Non??Thiol Farnesyltransferase Inhibitors: Utilization of the Far Aryl Binding Site by Arylthienylacryloylaminobenzophenones

…, M Altenkämper, I Sattler, M Schlitzer

Index: Mitsch, Andreas; Altenkaemper, Mirko; Sattler, Isabel; Schlitzer, Martin Archiv der Pharmazie, 2005 , vol. 338, # 1 p. 9 - 17

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Citation Number: 6

Abstract

Farnesyltransferase catalyzes the covalent modification of proteins carrying the CAAX-sequence at their C-terminus by the transfer of a farnesyl residue from farnesylpyro- phosphate to the thiol of a cysteine side chain. In the CAAX sequence, C represents a cysteine which side chain is farn- esylated, A amino acids which normally, but not necessarily, carry aliphatic side chains, and X mostly methionine or serine [1, 2]. ... Farnesyltransferase is one of the major ...