title: Evaluation of protein farnesyltransferase substrate specificity using synthetic peptide libraries.
abstract: Farnesylation, catalyzed by protein farnesyltransferase (FTase), is an important post-translational modification guiding cellular localization. Recently predictive models for identifying FTase substrates have been reported. Here we evaluate these models through screening of dansylated-GCaaS peptides, which also provides new insights into the protein substrate selectivity of FTase.
authors.affiliation: Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 575 Stadium Mall Drive, West Lafayette, IN 47907, USA.
authors.forename: Amanda J
authors.initials: AJ
authors.lastname: Krzysiak
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Scott
authors.forename: Katherine A
authors.initials: KA
authors.lastname: Hicks
authors.forename: Carol A
authors.initials: CA
authors.lastname: Fierke
authors.forename: Richard A
authors.initials: RA
authors.lastname: Gibbs
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D051231:Farnesyltranstransferase / Q000378:metabolism*; D015394:Molecular Structure; D019151:Peptide Library; D013379:Substrate Specificity