Identifying RNA Helicase Inhibitors Using Duplex Unwinding Assays
Explore this paper's citation graph
Summary
This chapter provides detailed protocols for utilizing a medium to high throughput approach for inhibitor discovery by optimizing and adapting standard helicase assays to function in high throughput modalities.
- Type
- article
- Published
- 2020-11-18
- Cited by
- 4
- References
- 11
- Access
- Open access
- OpenAlex
- https://openalex.org/W3100694020
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:226989029
Keywords
Helicase, RNA Helicase A, Computational biology, RNA, Biology
References
- Unzippers, Resolvers and Sensors: A Structural and Functional Biochemistry Tale of RNA Helicases
- Spectrophotometric assay for enzyme-mediated unwinding of double-stranded DNA.
- Coupling of DNA unwinding to nucleotide hydrolysis in a ring‐shaped helicase
- Unwinding of nucleic acids by HCV NS3 helicase is sensitive to the structure of the duplex.
- Identification and analysis of hepatitis C virus NS3 helicase inhibitors using nucleic acid binding assays
- Benzothiazole and Pyrrolone Flavivirus Inhibitors Targeting the Viral Helicase
- Unravelling the Mechanisms of RNA Helicase Regulation.
- New Insights Into DNA Helicases as Druggable Targets for Cancer Therapy
- N-Naphthoyl-substituted indole thio-barbituric acid analogs inhibit the helicase activity of the hepatitis C virus NS3
- Activation of PARP-1 by snoRNAs Controls Ribosome Biogenesis and Cell Growth via the RNA Helicase DDX21
- Bacterial replisomes.
Cited by
Related papers
- Identification and characterization of RNA duplex unwinding and ATPase activities of an alphatetravirus superfamily 1 helicase
- Molecular characterization of nuclear DNA helicase II (RNA helicase A).
- Nuclear DNA Helicase II (RNA Helicase A) Interacts with Werner Syndrome Helicase and Stimulates Its Exonuclease Activity*
- Helicase structure and mechanism.
- Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains
- The RNA helicase, nucleotide 5'-triphosphatase, and RNA 5'-triphosphatase activities of Dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core.
- The Human RNA Helicase DDX21 Presents a Dimerization Interface Necessary for Helicase Activity
- Structural basis of RNA-induced autoregulation of the DExH-type RNA helicase maleless