171354-06-6Relevant articles and documents
A scaffold merging approach to Hsp90 C-terminal inhibition: synthesis and evaluation of a chimeric library
Davis, Rachel E.,Zhang, Zheng,Blagg, Brian S. J.
supporting information, p. 593 - 598 (2017/03/31)
Inhibition of the Hsp90 C-terminus is an attractive therapeutic paradigm for the treatment of cancer, however the developmental space of C-terminal inhibitors is limited. It was hypothesized that the combination of two previously identified scaffolds into a single structure could provide a platform for which to probe the three-dimensional space within the Hsp90 C-terminal binding pocket. The resulting chimeric compounds displayed anti-proliferative activity at low micromolar concentrations and manifested inhibitory activity in an Hsp90-dependent rematuration assay. Initial structure-activity relationships suggest that this new scaffold binds Hsp90 in a conformation different from that of the parent compounds, and consequently, provides a new opportunity to develop more efficacious inhibitors of the Hsp90 C-terminal binding pocket.
BIS(ARYLOXY)ALKANES AS INHIBITORS OF PHOSPHOLIPASE A2 ENZYMES
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, (2008/06/13)
Compounds having the formula I: STR1 are inhibitors of the PLA 2 s enzymes. These compounds are useful as anti-allergic, anti-asthmatic, they are also useful in treating various inflammatory diseases such as rheumatoid arthritis, osteoarthritis, bursitis,
