Evidence map›Paper›PMID 24418573›Full record

ReviewAntiviral research2014

The SARS coronavirus nucleocapsid protein--forms and functions.

Chung-ke Chang, Ming-Hon Hou, Chi-Fon Chang, Chwan-Deng Hsiao, Tai-huang Huang

Abstract readReview
In one paragraph

Review in Antiviral research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 307 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
307citing papers in PubMed, 2 pooled it
3.8field-weighted citation impact, top 6% of its field
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

307 citing papers in PubMed, 2 syntheses or guidelines pooled it, 587 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  6. Article
  7. Article
  8. Review
  9. Mapping SARS-CoV-2 Nucleocapsid Function with Nanobodies.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
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  19. Article
  20. Definition of the components required for selective packaging of coronavirus genomic RNA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

247 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Chung-ke ChangInstitute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC.
Ming-Hon HouDepartment of Life Science, National Chung Hsing University, Taichung 40254, Taiwan, ROC.
Chi-Fon ChangThe Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan, ROC.
Chwan-Deng HsiaoInstitute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, ROC.
Tai-huang HuangInstitute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, ROC; The Genomics Research Center, Academia Sinica, Taipei 11529, Taiwan, ROC; Department of Physics, National Taiwan Normal University, Taipei 11677, Taiwan, ROC. Electronic address: bmthh@ibms.sinica.edu.tw.
Genomics Research Center, Academia Sinica · TWInstitute of Molecular Biology, Academia Sinica · TWNational Chung Hsing University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nucleocapsid phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV N protein) packages the viral genome into a helical ribonucleocapsid (RNP) and plays a fundamental role during viral self-assembly. It is a protein with multifarious activities. In this article we will review our current understanding of the N protein structure and its interaction with nucleic acid. Highlights of the progresses include uncovering the modular organization, determining the structures of the structural domains, realizing the roles of protein disorder in protein-protein and protein-nucleic acid interactions, and visualizing the ribonucleoprotein (RNP) structure inside the virions. It was also demonstrated that N-protein binds to nucleic acid at multiple sites with a coupled-allostery manner. We propose a SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses. The model highlights the critical role of modular organization and intrinsic disorder of the N protein in the formation and functions of the dynamic RNP capsid in RNA viruses. This paper forms part of a symposium in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses."

Indexed as

Virus AssemblyCoronavirus Nucleocapsid ProteinsHumansMacromolecular SubstancesModels, BiologicalModels, MolecularNucleocapsid ProteinsPhosphoproteinsProtein BindingProtein ConformationRNA, ViralSevere acute respiratory syndrome-related coronavirusCoronavirus Nucleocapsid ProteinsMacromolecular SubstancesNucleocapsid ProteinsPhosphoproteinsRNA, ViralCapsid packagingCoronavirusIntrinsic disorderNucleocapsid proteinRNPSARS

Identifiers

PMID24418573
PMCPMC7113676
OpenAlexW1974479059

What OpenQuestion holds

Textmetadata
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.