2688-85-9Relevant academic research and scientific papers
Probing the isoprenylcysteine carboxyl methyltransferase (Icmt) binding pocket: Sulfonamide modified farnesyl cysteine (SMFC) analogs as Icmt inhibitors
Majmudar, Jaimeen D.,Hahne, Kalub,Hrycyna, Christine A.,Gibbs, Richard A.
supporting information; experimental part, p. 2616 - 2620 (2011/06/20)
Human isoprenylcysteine carboxyl methyltransferase (hIcmt) is a promising anticancer target as it is important for the post-translational modification of oncogenic Ras proteins. We herein report the synthesis and biochemical activity of 41 farnesyl-cystei
Structure-based design of caspase-1 inhibitor containing a diphenyl ether sulfonamide
Shahripour, Aurash B,Plummer, Mark S,Lunney, Elizabeth A,Sawyer, Tomi K,Stankovic, Charles J,Connolly, Michael K,Rubin, John R,Walker, Nigel P.C,Brady, Kenneth D,Allen, Hamish J,Talanian, Robert V,Wong, Winnie W,Humblet, Christine
, p. 2779 - 2782 (2007/10/03)
A series of compounds was designed and prepared as inhibitors of interleukin-1β converting enzyme (ICE), also known as caspase-1. These inhibitors, which employ a diphenyl ether sulfonamide, were designed to improve potency by forming favorable interactions between the diphenyl ether rings and the prime side hydrophobic region. An X-ray crystal structure of a representative member of the diphenyl ether sulfonamide series bound to the active site of caspase-1 was obtained.
