Evidence map›Paper›PMID 19838190›Full record

ArticleNature structural & molecular biology2009

A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein.

Wataru Kamitani, Cheng Huang, Krishna Narayanan, Kumari G Lokugamage, Shinji Makino

Open access · bronzeAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 264 papers.

0numbers the graph read from it
0cells of the map it votes in
264citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

264 citing papers in PubMed, 450 citations in OpenAlex.

  1. SARS-CoV-2 and MERS-CoV disrupt host protein synthesis via nsp1 with differential effects on the integrated stress response.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  14. Anti-interferon armamentarium of human coronaviruses.Cellular and molecular life sciences : CMLS · 2025
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. SARS-CoV2 Nsp1 is a metal-dependent DNA and RNA endonuclease.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Article
  20. Review

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

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

5 authors at 2 institutions in 2 countries.

Wataru KamitaniDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, Texas, USA.
Cheng Huang
Krishna Narayanan
Kumari G Lokugamage
Shinji Makino
The University of Texas Medical Branch at Galveston · USBipar · FR

Funding

Analysis of SARS Coronavirus-Host Cell InteractionsR01AI072493 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI MAKINO, SHINJI · 2007 to 2011
$1.5M
NIAID NIH HHS AI72493NIAID NIH HHS R01 AI072493
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus nsp1 protein suppresses host gene expression, including type I interferon production, by promoting host mRNA degradation and inhibiting host translation, in infected cells. We present evidence that nsp1 uses a novel, two-pronged strategy to inhibit host translation and gene expression. Nsp1 bound to the 40S ribosomal subunit and inactivated the translational activity of the 40S subunits. Furthermore, the nsp1-40S ribosome complex induced the modification of the 5' region of capped mRNA template and rendered the template RNA translationally incompetent. Nsp1 also induced RNA cleavage in templates carrying the internal ribosome entry site (IRES) from encephalomyocarditis virus, but not in those carrying IRES elements from hepatitis C or cricket paralysis viruses, demonstrating that the nsp1-induced RNA modification was template-dependent. We speculate that the mRNAs that underwent the nsp1-mediated modification are marked for rapid turnover by the host RNA degradation machinery.

Indexed as

Cell LineHumansImmunoprecipitationLuciferases, RenillaProtein BindingProtein BiosynthesisRibosomesRNA-Dependent RNA PolymeraseRNA StabilityViral Nonstructural ProteinsLuciferases, RenillaNsp1 protein, SARS coronavirusRNA-Dependent RNA PolymeraseViral Nonstructural Proteins

Identifiers

PMID19838190
PMCPMC2784181
OpenAlexW2053186308

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.