Evidence map›Paper›PMID 16611118›Full record

ReviewCurrent pharmaceutical design2006

Understanding helicases as a means of virus control.

D N Frick, A M I Lam

Open access · greenAbstract readReview
In one paragraph

Review in Current pharmaceutical design, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 12% 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

62 citing papers in PubMed, 1 synthesis or guideline pooled it, 118 citations in OpenAlex.

  1. Pooled it
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  18. Insights into the global freshwater virome.Frontiers in microbiology · 2022
    Article
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2 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

2 authors at 1 institution in 1 country.

D N FrickDepartment of Biochemistry & Molecular Biology, New York Medical College, Valhalla, NY 10595, USA. David_Frick@NYMC.edu
A M I Lam
New York Medical College · US

Funding

Enzymatic Differences Among Hepatitis C Virus GenotypesR01AI052395 · NIAID · NEW YORK MEDICAL COLLEGE · PI FRICK, DAVID N · 2003 to 2007
$1.5M
NIAID NIH HHS AI052395NIAID NIH HHS R01 AI052395
6 · The paper itself

Abstract

Helicases are promising antiviral drug targets because their enzymatic activities are essential for viral genome replication, transcription, and translation. Numerous potent inhibitors of helicases encoded by herpes simplex virus, severe acute respiratory syndrome coronavirus, hepatitis C virus, Japanese encephalitis virus, West Nile virus, and human papillomavirus have been recently reported in the scientific literature. Some inhibitors have also been shown to decrease viral replication in cell culture and animal models. This review discusses recent progress in understanding the structure and function of viral helicases to help clarify how these potential antiviral compounds function and to facilitate the design of better inhibitors. The above helicases and all related viral proteins are classified here based on their evolutionary and functional similarities, and the key mechanistic features of each group are noted. All helicases share a common motor function fueled by ATP hydrolysis, but differ in exactly how the motor moves the protein and its cargo on a nucleic acid chain. The helicase inhibitors discussed here influence rates of helicase-catalyzed DNA (or RNA) unwinding by preventing ATP hydrolysis, nucleic acid binding, nucleic acid release, or by disrupting the interaction of a helicase with a required cofactor.

Indexed as

Antiviral AgentsDEAD-box RNA HelicasesDNA HelicasesDNA PrimaseEnzyme InhibitorsNucleoside-TriphosphatasePapillomaviridaeRNA HelicasesSerine EndopeptidasesSevere acute respiratory syndrome-related coronavirusSimplexvirusViral Nonstructural ProteinsViral ProteasesViral ProteinsAntiviral AgentsDEAD-box RNA HelicasesDNA HelicasesDNA PrimaseEnzyme Inhibitorshelicase-primase, Human herpesvirus 1NS3 protein, flavivirusNS3 protein, hepatitis C virusNucleoside-TriphosphataseRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesViral Proteins

Identifiers

PMID16611118
PMCPMC3571686
OpenAlexW2084710095

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.