메뉴 건너뛰기




Volumn 39, Issue 4, 2004, Pages 293-309

Isoprenoids: Remarkable diversity of form and function

Author keywords

[No Author keywords available]

Indexed keywords

ARRAYS; DEGRADATION; METABOLITES; MOLECULES; PHARMACODYNAMICS; PHOSPHATES;

EID: 3242785011     PISSN: 00244201     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11745-004-1233-3     Document Type: Review
Times cited : (184)

References (259)
  • 1
    • 0030846307 scopus 로고    scopus 로고
    • Creating isoprenoid diversity
    • Sacchettini, J.C., and Poulter, C.D. (1997) Creating Isoprenoid Diversity, Science 277, 1788-1789.
    • (1997) Science , vol.277 , pp. 1788-1789
    • Sacchettini, J.C.1    Poulter, C.D.2
  • 2
    • 0033527055 scopus 로고    scopus 로고
    • 2-Methylhopanoids as biomarkers for cyanobacterial oxygenic photosynthesis
    • Summons, R.E., Jahnke, L.L., Hope, J.M., and Logan, G.A. (1999) 2-Methylhopanoids as Biomarkers for Cyanobacterial Oxygenic Photosynthesis, Nature 400, 554-557.
    • (1999) Nature , vol.400 , pp. 554-557
    • Summons, R.E.1    Jahnke, L.L.2    Hope, J.M.3    Logan, G.A.4
  • 4
    • 0000007179 scopus 로고
    • Mevalonic kinase: Purification and properties
    • Tchen, T.T. (1958) Mevalonic Kinase: Purification and Properties, J. Biol. Chem. 233, 1100-1103.
    • (1958) J. Biol. Chem. , vol.233 , pp. 1100-1103
    • Tchen, T.T.1
  • 5
    • 3242766709 scopus 로고
    • On the biosynthesis of terpenes. XIV. On the determination of phosphomevalonic acid kinase and pyrophosphomevalonic acid decarboxylase in cell extracts
    • Tada, M., and Lynen, F. (1961) On the Biosynthesis of Terpenes. XIV. On the Determination of Phosphomevalonic Acid Kinase and Pyrophosphomevalonic Acid Decarboxylase in Cell Extracts, J. Biochem. 49, 758-764.
    • (1961) J. Biochem. , vol.49 , pp. 758-764
    • Tada, M.1    Lynen, F.2
  • 6
    • 0005226507 scopus 로고
    • Biosynthesis of terpenes. VII. Isopentenyl pyrophosphate isomerase
    • Agranoff, B.W., Eggerer, H., Henning, U., and Lynen, F. (1960) Biosynthesis of Terpenes. VII. Isopentenyl Pyrophosphate Isomerase, J. Biol. Chem. 235, 326-332.
    • (1960) J. Biol. Chem. , vol.235 , pp. 326-332
    • Agranoff, B.W.1    Eggerer, H.2    Henning, U.3    Lynen, F.4
  • 7
    • 0018199226 scopus 로고
    • 2-isopentenyl) adenosine and its nucleotide: Interaction with purified tRNAs and with bases, nucleosides and nucleotides of the isopentenyladenosine family
    • 2-isopentenyl) Adenosine and Its Nucleotide: Interaction with Purified tRNAs and with Bases, Nucleosides and Nucleotides of the Isopentenyladenosine Family, Nucleic Acids Res. 5, 3439-3455.
    • (1978) Nucleic Acids Res. , vol.5 , pp. 3439-3455
    • Milstone, D.S.1    Vold, B.S.2    Glitz, D.G.3    Shutt, N.4
  • 8
    • 0017837485 scopus 로고
    • 5′-AMP is a direct precursor of cytokinin in Dictyostelium discoideum
    • Taya, Y., Tanaka, Y., and Nishimura, S. (1978) 5′-AMP Is a Direct Precursor of Cytokinin in Dictyostelium discoideum, Nature 271, 545-547.
    • (1978) Nature , vol.271 , pp. 545-547
    • Taya, Y.1    Tanaka, Y.2    Nishimura, S.3
  • 9
    • 0000676652 scopus 로고
    • The prenyl transfer reaction: Enzymic and mechanistic studies on the 1′-4 coupling reaction in the terpene biosynthetic pathway
    • Poulter, C.D., and Rilling, H.C. (1978) The Prenyl Transfer Reaction: Enzymic and Mechanistic Studies on the 1′-4 Coupling Reaction in the Terpene Biosynthetic Pathway, Acc. Chem. Res. 11, 307-313.
    • (1978) Acc. Chem. Res. , vol.11 , pp. 307-313
    • Poulter, C.D.1    Rilling, H.C.2
  • 10
    • 0024686637 scopus 로고
    • Geranyl pyrophosphate synthase: Characterization of the enzyme and evidence that this chain-length-specific prenyltransferase is associated with monoterpene biosynthesis in sage (Salvia officinalis)
    • Croteau, R., and Purkett, P.T. (1989) Geranyl Pyrophosphate Synthase: Characterization of the Enzyme and Evidence That This Chain-Length-Specific Prenyltransferase Is Associated with Monoterpene Biosynthesis in Sage (Salvia officinalis), Arch. Biochem. Biophys. 271, 524-535.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 524-535
    • Croteau, R.1    Purkett, P.T.2
  • 11
    • 0015919475 scopus 로고
    • Squalene synthetase. 3. Mechanism of the reaction
    • Beytia, E., Qureshi, A.A., and Porter, J.W. (1973) Squalene Synthetase. 3. Mechanism of the Reaction, J. Biol. Chem. 248, 1856-1867.
    • (1973) J. Biol. Chem. , vol.248 , pp. 1856-1867
    • Beytia, E.1    Qureshi, A.A.2    Porter, J.W.3
  • 12
    • 0022109072 scopus 로고
    • Isoprenoid enzyme systems of silkworm. II. Formation of the juvenile hormone skeletons by farnesyl pyrophosphate synthetase II
    • Tokyo
    • Koyama, T., Matsubara, M., and Ogura, K. (1985) Isoprenoid Enzyme Systems of Silkworm. II. Formation of the Juvenile Hormone Skeletons by Farnesyl Pyrophosphate Synthetase II, J. Biochem. 98 (Tokyo), 457-463.
    • (1985) J. Biochem. , vol.98 , pp. 457-463
    • Koyama, T.1    Matsubara, M.2    Ogura, K.3
  • 13
    • 0000099415 scopus 로고
    • Purification of geranylgeranyl pyrophosphate synthetase from Micrococcus lysodeikticus
    • Kandutsch, A.A., Paulus, H., Levin, E., and Bloch, K. (1964) Purification of Geranylgeranyl Pyrophosphate Synthetase from Micrococcus lysodeikticus, J. Biol. Chem. 239, 2507-2515.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2507-2515
    • Kandutsch, A.A.1    Paulus, H.2    Levin, E.3    Bloch, K.4
  • 14
    • 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., and Brown, M.S. (1990) Inhibition of Purified p21ras Farnesyl:Protein Transferase by Cys-AAX Tetrapeptides, Cell 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
  • 15
    • 0026806554 scopus 로고
    • Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements
    • Moomaw, J.F., and Casey, P.J. (1992) Mammalian Protein Geranylgeranyltransferase. Subunit Composition and Metal Requirements, J. Biol. Chem. 267, 17438-17443.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17438-17443
    • Moomaw, J.F.1    Casey, P.J.2
  • 16
    • 0027416643 scopus 로고
    • Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex
    • Yokoyama, K., and Gelb, M.H. (1993) Purification of a Mammalian Protein Geranylgeranyltransferase. Formation and Catalytic Properties of an Enzyme-Geranylgeranyl Pyrophosphate Complex, J. Biol. Chem. 268, 4055-4060.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4055-4060
    • Yokoyama, K.1    Gelb, M.H.2
  • 17
    • 0027298707 scopus 로고
    • cDNA cloning and expression of the alpha and beta subunits of rat rab geranylgeranyl transferase
    • Armstrong, S.A., Seabra, M.C., Sudhof, T.C., Goldstein, J.L., and Brown, M.S. (1993) cDNA Cloning and Expression of the Alpha and Beta Subunits of Rat Rab Geranylgeranyl Transferase, J. Biol. Chem. 268, 12221-12229.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12221-12229
    • Armstrong, S.A.1    Seabra, M.C.2    Sudhof, T.C.3    Goldstein, J.L.4    Brown, M.S.5
  • 18
    • 0034672694 scopus 로고    scopus 로고
    • Isoprenyl diphosphate synthases
    • Wang, K.C., and Ohnuma, S. (2000) Isoprenyl Diphosphate Synthases, Biochim. Biophys. Acta 1529, 33-48.
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 33-48
    • Wang, K.C.1    Ohnuma, S.2
  • 19
    • 0027433040 scopus 로고
    • Biosynthesis of the side chain of ubiquinone:trans-prenyltransferase in rat liver microsomes
    • Teclebrhan, H., Olsson, J., Swiezewska, E., and Dallner, G. (1993) Biosynthesis of the Side Chain of Ubiquinone: trans-Prenyltransferase in Rat Liver Microsomes, J. Biol. Chem. 268, 23081-23086.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23081-23086
    • Teclebrhan, H.1    Olsson, J.2    Swiezewska, E.3    Dallner, G.4
  • 20
    • 0025793572 scopus 로고
    • Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver
    • Matsuoka, S., Sagami, H., Kurisaki, A., and Ogura, K. (1991) Variable Product Specificity of Microsomal Dehydrodolichyl Diphosphate Synthase from Rat Liver, J. Biol. Chem. 266, 3464-3468.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3464-3468
    • Matsuoka, S.1    Sagami, H.2    Kurisaki, A.3    Ogura, K.4
  • 21
    • 0020807234 scopus 로고
    • Long-chain betulaprenol-type polyprenols from the leaves of Ginkgo biloba
    • Ibata, K., Mizuno, M., Takigawa, T., and Tanaka, Y. (1983) Long-Chain Betulaprenol-Type Polyprenols from the Leaves of Ginkgo biloba, Biochem. J. 213, 305-311.
    • (1983) Biochem. J. , vol.213 , pp. 305-311
    • Ibata, K.1    Mizuno, M.2    Takigawa, T.3    Tanaka, Y.4
  • 22
    • 0025696050 scopus 로고
    • Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli
    • Fujisaki, S., Hara, H., Nishimura, Y., Horiuchi, K., and Nishino, T. (1990) Cloning and Nucleotide Sequence of the ispA Gene Responsible for Farnesyl Diphosphate Synthase Activity in Escherichia coli, J. Biochem. (Tokyo) 108, 995-1000.
    • (1990) J. Biochem. (Tokyo) , vol.108 , pp. 995-1000
    • Fujisaki, S.1    Hara, H.2    Nishimura, Y.3    Horiuchi, K.4    Nishino, T.5
  • 23
    • 0345313624 scopus 로고    scopus 로고
    • Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: Cloning, expression, and characterization of the essential uppS gene
    • Apfel, C.M., Takacs, B., Fountoulakis, M., Stieger, M., and Keck, W. (1999) Use of Genomics to Identify Bacterial Undecaprenyl Pyrophosphate Synthetase: Cloning, Expression, and Characterization of the Essential uppS Gene, J. Bacteriol. 181, 483-492.
    • (1999) J. Bacteriol. , vol.181 , pp. 483-492
    • Apfel, C.M.1    Takacs, B.2    Fountoulakis, M.3    Stieger, M.4    Keck, W.5
  • 25
    • 0026618026 scopus 로고
    • Identification of a cDNA for the plastid-located geranylgeranyl pyrophosphate synthase from Capsicum annuum: Correlative increase in enzyme activity and transcript level during fruit ripening
    • Kuntz, M., Romer, S., Suire, C., Hugueney, P., Weil, J.H., Schantz, R., and Camara, B. (1992) Identification of a cDNA for the Plastid-Located Geranylgeranyl Pyrophosphate Synthase from Capsicum annuum: Correlative Increase in Enzyme Activity and Transcript Level During Fruit Ripening, Plant J. 2, 25-34.
    • (1992) Plant J. , vol.2 , pp. 25-34
    • Kuntz, M.1    Romer, S.2    Suire, C.3    Hugueney, P.4    Weil, J.H.5    Schantz, R.6    Camara, B.7
  • 26
    • 0030696041 scopus 로고    scopus 로고
    • Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol
    • Sprenger, G.A., Schorken, U., Wiegert, T., Grolle, S., de Graaf, A.A., Taylor, S.V., Begley, T.P., Bringer-Meyer, S., and Sahm, H. (1997) Identification of a Thiamin-Dependent Synthase in Escherichia coli Required for the Formation of the 1-Deoxy-D-xylulose 5-phosphate Precursor to Isoprenoids, Thiamin, and Pyridoxol, Proc. Nat. Acad. Sci. USA 94, 12857-12862.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 12857-12862
    • Sprenger, G.A.1    Schorken, U.2    Wiegert, T.3    Grolle, S.4    De Graaf, A.A.5    Taylor, S.V.6    Begley, T.P.7    Bringer-Meyer, S.8    Sahm, H.9
  • 27
    • 0343614184 scopus 로고    scopus 로고
    • A family of transketolases that directs isoprenoid biosynthesis via a mevalonate-independent pathway
    • Lange, B.M., Wildung, M.R., McCaskill, D., and Croteau, R. (1998) A Family of Transketolases That Directs Isoprenoid Biosynthesis via a Mevalonate-Independent Pathway, Proc. Nat. Acad. Sci. USA 95, 2100-2104.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 2100-2104
    • Lange, B.M.1    Wildung, M.R.2    McCaskill, D.3    Croteau, R.4
  • 28
    • 0032170425 scopus 로고    scopus 로고
    • The deoxyxylulose phosphate pathway of terpenoid biosynthesis in plants and microorganisms
    • Eisenreich, W., Schwarz, M., Cartayrade, A., Arigoni, D., Zenk, M.H., and Bacher, A. (1998) The Deoxyxylulose Phosphate Pathway of Terpenoid Biosynthesis in Plants and Microorganisms, Chem. Biol. 5, R221-R233.
    • (1998) Chem. Biol. , vol.5
    • Eisenreich, W.1    Schwarz, M.2    Cartayrade, A.3    Arigoni, D.4    Zenk, M.H.5    Bacher, A.6
  • 29
    • 0024061058 scopus 로고
    • Prokaryotic hopanoids: The biosynthesis of the bacteriohopane skeleton. Formation of isoprenic units from two distinct acetate pools and a novel type of carbon/carbon linkage between a triterpene and D-ribose
    • Flesch, G., and Rohmer, M. (1988) Prokaryotic Hopanoids: The Biosynthesis of the Bacteriohopane Skeleton. Formation of Isoprenic Units from Two Distinct Acetate Pools and a Novel Type of Carbon/Carbon Linkage Between a Triterpene and D-Ribose, Eur. J. Biochem. 175, 405-411.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 405-411
    • Flesch, G.1    Rohmer, M.2
  • 30
    • 0033598845 scopus 로고    scopus 로고
    • Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: Isopentenyl monophosphate kinase catalyzes the terminal enzymatic step
    • Lange, B.M., and Croteau, R. (1999) Isopentenyl Diphosphate Biosynthesis via a Mevalonate-Independent Pathway: Isopentenyl Monophosphate Kinase Catalyzes the Terminal Enzymatic Step, Proc. Nat. Acad. Sci. USA 96, 13714-13719.
    • (1999) Proc. Nat. Acad. Sci. USA , vol.96 , pp. 13714-13719
    • Lange, B.M.1    Croteau, R.2
  • 31
    • 0031474261 scopus 로고    scopus 로고
    • Two independent biochemical pathways for isopentenyl diphosphate and isoprenoid biosynthesis in higher plants
    • Lichtenthaler, H.K., Rohmer, M., and Schwender, J. (1997) Two Independent Biochemical Pathways for Isopentenyl Diphosphate and Isoprenoid Biosynthesis in Higher Plants, Physiol. Plant. 101, 643-652.
    • (1997) Physiol. Plant. , vol.101 , pp. 643-652
    • Lichtenthaler, H.K.1    Rohmer, M.2    Schwender, J.3
  • 32
    • 0034700150 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes
    • Lange, B.M., Rujan, T., Martin, W., and Croteau, R. (2000) Isoprenoid Biosynthesis: The Evolution of Two Ancient and Distinct Pathways Across Genomes, Proc. Nat. Acad. Sci. USA 97, 13172-13177.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 13172-13177
    • Lange, B.M.1    Rujan, T.2    Martin, W.3    Croteau, R.4
  • 33
    • 0033859551 scopus 로고    scopus 로고
    • The role of lateral gene transfer in the evolution of isoprenoid biosynthesis pathways
    • Boucher, Y., and Doolittle, W.F. (2000) The Role of Lateral Gene Transfer in the Evolution of Isoprenoid Biosynthesis Pathways, Mol. Microbiol. 37, 703-716.
    • (2000) Mol. Microbiol. , vol.37 , pp. 703-716
    • Boucher, Y.1    Doolittle, W.F.2
  • 34
    • 0024730975 scopus 로고
    • Prokaryotic triterpenoids. A novel hopanoid from the ethanol-producing bacterium zymomonas mobilis
    • Flesch, G., and Rohmer, M. (1989) Prokaryotic Triterpenoids. A Novel Hopanoid from the Ethanol-Producing Bacterium Zymomonas mobilis, Biochem. J. 262, 673-675.
    • (1989) Biochem. J. , vol.262 , pp. 673-675
    • Flesch, G.1    Rohmer, M.2
  • 35
    • 0027368126 scopus 로고
    • Isoprenoid biosynthesis in bacteria: A novel pathway for the early steps leading to isopentenyl diphosphate
    • Rohmer, M., Knani, M., Simonin, P., Sutter, B., and Sahm, H. (1993) Isoprenoid Biosynthesis in Bacteria: A Novel Pathway for the Early Steps Leading to Isopentenyl Diphosphate, Biochem. J. 295, 517-524.
    • (1993) Biochem. J. , vol.295 , pp. 517-524
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 36
    • 0000725115 scopus 로고    scopus 로고
    • Distribution of mevalonate and glyceraldehyde 3-phosphate/pyruvate routes for isoprenoid biosynthesis in some gram-negative bacteria and mycobacteria
    • Putra, S.R., Disch, A., Bravo, J.M., and Rohmer, M. (1998) Distribution of Mevalonate and Glyceraldehyde 3-Phosphate/Pyruvate Routes for Isoprenoid Biosynthesis in Some Gram-Negative Bacteria and Mycobacteria, FEMS Microbiol. Lett. 164, 169-175.
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 169-175
    • Putra, S.R.1    Disch, A.2    Bravo, J.M.3    Rohmer, M.4
  • 37
    • 0030850424 scopus 로고    scopus 로고
    • Biosynthesis of the labdane diterpene marrubiin in Marrubium vulgare via a non-mevalonate pathway
    • Knöss, W., Reuter, B., and Zapp, J. (1997) Biosynthesis of the Labdane Diterpene Marrubiin in Marrubium vulgare via a Non-mevalonate Pathway, Biochem. J. 326, 449-454.
    • (1997) Biochem. J. , vol.326 , pp. 449-454
    • Knöss, W.1    Reuter, B.2    Zapp, J.3
  • 38
    • 0029938615 scopus 로고    scopus 로고
    • Biosynthesis of isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a novel pyruvate/glyceraldehyde 3-phosphate non-mevalonate pathway in the green alga Scenedesmus obliquus
    • Schwender, J., Seemann, M., Lichtenthaler, H.K., and Rohmer, M. (1996) Biosynthesis of Isoprenoids (carotenoids, sterols, prenyl side-chains of chlorophylls and plastoquinone) via a Novel Pyruvate/Glyceraldehyde 3-Phosphate Non-mevalonate Pathway in the Green Alga Scenedesmus obliquus, Biochem. J. 316, 73-80.
    • (1996) Biochem. J. , vol.316 , pp. 73-80
    • Schwender, J.1    Seemann, M.2    Lichtenthaler, H.K.3    Rohmer, M.4
  • 39
    • 0031731697 scopus 로고    scopus 로고
    • On the absence of the glyceraldehyde 3-phosphate/pyruvate pathway for isoprenoid biosynthesis in fungi and yeasts
    • Disch, A., and Rohmer, M. (1998) On the Absence of the Glyceraldehyde 3-Phosphate/Pyruvate Pathway for Isoprenoid Biosynthesis in Fungi and Yeasts, FEMS Microbiol. Lett. 168, 201-208.
    • (1998) FEMS Microbiol. Lett. , vol.168 , pp. 201-208
    • Disch, A.1    Rohmer, M.2
  • 40
    • 0036676584 scopus 로고    scopus 로고
    • Strategies for transgenic manipulation of monoterpene biosynthesis in plants
    • Mahmoud, S.S., and Croteau, R.B. (2002) Strategies for Transgenic Manipulation of Monoterpene Biosynthesis in Plants, Trends Plant Sci. 7, 366-373.
    • (2002) Trends Plant Sci. , vol.7 , pp. 366-373
    • Mahmoud, S.S.1    Croteau, R.B.2
  • 43
    • 0032980875 scopus 로고    scopus 로고
    • Prevention and therapy of cancer by dietary monoterpenes
    • Crowell, P.L. (1999) Prevention and Therapy of Cancer by Dietary Monoterpenes, J. Nutr. 129, 775S-778S.
    • (1999) J. Nutr. , vol.129
    • Crowell, P.L.1
  • 44
    • 0028229474 scopus 로고
    • Limonene chemoprevention of mammary carcinoma induction following direct in situ transfer of v-Ha-ras
    • Gould, M.N., Moore, C.J., Zhang, R., Wang, B., Kennan, W.S., and Haag, J.D. (1994) Limonene Chemoprevention of Mammary Carcinoma Induction Following Direct in situ Transfer of v-Ha-ras, Cancer Res. 54, 3540-3543.
    • (1994) Cancer Res. , vol.54 , pp. 3540-3543
    • Gould, M.N.1    Moore, C.J.2    Zhang, R.3    Wang, B.4    Kennan, W.S.5    Haag, J.D.6
  • 46
    • 0027965512 scopus 로고
    • Mammary carcinoma regression induced by perillyl alcohol, a hydroxylated analog of limonene
    • Haag, J.D., and Gould, M.N. (1994) Mammary Carcinoma Regression Induced by Perillyl Alcohol, a Hydroxylated Analog of Limonene, Cancer Chemother. Pharmacol. 34, 477-483.
    • (1994) Cancer Chemother. Pharmacol. , vol.34 , pp. 477-483
    • Haag, J.D.1    Gould, M.N.2
  • 47
  • 48
    • 0141791063 scopus 로고    scopus 로고
    • Perillyl alcohol and perillaldehyde induced cell cycle arrest and cell death in BroTo and A549 cells cultured in vitro
    • Elegbede, J.A., Flores, R., and Wang, R.C. (2003) Perillyl Alcohol and Perillaldehyde Induced Cell Cycle Arrest and Cell Death in BroTo and A549 Cells Cultured in vitro, Life Sci. 73, 2831-2840.
    • (2003) Life Sci. , vol.73 , pp. 2831-2840
    • Elegbede, J.A.1    Flores, R.2    Wang, R.C.3
  • 50
    • 0033984370 scopus 로고    scopus 로고
    • Perillyl alcohol, an inhibitor of geranylgeranyl transferase, induces apoptosis of immortalized human vascular smooth muscle cells in vitro
    • Unlu, S., Mason, C.D., Schachter, M., and Hughes, A.D. (2000) Perillyl Alcohol, an Inhibitor of Geranylgeranyl Transferase, Induces Apoptosis of Immortalized Human Vascular Smooth Muscle Cells in vitro, J. Cardiovasc. Pharmacol. 35, 341-344.
    • (2000) J. Cardiovasc. Pharmacol. , vol.35 , pp. 341-344
    • Unlu, S.1    Mason, C.D.2    Schachter, M.3    Hughes, A.D.4
  • 51
    • 0032827382 scopus 로고    scopus 로고
    • Perillyl alcohol selectively induces G0/G1 arrest and apoptosis in Bcr/Abl-transformed myeloid cell lines
    • Sahin, M.B., Perman, S.M., Jenkins, G., and Clark, S.S. (1999) Perillyl Alcohol Selectively Induces G0/G1 Arrest and Apoptosis in Bcr/Abl-Transformed Myeloid Cell Lines, Leukemia. 13, 1581-1591.
    • (1999) Leukemia , vol.13 , pp. 1581-1591
    • Sahin, M.B.1    Perman, S.M.2    Jenkins, G.3    Clark, S.S.4
  • 53
    • 0031834303 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of D-limonene in patients with advanced cancer
    • Cancer Research Campaign Phase I/II Clinical Trials Committee
    • Vigushin, D.M., Poon, G.K., Boddy, A., English, J., Halbert, G.W., Pagonis, C., Jarman, M., and Coombes, R.C. (1998) Phase I and Pharmacokinetic Study of D-Limonene in Patients with Advanced Cancer. Cancer Research Campaign Phase I/II Clinical Trials Committee, Cancer Chemother. Pharmacol. 42, 111-117.
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , pp. 111-117
    • Vigushin, D.M.1    Poon, G.K.2    Boddy, A.3    English, J.4    Halbert, G.W.5    Pagonis, C.6    Jarman, M.7    Coombes, R.C.8
  • 58
    • 0025952954 scopus 로고
    • Selective inhibition of isoprenylation of 21-26 kDa proteins by the anticarcinogen D-limonene and its metabolites
    • Crowell, P.L., Chang, R.R., Ren, Z.B., Elson, C.E., and Gould, M.N. (1991) Selective Inhibition of Isoprenylation of 21-26 kDa Proteins by the Anticarcinogen D-Limonene and Its Metabolites, J. Biol. Chem. 266, 17679-17685.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17679-17685
    • Crowell, P.L.1    Chang, R.R.2    Ren, Z.B.3    Elson, C.E.4    Gould, M.N.5
  • 59
    • 0029125753 scopus 로고
    • Differential effects of monoterpenes and lovastatin on RAS processing
    • Hohl, R.J., and Lewis, K. (1995) Differential Effects of Monoterpenes and Lovastatin on RAS Processing, J. Biol. Chem. 270, 17508-17512.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17508-17512
    • Hohl, R.J.1    Lewis, K.2
  • 60
    • 0142074249 scopus 로고    scopus 로고
    • Monoterpene regulation of Ras and Ras-related protein expression
    • Holstein, S.A., and Hohl, R.J. (2003) Monoterpene Regulation of Ras and Ras-Related Protein Expression, J. Lipid Res. 44, 1209-1215.
    • (2003) J. Lipid Res. , vol.44 , pp. 1209-1215
    • Holstein, S.A.1    Hohl, R.J.2
  • 62
    • 0037252940 scopus 로고    scopus 로고
    • New terpene hydrocarbons from the alligatoridae (Crocodylia, Reptilia)
    • Schulz, S., Kruckert, K., and Weldon, P.J. (2003) New Terpene Hydrocarbons from the Alligatoridae (Crocodylia, Reptilia), J. Nat. Prod. 66, 34-38.
    • (2003) J. Nat. Prod. , vol.66 , pp. 34-38
    • Schulz, S.1    Kruckert, K.2    Weldon, P.J.3
  • 63
    • 0025064030 scopus 로고
    • Chemistry of male dominance in the house mouse, Mus domesticus
    • Novotny, M., Harvey, S., and Jemiolo, B. (1990) Chemistry of Male Dominance in the House Mouse, Mus domesticus, Experientia 46, 109-113.
    • (1990) Experientia , vol.46 , pp. 109-113
    • Novotny, M.1    Harvey, S.2    Jemiolo, B.3
  • 64
    • 0036756619 scopus 로고    scopus 로고
    • Sex attractant pheromone of the red-shouldered stink bug Thyanta pallidovirens: A pheromone blend with multiple redundant components
    • McBrien, H.L., Millar, J.G., Rice, R.E., McElfresh, J.S., Cullen, E., and Zalom, F.G. (2002) Sex Attractant Pheromone of the Red-Shouldered Stink Bug Thyanta pallidovirens: A Pheromone Blend with Multiple Redundant Components, J. Chem. Ecol. 28, 1797-1818.
    • (2002) J. Chem. Ecol. , vol.28 , pp. 1797-1818
    • McBrien, H.L.1    Millar, J.G.2    Rice, R.E.3    McElfresh, J.S.4    Cullen, E.5    Zalom, F.G.6
  • 65
    • 0026827425 scopus 로고
    • Trans-beta-farnesene as a feeding stimulant for the sand fly Lutzomyia longipalpis (Diptera: Psychodidae)
    • Tesh, R.B., Guzman, H., and Wilson, M.L. (1992) Trans-Beta-Farnesene as a Feeding Stimulant for the Sand Fly Lutzomyia longipalpis (Diptera: Psychodidae), J. Med. Entomol. 29, 226-231.
    • (1992) J. Med. Entomol. , vol.29 , pp. 226-231
    • Tesh, R.B.1    Guzman, H.2    Wilson, M.L.3
  • 66
    • 0037357928 scopus 로고    scopus 로고
    • Interspecific variation in terpenoid composition of defensive secretions of European Reticulitermes termites
    • Quintana, A., Reinhard, J., Faure, R., Uva, P., Bagnères, A.G., Massiot, G., and Clément, J.L. (2003) Interspecific Variation in Terpenoid Composition of Defensive Secretions of European Reticulitermes Termites, J. Chem. Ecol. 29, 639-652.
    • (2003) J. Chem. Ecol. , vol.29 , pp. 639-652
    • Quintana, A.1    Reinhard, J.2    Faure, R.3    Uva, P.4    Bagnères, A.G.5    Massiot, G.6    Clément, J.L.7
  • 67
    • 0034840417 scopus 로고    scopus 로고
    • Conjugated triene oxidation products of α-farnesene induce symptoms of superficial scald on stored apples
    • Rowan, D.D., Hunt, M.B., Fielder, S., Norris, J., and Sherburn, M.S. (2001) Conjugated Triene Oxidation Products of α-Farnesene Induce Symptoms of Superficial Scald on Stored Apples, J. Agric. Food. Chem. 49, 2780-2787.
    • (2001) J. Agric. Food. Chem. , vol.49 , pp. 2780-2787
    • Rowan, D.D.1    Hunt, M.B.2    Fielder, S.3    Norris, J.4    Sherburn, M.S.5
  • 68
    • 0036009884 scopus 로고    scopus 로고
    • Structure-activity relationships of seco-Prezizaane terpenoids in γ-aminobutyric acid receptors of houseflies and rats
    • Kuriyama, T., Schmidt, T.J., Okuyama, E., and Ozoe, Y. (2002) Structure-Activity Relationships of seco-Prezizaane Terpenoids in γ-Aminobutyric Acid Receptors of Houseflies and Rats, Bioorg. Med. Chem. 10, 1873-1881.
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 1873-1881
    • Kuriyama, T.1    Schmidt, T.J.2    Okuyama, E.3    Ozoe, Y.4
  • 69
    • 0033760941 scopus 로고    scopus 로고
    • Inhibition of the transcription factor NF-κB by sesquiterpene lactones from Podachaenium eminens
    • Castro, V., Murillo, R., Klaas, C.A., Meunier, C., Mora, G., Pahl, H.L., and Merfort, I. (2000) Inhibition of the Transcription Factor NF-κB by Sesquiterpene Lactones from Podachaenium eminens, Planta Med. 66, 591-595.
    • (2000) Planta Med. , vol.66 , pp. 591-595
    • Castro, V.1    Murillo, R.2    Klaas, C.A.3    Meunier, C.4    Mora, G.5    Pahl, H.L.6    Merfort, I.7
  • 70
    • 0035015065 scopus 로고    scopus 로고
    • Immunosuppressive sesquiterpene alkaloids from Tripterygium wilfordii
    • Duan, H., Takaishi, Y., Momota, H., Ohmoto, Y., Taki, T., Jia, Y., and Li, D. (2001) Immunosuppressive Sesquiterpene Alkaloids from Tripterygium wilfordii, J. Nat. Prod. 64, 582-587.
    • (2001) J. Nat. Prod. , vol.64 , pp. 582-587
    • Duan, H.1    Takaishi, Y.2    Momota, H.3    Ohmoto, Y.4    Taki, T.5    Jia, Y.6    Li, D.7
  • 73
    • 0037058636 scopus 로고    scopus 로고
    • Costunolide, a sesquiterpene lactone from Saussurea lappa, Inhibits the VEGFR KDR/Flk-1 signaling pathway
    • Jeong, S.J., Itokawa, T., Shibuya, M., Kuwano, M., Ono, M., Higuchi, R., and Miyamoto, T. (2002) Costunolide, a Sesquiterpene Lactone from Saussurea lappa, Inhibits the VEGFR KDR/Flk-1 Signaling Pathway, Cancer Lett. 187, 129-133.
    • (2002) Cancer Lett. , vol.187 , pp. 129-133
    • Jeong, S.J.1    Itokawa, T.2    Shibuya, M.3    Kuwano, M.4    Ono, M.5    Higuchi, R.6    Miyamoto, T.7
  • 74
    • 0034062563 scopus 로고    scopus 로고
    • Sesquiterpene alkaloids from Tripterygium hypoglaucum and Tripterygium wilfordii: A new class of potent anti-HIV agents
    • Duan, H., Takaishi, Y., Imakura, Y., Jia, Y., Li, D., Cosentino, L.M., and Lee, K.H. (2000) Sesquiterpene Alkaloids from Tripterygium hypoglaucum and Tripterygium wilfordii: A New Class of Potent Anti-HIV Agents, J. Nat. Prod. 63, 357-361.
    • (2000) J. Nat. Prod. , vol.63 , pp. 357-361
    • Duan, H.1    Takaishi, Y.2    Imakura, Y.3    Jia, Y.4    Li, D.5    Cosentino, L.M.6    Lee, K.H.7
  • 75
    • 0000248311 scopus 로고
    • Studies on the biosynthesis of cholesterol: XIV. The origin of prenoic acids from allyl pyrophosphates in liver enzyme systems
    • Christophe, J., and Popják, G. (1961) Studies on the Biosynthesis of Cholesterol: XIV. The Origin of Prenoic Acids from Allyl Pyrophosphates in Liver Enzyme Systems, J. Lipid Res. 2, 244-257.
    • (1961) J. Lipid Res. , vol.2 , pp. 244-257
    • Christophe, J.1    Popják, G.2
  • 76
    • 0028035383 scopus 로고
    • Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes
    • Bansal, V.S., and Vaidya, S. (1994) Characterization of Two Distinct Allyl Pyrophosphatase Activities from Rat Liver Microsomes, Arch. Biochem. Biophys. 315, 393-399.
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 393-399
    • Bansal, V.S.1    Vaidya, S.2
  • 77
    • 0031239831 scopus 로고    scopus 로고
    • Farnesol as a regulator of HMG-CoA reductase degradation: Characterization and Role of farnesyl pyrophosphatase
    • Meigs, T.E., and Simoni, R.D. (1997) Farnesol as a Regulator of HMG-CoA Reductase Degradation: Characterization and Role of Farnesyl Pyrophosphatase, Arch. Biochem. Biophys. 345, 1-9.
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 1-9
    • Meigs, T.E.1    Simoni, R.D.2
  • 78
    • 0000021535 scopus 로고
    • Stereochemical studies of botryococcene biosynthesis: Analogies between 1′-1 and 1′-3 condensations in the isoprenoid pathway
    • Huang, Z., and Poulter, C.D. (1989) Stereochemical Studies of Botryococcene Biosynthesis: Analogies Between 1′-1 and 1′-3 Condensations in the Isoprenoid Pathway, J. Am. Chem. Soc. 111, 2713-2715.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 2713-2715
    • Huang, Z.1    Poulter, C.D.2
  • 79
    • 0029020395 scopus 로고
    • Farnesol is utilized for protein isoprenylation and the biosynthesis of cholesterol in mammalian cells
    • Crick, D.C., Andres, D.A., and Waechter, C.J. (1995) Farnesol Is Utilized for Protein Isoprenylation and the Biosynthesis of Cholesterol in Mammalian Cells, Biochem. Biophys. Res. Commun. 211, 590-599.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 590-599
    • Crick, D.C.1    Andres, D.A.2    Waechter, C.J.3
  • 80
    • 0028991308 scopus 로고
    • 3H]farnesol to cholesterol and cholesterogenic intermediates in the living rat eye
    • 3H]Farnesol to Cholesterol and Cholesterogenic Intermediates in the Living Rat Eye, Biochem. Biophys. Res. Commun. 210, 695-702.
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 695-702
    • Fliesler, S.J.1    Keller, R.K.2
  • 81
    • 0031584090 scopus 로고    scopus 로고
    • Metabolism of farnesol: Phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions
    • Westfall, D., Aboushadi, N., Shackelford, J.E., and Krisans, S.K. (1997) Metabolism of Farnesol: Phosphorylation of Farnesol by Rat Liver Microsomal and Peroxisomal Fractions, Biochem. Biophys. Res. Commun. 230, 562-568.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 562-568
    • Westfall, D.1    Aboushadi, N.2    Shackelford, J.E.3    Krisans, S.K.4
  • 82
    • 0030052970 scopus 로고    scopus 로고
    • Evidence for farnesol-mediated isoprenoid synthesis regulation in a halophilic archaeon, Haloferax volcanii
    • Tachibana, A., Tanaka, T., Taniguchi, M., and Oi, S. (1996) Evidence for Farnesol-Mediated Isoprenoid Synthesis Regulation in a Halophilic Archaeon, Haloferax volcanii, FEBS Lett. 379, 43-46.
    • (1996) FEBS Lett. , vol.379 , pp. 43-46
    • Tachibana, A.1    Tanaka, T.2    Taniguchi, M.3    Oi, S.4
  • 83
    • 0032524373 scopus 로고    scopus 로고
    • Phosphorylation of farnesol in rat liver microsomes: Properties of farnesol kinase and farnesyl phosphate kinase
    • Bentinger, M., Grunler, J., Peterson, E., Swiezewska, E., and Dallner, G. (1998) Phosphorylation of Farnesol in Rat Liver Microsomes: Properties of Farnesol Kinase and Farnesyl Phosphate Kinase, Arch. Biochem. Biophys. 353, 191-198.
    • (1998) Arch. Biochem. Biophys. , vol.353 , pp. 191-198
    • Bentinger, M.1    Grunler, J.2    Peterson, E.3    Swiezewska, E.4    Dallner, G.5
  • 84
    • 0033539526 scopus 로고    scopus 로고
    • Farnesol is utilized for isoprenoid biosynthesis in plant cells via farnesyl pyrophosphate formed by successive monophosphorylation reactions
    • Thai, L., Rush, J.S., Maul, J.E., Devarenne, T., Rodgers, D.L., Chappell, J., and Waechter, C.J. (1999) Farnesol Is Utilized for Isoprenoid Biosynthesis in Plant Cells via Farnesyl Pyrophosphate Formed by Successive Monophosphorylation Reactions, Proc. Natl. Acad. Sci. USA 96, 13080-13085.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13080-13085
    • Thai, L.1    Rush, J.S.2    Maul, J.E.3    Devarenne, T.4    Rodgers, D.L.5    Chappell, J.6    Waechter, C.J.7
  • 85
    • 0034634593 scopus 로고    scopus 로고
    • Phosphorylation of geranyl and farnesyl pyrophosphates by Nm23 proteins/nucleoside diphosphate kinases
    • Wagner, P.D., and Vu, N.D. (2000) Phosphorylation of Geranyl and Farnesyl Pyrophosphates by Nm23 Proteins/Nucleoside Diphosphate Kinases, J. Biol. Chem. 275, 35570-35576.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35570-35576
    • Wagner, P.D.1    Vu, N.D.2
  • 86
    • 0023874006 scopus 로고
    • Isopentenoid synthesis in isolated embryonic drosophila cells. Farnesol catabolism and omega-oxidation
    • Gonzalez-Pacanowska, D., Arison, B., Havel, C.M., and Watson, J.A. (1988) Isopentenoid Synthesis in Isolated Embryonic Drosophila Cells. Farnesol Catabolism and Omega-Oxidation, J. Biol. Chem. 263, 1301-1306.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1301-1306
    • Gonzalez-Pacanowska, D.1    Arison, B.2    Havel, C.M.3    Watson, J.A.4
  • 87
    • 0021051936 scopus 로고
    • Metabolism of mevalonic acid in cell-free homogenates of bovine retinas. Formation of novel isoprenoid acids
    • Fliesler, S.J., and Schroepfer, G.J., Jr. (1983) Metabolism of Mevalonic Acid in Cell-Free Homogenates of Bovine Retinas. Formation of Novel Isoprenoid Acids, J. Biol. Chem. 258, 15062-15070.
    • (1983) J. Biol. Chem. , vol.258 , pp. 15062-15070
    • Fliesler, S.J.1    Schroepfer Jr., G.J.2
  • 88
    • 0025974055 scopus 로고
    • Human liver alcohol dehydrogenases catalyze the oxidation of the intermediary alcohols of the shunt pathway of mevalonate metabolism
    • Keung, W.M. (1991) Human Liver Alcohol Dehydrogenases Catalyze the Oxidation of the Intermediary Alcohols of the Shunt Pathway of Mevalonate Metabolism, Biochem. Biophys. Res. Commun. 174, 701-707.
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 701-707
    • Keung, W.M.1
  • 89
    • 0030801368 scopus 로고    scopus 로고
    • Isolation and characterization of a prenylcysteine lyase from bovine brain
    • Zhang, L., Tschantz, W.R., and Casey, P.J. (1997) Isolation and Characterization of a Prenylcysteine Lyase from Bovine Brain, J. Biol. Chem. 272, 23354-23359.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23354-23359
    • Zhang, L.1    Tschantz, W.R.2    Casey, P.J.3
  • 91
    • 0032127143 scopus 로고    scopus 로고
    • Massive production of farnesol-derived dicarboxylic acids in mice treated with the squalene synthase inhibitor zaragozic acid A
    • Vaidya, S., Bostedor, R., Kurtz, M.M., Bergstrom, J.D., and Bansal, V.S. (1998) Massive Production of Farnesol-Derived Dicarboxylic Acids in Mice Treated with the Squalene Synthase Inhibitor Zaragozic Acid A, Arch. Biochem. Biophys. 355, 84-92.
    • (1998) Arch. Biochem. Biophys. , vol.355 , pp. 84-92
    • Vaidya, S.1    Bostedor, R.2    Kurtz, M.M.3    Bergstrom, J.D.4    Bansal, V.S.5
  • 92
    • 0020989036 scopus 로고
    • Farnesol and farnesal dehydrogenase(s) in corpora allata of the tobacco hornworm moth, Manduca sexta
    • Baker, F.C., Mauchamp, B., Tsai, L.W., and Schooley, D.A. (1983) Farnesol and Farnesal Dehydrogenase(s) in Corpora Allata of the Tobacco Hornworm Moth, Manduca sexta, J. Lipid Res. 24, 1586-1594.
    • (1983) J. Lipid Res. , vol.24 , pp. 1586-1594
    • Baker, F.C.1    Mauchamp, B.2    Tsai, L.W.3    Schooley, D.A.4
  • 93
    • 0000812012 scopus 로고    scopus 로고
    • Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver
    • Keller, R.K., Zhao, Z., Chambers, C., and Ness, G.C. (1996) Farnesol Is Not the Nonsterol Regulator Mediating Degradation of HMG-CoA Reductase in Rat Liver, Arch. Biochem. Biophys. 328, 324-330.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 324-330
    • Keller, R.K.1    Zhao, Z.2    Chambers, C.3    Ness, G.C.4
  • 95
    • 0031260487 scopus 로고    scopus 로고
    • Determination of farnesyl pyrophosphate in dog and human plasma by high-performance liquid chromatography with fluorescence detection
    • Saisho, Y., Morimoto, A., and Umeda, T. (1997) Determination of Farnesyl Pyrophosphate in Dog and Human Plasma by High-Performance Liquid Chromatography with Fluorescence Detection, Anal. Biochem. 252, 89-95.
    • (1997) Anal. Biochem. , vol.252 , pp. 89-95
    • Saisho, Y.1    Morimoto, A.2    Umeda, T.3
  • 96
    • 0023678371 scopus 로고
    • Determination of isopentenyl diphosphate and farnesyl diphosphate in tissue samples with a comment on secondary regulation of polyisoprenoid biosynthesis
    • Bruenger, E., and Rilling, H.C. (1988) Determination of Isopentenyl Diphosphate and Farnesyl Diphosphate in Tissue Samples with a Comment on Secondary Regulation of Polyisoprenoid Biosynthesis, Anal. Biochem. 173, 321-327.
    • (1988) Anal. Biochem. , vol.173 , pp. 321-327
    • Bruenger, E.1    Rilling, H.C.2
  • 97
    • 0036290647 scopus 로고    scopus 로고
    • Farnesol as an inhibitor and substrate for rabbit liver microsomal P450 enzymes
    • Raner, G.M., Muir, A.Q., Lowry, C.W., and Davis, B.A. (2002) Farnesol as an Inhibitor and Substrate for Rabbit Liver Microsomal P450 Enzymes, Biochem. Biophys. Res. Commun. 293, 1-6.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 1-6
    • Raner, G.M.1    Muir, A.Q.2    Lowry, C.W.3    Davis, B.A.4
  • 98
    • 0019443302 scopus 로고
    • Enzymic synthesis of juvenile hormone in locust corpora allata: Evidence for a microsomal cytochrome P-450 linked methyl farnesoate epoxidase
    • Feyereisen, R., Pratt, G.E., and Hamnett, A.F. (1981) Enzymic Synthesis of Juvenile Hormone in Locust Corpora Allata: Evidence for a Microsomal Cytochrome P-450 Linked Methyl Farnesoate Epoxidase, Eur. J. Biochem. 118, 231-238.
    • (1981) Eur. J. Biochem. , vol.118 , pp. 231-238
    • Feyereisen, R.1    Pratt, G.E.2    Hamnett, A.F.3
  • 99
    • 0031042230 scopus 로고    scopus 로고
    • Substrate specificity for the epoxidation of terpenoids and active site topology of house fly cytochrome P450 6A1
    • Andersen, J.F., Walding, J.K., Evans, P.H., Bowers, W.S., and Feyereisen, R. (1997) Substrate Specificity for the Epoxidation of Terpenoids and Active Site Topology of House Fly Cytochrome P450 6A1, Chem. Res. Toxicol. 10, 156-164.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 156-164
    • Andersen, J.F.1    Walding, J.K.2    Evans, P.H.3    Bowers, W.S.4    Feyereisen, R.5
  • 102
    • 0014010249 scopus 로고
    • Feedback control of mevalonate synthesis by dietary cholesterol
    • Siperstein, M.D., and Fagan, V.M. (1966) Feedback Control of Mevalonate Synthesis by Dietary Cholesterol, J. Biol. Chem. 241, 602-609.
    • (1966) J. Biol. Chem. , vol.241 , pp. 602-609
    • Siperstein, M.D.1    Fagan, V.M.2
  • 103
    • 0017894322 scopus 로고
    • Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts incubated with compactin (ML-236B), a competitive inhibitor of the reductase
    • Brown, M.S., Faust, J.R., and Goldstein, J.L. (1978) Induction of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase Activity in Human Fibroblasts Incubated with Compactin (ML-236B), a Competitive Inhibitor of the Reductase, J. Biol. Chem. 253, 1121-1128.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1121-1128
    • Brown, M.S.1    Faust, J.R.2    Goldstein, J.L.3
  • 105
    • 0026627805 scopus 로고
    • Post-transcriptional regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by 24(S),25-oxidolanosterol
    • Panini, S.R., Delate, T.A., and Sinensky, M. (1992) Post-transcriptional Regulation of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase by 24(S),25-Oxidolanosterol, J. Biol. Chem. 267, 12647-12654.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12647-12654
    • Panini, S.R.1    Delate, T.A.2    Sinensky, M.3
  • 106
    • 0025816877 scopus 로고
    • Genetic distinction between sterol-mediated transcriptional and posttranscriptional control of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Dawson, P.A., Metherall, J.E., Ridgway, N.D., Brown, M.S., and Goldstein, J.L. (1991) Genetic Distinction Between Sterol-Mediated Transcriptional and Posttranscriptional Control of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase, J. Biol. Chem. 266, 9128-9134.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9128-9134
    • Dawson, P.A.1    Metherall, J.E.2    Ridgway, N.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 107
    • 0023902411 scopus 로고
    • Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme
    • Nakanishi, M., Goldstein, J.L., and Brown, M.S. (1988) Multivalent Control of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase. Mevalonate-Derived Product Inhibits Translation of mRNA and Accelerates Degradation of Enzyme, J. Biol. Chem. 263, 8929-8937.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8929-8937
    • Nakanishi, M.1    Goldstein, J.L.2    Brown, M.S.3
  • 108
    • 0026461126 scopus 로고
    • Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Roitelman, J., and Simoni, R.D. (1992) Distinct Sterol and Nonsterol Signals for the Regulated Degradation of 3-Hydroxy-3-methylglutaryl-CoA Reductase, J. Biol. Chem. 267, 25264-25273.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25264-25273
    • Roitelman, J.1    Simoni, R.D.2
  • 109
    • 0028157541 scopus 로고
    • Mevalonic acid-dependent degradation of 3-hydroxy-3-methylglutaryl- coenzyme A reductase in vivo and in vitro
    • Correll, C.C., and Edwards, P.A. (1994) Mevalonic Acid-Dependent Degradation of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase in vivo and in vitro, J. Biol. Chem. 269, 633-638.
    • (1994) J. Biol. Chem. , vol.269 , pp. 633-638
    • Correll, C.C.1    Edwards, P.A.2
  • 110
    • 0028307290 scopus 로고
    • Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Correll, C.C., Ng, L., and Edwards, P.A. (1994) Identification of Farnesol as the Non-sterol Derivative of Mevalonic Acid Required for the Accelerated Degradation of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase, J. Biol. Chem. 269, 17390-17393.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17390-17393
    • Correll, C.C.1    Ng, L.2    Edwards, P.A.3
  • 111
    • 0028285272 scopus 로고
    • Non-sterol compounds that regulate cholesterogenesis. Analogues of farnesyl pyrophosphate reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels
    • Bradfute, D.L., and Simoni, R.D. (1994) Non-sterol Compounds That Regulate Cholesterogenesis. Analogues of Farnesyl Pyrophosphate Reduce 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase Levels, J. Biol. Chem. 269, 6645-6650.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6645-6650
    • Bradfute, D.L.1    Simoni, R.D.2
  • 112
    • 0027288196 scopus 로고
    • Tocotrienols regulate cholesterol production in mammalian cells by post-transcriptional suppression of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Parker, R.A., Pearce, B.C., Clark, R.W., Gordon, D.A., and Wright, J.J. (1993) Tocotrienols Regulate Cholesterol Production in Mammalian Cells by Post-transcriptional Suppression of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase, J. Biol. Chem. 268, 11230-11238.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11230-11238
    • Parker, R.A.1    Pearce, B.C.2    Clark, R.W.3    Gordon, D.A.4    Wright, J.J.5
  • 113
    • 0033615648 scopus 로고    scopus 로고
    • A highly conserved signal controls degradation of 3-hydroxy-3- methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes
    • Gardner, R.G., and Hampton, R.Y. (1999) A Highly Conserved Signal Controls Degradation of 3-Hydroxy-3-methylglutaryl-Coenzyme A (HMG-CoA) Reductase in Eukaryotes, J. Biol. Chem. 274, 31671-31678.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31671-31678
    • Gardner, R.G.1    Hampton, R.Y.2
  • 114
    • 0346101770 scopus 로고    scopus 로고
    • Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and geranylgeraniol
    • Sever, N., Song, B.L., Yabe, D., Goldstein, J.L., Brown, M.S., and DeBose-Boyd, R.A. (2003) Insig-Dependent Ubiquitination and Degradation of Mammalian 3-Hydroxy-3-methylglutaryl-CoA Reductase Stimulated by Sterols and Geranylgeraniol, J. Biol. Chem. 278, 52479-52490.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52479-52490
    • Sever, N.1    Song, B.L.2    Yabe, D.3    Goldstein, J.L.4    Brown, M.S.5    DeBose-Boyd, R.A.6
  • 115
    • 0037229435 scopus 로고    scopus 로고
    • Plant-derived monoterpenes suppress hamster kidney cell 3-hydroxy-3-methylglutaryl coenzyme A reductase synthesis at the post-transcriptional level
    • Peffley, D.M., and Gayen, A.K. (2003) Plant-Derived Monoterpenes Suppress Hamster Kidney Cell 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase Synthesis at the Post-transcriptional Level, J. Nutr. 133, 38-44.
    • (2003) J. Nutr. , vol.133 , pp. 38-44
    • Peffley, D.M.1    Gayen, A.K.2
  • 116
    • 0037209307 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of de novo isoprenoid pheromone production in the scolytidae
    • Seybold, S.J., and Tittiger, C. (2003) Biochemistry and Molecular Biology of de novo Isoprenoid Pheromone Production in the Scolytidae, Annu. Rev. Entomol. 48, 425-453.
    • (2003) Annu. Rev. Entomol. , vol.48 , pp. 425-453
    • Seybold, S.J.1    Tittiger, C.2
  • 118
    • 0037474139 scopus 로고    scopus 로고
    • Structure and juvenile hormone-mediated regulation of the HMG-CoA reductase gene from the Jeffrey pine beetle, Dendroctonus jeffreyi
    • Tittiger, C., Barkawi, L.S., Bengoa, C.S., Blomquist, G.J., and Seybold, S.J. (2003) Structure and Juvenile Hormone-Mediated Regulation of the HMG-CoA Reductase Gene from the Jeffrey Pine Beetle, Dendroctonus jeffreyi, Mol. Cell. Endocrinol. 199, 11-21.
    • (2003) Mol. Cell. Endocrinol. , vol.199 , pp. 11-21
    • Tittiger, C.1    Barkawi, L.S.2    Bengoa, C.S.3    Blomquist, G.J.4    Seybold, S.J.5
  • 119
    • 0028289750 scopus 로고
    • Regulation of HMG-CoA reductase activity in plants
    • Stermer, B.A., Bianchini, G.M., and Korth, K.L. (1994) Regulation of HMG-CoA Reductase Activity in Plants, J. Lipid Res. 35, 1133-1140.
    • (1994) J. Lipid Res. , vol.35 , pp. 1133-1140
    • Stermer, B.A.1    Bianchini, G.M.2    Korth, K.L.3
  • 120
    • 0036740929 scopus 로고    scopus 로고
    • Inhibition of squalene synthase and squalene epoxidase in tobacco cells triggers an up-regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Wentzinger, L.F., Bach, T.J., and Hartmann, M.A. (2002) Inhibition of Squalene Synthase and Squalene Epoxidase in Tobacco Cells Triggers an Up-regulation of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase, Plant Physiol. 130, 334-346.
    • (2002) Plant Physiol. , vol.130 , pp. 334-346
    • Wentzinger, L.F.1    Bach, T.J.2    Hartmann, M.A.3
  • 121
    • 0033836968 scopus 로고    scopus 로고
    • Farnesol-induced cell death and stimulation of 3-hydroxy-3- methylglutaryl-coenzyme A reductase activity in tobacco cv bright yellow-2 cells
    • Hemmerlin, A., and Bach, T.J. (2000) Farnesol-Induced Cell Death and Stimulation of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase Activity in Tobacco cv Bright Yellow-2 Cells, Plant Physiol. 123, 1257-1268.
    • (2000) Plant Physiol. , vol.123 , pp. 1257-1268
    • Hemmerlin, A.1    Bach, T.J.2
  • 122
    • 0017055252 scopus 로고
    • ML-236A, ML-236B, and ML-236C, new inhibitors of cholesterogenesis produced by Penicillium citrinium
    • Endo, A., Kuroda, M., and Tsujita, Y. (1976) ML-236A, ML-236B, and ML-236C, New Inhibitors of Cholesterogenesis Produced by Penicillium citrinium, J. Antibiot. (Tokyo) 29, 1346-1348.
    • (1976) J. Antibiot. (Tokyo) , vol.29 , pp. 1346-1348
    • Endo, A.1    Kuroda, M.2    Tsujita, Y.3
  • 123
    • 0024316475 scopus 로고
    • Genetic and pharmacological suppression of oncogenic mutations in RAS genes of yeast and humans
    • Schafer, W.R., Kim, R., Sterne, R., Thorner, J., Kim, S.H., and Rine, J. (1989) Genetic and Pharmacological Suppression of Oncogenic Mutations in RAS Genes of Yeast and Humans, Science 245, 379-385.
    • (1989) Science , vol.245 , pp. 379-385
    • Schafer, W.R.1    Kim, R.2    Sterne, R.3    Thorner, J.4    Kim, S.H.5    Rine, J.6
  • 124
    • 0025217828 scopus 로고
    • Inhibition of isoprenoid biosynthesis and the post-translational modification of pro-p21
    • Leonard, S., Beck, L., and Sinensky, M. (1990) Inhibition of Isoprenoid Biosynthesis and the Post-translational Modification of pro-p21, J. Biol. Chem. 265, 5157-5160.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5157-5160
    • Leonard, S.1    Beck, L.2    Sinensky, M.3
  • 125
    • 0037155865 scopus 로고    scopus 로고
    • Consequences of mevalonate depletion. Differential transcriptional, translational, and post-translational up-regulation of Ras, Rap1a, RhoA, and RhoB
    • Holstein, S.A., Wohlford-Lenane, C.L., and Hohl, R.J. (2002) Consequences of Mevalonate Depletion. Differential Transcriptional, Translational, and Post-translational Up-regulation of Ras, Rap1a, RhoA, and RhoB, J. Biol. Chem. 277, 10678-10682.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10678-10682
    • Holstein, S.A.1    Wohlford-Lenane, C.L.2    Hohl, R.J.3
  • 127
    • 0029079141 scopus 로고
    • Control of RAS mRNA level by the mevalonate pathway
    • Dimster-Denk, D., Schafer, W.R., and Rine, J. (1995) Control of RAS mRNA Level by the Mevalonate Pathway, Mol. Biol. Cell. 6, 59-70.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 59-70
    • Dimster-Denk, D.1    Schafer, W.R.2    Rine, J.3
  • 128
    • 0037137175 scopus 로고    scopus 로고
    • Isoprenoids influence the expression of Ras and Ras-related proteins
    • Holstein, S.A., Wohlford-Lenane, C.L., and Hohl, R.J. (2002) Isoprenoids Influence the Expression of Ras and Ras-Related Proteins, Biochemistry 41, 13698-13704.
    • (2002) Biochemistry , vol.41 , pp. 13698-13704
    • Holstein, S.A.1    Wohlford-Lenane, C.L.2    Hohl, R.J.3
  • 129
    • 0344059127 scopus 로고    scopus 로고
    • Isoprenoid pyrophosphate analogues regulate expression of Ras-related proteins
    • Holstein, S.A., Wohlford-Lenane, C.L., Wiemer, D.F., and Hohl, R.J. (2003) Isoprenoid Pyrophosphate Analogues Regulate Expression of Ras-Related Proteins, Biochemistry 42, 4384-4391.
    • (2003) Biochemistry , vol.42 , pp. 4384-4391
    • Holstein, S.A.1    Wohlford-Lenane, C.L.2    Wiemer, D.F.3    Hohl, R.J.4
  • 131
    • 0033026760 scopus 로고    scopus 로고
    • Endogenous bile acids are ligands for the nuclear receptor FXR/BAR
    • Wang, H., Chen, J., Hollister, K., Sowers, L.C., and Forman, B.M. (1999) Endogenous Bile Acids Are Ligands for the Nuclear Receptor FXR/BAR, Mol. Cell. 3, 543-553.
    • (1999) Mol. Cell , vol.3 , pp. 543-553
    • Wang, H.1    Chen, J.2    Hollister, K.3    Sowers, L.C.4    Forman, B.M.5
  • 136
    • 0029044946 scopus 로고
    • Activation of mammalian retinoid X receptors by the insect growth regulator methoprene
    • Harmon, M.A., Boehm, M.F., Heyman, R.A., and Mangelsdorf, D.J. (1995) Activation of Mammalian Retinoid X Receptors by the Insect Growth Regulator Methoprene, Proc. Natl. Acad. Sci. USA 92, 6157-6160.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6157-6160
    • Harmon, M.A.1    Boehm, M.F.2    Heyman, R.A.3    Mangelsdorf, D.J.4
  • 138
    • 0033968452 scopus 로고    scopus 로고
    • Preferential induction of apoptosis of leukaemic cells by farnesol
    • Rioja, A., Pizzey, A.R., Marson, C.M., and Thomas, N.S. (2000) Preferential Induction of Apoptosis of Leukaemic Cells by Farnesol, FEBS. Lett. 467, 291-295.
    • (2000) FEBS. Lett. , vol.467 , pp. 291-295
    • Rioja, A.1    Pizzey, A.R.2    Marson, C.M.3    Thomas, N.S.4
  • 139
    • 0029143223 scopus 로고
    • Mechanism of farnesol cytotoxicity: Further evidence for the role of PKC-dependent signal transduction in farnesol-induced apoptotic cell death
    • Voziyan, P.A., Haug, J.S., and Melnykovych, G. (1995) Mechanism of Farnesol Cytotoxicity: Further Evidence for the Role of PKC-Dependent Signal Transduction in Farnesol-Induced Apoptotic Cell Death, Biochem. Biophys. Res. Commun. 212, 479-486.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 479-486
    • Voziyan, P.A.1    Haug, J.S.2    Melnykovych, G.3
  • 140
    • 0032518762 scopus 로고    scopus 로고
    • Dihydroheptaprenyl and dihydrodecaprenyl monophosphates induce apoptosis mediated by activation of caspase-3-like protease
    • Yasugi, E., Nakata, K., Yokoyama, Y., Kano, K., Dohi, T., and Oshima, M. (1998) Dihydroheptaprenyl and Dihydrodecaprenyl Monophosphates Induce Apoptosis Mediated by Activation of Caspase-3-like Protease, Biochim. Biophys. Acta 1389, 132-140.
    • (1998) Biochim. Biophys. Acta , vol.1389 , pp. 132-140
    • Yasugi, E.1    Nakata, K.2    Yokoyama, Y.3    Kano, K.4    Dohi, T.5    Oshima, M.6
  • 141
    • 0032476029 scopus 로고    scopus 로고
    • Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells
    • Miquel, K., Pradines, A., Terce, F., Selmi, S., and Favre, G. (1998) Competitive Inhibition of Choline Phosphotransferase by Geranylgeraniol and Farnesol Inhibits Phosphatidylcholine Synthesis and Induces Apoptosis in Human Lung Adenocarcinoma A549 Cells, J. Biol. Chem. 273, 26179-26186.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26179-26186
    • Miquel, K.1    Pradines, A.2    Terce, F.3    Selmi, S.4    Favre, G.5
  • 142
    • 0031056450 scopus 로고    scopus 로고
    • Inhibition of pancreatic cancer growth by the dietary isoprenoids farnesol and geraniol
    • Burke, Y.D., Stark, M.J., Roach, S.L., Sen, S.E., and Crowell, P.L. (1997) Inhibition of Pancreatic Cancer Growth by the Dietary Isoprenoids Farnesol and Geraniol, Lipids 32, 151-156.
    • (1997) Lipids , vol.32 , pp. 151-156
    • Burke, Y.D.1    Stark, M.J.2    Roach, S.L.3    Sen, S.E.4    Crowell, P.L.5
  • 143
    • 0031721764 scopus 로고    scopus 로고
    • Farnesol-induced generation of reactive oxygen species via indirect inhibition of the mitochondrial electron transport chain in the yeast Saccharomyces cerevisiae
    • Machida, K., Tanaka, T., Fujita, K., and Taniguchi, M. (1998) Farnesol-Induced Generation of Reactive Oxygen Species via Indirect Inhibition of the Mitochondrial Electron Transport Chain in the Yeast Saccharomyces cerevisiae, J. Bacteriol. 180, 4460-4465.
    • (1998) J. Bacteriol. , vol.180 , pp. 4460-4465
    • Machida, K.1    Tanaka, T.2    Fujita, K.3    Taniguchi, M.4
  • 144
    • 0027496247 scopus 로고
    • Farnesol inhibits phosphatidylcholine biosynthesis in cultured cells by decreasing cholinephosphotransferase activity
    • Voziyan, P.A., Goldner, C.M., and Melnykovych, G. (1993) Farnesol Inhibits Phosphatidylcholine Biosynthesis in Cultured Cells by Decreasing Cholinephosphotransferase Activity, Biochem. J. 295, 757-762.
    • (1993) Biochem. J. , vol.295 , pp. 757-762
    • Voziyan, P.A.1    Goldner, C.M.2    Melnykovych, G.3
  • 145
    • 0035816579 scopus 로고    scopus 로고
    • Uncoupling farnesol-induced apoptosis from its inhibition of phosphatidylcholine synthesis
    • Wright, M.M., Henneberry, A.L., Lagace, T.A., Ridgway, N.D., and McMaster, C.R. (2001) Uncoupling Farnesol-Induced Apoptosis from Its Inhibition of Phosphatidylcholine Synthesis, J. Biol. Chem. 276, 25254-25261.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25254-25261
    • Wright, M.M.1    Henneberry, A.L.2    Lagace, T.A.3    Ridgway, N.D.4    McMaster, C.R.5
  • 146
    • 0028832005 scopus 로고
    • Selective farnesol toxicity and translocation of protein kinase C in neoplastic HeLa-S3K and non-neoplastic CF-3 cells
    • Yazlovitskaya, E.M., and Melnykovych, G. (1995) Selective Farnesol Toxicity and Translocation of Protein Kinase C in Neoplastic HeLa-S3K and Non-neoplastic CF-3 Cells, Cancer Lett. 88, 179-183.
    • (1995) Cancer Lett. , vol.88 , pp. 179-183
    • Yazlovitskaya, E.M.1    Melnykovych, G.2
  • 147
    • 0032759103 scopus 로고    scopus 로고
    • Farnesol-induced generation of reactive oxygen species dependent on mitochondrial transmembrane potential hyperpolarization mediated by F(0)F(1)-ATPase in yeast
    • Machida, K., and Tanaka, T. (1999) Farnesol-Induced Generation of Reactive Oxygen Species Dependent on Mitochondrial Transmembrane Potential Hyperpolarization Mediated by F(0)F(1)-ATPase in Yeast, FEBS Lett. 462, 108-112.
    • (1999) FEBS Lett. , vol.462 , pp. 108-112
    • Machida, K.1    Tanaka, T.2
  • 148
    • 0034979081 scopus 로고    scopus 로고
    • A new dehydrogeranylgeraniol antioxidant from Saururus cernuus that inhibits intracellular reactive oxygen species (ROS)-catalyzed oxidation within HL-60 cells
    • Rajbhandari, I., Takamatsu, S., and Nagle, D.G. (2001) A New Dehydrogeranylgeraniol Antioxidant from Saururus cernuus That Inhibits Intracellular Reactive Oxygen Species (ROS)-Catalyzed Oxidation Within HL-60 Cells, J. Nat. Prod. 64, 693-695.
    • (2001) J. Nat. Prod. , vol.64 , pp. 693-695
    • Rajbhandari, I.1    Takamatsu, S.2    Nagle, D.G.3
  • 151
    • 0035836681 scopus 로고    scopus 로고
    • Purification and characterization of an autoregulatory substance capable of regulating the morphological transition in Candida albicans
    • Oh, K.B., Miyazawa, H., Naito, T., and Matsuoka, H. (2001) Purification and Characterization of an Autoregulatory Substance Capable of Regulating the Morphological Transition in Candida albicans, Proc. Natl. Acad. Sci. USA 98, 4664-4668.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4664-4668
    • Oh, K.B.1    Miyazawa, H.2    Naito, T.3    Matsuoka, H.4
  • 152
    • 0037170796 scopus 로고    scopus 로고
    • Evaluation of morphogenic regulatory activity of farnesoic acid and its derivatives against Candida albicans dimorphism
    • Kim, S., Kim, E., Shin, D.S., Kang, H., and Oh, K.B. (2002) Evaluation of Morphogenic Regulatory Activity of Farnesoic Acid and Its Derivatives Against Candida albicans Dimorphism, Bioorg. Med. Chem. Lett. 12, 895-898.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 895-898
    • Kim, S.1    Kim, E.2    Shin, D.S.3    Kang, H.4    Oh, K.B.5
  • 154
    • 0038650921 scopus 로고    scopus 로고
    • Farnesol biosynthesis in Candida albicans: Cellular response to sterol inhibition by Zaragozic acid B
    • Hornby, J.M., Kebaara, B.W., and Nickerson, K.W. (2003) Farnesol Biosynthesis in Candida albicans: Cellular Response to Sterol Inhibition by Zaragozic Acid B, Antimicrob. Agents Chemother. 47, 2366-2369.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 2366-2369
    • Hornby, J.M.1    Kebaara, B.W.2    Nickerson, K.W.3
  • 155
    • 0036840116 scopus 로고    scopus 로고
    • Inhibition of Candida albicans biofilm formation by farnesol, a quorum-sensing molecule
    • Ramage, G., Saville, S.P., Wickes, B.L., and Lopez-Ribot, J.L. (2002) Inhibition of Candida albicans Biofilm Formation by Farnesol, a Quorum-Sensing Molecule, Appl. Environ. Microbiol. 68, 5459-5463.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5459-5463
    • Ramage, G.1    Saville, S.P.2    Wickes, B.L.3    Lopez-Ribot, J.L.4
  • 156
    • 0029903276 scopus 로고    scopus 로고
    • In-vitro and in-vivo antibacterial activity of plaunotol, a cytoprotective antiulcer agent, against Helicobacter pylori
    • Koga, T., Kawada, H., Utsui, Y., Domon, H., Ishii, C., and Yasuda, H. (1996) In-vitro and in-vivo Antibacterial Activity of Plaunotol, a Cytoprotective Antiulcer Agent, Against Helicobacter pylori, J. Antimicrob. Chemother. 37, 919-929.
    • (1996) J. Antimicrob. Chemother. , vol.37 , pp. 919-929
    • Koga, T.1    Kawada, H.2    Utsui, Y.3    Domon, H.4    Ishii, C.5    Yasuda, H.6
  • 158
    • 2642529526 scopus 로고    scopus 로고
    • In vitro antileishmanial effects of antibacterial diterpenes from two ethiopian Premna species: P. schimperi and P. oligotricha
    • Habtemariam, S. (2003) In vitro Antileishmanial Effects of Antibacterial Diterpenes from Two Ethiopian Premna Species: P. schimperi and P. oligotricha, BMC Pharmacol. 3, 6.
    • (2003) BMC Pharmacol. , vol.3 , pp. 6
    • Habtemariam, S.1
  • 160
    • 0036899026 scopus 로고    scopus 로고
    • Insect antifeedant activity of clerodane diterpenes and related model compounds
    • Klein Gebbinck, E.A., Jansen, B.J., and de Groot, A. (2002) Insect Antifeedant Activity of Clerodane Diterpenes and Related Model Compounds, Phytochemistry 61, 737-770.
    • (2002) Phytochemistry , vol.61 , pp. 737-770
    • Klein Gebbinck, E.A.1    Jansen, B.J.2    De Groot, A.3
  • 161
    • 0035666449 scopus 로고    scopus 로고
    • Blood glucose- and triglyceride-lowering effect of trans-dehydrocrotonin, a diterpene from Croton cajucara Benth., in rats
    • Silva, R.M., Santos, F.A., Rao, V.S., Maciel, M.A., and Pinto, A.C. (2001) Blood Glucose- and Triglyceride-Lowering Effect of trans-Dehydrocrotonin, a Diterpene from Croton cajucara Benth., in Rats, Diabetes Obes. Metab. 3, 452-456.
    • (2001) Diabetes Obes. Metab. , vol.3 , pp. 452-456
    • Silva, R.M.1    Santos, F.A.2    Rao, V.S.3    Maciel, M.A.4    Pinto, A.C.5
  • 162
    • 0034939302 scopus 로고    scopus 로고
    • Anti-tumor promoting diterpenes from the stem bark of Thuja standishii (Cupressaceae)
    • Iwamoto, M., Ohtsu, H., Tokuda, H., Nishino, H., Matsunaga, S., and Tanaka, R. (2001) Anti-tumor Promoting Diterpenes from the Stem Bark of Thuja standishii (Cupressaceae), Bioorg. Med. Chem. 9, 1911-1921.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 1911-1921
    • Iwamoto, M.1    Ohtsu, H.2    Tokuda, H.3    Nishino, H.4    Matsunaga, S.5    Tanaka, R.6
  • 163
    • 0036198699 scopus 로고    scopus 로고
    • Farnesol and geranylgeraniol: Prevention and reversion of lovastatin-induced effects in NIH3T3 cells
    • Ownby, S.E., and Hohl, R.J. (2002) Farnesol and Geranylgeraniol: Prevention and Reversion of Lovastatin-Induced Effects in NIH3T3 Cells, Lipids 37, 185-192.
    • (2002) Lipids , vol.37 , pp. 185-192
    • Ownby, S.E.1    Hohl, R.J.2
  • 164
    • 0029985373 scopus 로고    scopus 로고
    • Identification and characterization of geranylgeraniol kinase and geranylgeranyl phosphate kinase from the archaebacterium Sulfolobus acidocaldarius
    • Ohnuma, S., Watanabe, M., and Nishino, T. (1996) Identification and Characterization of Geranylgeraniol Kinase and Geranylgeranyl Phosphate Kinase from the Archaebacterium Sulfolobus acidocaldarius, J. Biochem. (Tokyo) 119, 541-547.
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 541-547
    • Ohnuma, S.1    Watanabe, M.2    Nishino, T.3
  • 165
    • 0036684886 scopus 로고    scopus 로고
    • Formation of (R)-2,3-dihydrogeranylgeranoic acid from geranylgeraniol in rat thymocytes
    • Kodaira, Y., Usui, K., Kon, I., and Sagami, H. (2002) Formation of (R)-2,3-Dihydrogeranylgeranoic Acid from Geranylgeraniol in Rat Thymocytes, J. Biochem. (Tokyo) 132, 327-334.
    • (2002) J. Biochem. (Tokyo) , vol.132 , pp. 327-334
    • Kodaira, Y.1    Usui, K.2    Kon, I.3    Sagami, H.4
  • 168
    • 0023176478 scopus 로고
    • Identification of urinary and microsomal metabolites of geranylgeranylacetone in rats
    • Nishizawa, Y., Abe, S., Yamada, K., Nakamura, T., Yamatsu, I., and Kinoshita, K. (1987) Identification of Urinary and Microsomal Metabolites of Geranylgeranylacetone in Rats, Xenobiotica 17, 575-584.
    • (1987) Xenobiotica , vol.17 , pp. 575-584
    • Nishizawa, Y.1    Abe, S.2    Yamada, K.3    Nakamura, T.4    Yamatsu, I.5    Kinoshita, K.6
  • 170
    • 0034792075 scopus 로고    scopus 로고
    • Geranylgeraniol, an intermediate product in mevalonate pathway, induces apoptotic cell death in human hepatoma cells: Death receptor-independent activation of caspase-8 with down-regulation of Bcl-xL expression
    • Takeda, Y., Nakao, K., Nakata, K., Kawakami, A., Ida, H., Ichikawa, T., Shigeno, M., Kajiya, Y., Hamasaki, K., Kato, Y., and Eguchi, K. (2001) Geranylgeraniol, an Intermediate Product in Mevalonate Pathway, Induces Apoptotic Cell Death in Human Hepatoma Cells: Death Receptor-Independent Activation of Caspase-8 with Down-Regulation of Bcl-xL Expression, Jpn. J. Cancer Res. 92, 918-925.
    • (2001) Jpn. J. Cancer Res. , vol.92 , pp. 918-925
    • Takeda, Y.1    Nakao, K.2    Nakata, K.3    Kawakami, A.4    Ida, H.5    Ichikawa, T.6    Shigeno, M.7    Kajiya, Y.8    Hamasaki, K.9    Kato, Y.10    Eguchi, K.11
  • 171
    • 0031550232 scopus 로고    scopus 로고
    • Rapid loss in the mitochondrial membrane potential during geranylgeranoic acid-induced apoptosis
    • Shidoji, Y., Nakamura, N., Moriwaki, H., and Muto, Y. (1997) Rapid Loss in the Mitochondrial Membrane Potential During Geranylgeranoic Acid-Induced Apoptosis, Biochem. Biophys. Res. Commun. 230, 58-63.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 58-63
    • Shidoji, Y.1    Nakamura, N.2    Moriwaki, H.3    Muto, Y.4
  • 172
    • 0036254464 scopus 로고    scopus 로고
    • Acyclo-retinoic acid induces apoptosis in human prostate cancer cells
    • Kotake-Nara, E., Kim, S.J., Kobori, M., Miyashita, K., and Nagao, A. (2002) Acyclo-Retinoic Acid Induces Apoptosis in Human Prostate Cancer Cells, Anticancer Res. 22, 689-695.
    • (2002) Anticancer Res. , vol.22 , pp. 689-695
    • Kotake-Nara, E.1    Kim, S.J.2    Kobori, M.3    Miyashita, K.4    Nagao, A.5
  • 173
    • 0030600384 scopus 로고    scopus 로고
    • Geranylgeraniol causes a decrease in levels of calreticulin and tyrosine phosphorylation of a 36-kDa protein prior to the appearance of apoptotic features in HL-60 cells
    • Nakajo, S., Okamoto, M., Masuda, Y., Sakai, I., Ohsawa, S., and Nakaya, K. (1996) Geranylgeraniol Causes a Decrease in Levels of Calreticulin and Tyrosine Phosphorylation of a 36-kDa Protein Prior to the Appearance of Apoptotic Features in HL-60 Cells, Biochem. Biophys. Res. Commun. 226, 741-745.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 741-745
    • Nakajo, S.1    Okamoto, M.2    Masuda, Y.3    Sakai, I.4    Ohsawa, S.5    Nakaya, K.6
  • 174
    • 0031589963 scopus 로고    scopus 로고
    • Geranylgeraniol potently induces caspase-3-like activity during apoptosis in human leukemia U937 cells
    • Masuda, Y., Nakaya, M., Nakajo, S., and Nakaya, K. (1997) Geranylgeraniol Potently Induces Caspase-3-Like Activity During Apoptosis in Human Leukemia U937 Cells, Biochem. Biophys. Res. Commun. 234, 641-645.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 641-645
    • Masuda, Y.1    Nakaya, M.2    Nakajo, S.3    Nakaya, K.4
  • 175
    • 0033730298 scopus 로고    scopus 로고
    • The mechanism of geranylgeraniol-induced apoptosis involves activation, by a caspase-3-like protease, of a c-jun N-terminal kinase signaling cascade and differs from mechanisms of apoptosis induced by conventional chemotherapeutic drugs
    • Masuda, Y., Nakaya, M., Aiuchi, T., Hashimoto, S., Nakajo, S., and Nakaya, K. (2000) The Mechanism of Geranylgeraniol-Induced Apoptosis Involves Activation, by a Caspase-3-like Protease, of a c-jun N-Terminal Kinase Signaling Cascade and Differs from Mechanisms of Apoptosis Induced by Conventional Chemotherapeutic Drugs, Leuk. Res. 24, 937-950.
    • (2000) Leuk. Res. , vol.24 , pp. 937-950
    • Masuda, Y.1    Nakaya, M.2    Aiuchi, T.3    Hashimoto, S.4    Nakajo, S.5    Nakaya, K.6
  • 176
    • 0030069102 scopus 로고    scopus 로고
    • Apoptosis in human hepatoma cell line induced by 4,5-didehydro geranylgeranoic acid (acyclic retinoid) via down-regulation of transforming growth factor-α
    • Nakamura, N., Shidoji, Y., Moriwaki, H., and Muto, Y. (1996) Apoptosis in Human Hepatoma Cell Line Induced by 4,5-Didehydro Geranylgeranoic Acid (acyclic retinoid) via Down-Regulation of Transforming Growth Factor-α, Biochem. Biophys. Res. Commun. 219, 100-104.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 100-104
    • Nakamura, N.1    Shidoji, Y.2    Moriwaki, H.3    Muto, Y.4
  • 177
    • 0019508881 scopus 로고
    • Antiulcer effect of geranylgeranylacetone, a new acyclic polyisoprenoid, on experimentally induced gastric and duodenal ulcers in rats
    • Murakami, M., Oketani, K., Fujisaki, H., Wakabayashi, T., and Ohgo, T. (1981) Antiulcer Effect of Geranylgeranylacetone, a New Acyclic Polyisoprenoid, on Experimentally Induced Gastric and Duodenal Ulcers in Rats, Arzneimittelforschung. 31, 799-804.
    • (1981) Arzneimittelforschung , vol.31 , pp. 799-804
    • Murakami, M.1    Oketani, K.2    Fujisaki, H.3    Wakabayashi, T.4    Ohgo, T.5
  • 178
    • 0022618659 scopus 로고
    • Geranylgeranylacetone, a novel anti-ulcer drug, stimulates mucus synthesis and secretion in rat gastric cultured cells
    • Terano, A., Hiraishi, H., Ota, S., and Sugimoto, T. (1986) Geranylgeranylacetone, a Novel Anti-ulcer Drug, Stimulates Mucus Synthesis and Secretion in Rat Gastric Cultured Cells, Digestion 33, 206-210.
    • (1986) Digestion , vol.33 , pp. 206-210
    • Terano, A.1    Hiraishi, H.2    Ota, S.3    Sugimoto, T.4
  • 179
    • 0036918371 scopus 로고    scopus 로고
    • Suppression of Helicobacter pylori-induced interleukin-8 production in gastric cancer cell lines by an anti-ulcer drug, geranylgeranylacetone
    • Yoshimura, N., Suzuki, Y., and Saito, Y. (2002) Suppression of Helicobacter pylori-Induced Interleukin-8 Production in Gastric Cancer Cell Lines by an Anti-ulcer Drug, Geranylgeranylacetone, J. Gastroenterol. Hepatol. 17, 1153-1160.
    • (2002) J. Gastroenterol. Hepatol. , vol.17 , pp. 1153-1160
    • Yoshimura, N.1    Suzuki, Y.2    Saito, Y.3
  • 180
    • 0032833875 scopus 로고    scopus 로고
    • Geranylgeranylacetone suppresses spontaneous apoptotic DNA fragmentation in cultured guinea pig gastric pit cells
    • Tsutsumi, S., Rokutan, K., Tsuchiya, T., and Mizushima, T. (1999) Geranylgeranylacetone Suppresses Spontaneous Apoptotic DNA Fragmentation in Cultured Guinea Pig Gastric Pit Cells, Biol. Pharm. Bull. 22, 886-887.
    • (1999) Biol. Pharm. Bull. , vol.22 , pp. 886-887
    • Tsutsumi, S.1    Rokutan, K.2    Tsuchiya, T.3    Mizushima, T.4
  • 181
    • 0030038266 scopus 로고    scopus 로고
    • Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa
    • Hirakawa, T., Rokutan, K., Nikawa, T., and Kishi, K. (1996) Geranylgeranylacetone Induces Heat Shock Proteins in Cultured Guinea Pig Gastric Mucosal Cells and Rat Gastric Mucosa, Gastroenterology 111, 345-357.
    • (1996) Gastroenterology , vol.111 , pp. 345-357
    • Hirakawa, T.1    Rokutan, K.2    Nikawa, T.3    Kishi, K.4
  • 183
    • 0142059091 scopus 로고    scopus 로고
    • Astroglial activation accompanies heat shock protein upregulation in rat brain following single oral dose of geranylgeranylacetone
    • Fujiki, M., Kobayashi, H., Abe, T., and Ishii, K. (2003) Astroglial Activation Accompanies Heat Shock Protein Upregulation in Rat Brain Following Single Oral Dose of Geranylgeranylacetone, Brain Res. 991, 254-257.
    • (2003) Brain Res. , vol.991 , pp. 254-257
    • Fujiki, M.1    Kobayashi, H.2    Abe, T.3    Ishii, K.4
  • 184
    • 1142298658 scopus 로고    scopus 로고
    • Retinal ganglion cell protection with geranylgeranylacetone, a heat shock protein inducer, in a rat glaucoma model
    • Caprioli, J., Ishii, Y., and Kwong, J.M. (2003) Retinal Ganglion Cell Protection with Geranylgeranylacetone, a Heat Shock Protein Inducer, in a Rat Glaucoma Model, Trans. Am. Ophthalmol. Soc. 101, 39-50.
    • (2003) Trans. Am. Ophthalmol. Soc. , vol.101 , pp. 39-50
    • Caprioli, J.1    Ishii, Y.2    Kwong, J.M.3
  • 185
    • 0034903787 scopus 로고    scopus 로고
    • Geranylgeranylacetone, a heat shock protein inducer, prevents primary graft nonfunction in rat liver transplantation
    • Fudaba, Y., Ohdan, H., Tashiro, H., Ito, H., Fukuda, Y., Dohi, K., and Asahara, T. (2001) Geranylgeranylacetone, a Heat Shock Protein Inducer, Prevents Primary Graft Nonfunction in Rat Liver Transplantation, Transplantation 72, 184-189.
    • (2001) Transplantation , vol.72 , pp. 184-189
    • Fudaba, Y.1    Ohdan, H.2    Tashiro, H.3    Ito, H.4    Fukuda, Y.5    Dohi, K.6    Asahara, T.7
  • 186
    • 0038123078 scopus 로고    scopus 로고
    • Role of protein kinase C in geranylgeranylacetone-induced expression of heat-shock protein 72 and cardioprotection in the rat heart
    • Yamanaka, K., Takahashi, N., Ooie, T., Kaneda, K., Yoshimatsu, H., and Saikawa, T. (2003) Role of Protein Kinase C in Geranylgeranylacetone-Induced Expression of Heat-Shock Protein 72 and Cardioprotection in the Rat Heart, J. Mol. Cell. Cardiol. 35, 785-794.
    • (2003) J. Mol. Cell. Cardiol. , vol.35 , pp. 785-794
    • Yamanaka, K.1    Takahashi, N.2    Ooie, T.3    Kaneda, K.4    Yoshimatsu, H.5    Saikawa, T.6
  • 188
    • 0023106470 scopus 로고
    • Stimulation of prostaglandin production by (2E,6Z,10E)-7-Hydroxymethyl-3, 11,15-trimethyl-2,6,10,14-hexadecatetraen-1-ol (plaunotol), a new anti-ulcer drug, in vitro and in vivo
    • Ushiyama, S., Matsuda, K., Asai, F., and Yamazaki, M. (1987) Stimulation of Prostaglandin Production by (2E,6Z,10E)-7-Hydroxymethyl-3,11,15-trimethyl-2, 6,10,14-hexadecatetraen-1-ol (plaunotol), a New Anti-Ulcer Drug, in vitro and in vivo, Biochem. Pharmacol. 36, 369-375.
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 369-375
    • Ushiyama, S.1    Matsuda, K.2    Asai, F.3    Yamazaki, M.4
  • 189
    • 0024843759 scopus 로고
    • Plaunotol stimulates endogenous secretin release and exocrine pancreatic secretion in rats
    • Chang, J.H., Watanabe, S., Shiratori, K., Moriyoshi, Y., and Takeuchi, T. (1989) Plaunotol Stimulates Endogenous Secretin Release and Exocrine Pancreatic Secretion in Rats, Digestion 44, 142-147.
    • (1989) Digestion , vol.44 , pp. 142-147
    • Chang, J.H.1    Watanabe, S.2    Shiratori, K.3    Moriyoshi, Y.4    Takeuchi, T.5
  • 190
    • 0028894995 scopus 로고
    • Effect of plaunotol on superoxide production activity in vivo
    • Okabe, N., Okada, M., Sakai, T., and Kuroiwa, A. (1995) Effect of Plaunotol on Superoxide Production Activity in vivo, Dig. Dis. Sci. 40, 2321-2322.
    • (1995) Dig. Dis. Sci. , vol.40 , pp. 2321-2322
    • Okabe, N.1    Okada, M.2    Sakai, T.3    Kuroiwa, A.4
  • 191
    • 0032892122 scopus 로고    scopus 로고
    • Plaunotol prevents indomethacin-induced gastric mucosal injury in rats by inhibiting neutrophil activation
    • Murakami, K., Okajima, K., Harada, N., Isobe, H., Liu, W., Johno, M., and Okabe, H. (1999) Plaunotol Prevents Indomethacin-Induced Gastric Mucosal Injury in Rats by Inhibiting Neutrophil Activation, Aliment. Pharmacol. Ther. 13, 521-530.
    • (1999) Aliment. Pharmacol. Ther. , vol.13 , pp. 521-530
    • Murakami, K.1    Okajima, K.2    Harada, N.3    Isobe, H.4    Liu, W.5    Johno, M.6    Okabe, H.7
  • 193
    • 0032729450 scopus 로고    scopus 로고
    • Biodegradation of free phytol by bacterial communities isolated from marine sediments under aerobic and denitrifying conditions
    • Rontani, J.F., Bonin, P.C., and Volkman, J.K. (1999) Biodegradation of Free Phytol by Bacterial Communities Isolated from Marine Sediments Under Aerobic and Denitrifying Conditions, Appl. Environ. Microbiol. 65, 5484-5492.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5484-5492
    • Rontani, J.F.1    Bonin, P.C.2    Volkman, J.K.3
  • 194
    • 0016262979 scopus 로고
    • Hydrocarbon metabolism by Brevibacterium erythrogenes: Normal and branched alkanes
    • Pirnik, M.P., Atlas, R.M., and Bartha, R. (1974) Hydrocarbon Metabolism by Brevibacterium erythrogenes: Normal and Branched Alkanes, J. Bacteriol. 119, 868-878.
    • (1974) J. Bacteriol. , vol.119 , pp. 868-878
    • Pirnik, M.P.1    Atlas, R.M.2    Bartha, R.3
  • 195
    • 0019884097 scopus 로고
    • Gas chromatographic separation of diastereomeric isoprenoids as molecular markers of oil pollution
    • Berthou, F., and Friovourt, M.P. (1981) Gas Chromatographic Separation of Diastereomeric Isoprenoids as Molecular Markers of Oil Pollution, J. Chromatogr. A. 219, 393-402.
    • (1981) J. Chromatogr. A , vol.219 , pp. 393-402
    • Berthou, F.1    Friovourt, M.P.2
  • 196
    • 0028840622 scopus 로고
    • Microbial degradation of monoterpenes in the absence of molecular oxygen
    • Harder, J., and Probian, C. (1995) Microbial Degradation of Monoterpenes in the Absence of Molecular Oxygen, Appl. Environ. Microbiol. 61, 3804-3808.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3804-3808
    • Harder, J.1    Probian, C.2
  • 197
    • 0036041829 scopus 로고    scopus 로고
    • Aerobic and anaerobic metabolism of squalene by a denitrifying bacterium isolated from marine sediment
    • Rontani, J.F., Mouzdahir, A., Michotey, V., and Bonin, P. (2002) Aerobic and Anaerobic Metabolism of Squalene by a Denitrifying Bacterium Isolated from Marine Sediment, Arch. Microbiol. 178, 279-287.
    • (2002) Arch. Microbiol. , vol.178 , pp. 279-287
    • Rontani, J.F.1    Mouzdahir, A.2    Michotey, V.3    Bonin, P.4
  • 198
    • 0030905387 scopus 로고    scopus 로고
    • Anaerobic mineralization of cholesterol by a novel type of denitrifying bacterium
    • Harder, J., and Probian, C. (1997) Anaerobic Mineralization of Cholesterol by a Novel Type of Denitrifying Bacterium, Arch. Microbiol. 167, 269-274.
    • (1997) Arch. Microbiol. , vol.167 , pp. 269-274
    • Harder, J.1    Probian, C.2
  • 200
    • 0041851188 scopus 로고    scopus 로고
    • Alcanivorax which prevails in oil-contaminated seawater exhibits broad substrate specificity for alkane degradation
    • Hara, A., Syutsubo, K., and Harayama, S. (2003) Alcanivorax Which Prevails in Oil-Contaminated Seawater Exhibits Broad Substrate Specificity for Alkane Degradation, Environ. Microbiol. 5, 746-753.
    • (2003) Environ. Microbiol. , vol.5 , pp. 746-753
    • Hara, A.1    Syutsubo, K.2    Harayama, S.3
  • 202
    • 0016913421 scopus 로고
    • Crystal and molecular structure of compactin, a new antifungal metabolite from Penicillium brevicompactum
    • Brown, A.G., Smale, T.C., King, T.J., Hasenkamp, R., and Thompson, R.H. (1976) Crystal and Molecular Structure of Compactin, a New Antifungal Metabolite from Penicillium brevicompactum, J. Chem. Soc. Perkin 1, 1165-1170.
    • (1976) J. Chem. Soc. Perkin. , vol.1 , pp. 1165-1170
    • Brown, A.G.1    Smale, T.C.2    King, T.J.3    Hasenkamp, R.4    Thompson, R.H.5
  • 203
    • 0018500225 scopus 로고
    • Kinetic analysis of the reaction catalyzed by rat-liver 3-hydroxy-3-methylglutaryl-coenzyme-A reductase using two specific inhibitors
    • Tanzawa, K., and Endo, A. (1979) Kinetic Analysis of the Reaction Catalyzed by Rat-Liver 3-Hydroxy-3-methylglutaryl-Coenzyme-A Reductase Using Two Specific Inhibitors, Eur. J. Biochem. 98, 195-201.
    • (1979) Eur. J. Biochem. , vol.98 , pp. 195-201
    • Tanzawa, K.1    Endo, A.2
  • 204
    • 0017807973 scopus 로고
    • Inhibitory effects on lipid metabolism in cultured cells of ML-236B, a potent inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase
    • Kaneko, I., Hazama-Shimada, Y., and Endo, A. (1978) Inhibitory Effects on Lipid Metabolism in Cultured Cells of ML-236B, a Potent Inhibitor of 3-Hydroxy-3-methylglutaryl-Coenzyme-A Reductase, Eur. J. Biochem. 87, 313-321.
    • (1978) Eur. J. Biochem. , vol.87 , pp. 313-321
    • Kaneko, I.1    Hazama-Shimada, Y.2    Endo, A.3
  • 205
    • 0018135853 scopus 로고
    • Specific inhibition of desmosterol synthesis by ML-236B in mouse LM cells grown in suspension in a lipid-free medium
    • Doi, O., and Endo, A. (1978) Specific Inhibition of Desmosterol Synthesis by ML-236B in Mouse LM Cells Grown in Suspension in a Lipid-Free Medium, Jpn. J. Med. Sci. Biol. 31, 225-233.
    • (1978) Jpn. J. Med. Sci. Biol. , vol.31 , pp. 225-233
    • Doi, O.1    Endo, A.2
  • 206
    • 0018381954 scopus 로고
    • Hypolipidemic effects in dogs of ML-236B, a competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Tsujita, Y., Kuroda, M., Tanzawa, K., Kitano, N., and Endo, A. (1979) Hypolipidemic Effects in Dogs of ML-236B, a Competitive Inhibitor of 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase, Atherosclerosis 32, 307-313.
    • (1979) Atherosclerosis , vol.32 , pp. 307-313
    • Tsujita, Y.1    Kuroda, M.2    Tanzawa, K.3    Kitano, N.4    Endo, A.5
  • 207
    • 0018749065 scopus 로고
    • Hypolipidemic effects in monkeys of ML-236B, a competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Kuroda, M., Tsujita, Y., Tanzawa, K., and Endo, A. (1979) Hypolipidemic Effects in Monkeys of ML-236B, a Competitive Inhibitor of 3-Hydroxy-3- methylglutaryl Coenzyme A Reductase, Lipids 14, 585-589.
    • (1979) Lipids , vol.14 , pp. 585-589
    • Kuroda, M.1    Tsujita, Y.2    Tanzawa, K.3    Endo, A.4
  • 208
    • 0018901408 scopus 로고
    • Therapeutic effects of ML-236B in primary hypercholesterolemia
    • Yamamoto, A., Sudo, H., and Endo, A. (1980) Therapeutic Effects of ML-236B in Primary Hypercholesterolemia, Atherosclerosis 35, 259-266.
    • (1980) Atherosclerosis , vol.35 , pp. 259-266
    • Yamamoto, A.1    Sudo, H.2    Endo, A.3
  • 210
    • 0027332512 scopus 로고
    • Pleurotus fungi produce mevinolin, an inhibitor of HMG CoA reductase
    • Gunde-Cimerman, N., Plemenitas, A., and Cimerman, A. (1993) Pleurotus Fungi Produce Mevinolin, an Inhibitor of HMG CoA Reductase, FEMS Microbiol. Lett. 113, 333-337.
    • (1993) FEMS Microbiol. Lett. , vol.113 , pp. 333-337
    • Gunde-Cimerman, N.1    Plemenitas, A.2    Cimerman, A.3
  • 211
    • 0028801112 scopus 로고
    • A hydroxymethylglutaryl-CoA reductase inhibitor synthesized by yeasts
    • Gunde-Cimerman, N., Plemenitas, A., and Cimerman, A. (1995) A Hydroxymethylglutaryl-CoA Reductase Inhibitor Synthesized by Yeasts, FEMS Microbiol. Lett. 132, 39-43.
    • (1995) FEMS Microbiol. Lett. , vol.132 , pp. 39-43
    • Gunde-Cimerman, N.1    Plemenitas, A.2    Cimerman, A.3
  • 212
    • 0018592266 scopus 로고
    • Monacolin K, a new hypocholesterolemic agent produced by a Monascus species
    • Endo, A. (1979) Monacolin K, a New Hypocholesterolemic Agent Produced by a Monascus Species, J. Antibiot. (Tokyo) 32, 852-854.
    • (1979) J. Antibiot. (Tokyo) , vol.32 , pp. 852-854
    • Endo, A.1
  • 213
    • 0033644892 scopus 로고    scopus 로고
    • Studies on mevinolin production by some fungi
    • Shindia, A.A. (2000) Studies on Mevinolin Production by Some Fungi, Microbios 102, 53-61.
    • (2000) Microbios , vol.102 , pp. 53-61
    • Shindia, A.A.1
  • 214
    • 1842765431 scopus 로고    scopus 로고
    • Intensive statin therapy - A sea change in cardiovascular prevention
    • Topol, E.J. (2004) Intensive Statin Therapy-A Sea Change in Cardiovascular Prevention, New Engl. J. Med. 350, 1562-1564.
    • (2004) New Engl. J. Med. , vol.350 , pp. 1562-1564
    • Topol, E.J.1
  • 215
  • 216
    • 0037235059 scopus 로고    scopus 로고
    • Blockade of HMG-CoA reductase activity causes changes in microtubule-stabilizing protein Tau via suppression of geranylgeranylpyrophosphate formation: Implications for Alzheimer's disease
    • Meske, V., Albert, F., Richter, D., Schwarze, J., and Ohm, T.G. (2003) Blockade of HMG-CoA Reductase Activity Causes Changes in Microtubule-Stabilizing Protein Tau via Suppression of Geranylgeranylpyrophosphate Formation: Implications for Alzheimer's Disease, Eur. J. Neurosci. 17, 93-102.
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 93-102
    • Meske, V.1    Albert, F.2    Richter, D.3    Schwarze, J.4    Ohm, T.G.5
  • 217
    • 0942276470 scopus 로고    scopus 로고
    • Use of statins and fracture: Results of 4 prospective studies and cumulative meta-analysis of observational studies and controlled trials
    • Bauer, D.C., Mundy, G.R., Jamal, S.A., Black, D.M., Cauley, J.A., Ensrud, K.E., van der Klift, M., and Pols, H.A. (2004) Use of Statins and Fracture: Results of 4 Prospective Studies and Cumulative Meta-analysis of Observational Studies and Controlled Trials, Arch. Intern. Med. 164, 146-152.
    • (2004) Arch. Intern. Med. , vol.164 , pp. 146-152
    • Bauer, D.C.1    Mundy, G.R.2    Jamal, S.A.3    Black, D.M.4    Cauley, J.A.5    Ensrud, K.E.6    Van Der Klift, M.7    Pols, H.A.8
  • 218
    • 0037711140 scopus 로고    scopus 로고
    • Early use of statins in acute coronary syndromes
    • Spin, J.M., and Vagelos, R.H. (2003) Early Use of Statins in Acute Coronary Syndromes, Curr. Atheroscler. Rep. 5, 44-51.
    • (2003) Curr. Atheroscler. Rep. , vol.5 , pp. 44-51
    • Spin, J.M.1    Vagelos, R.H.2
  • 219
  • 223
    • 0042833280 scopus 로고    scopus 로고
    • Effects of HMG-CoA reductase inhibitors on coagulation and fibrinolysis processes
    • Krysiak, R., Okopien, B., and Herman, Z. (2003) Effects of HMG-CoA Reductase Inhibitors on Coagulation and Fibrinolysis Processes, Drugs. 63, 1821-1854.
    • (2003) Drugs , vol.63 , pp. 1821-1854
    • Krysiak, R.1    Okopien, B.2    Herman, Z.3
  • 224
    • 0033373592 scopus 로고    scopus 로고
    • Statins as cellular antithrombotics
    • Fenton, J.W., Jr., and Shen, G.X. (1999) Statins as Cellular Antithrombotics, Haemostasis 29, 166-169.
    • (1999) Haemostasis , vol.29 , pp. 166-169
    • Fenton Jr., J.W.1    Shen, G.X.2
  • 225
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: A millennium review
    • Staunton, J., and Weissman, K.J. (2001) Polyketide Biosynthesis: A Millennium Review, Nat. Prod. Rep. 18, 380-416.
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 226
    • 0036321084 scopus 로고    scopus 로고
    • Molecular cloning and characterization of an ML-236B (compactin) biosynthetic gene cluster in Penicillium citrinum
    • Abe, Y., Suzuki, T., Ono, C., Iwamoto, K., Hosobuchi, M., and Yoshikawa, H. (2002) Molecular Cloning and Characterization of an ML-236B (compactin) Biosynthetic Gene Cluster in Penicillium citrinum, Mol. Genet. Genomics 267, 636-646.
    • (2002) Mol. Genet. Genomics , vol.267 , pp. 636-646
    • Abe, Y.1    Suzuki, T.2    Ono, C.3    Iwamoto, K.4    Hosobuchi, M.5    Yoshikawa, H.6
  • 227
    • 0034450187 scopus 로고    scopus 로고
    • Aspects of the biosynthesis of non-aromatic fungal polyketides by iterative polyketide synthases
    • Hutchinson, C.R., Kennedy, J., Park, C., Kendrew, S., Auclair, K., and Vederas, J. (2000) Aspects of the Biosynthesis of Non-aromatic Fungal Polyketides by Iterative Polyketide Synthases, Antonie van Leeuwenhoek 78, 287-295.
    • (2000) Antonie van Leeuwenhoek , vol.78 , pp. 287-295
    • Hutchinson, C.R.1    Kennedy, J.2    Park, C.3    Kendrew, S.4    Auclair, K.5    Vederas, J.6
  • 228
    • 0035378199 scopus 로고    scopus 로고
    • Lovastatin biosynthesis by Aspergillus terreus in a chemically defined medium
    • Hajjaj, H., Niederberger, P., and Duboc, P. (2001) Lovastatin Biosynthesis by Aspergillus terreus in a Chemically Defined Medium, Appl. Environ. Microbiol. 67, 2596-2602.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2596-2602
    • Hajjaj, H.1    Niederberger, P.2    Duboc, P.3
  • 229
    • 0035756722 scopus 로고    scopus 로고
    • Some nutritional factors influencing mevinolin production by Aspergillus terreus strain
    • Shindia, A.A. (2001) Some Nutritional Factors Influencing Mevinolin Production by Aspergillus terreus Strain, Folia Microbiol. (Praha) 46, 413-416.
    • (2001) Folia Microbiol. (Praha) , vol.46 , pp. 413-416
    • Shindia, A.A.1
  • 230
    • 0023713589 scopus 로고
    • Growth inhibition of yeast by compactin (ML-236B) analogues
    • Ikeura, R., Murakawa, S., and Endo, A. (1988) Growth Inhibition of Yeast by Compactin (ML-236B) Analogues, J. Antibiot. (Tokyo) 41, 1148-1150.
    • (1988) J. Antibiot. (Tokyo) , vol.41 , pp. 1148-1150
    • Ikeura, R.1    Murakawa, S.2    Endo, A.3
  • 231
    • 0020017592 scopus 로고
    • Mevinolin: A highly specific inhibitor of microsomal 3-hydroxy-3- methylglutaryl-coenzyme A reductase of radish plants
    • Bach, T.J., and Lichtenthaler, H.K. (1982) Mevinolin: A Highly Specific Inhibitor of Microsomal 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase of Radish Plants, Z. Naturforsch. [C] 37, 46-50.
    • (1982) Z. Naturforsch. [C] , vol.37 , pp. 46-50
    • Bach, T.J.1    Lichtenthaler, H.K.2
  • 232
    • 0031860650 scopus 로고    scopus 로고
    • Inhibition of plant growth by mevinolin and reversal of this inhibition by isoprenoids
    • Josekutty, P.C. (1998) Inhibition of Plant Growth by Mevinolin and Reversal of This Inhibition by Isoprenoids, S. Afr. J. Bot. 64, 18-24.
    • (1998) S. Afr. J. Bot. , vol.64 , pp. 18-24
    • Josekutty, P.C.1
  • 233
    • 0033554651 scopus 로고    scopus 로고
    • Farnesyl pyrophosphate synthase is the molecular target of nitrogen-containing bisphosphonates
    • van Beek, E., Pieterman, E., Cohen, L., Lowik, C., and Papapoulos, S. (1999) Farnesyl Pyrophosphate Synthase Is the Molecular Target of Nitrogen-Containing Bisphosphonates, Biochem. Biophys. Res. Commun. 264, 108-111.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 108-111
    • Van Beek, E.1    Pieterman, E.2    Cohen, L.3    Lowik, C.4    Papapoulos, S.5
  • 234
    • 0033590114 scopus 로고    scopus 로고
    • Mechanism of aminobisphosphonate action: Characterization of alendronate inhibition of the isoprenoid pathway
    • Keller, R.K., and Fliesler, S.J. (1999) Mechanism of Aminobisphosphonate Action: Characterization of Alendronate Inhibition of the Isoprenoid Pathway, Biochem. Biophys. Res. Commun. 266, 560-563.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 560-563
    • Keller, R.K.1    Fliesler, S.J.2
  • 236
    • 0031977199 scopus 로고    scopus 로고
    • Nitrogen-containing bisphosphonates inhibit the mevalonate pathway and prevent post-translational prenylation of GTP-binding proteins, including Ras
    • Luckman, S.P., Hughes, D.E., Coxon, F.P., Graham, R., Russell, G., and Rogers, M.J. (1998) Nitrogen-Containing Bisphosphonates Inhibit the Mevalonate Pathway and Prevent Post-translational Prenylation of GTP-Binding Proteins, Including Ras, J. Bone Miner. Res. 13, 581-589.
    • (1998) J. Bone Miner. Res. , vol.13 , pp. 581-589
    • Luckman, S.P.1    Hughes, D.E.2    Coxon, F.P.3    Graham, R.4    Russell, G.5    Rogers, M.J.6
  • 237
    • 0033520927 scopus 로고    scopus 로고
    • Bisphosphonates act directly on the osteoclast to induce caspase cleavage of Mstl kinase during apoptosis. A link between inhibition of the mevalonate pathway and regulation of an apoptosis-promoting kinase
    • Reszka, A.A., Halasy-Nagy, J.M., Masarachia, P.J., and Rodan, G.A. (1999) Bisphosphonates Act Directly on the Osteoclast to Induce Caspase Cleavage of Mstl Kinase During Apoptosis. A Link Between Inhibition of the Mevalonate Pathway and Regulation of an Apoptosis-Promoting Kinase, J. Biol. Chem. 274, 34967-34973.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34967-34973
    • Reszka, A.A.1    Halasy-Nagy, J.M.2    Masarachia, P.J.3    Rodan, G.A.4
  • 238
    • 0032996153 scopus 로고    scopus 로고
    • Farnesol and geranylgeraniol prevent activation of caspases by aminobisphosphonates: Biochemical evidence for two distinct pharmacological classes of bisphosphonate drugs
    • Benford, H.L., Frith, J.C., Auriola, S., Monkkonen, J., and Rogers, M.J. (1999) Farnesol and Geranylgeraniol Prevent Activation of Caspases by Aminobisphosphonates: Biochemical Evidence for Two Distinct Pharmacological Classes of Bisphosphonate Drugs, Mol. Pharmacol. 56, 131-140.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 131-140
    • Benford, H.L.1    Frith, J.C.2    Auriola, S.3    Monkkonen, J.4    Rogers, M.J.5
  • 239
    • 13044283050 scopus 로고    scopus 로고
    • Alendronate mechanism of action: Geranylgeraniol, an intermediate in the mevalonate pathway, prevents inhibition of osteoclast formation, bone resorption, and kinase activation in vitro
    • Fisher, J.E., Rogers, M.J., Halasy, J.M., Luckman, S.P., Hughes, D.E., Masarachia, P.J., Wesolowski, G., Russell, R.G., Rodan, G.A., and Reszka, A.A. (1999) Alendronate Mechanism of Action: Geranylgeraniol, an Intermediate in the Mevalonate Pathway, Prevents Inhibition of Osteoclast Formation, Bone Resorption, and Kinase Activation in vitro, Proc. Natl. Acad. Sci. USA 96, 133-138.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 133-138
    • Fisher, J.E.1    Rogers, M.J.2    Halasy, J.M.3    Luckman, S.P.4    Hughes, D.E.5    Masarachia, P.J.6    Wesolowski, G.7    Russell, R.G.8    Rodan, G.A.9    Reszka, A.A.10
  • 240
    • 0345161422 scopus 로고    scopus 로고
    • The role of geranylgeranylation in bone resorption and its suppression by bisphosphonates in fetal bone explants in vitro: A clue to the mechanism of action of nitrogen-containing bisphosphonates
    • van beek, E., Lowik, C., van der Pluijm, G., and Papapoulos, S. (1999) The Role of Geranylgeranylation in Bone Resorption and Its Suppression by Bisphosphonates in Fetal Bone Explants in vitro: A Clue to the Mechanism of Action of Nitrogen-Containing Bisphosphonates, J. Bone Miner. Res. 14, 722-729.
    • (1999) J. Bone Miner. Res. , vol.14 , pp. 722-729
    • Van Beek, E.1    Lowik, C.2    Van Der Pluijm, G.3    Papapoulos, S.4
  • 241
    • 0036569635 scopus 로고    scopus 로고
    • Alendronate inhibits invasion of PC-3 prostate cancer cells by affecting the mevalonate pathway
    • Virtanen, S.S., Vaananen, H.K., Harkonen, P.L., and Lakkakorpi, P.T. (2002) Alendronate Inhibits Invasion of PC-3 Prostate Cancer Cells by Affecting the Mevalonate Pathway, Cancer Res. 62, 2708-2714.
    • (2002) Cancer Res. , vol.62 , pp. 2708-2714
    • Virtanen, S.S.1    Vaananen, H.K.2    Harkonen, P.L.3    Lakkakorpi, P.T.4
  • 242
    • 0037161612 scopus 로고    scopus 로고
    • Inhibition of geranylgeranyl diphosphate synthase by bisphosphonates and diphosphates: A potential route to new bone antiresorption and antiparasitic agents
    • Szabo, C.M., Matsumura, Y., Fukura, S., Martin, M.B., Sanders, J.M., Sengupta, S., Cieslak, J.A., Loftus, T.C., Lea, C.R., Lee, H.J., et al. (2002) Inhibition of Geranylgeranyl Diphosphate Synthase by Bisphosphonates and Diphosphates: A Potential Route to New Bone Antiresorption and Antiparasitic Agents, J. Med. Chem. 45, 2185-2196.
    • (2002) J. Med. Chem. , vol.45 , pp. 2185-2196
    • Szabo, C.M.1    Matsumura, Y.2    Fukura, S.3    Martin, M.B.4    Sanders, J.M.5    Sengupta, S.6    Cieslak, J.A.7    Loftus, T.C.8    Lea, C.R.9    Lee, H.J.10
  • 245
    • 0038724543 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis in hereditary periodic fever syndromes and inflammation
    • Houten, S.M., Frenkel, J., and Waterham, H.R. (2003) Isoprenoid Biosynthesis in Hereditary Periodic Fever Syndromes and Inflammation, Cell. Mol. Life Sci. 60, 1118-1134.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1118-1134
    • Houten, S.M.1    Frenkel, J.2    Waterham, H.R.3
  • 249
    • 0035063676 scopus 로고    scopus 로고
    • Organization of the mevalonate kinase (MVK) gene and identification of novel mutations causing mevalonic aciduria and hyperimmunoglobulinaemia D and periodic fever syndrome
    • Houten, S.M., Koster, J., Romeijn, G.J., Frenkel, J., Di Rocco, M., Caruso, U., Landrieu, P., Kelley, R.I., Kuis, W., Poll-The, B.T., et al. (2001) Organization of the Mevalonate Kinase (MVK) Gene and Identification of Novel Mutations Causing Mevalonic Aciduria and Hyperimmunoglobulinaemia D and Periodic Fever Syndrome, Eur. J. Hum. Genet. 9, 253-259.
    • (2001) Eur. J. Hum. Genet. , vol.9 , pp. 253-259
    • Houten, S.M.1    Koster, J.2    Romeijn, G.J.3    Frenkel, J.4    Di Rocco, M.5    Caruso, U.6    Landrieu, P.7    Kelley, R.I.8    Kuis, W.9    Poll-The, B.T.10
  • 251
    • 0030671277 scopus 로고    scopus 로고
    • Identification of an active site alanine in mevalonate kinase through characterization of a novel mutation in mevalonate kinase deficiency
    • Hinson, D.D., Chambliss, K.L., Hoffmann, G.F., Krisans, S., Keller, R.K., and Gibson, K.M. (1997) Identification of an Active Site Alanine in Mevalonate Kinase Through Characterization of a Novel Mutation in Mevalonate Kinase Deficiency, J. Biol. Chem. 272, 26756-26760.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26756-26760
    • Hinson, D.D.1    Chambliss, K.L.2    Hoffmann, G.F.3    Krisans, S.4    Keller, R.K.5    Gibson, K.M.6
  • 254
    • 1842869873 scopus 로고    scopus 로고
    • Temperature dependence of mutant mevalonate kinase activity as a pathogenic factor in Hyper-IgD and periodic fever syndrome
    • Houten, S.M., Frenkel, J., Rijkers, G.T., Wanders, R.J., Kuis, W., and Waterham, H.R. (2002) Temperature Dependence of Mutant Mevalonate Kinase Activity as a Pathogenic Factor in Hyper-IgD and Periodic Fever Syndrome, Hum. Mol. Genet. 11, 3115-3124.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 3115-3124
    • Houten, S.M.1    Frenkel, J.2    Rijkers, G.T.3    Wanders, R.J.4    Kuis, W.5    Waterham, H.R.6
  • 255
    • 0023825226 scopus 로고
    • Mevalonic aciduria: Pathobiochemical effects of mevalonate kinase deficiency on cholesterol metabolism in intact fibroblasts
    • Hoffmann, G., Gibson, K.M., Nyhan, W.L., and Sweetman, L. (1988) Mevalonic Aciduria: Pathobiochemical Effects of Mevalonate Kinase Deficiency on Cholesterol Metabolism in Intact Fibroblasts, J. Inherit. Metab. Dis. 11, 229-232.
    • (1988) J. Inherit. Metab. Dis. , vol.11 , pp. 229-232
    • Hoffmann, G.1    Gibson, K.M.2    Nyhan, W.L.3    Sweetman, L.4
  • 256
    • 0025220132 scopus 로고
    • 3-Hydroxy-3-methylglutaryl coenzyme A reductase activity in cultured fibroblasts from patients with mevalonate kinase deficiency: Differential response to lipid supplied by fetal bovine serum in tissue culture medium
    • Gibson, K.M., Hoffmann, G., Schwall, A., Broock, R.L., Aramaki, S., Sweetman, L., Nyhan, W.L., Brandt, I.K., Wappner, R.S., Lehnert, W., and Trefz, F.H. (1990) 3-Hydroxy-3-methylglutaryl Coenzyme A Reductase Activity in Cultured Fibroblasts from Patients with Mevalonate Kinase Deficiency: Differential Response to Lipid Supplied by Fetal Bovine Serum in Tissue Culture Medium, J. Lipid Res. 31, 515-521.
    • (1990) J. Lipid Res. , vol.31 , pp. 515-521
    • Gibson, K.M.1    Hoffmann, G.2    Schwall, A.3    Broock, R.L.4    Aramaki, S.5    Sweetman, L.6    Nyhan, W.L.7    Brandt, I.K.8    Wappner, R.S.9    Lehnert, W.10    Trefz, F.H.11
  • 258
    • 0030888606 scopus 로고    scopus 로고
    • Regulatory adaptation of isoprenoid biosynthesis and the LDL receptor pathway in fibroblasts from patients with mevalonate kinase deficiency
    • Hoffmann, G.F., Wiesmann, U.N., Brendel, S., Keller, R.K., and Gibson, K.M. (1997) Regulatory Adaptation of Isoprenoid Biosynthesis and the LDL Receptor Pathway in Fibroblasts from Patients with Mevalonate Kinase Deficiency, Pediatr. Res. 41, 541-546.
    • (1997) Pediatr. Res. , vol.41 , pp. 541-546
    • Hoffmann, G.F.1    Wiesmann, U.N.2    Brendel, S.3    Keller, R.K.4    Gibson, K.M.5
  • 259
    • 0037458669 scopus 로고    scopus 로고
    • Regulation of isoprenoid/cholesterol biosynthesis in cells from mevalonate kinase-deficient patients
    • Houten, S.M., Schneiders, M.S., Wanders, R.J., and Waterham, H.R. (2003) Regulation of Isoprenoid/Cholesterol Biosynthesis in Cells from Mevalonate Kinase-Deficient Patients, J. Biol. Chem. 278, 5736-5743.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5736-5743
    • Houten, S.M.1    Schneiders, M.S.2    Wanders, R.J.3    Waterham, H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.