scattering (SANS)Structural flexibilityThermal stability

Identifiers

PMID41104677
PMCPMC12574207

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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.