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Volumn 30, Issue , 2011, Pages 1-11

The Enzymology of CAAX Protein Prenylation

Author keywords

CAAX protein; Farnesyl; Geranylgeranyl; Isoprenylation; Prenylation; Transferase

Indexed keywords


EID: 81255189465     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-415922-8.00001-X     Document Type: Chapter
Times cited : (2)

References (65)
  • 1
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: molecular mechanisms and functional consequences
    • Zhang F.L., Casey P.J. Protein prenylation: molecular mechanisms and functional consequences. Annu Rev Biochem 1996, 65:241-269.
    • (1996) Annu Rev Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 3
    • 0025194466 scopus 로고
    • Inhibition of purified p21ras farnesyl:protein transferase by cys-aax tetrapeptides
    • Reiss Y., Goldstein J.L., Seabra M.C., Casey P.J., Brown M.S. Inhibition of purified p21ras farnesyl:protein transferase by cys-aax tetrapeptides. Cell 1990, 62:81-88.
    • (1990) Cell , vol.62 , pp. 81-88
    • Reiss, Y.1    Goldstein, J.L.2    Seabra, M.C.3    Casey, P.J.4    Brown, M.S.5
  • 4
    • 0026072339 scopus 로고
    • Enzymatic modification of proteins with a geranylgeranyl isoprenoid
    • Casey P.J., Thissen J.A., Moomaw J.F. Enzymatic modification of proteins with a geranylgeranyl isoprenoid. Proc Natl Acad Sci USA 1991, 88:8631-8635.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8631-8635
    • Casey, P.J.1    Thissen, J.A.2    Moomaw, J.F.3
  • 5
    • 0026001936 scopus 로고
    • A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity
    • Yokoyama K., Goodwin G.W., Ghomashchi F., Glomset J.A., Gelb M.H. A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity. Proc Natl Acad Sci USA 1991, 88:5302-5306.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5302-5306
    • Yokoyama, K.1    Goodwin, G.W.2    Ghomashchi, F.3    Glomset, J.A.4    Gelb, M.H.5
  • 6
    • 0028331587 scopus 로고
    • Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic
    • Gibbs J.B., Oliff A., Kohl N.E. Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic. Cell 1994, 77:175-178.
    • (1994) Cell , vol.77 , pp. 175-178
    • Gibbs, J.B.1    Oliff, A.2    Kohl, N.E.3
  • 7
    • 0037805547 scopus 로고    scopus 로고
    • Ras oncogenes: the first 30 years
    • Malumbres M., Barbacid M. Ras oncogenes: the first 30 years. Nat Rev Cancer 2003, 3:459-465.
    • (2003) Nat Rev Cancer , vol.3 , pp. 459-465
    • Malumbres, M.1    Barbacid, M.2
  • 8
    • 34548815038 scopus 로고    scopus 로고
    • Development of farnesyltransferase inhibitors for clinical cancer therapy: focus on hematologic malignancies
    • Karp J.E., Lancet J.E. Development of farnesyltransferase inhibitors for clinical cancer therapy: focus on hematologic malignancies. Cancer Invest 2007, 25:484-494.
    • (2007) Cancer Invest , vol.25 , pp. 484-494
    • Karp, J.E.1    Lancet, J.E.2
  • 9
    • 47349089381 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: a detailed chemical view on an elusive biological problem
    • Sousa S., Fernandes P., Ramos M. Farnesyltransferase inhibitors: a detailed chemical view on an elusive biological problem. Curr Med Chem 2008, 15:1478-1492.
    • (2008) Curr Med Chem , vol.15 , pp. 1478-1492
    • Sousa, S.1    Fernandes, P.2    Ramos, M.3
  • 10
    • 79955505050 scopus 로고    scopus 로고
    • Phase accelerated dose-escalating safety and pharmacokinetic study of GGTI-2419, a novel geranylgeranyltransferase I inhibitor, in patients with refractory solid tumors
    • O'Dwyer P.J., Gallagher M., Nguyen B., Waddell M.J., Chiorean E.J. Phase accelerated dose-escalating safety and pharmacokinetic study of GGTI-2419, a novel geranylgeranyltransferase I inhibitor, in patients with refractory solid tumors. Ann Oncol 2010, 21(Suppl. 2):ii42.
    • (2010) Ann Oncol , vol.21 , Issue.SUPPL. 2
    • O'Dwyer, P.J.1    Gallagher, M.2    Nguyen, B.3    Waddell, M.J.4    Chiorean, E.J.5
  • 11
    • 0026806554 scopus 로고
    • Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements
    • Moomaw J.F., Casey P.J. Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements. J Biol Chem 1992, 267:17438-17443.
    • (1992) J Biol Chem , vol.267 , pp. 17438-17443
    • Moomaw, J.F.1    Casey, P.J.2
  • 12
    • 0027367333 scopus 로고
    • Cdna cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FTNA and FTNB loci and related sequences
    • Andres D.A., Milatovich A., Ozcelik T., Wenzlau J.M., Brown M.S., Goldstein J.L., Francke U. Cdna cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FTNA and FTNB loci and related sequences. Genomics 1993, 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
  • 13
    • 0027289625 scopus 로고
    • Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases
    • Omer C.A., Kral A.M., Diehl R.E., Prendergast G.C., Powers S., Allen C.M., Gibbs J.B., Kohl N.E. Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. Biochemistry 1993, 32:5167-5176.
    • (1993) Biochemistry , vol.32 , pp. 5167-5176
    • Omer, C.A.1    Kral, A.M.2    Diehl, R.E.3    Prendergast, G.C.4    Powers, S.5    Allen, C.M.6    Gibbs, J.B.7    Kohl, N.E.8
  • 14
    • 0030909826 scopus 로고    scopus 로고
    • Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution
    • Park H.W., Boduluri S.R., Moomaw J.F., Casey P.J., Beese L.S. Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution. Science 1997, 275:1800-1804.
    • (1997) Science , vol.275 , pp. 1800-1804
    • Park, H.W.1    Boduluri, S.R.2    Moomaw, J.F.3    Casey, P.J.4    Beese, L.S.5
  • 15
    • 0027267418 scopus 로고
    • High level expression of mammalian protein farnesyltransferase in a baculovirus system. The purified protein contains zinc
    • Chen W.J., Moomaw J.F., Overton L., Kost T.A., Casey P.J. High level expression of mammalian protein farnesyltransferase in a baculovirus system. The purified protein contains zinc. J Biol Chem 1993, 268:9675-9680.
    • (1993) J Biol Chem , vol.268 , pp. 9675-9680
    • Chen, W.J.1    Moomaw, J.F.2    Overton, L.3    Kost, T.A.4    Casey, P.J.5
  • 16
    • 0026657881 scopus 로고
    • Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme
    • Reiss Y., Brown M.S., Goldstein J.L. Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from rat brain, a zinc metalloenzyme. J Biol Chem 1992, 267:6403-6408.
    • (1992) J Biol Chem , vol.267 , pp. 6403-6408
    • Reiss, Y.1    Brown, M.S.2    Goldstein, J.L.3
  • 17
    • 0032493317 scopus 로고    scopus 로고
    • Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate
    • Long S.B., Casey P.J., Beese L.S. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry 1998, 37:9612-9618.
    • (1998) Biochemistry , vol.37 , pp. 9612-9618
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 18
    • 0037057707 scopus 로고    scopus 로고
    • Reaction path of protein farnesyltransferase at atomic resolution
    • Long S.B., Casey P.J., Beese L.S. Reaction path of protein farnesyltransferase at atomic resolution. Nature 2002, 419:645-650.
    • (2002) Nature , vol.419 , pp. 645-650
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 19
    • 0344874683 scopus 로고    scopus 로고
    • Structure of mammalian protein geranylgeranyltransferase type-I
    • Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S. Structure of mammalian protein geranylgeranyltransferase type-I. EMBO J 2003, 22:5963-5974.
    • (2003) EMBO J , vol.22 , pp. 5963-5974
    • Taylor, J.S.1    Reid, T.S.2    Terry, K.L.3    Casey, P.J.4    Beese, L.S.5
  • 20
    • 4644370323 scopus 로고    scopus 로고
    • Crystallographic analysis of caax prenyltransferases complexed with substrates defines rules of protein substrate selectivity
    • Reid T.S., Terry K.L., Casey P.J., Beese L.S. Crystallographic analysis of caax prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J Mol Biol 2004, 343:417-433.
    • (2004) J Mol Biol , vol.343 , pp. 417-433
    • Reid, T.S.1    Terry, K.L.2    Casey, P.J.3    Beese, L.S.4
  • 22
    • 0025923649 scopus 로고
    • Nonidentical subunits of p21H-ras farnesyltransferase. Peptide binding and farnesyl pyrophosphate carrier functions
    • Reiss Y., Seabra M.C., Armstrong S.A., Slaughter C.A., Goldstein J.L., Brown M.S. Nonidentical subunits of p21H-ras farnesyltransferase. Peptide binding and farnesyl pyrophosphate carrier functions. J Biol Chem 1991, 266:10672-10677.
    • (1991) J Biol Chem , vol.266 , pp. 10672-10677
    • Reiss, Y.1    Seabra, M.C.2    Armstrong, S.A.3    Slaughter, C.A.4    Goldstein, J.L.5    Brown, M.S.6
  • 23
    • 0027416643 scopus 로고
    • Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex
    • Yokoyama K., Gelb M.H. Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex. J Biol Chem 1993, 268:4055-4060.
    • (1993) J Biol Chem , vol.268 , pp. 4055-4060
    • Yokoyama, K.1    Gelb, M.H.2
  • 24
    • 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., Gelb M.H. Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase-I and protein farnesyltransferase and its consequence on the specificity of protein prenylation. J Biol Chem 1997, 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
  • 25
    • 0029007105 scopus 로고
    • Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release
    • Furfine E.S., Leban J.J., Landavazo A., Moomaw J.F., Casey P.J. Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. Biochemistry 1995, 34:6857-6862.
    • (1995) Biochemistry , vol.34 , pp. 6857-6862
    • Furfine, E.S.1    Leban, J.J.2    Landavazo, A.3    Moomaw, J.F.4    Casey, P.J.5
  • 26
    • 2442561561 scopus 로고    scopus 로고
    • Positively charged side chains in protein farnesyltransferase enhance catalysis by stabilizing the formation of the diphosphate leaving group
    • Bowers K.E., Fierke C.A. Positively charged side chains in protein farnesyltransferase enhance catalysis by stabilizing the formation of the diphosphate leaving group. Biochemistry 2004, 43:5256-5265.
    • (2004) Biochemistry , vol.43 , pp. 5256-5265
    • Bowers, K.E.1    Fierke, C.A.2
  • 27
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey P.J., Seabra M.C. Protein prenyltransferases. J Biol Chem 1996, 271:5289-5292.
    • (1996) J Biol Chem , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 29
    • 0032480805 scopus 로고    scopus 로고
    • H-ras peptide and protein substrates bind protein farnesyltransferase as an ionized thiolate
    • Hightower K.E., Huang C.C., Casey P.J., Fierke C.A. H-ras peptide and protein substrates bind protein farnesyltransferase as an ionized thiolate. Biochemistry 1998, 37:15555-15562.
    • (1998) Biochemistry , vol.37 , pp. 15555-15562
    • Hightower, K.E.1    Huang, C.C.2    Casey, P.J.3    Fierke, C.A.4
  • 30
    • 0034651550 scopus 로고    scopus 로고
    • The basis for K-ras4b binding specificity to protein farnesyltransferase revealed by 2 å resolution ternary complex structures
    • Long S.B., Casey P.J., Beese L.S. The basis for K-ras4b binding specificity to protein farnesyltransferase revealed by 2 å resolution ternary complex structures. Struct Fold Des 2000, 8:209-222.
    • (2000) Struct Fold Des , vol.8 , pp. 209-222
    • Long, S.B.1    Casey, P.J.2    Beese, L.S.3
  • 31
    • 0034646238 scopus 로고    scopus 로고
    • Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state
    • Huang C., Hightower K.E., Fierke C.A. Mechanistic studies of rat protein farnesyltransferase indicate an associative transition state. Biochemistry 2000, 39:2593-2602.
    • (2000) Biochemistry , vol.39 , pp. 2593-2602
    • Huang, C.1    Hightower, K.E.2    Fierke, C.A.3
  • 32
    • 0028988427 scopus 로고
    • Mammalian protein geranylgeranyltransferase-I: substrate specificity, kinetic mechanism, metal requirements, and affinity labeling
    • Yokoyama K., McGeady P., Gelb M.H. Mammalian protein geranylgeranyltransferase-I: substrate specificity, kinetic mechanism, metal requirements, and affinity labeling. Biochemistry 1995, 34:1344-1354.
    • (1995) Biochemistry , vol.34 , pp. 1344-1354
    • Yokoyama, K.1    McGeady, P.2    Gelb, M.H.3
  • 34
    • 72249106383 scopus 로고    scopus 로고
    • Synthesis and screening of a caal peptide library versus FTase reveals a surprising number of substrates
    • Krzysiak A.J., Aditya A.V., Hougland J.L., Fierke C.A., Gibbs R.A. Synthesis and screening of a caal peptide library versus FTase reveals a surprising number of substrates. Bioorg Med Chem Lett 2010, 20:767-770.
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 767-770
    • Krzysiak, A.J.1    Aditya, A.V.2    Hougland, J.L.3    Fierke, C.A.4    Gibbs, R.A.5
  • 35
    • 70450224430 scopus 로고    scopus 로고
    • Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities
    • Hougland J.L., Hicks K.A., Hartman H.L., Kelly R.A., Watt T.J., Fierke C.A. Identification of novel peptide substrates for protein farnesyltransferase reveals two substrate classes with distinct sequence selectivities. J Mol Biol 2010, 395:176-190.
    • (2010) J Mol Biol , vol.395 , pp. 176-190
    • Hougland, J.L.1    Hicks, K.A.2    Hartman, H.L.3    Kelly, R.A.4    Watt, T.J.5    Fierke, C.A.6
  • 36
    • 0030999833 scopus 로고    scopus 로고
    • Substrate binding is required for release of product from mammalian protein farnesyltransferase
    • Tschantz W.R., Furfine E.S., Casey P.J. Substrate binding is required for release of product from mammalian protein farnesyltransferase. J Biol Chem 1997, 272:9989-9993.
    • (1997) J Biol Chem , vol.272 , pp. 9989-9993
    • Tschantz, W.R.1    Furfine, E.S.2    Casey, P.J.3
  • 37
    • 0034649339 scopus 로고    scopus 로고
    • Conversion of Tyr361 beta to leu in mammalian protein farnesyltransferase impairs product release but not substrate recognition
    • Spence R.A., Hightower K.E., Terry K.L., Beese L.S., Fierke C.A., Casey P.J. Conversion of Tyr361 beta to leu in mammalian protein farnesyltransferase impairs product release but not substrate recognition. Biochemistry 2000, 39:13651-13659.
    • (2000) Biochemistry , vol.39 , pp. 13651-13659
    • Spence, R.A.1    Hightower, K.E.2    Terry, K.L.3    Beese, L.S.4    Fierke, C.A.5    Casey, P.J.6
  • 38
    • 0031017064 scopus 로고    scopus 로고
    • Evidence for a catalytic role of zinc in protein farnesyltransferase. Spectroscopy of Co2+-farnesyltransferase indicates metal coordination of the substrate thiolate
    • Huang C.C., Casey P.J., Fierke C.A. Evidence for a catalytic role of zinc in protein farnesyltransferase. Spectroscopy of Co2+-farnesyltransferase indicates metal coordination of the substrate thiolate. J Biol Chem 1997, 272:20-23.
    • (1997) J Biol Chem , vol.272 , pp. 20-23
    • Huang, C.C.1    Casey, P.J.2    Fierke, C.A.3
  • 39
    • 0032847980 scopus 로고    scopus 로고
    • Yeast protein farnesyltransferase. pKas of peptide substrates bound as zinc thiolates
    • Rozema D.B., Poulter C.D. Yeast protein farnesyltransferase. pKas of peptide substrates bound as zinc thiolates. Biochemistry 1999, 38:13138-13146.
    • (1999) Biochemistry , vol.38 , pp. 13138-13146
    • Rozema, D.B.1    Poulter, C.D.2
  • 40
    • 0034633953 scopus 로고    scopus 로고
    • Role of metals in the reaction catalyzed by protein farnesyltransferase
    • Saderholm M.J., Hightower K.E., Fierke C.A. Role of metals in the reaction catalyzed by protein farnesyltransferase. Biochemistry 2000, 39:12398-12405.
    • (2000) Biochemistry , vol.39 , pp. 12398-12405
    • Saderholm, M.J.1    Hightower, K.E.2    Fierke, C.A.3
  • 41
    • 0029007293 scopus 로고
    • A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase
    • Dolence J.M., Poulter C.D. A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase. Proc Natl Acad Sci USA 1995, 92:5008-5011.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5008-5011
    • Dolence, J.M.1    Poulter, C.D.2
  • 42
    • 0035799332 scopus 로고    scopus 로고
    • Stereochemical analysis of the reaction catalyzed by human protein geranylgeranyl transferase
    • Clausen V.A., Edelstein R.L., Distefano M.D. Stereochemical analysis of the reaction catalyzed by human protein geranylgeranyl transferase. Biochemistry 2001, 40:3920-3930.
    • (2001) Biochemistry , vol.40 , pp. 3920-3930
    • Clausen, V.A.1    Edelstein, R.L.2    Distefano, M.D.3
  • 43
    • 33845210617 scopus 로고    scopus 로고
    • Measurement of the alpha-secondary kinetic isotope effect for the reaction catalyzed by mammalian protein farnesyltransferase
    • Pais J.E., Bowers K.E., Fierke C.A. Measurement of the alpha-secondary kinetic isotope effect for the reaction catalyzed by mammalian protein farnesyltransferase. J Am Chem Soc 2006, 128:15086-15087.
    • (2006) J Am Chem Soc , vol.128 , pp. 15086-15087
    • Pais, J.E.1    Bowers, K.E.2    Fierke, C.A.3
  • 44
    • 0033621051 scopus 로고    scopus 로고
    • Farnesyl protein transferase: identification of K164 alpha and Y300 beta as catalytic residues by mutagenesis and kinetic studies
    • Wu Z., Demma M., Strickland C.L., Radisky E.S., Poulter C.D., Le H.V., Windsor W.T. Farnesyl protein transferase: identification of K164 alpha and Y300 beta as catalytic residues by mutagenesis and kinetic studies. Biochemistry 1999, 38:11239-11249.
    • (1999) Biochemistry , vol.38 , pp. 11239-11249
    • Wu, Z.1    Demma, M.2    Strickland, C.L.3    Radisky, E.S.4    Poulter, C.D.5    Le, H.V.6    Windsor, W.T.7
  • 45
    • 0025819073 scopus 로고
    • Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit
    • Seabra M.C., Reiss Y., Casey P.J., Brown M.S., Goldstein J.L. Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit. Cell 1991, 65:429-434.
    • (1991) Cell , vol.65 , pp. 429-434
    • Seabra, M.C.1    Reiss, Y.2    Casey, P.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 47
  • 48
    • 0025871919 scopus 로고
    • CDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast dpr1/ram1
    • Chen W.J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S. cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast dpr1/ram1. Cell 1991, 66:327-334.
    • (1991) Cell , vol.66 , pp. 327-334
    • Chen, W.J.1    Andres, D.A.2    Goldstein, J.L.3    Russell, D.W.4    Brown, M.S.5
  • 49
    • 0037013293 scopus 로고    scopus 로고
    • Inhibition of protein geranylgeranylation and rhoA/rhoA kinase pathway induces apoptosis in human endothelial cells
    • Li X., Liu L., Tupper J.C., Bannerman D.D., Winn R.K., Sebti S.M., Hamilton A.D., Harlan J.M. Inhibition of protein geranylgeranylation and rhoA/rhoA kinase pathway induces apoptosis in human endothelial cells. J Biol Chem 2002, 277:15309-15316.
    • (2002) J Biol Chem , vol.277 , pp. 15309-15316
    • Li, X.1    Liu, L.2    Tupper, J.C.3    Bannerman, D.D.4    Winn, R.K.5    Sebti, S.M.6    Hamilton, A.D.7    Harlan, J.M.8
  • 51
    • 27944455266 scopus 로고    scopus 로고
    • Peptide specificity of protein prenyltransferases is determined mainly by reactivity rather than binding affinity
    • Hartman H.L., Hicks K.A., Fierke C.A. Peptide specificity of protein prenyltransferases is determined mainly by reactivity rather than binding affinity. Biochemistry 2005, 44:15314-15324.
    • (2005) Biochemistry , vol.44 , pp. 15314-15324
    • Hartman, H.L.1    Hicks, K.A.2    Fierke, C.A.3
  • 53
    • 0028958919 scopus 로고
    • Polylysine and cvim sequences of k-rasb dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro
    • James G.L., Goldstein J.L., Brown M.S. Polylysine and cvim sequences of k-rasb dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro. J Biol Chem 1995, 270:6221-6226.
    • (1995) J Biol Chem , vol.270 , pp. 6221-6226
    • James, G.L.1    Goldstein, J.L.2    Brown, M.S.3
  • 55
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-ras in vivo
    • Rowell C.A., Kowalczyk J.J., Lewis M.D., Garcia A.M. Direct demonstration of geranylgeranylation and farnesylation of Ki-ras in vivo. J Biol Chem 1997, 272:14093-14097.
    • (1997) J Biol Chem , vol.272 , pp. 14093-14097
    • Rowell, C.A.1    Kowalczyk, J.J.2    Lewis, M.D.3    Garcia, A.M.4
  • 56
    • 0028920240 scopus 로고
    • CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to Rhob
    • Armstrong S.A., Hannah V.C., Goldstein J.L., Brown M.S. CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to Rhob. J Biol Chem 1995, 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
  • 57
    • 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., Thissen J.A. Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB. J Biol Chem 1997, 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
  • 58
    • 0034633651 scopus 로고    scopus 로고
    • RhoB prenylation is driven by the three carboxyl-terminal amino acids of the protein: evidenced in vivo by an anti-farnesyl cysteine antibody
    • Baron R., Fourcade E., Lajoie-Mazenc I., Allal C., Couderc B., Barbaras R., Favre G., Faye J.C., Pradines A. RhoB prenylation is driven by the three carboxyl-terminal amino acids of the protein: evidenced in vivo by an anti-farnesyl cysteine antibody. Proc Natl Acad Sci USA 2000, 97:11626-11631.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11626-11631
    • Baron, R.1    Fourcade, E.2    Lajoie-Mazenc, I.3    Allal, C.4    Couderc, B.5    Barbaras, R.6    Favre, G.7    Faye, J.C.8    Pradines, A.9
  • 59
    • 27944488368 scopus 로고    scopus 로고
    • Upstream polybasic region in peptides enhances dual specificity for prenylation by both farnesyltransferase and geranylgeranyltransferase type I
    • Hicks K.A., Hartman H.L., Fierke C.A. Upstream polybasic region in peptides enhances dual specificity for prenylation by both farnesyltransferase and geranylgeranyltransferase type I. Biochemistry 2005, 44:15325-15333.
    • (2005) Biochemistry , vol.44 , pp. 15325-15333
    • Hicks, K.A.1    Hartman, H.L.2    Fierke, C.A.3
  • 60
    • 0030962347 scopus 로고    scopus 로고
    • The potential of farnesyltransferase inhibitors as cancer chemotherapeutics
    • Gibbs J.B., Oliff A. The potential of farnesyltransferase inhibitors as cancer chemotherapeutics. Annu Rev Pharmacol Toxicol 1997, 37:143-166.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 143-166
    • Gibbs, J.B.1    Oliff, A.2
  • 61
    • 0027933505 scopus 로고
    • Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type I
    • Zhang F.L., Moomaw J.F., Casey P.J. Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type I. J Biol Chem 1994, 269:23465-23470.
    • (1994) J Biol Chem , vol.269 , pp. 23465-23470
    • Zhang, F.L.1    Moomaw, J.F.2    Casey, P.J.3
  • 62
    • 0030470834 scopus 로고    scopus 로고
    • Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I
    • Zhang F.L., Casey P.J. Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I. Biochem J 1996, 320(Pt 3):925-932.
    • (1996) Biochem J , vol.320 , Issue.PART 3 , pp. 925-932
    • Zhang, F.L.1    Casey, P.J.2


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