M
Michael B. Cable
Researcher at Schering-Plough
Publications - 14
Citations - 1434
Michael B. Cable is an academic researcher from Schering-Plough. The author has contributed to research in topics: Polymerase & Nucleic acid. The author has an hindex of 9, co-authored 14 publications receiving 1398 citations.
Papers
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Journal ArticleDOI
Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site
Charles A. Lesburg,Michael B. Cable,Eric Ferrari,Zhi Hong,Anthony F. Mannarino,Patricia C. Weber +5 more
TL;DR: The HCV NS5B apoenzyme structure reported here can accommodate a template:primer duplex without global conformational changes, supporting the hypothesis that this structure is essentially preserved during the reaction pathway.
Journal ArticleDOI
Structure of the hepatitis C virus RNA helicase domain.
Nanhua Yao,Thomas Hesson,Michael B. Cable,Zhi Hong,Ann D. Kwong,Hung V. Le,Patricia C. Weber +6 more
TL;DR: In this paper, a resolution structure of the HCV helicase from the positive-stranded RNA hepatitis C virus reveals a molecule with distinct NTPase and RNA binding domains, and the structure supports a mechanism of helicase activity involving initial recognition of the requisite 3' singlestranded region on the nucleic acid substrate by a conserved arginine-rich sequence on the RNA binding domain.
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Spin-labeled cardiolipin: preferential segregation in the boundary layer of cytochrome c oxidase
Michael B. Cable,Gary L. Powell +1 more
Journal ArticleDOI
Mechanism of allosteric regulation of the Ca,Mg-ATPase of sarcoplasmic reticulum: studies with 5'-adenylyl methylenediphosphate.
TL;DR: Four mechanisms for the allosteric regulation of the calcium and magnesium ion activated adenosinetriphosphatase (Ca,Mg-ATPase) of sarcoplasmic reticulum were examined and negative cooperativity in substrate binding was not supported by 3H-labeled 5'-adenylyl methylenediphosphate (AMPPCP) binding.
Journal ArticleDOI
Aminothiazole inhibitors of HCV RNA polymerase
Gerald W. Shipps,Yongqi Deng,Tong Wang,Janeta Popovici-Muller,Patrick J. Curran,Kristin E. Rosner,Alan B. Cooper,Viyyoor M. Girijavallabhan,Nancy Butkiewicz,Michael B. Cable +9 more
TL;DR: Aminothiazole-based inhibitors designed for HCV polymerase display low micromolar potencies in biochemical assays and the composition of these compounds suggests that they may be interacting at a recently discovered allosteric site on the polymerase.