J
Joanne M. Williamson
Researcher at Merck & Co.
Publications - 32
Citations - 1820
Joanne M. Williamson is an academic researcher from Merck & Co.. The author has contributed to research in topics: Glucocorticoid receptor & Thienamycin. The author has an hindex of 19, co-authored 32 publications receiving 1711 citations.
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Journal ArticleDOI
Metformin increases AMP-activated protein kinase activity in skeletal muscle of subjects with type 2 diabetes.
Nicolas Musi,Michael F. Hirshman,Jonas Nygren,Monika Svanfeldt,Peter Båvenholm,Olav Rooyackers,Gaochao Zhou,Joanne M. Williamson,Olle Ljunqvist,Suad Efendic,David E. Moller,Anders Thorell,Laurie J. Goodyear +12 more
TL;DR: The findings suggest that the metabolic effects of metformin in subjects with type 2 diabetes may be mediated by the activation of AMPK alpha2, which is implicated in the stimulation of glucose uptake into skeletal muscle and the inhibition of liver gluconeogenesis.
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Biosynthesis of fluorothreonine and fluoroacetic acid by the thienamycin producer, Streptomyces cattleya.
Minoru Sanada,Tetsuji Miyano,Shuichi Iwadare,Joanne M. Williamson,Byron H. Arison,Jack L. Smith,Alan W. Douglas,Jerrold M. Liesch,Edward S. Inamine +8 more
TL;DR: An antimetabolite, THX, was isolated from fermentation broths of the thienamycin producer, Streptomyces cattleya, when the organism was grown in the presence of a fluorine-containing substrate.
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Inhibitors of dihydrodipicolinate reductase, a key enzyme of the diaminopimelate pathway of Mycobacterium tuberculosis.
Anthony M. Paiva,Dana E. Vanderwall,John S. Blanchard,John W. Kozarich,Joanne M. Williamson,Theresa M. Kelly +5 more
TL;DR: The molecular modeling approach was very effective in identifying novel inhibitors of the enzyme and these compounds were obtained at a higher frequency based on the number of compounds analyzed than those inhibitors discovered via conventional screening, however, conventional screening proved beneficial in identifying compounds with greater structural diversity.
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A Structurally Unique, Potent, and Selective Oxytocin Antagonist Derived from Streptomyces silvensis
Douglas J. Pettibone,Bradley V. Clineschmidt,Paul S. Anderson,Roger M. Freidinger,George F. Lundell,Lawrence R. Koupal,Cheryl D. Schwartz,Joanne M. Williamson,Michael A. Goetz,Otto D. Hensens,Jerrold M. Liesch,James P. Springer +11 more
TL;DR: L-365,209 represents a unique class of compounds that provides an entirely new approach for the design of antagonists for these neurohypophyseal hormones.
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Determination of the Three-Dimensional Structure of Margatoxin by 1H, 13C, 15N Triple-Resonance Nuclear Magnetic Resonance Spectroscopy
TL;DR: The solution structure of the 39-residue peptide margatoxin, a scorpion toxin that selectively blocks the voltage-gated potassium-channel Kv1.3, has been determined by NMR spectroscopy.