Evidence map›Paper›PMID 41399519›Full record

ArticleiScience2025

The regulatory mechanisms of SARS-CoV-2 N protein helicase and its annealing activity.

Bo Zhang, Peng Zhou, Zhaoling Lan, Chaoshao Yang, Jida Li, Yi Zhang, Long Gao, Hongyi Wang, Cai Meng, Shizheng Wei and 4 more

Abstract read
In one paragraph

Article in iScience, 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

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

14 authors.

Bo ZhangCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Peng ZhouCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Zhaoling LanCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Chaoshao YangCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Jida LiSchool of Public Health, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Yi ZhangSchool of Public Health, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Long GaoCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Hongyi WangCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Cai MengCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Shizheng WeiCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Chenglang RuanCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Yangxue DaiCollege of Basic Medicine, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Yan XieSchool of Public Health, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.
Yang LiuSchool of Public Health, Zunyi Medical University, Zunyi, Guizhou Province 563000, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nucleocapsid (N) protein of SARS-CoV-2 performs multiple functions essential for viral replication and host adaptation. Here, we identify ionic strength as a critical determinant of its dual nucleic acid-manipulating activities. Under low-salt conditions (≤100 mM NaCl), SARS-CoV-2 N primarily promotes strand annealing, whereas at high ionic strength (≥300 mM NaCl), its helicase activity is additively enhanced. SARS-CoV-2 N also preferentially acts on DNA rather than RNA substrates and modulates the helicase activity of Nsp13 in an ion-dependent manner-inhibiting it under low-salt conditions but enhancing it under high-salt conditions. These findings reveal an ion concentration-dependent regulatory mechanism that enables SARS-CoV-2 N to dynamically switch between distinct biochemical states, thereby supporting viral adaptability and providing new insights into antiviral development.

Indexed as

BiochemistryBiophysicsVirology

Identifiers

PMID41399519
PMCPMC12702239

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.