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Gary Larson

Researcher at Valeant Pharmaceuticals

Publications -  22
Citations -  976

Gary Larson is an academic researcher from Valeant Pharmaceuticals. The author has contributed to research in topics: Kinase & RNA polymerase. The author has an hindex of 15, co-authored 22 publications receiving 916 citations. Previous affiliations of Gary Larson include University of California, Santa Barbara.

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RDEA119/BAY 869766: a potent, selective, allosteric inhibitor of MEK1/2 for the treatment of cancer.

TL;DR: Using pharmacokinetic and pharmacodynamic data, it is shown that maintaining adequate MEK inhibition throughout the dosing interval is likely more important than achieving high peak levels because greater efficacy was achieved with more frequent but lower dosing.
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Structure–activity relationship (SAR) studies of quinoxalines as novel HCV NS5B RNA-dependent RNA polymerase inhibitors

TL;DR: From chemical compound library screening using an HCV NS5B RNA-dependent RNA polymerase enzymatic assay, a substituted quinoxaline hit with an IC(50) of 5.5 microM was identified and a series of substituted quInoxaline amide derivatives were synthesized based on the hit's pharmacophore, and a good structure-activity relationship was observed.
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Biochemical and cellular characterization of VRX0466617, a novel and selective inhibitor for the checkpoint kinase Chk2.

TL;DR: The results underscore the specificity of VRX0466617 for Chk2, both in vitro and in vivo, and support the use of this compound as a biological probe to study the Chk 2-dependent pathways.
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2-Methoxyestradiol suppresses microtubule dynamics and arrests mitosis without depolymerizing microtubules

TL;DR: The results suggest that the major mechanism of mitotic arrest at the lowest effective concentrations of 2ME2 is suppression of microtubule dynamics rather than microtubules depolymerization per se.
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Selection of 3'-template bases and initiating nucleotides by hepatitis C virus NS5B RNA-dependent RNA polymerase.

TL;DR: De novo RNA synthesis by hepatitis C virus (HCV) nonstructural protein 5B (NS5B) RNA-dependent RNA polymerase has been investigated using short RNA templates and it was discovered that the secondary structure of a template was not essential for de novo initiation and that 3′-terminal bases of a templates conferred specificity in selection of an initiation site.