1999
DOI: 10.1002/(sici)1521-3765(19990104)5:1<227::aid-chem227>3.3.co;2-o
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Synthesis and In Vitro Evaluation of the Farnesyltransferase Inhibitor Pepticinnamin E

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Cited by 3 publications
(4 citation statements)
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“…Ras farnesyltransferase assay: The Ras farnesyltransferase activity was determined as previously described30, 31 by using a fluorescence‐based Ftase assay 32. As enzyme source we used an Escherichia coli strain overexpressing recombinant farnesyltransferase from Saccharomyces cerevisiae.…”
Section: Methodsmentioning
confidence: 99%
“…Ras farnesyltransferase assay: The Ras farnesyltransferase activity was determined as previously described30, 31 by using a fluorescence‐based Ftase assay 32. As enzyme source we used an Escherichia coli strain overexpressing recombinant farnesyltransferase from Saccharomyces cerevisiae.…”
Section: Methodsmentioning
confidence: 99%
“…The rational design of inhibitors, where a substrate analogue and a cofactor analogue are covalently linked to form a bisubstrate inhibitor, may provide innovative new lead structures in medicinal chemistry that feature both enhanced binding affinity and binding‐site selectivity. Some attempts have been made to construct bisubstrate inhibitors for kinases which target both the ATP and the substrate binding sites 1, 2. Other important targets are methyltransferases that depend on S ‐adenosylmethionine (SAM).…”
Section: Methodsmentioning
confidence: 99%
“…It is the first Ras protein substrate competition inhibitor derived from natural products. What is more, subsequent studies show that it is a dual substrate (Ras protein and FPP) competition inhibitor (IC 50 ¼ 42 lM) 34,115,116 . Structurally, compound 96 mimics the two substrates of FTase, CAAX, and FPP.…”
Section: Streptomyces Spmentioning
confidence: 99%
“…Hinterding et al 115 isolated pepticinnamin E (96) from secondary metabolites of Streptomyces sp. It is the first Ras protein substrate competition inhibitor derived from natural products.…”
Section: Streptomyces Spmentioning
confidence: 99%