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Protein farnesyltransferase

Lane KT, Beese LS (2006) Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. J Lipid Res 47 681-699... [Pg.693]

Park HW et al (1997) Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution. Science 275(5307) 1800-1804... [Pg.374]

Protein farnesyltransferase (PFT) is responsible for farnesylation of cellular proteins, and PFT inhibitors have recently been developed for treatment of diseases involving farnesylated proteins. [Pg.174]

Chen, W.J., Moomaw, J.F., Overton, L., Kost, T.A., and Casey, P.J. (1993). High level expression of mammalian protein farnesyltransferase in a baculovirus system. The purified protein contains zinc. J Biol Chem 268 9675-9680. [Pg.9]

Reiss, Y., Brown, M.S., and Goldstein, J.L. (1992). Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme. J Biol Chem 267 6403-6408. [Pg.9]

Long, S.B., Casey, P.J., and Beese, L.S. (1998). Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry 37 9612-9618. [Pg.9]

Yokoyama, K., Zimmerman, K., Scholten, J., and Gelb, M.H. (1997). Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation. J Biol Chem 272 3944-3952. [Pg.10]

Bowers, K.E., and Fierke, C. A. (2004). Positively charged side chains in protein farnesyltransferase enhance catalysis by stabilizing the formation of the diphosphate leaving group. Biochemistry 43 5256-5265. [Pg.10]

Huang, C., Hightower, K.E., and Fierke, C.A. (2000). Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state. Biochemistry 39 2593-2602. [Pg.10]

Hougland, J.L., Hicks, K.A., Hartman, H.L., Kelly, R.A., Watt, T.J., and Fierke, C.A. (2010). Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities. J Mol Biol 395 176-190. [Pg.10]

Tschantz, W.R., Furfine, E.S., and Casey, P.J. (1997). Substrate binding is required for release of product from manunalian protein farnesyltransferase. J Biol Chem 272 9989-9993. [Pg.10]

Huang, C.C., Casey, P.J., and Fierke, C. A. (1997). Evidence for a catalytic role of zinc in protein farnesyltransferase. Spectroscopy of Co2h—farnesyltransferase indicates metal coordination of the substrate thiolate. J Biol Chem 272 20-23. [Pg.11]

Rozema, D.B., and Poulter, C.D. (1999). Yeast protein farnesyltransferase. pKas of peptide substrates bound as zinc thiolates. Biochemistry 38 13138-13146. [Pg.11]

Dolence, J.M., and Poulter, C.D. (1995). A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase. Proc Natl Acad Sci USA 92 5008-5011. [Pg.11]

Yang, S.H., et al. (2005). Blocking protein farnesyltransferase improves nuclear blebbing in mouse fibroblasts with a targeted Hutchinson-Gilford progeria syndrome mutation. Proc Natl Acad Sci USA 102 10291-10296. [Pg.40]

Pickett, J.S., et al. (2003). Kinetic studies of protein farnesyltransferase mutants estabhsh active substrate conformation. Biochemistry 42 9741-9748. [Pg.122]

Overhand, M., et al. (1998). Inhibitors of protein farnesyltransferase and protein geranyl-geranyl transferase I Synthesis of homologous diphosphonate analogues of isoprenylated pyrophosphate. Bioorg Chem 26 269-282. [Pg.123]


See other pages where Protein farnesyltransferase is mentioned: [Pg.295]    [Pg.108]    [Pg.290]    [Pg.104]    [Pg.454]    [Pg.52]    [Pg.52]    [Pg.579]    [Pg.742]    [Pg.774]    [Pg.105]    [Pg.344]    [Pg.56]    [Pg.3]    [Pg.9]    [Pg.11]    [Pg.11]    [Pg.11]    [Pg.119]    [Pg.123]   


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