Evidence map›Paper›PMID 37929963›Full record

ArticleJournal of virology2023

SARS-CoV-2 NSP12 associates with TRiC and the P323L substitution acts as a host adaption.

Muhannad Alruwaili, Stuart Armstrong, Tessa Prince, Maximillian Erdmann, David A Matthews, Lisa Luu, Andrew Davidson, Waleed Aljabr, Julian A Hiscox

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

7 citing papers in PubMed, 8 citations in OpenAlex.

  1. Insights into SARS-CoV-2 replication controlActa pharmaceutica Sinica. B · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Protein folding by the CCT/TRiC chaperone complex.Current opinion in structural biology · 2025
    Review
  6. Article
  7. Review
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

9 authors at 5 institutions in 3 countries.

Muhannad AlruwailiInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, United Kingdom.ORCID 0000-0002-7642-4534
Stuart ArmstrongInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, United Kingdom.
Tessa PrinceInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, United Kingdom.
Maximillian ErdmannSchool of Cellular and Molecular Medicine, University of Bristol , Bristol, United Kingdom.
David A MatthewsSchool of Cellular and Molecular Medicine, University of Bristol , Bristol, United Kingdom.
Lisa LuuInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, United Kingdom.
Andrew DavidsonSchool of Cellular and Molecular Medicine, University of Bristol , Bristol, United Kingdom.
Waleed AljabrKing Fahad Medical City , Riyadh, Saudi Arabia.
Julian A HiscoxInstitute of Infection, Veterinary and Ecological Sciences, University of Liverpool , Liverpool, United Kingdom.ORCID 0000-0002-6582-0275
University of Bristol · GBUniversity of Liverpool · GBAgency for Science, Technology and Research · SGKing Fahd Medical City · SANorthern Border University · SA

Funding

Medical Research Council MR/V027506/1Medical Research Council MR/W005611/1
6 · The paper itself

Abstract

importanceSARS-CoV-2 has caused a worldwide health and economic crisis. During the course of the pandemic, genetic changes occurred in the virus, which have resulted in new properties of the virus-particularly around gains in transmission and the ability to partially evade either natural or vaccine-acquired immunity. Some of these viruses have been labeled Variants of Concern (VoCs). At the root of all VoCs are two mutations, one in the viral spike protein that has been very well characterized and the other in the virus polymerase (NSP12). This is the viral protein responsible for replicating the genome. We show that NSP12 associates with host cell proteins that act as a scaffold to facilitate the function of this protein. Furthermore, we found that different variants of NSP12 interact with host cell proteins in subtle and different ways, which affect function.

Indexed as

Coronavirus RNA-Dependent RNA PolymeraseCOVID-19MARVEL Domain Containing 2 ProteinSARS-CoV-2Adaptive ImmunityCytosolHumansMutationSpike Glycoprotein, CoronavirusCoronavirus RNA-Dependent RNA PolymeraseMARVELD2 protein, humanMARVEL Domain Containing 2 ProteinNSP12 protein, SARS-CoV-2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2NSP12P323LphosphataseSARS-CoV-2TRiC

Identifiers

PMID37929963
PMCPMC10688337
OpenAlexW4388422716

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.