Evidence map›Paper›PMID 10400784›Full record

ArticleJournal of virology1999

The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis.

M R Denison, W J Spaan, Y van der Meer, C A Gibson, A C Sims, E Prentice, X T Lu

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

73 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
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  8. The molecular virology of coronaviruses.The Journal of biological chemistry · 2020
    Review
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  14. Review
  15. Review
  16. Studying the dynamics of coronavirus replicative structures.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  17. Review
  18. Article
  19. Article
  20. Article

13 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

7 authors at 2 institutions in 2 countries.

M R DenisonDepartment of Pediatrics, Department of Microbiology and Immunology, and The Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University, Nashville, Tennessee, USA. mark.denison@mcmail.vanderbilt.edu
W J Spaan
Y van der Meer
C A Gibson
A C Sims
E Prentice
X T Lu
Vanderbilt University · USLeiden University Medical Center · NL

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
POLYMERASE PROTEINS IN CORONAVIRUS REPLICATIONR01AI026603 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DENISON, MARK R · 1994 to 2014
$4.1M
CORONAVIRUS 3CL PROTEINASE FUNCTION IN VIRUS REPLICATIONK02AI001479 · NIAID · VANDERBILT UNIVERSITY · PI DENISON, MARK R · 1997 to 2001
$196k
CORONAVIRUS--ANALYSIS OF POLYMERASE GENE PRODUCTSR29AI026603 · NIAID · VANDERBILT UNIVERSITY · PI DENISON, MARK R · 1988 to 1992
–
NCI NIH HHS IP30CA68485NCI NIH HHS P30 CA068485NIAID NIH HHS AI01479NIAID NIH HHS AI-26603NIAID NIH HHS R01 AI026603
6 · The paper itself

Abstract

The coronavirus mouse hepatitis virus (MHV) translates its replicase gene (gene 1) into two co-amino-terminal polyproteins, polyprotein 1a and polyprotein 1ab. The gene 1 polyproteins are processed by viral proteinases to yield at least 15 mature products, including a putative RNA helicase from polyprotein 1ab that is presumed to be involved in viral RNA synthesis. Antibodies directed against polypeptides encoded by open reading frame 1b were used to characterize the expression and processing of the MHV helicase and to define the relationship of helicase to the viral nucleocapsid protein (N) and to sites of viral RNA synthesis in MHV-infected cells. The antihelicase antibodies detected a 67-kDa protein in MHV-infected cells that was translated and processed throughout the virus life cycle. Processing of the 67-kDa helicase from polyprotein 1ab was abolished by E64d, a known inhibitor of the MHV 3C-like proteinase. When infected cells were probed for helicase by immunofluorescence laser confocal microscopy, the protein was detected in patterns that varied from punctate perinuclear complexes to large structures that occupied much of the cell cytoplasm. Dual-labeling studies of infected cells for helicase and bromo-UTP-labeled RNA demonstrated that the vast majority of helicase-containing complexes were active in viral RNA synthesis. Dual-labeling studies for helicase and the MHV N protein showed that the two proteins almost completely colocalized, indicating that N was associated with the helicase-containing complexes. This study demonstrates that the putative RNA helicase is closely associated with MHV RNA synthesis and suggests that complexes containing helicase, N, and new viral RNA are the viral replication complexes.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCell MembraneCytoplasmMiceMolecular Sequence DataMurine hepatitis virusNucleocapsidNucleocapsid ProteinsProteinsRNA-Dependent RNA PolymeraseRNA HelicasesRNA, Viralnucleocapsid protein, Hepatitis virusNucleocapsid ProteinsProteinsRNA-Dependent RNA PolymeraseRNA HelicasesRNA, Viral

Identifiers

PMID10400784
PMCPMC112771
OpenAlexW2156681639

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.