Evidence map›Paper›PMID 42515573›Full record

ReviewViruses2026

A Comprehensive Review of Coronavirus Non-Structure Protein 6 on Structure, Functions, Mechanisms and Its Implications for Antiviral Research.

Yingzhe Yu, Weimei He, Xiaohui Geng, Yulong He, Huapeng Feng, Jian Chen, Jianhong Shu

Abstract readReview
In one paragraph

Review in Viruses, 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

7 authors.

Yingzhe YuCollege of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.ORCID 0009-0002-8630-1447
Weimei HeHangzhou ISEEVAX Medical Sciences & Technology, Co., Ltd., Hangzhou 310018, China.
Xiaohui GengCollege of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.
Yulong HeCollege of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.ORCID 0000-0002-0265-5946
Huapeng FengCollege of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.ORCID 0000-0002-4889-7609
Jian ChenCollege of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.ORCID 0000-0003-2735-3925
Jianhong ShuCollege of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, China.

Funding

Pioneer 2025C01138
6 · The paper itself

Abstract

Coronaviruses encode a variety of non-structural proteins (NSPs) that collectively mediate viral genome replication, transcription and remodeling of the host cellular microenvironment. As a highly conserved transmembrane protein, non-structural protein 6 (NSP6) predominantly localizes to the endoplasmic reticulum. Through interactions with other viral proteins and host factors, NSP6 participates in multiple pivotal processes, including the formation and stabilization of double-membrane vesicles (DMVs), reprogramming of lipid metabolism, blockade of autophagic flux, and evasion of innate immunity. Recent advances in structural biology and research on virus-host interactions have further elucidated the essential roles of NSP6 throughout the viral life cycle. Mutations in NSP6 are closely associated with viral adaptability, transmissibility and pathogenicity. Herein, we comprehensively review the latest advances on the molecular structure, biological functions and mutation hotspots of coronavirus NSP6, as well as its implications for antiviral research. This review aims to provide a theoretical basis for further dissecting the pathogenic mechanisms of coronaviruses and developing broad-spectrum antiviral drugs.

Indexed as

Antiviral AgentsCoronavirusViral Nonstructural ProteinsAnimalsAutophagyCoronavirus InfectionsEndoplasmic ReticulumHost-Pathogen InteractionsHumansImmunity, InnateMutationVirus ReplicationAntiviral AgentsViral Nonstructural Proteinsantiviral targetautophagycoronavirusdouble-membrane vesicleinnate immunityNSP6

Identifiers

PMID42515573
PMCPMC13431472

What OpenQuestion holds

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LicenceCC BY
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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.