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overview My laboratory is interested in the enzymology and chemistry of nucleic acid enzymes. Helicases are enzymes that manipulate DNA and RNA in all aspects of nucleic acid metabolism. We are studying a DNA helicase from Bacteriophage T4 called Dda (for DNA-Dependent-ATPase) in order to develop a detailed chemical and kinetic mechanism for DNA unwinding by this model DNA helicase. A second enzyme we study is called Pif1. This helicase is involved in many aspects of DNA metabolism ranging from telomere maintenance to transcription. Pif1 binds tightly to unusual DNA structures called quadruplexes, for which the biological functions are being intensively explored. A second project involves the Hepatitis C viral helicase NS3 (Non-Structural Protein 3). NS3 is an RNA helicase that is capable of unwinding DNA. We are studying the mechanism of NS3 as well as its interactions with other HCV and cellular proteins. Our goal is to recapitulate RNA replication in vitro using biological relevant substrates and proteins and a biologically relevant sub-genomic replicon of HCV. Our research projects are currently expanding in development of new tools for studying and protein-protein interactions and post-translational modifications at specific sites in the genome using a Crispr-based approach coupled with protein mass spectrometry. In a new project, we have recently discovered a possible signaling mechanism by which cells respond to DNA damage. During oxidative stress, guanine residues are oxidized, leading to excision of the damaged DNA. When the excised DNA consists of specific sequences containing runs of guanine, the resulting DNA fragment can fold into a stable structure called quadruplex DNA. Telomeric DNA is particularly susceptible to oxidative stress and contains sequences that readily fold into quadruplex structures. The excised DNA quadruplexes can bind to proteins such as DHX36 (a helicase), leading to formation of sub-organelles called stress granules. The functional role of stress granules is to modulate translation. Hence, this mechanism provides a stepwise chemical mechanism for the cell to respond to DNA damage leading to changes in translation.

One or more keywords matched the following items that are connected to Raney, Kevin

Item TypeName
Academic Article Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus.
Academic Article Purification and characterization of hepatitis C virus non-structural protein 5A expressed in Escherichia coli.
Academic Article NS3 helicase from the hepatitis C virus can function as a monomer or oligomer depending on enzyme and substrate concentrations.
Academic Article Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro.
Academic Article Investigation of translocation, DNA unwinding, and protein displacement by NS3h, the helicase domain from the hepatitis C virus helicase.
Academic Article Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.
Academic Article Hepatitis C virus non-structural protein 3 (HCV NS3): a multifunctional antiviral target.
Academic Article RNA unwinding activity of the hepatitis C virus NS3 helicase is modulated by the NS5B polymerase.
Academic Article Binding by the hepatitis C virus NS3 helicase partially melts duplex DNA.
Academic Article Modulation of the hepatitis C virus RNA-dependent RNA polymerase activity by the non-structural (NS) 3 helicase and the NS4B membrane protein.
Academic Article Hepatitis C virus nonstructural protein 5A: biochemical characterization of a novel structural class of RNA-binding proteins.
Concept Hepatitis C
Academic Article Mutation in the Putative Nuclear Localization Sequence of the Hepatitis C NS3 Protein Reduce Colony Formation After Transfection of HCV Replicon RNA into Huh 7 Cell
Academic Article Structure of an Apparent Dimeric Form of the HCV NS3 Helicase Reveals Surface Residues that are required for HCV Replication
Academic Article Application of a Streptavidan Displacement assay in the Investigation of the avtive species of hepatitis C virus NS3 helicase
Academic Article Using Chemical Crosslinking to Examine the Oligomeric state of Hepatitis C Virus NS3 Helicase
Academic Article Improved Methods for Expression and Purification of the Hepatitis C Virus Helicase
Academic Article Structure and Biological Identification of Residue on the surface of NS3 Helicase that are required for optimal replication of the Hepatitis C virus
Academic Article Multiple Full- Length NS3 Molecules are Required for Optimal Unwinding Activity
Academic Article Identification of Protein Surfaces of NS3 that are required for HCV Replication
Academic Article Unwinding of Nucleic Acids by the HCVNS3 Helicase
Academic Article Identification of Protein-Protein Interactions among Non-Structural Protein from HCV and Evidence for a Dominant Negative Effect of an ATPase-deficient mutant of NS3
Academic Article Mutations in the Putative Nuclear Localization Sequence of the Hepatitis C NS3 Protein Conoly Formation after Transfection of HCV Replicon RNA into Huh 7 Cells
Academic Article Melting of Duplex DNA in the Absence of ATP by the NS3 Helicase Domain through Specific Interaction with a Single-Strand/Double-Strand Junction.
Academic Article N-Naphthoyl-substituted indole thio-barbituric acid analogs inhibit the helicase activity of the hepatitis C virus NS3.
Grant Mechanisms of RNA binding and remodeling proteins
Grant HCV NS3: Biological, Biochemical and Structural Analysis
Grant HCV NS3 and NS5A: Biochemical Mechanisms and Biological Functions
Grant MECHANISM OF HEPACIVIRUS REPLICASE ASSEMBLY
Grant MECHANISM OF THE RNA HELICASE OF THE HEPATITIS C VIRUS

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