Selective inhibitors of bacterial t-RNA-(N1G37) methyltransferase (TrmD) that demonstrate novel ordering of the lid domain

…, R Albert, B Andrews, MM Gagnon, N Gao…

文献索引：Hill, Pamela J.; Abibi, Ayome; Albert, Robert; Andrews, Beth; Gagnon, Moriah M.; Gao, Ning; Grebe, Tyler; Hajec, Laurel I.; Huang, Jian; Livchak, Stephania; Lahiri, Sushmita D.; McKinney, David C.; Thresher, Jason; Wang, Hongming; Olivier, Nelson; Buurman, Ed T. Journal of Medicinal Chemistry, 2013 , vol. 56, # 18 p. 7278 - 7288

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被引用次数: 7

摘要

The tRNA-(N1G37) methyltransferase (TrmD) is essential for growth and highly conserved in both Gram-positive and Gram-negative bacterial pathogens. Additionally, TrmD is very distinct from its human orthologue TRM5 and thus is a suitable target for the design of novel antibacterials. Screening of a collection of compound fragments using Haemophilus influenzae TrmD identified inhibitory, fused thieno-pyrimidones that were competitive with ...