Assays for inhibitors of CAAX farnesyltransferase in vitro and in intact cells.

[1]  M. Brown,et al.  PxF, a prenylated protein of peroxisomes. , 1994, The Journal of biological chemistry.

[2]  N. Kohl,et al.  Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic , 1994, Cell.

[3]  Richard G. W. Anderson,et al.  Molecular characterization of a membrane transporter for lactate, pyruvate, and other monocarboxylates: Implications for the Cori cycle , 1994, Cell.

[4]  S. Armstrong,et al.  REP-2, a Rab escort protein encoded by the choroideremia-like gene. , 1994, The Journal of biological chemistry.

[5]  J. Goldstein,et al.  Mad Bet for Rab , 1993, Nature.

[6]  M. Lewis,et al.  Peptidomimetic inhibitors of Ras farnesylation and function in whole cells. , 1993, The Journal of biological chemistry.

[7]  F. Tamanoi,et al.  Inhibitors of Ras farnesyltransferases. , 1993, Trends in biochemical sciences.

[8]  A. Levinson,et al.  Benzodiazepine peptidomimetics: potent inhibitors of Ras farnesylation in animal cells. , 1993, Science.

[9]  R L Smith,et al.  Selective inhibition of ras-dependent transformation by a farnesyltransferase inhibitor. , 1993, Science.

[10]  C. M. Allen,et al.  Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. , 1993, Biochemistry.

[11]  P. Casey,et al.  High level expression of mammalian protein farnesyltransferase in a baculovirus system. The purified protein contains zinc. , 1993, The Journal of biological chemistry.

[12]  M. Brown,et al.  Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role. , 1993, The Journal of biological chemistry.

[13]  P. Casey,et al.  Biochemistry of protein prenylation. , 1992, Journal of lipid research.

[14]  M. Brown,et al.  cDNA cloning of MEV, a mutant protein that facilitates cellular uptake of mevalonate, and identification of the point mutation responsible for its gain of function. , 1992, The Journal of biological chemistry.

[15]  A. Endo,et al.  The discovery and development of HMG-CoA reductase inhibitors. , 1992, Journal of lipid research.

[16]  J. Gibbs,et al.  Steady-state kinetic mechanism of Ras farnesyl:protein transferase. , 1992, Biochemistry.

[17]  Y. Reiss,et al.  Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme. , 1992, The Journal of biological chemistry.

[18]  S. Clarke,et al.  Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. , 1992, Annual review of biochemistry.

[19]  W. Schafer,et al.  Protein prenylation: genes, enzymes, targets, and functions. , 1992, Annual review of genetics.

[20]  L. Gierasch,et al.  Nonfarnesylated tetrapeptide inhibitors of protein farnesyltransferase. , 1991, The Journal of biological chemistry.

[21]  S. Moores,et al.  Sequence dependence of protein isoprenylation. , 1991, The Journal of biological chemistry.

[22]  D. Russell,et al.  cDNA cloning and expression of the peptide-binding β subunit of rat p21rasfarnesyltransferase, the counterpart of yeast DPR1/RAM1 , 1991, Cell.

[23]  S. Armstrong,et al.  Nonidentical subunits of p21H-ras farnesyltransferase. Peptide binding and farnesyl pyrophosphate carrier functions. , 1991, The Journal of biological chemistry.

[24]  P. Casey,et al.  Protein farnesyltransferase and geranylgeranyltransferase share a common α subunit , 1991, Cell.

[25]  Y. Reiss,et al.  Purification of ras farnesyl:Protein transferase , 1990 .

[26]  P. Casey,et al.  Inhibition of purified p21 ras farnesyl:protein transferase by Cys-AAX tetrapeptides , 1990, Cell.

[27]  J. Goldstein,et al.  Regulation of the mevalonate pathway , 1990, Nature.

[28]  C. Marshall,et al.  All ras proteins are polyisoprenylated but only some are palmitoylated , 1989, Cell.

[29]  M. Krieger,et al.  Expression of specific high capacity mevalonate transport in a Chinese hamster cell variant. , 1987, The Journal of biological chemistry.