Non-peptidic, non-prenylic inhibitors of the prenyl protein-specific protease Rce1.
Several compounds designed as bisubstrate analogues of protein farnesyltransferase inhibited the prenyl protein-specific protease Rce1, qualifying them as lead structures for a novel class of non-peptidic, non-prenylic inhibitors of this protease.
Schlitzer
M
M
Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Germany. schlitze@mailer.uni-marburg.de
Winter-Vann
A
A
Casey
P J
PJ
D019883:Alkyl and Aryl Transferases / Q000037:antagonists & inhibitors; D020650:Combinatorial Chemistry Techniques; D010450:Endopeptidases / Q000187:drug effects*; D051231:Farnesyltranstransferase; D006801:Humans; D020128:Inhibitory Concentration 50; D018716:Molecular Mimicry; D010455:Peptides / Q000138:chemical synthesis / Q000494:pharmacology; D011480:Protease Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology; D013329:Structure-Activity Relationship
D010455:Peptides; D011480:Protease Inhibitors; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase; D010450:Endopeptidases; C491326:RCE1 protein, human