RAM1/YDL090C Literature Guide Help

Other names published for RAM1: DPR1, FUS8, SCG2, SGP2, STE16, protein farnesyltransferase, YDL090C

RAM1 - Substrates/Ligands/Cofactors (23)

ReferenceOther Genes Addressed
Wang YC and Distefano MD  (2012) Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation. Chem Commun (Camb) 48(66):8228-30
Hovlid ML, et al.  (2010) Synthesis, properties, and applications of diazotrifluropropanoyl-containing photoactive analogs of farnesyl diphosphate containing modified linkages for enhanced stability. Chem Biol Drug Des 75(1):51-67
Henry O, et al.  (2009) A versatile photoactivatable probe designed to label the diphosphate binding site of farnesyl diphosphate utilizing enzymes. Bioorg Med Chem 17(13):4797-805
Rucktaschel R, et al.  (2009) Farnesylation of pex19p is required for its structural integrity and function in peroxisome biogenesis. J Biol Chem 284(31):20885-96
Labadie GR, et al.  (2007) Farnesyl Diphosphate Analogues with omega-Bioorthogonal Azide and Alkyne Functional Groups for Protein Farnesyl Transferase-Catalyzed Ligation Reactions. J Org Chem 72(24):9291-9297
Liu XH and Prestwich GD  (2004) Didehydrofarnesyl diphosphate: an intrinsically fluorescent inhibitor of protein farnesyltransferase. Bioorg Med Chem Lett 14(9):2137-40
Turek-Etienne TC, et al.  (2003) Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase. Biochemistry 42(13):3716-24
Harris CM, et al.  (2002) Modulation of the zinc(II) center in protein farnesyltransferase by mutagenesis of the zinc(II) ligands. Biochemistry 41(33):10554-62
Schlitzer M, et al.  (2002) Non-thiol farnesyltransferase inhibitors: structure-activity relationships of benzophenone-based bisubstrate analogue farnesyltransferase inhibitors. Bioorg Med Chem 10(3):615-20
Rozema DB and Poulter CD  (1999) Yeast protein farnesyltransferase. pKas of peptide substrates bound as zinc thiolates. Biochemistry 38(40):13138-46
Caplin BE, et al.  (1998) Amino acid residues that define both the isoprenoid and CAAX preferences of the Saccharomyces cerevisiae protein farnesyltransferase. Creating the perfect farnesyltransferase. J Biol Chem 273(16):9472-9
Dolence JM, et al.  (1997) Yeast protein farnesyltransferase. Site-directed mutagenesis of conserved residues in the beta-subunit. Biochemistry 36(30):9246-52
Mathis JR and Poulter CD  (1997) Yeast protein farnesyltransferase: a pre-steady-state kinetic analysis. Biochemistry 36(21):6367-76
Trueblood CE, et al.  (1997) Substrate specificity determinants in the farnesyltransferase beta-subunit. Proc Natl Acad Sci U S A 94(20):10774-9
Dolence JM and Poulter CD  (1995) A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase. Proc Natl Acad Sci U S A 92(11):5008-11
Dolence JM, et al.  (1995) Yeast protein farnesyltransferase: steady-state kinetic studies of substrate binding. Biochemistry 34(51):16687-94
Farh L, et al.  (1995) Farnesylation and proteolysis are sequential, but distinct steps in the CaaX box modification pathway. Arch Biochem Biophys 318(1):113-21
Caplin BE, et al.  (1994) Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase. Biochim Biophys Acta 1205(1):39-48
Whiteway MS and Thomas DY  (1994) Site-directed mutations altering the CAAX box of Ste18, the yeast pheromone-response pathway G gamma subunit. Genetics 137(4):967-76
Kolling R, et al.  (1993) Synthesis and farnesylation of a-factor fusion proteins in Saccharomyces cerevisiae. FEBS Lett 336(1):129-32
Trueblood CE, et al.  (1993) Genetic evidence for in vivo cross-specificity of the CaaX-box protein prenyltransferases farnesyltransferase and geranylgeranyltransferase-I in Saccharomyces cerevisiae. Mol Cell Biol 13(7):4260-75
Schafer WR, et al.  (1990) Enzymatic coupling of cholesterol intermediates to a mating pheromone precursor and to the ras protein. Science 249(4973):1133-9
Fujiyama A, et al.  (1987) A novel yeast mutant defective in the processing of ras proteins: assessment of the effect of the mutation on processing steps. EMBO J 6(1):223-8