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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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Metformin increases AMP-activated protein kinase activity in skeletal muscle of subjects with type 2 diabetes.

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.

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.

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

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.