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Volumn 384, Issue 7, 2003, Pages 977-989

Protein prenyltransferases: Anchor size, pseudogenes and parasites

Author keywords

Cancer; Farnesylation; Geranylgeranylation; Lipid anchor; Parasite; Posttranslational; Prenylation; Rab; Ras

Indexed keywords

ANTINEOPLASTIC AGENT; DIMETHYLALLYLTRANSFERASE; LIPID; PROTEIN FARNESYLTRANSFERASE INHIBITOR;

EID: 0042355181     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.110     Document Type: Review
Times cited : (23)

References (84)
  • 1
    • 0026640530 scopus 로고
    • Post-translational modifications of p21rho proteins
    • Adamson, P., Marshall, C.J., Hall, A., and Tilbrook, P.A. (1992). Post-translational modifications of p21rho proteins. J. Biol. Chem. 267, 20033-20038.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20033-20038
    • Adamson, P.1    Marshall, C.J.2    Hall, A.3    Tilbrook, P.A.4
  • 2
    • 0034632067 scopus 로고    scopus 로고
    • Molecular basis for Rab prenylation
    • Alory, C. and Balch, W.E. (2000). Molecular basis for Rab prenylation. J. Cell Biol. 150, 89-103.
    • (2000) J. Cell Biol. , vol.150 , pp. 89-103
    • Alory, C.1    Balch, W.E.2
  • 4
    • 0026570927 scopus 로고
    • In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits
    • Anant, J.S., Ong, O.C., Xie, H.Y., Clarke, S., O'Brien, P.J., and Fung, B.K. (1992). In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits. J. Biol. Chem. 267, 687-690.
    • (1992) J. Biol. Chem. , vol.267 , pp. 687-690
    • Anant, J.S.1    Ong, O.C.2    Xie, H.Y.3    Clarke, S.4    O'Brien, P.J.5    Fung, B.K.6
  • 5
    • 0027463466 scopus 로고
    • Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role
    • Andres, D.A., Goldstein, J.L., Ho, Y.K., and Brown, M.S. (1993a). Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role. J. Biol. Chem. 268, 1383-1390.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1383-1390
    • Andres, D.A.1    Goldstein, J.L.2    Ho, Y.K.3    Brown, M.S.4
  • 6
    • 0027367333 scopus 로고
    • cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences
    • Andres, D.A., Milatovich, A., Ozcelik, T., Wenzlau, J.M., Brown, M.S., Goldstein, J.L., and Francke, U. (1993b). cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences. Genomics 18, 105-112.
    • (1993) Genomics , vol.18 , pp. 105-112
    • Andres, D.A.1    Milatovich, A.2    Ozcelik, T.3    Wenzlau, J.M.4    Brown, M.S.5    Goldstein, J.L.6    Francke, U.7
  • 7
    • 0028920240 scopus 로고
    • CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB
    • Armstrong, S.A., Hannah, V.C., Goldstein, J.L., and Brown, M.S. (1995). CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB. J. Biol. Chem. 270, 7864-7868.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7864-7868
    • Armstrong, S.A.1    Hannah, V.C.2    Goldstein, J.L.3    Brown, M.S.4
  • 10
    • 0037119482 scopus 로고    scopus 로고
    • The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
    • Bracha, K., Lavy, M., and Yalovsky, S. (2002). The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity. J. Biol. Chem. 277, 29856-29864.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29856-29864
    • Bracha, K.1    Lavy, M.2    Yalovsky, S.3
  • 11
    • 0027958138 scopus 로고
    • Consequences of altered isoprenylation targets on a-factor export and bioactivity
    • Caldwell, G.A., Wang, S.H., Naider, F., and Becker, J.M. (1994). Consequences of altered isoprenylation targets on a-factor export and bioactivity. Proc. Natl. Acad. Sci. USA 91, 1275-1279.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1275-1279
    • Caldwell, G.A.1    Wang, S.H.2    Naider, F.3    Becker, J.M.4
  • 12
    • 0027518208 scopus 로고
    • Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras
    • Camp, L.A. and Hofmann, S.L. (1993). Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras. J. Biol. Chem. 268, 22566-22574.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22566-22574
    • Camp, L.A.1    Hofmann, S.L.2
  • 13
    • 0028199774 scopus 로고
    • Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase
    • 1205
    • Caplin, B.E., Hettich, L.A., and Marshall, M.S. (1994). Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase. Biochim. Biophys. Acta 1205, 39-48.
    • (1994) Biochim. Biophys. Acta , pp. 39-48
    • Caplin, B.E.1    Hettich, L.A.2    Marshall, M.S.3
  • 14
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey, P.J. and Seabra, M.C. (1996). Protein prenyltransferases. J. Biol. Chem. 271, 5289-5292.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 18
    • 0035666914 scopus 로고    scopus 로고
    • The GPI-anchor and protein sorting
    • Chatterjee, S. and Mayor, S. (2001). The GPI-anchor and protein sorting. Cell Mol. Life Sci. 58, 1969-1987.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1969-1987
    • Chatterjee, S.1    Mayor, S.2
  • 19
    • 0036667388 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: Promises and realities
    • Cox, A.D. and Der, C.J. (2002). Farnesyltransferase inhibitors: promises and realities. Curr. Opin. Pharmacol. 2, 388-393.
    • (2002) Curr. Opin. Pharmacol. , vol.2 , pp. 388-393
    • Cox, A.D.1    Der, C.J.2
  • 20
    • 0026659959 scopus 로고
    • Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein
    • Cox, A.D., Hisaka, M.M., Buss, J.E., and Der, C.J. (1992). Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein. Mol. Cell. Biol. 12, 2606-2615.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2606-2615
    • Cox, A.D.1    Hisaka, M.M.2    Buss, J.E.3    Der, C.J.4
  • 22
    • 0032571499 scopus 로고    scopus 로고
    • Genetic complexity of the human geranylgeranyltransferase I β subunit gene: A multigene family of pseudogenes derived from mis-spliced transcripts
    • Dhawan, P., Yang, E., Kumar, A., and Mehta, K.D. (1998). Genetic complexity of the human geranylgeranyltransferase Iβ subunit gene: a multigene family of pseudogenes derived from mis-spliced transcripts. Gene 210, 9-15.
    • (1998) Gene , vol.210 , pp. 9-15
    • Dhawan, P.1    Yang, E.2    Kumar, A.3    Mehta, K.D.4
  • 23
    • 0037174992 scopus 로고    scopus 로고
    • Stereospecificity and kinetic mechanism of human prenylcysteine lyase, an unusual thioether oxidase
    • Digits, J.A., Pyun, H.J., Coates, R.M., and Casey, P.J. (2002). Stereospecificity and kinetic mechanism of human prenylcysteine lyase, an unusual thioether oxidase. J. Biol. Chem. 277, 41086-41093.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41086-41093
    • Digits, J.A.1    Pyun, H.J.2    Coates, R.M.3    Casey, P.J.4
  • 24
    • 0034636066 scopus 로고    scopus 로고
    • Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p
    • Dolence, J.M., Steward, L.E., Dolence, E.K., Wong, D.H., and Poulter, C.D. (2000). Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p. Biochemistry 39, 4096-4104.
    • (2000) Biochemistry , vol.39 , pp. 4096-4104
    • Dolence, J.M.1    Steward, L.E.2    Dolence, E.K.3    Wong, D.H.4    Poulter, C.D.5
  • 25
    • 0033016719 scopus 로고    scopus 로고
    • Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB
    • Du, W., Lebowitz, P.F., and Prendergast, G.C. (1999). Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB. Mol. Cell. Biol. 19, 1831-1840.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1831-1840
    • Du, W.1    Lebowitz, P.F.2    Prendergast, G.C.3
  • 26
    • 0035049164 scopus 로고    scopus 로고
    • Post-translational GPI lipid anchor modification of proteins in kingdoms of life: Analysis of protein sequence data from complete genomes
    • Eisenhaber, B., Bork, P., and Eisenhaber, F. (2001). Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes. Protein Eng. 14, 17-25.
    • (2001) Protein Eng. , vol.14 , pp. 17-25
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 27
    • 0035081235 scopus 로고    scopus 로고
    • Gene duplication and the structure of eukaryotic genomes
    • Friedman, R. and Hughes, A.L. (2001). Gene duplication and the structure of eukaryotic genomes. Genome Res. 11, 373-381.
    • (2001) Genome Res. , vol.11 , pp. 373-381
    • Friedman, R.1    Hughes, A.L.2
  • 28
    • 0029127725 scopus 로고
    • Binding of prenylated and polybasic peptides to membranes: Affinities and intervesicle exchange
    • Ghomashchi, F., Zhang, X., Liu, L., and Gelb, M.H. (1995). Binding of prenylated and polybasic peptides to membranes: affinities and intervesicle exchange. Biochemistry 34, 11910-11918.
    • (1995) Biochemistry , vol.34 , pp. 11910-11918
    • Ghomashchi, F.1    Zhang, X.2    Liu, L.3    Gelb, M.H.4
  • 30
    • 0035851150 scopus 로고    scopus 로고
    • Prenylation of target GTPases contributes to signaling specificity of Ras-guanine nucleotide exchange factors
    • Gotoh, T., Tian, X., and Feig, L.A. (2001). Prenylation of target GTPases contributes to signaling specificity of Ras-guanine nucleotide exchange factors. J. Biol. Chem. 276, 38029-38035.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38029-38035
    • Gotoh, T.1    Tian, X.2    Feig, L.A.3
  • 31
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock, J.F., Magee, A.I., Childs, J.E., and Marshall, C.J. (1989). All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57, 1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 32
    • 0036314772 scopus 로고    scopus 로고
    • Studying genomes through the aeons: Protein families, pseudogenes and proteome evolution
    • Harrison, P.M. and Gerstein, M. (2002). Studying genomes through the aeons: protein families, pseudogenes and proteome evolution. J. Mol. Biol. 318, 1155-1174.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1155-1174
    • Harrison, P.M.1    Gerstein, M.2
  • 33
    • 0027363447 scopus 로고
    • Modification of eukaryotic signaling proteins by C-terminal methylation reactions
    • Hrycyna, C.A. and Clarke, S. (1993). Modification of eukaryotic signaling proteins by C-terminal methylation reactions. Pharmacol. Ther. 59, 281-300.
    • (1993) Pharmacol. Ther. , vol.59 , pp. 281-300
    • Hrycyna, C.A.1    Clarke, S.2
  • 34
    • 0034791773 scopus 로고    scopus 로고
    • Identification and characterisation of Toxoplasma gondii protein farnesyltransferase
    • Ibrahim, M., Azzouz, N., Gerold, P., and Schwarz, R.T. (2001). Identification and characterisation of Toxoplasma gondii protein farnesyltransferase. Int. J. Parasitol. 31, 1489-1497.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1489-1497
    • Ibrahim, M.1    Azzouz, N.2    Gerold, P.3    Schwarz, R.T.4
  • 35
    • 0026726050 scopus 로고
    • Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases
    • Inglese, J., Koch, W.J., Caron, M.G., and Lefkowitz, R.J. (1992). Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases. Nature 359, 147-150.
    • (1992) Nature , vol.359 , pp. 147-150
    • Inglese, J.1    Koch, W.J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 36
    • 0035930546 scopus 로고    scopus 로고
    • Gβγ affinity for bovine rhodopsin is determined by the carboxyl-terminal sequences of the γ subunit
    • Jian, X., Clark, W.A., Kowalak, J., Markey, S.P., Simonds, W.F., and Northup, J.K. (2001). Gβγ affinity for bovine rhodopsin is determined by the carboxyl-terminal sequences of the γ subunit. J. Biol. Chem. 276, 48518-48525.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48518-48525
    • Jian, X.1    Clark, W.A.2    Kowalak, J.3    Markey, S.P.4    Simonds, W.F.5    Northup, J.K.6
  • 37
    • 0017805865 scopus 로고
    • Structure of rhodotorucine A, a novel lipopeptide, inducing mating tube formation in Rhodosporidium toruloides
    • Kamiya, Y., Sakurai, A., Tamura, S., and Takahashi, N. (1978). Structure of rhodotorucine A, a novel lipopeptide, inducing mating tube formation in Rhodosporidium toruloides. Biochem. Biophys. Res. Commun. 83, 1077-1083.
    • (1978) Biochem. Biophys. Res. Commun. , vol.83 , pp. 1077-1083
    • Kamiya, Y.1    Sakurai, A.2    Tamura, S.3    Takahashi, N.4
  • 41
    • 0030916369 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB
    • Lebowitz, P.F., Casey, P.J., Prendergast, G.C., and Thissen, J.A. (1997). Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB. J. Biol. Chem. 272, 15591-15594.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15591-15594
    • Lebowitz, P.F.1    Casey, P.J.2    Prendergast, G.C.3    Thissen, J.A.4
  • 42
    • 0036375597 scopus 로고    scopus 로고
    • Structure, mechanism and function of prenyltransferases
    • Liang, P.H., Ko, T.P., and Wang, A.H. (2002). Structure, mechanism and function of prenyltransferases. Eur. J. Biochem. 269, 3339-3354.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3339-3354
    • Liang, P.H.1    Ko, T.P.2    Wang, A.H.3
  • 43
    • 0037057707 scopus 로고    scopus 로고
    • Reaction path of protein farnesyltransferase at atomic resolution
    • Long, S.B., Casey, P.J., and Beese, L.S. (2002). Reaction path of protein farnesyltransferase at atomic resolution. Nature 419, 645-650.
    • (2002) Nature , vol.419 , pp. 645-650
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 45
    • 0036290648 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: Prediction of substrate proteins from amino acid sequence
    • Maurer-Stroh, S., Eisenhaber, B., and Eisenhaber, F. (2002a). N-terminal N-myristoylation of proteins: prediction of substrate proteins from amino acid sequence. J. Mol. Biol. 317, 541-557.
    • (2002) J. Mol. Biol. , vol.317 , pp. 541-557
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 46
    • 0036295384 scopus 로고    scopus 로고
    • N-terminal N-myristoylation of proteins: Refinement of the sequence motif and its taxon-specific differences
    • Maurer-Stroh, S., Eisenhaber, B., and Eisenhaber, F. (2002b). N-terminal N-myristoylation of proteins: refinement of the sequence motif and its taxon-specific differences. J. Mol. Biol. 317, 523-540.
    • (2002) J. Mol. Biol. , vol.317 , pp. 523-540
    • Maurer-Stroh, S.1    Eisenhaber, B.2    Eisenhaber, F.3
  • 47
    • 0037118620 scopus 로고    scopus 로고
    • A protein-farnesyl transferase inhibitor interferes with the serum-induced conversion of Candida albicans from a cellular yeast form to a filamentous form
    • McGeady, P., Logan, D.A., and Wansley, D.L. (2002). A protein-farnesyl transferase inhibitor interferes with the serum-induced conversion of Candida albicans from a cellular yeast form to a filamentous form. FEMS Microbiol. Lett. 213, 41-44.
    • (2002) FEMS Microbiol. Lett. , vol.213 , pp. 41-44
    • McGeady, P.1    Logan, D.A.2    Wansley, D.L.3
  • 49
    • 0030346309 scopus 로고    scopus 로고
    • Palmitoylation: A posttranslational modification that regulates signalling from G-protein coupled receptors
    • Morello, J.P. and Bouvier, M. (1996). Palmitoylation: a posttranslational modification that regulates signalling from G-protein coupled receptors. Biochem. Cell Biol. 74, 449-457.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 449-457
    • Morello, J.P.1    Bouvier, M.2
  • 52
    • 0033004413 scopus 로고    scopus 로고
    • Characterization of the Ras homologue of Schistosoma mansoni
    • Osman, A., Niles, E.G., and LoVerde, P.T. (1999). Characterization of the Ras homologue of Schistosoma mansoni. Mol. Biochem. Parasitol. 100, 27-41.
    • (1999) Mol. Biochem. Parasitol. , vol.100 , pp. 27-41
    • Osman, A.1    Niles, E.G.2    LoVerde, P.T.3
  • 53
    • 0036359736 scopus 로고    scopus 로고
    • The evolution of gene duplicates
    • Otto, S.P. and Yong, P. (2002). The evolution of gene duplicates. Adv. Genet. 46, 451-483.
    • (2002) Adv. Genet. , vol.46 , pp. 451-483
    • Otto, S.P.1    Yong, P.2
  • 54
    • 0028353285 scopus 로고
    • S-oxidative cleavage of farnesylcysteine and farnesylcysteine methyl ester by the flavin-containing monooxygenase
    • Park, S.B., Howald, W.N., and Cashman, J.R. (1994). S-oxidative cleavage of farnesylcysteine and farnesylcysteine methyl ester by the flavin-containing monooxygenase. Chem. Res. Toxicol. 7, 191-198.
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 191-198
    • Park, S.B.1    Howald, W.N.2    Cashman, J.R.3
  • 55
    • 0035339494 scopus 로고    scopus 로고
    • Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases
    • Pei, J. and Grishin, N.V. (2001). Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem. Sci. 26, 275-277.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 275-277
    • Pei, J.1    Grishin, N.V.2
  • 56
    • 0032500887 scopus 로고    scopus 로고
    • Role of farnesyltransferase in ABA regulation of guard cell anion channels and plant water loss
    • Pei, Z.M., Ghassemian, M., Kwak, C.M., McCourt, P., and Schroeder, J.I. (1998). Role of farnesyltransferase in ABA regulation of guard cell anion channels and plant water loss. Science 282, 287-290.
    • (1998) Science , vol.282 , pp. 287-290
    • Pei, Z.M.1    Ghassemian, M.2    Kwak, C.M.3    McCourt, P.4    Schroeder, J.I.5
  • 57
    • 0035798385 scopus 로고    scopus 로고
    • Evolution of the Rab family of small GTP-binding proteins
    • Pereira-Leal, J.B. and Seabra, M.C. (2001). Evolution of the Rab family of small GTP-binding proteins. J. Mol. Biol. 313, 889-901.
    • (2001) J. Mol. Biol. , vol.313 , pp. 889-901
    • Pereira-Leal, J.B.1    Seabra, M.C.2
  • 58
    • 0035523359 scopus 로고    scopus 로고
    • Actin' up: RhoB in cancer and apoptosis
    • Prendergast, G.C. (2001). Actin' up: RhoB in cancer and apoptosis. Nature Rev. Cancer 1, 162-168.
    • (2001) Nature Rev. Cancer , vol.1 , pp. 162-168
    • Prendergast, G.C.1
  • 59
    • 0035216833 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: Mechanism and applications
    • Prendergast, G.C. and Rane, N. (2001). Farnesyltransferase inhibitors: mechanism and applications. Expert. Opin. Investig. Drugs 10, 2105-2116.
    • (2001) Expert. Opin. Investig. Drugs , vol.10 , pp. 2105-2116
    • Prendergast, G.C.1    Rane, N.2
  • 60
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • 1451
    • Resh, M.D. (1999). Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16.
    • (1999) Biochim. Biophys. Acta , pp. 1-16
    • Resh, M.D.1
  • 61
    • 0345020362 scopus 로고    scopus 로고
    • Role of the carboxyterminal residue in peptide binding to protein farnesyltransferase and protein geranylgeranyltransferase
    • Roskoski Jr., R., and Ritchie, P. (1998). Role of the carboxyterminal residue in peptide binding to protein farnesyltransferase and protein geranylgeranyltransferase. Arch. Biochem. Biophys. 356, 167-176.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 167-176
    • Roskoski R., Jr.1    Ritchie, P.2
  • 62
    • 0019521320 scopus 로고
    • Peptidal sex hormones inducing conjugation tube formation in compatible mating-type cells of Tremella mesenterica
    • Sakagami, Y., Yoshida, M., Isogai, A., and Suzuki, A. (1981). Peptidal sex hormones inducing conjugation tube formation in compatible mating-type cells of Tremella mesenterica. Science 212, 1525-1527.
    • (1981) Science , vol.212 , pp. 1525-1527
    • Sakagami, Y.1    Yoshida, M.2    Isogai, A.3    Suzuki, A.4
  • 63
    • 0021204120 scopus 로고
    • Evidence for post-translational incorporation of a product of mevalonic acid into Swiss 3T3 cell proteins
    • Schmidt, R.A., Schneider, C.J., and Glomset, J.A. (1984). Evidence for post-translational incorporation of a product of mevalonic acid into Swiss 3T3 cell proteins. J. Biol. Chem. 259, 10175-10180.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10175-10180
    • Schmidt, R.A.1    Schneider, C.J.2    Glomset, J.A.3
  • 64
    • 0036137684 scopus 로고    scopus 로고
    • Rab GTPases, intracellular traffic and disease
    • Seabra, M.C., Mules, E.H., and Hume, A.N. (2002). Rab GTPases, intracellular traffic and disease. Trends Mol. Med. 8, 23-30.
    • (2002) Trends Mol. Med. , vol.8 , pp. 23-30
    • Seabra, M.C.1    Mules, E.H.2    Hume, A.N.3
  • 65
    • 0028196986 scopus 로고
    • Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers
    • Silvius, J.R. and l'Heureux, F. (1994). Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry 33, 3014-3022.
    • (1994) Biochemistry , vol.33 , pp. 3014-3022
    • Silvius, J.R.1    l'Heureux, F.2
  • 66
    • 0034672686 scopus 로고    scopus 로고
    • Functional aspects of polyisoprenoid protein substituents: Roles in protein-protein interaction and trafficking
    • 1529
    • Sinensky, M. (2000a). Functional aspects of polyisoprenoid protein substituents: roles in protein-protein interaction and trafficking. Biochim. Biophys. Acta 1529, 203-209.
    • (2000) Biochim. Biophys. Acta , pp. 203-209
    • Sinensky, M.1
  • 67
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • 1484
    • Sinensky, M. (2000b). Recent advances in the study of prenylated proteins. Biochim. Biophys. Acta 1484, 93-106.
    • (2000) Biochim. Biophys. Acta , pp. 93-106
    • Sinensky, M.1
  • 68
    • 0037118692 scopus 로고    scopus 로고
    • Sequencing of full-length cDNA encoding the α and β subunits of human casein kinase II from human platelets and megakaryocytic cells. Expression of the casein kinase IIα intronless gene in a megakaryocytic cell line
    • Singh, L.S. and Kalafatis, M. (2002). Sequencing of full-length cDNA encoding the α and β subunits of human casein kinase II from human platelets and megakaryocytic cells. Expression of the casein kinase IIα intronless gene in a megakaryocytic cell line. Biochemistry 41, 8935-8940.
    • (2002) Biochemistry , vol.41 , pp. 8935-8940
    • Singh, L.S.1    Kalafatis, M.2
  • 69
    • 0028153018 scopus 로고
    • Geranylgeranylated Rab proteins terminating in Cys-Ala-Cys, but not Cys-Cys, are carboxyl-methylated by bovine brain membranes in vitro
    • Smeland, T.E., Seabra, M.C., Goldstein, J.L., and Brown, M.S. (1994). Geranylgeranylated Rab proteins terminating in Cys-Ala-Cys, but not Cys-Cys, are carboxyl-methylated by bovine brain membranes in vitro. Proc. Natl. Acad. Sci. USA 91, 10712-10716.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10712-10716
    • Smeland, T.E.1    Seabra, M.C.2    Goldstein, J.L.3    Brown, M.S.4
  • 70
    • 0036024856 scopus 로고    scopus 로고
    • RhoA biological activity is dependent on prenylation but independent of specific isoprenoid modification
    • Solski, P.A., Helms, W., Keely, P.J., Su, L., and Der, C.J. (2002). RhoA biological activity is dependent on prenylation but independent of specific isoprenoid modification. Cell Growth Differ. 13, 363-373.
    • (2002) Cell Growth Differ. , vol.13 , pp. 363-373
    • Solski, P.A.1    Helms, W.2    Keely, P.J.3    Su, L.4    Der, C.J.5
  • 71
    • 0034777538 scopus 로고    scopus 로고
    • Protein farnesylation in mammalian cells: Effects of farnesyltransferase inhibitors on cancer cells
    • Tamanoi, F., Gau, C.L., Jiang, C., Edamatsu, H., and Kato-Stankiewicz, J. (2001a). Protein farnesylation in mammalian cells: effects of farnesyltransferase inhibitors on cancer cells. Cell Mol. Life Sci. 58, 1636-1649.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 1636-1649
    • Tamanoi, F.1    Gau, C.L.2    Jiang, C.3    Edamatsu, H.4    Kato-Stankiewicz, J.5
  • 73
    • 0035830388 scopus 로고    scopus 로고
    • Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II
    • Thoma, N.H., Iakovenko, A., Kalinin, A., Waldmann, H., Goody, R.S., and Alexandrov, K. (2001). Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II. Biochemistry 40, 268-274.
    • (2001) Biochemistry , vol.40 , pp. 268-274
    • Thoma, N.H.1    Iakovenko, A.2    Kalinin, A.3    Waldmann, H.4    Goody, R.S.5    Alexandrov, K.6
  • 75
    • 0037012905 scopus 로고    scopus 로고
    • Cell biology. The different hues of lipid rafts
    • van Meer, G. (2002). Cell biology. The different hues of lipid rafts. Science 296, 855-857.
    • (2002) Science , vol.296 , pp. 855-857
    • van Meer, G.1
  • 78
    • 0032588904 scopus 로고    scopus 로고
    • CK2α loci in the human genome: Structure and transcriptional activity
    • Wirkner, U. and Pyerin, W. (1999). CK2α loci in the human genome: structure and transcriptional activity. Mol. Cell Biochem. 191, 59-64.
    • (1999) Mol. Cell Biochem. , vol.191 , pp. 59-64
    • Wirkner, U.1    Pyerin, W.2
  • 79
    • 0033823696 scopus 로고    scopus 로고
    • Functional requirement of plant farnesyltransferase during development in Arabidopsis
    • Yalovsky, S., Kulukian, A., Rodriguez-Concepcion, M., Young, C.A., and Gruissem, W. (2000). Functional requirement of plant farnesyltransferase during development in Arabidopsis. Plant Cell 12, 1267-1278.
    • (2000) Plant Cell , vol.12 , pp. 1267-1278
    • Yalovsky, S.1    Kulukian, A.2    Rodriguez-Concepcion, M.3    Young, C.A.4    Gruissem, W.5
  • 81
    • 0031055466 scopus 로고    scopus 로고
    • Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation
    • Yokoyama, K., Zimmerman, K., Scholten, J., and Gelb, M.H. (1997b). 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.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3944-3952
    • Yokoyama, K.1    Zimmerman, K.2    Scholten, J.3    Gelb, M.H.4
  • 82
  • 83
    • 0032500692 scopus 로고    scopus 로고
    • Protein farnesyltransferase from Trypanosoma brucei. A heterodimer of 61- and 65-kDa subunits as a new target for antiparasite therapeutics
    • Yokoyama, K., Trobridge, P., Buckner, F.S., Van Voorhis, W.C., Stuart, K.D., and Gelb, M.H. (1998b). Protein farnesyltransferase from Trypanosoma brucei. A heterodimer of 61- and 65-kDa subunits as a new target for antiparasite therapeutics. J. Biol. Chem. 273, 26497-26505.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26497-26505
    • Yokoyama, K.1    Trobridge, P.2    Buckner, F.S.3    Van Voorhis, W.C.4    Stuart, K.D.5    Gelb, M.H.6
  • 84
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A., Violin, J.D., Newton, A.C., and Tsien, R.Y. (2002). Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


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