945606-87-1Relevant articles and documents
Discovery of inhibitors of the channel-activating protease prostasin (CAP1/PRSS8) utilizing structure-based design
Tully, David C.,Vidal, Agnes,Chatterjee, Arnab K.,Williams, Jennifer A.,Roberts, Michael J.,Petrassi, H. Michael,Spraggon, Glen,Bursulaya, Badry,Pacoma, Reynand,Shipway, Aaron,Schumacher, Andrew M.,Danahay, Henry,Harris, Jennifer L.
scheme or table, p. 5895 - 5899 (2009/05/31)
Structure-based design was utilized to guide the early stage optimization of a substrate-like inhibitor to afford potent peptidomimetic inhibitors of the channel-activating protease prostasin. The first X-ray crystal structures of prostasin with small molecule inhibitors bound to the active site are also reported.
Compounds and Compositions as Channel Activating Protease Inhibitors
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Page/Page column 10-11, (2008/06/13)
The invention provides compounds and pharmaceutical compositions thereof, which are useful for modulating channel activating proteases, and methods for using such compounds to treat, ameliorate or prevent a condition associated with a channel activating protease, including but not limited to prostasin, PRSS22, TMPRSS11 (e.g., TMPRSS11B, TMPRSS11E), TMPRSS2, TMPRSS3, TMPRSS4 (MTSP-2), matriptase (MTSP-1), CAP2, CAP3, trypsin, cathepsin A, or neutrophil elastase.
Compounds and Compositions as Channel Activating Protease Inhibitors
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Page/Page column 14, (2008/06/13)
The invention provides compounds and pharmaceutical compositions thereof, which are useful for modulating channel activating proteases, and methods for, using such compounds to treat, ameliorate or prevent a condition associated with a channel activating protease, including but not limited to prostasin, PRSS22, TMPRSS11 (e.g., TMPRSS11B, TMPRSS11E), TMPRSS2, TMPRSS3, TMPRSS4 (MTSP-2), matriptase (MTSP-1), CAP2, CAP3, trypsin, cathepsin A, or neutrophil elastase.
Expanding the scope of PNA-encoded libraries: divergent synthesis of libraries targeting cysteine, serine and metallo-proteases as well as tyrosine phosphatases
Debaene, Fran?ois,Da Silva, Julien A.,Pianowski, Zbigniew,Duran, Fernando J.,Winssinger, Nicolas
, p. 6577 - 6586 (2008/02/05)
Seven PNA-encoded combinatorial libraries targeting proteases and phosphatases with covalent reversible and irreversible mechanism-based inhibitors were prepared. The libraries were synthesized using modified PNA monomers, which dramatically increase the water solubility of the libraries in biologically relevant buffers. The libraries were shown to selectively inhibit targeted enzymes.
