Evidence map›Paper›PMID 20051491›Full record

ArticleRNA (New York, N.Y.)2010

Enzymatic and nonenzymatic functions of viral RNA-dependent RNA polymerases within oligomeric arrays.

Jeannie F Spagnolo, Evan Rossignol, Esther Bullitt, Karla Kirkegaard

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

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  18. Common and unique features of viral RNA-dependent polymerases.Cellular and molecular life sciences : CMLS · 2014
    Review
  19. Double-membraned liposomes sculpted by poliovirus 3AB protein.The Journal of biological chemistry · 2013
    Article
  20. 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

4 authors at 2 institutions in 1 country.

Jeannie F Spagnolo1Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Evan Rossignol
Esther Bullitt
Karla Kirkegaard
Boston University · USStanford University · US

Funding

PROTEIN-RNA INTERACTIONS AND POLIOVIRUS RNA REPLICATIONR01AI025166 · NIAID · UNIVERSITY OF COLORADO AT BOULDER · PI KIRKEGAARD, KARLA · 1994 to 1998
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NUCLEIC ACID--PROTEIN INTERACTIONS AND POLIOVIRUSR29AI025166 · NIAID · UNIVERSITY OF COLORADO AT BOULDER · PI KIRKEGAARD, KARLA · 1987 to 1991
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NIAID NIH HHS AI-25166
6 · The paper itself

Abstract

Few antivirals are effective against positive-strand RNA viruses, primarily because the high error rate during replication of these viruses leads to the rapid development of drug resistance. One of the favored current targets for the development of antiviral compounds is the active site of viral RNA-dependent RNA polymerases. However, like many subcellular processes, replication of the genomes of all positive-strand RNA viruses occurs in highly oligomeric complexes on the cytosolic surfaces of the intracellular membranes of infected host cells. In this study, catalytically inactive polymerases were shown to participate productively in functional oligomer formation and catalysis, as assayed by RNA template elongation. Direct protein transduction to introduce either active or inactive polymerases into cells infected with mutant virus confirmed the structural role for polymerase molecules during infection. Therefore, we suggest that targeting the active sites of polymerase molecules is not likely to be the best antiviral strategy, as inactivated polymerases do not inhibit replication of other viruses in the same cell and can, in fact, be useful in RNA replication complexes. On the other hand, polymerases that could not participate in functional RNA replication complexes were those that contained mutations in the amino terminus, leading to altered contacts in the folded polymerase and mutations in a known polymerase-polymerase interaction in the two-dimensional protein lattice. Thus, the functional nature of multimeric arrays of RNA-dependent RNA polymerase supplies a novel target for antiviral compounds and provides a new appreciation for enzymatic catalysis on membranous surfaces within cells.

Indexed as

Antiviral AgentsCatalytic DomainDrug Resistance, ViralGenetic Complementation TestHeLa CellsHumansMacromolecular SubstancesModels, MolecularMutagenesis, Site-DirectedMutationRecombinant ProteinsRNA-Dependent RNA PolymeraseRNA, ViralRNA VirusesTransduction, GeneticVirus ReplicationAntiviral AgentsMacromolecular Substancespolymerase 3Dpol, poliovirusRecombinant ProteinsRNA-Dependent RNA PolymeraseRNA, Viral

Identifiers

PMID20051491
PMCPMC2811667
OpenAlexW2110734032

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.