166169-81-9Relevant articles and documents
Potent, cell active, non-thiol tetrapeptide inhibitors of farnesyltransferase.
Hunt, John T.,Lee, Ving G.,Leftheris, Katerina,Seizinger, Bernd,Carboni, Joan,et al.
, p. 353 - 358 (1996)
All previously reported CAAX-based farnesyltransferase inhibitors contain a thiol functionality. We report that attachment of the 4-imidazolyl group, via 1-, 2-, or 3-carbon alkyl or alkanoyl spacers, to Val-Tic-Met or tLeu-Tic-Gln provides potent FT inhibitors. (R*)-N-[[1,2,3,4-Tetrahydro-2-[N-[2-(1H-imidazol-4-yl)ethyl] -L-valyl]-3-isoquinolinyl]carbonyl]-L-methionine ([imidazol- 4-yl-ethyl]-Val-Tic-Met), with FT IC50 = 0.79 nM, displayed potent cell activity in the absence of prodrug formation (SAG EC50 = 3.8 muM).
Development of highly potent inhibitors of Ras farnesyltransferase possessing cellular and in vivo activity
Leftheris, Katerina,Kline, Toni,Vite, Gregory D.,Cho, Young H.,Bhide, Rajeev S.,Patel, Dinesh V.,Patel, Manorama M.,Schmidt, Robert J.,Weller, Harold N.,Andahazy, Mary L.,Carboni, Joan M.,Gullo-Brown, Johnni L.,Lee, Francis Y. F.,Ricca, Carol,Rose, William C.,Yan, Ning,Barbacid, Mariano,Hunt, John T.,Meyers, Chester A.,Seizinger, Bernd R.,Zahler, Robert,Manne, Veeraswamy
, p. 224 - 236 (2007/10/03)
Analogs of CVFM (a known nonsubstrate farnesyltransferase (FT) inhibitor derived from a CA2A2X sequence where C is cysteine, A is an aliphatic residue, and X is any residue) were prepared where phenylalanine was replaced by (Z)-dehyd
