Evidence map›Paper›PMID 19969541›Full record

ArticleNucleic acids research2010

Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.

Qixin Wang, Jamie J Arnold, Akira Uchida, Kevin D Raney, Craig E Cameron

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-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

25 citing papers in PubMed, 39 citations in OpenAlex.

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  20. RNA helicases and remodeling proteins.Current opinion in chemical biology · 2011
    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

5 authors at 3 institutions in 2 countries.

Qixin WangDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Jamie J Arnold
Akira Uchida
Kevin D Raney
Craig E Cameron
University of Arkansas for Medical Sciences · USUniversity of Chinese Academy of Sciences · CNPennsylvania State University · US

Funding

Mechanisms of RNA binding and remodeling proteinsR01GM089001 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI CAMERON, CRAIG E., RANEY, KEVIN DOUGLAS · 2009 to 2012
$1.7M
HCV NS3: Biological, Biochemical and Structural AnalysisR01AI060563 · NIAID · UNIV OF ARKANSAS FOR MED SCIS · PI RANEY, KEVIN D · 2003 to 2006
$1.7M
HCV NS3 and NS5A: Biochemical Mechanisms and Biological FunctionsR56AI060563 · NIAID · UNIV OF ARKANSAS FOR MED SCIS · PI RANEY, KEVIN DOUGLAS · 2008 to 2009
$786k
NIAID NIH HHS AI060563NIGMS NIH HHS R01 GM089001
6 · The paper itself

Abstract

RNA helicases function in numerous aspects of RNA biology. These enzymes are RNA-stimulated ATPases that translocate on RNA and unwind or remodel structured RNA in an ATP-dependent fashion. How ATP and the ATPase cycle fuel the work performed by helicases is not completely clear. The hepatitis C virus RNA helicase, NS3, is an important model system for this class of enzymes. NS3 binding to a single-/double-strand RNA or DNA junction leads to ATP-independent melting of the duplex and formation of a complex capable of ATP-dependent unwinding by using a spring-loaded mechanism. We have established an RNA substrate for NS3 that can be unwound in a single sub-step. Our studies are consistent with a model in which a single ATP binding and/or hydrolysis event sets the unwinding spring and phosphate dissociation contributes to release of the spring, thereby driving the power stroke used for unwinding.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBiocatalysisDEAD-box RNA HelicasesKineticsNucleoside-TriphosphataseOligoribonucleotidesPhosphatesProtein BindingRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral ProteasesAdenosine TriphosphatasesAdenosine TriphosphateDEAD-box RNA HelicasesNS3 protein, hepatitis C virusNucleoside-TriphosphataseOligoribonucleotidesPhosphatesRNA HelicasesSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID19969541
PMCPMC2831328
OpenAlexW2066411972

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.