Evidence map›Paper›PMID 34793288›Full record

ArticleRNA biology2021

Nsp1 of SARS-CoV-2 stimulates host translation termination.

Alexey Shuvalov, Ekaterina Shuvalova, Nikita Biziaev, Elizaveta Sokolova, Konstantin Evmenov, Nikolay Pustogarov, Aleksandra Arnautova, Vera Matrosova, Tatiana Egorova, Elena Alkalaeva

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
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  4. Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024
    Article
  5. Article
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  10. Review
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  13. Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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

10 authors at 1 institution in 1 country.

Alexey ShuvalovCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Ekaterina ShuvalovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Nikita BiziaevEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Elizaveta SokolovaCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Konstantin EvmenovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Nikolay PustogarovCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Aleksandra ArnautovaCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Vera MatrosovaCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Tatiana EgorovaCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Elena AlkalaevaCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.ORCID 0000-0003-2078-7261
Engelhardt Institute of Molecular Biology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nsp1 of SARS-CoV-2 regulates the translation of host and viral mRNAs in cells. Nsp1 inhibits host translation initiation by occluding the entry channel of the 40S ribosome subunit. The structural study of the Nsp1-ribosomal complexes reported post-termination 80S complex containing Nsp1, eRF1 and ABCE1. Considering the presence of Nsp1 in the post-termination 80S ribosomal complex, we hypothesized that Nsp1 may be involved in translation termination. Using a cell-free translation system and reconstituted

Indexed as

Protein BiosynthesisSARS-CoV-2AnimalsCell-Free SystemCodon, TerminatorGTP PhosphohydrolasesHeLa CellsHumansMutationPeptide Chain Termination, TranslationalPeptidesPeptide Termination FactorsProtein BindingProtein ConformationProtein DomainsRabbitsCodon, TerminatorGTP PhosphohydrolasesORF1ab polyprotein, SARS-CoV-2peptide-chain-release factor 3PeptidesPeptide Termination FactorsRNA, MessengerViral Nonstructural ProteinseRF1eRF3Nsp1ribosomeSARS-CoV-2

Identifiers

PMID34793288
PMCPMC8782162
OpenAlexW3213145349

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.