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Volumn 113, Issue 11, 2011, Pages 1299-1320

Squalene - biochemistry, molecular biology, process biotechnology, and applications

Author keywords

Isoprenoid; Methylerythritol phosphate; Mevalonate; Squalene; Sterol

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 81155145933     PISSN: 14387697     EISSN: 14389312     Source Type: Journal    
DOI: 10.1002/ejlt.201100203     Document Type: Review
Times cited : (219)

References (305)
  • 1
    • 0742307297 scopus 로고    scopus 로고
    • On the origins of triterpenoid skeletal diversity
    • Xu, R., Fazio, G. C., Matsuda, S. P. T., On the origins of triterpenoid skeletal diversity. Phytochemistry 2004, 65, 261-291.
    • (2004) Phytochemistry , vol.65 , pp. 261-291
    • Xu, R.1    Fazio, G.C.2    Matsuda, S.P.T.3
  • 2
    • 0028913277 scopus 로고
    • Kinetic study of quenching reaction of singlet oxygen and scavenging reaction of free radical by squalene in n-butanol
    • Kohno, Y., Egawa, Y., Itoh, S., Nagaoka, S., et al., Kinetic study of quenching reaction of singlet oxygen and scavenging reaction of free radical by squalene in n-butanol. Biochim. Biophys. Acta 1995, 1256, 52-56.
    • (1995) Biochim. Biophys. Acta , vol.1256 , pp. 52-56
    • Kohno, Y.1    Egawa, Y.2    Itoh, S.3    Nagaoka, S.4
  • 3
    • 59349087925 scopus 로고    scopus 로고
    • Biological and pharmacological activities of squalene and related compounds: Potential uses in cosmetic dermatology
    • Huang, Z. R., Lin, Y. K., Fang, J. Y., Biological and pharmacological activities of squalene and related compounds: Potential uses in cosmetic dermatology. Molecules 2009, 14, 540-554.
    • (2009) Molecules , vol.14 , pp. 540-554
    • Huang, Z.R.1    Lin, Y.K.2    Fang, J.Y.3
  • 4
    • 70349559750 scopus 로고    scopus 로고
    • Squalene emulsions for parenteral vaccine and drug delivery
    • Fox, C. B., Squalene emulsions for parenteral vaccine and drug delivery. Molecules 2009, 14, 3286-3312.
    • (2009) Molecules , vol.14 , pp. 3286-3312
    • Fox, C.B.1
  • 5
    • 0033426940 scopus 로고    scopus 로고
    • Squalene, olive oil, and cancer risk. Review and hypothesis
    • Newmark, H. L., Squalene, olive oil, and cancer risk. Review and hypothesis. Ann. N.Y. Acad. Sci. 1999, 889, 193-203.
    • (1999) Ann. N.Y. Acad. Sci. , vol.889 , pp. 193-203
    • Newmark, H.L.1
  • 6
    • 0031843397 scopus 로고    scopus 로고
    • Chemopreventive effect of squalene on colon cancer
    • Rao, C. V., Newmark, H. L., Reddy, B. S., Chemopreventive effect of squalene on colon cancer. Carcinogenesis 1998, 19, 287-290.
    • (1998) Carcinogenesis , vol.19 , pp. 287-290
    • Rao, C.V.1    Newmark, H.L.2    Reddy, B.S.3
  • 7
    • 0033945291 scopus 로고    scopus 로고
    • Phenolic compounds and squalene in olive oils: The concentration and antioxidant potential of total phenols, simple phenols, secoiridoids, lignans and squalene
    • Owen, R. W., Mier, W., Giacosa, A., Hull, W. E., et al., Phenolic compounds and squalene in olive oils: The concentration and antioxidant potential of total phenols, simple phenols, secoiridoids, lignans and squalene. Food Chem. Toxicol. 2000, 38, 647-659.
    • (2000) Food Chem. Toxicol. , vol.38 , pp. 647-659
    • Owen, R.W.1    Mier, W.2    Giacosa, A.3    Hull, W.E.4
  • 9
    • 15244344677 scopus 로고    scopus 로고
    • The protective role of squalene in alcohol damage in the chick embryo retina
    • Aguilera, Y., Dorado, M. E., Prada, F. A., Martinez, J. J., et al., The protective role of squalene in alcohol damage in the chick embryo retina. Exp. Eye Res. 2005, 80, 535-543.
    • (2005) Exp. Eye Res. , vol.80 , pp. 535-543
    • Aguilera, Y.1    Dorado, M.E.2    Prada, F.A.3    Martinez, J.J.4
  • 10
    • 77950858351 scopus 로고    scopus 로고
    • Squalenoyl nucleoside monophosphate nanoassemblies: New prodrug strategy for the delivery of nucleotide analogues
    • Caron, J., Reddy, L. H., Lepetre-Mouelhi, S., Wack, S., et al., Squalenoyl nucleoside monophosphate nanoassemblies: New prodrug strategy for the delivery of nucleotide analogues. Bioorg. Med. Chem. Lett. 2010, 20, 2761-2764.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 2761-2764
    • Caron, J.1    Reddy, L.H.2    Lepetre-Mouelhi, S.3    Wack, S.4
  • 11
    • 34948844031 scopus 로고    scopus 로고
    • Enhancement of gemcitabine affinity for biomembranes by conjugation with squalene: Differential scanning calorimetry and Langmuir-Blodgett studies using biomembrane models
    • Castelli, F., Sarpietro, M. G., Micieli, D., Stella, B., et al., Enhancement of gemcitabine affinity for biomembranes by conjugation with squalene: Differential scanning calorimetry and Langmuir-Blodgett studies using biomembrane models. J. Colloid Interface Sci. 2007, 316, 43-52.
    • (2007) J. Colloid Interface Sci. , vol.316 , pp. 43-52
    • Castelli, F.1    Sarpietro, M.G.2    Micieli, D.3    Stella, B.4
  • 12
    • 77953810106 scopus 로고    scopus 로고
    • Interaction of a new anticancer prodrug, gemcitabine-squalene, with a model membrane: Coupled DSC and XRD study
    • Pili, B., Bourgaux, C., Amenitsch, H., Keller, G., et al., Interaction of a new anticancer prodrug, gemcitabine-squalene, with a model membrane: Coupled DSC and XRD study. Biochim. Biophys. Acta 2010, 1798, 1522-1532.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1522-1532
    • Pili, B.1    Bourgaux, C.2    Amenitsch, H.3    Keller, G.4
  • 13
    • 0037070030 scopus 로고    scopus 로고
    • Stability of virgin olive oil. 2. Photo-oxidation studies
    • Psomiadou, E., Tsimidou, M., Stability of virgin olive oil. 2. Photo-oxidation studies. J. Agric. Food Chem. 2002, 50, 722-727.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 722-727
    • Psomiadou, E.1    Tsimidou, M.2
  • 14
    • 0037070025 scopus 로고    scopus 로고
    • Stability of virgin olive oil. 1. Autoxidation studies
    • Psomiadou, E., Tsimidou, M., Stability of virgin olive oil. 1. Autoxidation studies. J. Agric. Food Chem. 2002, 50, 716-721.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 716-721
    • Psomiadou, E.1    Tsimidou, M.2
  • 15
    • 0031966097 scopus 로고    scopus 로고
    • Natural antioxidants in the unsaponifiable fraction of virgin olive oils from different cultivars
    • Manzi, P., Panfili, G., Esti, M., Pizzoferrato, L., Natural antioxidants in the unsaponifiable fraction of virgin olive oils from different cultivars. J. Sci. Food Agr. 1998, 77, 115-120.
    • (1998) J. Sci. Food Agr. , vol.77 , pp. 115-120
    • Manzi, P.1    Panfili, G.2    Esti, M.3    Pizzoferrato, L.4
  • 16
    • 57849134301 scopus 로고    scopus 로고
    • Processing stability of squalene in amaranth and antioxidant potential of amaranth extract
    • Tikekar, R. V., Ludescher, R. D., Karwe, M. V., Processing stability of squalene in amaranth and antioxidant potential of amaranth extract. J. Agric. Food Chem. 2008, 56, 10675-10678.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 10675-10678
    • Tikekar, R.V.1    Ludescher, R.D.2    Karwe, M.V.3
  • 17
    • 15444363338 scopus 로고    scopus 로고
    • Relation between the endogenous antioxidant system and the quality of extra virgin olive oil under accelerated storage conditions
    • Hrncirik, K., Fritsche, S., Relation between the endogenous antioxidant system and the quality of extra virgin olive oil under accelerated storage conditions. J. Agric. Food Chem. 2005, 53, 2103-2110.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 2103-2110
    • Hrncirik, K.1    Fritsche, S.2
  • 18
    • 62549127278 scopus 로고    scopus 로고
    • Pan-frying of French fries in three different edible oils enriched with olive leaf extract: Oxidative stability and fate of microconstituents
    • Chiou, A., Kalogeropoulos, N., Salta, F. N., Efstathiou, P., et al., Pan-frying of French fries in three different edible oils enriched with olive leaf extract: Oxidative stability and fate of microconstituents. Lwt- Food Sci. Technol. 2009, 42, 1090-1097.
    • (2009) Lwt- Food Sci. Technol. , vol.42 , pp. 1090-1097
    • Chiou, A.1    Kalogeropoulos, N.2    Salta, F.N.3    Efstathiou, P.4
  • 19
    • 77949264892 scopus 로고    scopus 로고
    • Squalene-based oil-in-water emulsion adjuvants perturb metabolism of neutral lipids and enhance lipid droplet formation
    • Kalvodova, L., Squalene-based oil-in-water emulsion adjuvants perturb metabolism of neutral lipids and enhance lipid droplet formation. Biochem. Biophys. Res. Commun. 2010, 393, 350-355.
    • (2010) Biochem. Biophys. Res. Commun. , vol.393 , pp. 350-355
    • Kalvodova, L.1
  • 20
    • 0025695386 scopus 로고
    • Lipid droplets in Schwann cells during tellurium neuropathy are derived from newly synthesized lipid
    • Goodrum, J. F., Earnhardt, T. S., Goines, N. D., Bouldin, T. W., Lipid droplets in Schwann cells during tellurium neuropathy are derived from newly synthesized lipid. J. Neurochem. 1990, 55, 1928-1932.
    • (1990) J. Neurochem. , vol.55 , pp. 1928-1932
    • Goodrum, J.F.1    Earnhardt, T.S.2    Goines, N.D.3    Bouldin, T.W.4
  • 21
    • 77949889871 scopus 로고    scopus 로고
    • Effect of lipid particle biogenesis on the subcellular distribution of squalene in the yeast Saccharomyces cerevisiae
    • Spanova, M., Czabany, T., Zellnig, G., Leitner, E., et al., Effect of lipid particle biogenesis on the subcellular distribution of squalene in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 2010, 285, 6127-6133.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6127-6133
    • Spanova, M.1    Czabany, T.2    Zellnig, G.3    Leitner, E.4
  • 22
    • 0037169489 scopus 로고    scopus 로고
    • Yeast oxidosqualene cyclase (Erg7p) is a major component of lipid particles
    • Milla, P., Athenstaedt, K., Viola, F., Oliaro-Bosso, S., et al., Yeast oxidosqualene cyclase (Erg7p) is a major component of lipid particles. J. Biol. Chem. 2002, 277, 2406-2412.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2406-2412
    • Milla, P.1    Athenstaedt, K.2    Viola, F.3    Oliaro-Bosso, S.4
  • 24
    • 17544384829 scopus 로고    scopus 로고
    • Squalane is in the midplane of the lipid bilayer: Implications for its function as a proton permeability barrier
    • Hauss, T., Dante, S., Dencher, N. A., Haines, T. H., Squalane is in the midplane of the lipid bilayer: Implications for its function as a proton permeability barrier. Biochim. Biophys. Acta 2002, 1556, 149-154.
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 149-154
    • Hauss, T.1    Dante, S.2    Dencher, N.A.3    Haines, T.H.4
  • 25
    • 0027376103 scopus 로고
    • Squalene promotes the formation of non-bilayer structures in phospholipid model membranes
    • Lohner, K., Degovics, G., Laggner, P., Gnamusch, E., et al., Squalene promotes the formation of non-bilayer structures in phospholipid model membranes. Biochim. Biophys. Acta 1993, 1152, 69-77.
    • (1993) Biochim. Biophys. Acta , vol.1152 , pp. 69-77
    • Lohner, K.1    Degovics, G.2    Laggner, P.3    Gnamusch, E.4
  • 26
    • 38949218032 scopus 로고    scopus 로고
    • Thematic review series: Skin lipids. Sebaceous gland lipids: friend or foe
    • Smith, K. R., Thiboutot, D. M., Thematic review series: Skin lipids. Sebaceous gland lipids: friend or foe? J. Lipid Res. 2008, 49, 271-281.
    • (2008) J. Lipid Res. , vol.49 , pp. 271-281
    • Smith, K.R.1    Thiboutot, D.M.2
  • 27
    • 70449153370 scopus 로고
    • Studies of sebum. VIII. Observations on the squalene and cholesterol content and the possible functions of squalene in human sebum
    • Boughton, B., Mackenna, R. M., Wheatley, V. R., Wormall, A., Studies of sebum. VIII. Observations on the squalene and cholesterol content and the possible functions of squalene in human sebum. Biochem. J. 1957, 66, 32-38.
    • (1957) Biochem. J. , vol.66 , pp. 32-38
    • Boughton, B.1    Mackenna, R.M.2    Wheatley, V.R.3    Wormall, A.4
  • 28
    • 0014760225 scopus 로고
    • Anatomical variation in the amount and composition of human skin surface lipid
    • Greene, R. S., Downing, D. T., Pochi, P. E., Strauss, J. S., Anatomical variation in the amount and composition of human skin surface lipid. J. Invest. Dermatol. 1970, 54, 240-247.
    • (1970) J. Invest. Dermatol. , vol.54 , pp. 240-247
    • Greene, R.S.1    Downing, D.T.2    Pochi, P.E.3    Strauss, J.S.4
  • 29
    • 0016215212 scopus 로고
    • In vivo studies of sterol and squalene secretion by human skin
    • Nikkari, T., Schreibman, P. H., Ahrens, E. H., Jr., In vivo studies of sterol and squalene secretion by human skin. J. Lipid Res. 1974, 15, 563-573.
    • (1974) J. Lipid Res. , vol.15 , pp. 563-573
    • Nikkari, T.1    Schreibman, P.H.2    Ahrens Jr., E.H.3
  • 30
    • 0025900025 scopus 로고
    • Effect of a novel squalene epoxidase inhibitor, NB-598, on the regulation of cholesterol metabolism in Hep G2 cells
    • Hidaka, Y., Hotta, H., Nagata, Y., Iwasawa, Y., et al., Effect of a novel squalene epoxidase inhibitor, NB-598, on the regulation of cholesterol metabolism in Hep G2 cells. J. Biol. Chem. 1991, 266, 13171-13177.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13171-13177
    • Hidaka, Y.1    Hotta, H.2    Nagata, Y.3    Iwasawa, Y.4
  • 31
    • 0025033769 scopus 로고
    • Metabolic variables of cholesterol during squalene feeding in humans: Comparison with cholestyramine treatment
    • Strandberg, T. E., Tilvis, R. S., Miettinen, T. A., Metabolic variables of cholesterol during squalene feeding in humans: Comparison with cholestyramine treatment. J. Lipid Res. 1990, 31, 1637-1643.
    • (1990) J. Lipid Res. , vol.31 , pp. 1637-1643
    • Strandberg, T.E.1    Tilvis, R.S.2    Miettinen, T.A.3
  • 32
    • 0032913670 scopus 로고    scopus 로고
    • Squalene and its potential clinical uses
    • Kelly, G. S., Squalene and its potential clinical uses. Altern. Med. Rev. 1999, 4, 29-36.
    • (1999) Altern. Med. Rev. , vol.4 , pp. 29-36
    • Kelly, G.S.1
  • 33
    • 0033902052 scopus 로고    scopus 로고
    • Squalene: Potential chemopreventive agent
    • Smith, T. J., Squalene: Potential chemopreventive agent. Expert. Opin. Investig. Drugs 2000, 9, 1841-1848.
    • (2000) Expert. Opin. Investig. Drugs , vol.9 , pp. 1841-1848
    • Smith, T.J.1
  • 34
    • 0031253592 scopus 로고    scopus 로고
    • Extraction of squalene from shark liver oil in a packed column using supercritical carbon dioxide
    • Catchpole, O. J., von Kamp, J. C., Grey, J. B., Extraction of squalene from shark liver oil in a packed column using supercritical carbon dioxide. Ind. Eng. Chem. Res. 1997, 36, 4318-4324.
    • (1997) Ind. Eng. Chem. Res. , vol.36 , pp. 4318-4324
    • Catchpole, O.J.1    von Kamp, J.C.2    Grey, J.B.3
  • 36
    • 0034249634 scopus 로고    scopus 로고
    • Fatty acid and triacylglycerol compositions of seed oils of five Amaranthus; accessions and their comparison to other oils
    • Jahaniaval, F., Kakuda, Y., Marcone, M., Fatty acid and triacylglycerol compositions of seed oils of five Amaranthus; accessions and their comparison to other oils. J. Am. Oil Chem. Soc. 2000, 77, 847-852.
    • (2000) J. Am. Oil Chem. Soc. , vol.77 , pp. 847-852
    • Jahaniaval, F.1    Kakuda, Y.2    Marcone, M.3
  • 37
    • 30344473341 scopus 로고    scopus 로고
    • Protein sensors for membrane sterols
    • Goldstein, J. L., Bose-Boyd, R. A., Brown, M. S., Protein sensors for membrane sterols. Cell 2006, 124, 35-46.
    • (2006) Cell , vol.124 , pp. 35-46
    • Goldstein, J.L.1    Bose-Boyd, R.A.2    Brown, M.S.3
  • 38
    • 18544378347 scopus 로고    scopus 로고
    • Insig-mediated degradation of HMG-CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol
    • Song, B. L., Javitt, N. B., Bose-Boyd, R. A., Insig-mediated degradation of HMG-CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol. Cell Metab. 2005, 1, 179-189.
    • (2005) Cell Metab. , vol.1 , pp. 179-189
    • Song, B.L.1    Javitt, N.B.2    Bose-Boyd, R.A.3
  • 39
    • 3142654791 scopus 로고    scopus 로고
    • Ubiquitination of 3-hydroxy-3-methylglutaryl-CoA reductase in permeabilized cells mediated by cytosolic E1 and a putative membrane-bound ubiquitin ligase
    • Song, B. L., Bose-Boyd, R. A., Ubiquitination of 3-hydroxy-3-methylglutaryl-CoA reductase in permeabilized cells mediated by cytosolic E1 and a putative membrane-bound ubiquitin ligase. J. Biol. Chem. 2004, 279, 28798-28806.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28798-28806
    • Song, B.L.1    Bose-Boyd, R.A.2
  • 41
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L., Brown, M. S., Regulation of the mevalonate pathway. Nature 1990, 343, 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 42
    • 0032851111 scopus 로고    scopus 로고
    • Sterols and isoprenoids: Signaling molecules derived from the cholesterol biosynthetic pathway
    • Edwards, P. A., Ericsson, J., Sterols and isoprenoids: Signaling molecules derived from the cholesterol biosynthetic pathway. Annu. Rev. Biochem. 1999, 68, 157-185.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 157-185
    • Edwards, P.A.1    Ericsson, J.2
  • 43
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock, J. F., Magee, A. I., Childs, J. E., Marshall, C. J., All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 1989, 57, 1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 44
    • 0024443048 scopus 로고
    • Cloning, analysis, and bacterial expression of human farnesyl pyrophosphate synthetase and its regulation in Hep G2 cells
    • Sheares, B. T., White, S. S., Molowa, D. T., Chan, K., et al., Cloning, analysis, and bacterial expression of human farnesyl pyrophosphate synthetase and its regulation in Hep G2 cells. Biochemistry 1989, 28, 8129-8135.
    • (1989) Biochemistry , vol.28 , pp. 8129-8135
    • Sheares, B.T.1    White, S.S.2    Molowa, D.T.3    Chan, K.4
  • 45
    • 0023917971 scopus 로고
    • Evidence for modification of lamin B by a product of mevalonic acid
    • Wolda, S. L., Glomset, J. A., Evidence for modification of lamin B by a product of mevalonic acid. J. Biol. Chem. 1988, 263, 5997-6000.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5997-6000
    • Wolda, S.L.1    Glomset, J.A.2
  • 46
    • 0019135838 scopus 로고
    • Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth
    • Brown, M. S., Goldstein, J. L., Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth. J. Lipid Res. 1980, 21, 505-517.
    • (1980) J. Lipid Res. , vol.21 , pp. 505-517
    • Brown, M.S.1    Goldstein, J.L.2
  • 47
    • 0015764584 scopus 로고
    • Regulation of cholesterol synthesis in normal and malignant tissue
    • Brown, M. S., Goldstein, J. L., Siperstein, M. D., Regulation of cholesterol synthesis in normal and malignant tissue. Fed. Proc. 1973, 32, 2168-2173.
    • (1973) Fed. Proc. , vol.32 , pp. 2168-2173
    • Brown, M.S.1    Goldstein, J.L.2    Siperstein, M.D.3
  • 48
    • 0034672674 scopus 로고    scopus 로고
    • Structure and regulation of mammalian squalene synthase
    • Tansey, T. R., Shechter, I., Structure and regulation of mammalian squalene synthase. Biochim. Biophys. Acta 2000, 1529, 49-62.
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 49-62
    • Tansey, T.R.1    Shechter, I.2
  • 49
    • 0342662303 scopus 로고
    • Squalene synthetase activity in human fibroblasts: Regulation via the low density lipoprotein receptor
    • Faust, J. R., Goldstein, J. L., Brown, M. S., Squalene synthetase activity in human fibroblasts: Regulation via the low density lipoprotein receptor. Proc. Natl. Acad. Sci. U. S. A 1979, 76, 5018-5022.
    • (1979) Proc. Natl. Acad. Sci. U. S. A , vol.76 , pp. 5018-5022
    • Faust, J.R.1    Goldstein, J.L.2    Brown, M.S.3
  • 50
    • 0032475889 scopus 로고    scopus 로고
    • Differential stimulation of cholesterol and unsaturated fatty acid biosynthesis in cells expressing individual nuclear sterol regulatory element-binding proteins
    • Pai, J. T., Guryev, O., Brown, M. S., Goldstein, J. L., Differential stimulation of cholesterol and unsaturated fatty acid biosynthesis in cells expressing individual nuclear sterol regulatory element-binding proteins. J. Biol. Chem. 1998, 273, 26138-26148.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26138-26148
    • Pai, J.T.1    Guryev, O.2    Brown, M.S.3    Goldstein, J.L.4
  • 51
    • 0028797302 scopus 로고
    • Nucleotide sequence of a cDNA for mouse squalene epoxidase
    • Kosuga, K., Hata, S., Osumi, T., Sakakibara, J., et al., Nucleotide sequence of a cDNA for mouse squalene epoxidase. Biochim. Biophys. Acta 1995, 1260, 345-348.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 345-348
    • Kosuga, K.1    Hata, S.2    Osumi, T.3    Sakakibara, J.4
  • 52
    • 0034652257 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase
    • Laden, B. P., Tang, Y., Porter, T. D., Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase. Arch. Biochem. Biophys. 2000, 374, 381-388.
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 381-388
    • Laden, B.P.1    Tang, Y.2    Porter, T.D.3
  • 53
    • 0016641043 scopus 로고
    • Solubilization and partial characterization of rat liver squalene epoxidase
    • Ono, T., Bloch, K., Solubilization and partial characterization of rat liver squalene epoxidase. J. Biol. Chem. 1975, 250, 1571-1579.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1571-1579
    • Ono, T.1    Bloch, K.2
  • 54
    • 0021894241 scopus 로고
    • Squalene epoxidase from rat liver microsomes
    • Ono, T., Imai, Y., Squalene epoxidase from rat liver microsomes. Methods Enzymol. 1985, 110, 375-380.
    • (1985) Methods Enzymol. , vol.110 , pp. 375-380
    • Ono, T.1    Imai, Y.2
  • 55
    • 0020476463 scopus 로고
    • Purification and partial characterization of squalene epoxidase from rat liver microsomes
    • Ono, T., Nakazono, K., Kosaka, H., Purification and partial characterization of squalene epoxidase from rat liver microsomes. Biochim. Biophys. Acta 1982, 709, 84-90.
    • (1982) Biochim. Biophys. Acta , vol.709 , pp. 84-90
    • Ono, T.1    Nakazono, K.2    Kosaka, H.3
  • 56
    • 0014939325 scopus 로고
    • Studies on squalene epoxidase of rat liver
    • Yamamoto, S., Bloch, K., Studies on squalene epoxidase of rat liver. J. Biol. Chem. 1970, 245, 1670-1674.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1670-1674
    • Yamamoto, S.1    Bloch, K.2
  • 57
    • 0037211467 scopus 로고    scopus 로고
    • Squalene epoxidase as hypocholesterolemic drug target revisited
    • Chugh, A., Ray, A., Gupta, J. B., Squalene epoxidase as hypocholesterolemic drug target revisited. Prog. Lipid Res. 2003, 42, 37-50.
    • (2003) Prog. Lipid Res. , vol.42 , pp. 37-50
    • Chugh, A.1    Ray, A.2    Gupta, J.B.3
  • 58
    • 0025651856 scopus 로고
    • Regulation of squalene epoxidase in HepG2 cells
    • Hidaka, Y., Satoh, T., Kamei, T., Regulation of squalene epoxidase in HepG2 cells. J. Lipid Res. 1990, 31, 2087-2094.
    • (1990) J. Lipid Res. , vol.31 , pp. 2087-2094
    • Hidaka, Y.1    Satoh, T.2    Kamei, T.3
  • 59
    • 1242329391 scopus 로고    scopus 로고
    • Mevalonate kinase is a cytosolic enzyme in humans
    • Hogenboom, S., Tuyp, J. J. M., Espeel, M., Koster, J., et al., Mevalonate kinase is a cytosolic enzyme in humans. J. Cell Sci. 2004, 117, 631-639.
    • (2004) J. Cell Sci. , vol.117 , pp. 631-639
    • Hogenboom, S.1    Tuyp, J.J.M.2    Espeel, M.3    Koster, J.4
  • 60
    • 1642547058 scopus 로고    scopus 로고
    • Phosphomevalonate kinase is a cytosolic protein in humans
    • Hogenboom, S., Tuyp, J. J. M., Espeel, M., Koster, J., et al., Phosphomevalonate kinase is a cytosolic protein in humans. J. Lipid Res. 2004, 45, 697-705.
    • (2004) J. Lipid Res. , vol.45 , pp. 697-705
    • Hogenboom, S.1    Tuyp, J.J.M.2    Espeel, M.3    Koster, J.4
  • 61
    • 0036018142 scopus 로고    scopus 로고
    • Central role of peroxisomes in isoprenoid biosynthesis
    • Kovacs, W. J., Olivier, L. M., Krisans, S. K., Central role of peroxisomes in isoprenoid biosynthesis. Prog. Lipid Res. 2002, 41, 369-391.
    • (2002) Prog. Lipid Res. , vol.41 , pp. 369-391
    • Kovacs, W.J.1    Olivier, L.M.2    Krisans, S.K.3
  • 62
    • 0346993671 scopus 로고    scopus 로고
    • Disturbed cholesterol homeostasis in a peroxisome-deficient PEX2 knockout mouse model
    • Kovacs, W. J., Shackelford, J. E., Tape, K. N., Richards, M. J., et al., Disturbed cholesterol homeostasis in a peroxisome-deficient PEX2 knockout mouse model. Mol. Cell. Biol. 2004, 24, 1-13.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1-13
    • Kovacs, W.J.1    Shackelford, J.E.2    Tape, K.N.3    Richards, M.J.4
  • 63
    • 33846991643 scopus 로고    scopus 로고
    • Localization of the pre-squalene segment of the isoprenoid biosynthetic pathway in mammalian peroxisomes
    • Kovacs, W. J., Tape, K. N., Shackelford, J. E., Duan, X. Y., et al., Localization of the pre-squalene segment of the isoprenoid biosynthetic pathway in mammalian peroxisomes. Histochem. Cell Biol. 2007, 127, 273-290.
    • (2007) Histochem. Cell Biol. , vol.127 , pp. 273-290
    • Kovacs, W.J.1    Tape, K.N.2    Shackelford, J.E.3    Duan, X.Y.4
  • 64
    • 0017274680 scopus 로고
    • Measurement of squalene in human tissues and plasma: Validation and application
    • Liu, G. C., Ahrens, E. H., Jr., Schreibman, P. H., Crouse, J. R., Measurement of squalene in human tissues and plasma: Validation and application. J. Lipid Res. 1976, 17, 38-45.
    • (1976) J. Lipid Res. , vol.17 , pp. 38-45
    • Liu, G.C.1    Ahrens Jr., E.H.2    Schreibman, P.H.3    Crouse, J.R.4
  • 65
    • 37549003700 scopus 로고    scopus 로고
    • Active components and clinical applications of olive oil
    • Waterman, E., Lockwood, B., Active components and clinical applications of olive oil. Altern. Med. Rev. 2007, 12, 331-342.
    • (2007) Altern. Med. Rev. , vol.12 , pp. 331-342
    • Waterman, E.1    Lockwood, B.2
  • 66
    • 0034309109 scopus 로고    scopus 로고
    • Olive-oil consumption and health: The possible role of antioxidants
    • Owen, R. W., Giacosa, A., Hull, W. E., Haubner, R., et al., Olive-oil consumption and health: The possible role of antioxidants. Lancet Oncol. 2000, 1, 107-112.
    • (2000) Lancet Oncol. , vol.1 , pp. 107-112
    • Owen, R.W.1    Giacosa, A.2    Hull, W.E.3    Haubner, R.4
  • 67
    • 70450176714 scopus 로고    scopus 로고
    • Cellular processes relying on sterol function in plants
    • Boutte, Y., Grebe, M., Cellular processes relying on sterol function in plants. Curr. Opin. Plant Biol. 2009, 12, 705-713.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 705-713
    • Boutte, Y.1    Grebe, M.2
  • 68
    • 0034657215 scopus 로고    scopus 로고
    • Plant sterols: Biosynthesis, biological function and their importance to human nutrition
    • Piironen, V., Lindsay, D. G., Miettinen, T. A., Toivo, J., et al., Plant sterols: Biosynthesis, biological function and their importance to human nutrition. J. Sci. Food Agr. 2000, 80, 939-966.
    • (2000) J. Sci. Food Agr. , vol.80 , pp. 939-966
    • Piironen, V.1    Lindsay, D.G.2    Miettinen, T.A.3    Toivo, J.4
  • 69
    • 27744577599 scopus 로고    scopus 로고
    • Biogenesis, molecular regulation and function of plant isoprenoids
    • Bouvier, F., Rahier, A., Camara, B., Biogenesis, molecular regulation and function of plant isoprenoids. Prog. Lipid Res. 2005, 44, 357-429.
    • (2005) Prog. Lipid Res. , vol.44 , pp. 357-429
    • Bouvier, F.1    Rahier, A.2    Camara, B.3
  • 70
    • 0000276203 scopus 로고
    • Plant membrane sterols: Isolation, identification and biosynthesis
    • Hartmann, M. A., Benveniste, P., Plant membrane sterols: Isolation, identification and biosynthesis. Methods Enzymol. 1987, 148, 632-650.
    • (1987) Methods Enzymol. , vol.148 , pp. 632-650
    • Hartmann, M.A.1    Benveniste, P.2
  • 72
    • 0041423608 scopus 로고    scopus 로고
    • Arabidopsis sterol endocytosis involves actin-mediated trafficking via ARA6-positive early endosomes
    • Grebe, M., Xu, J., Mobius, W., Ueda, T., et al., Arabidopsis sterol endocytosis involves actin-mediated trafficking via ARA6-positive early endosomes. Curr. Biol. 2003, 13, 1378-1387.
    • (2003) Curr. Biol. , vol.13 , pp. 1378-1387
    • Grebe, M.1    Xu, J.2    Mobius, W.3    Ueda, T.4
  • 74
    • 0031474261 scopus 로고    scopus 로고
    • Two independent biochemical pathways for isopentenyl diphosphate and isoprenoid biosynthesis in higher plants
    • Lichtenthaler, H. K., Rohmer, M., Schwender, J., Two independent biochemical pathways for isopentenyl diphosphate and isoprenoid biosynthesis in higher plants. Physiol. Plant. 1997, 101, 643-652.
    • (1997) Physiol. Plant. , vol.101 , pp. 643-652
    • Lichtenthaler, H.K.1    Rohmer, M.2    Schwender, J.3
  • 75
    • 0024869502 scopus 로고
    • Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Caelles, C., Ferrer, A., Balcells, L., Hegardt, F. G., et al., Isolation and structural characterization of a cDNA encoding Arabidopsis thaliana 3-hydroxy-3-methylglutaryl coenzyme A reductase. Plant Mol. Biol. 1989, 13, 627-638.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 627-638
    • Caelles, C.1    Ferrer, A.2    Balcells, L.3    Hegardt, F.G.4
  • 76
    • 0028147680 scopus 로고
    • Arabidopsis thaliana contains two differentially expressed 3-hydroxy-3-methylglutaryl-CoA reductase genes, which encode microsomal forms of the enzyme
    • Enjuto, M., Balcells, L., Campos, N., Caelles, C., et al., Arabidopsis thaliana contains two differentially expressed 3-hydroxy-3-methylglutaryl-CoA reductase genes, which encode microsomal forms of the enzyme. Proc. Natl. Acad. Sci. U. S. A 1994, 91, 927-931.
    • (1994) Proc. Natl. Acad. Sci. U. S. A , vol.91 , pp. 927-931
    • Enjuto, M.1    Balcells, L.2    Campos, N.3    Caelles, C.4
  • 77
    • 0028289750 scopus 로고
    • Regulation of HMG-CoA reductase activity in plants
    • Stermer, B. A., Bianchini, G. M., Korth, K. L., Regulation of HMG-CoA reductase activity in plants. J. Lipid Res. 1994, 35, 1133-1140.
    • (1994) J. Lipid Res. , vol.35 , pp. 1133-1140
    • Stermer, B.A.1    Bianchini, G.M.2    Korth, K.L.3
  • 78
    • 0029278035 scopus 로고
    • Features of the hmg1 subfamily of genes encoding HMG-CoA reductase in potato
    • Bhattacharyya, M. K., Paiva, N. L., Dixon, R. A., Korth, K. L., et al., Features of the hmg1 subfamily of genes encoding HMG-CoA reductase in potato. Plant Mol. Biol. 1995, 28, 1-15.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 1-15
    • Bhattacharyya, M.K.1    Paiva, N.L.2    Dixon, R.A.3    Korth, K.L.4
  • 79
    • 59049106449 scopus 로고    scopus 로고
    • Arabidopsis 3-hydroxy-3-methylglutaryl-CoA reductase is regulated at the post-translational level in response to alterations of the sphingolipid and the sterol biosynthetic pathways
    • Nieto, B., Fores, O., Arro, M., Ferrer, A., Arabidopsis 3-hydroxy-3-methylglutaryl-CoA reductase is regulated at the post-translational level in response to alterations of the sphingolipid and the sterol biosynthetic pathways. Phytochemistry 2009, 70, 53-59.
    • (2009) Phytochemistry , vol.70 , pp. 53-59
    • Nieto, B.1    Fores, O.2    Arro, M.3    Ferrer, A.4
  • 80
    • 10744224664 scopus 로고    scopus 로고
    • Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility, and reduced sterol levels
    • Suzuki, M., Kamide, Y., Nagata, N., Seki, H., et al., Loss of function of 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG1) in Arabidopsis leads to dwarfing, early senescence and male sterility, and reduced sterol levels. Plant J. 2004, 37, 750-761.
    • (2004) Plant J. , vol.37 , pp. 750-761
    • Suzuki, M.1    Kamide, Y.2    Nagata, N.3    Seki, H.4
  • 81
    • 66249123951 scopus 로고    scopus 로고
    • Complete blockage of the mevalonate pathway results in male gametophyte lethality
    • Suzuki, M., Nakagawa, S., Kamide, Y., Kobayashi, K., et al., Complete blockage of the mevalonate pathway results in male gametophyte lethality. J. Exp. Bot. 2009, 60, 2055-2064.
    • (2009) J. Exp. Bot. , vol.60 , pp. 2055-2064
    • Suzuki, M.1    Nakagawa, S.2    Kamide, Y.3    Kobayashi, K.4
  • 82
    • 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., Hartmann, M. A., Inhibition of squalene synthase and squalene epoxidase in tobacco cells triggers an up-regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Plant Physiol. 2002, 130, 334-346.
    • (2002) Plant Physiol. , vol.130 , pp. 334-346
    • Wentzinger, L.F.1    Bach, T.J.2    Hartmann, M.A.3
  • 83
    • 0029199868 scopus 로고
    • Expression of the Hevea brasiliensis (H.B.K.) mull. Arg. 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 in tobacco results in sterol overproduction
    • Schaller, H., Grausem, B., Benveniste, P., Chye, M. L., et al., Expression of the Hevea brasiliensis (H.B.K.) mull. Arg. 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 in tobacco results in sterol overproduction. Plant Physiol. 1995, 109, 761-770.
    • (1995) Plant Physiol. , vol.109 , pp. 761-770
    • Schaller, H.1    Grausem, B.2    Benveniste, P.3    Chye, M.L.4
  • 84
    • 26444516348 scopus 로고    scopus 로고
    • Characterization of the Arabidopsis clb6 mutant illustrates the importance of posttranscriptional regulation of the methyl-D-erythritol 4-phosphate pathway
    • Guevara-Garcia, A., San Roman, C., Arroyo, A., Cortes, M.E., et al., Characterization of the Arabidopsis clb6 mutant illustrates the importance of posttranscriptional regulation of the methyl-D-erythritol 4-phosphate pathway. Plant Cell 2005, 17, 628-643.
    • (2005) Plant Cell , vol.17 , pp. 628-643
    • Guevara-Garcia, A.1    San Roman, C.2    Arroyo, A.3    Cortes, M.E.4
  • 85
    • 4444264888 scopus 로고    scopus 로고
    • Rapid regulation of the methylerythritol 4-phosphate pathway during isoprene synthesis
    • Wolfertz, M., Sharkey, T. D., Boland, W., Kuhnemann, F., Rapid regulation of the methylerythritol 4-phosphate pathway during isoprene synthesis. Plant Physiol. 2004, 135, 1939-1945.
    • (2004) Plant Physiol. , vol.135 , pp. 1939-1945
    • Wolfertz, M.1    Sharkey, T.D.2    Boland, W.3    Kuhnemann, F.4
  • 86
    • 0030140330 scopus 로고    scopus 로고
    • CLA1, a novel gene required for chloroplast development, is highly conserved in evolution
    • Mandel, M. A., Feldmann, K. A., Herrera-Estrella, L., Rocha-Sosa, M., et al., CLA1, a novel gene required for chloroplast development, is highly conserved in evolution. Plant J. 1996, 9, 649-658.
    • (1996) Plant J. , vol.9 , pp. 649-658
    • Mandel, M.A.1    Feldmann, K.A.2    Herrera-Estrella, L.3    Rocha-Sosa, M.4
  • 87
    • 0034001256 scopus 로고    scopus 로고
    • Temperature-sensitive Arabidopsis mutant defective in 1-deoxy-D-xylulose 5-phosphate synthase within the plastid non-mevalonate pathway of isoprenoid biosynthesis
    • Araki, N., Kusumi, K., Masamoto, K., Niwa, Y., et al., Temperature-sensitive Arabidopsis mutant defective in 1-deoxy-D-xylulose 5-phosphate synthase within the plastid non-mevalonate pathway of isoprenoid biosynthesis. Physiol. Plant. 2000, 108, 19-24.
    • (2000) Physiol. Plant. , vol.108 , pp. 19-24
    • Araki, N.1    Kusumi, K.2    Masamoto, K.3    Niwa, Y.4
  • 88
    • 0033825557 scopus 로고    scopus 로고
    • Analysis of the expression of CLA1, a gene that encodes the 1-deoxyxylulose 5-phosphate synthase of the 2-C-methyl-D-erythritol-4-phosphate pathway in Arabidopsis
    • Estevez, J. M., Cantero, A., Romero, C., Kawaide, H., et al., Analysis of the expression of CLA1, a gene that encodes the 1-deoxyxylulose 5-phosphate synthase of the 2-C-methyl-D-erythritol-4-phosphate pathway in Arabidopsis. Plant Physiol. 2000, 124, 95-103.
    • (2000) Plant Physiol. , vol.124 , pp. 95-103
    • Estevez, J.M.1    Cantero, A.2    Romero, C.3    Kawaide, H.4
  • 89
    • 0036851226 scopus 로고    scopus 로고
    • Elucidation of the methylerythritol phosphate pathway for isoprenoid biosynthesis in bacteria and plastids. A metabolic milestone achieved through genomics
    • Rodriguez-Concepcion, M., Boronat, A., Elucidation of the methylerythritol phosphate pathway for isoprenoid biosynthesis in bacteria and plastids. A metabolic milestone achieved through genomics. Plant Physiol. 2002, 130, 1079-1089.
    • (2002) Plant Physiol. , vol.130 , pp. 1079-1089
    • Rodriguez-Concepcion, M.1    Boronat, A.2
  • 90
    • 2442706819 scopus 로고    scopus 로고
    • Chloroplast biogenesis genes act cell and noncell autonomously in early chloroplast development
    • Gutierrez-Nava, M. D. L., Gillmor, C. S., Jimenez, L. F., Guevara-Garcia, A., et al., Chloroplast biogenesis genes act cell and noncell autonomously in early chloroplast development. Plant Physiol. 2004, 135, 471-482.
    • (2004) Plant Physiol. , vol.135 , pp. 471-482
    • Gutierrez-Nava, M.D.L.1    Gillmor, C.S.2    Jimenez, L.F.3    Guevara-Garcia, A.4
  • 91
    • 0035697442 scopus 로고    scopus 로고
    • Arabidopsis genes essential for seedling viability: Isolation of Insertional mutants and molecular cloning
    • Budziszewski, G. J., Lewis, S. P., Glover, L. W., Reineke, J., et al., Arabidopsis genes essential for seedling viability: Isolation of Insertional mutants and molecular cloning. Genetics 2001, 159, 1765-1778.
    • (2001) Genetics , vol.159 , pp. 1765-1778
    • Budziszewski, G.J.1    Lewis, S.P.2    Glover, L.W.3    Reineke, J.4
  • 92
    • 0029868992 scopus 로고    scopus 로고
    • Arabidopsis thaliana contains two differentially expressed farnesyl-diphosphate synthase genes
    • Cunillera, N., Arro, M., Delourme, D., Karst, F., et al., Arabidopsis thaliana contains two differentially expressed farnesyl-diphosphate synthase genes. J. Biol. Chem. 1996, 271, 7774-7780.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7774-7780
    • Cunillera, N.1    Arro, M.2    Delourme, D.3    Karst, F.4
  • 93
    • 0030919438 scopus 로고    scopus 로고
    • The Arabidopsis thaliana FPS1 gene generates a novel mRNA that encodes a mitochondrial farnesyl-diphosphate synthase isoform
    • Cunillera, N., Boronat, A., Ferrer, A., The Arabidopsis thaliana FPS1 gene generates a novel mRNA that encodes a mitochondrial farnesyl-diphosphate synthase isoform. J. Biol. Chem. 1997, 272, 15381-15388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15381-15388
    • Cunillera, N.1    Boronat, A.2    Ferrer, A.3
  • 94
    • 77954946628 scopus 로고    scopus 로고
    • The Arabidopsis thaliana FPP synthase isozymes have overlapping and specific functions in isoprenoid biosynthesis, and complete loss of FPP synthase activity causes early developmental arrest
    • Closa, M., Vranova, E., Bortolotti, C., Bigler, L., et al., The Arabidopsis thaliana FPP synthase isozymes have overlapping and specific functions in isoprenoid biosynthesis, and complete loss of FPP synthase activity causes early developmental arrest. Plant J. 2010, 63, 512-525.
    • (2010) Plant J. , vol.63 , pp. 512-525
    • Closa, M.1    Vranova, E.2    Bortolotti, C.3    Bigler, L.4
  • 95
    • 0035999890 scopus 로고    scopus 로고
    • Overexpression of Arabidopsis thaliana farnesyl diphosphate synthase (FPS1S) in transgenic Arabidopsis induces a cell death/senescence-like response and reduced cytokinin levels
    • Masferrer, A., Arro, M., Manzano, D., Schaller, H., et al., Overexpression of Arabidopsis thaliana farnesyl diphosphate synthase (FPS1S) in transgenic Arabidopsis induces a cell death/senescence-like response and reduced cytokinin levels. Plant J. 2002, 30, 123-132.
    • (2002) Plant J. , vol.30 , pp. 123-132
    • Masferrer, A.1    Arro, M.2    Manzano, D.3    Schaller, H.4
  • 96
    • 0001393445 scopus 로고    scopus 로고
    • Expression of the farnesyldiphosphate synthase gene of Saccharomyces cerevisiae in tobacco
    • Daudonnet, S., Karst, F., Tourte, Y., Expression of the farnesyldiphosphate synthase gene of Saccharomyces cerevisiae in tobacco. Mol. Breeding 1997, 3, 137-145.
    • (1997) Mol. Breeding , vol.3 , pp. 137-145
    • Daudonnet, S.1    Karst, F.2    Tourte, Y.3
  • 97
    • 0002869606 scopus 로고
    • Biosynthesis of non-head-to-tail terpenes. Formation of 1'-1 and 1'-3 linkages
    • Poulter, C. D., Biosynthesis of non-head-to-tail terpenes. Formation of 1'-1 and 1'-3 linkages. Acc. Chem. Res. 1990, 23, 70-77.
    • (1990) Acc. Chem. Res. , vol.23 , pp. 70-77
    • Poulter, C.D.1
  • 98
    • 0030613753 scopus 로고    scopus 로고
    • Cloning and characterization of the Arabidopsis thaliana SQS1 gene encoding squalene synthase-involvement of the C-terminal region of the enzyme in the channeling of squalene through the sterol pathway
    • Kribii, R., Arro, M., del Arco, A., Gonzalez, V., et al., Cloning and characterization of the Arabidopsis thaliana SQS1 gene encoding squalene synthase-involvement of the C-terminal region of the enzyme in the channeling of squalene through the sterol pathway. Eur. J. Biochem. 1997, 249, 61-69.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 61-69
    • Kribii, R.1    Arro, M.2    del Arco, A.3    Gonzalez, V.4
  • 99
    • 42149084450 scopus 로고    scopus 로고
    • Arabidopsis thaliana contains a single gene encoding squalene synthase
    • Busquets, A., Keim, V., Closa, M., del Arco, A., et al., Arabidopsis thaliana contains a single gene encoding squalene synthase. Plant Mol. Biol. 2008, 67, 25-36.
    • (2008) Plant Mol. Biol. , vol.67 , pp. 25-36
    • Busquets, A.1    Keim, V.2    Closa, M.3    del Arco, A.4
  • 100
    • 0026635536 scopus 로고
    • Squalestatin 1, a potent inhibitor of squalene synthase, which lowers serum cholesterol in vivo
    • Baxter, A., Fitzgerald, B. J., Hutson, J. L., McCarthy, A. D., et al., Squalestatin 1, a potent inhibitor of squalene synthase, which lowers serum cholesterol in vivo. J. Biol. Chem. 1992, 267, 11705-11708.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11705-11708
    • Baxter, A.1    Fitzgerald, B.J.2    Hutson, J.L.3    McCarthy, A.D.4
  • 101
    • 34447117580 scopus 로고    scopus 로고
    • Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development
    • Rasbery, J. M., Shan, H., LeClair, R. J., Norman, M., et al., Arabidopsis thaliana squalene epoxidase 1 is essential for root and seed development. J. Biol. Chem. 2007, 282, 17002-17013.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17002-17013
    • Rasbery, J.M.1    Shan, H.2    LeClair, R.J.3    Norman, M.4
  • 102
    • 67649482618 scopus 로고    scopus 로고
    • Identification of the Arabidopsis dry2/sqe 1-5 mutant reveals a central role for sterols in drought tolerance and regulation of reactive oxygen species
    • Pose, D., Castanedo, I., Borsani, O., Nieto, B., et al., Identification of the Arabidopsis dry2/sqe 1-5 mutant reveals a central role for sterols in drought tolerance and regulation of reactive oxygen species. Plant J. 2009, 59, 63-76.
    • (2009) Plant J. , vol.59 , pp. 63-76
    • Pose, D.1    Castanedo, I.2    Borsani, O.3    Nieto, B.4
  • 103
    • 33644794386 scopus 로고    scopus 로고
    • Transcription factor families have much higher expansion rates in plants than in animals
    • Shiu, S. H., Shih, M. C., Li, W. H., Transcription factor families have much higher expansion rates in plants than in animals. Plant Physiol. 2005, 139, 18-26.
    • (2005) Plant Physiol. , vol.139 , pp. 18-26
    • Shiu, S.H.1    Shih, M.C.2    Li, W.H.3
  • 104
    • 2442591728 scopus 로고    scopus 로고
    • Comparative analysis of the receptor-like kinase family in Arabidopsis and rice
    • Shiu, S. H., Karlowski, W. M., Pan, R., Tzeng, Y. H., et al., Comparative analysis of the receptor-like kinase family in Arabidopsis and rice. Plant Cell 2004, 16, 1220-1234.
    • (2004) Plant Cell , vol.16 , pp. 1220-1234
    • Shiu, S.H.1    Karlowski, W.M.2    Pan, R.3    Tzeng, Y.H.4
  • 105
    • 0027484782 scopus 로고
    • Influence of fermentation conditions on specific activity of the enzymes alcohol and aldehyde dehydrogenase from yeasts
    • Mauricio, J. C., Ortega, J. M., Influence of fermentation conditions on specific activity of the enzymes alcohol and aldehyde dehydrogenase from yeasts. Microbios 1993, 75, 95-106.
    • (1993) Microbios , vol.75 , pp. 95-106
    • Mauricio, J.C.1    Ortega, J.M.2
  • 106
    • 0014286661 scopus 로고
    • Biogenesis of mitochondria. 3. Lipid composition of aerobically and anaerobically grown Saccharomyces cerevisiae as related to membrane systems of cells
    • Jollow, D., Kellerma, G. M., Linnane, A. W., Biogenesis of mitochondria. 3. Lipid composition of aerobically and anaerobically grown Saccharomyces cerevisiae as related to membrane systems of cells. J. Cell Biol. 1968, 37, 221-230.
    • (1968) J. Cell Biol. , vol.37 , pp. 221-230
    • Jollow, D.1    Kellerma, G.M.2    Linnane, A.W.3
  • 107
    • 0028004134 scopus 로고
    • Construction of squalene-accumulating Saccharomyces cerevisiae mutants by gene disruption through homologous recombination
    • Kamimura, K., Hidaka, M., Masaki, H., Uozumi, T., Construction of squalene-accumulating Saccharomyces cerevisiae mutants by gene disruption through homologous recombination. Appl. Microbiol. Biotechnol. 1994, 42, 353-357.
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 353-357
    • Kamimura, K.1    Hidaka, M.2    Masaki, H.3    Uozumi, T.4
  • 108
    • 0028879103 scopus 로고
    • In vitro yeast (Saccharomyces cerevisiae) presqualene and squalene synthesis related to substrate and cofactor availability
    • Socaciu, C., Faye, M., Salin, F., Pauly, G., et al., In vitro yeast (Saccharomyces cerevisiae) presqualene and squalene synthesis related to substrate and cofactor availability. Compt. Rendus Acad. Sci. III Sci. Vie. 1995, 318, 919-926.
    • (1995) Compt. Rendus Acad. Sci. III Sci. Vie. , vol.318 , pp. 919-926
    • Socaciu, C.1    Faye, M.2    Salin, F.3    Pauly, G.4
  • 109
    • 0001904922 scopus 로고    scopus 로고
    • Effect of ethanol on fermentation and lipid composition in Saccharomyces cerevisiae
    • Ciesarova, Z., Sajbidor, J., Smogrovicova, D., Bafrncova, P., Effect of ethanol on fermentation and lipid composition in Saccharomyces cerevisiae. Food Biotechnol. 1996, 10, 1-12.
    • (1996) Food Biotechnol. , vol.10 , pp. 1-12
    • Ciesarova, Z.1    Sajbidor, J.2    Smogrovicova, D.3    Bafrncova, P.4
  • 111
    • 0008039028 scopus 로고
    • Bacterial production of squalene
    • Uragami, S., Koga, S., Bacterial production of squalene. Jpn. Appl. Pub. 61, 290. 1986.
    • (1986) Jpn. Appl. Pub. , vol.61 , pp. 290
    • Uragami, S.1    Koga, S.2
  • 114
    • 0036374868 scopus 로고    scopus 로고
    • Oxidative stability of polyunsaturated fatty acids: Effect of squalene
    • Dessi, M. A., Deiana, M., Day, B. W., Rosa, A., et al., Oxidative stability of polyunsaturated fatty acids: Effect of squalene. Eur. J. Lipid Sci. Technol. 2002, 104, 506-512.
    • (2002) Eur. J. Lipid Sci. Technol. , vol.104 , pp. 506-512
    • Dessi, M.A.1    Deiana, M.2    Day, B.W.3    Rosa, A.4
  • 115
    • 1542317132 scopus 로고    scopus 로고
    • Fatty acid composition and squalene content of the marine microalga Schizochytrium mangrovei
    • Jiang, Y., Fan, K. W., Wong, R. D. Y., Chen, F., Fatty acid composition and squalene content of the marine microalga Schizochytrium mangrovei. J. Agric. Food Chem. 2004, 52, 1196-1200.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1196-1200
    • Jiang, Y.1    Fan, K.W.2    Wong, R.D.Y.3    Chen, F.4
  • 116
    • 67349157741 scopus 로고    scopus 로고
    • Impact of methyl jasmonate on squalene biosynthesis in microalga Schizochytrium mangrovei
    • Yue, C. J., Jiang, Y., Impact of methyl jasmonate on squalene biosynthesis in microalga Schizochytrium mangrovei. Process Biochem. 2009, 44, 923-927.
    • (2009) Process Biochem. , vol.44 , pp. 923-927
    • Yue, C.J.1    Jiang, Y.2
  • 117
    • 0036407352 scopus 로고    scopus 로고
    • Botryococcus braunii: A renewable source of hydrocarbons and other chemicals
    • Banerjee, A., Sharma, R., Chisti, Y., Banerjee, U. C., Botryococcus braunii: A renewable source of hydrocarbons and other chemicals. Crit. Rev. Biotechnol. 2002, 22, 245-279.
    • (2002) Crit. Rev. Biotechnol. , vol.22 , pp. 245-279
    • Banerjee, A.1    Sharma, R.2    Chisti, Y.3    Banerjee, U.C.4
  • 119
    • 0034700150 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes
    • Lange, B. M., Rujan, T., Martin, W., Croteau, R., Isoprenoid biosynthesis: The evolution of two ancient and distinct pathways across genomes. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 13172-13177.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13172-13177
    • Lange, B.M.1    Rujan, T.2    Martin, W.3    Croteau, R.4
  • 120
    • 0032512051 scopus 로고    scopus 로고
    • The genome sequence of Rickettsia prowazekii and the origin of mitochondria
    • Andersson, S. G. E., Zomorodipour, A., Andersson, J. O., Sicheritz-Ponten, T., et al., The genome sequence of Rickettsia prowazekii and the origin of mitochondria. Nature 1998, 396, 133-140.
    • (1998) Nature , vol.396 , pp. 133-140
    • Andersson, S.G.E.1    Zomorodipour, A.2    Andersson, J.O.3    Sicheritz-Ponten, T.4
  • 121
    • 0028829125 scopus 로고
    • The minimal gene complement of Mycoplasma genitalium
    • Fraser, C. M., Gocayne, J. D., White, O., Adams, M. D., et al., The minimal gene complement of Mycoplasma genitalium. Science 1995, 270, 397-403.
    • (1995) Science , vol.270 , pp. 397-403
    • Fraser, C.M.1    Gocayne, J.D.2    White, O.3    Adams, M.D.4
  • 122
    • 34547609909 scopus 로고    scopus 로고
    • The non-mevalonate pathway of isoprenoid precursor biosynthesis
    • Hunter, W. N., The non-mevalonate pathway of isoprenoid precursor biosynthesis. J. Biol. Chem. 2007, 282, 21573-21577.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21573-21577
    • Hunter, W.N.1
  • 123
    • 0033859551 scopus 로고    scopus 로고
    • The role of lateral gene transfer in the evolution of isoprenoid biosynthesis pathways
    • Boucher, Y., Doolittle, W. F., The role of lateral gene transfer in the evolution of isoprenoid biosynthesis pathways. Mol. Microbiol. 2000, 37, 703-716.
    • (2000) Mol. Microbiol. , vol.37 , pp. 703-716
    • Boucher, Y.1    Doolittle, W.F.2
  • 124
    • 0033057722 scopus 로고    scopus 로고
    • Expression of prokaryotic 1-deoxy-D-xylulose-5-phosphatases in Escherichia coli increases carotenoid and ubiquinone biosynthesis
    • Harker, M., Bramley, P. M., Expression of prokaryotic 1-deoxy-D-xylulose-5-phosphatases in Escherichia coli increases carotenoid and ubiquinone biosynthesis. FEBS Lett. 1999, 448, 115-119.
    • (1999) FEBS Lett. , vol.448 , pp. 115-119
    • Harker, M.1    Bramley, P.M.2
  • 125
    • 0033985493 scopus 로고    scopus 로고
    • Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis
    • Kuzuyama, T., Takagi, M., Takahashi, S., Seto, H., Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis. J. Bacteriol. 2000, 182, 891-897.
    • (2000) J. Bacteriol. , vol.182 , pp. 891-897
    • Kuzuyama, T.1    Takagi, M.2    Takahashi, S.3    Seto, H.4
  • 126
    • 0034105938 scopus 로고    scopus 로고
    • Metabolic engineering of carotenoid accumulation in Escherichia coli by modulation of the isoprenoid precursor pool with expression of deoxyxylulose phosphate synthase
    • Matthews, P. D., Wurtzel, E. T., Metabolic engineering of carotenoid accumulation in Escherichia coli by modulation of the isoprenoid precursor pool with expression of deoxyxylulose phosphate synthase. Appl. Microbiol. Biotechnol. 2000, 53, 396-400.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 396-400
    • Matthews, P.D.1    Wurtzel, E.T.2
  • 127
    • 0032731682 scopus 로고    scopus 로고
    • A Synechococcus leopoliensis SAUG 1402-1 operon harboring the 1-deoxyxylulose 5-phosphate synthase gene and two additional open reading frames is functionally involved in the dimethylallyl diphosphate synthesis
    • Miller, B., Heuser, T., Zimmer, W., A Synechococcus leopoliensis SAUG 1402-1 operon harboring the 1-deoxyxylulose 5-phosphate synthase gene and two additional open reading frames is functionally involved in the dimethylallyl diphosphate synthesis. FEBS Lett. 1999, 460, 485-490.
    • (1999) FEBS Lett. , vol.460 , pp. 485-490
    • Miller, B.1    Heuser, T.2    Zimmer, W.3
  • 128
    • 0034703371 scopus 로고    scopus 로고
    • Functional involvement of a deoxy-D-xylulose 5-phosphate reductoisomerase gene harboring locus of Synechococcus leopoliensis in isoprenoid biosynthesis
    • Miller, B., Heuser, T., Zimmer, W., Functional involvement of a deoxy-D-xylulose 5-phosphate reductoisomerase gene harboring locus of Synechococcus leopoliensis in isoprenoid biosynthesis. FEBS Lett. 2000, 481, 221-226.
    • (2000) FEBS Lett. , vol.481 , pp. 221-226
    • Miller, B.1    Heuser, T.2    Zimmer, W.3
  • 129
    • 0037010723 scopus 로고    scopus 로고
    • Fructose 6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars
    • Schurmann, M., Schurmann, M., Sprenger, G. A., Fructose 6-phosphate aldolase and 1-deoxy-D-xylulose 5-phosphate synthase from Escherichia coli as tools in enzymatic synthesis of 1-deoxysugars. Mol. Catal. B Enzym. 2002, 19, 247-252.
    • (2002) Mol. Catal. B Enzym. , vol.19 , pp. 247-252
    • Schurmann, M.1    Schurmann, M.2    Sprenger, G.A.3
  • 130
    • 77956282463 scopus 로고    scopus 로고
    • A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria
    • Sangari, F. J., Perez-Gil, J., Carretero-Paulet, L., Garcia-Lobo, J. M., et al., A new family of enzymes catalyzing the first committed step of the methylerythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in bacteria. Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 14081-14086.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14081-14086
    • Sangari, F.J.1    Perez-Gil, J.2    Carretero-Paulet, L.3    Garcia-Lobo, J.M.4
  • 131
    • 0036724815 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis in Synechocystis sp strain PCC6803 is stimulated by compounds of the pentose phosphate cycle but not by pyruvate or deoxyxylulose-5-phosphate
    • Ershov, Y. V., Gantt, R. R., Cunningham, F. X., Gantt, E., Isoprenoid biosynthesis in Synechocystis sp strain PCC6803 is stimulated by compounds of the pentose phosphate cycle but not by pyruvate or deoxyxylulose-5-phosphate. J. Bacteriol. 2002, 184, 5045-5051.
    • (2002) J. Bacteriol. , vol.184 , pp. 5045-5051
    • Ershov, Y.V.1    Gantt, R.R.2    Cunningham, F.X.3    Gantt, E.4
  • 132
    • 3042732189 scopus 로고    scopus 로고
    • Inactivation of sll1556 in Synechocystis strain PCC 6803 impairs isoprenoid biosynthesis from pentose phosphate cycle substrates in vitro
    • Poliquin, K., Ershov, Y. V., Cunningham, F. X., Woreta, T. T., et al., Inactivation of sll1556 in Synechocystis strain PCC 6803 impairs isoprenoid biosynthesis from pentose phosphate cycle substrates in vitro. J. Bacteriol. 2004, 186, 4685-4693.
    • (2004) J. Bacteriol. , vol.186 , pp. 4685-4693
    • Poliquin, K.1    Ershov, Y.V.2    Cunningham, F.X.3    Woreta, T.T.4
  • 133
    • 0035970116 scopus 로고    scopus 로고
    • An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp. strain CL190
    • Kaneda, K., Kuzuyama, T., Takagi, M., Hayakawa, Y., et al., An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp. strain CL190. Proc. Natl. Acad. Sci. U.S.A 2001, 98, 932-937.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 932-937
    • Kaneda, K.1    Kuzuyama, T.2    Takagi, M.3    Hayakawa, Y.4
  • 134
    • 27744599634 scopus 로고    scopus 로고
    • Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics
    • de Ruyck, J., Rothman, S. C., Poulter, C. D., Wouters, J., Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics. Biochem. Biophys. Res. Commun. 2005, 338, 1515-1518.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1515-1518
    • de Ruyck, J.1    Rothman, S.C.2    Poulter, C.D.3    Wouters, J.4
  • 135
    • 0037868855 scopus 로고    scopus 로고
    • Crystal structure of the type II isopentenyl diphosphate: Dimethylallyl diphosphate isomerase from Bacillus subtilis
    • Steinbacher, S., Kaiser, J., Gerhardt, S., Eisenreich, W., et al., Crystal structure of the type II isopentenyl diphosphate: Dimethylallyl diphosphate isomerase from Bacillus subtilis. J. Mol. Biol. 2003, 329, 973-982.
    • (2003) J. Mol. Biol. , vol.329 , pp. 973-982
    • Steinbacher, S.1    Kaiser, J.2    Gerhardt, S.3    Eisenreich, W.4
  • 136
    • 0027234835 scopus 로고
    • Isoprenoid biosynthesis in bacteria - 2 different pathways
    • Horbach, S., Sahm, H., Welle, R., Isoprenoid biosynthesis in bacteria - 2 different pathways. FEMS Microbiol. Lett. 1993, 111, 135-140.
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 135-140
    • Horbach, S.1    Sahm, H.2    Welle, R.3
  • 137
    • 0000191166 scopus 로고
    • Regularity of isoprenoid biosynthesis in the ether lipids of archaebacteria
    • Derosa, M., Gambacorta, A., Nicolaus, B., Regularity of isoprenoid biosynthesis in the ether lipids of archaebacteria. Phytochemistry 1980, 19, 791-793.
    • (1980) Phytochemistry , vol.19 , pp. 791-793
    • Derosa, M.1    Gambacorta, A.2    Nicolaus, B.3
  • 138
    • 0031691311 scopus 로고    scopus 로고
    • Studies on the biosynthesis of terpenoid compounds produced by actinomycetes - 3. Biosynthesis of the isoprenoid side chain of novobiocin via the non-mevalonate pathway in Streptomyces niveus
    • Orihara, N., Kuzuyama, T., Takahashi, S., Furihata, K., et al., Studies on the biosynthesis of terpenoid compounds produced by actinomycetes - 3. Biosynthesis of the isoprenoid side chain of novobiocin via the non-mevalonate pathway in Streptomyces niveus. J. Antibiot. 1998, 51, 676-678.
    • (1998) J. Antibiot. , vol.51 , pp. 676-678
    • Orihara, N.1    Kuzuyama, T.2    Takahashi, S.3    Furihata, K.4
  • 139
    • 0032542140 scopus 로고    scopus 로고
    • Studies on the biosynthesis of terpenoids produced by actinomycetes. Part 4. Formation of BE-40644 by the mevalonate and nonmevalonate pathways
    • Seto, H., Orihara, N., Furihata, K., Studies on the biosynthesis of terpenoids produced by actinomycetes. Part 4. Formation of BE-40644 by the mevalonate and nonmevalonate pathways. Tetrahedron Lett. 1998, 39, 9497-9500.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 9497-9500
    • Seto, H.1    Orihara, N.2    Furihata, K.3
  • 140
    • 0030605182 scopus 로고    scopus 로고
    • Simultaneous operation of the mevalonate and non-mevalonate pathways in the biosynthesis of isopentenyl diphosphate in Streptomyces aeriouvifer
    • Seto, H., Watanabe, H., Furihata, K., Simultaneous operation of the mevalonate and non-mevalonate pathways in the biosynthesis of isopentenyl diphosphate in Streptomyces aeriouvifer. Tetrahedron Lett. 1996, 37, 7979-7982.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 7979-7982
    • Seto, H.1    Watanabe, H.2    Furihata, K.3
  • 141
    • 44349097602 scopus 로고    scopus 로고
    • Cloning, solubilization, and characterization of squalene synthase from Thermosynechococcus elongatus BP-1
    • Lee, S., Poulter, C. D., Cloning, solubilization, and characterization of squalene synthase from Thermosynechococcus elongatus BP-1. J. Bacteriol. 2008, 190, 3808-3816.
    • (2008) J. Bacteriol. , vol.190 , pp. 3808-3816
    • Lee, S.1    Poulter, C.D.2
  • 142
    • 0023515798 scopus 로고
    • Prokaryotic hopanoids and other polyterpenoid sterol surrogates
    • Ourisson, G., Rohmer, M., Poralla, K., Prokaryotic hopanoids and other polyterpenoid sterol surrogates. Ann. Rev. Microbiol. 1987, 41, 301-333.
    • (1987) Ann. Rev. Microbiol. , vol.41 , pp. 301-333
    • Ourisson, G.1    Rohmer, M.2    Poralla, K.3
  • 143
    • 0032943554 scopus 로고    scopus 로고
    • Hopanoid biosynthesis and function in bacteria
    • Kannenberg, E. L., Poralla, K., Hopanoid biosynthesis and function in bacteria. Naturwissenschaften 1999, 86, 168-176.
    • (1999) Naturwissenschaften , vol.86 , pp. 168-176
    • Kannenberg, E.L.1    Poralla, K.2
  • 144
    • 70349088644 scopus 로고    scopus 로고
    • Hopanoids play a role in membrane integrity and pH homeostasis in Rhodopseudomonas palustris TIE-1
    • Welander, P. V., Hunter, R. C., Zhang, L., Sessions, A. L., et al., Hopanoids play a role in membrane integrity and pH homeostasis in Rhodopseudomonas palustris TIE-1. J. Bacteriol. 2009, 191, 6145-6156.
    • (2009) J. Bacteriol. , vol.191 , pp. 6145-6156
    • Welander, P.V.1    Hunter, R.C.2    Zhang, L.3    Sessions, A.L.4
  • 145
    • 0025730267 scopus 로고
    • Effect of azasqualene on hopanoid biosynthesis and ethanol tolerance of Zymomonas mobilis
    • Horbach, S., Neuss, B., Sahm, H., Effect of azasqualene on hopanoid biosynthesis and ethanol tolerance of Zymomonas mobilis. FEMS Microbiol. Lett. 1991, 79, 347-350.
    • (1991) FEMS Microbiol. Lett. , vol.79 , pp. 347-350
    • Horbach, S.1    Neuss, B.2    Sahm, H.3
  • 146
    • 0027176916 scopus 로고
    • Hopanoid lipids compose the Frankia vesicle envelope, presumptive barrier of oxygen diffusion to nitrogenase. Proc
    • Berry, A. M., Harriott, O. T., Moreau, R. A., Osman, S. F., et al., Hopanoid lipids compose the Frankia vesicle envelope, presumptive barrier of oxygen diffusion to nitrogenase. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 6091-6094.
    • (1993) Natl. Acad. Sci. U.S.A. , vol.90 , pp. 6091-6094
    • Berry, A.M.1    Harriott, O.T.2    Moreau, R.A.3    Osman, S.F.4
  • 147
    • 0034255872 scopus 로고    scopus 로고
    • Hopanoids are formed during transition from substrate to aerial hyphae in Streptomyces coelicolor A3(2)
    • Poralla, K., Muth, G., Hartner, T., Hopanoids are formed during transition from substrate to aerial hyphae in Streptomyces coelicolor A3(2). FEMS Microbiol. Lett. 2000, 189, 93-95.
    • (2000) FEMS Microbiol. Lett. , vol.189 , pp. 93-95
    • Poralla, K.1    Muth, G.2    Hartner, T.3
  • 148
    • 0019131757 scopus 로고
    • Nonspecific lanosterol and hopanoid biosynthesis by a cell-free system from the bacterium Methylococcus capsulatus
    • Rohmer, M., Bouvier, P., Ourisson, G., Nonspecific lanosterol and hopanoid biosynthesis by a cell-free system from the bacterium Methylococcus capsulatus. Eur. J. Biochem. 1980, 112, 557-560.
    • (1980) Eur. J. Biochem. , vol.112 , pp. 557-560
    • Rohmer, M.1    Bouvier, P.2    Ourisson, G.3
  • 149
    • 0037238414 scopus 로고    scopus 로고
    • Steroid biosynthesis in prokaryotes: Identification of myxobacterial steroids and cloning of the first bacterial 2,3(S)-oxidosqualene cyclase from the myxobacterium Stigmatella aurantiaca
    • Bode, H. B., Zeggel, B., Silakowski, B., Wenzel, S. C., et al., Steroid biosynthesis in prokaryotes: Identification of myxobacterial steroids and cloning of the first bacterial 2, 3(S)-oxidosqualene cyclase from the myxobacterium Stigmatella aurantiaca. Mol. Microbiol. 2003, 47, 471-481.
    • (2003) Mol. Microbiol. , vol.47 , pp. 471-481
    • Bode, H.B.1    Zeggel, B.2    Silakowski, B.3    Wenzel, S.C.4
  • 150
    • 34547781221 scopus 로고    scopus 로고
    • Lanosterol biosynthesis in the prokaryote Methylococcus capsulatus: Insight into the evolution of sterol biosynthesis
    • Lamb, D. C., Jackson, C. J., Warrilow, A. G. S., Manning, N. J., et al., Lanosterol biosynthesis in the prokaryote Methylococcus capsulatus: Insight into the evolution of sterol biosynthesis. Mol. Biol. Evol. 2007, 24, 1714-1721.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1714-1721
    • Lamb, D.C.1    Jackson, C.J.2    Warrilow, A.G.S.3    Manning, N.J.4
  • 151
    • 0000165492 scopus 로고
    • Hydration of squalene and oleic acid by Corynebacterium Sp S-401
    • Seo, C. W., Yamada, Y., Takada, N., Okada, H., Hydration of squalene and oleic acid by Corynebacterium Sp S-401. Agric. Biol. Chem. 1981, 45, 2025-2030.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 2025-2030
    • Seo, C.W.1    Yamada, Y.2    Takada, N.3    Okada, H.4
  • 152
    • 0020660935 scopus 로고
    • Microbial transformation of squalene - terminal methyl group oxidation by Corynebacterium sp
    • Seo, C. W., Yamada, Y., Takada, N., Okada, H., Microbial transformation of squalene - terminal methyl group oxidation by Corynebacterium sp. Appl. Environ. Microbiol. 1983, 45, 522-525.
    • (1983) Appl. Environ. Microbiol. , vol.45 , pp. 522-525
    • Seo, C.W.1    Yamada, Y.2    Takada, N.3    Okada, H.4
  • 153
    • 0032953353 scopus 로고    scopus 로고
    • Corynebacterium terpenotabidum sp. nov., a bacterium capable of degrading squalene
    • Takeuchi, M., Sakane, T., Nihira, T., Yamada, Y., et al., Corynebacterium terpenotabidum sp. nov., a bacterium capable of degrading squalene. Int. J. Syst. Bacteriol. 1999, 49, 223-229.
    • (1999) Int. J. Syst. Bacteriol. , vol.49 , pp. 223-229
    • Takeuchi, M.1    Sakane, T.2    Nihira, T.3    Yamada, Y.4
  • 154
    • 0021943912 scopus 로고
    • Microbial transformation of squalene - Formation of a novel ketone from squalene by a Rhodococcus Sp
    • Setchell, C. H., Bonner, J. F., Wright, S. J., Caunt, P., et al., Microbial transformation of squalene - Formation of a novel ketone from squalene by a Rhodococcus Sp. Appl. Microbiol. Biotechnol. 1985, 21, 255-257.
    • (1985) Appl. Microbiol. Biotechnol. , vol.21 , pp. 255-257
    • Setchell, C.H.1    Bonner, J.F.2    Wright, S.J.3    Caunt, P.4
  • 155
    • 0017847283 scopus 로고
    • Biodegradation of acyclic isoprenoids by Pseudomonas species
    • Cantwell, S. G., Lau, E. P., Watt, D. S., Fall, R. R., Biodegradation of acyclic isoprenoids by Pseudomonas species. J. Bacteriol. 1978, 135, 324-333.
    • (1978) J. Bacteriol. , vol.135 , pp. 324-333
    • Cantwell, S.G.1    Lau, E.P.2    Watt, D.S.3    Fall, R.R.4
  • 156
    • 0016609393 scopus 로고
    • Oxidative degradation of squalene by Arthrobacter species
    • Yamada, Y., Motoi, H., Kinoshita, S., Takada, N., et al., Oxidative degradation of squalene by Arthrobacter species. Appl. Microbiol. 1975, 29, 400-404.
    • (1975) Appl. Microbiol. , vol.29 , pp. 400-404
    • Yamada, Y.1    Motoi, H.2    Kinoshita, S.3    Takada, N.4
  • 157
    • 0017328647 scopus 로고
    • Oxidation of linear terpenes and squalene variants by Arthrobacter sp
    • Yamada, Y., Kusuhara, N., Okada, H., Oxidation of linear terpenes and squalene variants by Arthrobacter sp. Appl. Environ. Microbiol. 1977, 33, 771-776.
    • (1977) Appl. Environ. Microbiol. , vol.33 , pp. 771-776
    • Yamada, Y.1    Kusuhara, N.2    Okada, H.3
  • 158
    • 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., Bonin, P., Aerobic and anaerobic metabolism of squalene by a denitrifying bacterium isolated from marine sediment. Arch. Microbiol. 2002, 178, 279-287.
    • (2002) Arch. Microbiol. , vol.178 , pp. 279-287
    • Rontani, J.F.1    Mouzdahir, A.2    Michotey, V.3    Bonin, P.4
  • 159
    • 0038492676 scopus 로고    scopus 로고
    • Production of a polyunsaturated isoprenoid wax ester during aerobic metabolism of squalene by Marinobacter squalenivorans sp nov
    • Rontani, J. F., Mouzdahir, A., Michotey, V., Caumette, P., et al., Production of a polyunsaturated isoprenoid wax ester during aerobic metabolism of squalene by Marinobacter squalenivorans sp nov. Appl. Environ. Microbiol. 2003, 69, 4167-4176.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4167-4176
    • Rontani, J.F.1    Mouzdahir, A.2    Michotey, V.3    Caumette, P.4
  • 160
    • 0032457071 scopus 로고    scopus 로고
    • Biotransformation of monoterpenes, bile acids, and other isoprenoids in anaerobic ecosystems
    • Hylemon, P. B., Harder, J., Biotransformation of monoterpenes, bile acids, and other isoprenoids in anaerobic ecosystems. FEMS Microbiol. Rev. 1998, 22, 475-488.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 475-488
    • Hylemon, P.B.1    Harder, J.2
  • 161
    • 0021828003 scopus 로고
    • Degradation of unsaturated hydrocarbons by methanogenic enrichment cultures
    • Schink, B., Degradation of unsaturated hydrocarbons by methanogenic enrichment cultures. FEMS Microbiol. Ecol. 1985, 31, 69-77.
    • (1985) FEMS Microbiol. Ecol. , vol.31 , pp. 69-77
    • Schink, B.1
  • 162
    • 70449395041 scopus 로고    scopus 로고
    • Improved squalene production via modulation of the methylerythritol 4-phosphate pathway and heterologous expression of genes from Streptomyces peucetius ATCC 27952 in Escherichia coli
    • Ghimire, G. P., Lee, H. C., Sohng, J. K., Improved squalene production via modulation of the methylerythritol 4-phosphate pathway and heterologous expression of genes from Streptomyces peucetius ATCC 27952 in Escherichia coli. Appl. Environ. Microbiol. 2009, 75, 7291-7293.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 7291-7293
    • Ghimire, G.P.1    Lee, H.C.2    Sohng, J.K.3
  • 163
    • 0018779981 scopus 로고
    • Esr determination of membrane order parameter in yeast sterol mutants
    • Lees, N. D., Bard, M., Kemple, M. D., Haak, R. A., et al., Esr determination of membrane order parameter in yeast sterol mutants. Biochim. Biophys. Acta 1979, 553, 469-475.
    • (1979) Biochim. Biophys. Acta , vol.553 , pp. 469-475
    • Lees, N.D.1    Bard, M.2    Kemple, M.D.3    Haak, R.A.4
  • 164
    • 0018129955 scopus 로고
    • Differences in crystal violet uptake and cation-induced death among yeast sterol mutants
    • Bard, M., Lees, N. D., Burrows, L. S., Kleinhans, F. W., Differences in crystal violet uptake and cation-induced death among yeast sterol mutants. J. Bacteriol. 1978, 135, 1146-1148.
    • (1978) J. Bacteriol. , vol.135 , pp. 1146-1148
    • Bard, M.1    Lees, N.D.2    Burrows, L.S.3    Kleinhans, F.W.4
  • 165
    • 0018400975 scopus 로고
    • Esr determinations of membrane-permeability in a yeast sterol mutant
    • Kleinhans, F. W., Lees, N. D., Bard, M., Haak, R. A., et al., Esr determinations of membrane-permeability in a yeast sterol mutant. Chem. Phys. Lipids 1979, 23, 143-154.
    • (1979) Chem. Phys. Lipids , vol.23 , pp. 143-154
    • Kleinhans, F.W.1    Lees, N.D.2    Bard, M.3    Haak, R.A.4
  • 166
    • 0018955572 scopus 로고
    • The effects of varied energy-source and detergent on the growth of sterol mutants of Saccharomyces cerevisiae
    • Lees, N. D., Lofton, S. L., Woods, R. A., Bard, M., The effects of varied energy-source and detergent on the growth of sterol mutants of Saccharomyces cerevisiae. J. Gen. Microbiol. 1980, 118, 209-214.
    • (1980) J. Gen. Microbiol. , vol.118 , pp. 209-214
    • Lees, N.D.1    Lofton, S.L.2    Woods, R.A.3    Bard, M.4
  • 167
    • 0015619047 scopus 로고
    • Effect of altered membrane sterol composition on temperature-dependence of yeast mitochondrial ATPase
    • Cobon, G. S., Haslam, J. M., Effect of altered membrane sterol composition on temperature-dependence of yeast mitochondrial ATPase. Biochem. Biophys. Res. Commun. 1973, 52, 320-326.
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 320-326
    • Cobon, G.S.1    Haslam, J.M.2
  • 168
    • 0022522115 scopus 로고
    • Biosynthesis of the farnesyl moiety of heme A from exogenous mevalonic acid by cultured chick liver cells
    • Weinstein, J. D., Branchaud, R., Beale, S. I., Bement, W. J., et al., Biosynthesis of the farnesyl moiety of heme A from exogenous mevalonic acid by cultured chick liver cells. Arch. Biochem. Biophys. 1986, 245, 44-50.
    • (1986) Arch. Biochem. Biophys. , vol.245 , pp. 44-50
    • Weinstein, J.D.1    Branchaud, R.2    Beale, S.I.3    Bement, W.J.4
  • 169
    • 0020988620 scopus 로고
    • Biosynthesis of ubiquinone
    • Olson, R. E., Rudney, H., Biosynthesis of ubiquinone. Vitam. Horm. 1983, 40, 1-43.
    • (1983) Vitam. Horm. , vol.40 , pp. 1-43
    • Olson, R.E.1    Rudney, H.2
  • 170
    • 0025793572 scopus 로고
    • Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver
    • Matsuoka, S., Sagami, H., Kurisaki, A., Ogura, K., Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver. J. Biol. Chem. 1991, 266, 3464-3468.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3464-3468
    • Matsuoka, S.1    Sagami, H.2    Kurisaki, A.3    Ogura, K.4
  • 171
    • 1442283623 scopus 로고
    • Saccharomyces cerevisiae contains 2 functional genes encoding 3-hydroxy-3-methylglutaryl coenzyme-A reductase
    • Basson, M. E., Thorsness, M., Rine, J., Saccharomyces cerevisiae contains 2 functional genes encoding 3-hydroxy-3-methylglutaryl coenzyme-A reductase. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 5563-5567.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 5563-5567
    • Basson, M.E.1    Thorsness, M.2    Rine, J.3
  • 172
    • 0031962865 scopus 로고    scopus 로고
    • Overexpression of a cytosolic hydroxymethylglutaryl-CoA reductase leads to squalene accumulation in yeast
    • Polakowski, T., Stahl, U., Lang, C., Overexpression of a cytosolic hydroxymethylglutaryl-CoA reductase leads to squalene accumulation in yeast. Appl. Microbiol. Biotechnol. 1998, 49, 66-71.
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 66-71
    • Polakowski, T.1    Stahl, U.2    Lang, C.3
  • 173
    • 0019855333 scopus 로고
    • Genetic and biochemical aspects of yeast sterol regulation involving 3-hydroxy-3-methylglutaryl coenzyme-A reductase
    • Bard, M., Downing, J. F., Genetic and biochemical aspects of yeast sterol regulation involving 3-hydroxy-3-methylglutaryl coenzyme-A reductase. J. Gen. Microbiol. 1981, 125, 415-420.
    • (1981) J. Gen. Microbiol. , vol.125 , pp. 415-420
    • Bard, M.1    Downing, J.F.2
  • 174
    • 0018397250 scopus 로고
    • Effects of catabolite derepression on the accumulation of steryl esters and the activity of beta-hydroxymethylglutaryl-CoA reductase in Saccharomyces cerevisiae
    • Quain, D. E., Haslam, J. M., Effects of catabolite derepression on the accumulation of steryl esters and the activity of beta-hydroxymethylglutaryl-CoA reductase in Saccharomyces cerevisiae. J. Gen. Microbiol. 1979, 111, 343-351.
    • (1979) J. Gen. Microbiol. , vol.111 , pp. 343-351
    • Quain, D.E.1    Haslam, J.M.2
  • 175
    • 72149122372 scopus 로고    scopus 로고
    • Geranylgeranyl pyrophosphate is a potent regulator of HRD-dependent 3-hydroxy-3-methylglutaryl-CoA reductase degradation in yeast
    • Garza, R. M., Tran, P. N., Hampton, R. Y., Geranylgeranyl pyrophosphate is a potent regulator of HRD-dependent 3-hydroxy-3-methylglutaryl-CoA reductase degradation in yeast. J. Biol. Chem. 2009, 284, 35368-35380.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35368-35380
    • Garza, R.M.1    Tran, P.N.2    Hampton, R.Y.3
  • 176
    • 0024306198 scopus 로고
    • Positive and negative transcriptional control by heme of genes encoding 3-hydroxy-3-methylglutaryl coenzyme-A reductase in Saccharomyces cerevisiae
    • Thorsness, M., Schafer, W., Dari, L., Rine, J., Positive and negative transcriptional control by heme of genes encoding 3-hydroxy-3-methylglutaryl coenzyme-A reductase in Saccharomyces cerevisiae. Mol. Cell. Biol. 1989, 9, 5702-5712.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5702-5712
    • Thorsness, M.1    Schafer, W.2    Dari, L.3    Rine, J.4
  • 177
    • 0029839311 scopus 로고    scopus 로고
    • Molecular, functional and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast Schizosaccharomyces pombe
    • Lum, P. Y., Edwards, S., Wright, R., Molecular, functional and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast Schizosaccharomyces pombe. Yeast 1996, 12, 1107-1124.
    • (1996) Yeast , vol.12 , pp. 1107-1124
    • Lum, P.Y.1    Edwards, S.2    Wright, R.3
  • 178
    • 0025745086 scopus 로고
    • Molecular cloning and characterization of the yeast gene for squalene synthetase
    • Jennings, S. M., Tsay, Y. H., Fisch, T. M., Robinson, G. W., Molecular cloning and characterization of the yeast gene for squalene synthetase. Proc. Natl. Acad. Sci. U.S.A 1991, 88, 6038-6042.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 6038-6042
    • Jennings, S.M.1    Tsay, Y.H.2    Fisch, T.M.3    Robinson, G.W.4
  • 179
    • 0027312026 scopus 로고
    • Conservation between human and fungal squalene synthetases - similarities in structure, function and regulation
    • Robinson, G. W., Tsay, Y. H., Kienzle, B. K., Smithmonroy, C. A., et al., Conservation between human and fungal squalene synthetases - similarities in structure, function and regulation. Mol. Cell. Biol. 1993, 13, 2706-2717.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2706-2717
    • Robinson, G.W.1    Tsay, Y.H.2    Kienzle, B.K.3    Smithmonroy, C.A.4
  • 180
    • 19444375356 scopus 로고    scopus 로고
    • Lipid analysis of the plasma membrane and mitochondria of brewer's yeast
    • Blagovic, B., Rupcic, J., Mesaric, M., Maric, V., Lipid analysis of the plasma membrane and mitochondria of brewer's yeast. Folia Microbiol. (Praha) 2005, 50, 24-30.
    • (2005) Folia Microbiol. (Praha) , vol.50 , pp. 24-30
    • Blagovic, B.1    Rupcic, J.2    Mesaric, M.3    Maric, V.4
  • 181
    • 0026041521 scopus 로고
    • The gene encoding squalene epoxidase from Saccharomyces cerevisiae - Cloning and characterization
    • Jandrositz, A., Turnowsky, F., Hogenauer, G., The gene encoding squalene epoxidase from Saccharomyces cerevisiae - Cloning and characterization. Gene 1991, 107, 155-160.
    • (1991) Gene , vol.107 , pp. 155-160
    • Jandrositz, A.1    Turnowsky, F.2    Hogenauer, G.3
  • 182
    • 0020804291 scopus 로고
    • Oxygen requirements for formation and activity of the squalene epoxidase in Saccharomyces cerevisiae
    • Jahnke, L., Klein, H. P., Oxygen requirements for formation and activity of the squalene epoxidase in Saccharomyces cerevisiae. J. Bacteriol. 1983, 155, 488-492.
    • (1983) J. Bacteriol. , vol.155 , pp. 488-492
    • Jahnke, L.1    Klein, H.P.2
  • 183
    • 0031931498 scopus 로고    scopus 로고
    • Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles
    • Leber, R., Landl, K., Zinser, E., Ahorn, H., et al., Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles. Mol. Biol. Cell 1998, 9, 375-386.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 375-386
    • Leber, R.1    Landl, K.2    Zinser, E.3    Ahorn, H.4
  • 184
    • 0028325230 scopus 로고
    • Molecular cloning, characterization and overexpression of Erg7 the Saccharomyces cerevisiae gene encoding lanosterol synthase
    • Corey, E. J., Matsuda, S. P. T., Bartel, B., Molecular cloning, characterization and overexpression of Erg7 the Saccharomyces cerevisiae gene encoding lanosterol synthase. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 2211-2215.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 2211-2215
    • Corey, E.J.1    Matsuda, S.P.T.2    Bartel, B.3
  • 185
    • 0028283156 scopus 로고
    • Isolation and characterization of the gene encoding 2,3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae
    • Shi, Z., Buntel, C. J., Griffin, J. H., Isolation and characterization of the gene encoding 2, 3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 7370-7374.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7370-7374
    • Shi, Z.1    Buntel, C.J.2    Griffin, J.H.3
  • 186
    • 0032412784 scopus 로고    scopus 로고
    • Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae
    • Daum, G., Lees, N. D., Bard, M., Dickson, R., Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast 1998, 14, 1471-1510.
    • (1998) Yeast , vol.14 , pp. 1471-1510
    • Daum, G.1    Lees, N.D.2    Bard, M.3    Dickson, R.4
  • 187
    • 0032989082 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of sterol synthesis in Saccharomyces cerevisiae
    • Lees, N. D., Bard, M., Kirsch, D. R., Biochemistry and molecular biology of sterol synthesis in Saccharomyces cerevisiae. Crit. Rev. Biochem. Mol. Biol. 1999, 34, 33-47.
    • (1999) Crit. Rev. Biochem. Mol. Biol. , vol.34 , pp. 33-47
    • Lees, N.D.1    Bard, M.2    Kirsch, D.R.3
  • 188
    • 0018106855 scopus 로고
    • Metabolism of sterols in yeast
    • Parks, L. W., Metabolism of sterols in yeast. Crit. Rev. Microbiol. 1978, 6, 301-341.
    • (1978) Crit. Rev. Microbiol. , vol.6 , pp. 301-341
    • Parks, L.W.1
  • 189
    • 0026668882 scopus 로고
    • Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts
    • Nagy, M., Lacroute, F., Thomas, D., Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 8966-8970.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 8966-8970
    • Nagy, M.1    Lacroute, F.2    Thomas, D.3
  • 190
    • 0034646230 scopus 로고    scopus 로고
    • Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit
    • Chabes, A., Domkin, V., Larsson, G., Liu, A., et al., Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 2474-2479.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2474-2479
    • Chabes, A.1    Domkin, V.2    Larsson, G.3    Liu, A.4
  • 191
    • 0000493179 scopus 로고
    • Anaerobic nutrition of Saccharomyces cerevisiae. II. Unsaturated fatty acid requirement for growth in a defined medium
    • Andreasen, A. A., Stier, T. J., Anaerobic nutrition of Saccharomyces cerevisiae. II. Unsaturated fatty acid requirement for growth in a defined medium. J. Cell Physiol. 1954, 43, 271-281.
    • (1954) J. Cell Physiol. , vol.43 , pp. 271-281
    • Andreasen, A.A.1    Stier, T.J.2
  • 192
    • 0002587184 scopus 로고
    • Anaerobic nutrition of Saccharomyces cerevisiae. I. Ergosterol requirement for growth in a defined medium
    • Andreasen, A. A., Stier, T. J., Anaerobic nutrition of Saccharomyces cerevisiae. I. Ergosterol requirement for growth in a defined medium. J. Cell Physiol. 1953, 41, 23-36.
    • (1953) J. Cell Physiol. , vol.41 , pp. 23-36
    • Andreasen, A.A.1    Stier, T.J.2
  • 193
    • 67650928565 scopus 로고    scopus 로고
    • Squalene versus ergosterol formation using Saccharomyces cerevisiae: Combined effect of oxygen supply, inoculum size, and fermentation time on yield and selectivity of the bioprocess
    • Mantzouridou, F., Naziri, E., Tsimidou, M. Z., Squalene versus ergosterol formation using Saccharomyces cerevisiae: Combined effect of oxygen supply, inoculum size, and fermentation time on yield and selectivity of the bioprocess. J. Agric. Food Chem. 2009, 57, 6189-6198.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 6189-6198
    • Mantzouridou, F.1    Naziri, E.2    Tsimidou, M.Z.3
  • 194
    • 0027360859 scopus 로고
    • Sterol synthesis and viability of erg11 (cytochrome P450 lanosterol demethylase) mutations in Saccharomyces cerevisiae and Candida albicans
    • Bard, M., Lees, N. D., Turi, T., Craft, D., et al., Sterol synthesis and viability of erg11 (cytochrome P450 lanosterol demethylase) mutations in Saccharomyces cerevisiae and Candida albicans. Lipids 1993, 28, 963-967.
    • (1993) Lipids , vol.28 , pp. 963-967
    • Bard, M.1    Lees, N.D.2    Turi, T.3    Craft, D.4
  • 195
    • 0031856845 scopus 로고    scopus 로고
    • A mutation in a purported regulatory gene affects control of sterol uptake in Saccharomyces cerevisiae
    • Crowley, J. H., Leak, F. W., Jr., Shianna, K. V., Tove, S., et al., A mutation in a purported regulatory gene affects control of sterol uptake in Saccharomyces cerevisiae. J. Bacteriol. 1998, 180, 4177-4183.
    • (1998) J. Bacteriol. , vol.180 , pp. 4177-4183
    • Crowley, J.H.1    Leak Jr., F.W.2    Shianna, K.V.3    Tove, S.4
  • 196
    • 0024028454 scopus 로고
    • Pleiotropic mutations in Saccharomyces cerevisiae affecting sterol uptake and metabolism
    • Lewis, T. L., Keesler, G. A., Fenner, G. P., Parks, L. W., Pleiotropic mutations in Saccharomyces cerevisiae affecting sterol uptake and metabolism. Yeast 1988, 4, 93-106.
    • (1988) Yeast , vol.4 , pp. 93-106
    • Lewis, T.L.1    Keesler, G.A.2    Fenner, G.P.3    Parks, L.W.4
  • 197
    • 0030772492 scopus 로고    scopus 로고
    • Effects of overproduction of the catalytic domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase on squalene synthesis in Saccharomyces cerevisiae
    • Donald, K. A., Hampton, R. Y., Fritz, I. B., Effects of overproduction of the catalytic domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase on squalene synthesis in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 1997, 63, 3341-3344.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3341-3344
    • Donald, K.A.1    Hampton, R.Y.2    Fritz, I.B.3
  • 198
    • 33646253659 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation is required for cold adaptation and regulation of sterol biosynthesis in the yeast Saccharomyces cerevisiae
    • Loertscher, J., Larson, L. L., Matson, C. K., Parrish, M. L., et al., Endoplasmic reticulum-associated degradation is required for cold adaptation and regulation of sterol biosynthesis in the yeast Saccharomyces cerevisiae. Eukaryot. Cell 2006, 5, 712-722.
    • (2006) Eukaryot. Cell , vol.5 , pp. 712-722
    • Loertscher, J.1    Larson, L.L.2    Matson, C.K.3    Parrish, M.L.4
  • 199
    • 77955796740 scopus 로고    scopus 로고
    • Observations on squalene accumulation in Saccharomyces cerevisiae due to the manipulation of HMG2 and ERG6
    • Mantzouridou, F., Tsimidou, M. Z., Observations on squalene accumulation in Saccharomyces cerevisiae due to the manipulation of HMG2 and ERG6. FEMS Yeast Res. 2010, 10, 699-707.
    • (2010) FEMS Yeast Res. , vol.10 , pp. 699-707
    • Mantzouridou, F.1    Tsimidou, M.Z.2
  • 200
    • 79951517708 scopus 로고    scopus 로고
    • Observations on squalene accumulation in Saccharomyces cerevisiae due to the manipulation of HMG2 and ERG6
    • Mantzouridou, F., Tsimidou, M. Z., Observations on squalene accumulation in Saccharomyces cerevisiae due to the manipulation of HMG2 and ERG6. FEMS Yeast Res. 2011, 11, 238.
    • (2011) FEMS Yeast Res. , vol.11 , pp. 238
    • Mantzouridou, F.1    Tsimidou, M.Z.2
  • 201
    • 0004233511 scopus 로고
    • 5th Edn. Merrill Publishing Company, Columbus, OH, USA.
    • Thurman, H. V., Introductory Oceanography, 5th Edn. Merrill Publishing Company, Columbus, OH, USA 1988.
    • (1988) Introductory Oceanography
    • Thurman, H.V.1
  • 202
    • 66149148930 scopus 로고    scopus 로고
    • Screening and characterization of squalene-producing Thraustochytrids from Hong Kong mangroves
    • Li, Q., Chen, G. Q., Fan, K. W., Lu, F. P., et al., Screening and characterization of squalene-producing Thraustochytrids from Hong Kong mangroves. J. Agric. Food Chem. 2009, 57, 4267-4272.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 4267-4272
    • Li, Q.1    Chen, G.Q.2    Fan, K.W.3    Lu, F.P.4
  • 203
    • 0030298327 scopus 로고    scopus 로고
    • High cell density culture of microalgae in heterotrophic growth
    • Chen, F., High cell density culture of microalgae in heterotrophic growth. Trends Biotechnol. 1996, 14, 421-426.
    • (1996) Trends Biotechnol. , vol.14 , pp. 421-426
    • Chen, F.1
  • 204
    • 77955095940 scopus 로고    scopus 로고
    • Optimization of nitrogen source for enhanced production of squalene from thraustochytrid Aurantiochytrium sp
    • Chen, G. Q., Fan, K. W., Lu, F. P., Li, Q. A., et al., Optimization of nitrogen source for enhanced production of squalene from thraustochytrid Aurantiochytrium sp. New Biotechnol. 2010, 27, 382-389.
    • (2010) New Biotechnol. , vol.27 , pp. 382-389
    • Chen, G.Q.1    Fan, K.W.2    Lu, F.P.3    Li, Q.A.4
  • 205
    • 77953693321 scopus 로고    scopus 로고
    • Enhanced production of squalene in the thraustochytrid Aurantiochytrium mangrovei by medium optimization and treatment with terbinafine
    • Fan, K. W., Aki, T., Chen, F., Jiang, Y., Enhanced production of squalene in the thraustochytrid Aurantiochytrium mangrovei by medium optimization and treatment with terbinafine. World J. Microbiol. Biotechnol. 2010, 26, 1303-1309.
    • (2010) World J. Microbiol. Biotechnol. , vol.26 , pp. 1303-1309
    • Fan, K.W.1    Aki, T.2    Chen, F.3    Jiang, Y.4
  • 206
    • 12544258708 scopus 로고    scopus 로고
    • Botryococcus braunii: A rich source for hydrocarbons and related ether lipids
    • Metzger, P., Largeau, C., Botryococcus braunii: A rich source for hydrocarbons and related ether lipids. Appl. Microbiol. Biotechnol. 2005, 66, 486-496.
    • (2005) Appl. Microbiol. Biotechnol. , vol.66 , pp. 486-496
    • Metzger, P.1    Largeau, C.2
  • 207
    • 84986817159 scopus 로고
    • Structure and chemistry of a new chemical race of Botryococcus braunii (Chlorophyceae) that produces lycopadiene, a tetraterpenoid hydrocarbon
    • Metzger, P., Allard, B., Casadevall, E., Berkaloff, C., et al., Structure and chemistry of a new chemical race of Botryococcus braunii (Chlorophyceae) that produces lycopadiene, a tetraterpenoid hydrocarbon. J. Phycol. 1990, 26, 258-266.
    • (1990) J. Phycol. , vol.26 , pp. 258-266
    • Metzger, P.1    Allard, B.2    Casadevall, E.3    Berkaloff, C.4
  • 208
    • 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., Rohmer, M., 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. 1996, 316, 73-80.
    • (1996) Biochem. J. , vol.316 , pp. 73-80
    • Schwender, J.1    Seemann, M.2    Lichtenthaler, H.K.3    Rohmer, M.4
  • 209
    • 0042158199 scopus 로고    scopus 로고
    • Biosynthesis of the triterpenoids, botryococcenes and tetramethylsqualene in the B race of Botryococcus braunii via the non-mevalonate pathway
    • Sato, Y., Ito, Y., Okada, S., Murakami, M., et al., Biosynthesis of the triterpenoids, botryococcenes and tetramethylsqualene in the B race of Botryococcus braunii via the non-mevalonate pathway. Tetrahedron Lett. 2003, 44, 7035-7037.
    • (2003) Tetrahedron Lett. , vol.44 , pp. 7035-7037
    • Sato, Y.1    Ito, Y.2    Okada, S.3    Murakami, M.4
  • 210
    • 0028210719 scopus 로고
    • Phosphorylation of farnesol by a cell-free system from Botryococcus braunii
    • Inoue, H., Korenaga, T., Sagami, H., Koyama, T., et al., Phosphorylation of farnesol by a cell-free system from Botryococcus braunii. Biochem. Biophys. Res. Commun. 1994, 200, 1036-1041.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 1036-1041
    • Inoue, H.1    Korenaga, T.2    Sagami, H.3    Koyama, T.4
  • 211
    • 0027424893 scopus 로고
    • Formation of farnesal and 3-hydroxy-2, 3-dihydrofarnesal from farnesol by protoplasts of Botryococcus braunii
    • Inoue, H., Korenaga, T., Sagami, H., Koyama, T., et al., Formation of farnesal and 3-hydroxy-2, 3-dihydrofarnesal from farnesol by protoplasts of Botryococcus braunii. Biochem. Biophys. Res. Commun. 1993, 196, 1401-1405.
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 1401-1405
    • Inoue, H.1    Korenaga, T.2    Sagami, H.3    Koyama, T.4
  • 212
    • 0346059444 scopus 로고    scopus 로고
    • Characterization of botryococcene synthase enzyme activity, a squalene synthase-like activity from the green microalga Botryococcus braunii, Race B
    • Okada, S., Devarenne, T. P., Murakami, M., Abe, H., et al., Characterization of botryococcene synthase enzyme activity, a squalene synthase-like activity from the green microalga Botryococcus braunii, Race B. Arch. Biochem. Biophys. 2004, 422, 110-118.
    • (2004) Arch. Biochem. Biophys. , vol.422 , pp. 110-118
    • Okada, S.1    Devarenne, T.P.2    Murakami, M.3    Abe, H.4
  • 213
    • 0034650537 scopus 로고    scopus 로고
    • Molecular characterization of squalene synthase from the green microalga Botryococcus braunii, Race B
    • Okada, S., Devarenne, T. P., Chappell, J., Molecular characterization of squalene synthase from the green microalga Botryococcus braunii, Race B. Arch. Biochem. Biophys. 2000, 373, 307-317.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 307-317
    • Okada, S.1    Devarenne, T.P.2    Chappell, J.3
  • 214
    • 0000021535 scopus 로고
    • Stereochemical studies of botryococcene biosynthesis - analogies between 1'-1 and 1'-3 condensations in the isoprenoid pathway
    • Huang, Z., Poulter, C. D., Stereochemical studies of botryococcene biosynthesis - analogies between 1'-1 and 1'-3 condensations in the isoprenoid pathway. J. Am. Chem. Soc. 1989, 111, 2713-2715.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 2713-2715
    • Huang, Z.1    Poulter, C.D.2
  • 215
    • 0030062843 scopus 로고    scopus 로고
    • A member of a new class of carotenoids from the green microalga Botryococcus braunii Berkeley
    • Okada, S., Matsuda, H., Murakami, M., Yamaguchi, K., Botryoxanthin, A., A member of a new class of carotenoids from the green microalga Botryococcus braunii Berkeley. Tetrahedron Lett. 1996, 37, 1065-1068.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 1065-1068
    • Okada, S.1    Matsuda, H.2    Murakami, M.3    Yamaguchi, K.4    Botryoxanthin, A.5
  • 216
    • 0030824745 scopus 로고    scopus 로고
    • Braunixanthins 1 and 2, new carotenoids from the green microalga Botryococcus braunii
    • Okada, S., Tonegawa, I., Matsuda, H., Murakami, M., et al., Braunixanthins 1 and 2, new carotenoids from the green microalga Botryococcus braunii. Tetrahedron Lett. 1997, 53, 11307-11316.
    • (1997) Tetrahedron Lett. , vol.53 , pp. 11307-11316
    • Okada, S.1    Tonegawa, I.2    Matsuda, H.3    Murakami, M.4
  • 217
    • 0031081193 scopus 로고    scopus 로고
    • Four polymethylsqualene epoxides and one acyclic tetraterpene epoxide from Botryococcus braunii
    • Delahais, V., Metzger, P., Four polymethylsqualene epoxides and one acyclic tetraterpene epoxide from Botryococcus braunii. Phytochemistry 1997, 44, 671-678.
    • (1997) Phytochemistry , vol.44 , pp. 671-678
    • Delahais, V.1    Metzger, P.2
  • 219
    • 0037063401 scopus 로고    scopus 로고
    • Squalene content and antioxidant activity of Terminalia catappa leaves and seeds
    • Ko, T. F., Weng, Y. M., Chiou, R. Y., Squalene content and antioxidant activity of Terminalia catappa leaves and seeds. J. Agric. Food Chem. 2002, 50, 5343-5348.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 5343-5348
    • Ko, T.F.1    Weng, Y.M.2    Chiou, R.Y.3
  • 220
    • 78751576018 scopus 로고    scopus 로고
    • 2 extraction of oil, carotenoids, squalene and sterols from lotus (Nelumbo nucifera Gaertn) bee pollen
    • 2 extraction of oil, carotenoids, squalene and sterols from lotus (Nelumbo nucifera Gaertn) bee pollen. Food Bioprod. Proc. 2011, 89, 47-52.
    • (2011) Food Bioprod. Proc. , vol.89 , pp. 47-52
    • Xu, X.1    Dong, J.2    Mu, X.3    Sun, L.4
  • 221
    • 57749106606 scopus 로고    scopus 로고
    • Breaking the cells of rape bee pollen and consecutive extraction of functional oil with supercritical carbon dioxide
    • Xu, X., Sun, L., Dong, J., Zhang, H., Breaking the cells of rape bee pollen and consecutive extraction of functional oil with supercritical carbon dioxide. Innov. Food Sci. Emerg. Technol. 2009, 10, 42-46.
    • (2009) Innov. Food Sci. Emerg. Technol. , vol.10 , pp. 42-46
    • Xu, X.1    Sun, L.2    Dong, J.3    Zhang, H.4
  • 222
    • 0028447781 scopus 로고
    • A new short-path distillation system applied to the reduction of cholesterol in butter and lard
    • Lanzani, A., Bondioli, P., Mariani, C., Folegatti, L., et al., A new short-path distillation system applied to the reduction of cholesterol in butter and lard. J. Am. Oil Chem. Soc. 1994, 71, 609-614.
    • (1994) J. Am. Oil Chem. Soc. , vol.71 , pp. 609-614
    • Lanzani, A.1    Bondioli, P.2    Mariani, C.3    Folegatti, L.4
  • 223
    • 12944260098 scopus 로고
    • Squalene a highly unsaturated hydrocarbon in shark liver oil
    • Tsujimoto, M., Squalene a highly unsaturated hydrocarbon in shark liver oil. Ind. Eng. Chem. 1920, 12, 63-72.
    • (1920) Ind. Eng. Chem. , vol.12 , pp. 63-72
    • Tsujimoto, M.1
  • 224
    • 0043027011 scopus 로고    scopus 로고
    • Polychlorinated biphenyl, heavy metal and methylmercury residues in hammerhead sharks: Contaminant status and assessment
    • Storelli, M. M., Ceci, E., Storelli, A., Marcotrigiano, G. O., Polychlorinated biphenyl, heavy metal and methylmercury residues in hammerhead sharks: Contaminant status and assessment. Mar. Pollut. Bull. 2003, 46, 1035-1039.
    • (2003) Mar. Pollut. Bull. , vol.46 , pp. 1035-1039
    • Storelli, M.M.1    Ceci, E.2    Storelli, A.3    Marcotrigiano, G.O.4
  • 225
    • 0033795327 scopus 로고    scopus 로고
    • Observations on metal concentrations in three species of shark (Deania calcea, Centroscymnus crepidater and Centroscymnus owstoni) from southeastern Australian waters
    • Turoczy, N. J., Laurenson, L. J. B., Allinson, G., Nishikawa, M., et al., Observations on metal concentrations in three species of shark (Deania calcea, Centroscymnus crepidater and Centroscymnus owstoni) from southeastern Australian waters. J. Agric. Food Chem. 2000, 48, 4357-4364.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 4357-4364
    • Turoczy, N.J.1    Laurenson, L.J.B.2    Allinson, G.3    Nishikawa, M.4
  • 226
    • 36348983891 scopus 로고    scopus 로고
    • Concentration of squalene from shark liver oil by short-path distillation
    • Pietsch, A., Jaeger, P., Concentration of squalene from shark liver oil by short-path distillation. Eur. J. Lipid Sci. Technol. 2007, 109, 1077-1082.
    • (2007) Eur. J. Lipid Sci. Technol. , vol.109 , pp. 1077-1082
    • Pietsch, A.1    Jaeger, P.2
  • 227
    • 38849141948 scopus 로고    scopus 로고
    • Supercritical carbon dioxide fractionation of the model mixture squalene/oleic acid in a membrane contactor
    • Ruivo, R., Couto, R., Simoes, P. C., Supercritical carbon dioxide fractionation of the model mixture squalene/oleic acid in a membrane contactor. Separ. Purif. Technol. 2008, 59, 231-237.
    • (2008) Separ. Purif. Technol. , vol.59 , pp. 231-237
    • Ruivo, R.1    Couto, R.2    Simoes, P.C.3
  • 229
    • 0035877104 scopus 로고    scopus 로고
    • Differential permeation of oil constituents in nonporous denser polymeric membranes
    • Subramanian, R., Raghavarao, K. S. M. S., Nabetani, H., Nakajima, M., et al., Differential permeation of oil constituents in nonporous denser polymeric membranes. J. Membr. Sci. 2001, 187, 57-69.
    • (2001) J. Membr. Sci. , vol.187 , pp. 57-69
    • Subramanian, R.1    Raghavarao, K.S.M.S.2    Nabetani, H.3    Nakajima, M.4
  • 230
    • 0000225980 scopus 로고    scopus 로고
    • The mixer-settler principle as a separation unit in supercritical fluid processes
    • Pietsch, A., Eggers, R., The mixer-settler principle as a separation unit in supercritical fluid processes. J. Supercrit. Fluids 1999, 14, 163-171.
    • (1999) J. Supercrit. Fluids , vol.14 , pp. 163-171
    • Pietsch, A.1    Eggers, R.2
  • 231
    • 0034388174 scopus 로고    scopus 로고
    • Fractionation of lipids in a static mixer and packed column using supercritical carbon dioxide
    • Catchpole, O. J., Simoes, P., Grey, J. B., Nogueiro, E. M. M., et al., Fractionation of lipids in a static mixer and packed column using supercritical carbon dioxide. Ind. Eng. Chem. Res. 2000, 39, 4820-4827.
    • (2000) Ind. Eng. Chem. Res. , vol.39 , pp. 4820-4827
    • Catchpole, O.J.1    Simoes, P.2    Grey, J.B.3    Nogueiro, E.M.M.4
  • 232
    • 0001166779 scopus 로고
    • Food uses of grain amaranth
    • Breene, W. M., Food uses of grain amaranth. Cereal Foods World 1991, 36, 426-430.
    • (1991) Cereal Foods World , vol.36 , pp. 426-430
    • Breene, W.M.1
  • 235
    • 0030628714 scopus 로고    scopus 로고
    • Evaluation of the antioxidant and hepatoprotective activity of Terminalia catappa
    • Lin, C. C., Chen, Y. L., Lin, J. M., Ujiie, T., Evaluation of the antioxidant and hepatoprotective activity of Terminalia catappa. Am. J. Chin. Med. 1997, 25, 153-161.
    • (1997) Am. J. Chin. Med. , vol.25 , pp. 153-161
    • Lin, C.C.1    Chen, Y.L.2    Lin, J.M.3    Ujiie, T.4
  • 236
    • 0034193611 scopus 로고    scopus 로고
    • Folk medicine Terminalia catappa and its major tannin component, punicalagin, are effective against bleomycin-induced genotoxicity in Chinese hamster ovary cells
    • Chen, P. S., Li, J. H., Liu, T. Y., Lin, T. C., Folk medicine Terminalia catappa and its major tannin component, punicalagin, are effective against bleomycin-induced genotoxicity in Chinese hamster ovary cells. Cancer Lett. 2000, 152, 115-122.
    • (2000) Cancer Lett. , vol.152 , pp. 115-122
    • Chen, P.S.1    Li, J.H.2    Liu, T.Y.3    Lin, T.C.4
  • 237
    • 81155136178 scopus 로고
    • Production of vegetable squalane concentrate
    • Hirata, Y., Ota, Y., Production of vegetable squalane concentrate. Japan Appl. Pub. 07-351785. 1995.
    • (1995) Japan Appl. Pub. , pp. 07-351785
    • Hirata, Y.1    Ota, Y.2
  • 240
    • 75649108521 scopus 로고    scopus 로고
    • Novel fractionation method for squalene and phytosterols contained in the deodorization distillate of rice bran oil
    • Sugihara, N., Kanda, A., Nakano, T., Nakamura, T., et al., Novel fractionation method for squalene and phytosterols contained in the deodorization distillate of rice bran oil. J. Oleo Sci. 2010, 59, 65-70.
    • (2010) J. Oleo Sci. , vol.59 , pp. 65-70
    • Sugihara, N.1    Kanda, A.2    Nakano, T.3    Nakamura, T.4
  • 241
    • 0002674643 scopus 로고
    • Separation of tocopherols from deodorizer condensates by countercurrent extraction with carbon dioxide
    • Brunner, G., Malchow, T., Stuerken, K., Gottschau, T., Separation of tocopherols from deodorizer condensates by countercurrent extraction with carbon dioxide. J. Supercrit. Fluids 1991, 4, 72-80.
    • (1991) J. Supercrit. Fluids , vol.4 , pp. 72-80
    • Brunner, G.1    Malchow, T.2    Stuerken, K.3    Gottschau, T.4
  • 242
    • 2442650435 scopus 로고    scopus 로고
    • Separation of alpha-tocopherol and squalene by pressure swing adsorption in supercritical carbon dioxide
    • Wang, H. T., Goto, M., Sasaki, M., Hirose, T., Separation of alpha-tocopherol and squalene by pressure swing adsorption in supercritical carbon dioxide. Ind. Eng. Chem. Res. 2004, 43, 2753-2758.
    • (2004) Ind. Eng. Chem. Res. , vol.43 , pp. 2753-2758
    • Wang, H.T.1    Goto, M.2    Sasaki, M.3    Hirose, T.4
  • 243
    • 43349098592 scopus 로고    scopus 로고
    • The isolation and characterization of Pseudozyma sp. JCC 207, a novel producer of squalene
    • Chang, M. H., Kim, H. J., Jahng, K. Y., Hong, S. C., The isolation and characterization of Pseudozyma sp. JCC 207, a novel producer of squalene. Appl. Microbiol. Biotechnol. 2008, 78, 963-972.
    • (2008) Appl. Microbiol. Biotechnol. , vol.78 , pp. 963-972
    • Chang, M.H.1    Kim, H.J.2    Jahng, K.Y.3    Hong, S.C.4
  • 244
    • 34547474610 scopus 로고    scopus 로고
    • Rubritalea squalenifaciens sp nov., a squalene-producing marine bacterium belonging to subdivision 1 of the phylum 'Verrucomicrobia'
    • Kasai, H., Katsuta, A., Sekiguchi, H., Matsuda, S., et al., Rubritalea squalenifaciens sp nov., a squalene-producing marine bacterium belonging to subdivision 1 of the phylum 'Verrucomicrobia'. Int. J. Syst. Evol. Microbiol. 2007, 57, 1630-1634.
    • (2007) Int. J. Syst. Evol. Microbiol. , vol.57 , pp. 1630-1634
    • Kasai, H.1    Katsuta, A.2    Sekiguchi, H.3    Matsuda, S.4
  • 245
    • 47249131220 scopus 로고    scopus 로고
    • Rubritalea sabuli sp nov., a carotenoid- and squalene-producing member of the family Verrucomicrobiaceae, isolated from marine sediment
    • Yoon, J., Matsuo, Y., Matsuda, S., Adachi, K., et al., Rubritalea sabuli sp nov., a carotenoid- and squalene-producing member of the family Verrucomicrobiaceae, isolated from marine sediment. Int. J. Syst. Evol. Microbiol. 2008, 58, 992-997.
    • (2008) Int. J. Syst. Evol. Microbiol. , vol.58 , pp. 992-997
    • Yoon, J.1    Matsuo, Y.2    Matsuda, S.3    Adachi, K.4
  • 246
    • 35648977550 scopus 로고    scopus 로고
    • Rubritalea spongiae sp nov and Rubritalea tangerina sp nov., two carotenoid- and squalene-producing marine bacteria of the family Verrucomicrobiaceae within the phylum 'Verrucomicrobia', isolated from marine animals
    • Yoon, J., Matsuo, Y., Matsuda, S., Adachi, K., et al., Rubritalea spongiae sp nov and Rubritalea tangerina sp nov., two carotenoid- and squalene-producing marine bacteria of the family Verrucomicrobiaceae within the phylum 'Verrucomicrobia', isolated from marine animals. Int. J. Syst. Evol. Microbiol. 2007, 57, 2337-2343.
    • (2007) Int. J. Syst. Evol. Microbiol. , vol.57 , pp. 2337-2343
    • Yoon, J.1    Matsuo, Y.2    Matsuda, S.3    Adachi, K.4
  • 247
    • 71649103780 scopus 로고    scopus 로고
    • Squalene: A natural triterpene for use in disease management and therapy
    • Reddy, L. H., Couvreur, P., Squalene: A natural triterpene for use in disease management and therapy. Adv. Drug Deliv. Rev. 2009, 61, 1412-1426.
    • (2009) Adv. Drug Deliv. Rev. , vol.61 , pp. 1412-1426
    • Reddy, L.H.1    Couvreur, P.2
  • 248
    • 0022646452 scopus 로고
    • A possible role for squalene in the pathogenesis of acne 2. In vivo study of squalene oxides in skin surface and intra-comedonal lipids of acne patients
    • Saintleger, D., Bague, A., Lefebvre, E., Cohen, E., et al., A possible role for squalene in the pathogenesis of acne 2. In vivo study of squalene oxides in skin surface and intra-comedonal lipids of acne patients. Br. J. Dermatol. 1986, 114, 543-552.
    • (1986) Br. J. Dermatol. , vol.114 , pp. 543-552
    • Saintleger, D.1    Bague, A.2    Lefebvre, E.3    Cohen, E.4
  • 249
    • 0034531005 scopus 로고    scopus 로고
    • Oxidants and antioxidants in breast cancer
    • Ambrosone, C. B., Oxidants and antioxidants in breast cancer. Antioxid. Redox Signal. 2000, 2, 903-918.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 903-918
    • Ambrosone, C.B.1
  • 250
    • 77649192253 scopus 로고    scopus 로고
    • Squalene protects against oxidative DNA damage in MCF10A human mammary epithelial cells but not in MCF7 and MDA-MB-231 human breast cancer cells
    • Warleta, F., Campos, M., Allouche, Y., Sanchez-Quesada, C., et al., Squalene protects against oxidative DNA damage in MCF10A human mammary epithelial cells but not in MCF7 and MDA-MB-231 human breast cancer cells. Food Chem. Toxicol. 2010, 48, 1092-1100.
    • (2010) Food Chem. Toxicol. , vol.48 , pp. 1092-1100
    • Warleta, F.1    Campos, M.2    Allouche, Y.3    Sanchez-Quesada, C.4
  • 251
    • 0033213499 scopus 로고    scopus 로고
    • On the role of squalene in olive oil stability
    • Psomiadou, E., Tsimidou, M., On the role of squalene in olive oil stability. J. Agric. Food Chem. 1999, 47, 4025-4032.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4025-4032
    • Psomiadou, E.1    Tsimidou, M.2
  • 252
    • 21144440284 scopus 로고    scopus 로고
    • In vitro antioxidant effect and inhibition of alpha-amylase of two varieties of Amaranthus caudatus seeds
    • Conforti, F., Statti, G., Loizzo, M. R., Sacchetti, G., et al., In vitro antioxidant effect and inhibition of alpha-amylase of two varieties of Amaranthus caudatus seeds. Biol. Pharm. Bull. 2005, 28, 1098-1102.
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 1098-1102
    • Conforti, F.1    Statti, G.2    Loizzo, M.R.3    Sacchetti, G.4
  • 253
    • 0034298039 scopus 로고    scopus 로고
    • Synergistic effects of alpha-tocopherol, beta-sitosterol and squalene on antioxidant activity assayed by crocin bleaching method
    • Finotti, E., D'Ambrosio, M., Paoletti, F., Vivanti, V., et al., Synergistic effects of alpha-tocopherol, beta-sitosterol and squalene on antioxidant activity assayed by crocin bleaching method. Nahrung-Food 2000, 44, 373-374.
    • (2000) Nahrung-Food , vol.44 , pp. 373-374
    • Finotti, E.1    D'Ambrosio, M.2    Paoletti, F.3    Vivanti, V.4
  • 254
    • 34247601535 scopus 로고    scopus 로고
    • Synergistic effects of squalene and polyunsaturated fatty acid concentrate on lipid peroxidation and antioxidant status in isoprenaline-induced myocardial infarction in rats
    • Dhandapani, N., Ganesan, B., Anandan, R., Jeyakumar, R., et al., Synergistic effects of squalene and polyunsaturated fatty acid concentrate on lipid peroxidation and antioxidant status in isoprenaline-induced myocardial infarction in rats. Afr. J. Biotechnol. 2007, 6, 1021-1027.
    • (2007) Afr. J. Biotechnol. , vol.6 , pp. 1021-1027
    • Dhandapani, N.1    Ganesan, B.2    Anandan, R.3    Jeyakumar, R.4
  • 255
    • 54249135351 scopus 로고    scopus 로고
    • Squalene selectively protects mouse bone marrow progenitors against cisplatin and carboplatin-induced cytotoxicity in vivo without protecting tumor growth
    • Das, B., Antoon, R., Tsuchida, R., Lotfi, S., et al., Squalene selectively protects mouse bone marrow progenitors against cisplatin and carboplatin-induced cytotoxicity in vivo without protecting tumor growth. Neoplasia 2008, 10, 1105-1U53.
    • (2008) Neoplasia , vol.10
    • Das, B.1    Antoon, R.2    Tsuchida, R.3    Lotfi, S.4
  • 256
    • 0242299690 scopus 로고    scopus 로고
    • In vitro cytoprotective activity of squalene on a bone marrow versus neuroblastoma model of cisplatin-induced toxicity: Implications in cancer chemotherapy
    • Das, B., Yeger, H., Baruchel, H., Freedman, M. H., et al., In vitro cytoprotective activity of squalene on a bone marrow versus neuroblastoma model of cisplatin-induced toxicity: Implications in cancer chemotherapy. Eur. J. Cancer 2003, 39, 2556-2565.
    • (2003) Eur. J. Cancer , vol.39 , pp. 2556-2565
    • Das, B.1    Yeger, H.2    Baruchel, H.3    Freedman, M.H.4
  • 258
    • 0029947979 scopus 로고    scopus 로고
    • Effectiveness and safety of low-dose pravastatin and squalene, alone and in combination, in elderly patients with hypercholesterolemia
    • Chan, P., Tomlinson, B., Lee, C. B., Lee, Y. S., Effectiveness and safety of low-dose pravastatin and squalene, alone and in combination, in elderly patients with hypercholesterolemia. J. Clin. Pharmacol. 1996, 36, 422-427.
    • (1996) J. Clin. Pharmacol. , vol.36 , pp. 422-427
    • Chan, P.1    Tomlinson, B.2    Lee, C.B.3    Lee, Y.S.4
  • 259
    • 2342538411 scopus 로고    scopus 로고
    • Leptin and hyperleptinemia - from friend to foe for cardiovascular function
    • Ren, J., Leptin and hyperleptinemia - from friend to foe for cardiovascular function. J. Endocrinol. 2004, 181, 1-10.
    • (2004) J. Endocrinol. , vol.181 , pp. 1-10
    • Ren, J.1
  • 260
    • 21744462095 scopus 로고    scopus 로고
    • Leptin is independently associated with systolic blood pressure, pulse pressure and arterial compliance in hypertensive African women with increased adiposity: The POWIRS study
    • Schutte, R., Huisman, H. W., Schutte, A. E., Malan, N. T., Leptin is independently associated with systolic blood pressure, pulse pressure and arterial compliance in hypertensive African women with increased adiposity: The POWIRS study. J. Hum. Hypertens. 2005, 19, 535-541.
    • (2005) J. Hum. Hypertens. , vol.19 , pp. 535-541
    • Schutte, R.1    Huisman, H.W.2    Schutte, A.E.3    Malan, N.T.4
  • 262
    • 2342449315 scopus 로고    scopus 로고
    • Triglycerides induce leptin resistance at the blood-brain barrier
    • Banks, W. A., Coon, A. B., Robinson, S. M., Moinuddin, A., et al., Triglycerides induce leptin resistance at the blood-brain barrier. Diabetes 2004, 53, 1253-1260.
    • (2004) Diabetes , vol.53 , pp. 1253-1260
    • Banks, W.A.1    Coon, A.B.2    Robinson, S.M.3    Moinuddin, A.4
  • 263
    • 38549085457 scopus 로고    scopus 로고
    • Progress of preparation and application in squalene
    • Xu, R. B., Liu, W. W., Wang, M. Y., Progress of preparation and application in squalene. Shandong J. Med. 2005, 45, 69-70.
    • (2005) Shandong J. Med. , vol.45 , pp. 69-70
    • Xu, R.B.1    Liu, W.W.2    Wang, M.Y.3
  • 264
    • 65949091104 scopus 로고    scopus 로고
    • Improvement of people's life quality-the mysteries of squalene
    • Pan, F., Improvement of people's life quality-the mysteries of squalene. SH Quali. 2001, 8, 47.
    • (2001) SH Quali. , vol.8 , pp. 47
    • Pan, F.1
  • 265
    • 0024320740 scopus 로고
    • Studies on distribution, excretion and subacute toxicity of squalane in dogs
    • Kamimura, H., Koga, N., Oguri, K., Yoshimura, H., et al., Studies on distribution, excretion and subacute toxicity of squalane in dogs. Fukuoka Igaku Zasshi 1989, 80, 269-280.
    • (1989) Fukuoka Igaku Zasshi , vol.80 , pp. 269-280
    • Kamimura, H.1    Koga, N.2    Oguri, K.3    Yoshimura, H.4
  • 266
    • 0025910838 scopus 로고
    • Studies on distribution and excretion of squalane in dogs administered for 2 weeks
    • Kamimura, H., Fuchigami, K., Inoue, H., Kodama, R., et al., Studies on distribution and excretion of squalane in dogs administered for 2 weeks. Fukuoka Igaku Zasshi 1991, 82, 300-304.
    • (1991) Fukuoka Igaku Zasshi , vol.82 , pp. 300-304
    • Kamimura, H.1    Fuchigami, K.2    Inoue, H.3    Kodama, R.4
  • 267
    • 65949120923 scopus 로고    scopus 로고
    • Influence of squalene feeding on plasma leptin, testosterone and blood pressure in rats
    • Liu, Y., Xu, X., Bi, D., Wang, X., et al., Influence of squalene feeding on plasma leptin, testosterone and blood pressure in rats. Indian J. Med. Res. 2009, 129, 150-153.
    • (2009) Indian J. Med. Res. , vol.129 , pp. 150-153
    • Liu, Y.1    Xu, X.2    Bi, D.3    Wang, X.4
  • 268
    • 77953752616 scopus 로고    scopus 로고
    • Improvement of reproduction performance in AA(+) meat-type male chicken by feeding with squalene
    • Li, S. J., Liang, Z. H., Wang, C., Feng, Y. P., et al., Improvement of reproduction performance in AA(+) meat-type male chicken by feeding with squalene. J. Anim. Vet. Adv. 2010, 9, 486-490.
    • (2010) J. Anim. Vet. Adv. , vol.9 , pp. 486-490
    • Li, S.J.1    Liang, Z.H.2    Wang, C.3    Feng, Y.P.4
  • 269
    • 77955050262 scopus 로고    scopus 로고
    • Cytoprotective effects of DL-alpha-lipoic acid or squalene on cyclophosphamide-induced oxidative injury: An experimental study on rat myocardium, testicles and urinary bladder
    • Motawi, T. M., Sadik, N. A., Refaat, A., Cytoprotective effects of DL-alpha-lipoic acid or squalene on cyclophosphamide-induced oxidative injury: An experimental study on rat myocardium, testicles and urinary bladder. Food Chem. Toxicol. 2010, 48, 2326-2336.
    • (2010) Food Chem. Toxicol. , vol.48 , pp. 2326-2336
    • Motawi, T.M.1    Sadik, N.A.2    Refaat, A.3
  • 270
    • 65649098071 scopus 로고    scopus 로고
    • High-dose squalene ingestion increases type I procollagen and decreases ultraviolet-induced DNA damage in human skin in vivo but is associated with transient adverse effects
    • Cho, S., Choi, C. W., Lee, D. H., Won, C. H., et al., High-dose squalene ingestion increases type I procollagen and decreases ultraviolet-induced DNA damage in human skin in vivo but is associated with transient adverse effects. Clin. Exp. Dermatol. 2009, 34, 500-508.
    • (2009) Clin. Exp. Dermatol. , vol.34 , pp. 500-508
    • Cho, S.1    Choi, C.W.2    Lee, D.H.3    Won, C.H.4
  • 271
    • 0026621668 scopus 로고
    • Inhibition by squalene of the tumor-promoting activity of 12-O-tetradecanoylphorbol-13-acetate in mouse skin carcinogenesis
    • Murakoshi, M., Nishino, H., Tokuda, H., Iwashima, A., et al., Inhibition by squalene of the tumor-promoting activity of 12-O-tetradecanoylphorbol-13-acetate in mouse skin carcinogenesis. Int. J. Cancer Suppl. 1992, 52, 950-952.
    • (1992) Int. J. Cancer Suppl. , vol.52 , pp. 950-952
    • Murakoshi, M.1    Nishino, H.2    Tokuda, H.3    Iwashima, A.4
  • 272
    • 0020569982 scopus 로고
    • Intensification of hosts immunity by squalene in sarcoma-180 bearing Icr mice
    • Ohkuma, T., Otagiri, K., Tanaka, S., Ikekawa, T., Intensification of hosts immunity by squalene in sarcoma-180 bearing Icr mice. J. Pharmacobiodyn. 1983, 6, 148-151.
    • (1983) J. Pharmacobiodyn. , vol.6 , pp. 148-151
    • Ohkuma, T.1    Otagiri, K.2    Tanaka, S.3    Ikekawa, T.4
  • 274
    • 24344504061 scopus 로고    scopus 로고
    • Potential anti-cancer effects of virgin olive oil phenols on colorectal carcinogenesis models in vitro
    • Gill, C. I., Boyd, A., McDermott, E., McCann, M., et al., Potential anti-cancer effects of virgin olive oil phenols on colorectal carcinogenesis models in vitro. Int. J. Cancer 2005, 117, 1-7.
    • (2005) Int. J. Cancer , vol.117 , pp. 1-7
    • Gill, C.I.1    Boyd, A.2    McDermott, E.3    McCann, M.4
  • 275
    • 33646427200 scopus 로고    scopus 로고
    • Blood pressure lowering effect of olive is mediated through calcium channel blockade
    • Gilani, A. H., Khan, A. U., Shah, A. J., Connor, J., et al., Blood pressure lowering effect of olive is mediated through calcium channel blockade. Int. J. Food Sci. Nutr. 2005, 56, 613-620.
    • (2005) Int. J. Food Sci. Nutr. , vol.56 , pp. 613-620
    • Gilani, A.H.1    Khan, A.U.2    Shah, A.J.3    Connor, J.4
  • 276
    • 33646474254 scopus 로고    scopus 로고
    • Monounsaturated fatty acids, olive oil and blood pressure: epidemiological, clinical and experimental evidence
    • Alonso, A., Ruiz-Gutierrez, V., Martinez-Gonzalez, M. A., Monounsaturated fatty acids, olive oil and blood pressure: epidemiological, clinical and experimental evidence. Public Health Nutr. 2006, 9, 251-257.
    • (2006) Public Health Nutr. , vol.9 , pp. 251-257
    • Alonso, A.1    Ruiz-Gutierrez, V.2    Martinez-Gonzalez, M.A.3
  • 277
    • 24344452961 scopus 로고    scopus 로고
    • Phytochemistry: Ibuprofen-like activity in extra-virgin olive oil
    • Beauchamp, G. K., Keast, R. S., Morel, D., Lin, J., et al., Phytochemistry: Ibuprofen-like activity in extra-virgin olive oil. Nature 2005, 437, 45-46.
    • (2005) Nature , vol.437 , pp. 45-46
    • Beauchamp, G.K.1    Keast, R.S.2    Morel, D.3    Lin, J.4
  • 278
    • 0032795847 scopus 로고    scopus 로고
    • Dietary factors in relation to rheumatoid arthritis: A role for olive oil and cooked vegetables
    • Linos, A., Kaklamani, V. G., Kaklamani, E., Koumantaki, Y., et al., Dietary factors in relation to rheumatoid arthritis: A role for olive oil and cooked vegetables? Am. J. Clin. Nutr. 1999, 70, 1077-1082.
    • (1999) Am. J. Clin. Nutr. , vol.70 , pp. 1077-1082
    • Linos, A.1    Kaklamani, V.G.2    Kaklamani, E.3    Koumantaki, Y.4
  • 279
    • 0024496727 scopus 로고
    • Variations of hepatic cholesterol precursors during altered flows of endogenous and exogenous squalene in the rat
    • Strandberg, T. E., Tilvis, R. S., Miettinen, T. A., Variations of hepatic cholesterol precursors during altered flows of endogenous and exogenous squalene in the rat. Biochim. Biophys. Acta 1989, 1001, 150-156.
    • (1989) Biochim. Biophys. Acta , vol.1001 , pp. 150-156
    • Strandberg, T.E.1    Tilvis, R.S.2    Miettinen, T.A.3
  • 280
    • 0031022932 scopus 로고    scopus 로고
    • Prevention of mammary preneoplastic transformation by naturally-occurring tumor inhibitors
    • Katdare, M., Singhal, H., Newmark, H., Osborne, M. P., et al., Prevention of mammary preneoplastic transformation by naturally-occurring tumor inhibitors. Cancer Lett. 1997, 111, 141-147.
    • (1997) Cancer Lett. , vol.111 , pp. 141-147
    • Katdare, M.1    Singhal, H.2    Newmark, H.3    Osborne, M.P.4
  • 281
    • 0037452434 scopus 로고    scopus 로고
    • The effects of serum on the stability and the transfection activity of the cationic lipid emulsion with various oils
    • Kim, Y. J., Kim, T. W., Chung, H., Kwon, I. C., et al., The effects of serum on the stability and the transfection activity of the cationic lipid emulsion with various oils. Int. J. Pharm. 2003, 252, 241-252.
    • (2003) Int. J. Pharm. , vol.252 , pp. 241-252
    • Kim, Y.J.1    Kim, T.W.2    Chung, H.3    Kwon, I.C.4
  • 282
    • 33745297964 scopus 로고    scopus 로고
    • Skin constituents as cosmetic ingredients. Part I: A study of bio-mimetic monoglycerides behavior at the squalene-water interface by the "pendant drop" method in a static mode
    • Blasco, L., Duracher, L., Forestier, J. P., Vian, L., et al., Skin constituents as cosmetic ingredients. Part I: A study of bio-mimetic monoglycerides behavior at the squalene-water interface by the "pendant drop" method in a static mode. J. Disp. Sci. Technol. 2006, 27, 799-810.
    • (2006) J. Disp. Sci. Technol. , vol.27 , pp. 799-810
    • Blasco, L.1    Duracher, L.2    Forestier, J.P.3    Vian, L.4
  • 283
    • 33749835512 scopus 로고    scopus 로고
    • Submicron lipid emulsion as a drug delivery system for nalbuphine and its prodrugs
    • Wang, J. J., Sung, K. C., Hu, O. Y., Yeh, C. H., et al., Submicron lipid emulsion as a drug delivery system for nalbuphine and its prodrugs. J. Control Release 2006, 115, 140-149.
    • (2006) J. Control Release , vol.115 , pp. 140-149
    • Wang, J.J.1    Sung, K.C.2    Hu, O.Y.3    Yeh, C.H.4
  • 284
    • 54949138806 scopus 로고    scopus 로고
    • Vaccine adjuvants - The dream becomes real
    • Tagliabue, A., Rappuoli, R., Vaccine adjuvants - The dream becomes real. Hum. Vaccines 2008, 4, 347-349.
    • (2008) Hum. Vaccines , vol.4 , pp. 347-349
    • Tagliabue, A.1    Rappuoli, R.2
  • 286
    • 77549088441 scopus 로고    scopus 로고
    • Vaccination, squalene and anti-squalene antibodies: Facts or fiction
    • Lippi, G., Targher, G., Franchini, M., Vaccination, squalene and anti-squalene antibodies: Facts or fiction? Eur. J. Intern. Med. 2010, 21, 70-73.
    • (2010) Eur. J. Intern. Med. , vol.21 , pp. 70-73
    • Lippi, G.1    Targher, G.2    Franchini, M.3
  • 287
    • 14744297261 scopus 로고    scopus 로고
    • Gulf War syndrome: A toxic exposure? A systematic review
    • Gronseth, G. S., Gulf War syndrome: A toxic exposure? A systematic review. Neurol. Clin. 2005, 23, 523.
    • (2005) Neurol. Clin. , vol.23 , pp. 523
    • Gronseth, G.S.1
  • 288
    • 0033974771 scopus 로고    scopus 로고
    • Antibodies to squalene in Gulf War Syndrome
    • Asa, P. B., Cao, Y., Garry, R. F., Antibodies to squalene in Gulf War Syndrome. Exp. Mol. Pathol. 2000, 68, 55-64.
    • (2000) Exp. Mol. Pathol. , vol.68 , pp. 55-64
    • Asa, P.B.1    Cao, Y.2    Garry, R.F.3
  • 289
    • 0036075888 scopus 로고    scopus 로고
    • Antibodies to squalene in recipients of anthrax vaccine
    • Asa, P. B., Wilson, R. B., Garry, R. F., Antibodies to squalene in recipients of anthrax vaccine. Exp. Mol. Pathol. 2002, 73, 19-27.
    • (2002) Exp. Mol. Pathol. , vol.73 , pp. 19-27
    • Asa, P.B.1    Wilson, R.B.2    Garry, R.F.3
  • 290
    • 1842861810 scopus 로고    scopus 로고
    • Detection of antibodies to squalene III. Naturally occurring antibodies to squalene in humans and mice
    • Matyas, G. R., Rao, M., Pittman, P. R., Burge, R., et al., Detection of antibodies to squalene III. Naturally occurring antibodies to squalene in humans and mice. J. Immunol. Methods 2004, 286, 47-67.
    • (2004) J. Immunol. Methods , vol.286 , pp. 47-67
    • Matyas, G.R.1    Rao, M.2    Pittman, P.R.3    Burge, R.4
  • 291
    • 33749472242 scopus 로고    scopus 로고
    • Vaccines with the MF59 adjuvant do not stimulate antibody responses against squalene
    • Del Giudice, G., Fragapane, E., Bugarini, R., Hora, M., et al., Vaccines with the MF59 adjuvant do not stimulate antibody responses against squalene. Clin. Vaccine Immunol. 2006, 13, 1010-1013.
    • (2006) Clin. Vaccine Immunol. , vol.13 , pp. 1010-1013
    • Del Giudice, G.1    Fragapane, E.2    Bugarini, R.3    Hora, M.4
  • 292
    • 1642471800 scopus 로고    scopus 로고
    • Mechanisms of apoptosis induction by nucleoside analogs
    • Sampath, D., Rao, V. A., Plunkett, W., Mechanisms of apoptosis induction by nucleoside analogs. Oncogene 2003, 22, 9063-9074.
    • (2003) Oncogene , vol.22 , pp. 9063-9074
    • Sampath, D.1    Rao, V.A.2    Plunkett, W.3
  • 293
    • 0036636579 scopus 로고    scopus 로고
    • Nucleoside analogues and nucleobases in cancer treatment
    • Galmarini, C. M., Mackey, J. R., Dumontet, C., Nucleoside analogues and nucleobases in cancer treatment. Lancet Oncol. 2002, 3, 415-424.
    • (2002) Lancet Oncol. , vol.3 , pp. 415-424
    • Galmarini, C.M.1    Mackey, J.R.2    Dumontet, C.3
  • 294
    • 33846178254 scopus 로고    scopus 로고
    • Squalenoyl nanomedicines as potential therapeutics
    • Couvreur, P., Stella, B., Reddy, L. H., Hillaireau, H., et al., Squalenoyl nanomedicines as potential therapeutics. Nano. Lett. 2006, 6, 2544-2548.
    • (2006) Nano. Lett. , vol.6 , pp. 2544-2548
    • Couvreur, P.1    Stella, B.2    Reddy, L.H.3    Hillaireau, H.4
  • 295
    • 70350210492 scopus 로고    scopus 로고
    • Conjugation of squalene to acyclovir improves the affinity for biomembrane models
    • Sarpietro, M. G., Micieli, D., Rocco, F., Ceruti, M., et al., Conjugation of squalene to acyclovir improves the affinity for biomembrane models. Int. J. Pharm. 2009, 382, 73-79.
    • (2009) Int. J. Pharm. , vol.382 , pp. 73-79
    • Sarpietro, M.G.1    Micieli, D.2    Rocco, F.3    Ceruti, M.4
  • 296
    • 0001530996 scopus 로고
    • Metabolism of exogenously supplied nucleotides by Escherichia coli
    • Lichtenstein, J., Barner, H. D., Cohen, S. S., Metabolism of exogenously supplied nucleotides by Escherichia coli. J. Biol. Chem. 1960, 235, 457-465.
    • (1960) J. Biol. Chem. , vol.235 , pp. 457-465
    • Lichtenstein, J.1    Barner, H.D.2    Cohen, S.S.3
  • 297
    • 39449128320 scopus 로고    scopus 로고
    • Discovery of new hexagonal supramolecular nanostructures formed by squalenoylation of an anticancer nucleoside analogue
    • Couvreur, P., Reddy, L. H., Mangenot, S., Poupaert, J. H., et al., Discovery of new hexagonal supramolecular nanostructures formed by squalenoylation of an anticancer nucleoside analogue. Small 2008, 4, 247-253.
    • (2008) Small , vol.4 , pp. 247-253
    • Couvreur, P.1    Reddy, L.H.2    Mangenot, S.3    Poupaert, J.H.4
  • 298
    • 56749158321 scopus 로고    scopus 로고
    • Novel PEGylated nanoassemblies made of self-assembled squalenoyl nucleoside analogues
    • Bekkara-Aounallah, F., Gref, R., Othman, M., Reddy, L. H., et al., Novel PEGylated nanoassemblies made of self-assembled squalenoyl nucleoside analogues. Adv. Funct. Mat. 2008, 18, 3715-3725.
    • (2008) Adv. Funct. Mat. , vol.18 , pp. 3715-3725
    • Bekkara-Aounallah, F.1    Gref, R.2    Othman, M.3    Reddy, L.H.4
  • 299
    • 65349102226 scopus 로고    scopus 로고
    • A unified mechanism of action for volatile isoprenoids in plant abiotic stress
    • Vickers, C. E., Gershenzon, J., Lerdau, M. T., Loreto, F., A unified mechanism of action for volatile isoprenoids in plant abiotic stress. Nat. Chem. Biol. 2009, 5, 283-291.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 283-291
    • Vickers, C.E.1    Gershenzon, J.2    Lerdau, M.T.3    Loreto, F.4
  • 300
    • 3042732189 scopus 로고    scopus 로고
    • Inactivation of sll1556 in Synechocystis strain PCC 6803 impairs isoprenoid biosynthesis from pentose phosphate cycle substrates in vitro
    • Poliquin, K., Ershov, Y. V., Cunningham, F. X., Jr., Woreta, T. T., et al., Inactivation of sll1556 in Synechocystis strain PCC 6803 impairs isoprenoid biosynthesis from pentose phosphate cycle substrates in vitro. J. Bacteriol. 2004, 186, 4685-4693.
    • (2004) J. Bacteriol. , vol.186 , pp. 4685-4693
    • Poliquin, K.1    Ershov, Y.V.2    Cunningham Jr., F.X.3    Woreta, T.T.4
  • 301
    • 9244259666 scopus 로고    scopus 로고
    • Type II isopentenyl diphosphate isomerase from Synechocystis sp strain PCC 6803
    • Barkley, S. J., Desai, S. B., Poulter, C. D., Type II isopentenyl diphosphate isomerase from Synechocystis sp strain PCC 6803. J. Bacteriol. 2004, 186, 8156-8158.
    • (2004) J. Bacteriol. , vol.186 , pp. 8156-8158
    • Barkley, S.J.1    Desai, S.B.2    Poulter, C.D.3
  • 302
  • 303
    • 50849084804 scopus 로고    scopus 로고
    • Evaluation of asymmetric liposomal nanoparticles for encapsulation of polynucleotides
    • Whittenton, J., Harendra, S., Pitchumani, R., Mohanty, K., et al., Evaluation of asymmetric liposomal nanoparticles for encapsulation of polynucleotides. Langmuir 2008, 24, 8533-8540.
    • (2008) Langmuir , vol.24 , pp. 8533-8540
    • Whittenton, J.1    Harendra, S.2    Pitchumani, R.3    Mohanty, K.4
  • 304
    • 85087250867 scopus 로고
    • A compendium of vaccine adjuvants and excipients
    • Vogel, F. R., Powell, M. F., A compendium of vaccine adjuvants and excipients. Pharm. Biotechnol. 1995, 6.
    • (1995) Pharm. Biotechnol. , pp. 6
    • Vogel, F.R.1    Powell, M.F.2
  • 305
    • 0035962389 scopus 로고    scopus 로고
    • Oil components modulate physical characteristics and function of the natural oil emulsions as drug or gene delivery system
    • Chung, H., Kim, T. W., Kwon, M., Kwon, I. C., et al., Oil components modulate physical characteristics and function of the natural oil emulsions as drug or gene delivery system. J. Control Release 2001, 71, 339-350.
    • (2001) J. Control Release , vol.71 , pp. 339-350
    • Chung, H.1    Kim, T.W.2    Kwon, M.3    Kwon, I.C.4


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