ArticleBioorganic & medicinal chemistry2009
Mechanism-based inhibitors of serine proteases with high selectivity through optimization of S' subsite binding.
Article in Bioorganic & medicinal chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Dual function inhibitors of relevance to chronic obstructive pulmonary disease.Bioorganic & medicinal chemistry letters · 2011Article
- Neutrophil elastase inhibitors.Expert opinion on therapeutic patents · 2011Review
- Effects of structure on inhibitory activity in a series of mechanism-based inhibitors of human neutrophil elastase.Bioorganic & medicinal chemistry · 2010Article
- Inhibitors of human neutrophil elastase based on a highly functionalized N-amino-4-imidazolidinone scaffold.European journal of medicinal chemistry · 2010Article
- Utilization of the 1,2,3,5-thiatriazolidin-3-one 1,1-dioxide scaffold in the design of potential inhibitors of human neutrophil proteinase 3.Bioorganic & medicinal chemistry · 2010Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
A series of mechanism-based inhibitors designed to interact with the S' subsites of serine proteases was synthesized and their inhibitory activity toward the closely-related serine proteases human neutrophil elastase (HNE) and proteinase 3 (PR 3) was investigated. The compounds were found to be time-dependent inhibitors of HNE and were devoid of any inhibitory activity toward PR 3. The results suggest that highly selective inhibitors of serine proteases whose primary substrate specificity and active sites are similar can be identified by exploiting differences in their S' subsites. The best inhibitor (compound 16) had a k(inact)/K(I) value of 4580 M(-1)s(-1).
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