title: A tagging-via-substrate technology for genome-wide detection and identification of farnesylated proteins.
abstract: Protein farnesylation is one of the most common lipid modifications and has an important role in the regulation of various cellular functions. We have recently developed a novel proteomics strategy, designated the tagging-via-substrate (TAS) approach, for the detection and proteomic analysis of farnesylated proteins. This chapter describes the principle of TAS technology and details the method for detection and enrichment of farnesylated proteins.
authors.affiliation: Department of Biochemistry, UT Southwestern Medical Center at Dallas, Dallas, Texas, USA.
authors.forename: Sung
authors.initials: S
authors.lastname: Chan Kim
authors.forename: Yoonjung
authors.initials: Y
authors.lastname: Kho
authors.forename: Deb
authors.initials: D
authors.lastname: Barma
authors.forename: John
authors.initials: J
authors.lastname: Falck
authors.forename: Yingming
authors.initials: Y
authors.lastname: Zhao
mesh_terms: D000818:Animals; D001386:Azides / Q000737:chemistry; D019556:COS Cells; D002522:Chlorocebus aethiops; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D024202:Electrophoretic Mobility Shift Assay; D050956:HSP40 Heat-Shock Proteins / Q000737:chemistry; D006801:Humans; D017368:Protein Prenylation; D040901:Proteomics / Q000379:methods*; D013194:Staining and Labeling / Q000379:methods; D053719:Tandem Mass Spectrometry; D018631:ras Proteins / Q000737:chemistry
chemical_list: D001386:Azides; C107481:DNAJA1 protein, human; D050956:HSP40 Heat-Shock Proteins; D018631:ras Proteins