Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA. (Q41841562)

13 October 2017

Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA. (English)

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13 October 2017

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5

Craig E Cameron

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13 October 2017

Veronica M Raney

1

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13 October 2017

Kimberly A Reynolds

2

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13 October 2017

Melody K Harrison

3

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13 October 2017

David K Harrison

4

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13 October 2017

Kevin D Raney

6

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13 October 2017

language of work or name

English

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publication date

13 September 2012

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13 October 2017

12

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published in

Biochemistry

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13 October 2017

51

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13 October 2017

38

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13 October 2017

7596-7607

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describes a project that uses

13 October 2017

ImageQuant

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11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3554864/fullTextXML

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cites work

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Hepatitis C Virus NS3 Protein Can Activate the Notch-Signaling Pathway through Binding to a Transcription Factor, SRCAP

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One-step DNA melting in the RNA polymerase cleft opens the initiation bubble to form an unstable open complex

6 June 2018

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Investigation of Translocation, DNA Unwinding, and Protein Displacement by NS3h, the Helicase Domain from the Hepatitis C Virus Helicase

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Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism

6 June 2018

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

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The NS4A Protein of Hepatitis C Virus Promotes RNA-Coupled ATP Hydrolysis by the NS3 Helicase

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NS3 Helicase from the Hepatitis C Virus Can Function as a Monomer or Oligomer Depending on Enzyme and Substrate Concentrations

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Establishing a Mechanistic Basis for the Large Kinetic Steps of the NS3 Helicase

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Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro

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Hepatitis C virus NS3/4A protein interacts with ATM, impairs DNA repair and enhances sensitivity to ionizing radiation.

6 June 2018

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NS3 helicase actively separates RNA strands and senses sequence barriers ahead of the opening fork

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Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro

6 June 2018

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Enhanced nucleic acid binding to ATP-bound hepatitis C virus NS3 helicase at low pH activates RNA unwinding

6 June 2018

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Permanganate Oxidation Reactions of DNA: Perspective in Biological Studies

6 June 2018

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Hepatitis C Virus NS3 ATPases/Helicases from Different Genotypes Exhibit Variations in Enzymatic Properties

6 June 2018

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The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding

6 June 2018

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Unwinding of nucleic acids by HCV NS3 helicase is sensitive to the structure of the duplex

6 June 2018

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Subcellular localisation of NS3 in HCV-infected hepatocytes.

6 June 2018

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Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding

6 June 2018

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The RecBCD enzyme initiation complex for DNA unwinding: enzyme positioning and DNA opening

6 June 2018

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Analysis of Open Complex Formation during RNA Polymerase II Transcription Initiation Using Heteroduplex Templates and Potassium Permanganate Probing

6 June 2018

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Nuclear localization of the NS3 protein of hepatitis C virus and factors affecting the localization

6 June 2018

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Kinetic control of Mg2 -dependent melting of duplex DNA ends by Escherichia coli RecBC.

6 June 2018

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A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase

18 August 2018

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Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase

18 August 2018

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The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity

18 August 2018

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Helicase from hepatitis C virus, energetics of DNA binding

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3554864

18 August 2018

Identifiers

DOI

10.1021/BI300654V

1 reference

13 October 2017

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13 October 2017

PubMed publication ID

22916835

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