Evidence map›Paper›PMID 18295294›Full record

ArticleVirology2008

Mutation in murine coronavirus replication protein nsp4 alters assembly of double membrane vesicles.

Mark A Clementz, Amornrat Kanjanahaluethai, Timothy E O'Brien, Susan C Baker

Open access · greenAbstract read
In one paragraph

Article in Virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

63 citing papers in PubMed, 96 citations in OpenAlex.

  1. Structural insights into SARS-CoV-2 nonstructural protein 4 (nsp4) biogenesis.Protein science : a publication of the Protein Society · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Expression and immunogenicity of non-structural protein 8 of porcine epidemic diarrhea virus.Veterinary research forum : an international quarterly journal · 2024
    Article
  7. Nsp3-N interactions are critical for SARS-CoV-2 fitness and virulence.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Why do SARS-CoV-2 NSPs rush to the ER?Journal of neurology · 2021
    Review
  17. Article
  18. Exploiting Connections for Viral Replication.Frontiers in cell and developmental biology · 2021
    Article
  19. Review
  20. Review

3 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

4 authors at 2 institutions in 2 countries.

Mark A ClementzDepartment of Microbiology and Immunology, Loyola University Stritch School of Medicine, Maywood, IL 60153 USA.
Amornrat Kanjanahaluethai
Timothy E O'Brien
Susan C Baker
Loyola University Chicago · USChiang Mai University · TH

Funding

STRUCTURE AND FUNCTION OF THE CORONAVIRUS REPLICASER01AI045798 · NIAID · LOYOLA UNIVERSITY CHICAGO · PI BAKER, SUSAN C. · 2001 to 2005
$1.5M
NIAID NIH HHS AI 45798NIAID NIH HHS R01 AI045798
6 · The paper itself

Abstract

Coronaviruses are positive-strand RNA viruses that replicate in the cytoplasm of infected cells by generating a membrane-associated replicase complex. The replicase complex assembles on double membrane vesicles (DMVs). Here, we studied the role of a putative replicase anchor, nonstructural protein 4 (nsp4), in the assembly of murine coronavirus DMVs. We used reverse genetics to generate infectious clone viruses (icv) with an alanine substitution at nsp4 glycosylation site N176 or N237, or an asparagine to threonine substitution (nsp4-N258T), which is proposed to confer a temperature sensitive phenotype. We found that nsp4-N237A is lethal and nsp4-N258T generated a virus (designated Alb ts6 icv) that is temperature sensitive for viral replication. Analysis of Alb ts6 icv-infected cells revealed that there was a dramatic reduction in DMVs and that both nsp4 and nsp3 partially localized to mitochondria when cells were incubated at the non-permissive temperature. These results reveal a critical role of nsp4 in directing coronavirus DMV assembly.

Indexed as

Virus AssemblyAmino Acid SubstitutionAnimalsCell LineCell MembraneCricetinaeHumansMicroscopy, Electron, TransmissionMitochondriaMurine hepatitis virusMutagenesis, Site-DirectedViral Nonstructural Proteinsnonstructural protein, coronavirusViral Nonstructural Proteins

Identifiers

PMID18295294
PMCPMC2443636
OpenAlexW2163209522

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.