Non-peptidic, non-prenylic inhibitors of the prenyl protein-specific protease Rce1

Bioorg Med Chem Lett. 2001 Feb 12;11(3):425-7. doi: 10.1016/s0960-894x(00)00685-5.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alkyl and Aryl Transferases / antagonists & inhibitors
  • Combinatorial Chemistry Techniques
  • Endopeptidases / drug effects*
  • Farnesyltranstransferase
  • Humans
  • Inhibitory Concentration 50
  • Molecular Mimicry
  • Peptides / chemical synthesis
  • Peptides / pharmacology
  • Protease Inhibitors / chemical synthesis*
  • Protease Inhibitors / pharmacology
  • Structure-Activity Relationship

Substances

  • Peptides
  • Protease Inhibitors
  • Alkyl and Aryl Transferases
  • Farnesyltranstransferase
  • Endopeptidases
  • RCE1 protein, human