Evidence map›Paper›PMID 17084859›Full record

ArticleJournal of molecular biology2007

Role of divalent metal cations in ATP hydrolysis catalyzed by the hepatitis C virus NS3 helicase: magnesium provides a bridge for ATP to fuel unwinding.

David N Frick, Sukalyani Banik, Ryan S Rypma

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  6. Review
  7. Article
  8. Article
  9. Magnesium and liver disease.Annals of translational medicine · 2019
    Review
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  12. Review
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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

3 authors at 1 institution in 1 country.

David N FrickDepartment of Biochemistry and Molecular Biology, New York Medical College, Valhalla, NY 10595, USA. David_Frick@NYMC.edu
Sukalyani Banik
Ryan S Rypma
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

This study investigates the role of magnesium ions in coupling ATP hydrolysis to the nucleic acid unwinding catalyzed by the NS3 protein encoded by the hepatitis C virus (HCV). Analyses of steady-state ATP hydrolysis rates at various RNA and magnesium concentrations were used to determine values for the 15 dissociation constants describing the formation of a productive enzyme-metal-ATP-RNA complex and the four rate constants describing hydrolysis of ATP by the possible enzyme-ATP complexes. These values coupled with direct binding studies, specificity studies and analyses of site-directed mutants reveal only one ATP binding site on HCV helicase centered on the catalytic base Glu291. An adjacent residue, Asp290, binds a magnesium ion that forms a bridge to ATP, reorienting the nucleotide in the active site. RNA stimulates hydrolysis while decreasing the affinity of the enzyme for ATP, magnesium, and MgATP. The binding scheme described here explains the unusual regulation of the enzyme by ATP that has been reported previously. Binding of either free magnesium or free ATP to HCV helicase competes with MgATP, the true fuel for helicase movements, and leads to slower hydrolysis and nucleic acid unwinding.

Indexed as

Adenosine TriphosphateAspartic AcidBinding SitesCatalysisCationsDEAD-box RNA HelicasesFluorescence Resonance Energy TransferGlutamic AcidHydrolysisKineticsMagnesiumMetalsModels, ChemicalNucleoside-TriphosphataseNucleotidesSerine EndopeptidasesAdenosine TriphosphateAspartic AcidCationsDEAD-box RNA HelicasesGlutamic AcidMagnesiumMetalsNS3 protein, hepatitis C virusNucleoside-TriphosphataseNucleotidesSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID17084859
PMCPMC1829317
OpenAlexW1965681005

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.