Evidence map›Paper›PMID 15919933›Full record

ArticleJournal of virology2005

Allosteric effects of ligands and mutations on poliovirus RNA-dependent RNA polymerase.

Joanna E Boerner, John M Lyle, Sarah Daijogo, Bert L Semler, Stephen C Schultz, Karla Kirkegaard, Oliver C Richards

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Mapping allosteric pathway in NIa-Pro using computational approach.Quantitative biology (Beijing, China) · 2023
    Article
  3. Allosteric inhibitors of Coxsackie virus A24 RNA polymerase.Bioorganic & medicinal chemistry · 2016
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Structure-function relationships among RNA-dependent RNA polymerases.Current topics in microbiology and immunology · 2008
    Review
  13. Article
  14. Article
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  16. 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

7 authors at 3 institutions in 1 country.

Joanna E BoernerStanford University School of Medicine, Department of Microbiology and Immunology, Fairchild Science Building D309A, Stanford, CA 94305-5402, USA.
John M Lyle
Sarah Daijogo
Bert L Semler
Stephen C Schultz
Karla Kirkegaard
Oliver C Richards
Stanford University · USUniversity of California, Irvine · USUniversity of Colorado Boulder · US

Funding

POLIOVIRUS GENE FUNCTION AND REGULATIONR01AI022693 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI SEMLER, BERT L · 1985 to 2015
$4.6M
POLIOVIRUS 3D--COOPERATIVE RNA BINDING &POLYMERIZATIONR01AI042119 · NIAID · STANFORD UNIVERSITY · PI KIRKEGAARD, KARLA · 1998 to 2007
$2.4M
MECHANISM OF DNA POLYMERASE ALPHA-PRIMASER01GM054194 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI KUCHTA, ROBERT D · 1996 to 2009
$1.4M
HUMAN MONOCLONAL IGE-BINDING FACTORSR23AI022696 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI HUFF, THOMAS F · 1985 to 1987
–
NIAID NIH HHS AI-22696NIAID NIH HHS AI-42119NIAID NIH HHS R01 AI022693NIAID NIH HHS R01 AI042119NIGMS NIH HHS GM-54194NIGMS NIH HHS R01 GM054194
6 · The paper itself

Abstract

Protein priming of viral RNA synthesis plays an essential role in the replication of picornavirus RNA. Both poliovirus and coxsackievirus encode a small polypeptide, VPg, which serves as a primer for addition of the first nucleotide during synthesis of both positive and negative strands. This study examined the effects on the VPg uridylylation reaction of the RNA template sequence, the origin of VPg (coxsackievirus or poliovirus), the origin of 3D polymerase (coxsackievirus or poliovirus), the presence and origin of interacting protein 3CD, and the introduction of mutations at specific regions in the poliovirus 3D polymerase. Substantial effects associated with VPg origin were traced to differences in VPg-polymerase interactions. The effects of 3CD proteins and mutations at polymerase-polymerase intermolecular Interface I were most consistent with allosteric effects on the catalytic 3D polymerase molecule. In conclusion, the efficiency and specificity of VPg uridylylation by picornavirus polymerases is greatly influenced by allosteric effects of ligand binding that are likely to be relevant during the viral replicative cycle.

Indexed as

Gene Expression Regulation, ViralLigandsMutationAllosteric RegulationAllosteric SiteBinding SitesHumansModels, MolecularPoliovirusRNA-Dependent RNA PolymeraseRNA, ViralTemplates, GeneticUridine MonophosphateViral Core ProteinsLigandspolymerase 3Dpol, poliovirusRNA-Dependent RNA PolymeraseRNA, ViralUridine MonophosphateViral Core Proteins

Identifiers

PMID15919933
PMCPMC1143668
OpenAlexW2110451367

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.