期刊
NATURE CHEMICAL BIOLOGY
卷 7, 期 1, 页码 22-24出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.492
关键词
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Designing selective inhibitors of proteases has proven problematic, in part because pharmacophores that confer potency exploit the conserved catalytic apparatus. We developed a fundamentally different approach by designing irreversible inhibitors that target noncatalytic cysteines that are structurally unique to a target in a protein family. We have successfully applied this approach to the important therapeutic target HCV protease, which has broad implications for the design of other selective protease inhibitors.
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