Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase (Q42986507)

12 November 2017

title

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

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12 November 2017

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Victor Serebrov

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12 November 2017

Anna Marie Pyle

series ordinal

2

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12 November 2017

language of work or name

English

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publication date

1 July 2004

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12 November 2017

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12 November 2017

volume

430

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12 November 2017

issue

6998

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12 November 2017

page(s)

476-480

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Membrane association of hepatitis C virus nonstructural proteins and identification of the membrane alteration that harbors the viral replication complex

12 November 2017

cites work

1 reference

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Protein-Protein Interactions between Hepatitis C Virus Nonstructural Proteins

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Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein.

21 January 2018

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Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Helicases: a unifying structural theme?

21 January 2018

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https://api.crossref.org/works/10.1038%2FNATURE02704

Mechanical devices of the spliceosome: motors, clocks, springs, and things

21 January 2018

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Helicase structure and mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

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

21 January 2018

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https://api.crossref.org/works/10.1038%2FNATURE02704

Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

The way things move: looking under the hood of molecular motor proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

The NS3/4A proteinase of the hepatitis C virus: unravelling structure and function of an unusual enzyme and a prime target for antiviral therapy

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Enzymatic properties of hepatitis C virus NS3-associated helicase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Translocation step size and mechanism of the RecBC DNA helicase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

The DExH protein NPH-II is a processive and directional motor for unwinding RNA

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Processive translocation and DNA unwinding by individual RecBCD enzyme molecules

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase

21 January 2018

1 reference

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21 January 2018

1 reference

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Single-molecule assay reveals strand switching and enhanced processivity of UvrD

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

The helicase from hepatitis C virus is active as an oligomer

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Hepatitis C virus NS3 ATPase/helicase: an ATP switch regulates the cooperativity among the different substrate binding sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Backbone tracking by the SF2 helicase NPH-II.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

Mutational analysis of the hepatitis C virus RNA helicase

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

inferred from DOI database lookup

7 January 2021

based on heuristic

Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

inferred from DOI database lookup

7 January 2021

based on heuristic

General Methods for Analysis of Sequential “n-step” Kinetic Mechanisms: Application to Single Turnover Kinetics of Helicase-Catalyzed DNA Unwinding

1 reference

https://api.crossref.org/works/10.1038%2FNATURE02704

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NATURE02704

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Dimensions Publication ID

12 November 2017

1025929939

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