Evidence map›Paper›PMID 11911365›Full record

ArticleRNA (New York, N.Y.)2002

Determinants of the recognition of enteroviral cloverleaf RNA by coxsackievirus B3 proteinase 3C.

Roland Zell, Karim Sidigi, Enrico Bucci, Axel Stelzner, Matthias Görlach

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2002. 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
2.3field-weighted citation impact, top 10% 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, 63 citations in OpenAlex.

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  11. Inhibitory antibodies identify unique sites of therapeutic vulnerability in rhinovirus and other enteroviruses.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  18. A picornaviral loop-to-loop replication complex.Journal of structural biology · 2009
    Article
  19. Article
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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

5 authors at 3 institutions in 2 countries.

Roland ZellInstitut für Virologie, Klinikum der Friedrich-Schiller-Universität, Jena, Germany. i6zero@rz.uni-jena.de
Karim Sidigi
Enrico Bucci
Axel Stelzner
Matthias Görlach
Friedrich Schiller University Jena · DECentro di Riferimento Oncologico · ITLeibniz-Forschungsinstitut für Molekulare Pharmakologie · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The initiation of enteroviral positive-strand RNA synthesis requires the presence of a functional ribonucleoprotein complex containing a cloverleaf-like RNA secondary structure at the 5' end of the viral genome. Other components of the ribonucleoprotein complex are the viral 3CD proteinase (the precursor protein of the 3C proteinase and the 3D polymerase), the viral 3AB protein and the cellular poly(rC)-binding protein 2. For a molecular characterization of the RNA-binding properties of the enteroviral proteinase, the 3C proteinase of coxsackievirus B3 (CVB3) was bacterially expressed and purified. The recombinant protein is proteolytically active and forms a stable complex with in vitro-transcribed cloverleaf RNA of CVB3. The formation of stable complexes is also demonstrated with cloverleaf RNA of poliovirus (PV) 1, the first cloverleaf of bovine enterovirus (BEV) 1, and human rhinovirus (HRV) 2 but not with cloverleaf RNA of HRV14 and the second cloverleaf of BEV1. The apparent dissociation constants of the protein:RNA complexes range from approx. 1.7 to 4.6 microM. An electrophoretic mobility shift assay with subdomain D of the CVB3 cloverleaf demonstrates that this RNA is sufficient to bind the CVB3 3C proteinase. Binding assays using mutated versions of CVB3 and HRV14 cloverleaf RNAs suggest that the presence of structural features rather than a defined sequence motif of loop D are important for 3C proteinase-RNA interaction.

Indexed as

DNA-Binding ProteinsHeterogeneous-Nuclear RibonucleoproteinsTranscription Factors3C Viral ProteasesBase SequenceBinding SitesCloning, MolecularCysteine EndopeptidasesDNA, ComplementaryDNA PrimersEnterovirusEnterovirus B, HumanHumansKineticsMolecular Sequence DataNucleic Acid Conformation3C Viral ProteasesCysteine EndopeptidasesDNA-Binding ProteinsDNA, ComplementaryDNA PrimersHeterogeneous-Nuclear RibonucleoproteinsRecombinant ProteinsRNA-Binding ProteinsRNA, ViralTranscription FactorsViral Proteins

Identifiers

PMID11911365
PMCPMC1370242
OpenAlexW2139651462

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.