Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Mary T. Macdonald"'
Autor:
Alex G. Waterson, Gary A. Sulikowski, Edward J. Metzger, Alec Walter, Richard J. Sciotti, Sydney L. Drury, Scott B Joseph, Chad C. Black, E. Duco Jansen, Eric P. Skaar, Mary T. Macdonald, Mingfeng Bai, Brendan F. Dutter, Clare L. Laut, Meng Su, James E. Crowe, Charles E. Bane, Anderson R. Miller, Monique R. Bennett, Ian M. Romaine, Bingwen Jing
Publikováno v:
Antimicrob Agents Chemother
Staphylococcus aureus is a serious threat to public health due to the rise of antibiotic resistance in this organism, which can prolong or exacerbate skin and soft tissue infections (SSTIs). Methicillin-resistant S. aureus is a Gram-positive bacteriu
Autor:
Laurence J. Altobell, Mary T. MacDonald, Kim D. Janda, Richard A. Lerner, Lyn H. Jones, Paul Wentworth, Nicholas A. Boyle
Publikováno v:
Angewandte Chemie International Edition. 41:4241-4244
Publikováno v:
Mini-Reviews in Medicinal Chemistry. 2:463-473
The replacement of the amide bond in a peptide backbone is a widely used form of peptide mimicry. Several of the most common amide bond surrogates, including peptidomimetic work done in this laboratory, and their biological applications are presented
Autor:
Jeffrey Aubé, Mary T. MacDonald
Publikováno v:
ChemInform. 32
Autor:
Huong-Thu Ton-Nu, Andrew H. Miller, Kelly Scheyhing, Hongfeng Gao, Erika M. Podar, Eric Y. Wang, Matthew D. Linnik, Christina A. Kessler, Mary T. Macdonald, Anne M. O'Rourke, Li Huang, David S. Jones
Publikováno v:
The Journal of pharmacology and experimental therapeutics. 324(2)
Semicarbazide-sensitive amine oxidase (SSAO, amine oxidase, copper-containing 3, and vascular adhesion protein-1) is a copper-containing enzyme that catalyzes the oxidative deamination of primary amines to an aldehyde, ammonia, and hydrogen peroxide.
Autor:
Lyn H, Jones, Laurence J, Altobell, Mary T, MacDonald, Nicholas A, Boyle, Paul, Wentworth, Richard A, Lerner, Kim D, Janda
Publikováno v:
Angewandte Chemie (International ed. in English). 41(22)
Publikováno v:
ChemInform. 31