Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction-Reference-Cited by-同舟云学术

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Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction

Published:2015-07-02 Issue:27 Volume:54 Page:4248-4258
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Reynolds Kimberly A.¹,Cameron Craig E.²,Raney Kevin D.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205, United States

2. Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00214

Reference52 articles.

1. DEAD-box protein CYT-19 is activated by exposed helices in a group I intron RNA

2. Human RecQ Helicases in DNA Repair, Recombination, and Replication

3. Superfamily 2 helicases

4. Translocation and Unwinding Mechanisms of RNA and DNA Helicases

5. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes

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2. Hepatitis C virus nonstructural protein NS3 unfolds viral G-quadruplex RNA structures;Journal of Biological Chemistry;2022-11

3. A second DNA binding site on RFC facilitates clamp loading at gapped or nicked DNA;eLife;2022-06-22

4. A second DNA binding site on RFC facilitates clamp loading at gapped or nicked DNA;2022-01-31

5. Structural Basis of Zika Virus Helicase in RNA Unwinding and ATP Hydrolysis;ACS Infectious Diseases;2021-12-14

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