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Single-base pair unwinding and asynchronous RNA release by the hepatitis C virus NS3 helicase.
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Zika virus NS3 is a canonical RNA helicase stimulated by NS5 RNA polymerase.
Nucleic Acids Res. 2019 Sep 19;47(16):8693-8707. doi: 10.1093/nar/gkz650.
3
Enzymatic properties of hepatitis C virus NS3-associated helicase.
J Gen Virol. 2000 May;81(Pt 5):1335-45. doi: 10.1099/0022-1317-81-5-1335.
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RNA translocation and unwinding mechanism of HCV NS3 helicase and its coordination by ATP.
Nature. 2006 Jan 5;439(7072):105-8. doi: 10.1038/nature04331.
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RNA unwinding by NS3 helicase: a statistical approach.
PLoS One. 2009 Sep 22;4(9):e6937. doi: 10.1371/journal.pone.0006937.
6
Coupling translocation with nucleic acid unwinding by NS3 helicase.
J Mol Biol. 2010 Dec 3;404(3):439-55. doi: 10.1016/j.jmb.2010.09.047. Epub 2010 Sep 29.
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Spring-loaded mechanism of DNA unwinding by hepatitis C virus NS3 helicase.
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10
Structure-based mutational analysis of the hepatitis C virus NS3 helicase.
J Virol. 2001 Sep;75(17):8289-97. doi: 10.1128/jvi.75.17.8289-8297.2001.

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Duplex Unwinding Mechanism of Coronavirus MERS-CoV nsp13 Helicase.
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Mechanical regulation of the helicase activity of Zika virus NS3.
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Insight into the biochemical mechanism of DNA helicases provided by bulk-phase and single-molecule assays.
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Kinetic and structural mechanism for DNA unwinding by a non-hexameric helicase.
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Optical tweezers in single-molecule biophysics.
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The NEOtrap - en route with a new single-molecule technique.
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DNA replication: single-molecule manipulation data analysis and models.
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本文引用的文献

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Visualizing ATP-dependent RNA translocation by the NS3 helicase from HCV.
J Mol Biol. 2011 Feb 4;405(5):1139-53. doi: 10.1016/j.jmb.2010.11.034. Epub 2010 Dec 9.
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RNA helicases at work: binding and rearranging.
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Use of tapered amplifier diode laser for biological-friendly high-resolution optical trapping.
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Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral target.
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The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.
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Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism.
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A point process driven multiple change point model: a robust resistant approach.
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NS3 helicase from the hepatitis C virus can function as a monomer or oligomer depending on enzyme and substrate concentrations.
J Biol Chem. 2009 Feb 20;284(8):4806-14. doi: 10.1074/jbc.M805540200. Epub 2008 Dec 16.
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Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis.
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Establishing a mechanistic basis for the large kinetic steps of the NS3 helicase.
J Biol Chem. 2009 Jan 23;284(4):2512-21. doi: 10.1074/jbc.M805460200. Epub 2008 Nov 14.

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