Evidence map›Paper›PMID 26762834›Full record

ArticleBioorganic & medicinal chemistry2016

Allosteric inhibitors of Coxsackie virus A24 RNA polymerase.

Catherine H Schein, Diane Rowold, Kyung H Choi

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioorganic & medicinal chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact, top 88% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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

3 authors at 3 institutions in 1 country.

Catherine H ScheinFoundation for Applied Molecular Evolution, 13709 Progress Blvd, Box 7, Alachua, FL 32616, United States; Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, United States. Electronic address: chschein@ffame.org.
Diane RowoldFoundation for Applied Molecular Evolution, 13709 Progress Blvd, Box 7, Alachua, FL 32616, United States.
Kyung H ChoiDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, United States; Sealy Center for Structural Biology and Molecular Biophysics, UTMB, United States.
Foundation for Applied Molecular Evolution · USJohn Sealy Hospital · USThe University of Texas Medical Branch at Galveston · US

Funding

MECHANISM OF RNA SYNTHESIS BY DENGUE VIRUS NS5R01AI087856 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI Kyung H Choi · 2011 to 2026
$5.5M
Inhibiting protein-primed replication of human enteroviruses.R21AI105985 · NIAID · FOUNDATION FOR APPLIED MOLECULAR EVOLUTN · PI SCHEIN, CATHERINE H · 2013 to 2014
$442k
NIAID NIH HHS AI087856NIAID NIH HHS AI105985NIAID NIH HHS R01 AI087856NIAID NIH HHS R21 AI105985
6 · The paper itself

Abstract

Coxsackie virus A24 (CVA24), a causative agent of acute hemorrhagic conjunctivitis, is a prototype of enterovirus (EV) species C. The RNA polymerase (3D(pol)) of CVA24 can uridylylate the viral peptide linked to the genome (VPg) from distantly related EV and is thus, a good model for studying this reaction. Once UMP is bound, VPgpU primes RNA elongation. Structural and mutation data have identified a conserved binding surface for VPg on the RNA polymerase (3D(pol)), located about 20Å from the active site. Here, computational docking of over 60,000 small compounds was used to select those with the lowest (best) specific binding energies (BE) for this allosteric site. Compounds with varying structures and low BE were assayed for their effect on formation of VPgU by CVA24-3D(pol). Two compounds with the lowest specific BE for the site inhibited both uridylylation and formation of VPgpolyU at 10-20μM. These small molecules can be used to probe the role of this allosteric site in polymerase function, and may be the basis for novel antiviral compounds.

Indexed as

Allosteric RegulationAntiviral AgentsDNA-Directed RNA PolymerasesDose-Response Relationship, DrugEnterovirus C, HumanEnzyme InhibitorsMicrobial Sensitivity TestsMolecular Docking SimulationMolecular StructureSmall Molecule LibrariesStructure-Activity RelationshipVirus ReplicationAntiviral AgentsDNA-Directed RNA PolymerasesEnzyme InhibitorsSmall Molecule LibrariesAntiviral compoundsCoxsackie virusDocking compound librariesEnterovirus RNA polymerasePoliovirusProtein-primed RNA synthesis+-Strand RNA virusUridylylation mechanism

Identifiers

PMID26762834
PMCPMC4743507
OpenAlexW2205413947

What OpenQuestion holds

Textmetadata
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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.