J
John S. Blanchard
Researcher at Albert Einstein College of Medicine
Publications - 213
Citations - 11344
John S. Blanchard is an academic researcher from Albert Einstein College of Medicine. The author has contributed to research in topics: Enzyme & Mycobacterium tuberculosis. The author has an hindex of 55, co-authored 212 publications receiving 10558 citations. Previous affiliations of John S. Blanchard include Venezuelan Institute for Scientific Research & John Innes Centre.
Papers
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Journal ArticleDOI
Molecular Insights into Aminoglycoside Action and Resistance
Sophie Magnet,John S. Blanchard +1 more
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Structure and functions of the GNAT superfamily of acetyltransferases
Matthew W. Vetting,Luiz Pedro S. de Carvalho,Michael Yu,Subray S. Hegde,Sophie Magnet,Steven L. Roderick,John S. Blanchard +6 more
TL;DR: This review of the Gcn5-related N-acetyltransferases will examine those members of this superfamily that have been both structurally and mechanistically characterized.
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Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis
TL;DR: When meropenem was combined with the β-lactamase inhibitor clavulanate, potent activity against laboratory strains of M. tuberculosis was observed and could potentially be used to treat patients with currently untreatable disease.
Journal ArticleDOI
Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis.
TL;DR: The three-dimensional structures of wild-type and mutant InhA revealed that drug resistance is directly related to a perturbation in the hydrogen-bonding network that stabilizes NADH binding.
Journal ArticleDOI
Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis.
Annaiek Quemard,James C. Sacchettini,Andréa Dessen,Catherine Vilchèze,Robert Bittman,William R. Jacobs,John S. Blanchard +6 more
TL;DR: Kinetic and microcalorimetric analysis demonstrates that the binding of NADH to the S94A mutant InhA, known to confer resistance to both isoniazid and ethionamide, is altered, with the formation of a binary InHA-NADH complex required for drug binding.