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Search Results to Kevin Raney

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

Item TypeName
Academic Article Chemically modified DNA substrates implicate the importance of electrostatic interactions for DNA unwinding by Dda helicase.
Academic Article Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro.
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 Alteration of the aflatoxin cyclopentenone ring to a delta-lactone reduces intercalation with DNA and decreases formation of guanine N7 adducts by aflatoxin epoxides.
Academic Article NS3 helicase from the hepatitis C virus can function as a monomer or oligomer depending on enzyme and substrate concentrations.
Academic Article Dda helicase tightly couples translocation on single-stranded DNA to unwinding of duplex DNA: Dda is an optimally active helicase.
Academic Article Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.
Academic Article Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA.
Academic Article DNA helicases displace streptavidin from biotin-labeled oligonucleotides.
Academic Article Unwinding of unnatural substrates by a DNA helicase.
Academic Article Biotin-streptavidin-labeled oligonucleotides as probes of helicase mechanisms.
Concept Oligonucleotides
Academic Article Displacement of Streptavidin from the 5'-ends of biotin labeled Oligonucleotides by 3'-to-5' Helicases
Academic Article "Biotin-Streptavidin Labeled Oligonucleotides as probes of Helicase Mechanism"
Academic Article HCV NS3 and SV40 T Antigen Helicases displace streptavidin from 5’-biotinylated oligonucleotides but not from 3’-biotinylated oligonucleotides: Evidence for Unidirectional Translocation on Single-stranded DNA
Academic Article DNA Helicase Displaces Streptavidin from Biotin-Labeled Oligonucleotides with a 5'-to-3' Directional Bias
Grant MOLECULAR PROBES FOR STUDYING TELOMERASE

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