메뉴 건너뛰기




Volumn 221, Issue 4, 1999, Pages 294-311

Isoprenoid-mediated inhibition of mevalonate synthesis: Potential application to cancer

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TOCOPHEROL; ALPHA TOCOTRIENOL; ASCORBIC ACID; BETA CAROTENE; BETA IONONE; CHOLESTEROL; FARNESOL; GERANIOL; GROWTH HORMONE RECEPTOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; ISOPRENOID; LAMIN A; LAMIN B; LIMONENE; MESSENGER RNA; MEVINOLIN; PERILLYL ALCOHOL; RAS PROTEIN;

EID: 0032868926     PISSN: 00379727     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1525-1373.1999.d01-87.x     Document Type: Short Survey
Times cited : (126)

References (315)
  • 1
    • 0003966001 scopus 로고
    • Washington, DC: National Academy Press
    • Committee on Diet, Nutrition, and Cancer. Diet, Nutrition, and Cancer. Washington, DC: National Academy Press, 1982.
    • (1982) Diet, Nutrition, and Cancer
  • 2
    • 0003406921 scopus 로고
    • Washington, DC: U.S. Government Printing Office, Home and Garden Bulletin No. 232 (Fourth Edition)
    • U.S. Department of Agriculture, U.S. Department of Health and Human Services. Nutrition and Your Health: Dietary Guidelines for Americans. Washington, DC: U.S. Government Printing Office, Home and Garden Bulletin No. 232 (Fourth Edition), 1995.
    • (1995) Nutrition and Your Health: Dietary Guidelines for Americans
  • 3
    • 0003500939 scopus 로고
    • Washington, DC: U.S. Government Printing Office, NIH Publication No. 86-2880
    • U.S. Department of Health and Human Services, Public Health Service, National Institutes of Health. NCI monographs: Cancer Control Objectives for the Nation, 1985-2000. Washington, DC: U.S. Government Printing Office, NIH Publication No. 86-2880, 1986.
    • (1986) NCI Monographs: Cancer Control Objectives for the Nation, 1985-2000
  • 6
    • 0026526132 scopus 로고
    • The lessons of life: Keynote address to the nutrition and cancer conference
    • Doll R. The lessons of life: Keynote address to the nutrition and cancer conference. Cancer Res 52:S2024-S2029, 1992.
    • (1992) Cancer Res , vol.52
    • Doll, R.1
  • 7
    • 0029568005 scopus 로고
    • Diet, nutrition, and avoidable cancer
    • Willett WC. Diet, nutrition, and avoidable cancer. Environ Health Perspect 103:S165-S170, 1995.
    • (1995) Environ Health Perspect , vol.103
    • Willett, W.C.1
  • 8
    • 3643049982 scopus 로고    scopus 로고
    • Can we prevent cancer by diet today?
    • Willett WC. Can we prevent cancer by diet today? Proc Am Assn Cancer Res 37:644-645, 1996.
    • (1996) Proc Am Assn Cancer Res , vol.37 , pp. 644-645
    • Willett, W.C.1
  • 9
    • 0028176277 scopus 로고
    • Diet and cancer
    • Austoker J. Diet and cancer. BMJ 308:1610-1614, 1994.
    • (1994) BMJ , vol.308 , pp. 1610-1614
    • Austoker, J.1
  • 11
  • 13
    • 0029816924 scopus 로고    scopus 로고
    • Nutrient intake in relation to bladder cancer among middle-aged men and women
    • Bruemmer B, White E, Vaughan TL, Cheney CL. Nutrient intake in relation to bladder cancer among middle-aged men and women. Am J Epidemiol 144:485-495, 1996.
    • (1996) Am J Epidemiol , vol.144 , pp. 485-495
    • Bruemmer, B.1    White, E.2    Vaughan, T.L.3    Cheney, C.L.4
  • 15
    • 0027872310 scopus 로고
    • Reduced risk of colon cancer with high intake of vitamin E: The Iowa women's health study
    • Steinmetz KA, Folsom AR. Reduced risk of colon cancer with high intake of vitamin E: The Iowa women's health study. Cancer Res 53:4230-4237, 1993.
    • (1993) Cancer Res , vol.53 , pp. 4230-4237
    • Steinmetz, K.A.1    Folsom, A.R.2
  • 18
    • 0025232254 scopus 로고
    • Dietary fiber, vegetables, and colon cancer: Critical review and meta-analyses of the epidemiologic data
    • Trock B, Lanza E, Greenwald P. Dietary fiber, vegetables, and colon cancer: Critical review and meta-analyses of the epidemiologic data. J Natl Cancer Inst 82:650-661, 1990.
    • (1990) J Natl Cancer Inst , vol.82 , pp. 650-661
    • Trock, B.1    Lanza, E.2    Greenwald, P.3
  • 19
    • 0020587373 scopus 로고
    • Inhibition of neoplasia by minor dietary constituents
    • Wattenberg LW. Inhibition of neoplasia by minor dietary constituents. Cancer Res 43:S2448-S2453, 1983.
    • (1983) Cancer Res , vol.43
    • Wattenberg, L.W.1
  • 20
    • 0025454581 scopus 로고
    • Inhibition of carcinogenesis by minor anutrient constituents of the diet
    • Wattenberg LW. Inhibition of carcinogenesis by minor anutrient constituents of the diet. Proc Nutr Soc 49:173-183, 1990.
    • (1990) Proc Nutr Soc , vol.49 , pp. 173-183
    • Wattenberg, L.W.1
  • 21
    • 0026590679 scopus 로고
    • Inhibition of carcinogenesis by minor dietary constituents
    • Wattenberg LW. Inhibition of carcinogenesis by minor dietary constituents. Cancer Res 52:S2085-S2091, 1992.
    • (1992) Cancer Res , vol.52
    • Wattenberg, L.W.1
  • 22
    • 0029864694 scopus 로고    scopus 로고
    • Chemoprevention of cancer
    • Wattenberg LW. Chemoprevention of cancer. Prev Med 25:44-45, 1996.
    • (1996) Prev Med , vol.25 , pp. 44-45
    • Wattenberg, L.W.1
  • 23
    • 0023870472 scopus 로고
    • Anticarcinogenic activity of d-limonene during the initiation and promotion/progression stages of DMBA-induced rat mammary carcinogenesis
    • Elson CE, Maltzman TH, Boston JL, Tanner MA, Gould MN. Anticarcinogenic activity of d-limonene during the initiation and promotion/progression stages of DMBA-induced rat mammary carcinogenesis. Carcinogenesis 9:331-332, 1988.
    • (1988) Carcinogenesis , vol.9 , pp. 331-332
    • Elson, C.E.1    Maltzman, T.H.2    Boston, J.L.3    Tanner, M.A.4    Gould, M.N.5
  • 24
    • 0030846307 scopus 로고    scopus 로고
    • Creating isoprenoid diversity
    • Sacchettini JC, Poulter CD. Creating isoprenoid diversity. Science 277:1788-1789, 1997.
    • (1997) Science , vol.277 , pp. 1788-1789
    • Sacchettini, J.C.1    Poulter, C.D.2
  • 25
    • 0028906885 scopus 로고
    • Some new aspects of isoprenoid biosynthesis in plants: A review
    • Bach TJ. Some new aspects of isoprenoid biosynthesis in plants: A review. Lipids 30:191-202, 1995.
    • (1995) Lipids , vol.30 , pp. 191-202
    • Bach, T.J.1
  • 26
    • 0032520232 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: Manifold chemistry catalyzed by similar enzymes
    • London
    • Wendt KU, Schulz GE. Isoprenoid biosynthesis: Manifold chemistry catalyzed by similar enzymes. Structure (London) 6:127-133, 1998.
    • (1998) Structure , vol.6 , pp. 127-133
    • Wendt, K.U.1    Schulz, G.E.2
  • 27
    • 0030295152 scopus 로고    scopus 로고
    • Isoprenylated flavonoids: A survey
    • Barron D, Ibrahim RA. Isoprenylated flavonoids: A survey. Phytochem 43:921-982, 1996.
    • (1996) Phytochem , vol.43 , pp. 921-982
    • Barron, D.1    Ibrahim, R.A.2
  • 28
    • 0023022871 scopus 로고
    • The structure of an inhibitor of cholesterol biosynthesis isolated from barley
    • Qureshi AA, Burger WC, Peterson DA, Elson CE. The structure of an inhibitor of cholesterol biosynthesis isolated from barley. J Biol Chem 261:10544-10550, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 10544-10550
    • Qureshi, A.A.1    Burger, W.C.2    Peterson, D.A.3    Elson, C.E.4
  • 29
    • 0027288196 scopus 로고
    • Tocotrienols regulate cholesterol production in mammalian cells by post-transcriptional suppression of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Parker RA, Pearce BC, Clark RW, Gordan DA, Wright JJK. Tocotrienols regulate cholesterol production in mammalian cells by post-transcriptional suppression of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J Biol Chem 268:11230-11238, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 11230-11238
    • Parker, R.A.1    Pearce, B.C.2    Clark, R.W.3    Gordan, D.A.4    Wright, J.J.K.5
  • 30
    • 0027451612 scopus 로고
    • Importance of mevalonate-derived products in the control of HMG-CoA reductase activity and growth of human lung adenocarcinoma cell line A549
    • Bennis F, Favre G, Le Gaillard F, Soula G. Importance of mevalonate-derived products in the control of HMG-CoA reductase activity and growth of human lung adenocarcinoma cell line A549. Int J Cancer 55:640-645, 1993.
    • (1993) Int J Cancer , vol.55 , pp. 640-645
    • Bennis, F.1    Favre, G.2    Le Gaillard, F.3    Soula, G.4
  • 32
    • 0019941618 scopus 로고
    • The mechanism of cyclic monoterpene inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase in vivo in the rat
    • Clegg RJ, Middleton B, Bell GD, White DA. The mechanism of cyclic monoterpene inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase in vivo in the rat. J Biol Chem 257:2294-2299, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 2294-2299
    • Clegg, R.J.1    Middleton, B.2    Bell, G.D.3    White, D.A.4
  • 33
    • 0021228387 scopus 로고
    • Inhibition of hepatic cholesterogenesis by d-limonene and abscisic acid in chickens
    • Haq PU, Din ZZ, Shrago E, Elson CE, Qureshi AA. Inhibition of hepatic cholesterogenesis by d-limonene and abscisic acid in chickens. Fed Proc 43:1866A, 1984.
    • (1984) Fed Proc , vol.43
    • Haq, P.U.1    Din, Z.Z.2    Shrago, E.3    Elson, C.E.4    Qureshi, A.A.5
  • 34
    • 0028245392 scopus 로고
    • The chemoprevention of cancer by mevalonate-derived constituents of fruits and vegetables
    • Elson CE, Yu SG. The chemoprevention of cancer by mevalonate-derived constituents of fruits and vegetables. J Nutr 124:607-614, 1994.
    • (1994) J Nutr , vol.124 , pp. 607-614
    • Elson, C.E.1    Yu, S.G.2
  • 35
    • 0029048924 scopus 로고
    • Suppression of mevalonate pathway activities by dietary isoprenoids: Protective roles in cancer and cardiovascular disease
    • Elson CE. Suppression of mevalonate pathway activities by dietary isoprenoids: Protective roles in cancer and cardiovascular disease. J Nutr 125:S1666-S1672, 1995.
    • (1995) J Nutr , vol.125
    • Elson, C.E.1
  • 36
    • 0029903431 scopus 로고    scopus 로고
    • Novel lipids and cancer: Isoprenoids and other phytochemicals
    • Heber D, Kritchevsky D, Eds. New York: Plenum Publishing Corporation
    • Elson CE. Novel lipids and cancer: Isoprenoids and other phytochemicals. In: Heber D, Kritchevsky D, Eds. Dietary Fats, Lipids, Hormones, and Tumorigenesis. New York: Plenum Publishing Corporation, pp 71-86, 1996.
    • (1996) Dietary Fats, Lipids, Hormones, and Tumorigenesis , pp. 71-86
    • Elson, C.E.1
  • 37
    • 0003053770 scopus 로고    scopus 로고
    • Targeting the action of isoprenoids and related phytochemicals to tumors
    • Heber D, Blackburn GL, Go VLW, Eds. San Diego, CA: Academic Press
    • Mo H, Peffley DM, Elson CE. Targeting the action of isoprenoids and related phytochemicals to tumors. In: Heber D, Blackburn GL, Go VLW, Eds. Nutritional Oncology. San Diego, CA: Academic Press, pp 379-391, 1998.
    • (1998) Nutritional Oncology , pp. 379-391
    • Mo, H.1    Peffley, D.M.2    Elson, C.E.3
  • 39
    • 0027965512 scopus 로고
    • Mammary carcinoma regression induced by perillyl alcohol, a hydroxylated analog of limonene
    • Haag JD, Gould MN. Mammary carcinoma regression induced by perillyl alcohol, a hydroxylated analog of limonene. Cancer Chemother Pharmacol 34:477-483, 1994.
    • (1994) Cancer Chemother Pharmacol , vol.34 , pp. 477-483
    • Haag, J.D.1    Gould, M.N.2
  • 40
    • 0032906921 scopus 로고    scopus 로고
    • Apoptosis and cell-cycle arrest in human and murine tumor cells are initiated by isoprenoids
    • Mo H, Elson CE. Apoptosis and cell-cycle arrest in human and murine tumor cells are initiated by isoprenoids. J Nutr 129:804-813, 1999.
    • (1999) J Nutr , vol.129 , pp. 804-813
    • Mo, H.1    Elson, C.E.2
  • 41
    • 0030994450 scopus 로고    scopus 로고
    • Vitamin K2 and its derivatives induce apoptosis in leukemia cells and enhance the effect of all-trans-retinoic acid
    • Yaguchi M, Miyazawa K, Katagiri T, Nishimaki J, Kizaki M, Tohyama K, Toyama K. Vitamin K2 and its derivatives induce apoptosis in leukemia cells and enhance the effect of all-trans-retinoic acid. Leukemia 11:779-787, 1997.
    • (1997) Leukemia , vol.11 , pp. 779-787
    • Yaguchi, M.1    Miyazawa, K.2    Katagiri, T.3    Nishimaki, J.4    Kizaki, M.5    Tohyama, K.6    Toyama, K.7
  • 42
    • 0028289655 scopus 로고
    • Differences in sensitivity to farnesol toxicity between neoplastically-and non-neoplastically-derived cells in culture
    • Adany I, Yazlovitskaya EM, Haug JS, Voziyan PA, Melnykovych G. Differences in sensitivity to farnesol toxicity between neoplastically-and non-neoplastically-derived cells in culture. Cancer Lett 79:175-179, 1994.
    • (1994) Cancer Lett , vol.79 , pp. 175-179
    • Adany, I.1    Yazlovitskaya, E.M.2    Haug, J.S.3    Voziyan, P.A.4    Melnykovych, G.5
  • 43
    • 0026707248 scopus 로고
    • Growth inhibition of leukemia cell line CEM-C1 by farnesol: Effects of phosphatidylcholine and diacylglycerol
    • Melnykovysh G, Haug JS, Goldner CM. Growth inhibition of leukemia cell line CEM-C1 by farnesol: Effects of phosphatidylcholine and diacylglycerol. Biochem Biophys Res Commun 186:543-548, 1992.
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 543-548
    • Melnykovysh, G.1    Haug, J.S.2    Goldner, C.M.3
  • 44
    • 0028300763 scopus 로고
    • Modulation of the mevalonate pathway and cell growth by pravastatin and d-limonene in a human hepatoma cell line (Hep G2)
    • Kawata S, Nagase T, Yamasaki E, Ishiguro H, Matsuzawa Y. Modulation of the mevalonate pathway and cell growth by pravastatin and d-limonene in a human hepatoma cell line (Hep G2). Br J Cancer 69:1015-1020, 1994.
    • (1994) Br J Cancer , vol.69 , pp. 1015-1020
    • Kawata, S.1    Nagase, T.2    Yamasaki, E.3    Ishiguro, H.4    Matsuzawa, Y.5
  • 45
    • 0030598825 scopus 로고    scopus 로고
    • Farnesol and geranylgeraniol induce actin cytoskeleton disorganization and apoptosis in A549 lung adenocarcinoma cells
    • Miquel K, Pradines A, Favre G. Farnesol and geranylgeraniol induce actin cytoskeleton disorganization and apoptosis in A549 lung adenocarcinoma cells. Biochem Biophys Res Commun 225:869-876, 1996.
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 869-876
    • Miquel, K.1    Pradines, A.2    Favre, G.3
  • 46
    • 0028863013 scopus 로고
    • Lycopene is a more potent inhibitor of human cancer cell proliferation than either α-carotene or β-carotene
    • Levy J, Bosin E, Feldman B, Giat Y, Miinster A, Danilenko M, Sharoni Y. Lycopene is a more potent inhibitor of human cancer cell proliferation than either α-carotene or β-carotene. Nutr Cancer 24:257-266, 1995.
    • (1995) Nutr Cancer , vol.24 , pp. 257-266
    • Levy, J.1    Bosin, E.2    Feldman, B.3    Giat, Y.4    Miinster, A.5    Danilenko, M.6    Sharoni, Y.7
  • 47
    • 0031056450 scopus 로고    scopus 로고
    • Inhibition of pancreatic cancer growth by the dietary isoprenoids farnesol and geraniol
    • Burke YD, Stark MJ, Roach SL, Sen SE, Crowell PL. Inhibition of pancreatic cancer growth by the dietary isoprenoids farnesol and geraniol. Lipids 32:151-156, 1997.
    • (1997) Lipids , vol.32 , pp. 151-156
    • Burke, Y.D.1    Stark, M.J.2    Roach, S.L.3    Sen, S.E.4    Crowell, P.L.5
  • 48
    • 0028832005 scopus 로고
    • Selective farnesol toxicity and translocation of protein kinase C in neoplastic HeLa-S3K and non-neoplastic CF-3 cells
    • Yazlovitskaya EM, Melnykovych G. Selective farnesol toxicity and translocation of protein kinase C in neoplastic HeLa-S3K and non-neoplastic CF-3 cells. Cancer Lett 88:179-183, 1995.
    • (1995) Cancer Lett , vol.88 , pp. 179-183
    • Yazlovitskaya, E.M.1    Melnykovych, G.2
  • 49
    • 0031427722 scopus 로고    scopus 로고
    • Induction of the apoptosis-promoting protein Bak by perillyl alcohol in pancreatic ductal adenocarcinoma relative to untransformed ductal epithelial cells
    • Stayrook KR, McKinzie JH, Burke YD, Burke YA, Crowell PL. Induction of the apoptosis-promoting protein Bak by perillyl alcohol in pancreatic ductal adenocarcinoma relative to untransformed ductal epithelial cells. Carcinogenesis 18:1655-1658, 1997.
    • (1997) Carcinogenesis , vol.18 , pp. 1655-1658
    • Stayrook, K.R.1    McKinzie, J.H.2    Burke, Y.D.3    Burke, Y.A.4    Crowell, P.L.5
  • 50
    • 0028843982 scopus 로고
    • Geraniol, an inhibitor of mevalonate biosynthesis, suppresses the growth of hepatomas and melanomas transplanted to rats and mice
    • Yu SG, Hildebrandt LA, Elson CE. Geraniol, an inhibitor of mevalonate biosynthesis, suppresses the growth of hepatomas and melanomas transplanted to rats and mice. J Nutr 125:2763-2767, 1995.
    • (1995) J Nutr , vol.125 , pp. 2763-2767
    • Yu, S.G.1    Hildebrandt, L.A.2    Elson, C.E.3
  • 51
    • 0026027665 scopus 로고
    • Concentration-dependent increase in murine P388 and B16 population doubling time by the acyclic monoterpene geraniol
    • Shoff SM, Grummer M, Yatvin MB, Elson CE. Concentration-dependent increase in murine P388 and B16 population doubling time by the acyclic monoterpene geraniol. Cancer Res 51:37-42, 1991.
    • (1991) Cancer Res , vol.51 , pp. 37-42
    • Shoff, S.M.1    Grummer, M.2    Yatvin, M.B.3    Elson, C.E.4
  • 52
    • 0029792650 scopus 로고    scopus 로고
    • Effects of monoterpenes and mevinolin on murine colon tumor CT-26 in vitro and its hepatic metastases in vivo
    • American Institute for Cancer Research, Ed. New York: Plenum Press
    • Broitman SA, Wilkinson J IV, Cerda S, Branch SK. Effects of monoterpenes and mevinolin on murine colon tumor CT-26 in vitro and its hepatic metastases in vivo. In: American Institute for Cancer Research, Ed. Dietary Phytochemicals in Cancer Prevention and Treatment. New York: Plenum Press, pp 111-130, 1996.
    • (1996) Dietary Phytochemicals in Cancer Prevention and Treatment , pp. 111-130
    • Broitman, S.A.1    Wilkinson IV, J.2    Cerda, S.3    Branch, S.K.4
  • 53
    • 0030950694 scopus 로고    scopus 로고
    • Isoprenoids suppress the growth of murine B16 melanomas in vitro and in vivo
    • He L, Mo H, Hadisusilo S, Qureshi AA, Elson CE. Isoprenoids suppress the growth of murine B16 melanomas in vitro and in vivo. J Nutr 127:668-674, 1997.
    • (1997) J Nutr , vol.127 , pp. 668-674
    • He, L.1    Mo, H.2    Hadisusilo, S.3    Qureshi, A.A.4    Elson, C.E.5
  • 54
    • 33751156171 scopus 로고
    • The efficacy of β-ionone in the chemoprevention of rat mammary carcinogenesis
    • Yu SG, Anderson PJ, Elson CE. The efficacy of β-ionone in the chemoprevention of rat mammary carcinogenesis. J Agric Food Chem 43:2144-2147, 1995.
    • (1995) J Agric Food Chem , vol.43 , pp. 2144-2147
    • Yu, S.G.1    Anderson, P.J.2    Elson, C.E.3
  • 55
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • London
    • Goldstein JL, Brown MS. Regulation of the mevalonate pathway. Nature (London) 343:425-430, 1990.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 56
    • 0019135838 scopus 로고
    • Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth
    • Brown MS, Goldstein JL. Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth. J Lipid Res 21:505-517, 1980.
    • (1980) J Lipid Res , vol.21 , pp. 505-517
    • Brown, M.S.1    Goldstein, J.L.2
  • 57
    • 0030632619 scopus 로고    scopus 로고
    • Signaling molecules derived from the cholesterol biosynthetic pathway
    • Jackson SM, Ericsson J, Edwards PA. Signaling molecules derived from the cholesterol biosynthetic pathway. Subcellular Biochem 28:1-21, 1997.
    • (1997) Subcellular Biochem , vol.28 , pp. 1-21
    • Jackson, S.M.1    Ericsson, J.2    Edwards, P.A.3
  • 58
    • 0018369386 scopus 로고
    • Synthesis of ubiquinone and cholesterol in human fibroblasts: Regulation of a branched pathway
    • Faust JR, Goldstein JL, Brown MS. Synthesis of ubiquinone and cholesterol in human fibroblasts: Regulation of a branched pathway. Arch Biochem Biophys 192:86-89, 1979.
    • (1979) Arch Biochem Biophys , vol.192 , pp. 86-89
    • Faust, J.R.1    Goldstein, J.L.2    Brown, M.S.3
  • 59
    • 0031568243 scopus 로고    scopus 로고
    • Inhibition of squalene synthase but not squalene cyclase prevents mevalonate-mediated suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase synthesis at a post-transcriptional level
    • Peffley DM, Gayen AK. Inhibition of squalene synthase but not squalene cyclase prevents mevalonate-mediated suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase synthesis at a post-transcriptional level. Arch Biochem Biophy 337:251-260, 1997.
    • (1997) Arch Biochem Biophy , vol.337 , pp. 251-260
    • Peffley, D.M.1    Gayen, A.K.2
  • 60
    • 0022383696 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase synthesis by a nonsterol mevalonate-derived product in Mev-1 cells
    • Peffley D, Sinensky M. Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase synthesis by a nonsterol mevalonate-derived product in Mev-1 cells. J Biol Chem 260:9949-9952, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 9949-9952
    • Peffley, D.1    Sinensky, M.2
  • 61
    • 0026521041 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase synthesis in Syrian hamster C100 cells by mevinolin, 25-hydroxycholesterol, and mevalonate: The role of post-transcriptional control
    • Peffley DM. Regulation of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase synthesis in Syrian hamster C100 cells by mevinolin, 25-hydroxycholesterol, and mevalonate: The role of post-transcriptional control. Somat Cell Mol Genet 18:19-32, 1992.
    • (1992) Somat Cell Mol Genet , vol.18 , pp. 19-32
    • Peffley, D.M.1
  • 62
    • 0023902411 scopus 로고
    • Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase: Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme
    • Nakanishi M, Goldstein JL, Brown MS. Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase: Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme. J Biol Chem 263:8929-8937, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 8929-8937
    • Nakanishi, M.1    Goldstein, J.L.2    Brown, M.S.3
  • 63
    • 0024237563 scopus 로고
    • Further characterization of a somatic cell mutant defective in regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Peffley D, Miyake J, Leonard S, vonGunten C, Sinensky M. Further characterization of a somatic cell mutant defective in regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Somat Cell Mol Genet 14:527-539, 1988.
    • (1988) Somat Cell Mol Genet , vol.14 , pp. 527-539
    • Peffley, D.1    Miyake, J.2    Leonard, S.3    VonGunten, C.4    Sinensky, M.5
  • 64
    • 0027771498 scopus 로고
    • Inhibition of protein synthesis in baby hamster kidney cells blocks oxysterol-mediated suppression of 3-hydroxy-3-methylglutaryl-CoA reductase mRNA at a post-transcriptional level
    • Choi JW, Lundquist EN, Peffley DM. Inhibition of protein synthesis in baby hamster kidney cells blocks oxysterol-mediated suppression of 3-hydroxy-3-methylglutaryl-CoA reductase mRNA at a post-transcriptional level. Biochem J 296:859-866, 1993.
    • (1993) Biochem J , vol.296 , pp. 859-866
    • Choi, J.W.1    Lundquist, E.N.2    Peffley, D.M.3
  • 65
    • 0021243768 scopus 로고
    • Diurnal rhythm of rat liver mRNAs encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Clarke CF, Fogelman AM, Edwards PA. Diurnal rhythm of rat liver mRNAs encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem 259:10439-10447, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 10439-10447
    • Clarke, C.F.1    Fogelman, A.M.2    Edwards, P.A.3
  • 66
    • 0022384475 scopus 로고
    • 5′-End of HMG-CoA reductase gene contains sequences responsible for cholesterol-mediated inhibition of transcription
    • Osborne TF, Goldstein JL, Brown MS. 5′-End of HMG-CoA reductase gene contains sequences responsible for cholesterol-mediated inhibition of transcription. Cell 42:203-212, 1985.
    • (1985) Cell , vol.42 , pp. 203-212
    • Osborne, T.F.1    Goldstein, J.L.2    Brown, M.S.3
  • 67
    • 0023833752 scopus 로고
    • Operator constitutive mutation of 3-hydroxy-3-methylglutaryl coenzyme A reductase promoter abolishes protein binding to sterol regulatory element
    • Osborne TF, Gil G, Goldstein JL, Brown MS. Operator constitutive mutation of 3-hydroxy-3-methylglutaryl coenzyme A reductase promoter abolishes protein binding to sterol regulatory element. J Biol Chem 263:3380-3387, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 3380-3387
    • Osborne, T.F.1    Gil, G.2    Goldstein, J.L.3    Brown, M.S.4
  • 68
    • 0343395006 scopus 로고
    • Multiple genes encode nuclear factor 1-like proteins that bind to the promoter for 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Gil G, Smith JR, Goldstein JL, Slaughter CA, Orth K, Brown MS, Osborne TF. Multiple genes encode nuclear factor 1-like proteins that bind to the promoter for 3-hydroxy-3-methylglutaryl coenzyme A reductase. Proc Natl Acad Sci USA 85:8963-8967, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8963-8967
    • Gil, G.1    Smith, J.R.2    Goldstein, J.L.3    Slaughter, C.A.4    Orth, K.5    Brown, M.S.6    Osborne, T.F.7
  • 70
    • 0021985646 scopus 로고
    • Mechanisms of 3-hydroxy-3-methylglutaryl coenzyme A reductase overaccumulation in three compactin-resistant cell lines
    • Skalnik DG, Brown DA, Brown PC, Friedman RL, Hardeman EC, Schimke RF, Simoni RD. Mechanisms of 3-hydroxy-3-methylglutaryl coenzyme A reductase overaccumulation in three compactin-resistant cell lines. J Biol Chem 260:1991-1994, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 1991-1994
    • Skalnik, D.G.1    Brown, D.A.2    Brown, P.C.3    Friedman, R.L.4    Hardeman, E.C.5    Schimke, R.F.6    Simoni, R.D.7
  • 71
    • 0025934102 scopus 로고
    • Regulation of gene expression and synthesis and degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by micellar cholesterol in CaCo-2 cells
    • Field JF, Shreves T, Fujiwara D, Murthy S, Albright E, Mathur SN. Regulation of gene expression and synthesis and degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by micellar cholesterol in CaCo-2 cells. J Lipid Res 32:1811-1821, 1991.
    • (1991) J Lipid Res , vol.32 , pp. 1811-1821
    • Field, J.F.1    Shreves, T.2    Fujiwara, D.3    Murthy, S.4    Albright, E.5    Mathur, S.N.6
  • 72
    • 0021039333 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl coenzyme A activity in avian rnyeloblasts
    • Tanaka RD, Edwards PA, Lau SF, Fogelman AM. Regulation of 3-hydroxy-3-methylglutaryl coenzyme A activity in avian rnyeloblasts. J Biol Chem 258:13331-13339, 1980.
    • (1980) J Biol Chem , vol.258 , pp. 13331-13339
    • Tanaka, R.D.1    Edwards, P.A.2    Lau, S.F.3    Fogelman, A.M.4
  • 73
    • 0027525579 scopus 로고
    • Modulation of 3-hydroxy-3-methylglutaryl-CoA reductase by 15α-fluorolanost-7-en-3β-ol: A mechanism-based inhibitor of cholesterol biosynthesis
    • Trzaskos JM, Magolda RL, Favata MG, Fischer RT, Johnson PR, Chen HW, Ko SS, Leonard DA, Gaylor JL. Modulation of 3-hydroxy-3-methylglutaryl-CoA reductase by 15α-fluorolanost-7-en-3β-ol: A mechanism-based inhibitor of cholesterol biosynthesis. J Biol Chem 268:22591-22599, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 22591-22599
    • Trzaskos, J.M.1    Magolda, R.L.2    Favata, M.G.3    Fischer, R.T.4    Johnson, P.R.5    Chen, H.W.6    Ko, S.S.7    Leonard, D.A.8    Gaylor, J.L.9
  • 74
    • 0025993049 scopus 로고
    • Differences between the regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and low-density lipoprotein receptor in human hepatoma cells and fibroblasts reside primarily at the translational and post-translational levels
    • Tam SP, Brissette L, Ramharack R, Deeley RG. Differences between the regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and low-density lipoprotein receptor in human hepatoma cells and fibroblasts reside primarily at the translational and post-translational levels. J Biol Chem 266:16764-16773, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 16764-16773
    • Tam, S.P.1    Brissette, L.2    Ramharack, R.3    Deeley, R.G.4
  • 75
    • 0020619724 scopus 로고
    • Mevalonolactone inhibits the rate of synthesis and enhances the rate of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes
    • Edwards PA, Lan SF, Tanaka RD, Fogelman AM. Mevalonolactone inhibits the rate of synthesis and enhances the rate of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes. J Biol Chem 258:7272-7275, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 7272-7275
    • Edwards, P.A.1    Lan, S.F.2    Tanaka, R.D.3    Fogelman, A.M.4
  • 76
    • 0021473810 scopus 로고
    • Effects of compactin on the levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase in compactin-resistant C100 and wild-type cells
    • Hardeman E, Endo A, Simoni R. Effects of compactin on the levels of 3-hydroxy-3-methylglutaryl coenzyme A reductase in compactin-resistant C100 and wild-type cells. Arch Biochem Biophys 232:549-561, 1984.
    • (1984) Arch Biochem Biophys , vol.232 , pp. 549-561
    • Hardeman, E.1    Endo, A.2    Simoni, R.3
  • 77
    • 0024547018 scopus 로고
    • Phosphorylation of native 97-kDa 3-hydroxy-3-methylglutaryl coenzyme A reductase from rat liver
    • Parker RA, Miller SJ, Gibson DM. Phosphorylation of native 97-kDa 3-hydroxy-3-methylglutaryl coenzyme A reductase from rat liver. J Biol Chem 264:4877-4887, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 4877-4887
    • Parker, R.A.1    Miller, S.J.2    Gibson, D.M.3
  • 78
    • 0028157541 scopus 로고
    • Mevalonic acid-dependent degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo and in vitro
    • Correll CC, Edwards PA. Mevalonic acid-dependent degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo and in vitro. J Biol Chem 269:633-638, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 633-638
    • Correll, C.C.1    Edwards, P.A.2
  • 79
    • 0021856440 scopus 로고
    • Membrane-bound domain of HMG-CoA reductase is required for sterol-enhanced degradation of the enzyme
    • Gil G, Faust JR, Chin DJ, Goldstein JL, Brown MS. Membrane-bound domain of HMG-CoA reductase is required for sterol-enhanced degradation of the enzyme. Cell 41:249-258, 1985.
    • (1985) Cell , vol.41 , pp. 249-258
    • Gil, G.1    Faust, J.R.2    Chin, D.J.3    Goldstein, J.L.4    Brown, M.S.5
  • 80
    • 0020571671 scopus 로고
    • Inhibition of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by mevinolin
    • Sinensky S, Logel J. Inhibition of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by mevinolin. J Biol Chem 258:8547-8549, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 8547-8549
    • Sinensky, S.1    Logel, J.2
  • 81
    • 0031239831 scopus 로고    scopus 로고
    • Farnesol as a regulator of HMG-CoA reductase degradation: Characterization and role of farnesyl pyrophosphatase
    • Meigs TE, Simoni RD. Farnesol as a regulator of HMG-CoA reductase degradation: Characterization and role of farnesyl pyrophosphatase. Arch Biochem Biophys 345:1-9, 1997.
    • (1997) Arch Biochem Biophys , vol.345 , pp. 1-9
    • Meigs, T.E.1    Simoni, R.D.2
  • 82
    • 0028307290 scopus 로고
    • Identification of farnesol as the nonsterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Correll CC, Ng L, Edwards PA. Identification of farnesol as the nonsterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J Biol Chem 269:17390-17393, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 17390-17393
    • Correll, C.C.1    Ng, L.2    Edwards, P.A.3
  • 83
    • 0029969302 scopus 로고    scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the nonsterol mevalonate metabolite farnesol in vivo
    • Meigs TE, Roseman DS, Simoni RD. Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the nonsterol mevalonate metabolite farnesol in vivo. J Biol Chem 271:7916-7922, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 7916-7922
    • Meigs, T.E.1    Roseman, D.S.2    Simoni, R.D.3
  • 84
    • 0026742623 scopus 로고
    • Red25, a protein that binds specifically to the sterol regulatory region in the promoter for 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Osborne TF, Bennett M, Rhee K. Red25, a protein that binds specifically to the sterol regulatory region in the promoter for 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem 267:18973-18982, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 18973-18982
    • Osborne, T.F.1    Bennett, M.2    Rhee, K.3
  • 86
    • 0011176887 scopus 로고    scopus 로고
    • A direct role for sterol regulatory element binding protein in activation of 3-hydroxy-3-methylglutaryl coenzyme A reductase gene
    • Vallet SM, Sanchez HB, Rosenfeld JM, Osborne TF. A direct role for sterol regulatory element binding protein in activation of 3-hydroxy-3-methylglutaryl coenzyme A reductase gene. J Biol Chem 271:12247-12253, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 12247-12253
    • Vallet, S.M.1    Sanchez, H.B.2    Rosenfeld, J.M.3    Osborne, T.F.4
  • 87
    • 0000248311 scopus 로고
    • Studies on the biosynthesis of cholesterol: The origin of prenoic acids from allyl pyrophosphates in liver enzyme systems
    • Christophe J, Popjak G. Studies on the biosynthesis of cholesterol: The origin of prenoic acids from allyl pyrophosphates in liver enzyme systems. J Lipid Res 2:244-257, 1961.
    • (1961) J Lipid Res , vol.2 , pp. 244-257
    • Christophe, J.1    Popjak, G.2
  • 88
    • 0028035383 scopus 로고
    • Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes
    • Bansal VS, Vaidya S. Characterization of two distinct allyl pyrophosphatase activities from rat liver microsomes. Arch Biochem Biophys 315:393-399, 1994.
    • (1994) Arch Biochem Biophys , vol.315 , pp. 393-399
    • Bansal, V.S.1    Vaidya, S.2
  • 89
    • 0031584090 scopus 로고    scopus 로고
    • Metabolism of farnesol: Phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions
    • Westfall D, Aboushadi N, Shackelford JE, Krisans SK. Metabolism of farnesol: Phosphorylation of farnesol by rat liver microsomal and peroxisomal fractions. Biochem Biophys Res Commun 230:562-568, 1997.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 562-568
    • Westfall, D.1    Aboushadi, N.2    Shackelford, J.E.3    Krisans, S.K.4
  • 91
    • 0031017097 scopus 로고    scopus 로고
    • Regulation of gene expression by nuclear hormone receptors
    • Meier CA. Regulation of gene expression by nuclear hormone receptors. J Recept Signal Transduct Res 17:319-335, 1997.
    • (1997) J Recept Signal Transduct Res , vol.17 , pp. 319-335
    • Meier, C.A.1
  • 94
    • 0023874006 scopus 로고
    • Isopentenoid synthesis in isolated embryonic Drosophila cells. II. Farnesol catabolism and ω-oxidation
    • Gonzalez-Pacanowska D, Arison B, Havel CM, Watson JA. Isopentenoid synthesis in isolated embryonic Drosophila cells. II. Farnesol catabolism and ω-oxidation. J Biol Chem 263:1301-1306, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 1301-1306
    • Gonzalez-Pacanowska, D.1    Arison, B.2    Havel, C.M.3    Watson, J.A.4
  • 95
    • 0023851527 scopus 로고
    • Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases
    • Julia P, Pares X, Jornvall H. Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases. Eur J Biochem 172:73-83, 1988.
    • (1988) Eur J Biochem , vol.172 , pp. 73-83
    • Julia, P.1    Pares, X.2    Jornvall, H.3
  • 96
    • 0025974055 scopus 로고
    • Human liver alcohol dehydrogenases catalyze the oxidation of the intermediary alcohols of the shunt pathway of mevalonate metabolism
    • Keung WM. Human liver alcohol dehydrogenases catalyze the oxidation of the intermediary alcohols of the shunt pathway of mevalonate metabolism. Biochem Biophys Res Commun 174:701-707, 1991.
    • (1991) Biochem Biophys Res Commun , vol.174 , pp. 701-707
    • Keung, W.M.1
  • 97
    • 0023618296 scopus 로고
    • Developmental changes in aldehyde dehydrogenases from mouse tissues
    • Rout UK, Elkington JSH, Holmes RS. Developmental changes in aldehyde dehydrogenases from mouse tissues. Mech Ageing Dev 40:103-113, 1987.
    • (1987) Mech Ageing Dev , vol.40 , pp. 103-113
    • Rout, U.K.1    Elkington, J.S.H.2    Holmes, R.S.3
  • 98
    • 0023786009 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl CoA reductase mRNA contents in human hepatoma cell line HepG2 by distinct classes of mevalonate-derived metabolites
    • Cohen LH, Griffioen M. Regulation of 3-hydroxy-3-methylglutaryl CoA reductase mRNA contents in human hepatoma cell line HepG2 by distinct classes of mevalonate-derived metabolites. Biochem J 255:61-67, 1988.
    • (1988) Biochem J , vol.255 , pp. 61-67
    • Cohen, L.H.1    Griffioen, M.2
  • 99
    • 0030598885 scopus 로고    scopus 로고
    • A signaling pathway to translational control
    • Brown EJ, Schreiber SL. A signaling pathway to translational control. Cell 86:517-520, 1996.
    • (1996) Cell , vol.86 , pp. 517-520
    • Brown, E.J.1    Schreiber, S.L.2
  • 100
    • 0030272660 scopus 로고    scopus 로고
    • Mechanisms of translational control in early development
    • Seydoux G. Mechanisms of translational control in early development. Curr Opin Genet Dev 6:555-561, 1996.
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 555-561
    • Seydoux, G.1
  • 101
    • 0028826152 scopus 로고
    • Mevalonate regulates polysome distribution and blocks translation-dependent suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase mRNA: Relationship to translational control
    • Peffley DM, Gayen AK. Mevalonate regulates polysome distribution and blocks translation-dependent suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase mRNA: Relationship to translational control. Somat Cell Mol Genet 21:198-204, 1995.
    • (1995) Somat Cell Mol Genet , vol.21 , pp. 198-204
    • Peffley, D.M.1    Gayen, A.K.2
  • 102
    • 0028223422 scopus 로고
    • Mevalonate-mediated suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase function in α-toxin perforated cells
    • Giron MD, Havel CM, Watson JA. Mevalonate-mediated suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase function in α-toxin perforated cells. Proc Natl Acad Sci USA 91:6398-6402, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6398-6402
    • Giron, M.D.1    Havel, C.M.2    Watson, J.A.3
  • 103
    • 33749767457 scopus 로고    scopus 로고
    • Translational efficiency of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase is regulated by 5′ untranslated (UTR) mRNA secondary structure
    • Fritz TN, Buechler RD, Peffley DM. Translational efficiency of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase is regulated by 5′ untranslated (UTR) mRNA secondary structure. Circulation 98:379A, 1998.
    • (1998) Circulation , vol.98
    • Fritz, T.N.1    Buechler, R.D.2    Peffley, D.M.3
  • 104
    • 0028987202 scopus 로고
    • 3′-Untranslated sequences mediate post-transcriptional regulation of 3-hydroxy-3-methylglutaryl-CoA reductase mRNA by 25-hydroxycholesterol
    • Choi JW, Peffley DM. 3′-Untranslated sequences mediate post-transcriptional regulation of 3-hydroxy-3-methylglutaryl-CoA reductase mRNA by 25-hydroxycholesterol. Biochem J 307:233-238, 1995.
    • (1995) Biochem J , vol.307 , pp. 233-238
    • Choi, J.W.1    Peffley, D.M.2
  • 105
    • 0343665273 scopus 로고
    • The biochemical approach to the cancer problem
    • Potter VR. The biochemical approach to the cancer problem. Fed Proc 17:691-697, 1958.
    • (1958) Fed Proc , vol.17 , pp. 691-697
    • Potter, V.R.1
  • 106
    • 0000611328 scopus 로고
    • Deletion of the cholesterol-negative feedback system in liver tumors
    • Siperstein MD, Fagan VM. Deletion of the cholesterol-negative feedback system in liver tumors. Cancer Res 24:1108-1115, 1964.
    • (1964) Cancer Res , vol.24 , pp. 1108-1115
    • Siperstein, M.D.1    Fagan, V.M.2
  • 108
    • 0019200281 scopus 로고
    • Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in Morris hepatoma 7800 after intravenous injection of mevalonic acid
    • George R, Goldfarb S. Inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in Morris hepatoma 7800 after intravenous injection of mevalonic acid. Cancer Res 40:4717-4721, 1980.
    • (1980) Cancer Res , vol.40 , pp. 4717-4721
    • George, R.1    Goldfarb, S.2
  • 109
    • 0020318487 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat liver and Morris hepatomas 5123C, 9618A, and 5123tc
    • Gregg RG, Sabine JR, Wilce PA. Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat liver and Morris hepatomas 5123C, 9618A, and 5123tc. Biochem J 204:457-462, 1982.
    • (1982) Biochem J , vol.204 , pp. 457-462
    • Gregg, R.G.1    Sabine, J.R.2    Wilce, P.A.3
  • 110
    • 0021361016 scopus 로고
    • Divergence in cholesterol biosynthetic rates and 3-hydroxy-3-methylglutaryl-CoA reductase activity as a consequence of granulocyte versus monocyte-macrophage differentiation in HL-60 cells
    • Yachnin S, Toub DB, Mannickarottu V. Divergence in cholesterol biosynthetic rates and 3-hydroxy-3-methylglutaryl-CoA reductase activity as a consequence of granulocyte versus monocyte-macrophage differentiation in HL-60 cells. Proc Natl Acad Sci USA 81:894-897, 1984.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 894-897
    • Yachnin, S.1    Toub, D.B.2    Mannickarottu, V.3
  • 111
    • 0022227022 scopus 로고
    • True uncoupling between cholesterol synthesis and 3-hydroxy-3-methylglutaryl coenzyme A reductase in an early stage of liver generation
    • Bruscalalupi G, Leoni S, Mangiantini MT, Minieri M, Spagnuolo S, Trentlanc A. True uncoupling between cholesterol synthesis and 3-hydroxy-3-methylglutaryl coenzyme A reductase in an early stage of liver generation. Cell Mol Biol 31:365-368, 1985.
    • (1985) Cell Mol Biol , vol.31 , pp. 365-368
    • Bruscalalupi, G.1    Leoni, S.2    Mangiantini, M.T.3    Minieri, M.4    Spagnuolo, S.5    Trentlanc, A.6
  • 112
    • 0023261745 scopus 로고
    • Expression of the 3-hydroxy-3-methylglutaryl coenzyme A-reductase and LDI-receptor genes in human embryonic tumors and in normal fetal tissues
    • Engstrom W, Schofield PN. Expression of the 3-hydroxy-3-methylglutaryl coenzyme A-reductase and LDI-receptor genes in human embryonic tumors and in normal fetal tissues. Anticancer Res 7:337-342, 1987.
    • (1987) Anticancer Res , vol.7 , pp. 337-342
    • Engstrom, W.1    Schofield, P.N.2
  • 114
    • 0024548859 scopus 로고
    • A discoordinant increase in the cellular amount of 3-hydroxy-3-methylglutaryl-CoA reductase results in the loss of rate-limiting control over cholesterogenesis in a tumor cell-free system
    • Azrolan NI, Coleman PS. A discoordinant increase in the cellular amount of 3-hydroxy-3-methylglutaryl-CoA reductase results in the loss of rate-limiting control over cholesterogenesis in a tumor cell-free system. Biochem J 258:421-425, 1989.
    • (1989) Biochem J , vol.258 , pp. 421-425
    • Azrolan, N.I.1    Coleman, P.S.2
  • 115
    • 0027451612 scopus 로고
    • Importance of mevalonate-derived products in the control of HMG-CoA reductase activity and growth of human lung adenocarcinoma cell line A549
    • Bennis F, Favre G, Le Gaillard F, Soula G. Importance of mevalonate-derived products in the control of HMG-CoA reductase activity and growth of human lung adenocarcinoma cell line A549. Int J Cancer 55:640-645, 1993.
    • (1993) Int J Cancer , vol.55 , pp. 640-645
    • Bennis, F.1    Favre, G.2    Le Gaillard, F.3    Soula, G.4
  • 116
    • 0026589729 scopus 로고
    • Hypomethylation of β-hydroxy-β-methylglutaryl coenzyme A reductase gene and its expression during hepatocarcinogenesis in the rat
    • Coni P, Pang J, Pichiri-Coni G, Hsu S, Rao PM, Rakalakshmi S, Sarma DSR. Hypomethylation of β-hydroxy-β-methylglutaryl coenzyme A reductase gene and its expression during hepatocarcinogenesis in the rat. Carcinogenesis 13:497-499, 1992.
    • (1992) Carcinogenesis , vol.13 , pp. 497-499
    • Coni, P.1    Pang, J.2    Pichiri-Coni, G.3    Hsu, S.4    Rao, P.M.5    Rakalakshmi, S.6    Sarma, D.S.R.7
  • 117
    • 0027934698 scopus 로고
    • Similar patterns of hypomethylation in the β-hydroxy-β-methylglutaryl coenzyme. A reductase gene in hepatic nodules induced by different carcinogens
    • Rossiello MR, Rao P, Rajalakshmi S, Sarma DAR. Similar patterns of hypomethylation in the β-hydroxy-β-methylglutaryl coenzyme. A reductase gene in hepatic nodules induced by different carcinogens. Mol Carcinog 10:237-245, 1994.
    • (1994) Mol Carcinog , vol.10 , pp. 237-245
    • Rossiello, M.R.1    Rao, P.2    Rajalakshmi, S.3    Sarma, D.A.R.4
  • 118
    • 0031040015 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl-CoA reductase gene of Gibberella fujikuroi: Isolation and characterization
    • Woitek S, Unkles SE, Kinghorn JR, Tudzynski B. 3-Hydroxy-3-methylglutaryl-CoA reductase gene of Gibberella fujikuroi: Isolation and characterization. Curr Genet 31:38-47, 1997.
    • (1997) Curr Genet , vol.31 , pp. 38-47
    • Woitek, S.1    Unkles, S.E.2    Kinghorn, J.R.3    Tudzynski, B.4
  • 119
    • 0028213166 scopus 로고
    • Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast
    • Hampton RY, Rine J. Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast. J Cell Biol 125:299-312, 1994.
    • (1994) J Cell Biol , vol.125 , pp. 299-312
    • Hampton, R.Y.1    Rine, J.2
  • 120
    • 0030660267 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Hampton RY, Bhakta H. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc Natl Acad Sci USA 94:12944-12948, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12944-12948
    • Hampton, R.Y.1    Bhakta, H.2
  • 121
    • 0029165402 scopus 로고
    • Degradation of HMG-CoA reductase-induced membranes in the fission yeast, Schizosaccharomyces pombe
    • Lum PY, Wright R. Degradation of HMG-CoA reductase-induced membranes in the fission yeast, Schizosaccharomyces pombe. J Cell Biol 131:81-94, 1995.
    • (1995) J Cell Biol , vol.131 , pp. 81-94
    • Lum, P.Y.1    Wright, R.2
  • 122
    • 0029839311 scopus 로고    scopus 로고
    • Molecular, functional, and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe
    • Lum PY, Edwards S, Wright R. Molecular, functional, and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe. Yeast 12:1107-1124, 1996.
    • (1996) Yeast , vol.12 , pp. 1107-1124
    • Lum, P.Y.1    Edwards, S.2    Wright, R.3
  • 123
    • 0028336801 scopus 로고
    • Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cervisiae
    • Dimster-Denk D, Thorsness MK, Rine J. Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in Saccharomyces cervisiae. Mol Biol Cell 5:655-665, 1994.
    • (1994) Mol Biol Cell , vol.5 , pp. 655-665
    • Dimster-Denk, D.1    Thorsness, M.K.2    Rine, J.3
  • 124
    • 0028864187 scopus 로고
    • Identification of the sequences in HMG-CoA reductase required for karmellae assembly
    • Parrish ML, Sengstag C, Rine JD, Wright RL. Identification of the sequences in HMG-CoA reductase required for karmellae assembly. Mol Biol Cell 6:1535-1547, 1995.
    • (1995) Mol Biol Cell , vol.6 , pp. 1535-1547
    • Parrish, M.L.1    Sengstag, C.2    Rine, J.D.3    Wright, R.L.4
  • 125
    • 0029926584 scopus 로고    scopus 로고
    • Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations
    • Koning AJ, Roberts CJ, Wright RL. Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations. Mol Biol Cell 7:769-789, 1996.
    • (1996) Mol Biol Cell , vol.7 , pp. 769-789
    • Koning, A.J.1    Roberts, C.J.2    Wright, R.L.3
  • 126
    • 0029865434 scopus 로고    scopus 로고
    • The mevalonate pathway in parasitic protozoa and helminths
    • Coppens I, Courtoy PJ. The mevalonate pathway in parasitic protozoa and helminths. Exp Parasitol 82:76-85, 1996.
    • (1996) Exp Parasitol , vol.82 , pp. 76-85
    • Coppens, I.1    Courtoy, P.J.2
  • 127
    • 0024853856 scopus 로고
    • Molecular cloning and sequence analysis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase from the human parasite Schistoma mansoni
    • Rajkovic A, Simonsen JN, Davis RE, Rottman FM. Molecular cloning and sequence analysis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase from the human parasite Schistoma mansoni. Proc Natl Acad Sci USA 86:8217-8221, 1989.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 8217-8221
    • Rajkovic, A.1    Simonsen, J.N.2    Davis, R.E.3    Rottman, F.M.4
  • 128
    • 0024374074 scopus 로고
    • Physiological role of HMG-CoA reductase in regulating egg production by Schistoma mansoni
    • Regulatory Integrative Comp Physiol 26
    • Vandewaa EA, Mills G, Chen GZ, Foster LA, Bennett JL. Physiological role of HMG-CoA reductase in regulating egg production by Schistoma mansoni. Am J Physiol 257 (Regulatory Integrative Comp Physiol 26):R618-R625, 1989.
    • (1989) Am J Physiol , vol.257
    • Vandewaa, E.A.1    Mills, G.2    Chen, G.Z.3    Foster, L.A.4    Bennett, J.L.5
  • 129
    • 0030239949 scopus 로고    scopus 로고
    • Coordinated expression and activity of 3-hydroxy-3-methylglutaryl coenzyme A synthase and reductase in the fat body of Blattella germanica (L.) during vitellogenesis
    • Casals N, Buesa C, Piulachs MD, Cabano J, Marrero PF, Belles X, Hegardt FG. Coordinated expression and activity of 3-hydroxy-3-methylglutaryl coenzyme A synthase and reductase in the fat body of Blattella germanica (L.) during vitellogenesis. Insect Biochem Mol Biol 26:837-843, 1996.
    • (1996) Insect Biochem Mol Biol , vol.26 , pp. 837-843
    • Casals, N.1    Buesa, C.2    Piulachs, M.D.3    Cabano, J.4    Marrero, P.F.5    Belles, X.6    Hegardt, F.G.7
  • 130
    • 0024039673 scopus 로고
    • Developmental and metabolic regulation of the Drosophila melannogaster 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Gertler FB, Chiu CY, Richter ML, Chin DJ. Developmental and metabolic regulation of the Drosophila melannogaster 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mol Cell Biol 8:2713-2721, 1988.
    • (1988) Mol Cell Biol , vol.8 , pp. 2713-2721
    • Gertler, F.B.1    Chiu, C.Y.2    Richter, M.L.3    Chin, D.J.4
  • 131
    • 0021052720 scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A reductase (EC 1.1.1.34): A transmembrane glycoprotein of the endoplasmic reticulum with N-linked "high-mannose" oligosaccharides
    • Liscum L, Cummings RD, Anderson RGW, Demartino GN, Goldstein JL, Brown MS. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase (EC 1.1.1.34): A transmembrane glycoprotein of the endoplasmic reticulum with N-linked "high-mannose" oligosaccharides. Proc Natl Acad Sci USA 80:7165-7169, 1983.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 7165-7169
    • Liscum, L.1    Cummings, R.D.2    Anderson, R.G.W.3    Demartino, G.N.4    Goldstein, J.L.5    Brown, M.S.6
  • 133
    • 0020044788 scopus 로고
    • 3-Hydroxy-3-methylglutaryl coenzyme A reductase (EC 1.1.1.34) from rat intestine: Subcellular localization and in vitro regulation
    • Field FJ, Erickson SK, Shrewsbury MA, Cooper AD. 3-Hydroxy-3-methylglutaryl coenzyme A reductase (EC 1.1.1.34) from rat intestine: Subcellular localization and in vitro regulation. J Lipid Res 23:105-113, 1982.
    • (1982) J Lipid Res , vol.23 , pp. 105-113
    • Field, F.J.1    Erickson, S.K.2    Shrewsbury, M.A.3    Cooper, A.D.4
  • 134
    • 0021204120 scopus 로고
    • Evidence for post-translational incorporation of a product of mevalonic acid into Swiss 3T3 cell proteins
    • Schmidt RA, Schneider CJ, Glomset JA. Evidence for post-translational incorporation of a product of mevalonic acid into Swiss 3T3 cell proteins. J Biol Chem 259:10175-10180, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 10175-10180
    • Schmidt, R.A.1    Schneider, C.J.2    Glomset, J.A.3
  • 135
    • 0023917971 scopus 로고
    • Evidence for the modification of lamin B by a product of mevalonic acid
    • Wolda SL, Glomset JA. Evidence for the modification of lamin B by a product of mevalonic acid. J Biol Chem 263:5997-6000, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 5997-6000
    • Wolda, S.L.1    Glomset, J.A.2
  • 136
    • 0024094640 scopus 로고
    • Incorporation of a product of mevalonic acid metabolism into proteins of Chinese ovary cell nuclei
    • Beck LA, Hosick TJ, Sinensky M. Incorporation of a product of mevalonic acid metabolism into proteins of Chinese ovary cell nuclei. J Cell Biol 107:1307-1316, 1988.
    • (1988) J Cell Biol , vol.107 , pp. 1307-1316
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 138
    • 0024406286 scopus 로고
    • All ras proteins are isoprenylated but only some are palmitoylated
    • Hancock JF, Magee AI, Childs JE, Marshall CJ. All ras proteins are isoprenylated but only some are palmitoylated. Cell 577:1167-1177, 1989.
    • (1989) Cell , vol.577 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 139
    • 0024316475 scopus 로고
    • Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans
    • Shafer WR, Kim R, Sterne R, Thorner J, Kim SH, Rine J. Genetic and pharmacological suppression of oncogenic mutations in ras genes of yeast and humans. Science 245:379-385, 1989.
    • (1989) Science , vol.245 , pp. 379-385
    • Shafer, W.R.1    Kim, R.2    Sterne, R.3    Thorner, J.4    Kim, S.H.5    Rine, J.6
  • 141
    • 0024446855 scopus 로고
    • Characterization of isoprenoid involved in the post-translational modification of mammalian cell proteins
    • Maltese WA, Erdman RA. Characterization of isoprenoid involved in the post-translational modification of mammalian cell proteins. J Biol Chem 264:18168-18172, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 18168-18172
    • Maltese, W.A.1    Erdman, R.A.2
  • 142
    • 0025649688 scopus 로고
    • Post-translational modification of proteins by isoprenoids in mammalian cells
    • Maltese WA. Post-translational modification of proteins by isoprenoids in mammalian cells. FASEB J 4:3319-3328, 1990.
    • (1990) FASEB J , vol.4 , pp. 3319-3328
    • Maltese, W.A.1
  • 143
    • 0026436279 scopus 로고
    • The prenylation of proteins
    • Sinensky M, Lutz RJ. The prenylation of proteins. Bioessays 14:25-31, 1992.
    • (1992) Bioessays , vol.14 , pp. 25-31
    • Sinensky, M.1    Lutz, R.J.2
  • 144
    • 0027284950 scopus 로고
    • Protein prenylation: A mediator of protein-protein interactions
    • Marshall CJ. Protein prenylation: A mediator of protein-protein interactions. Science 259:1865-1866, 1993.
    • (1993) Science , vol.259 , pp. 1865-1866
    • Marshall, C.J.1
  • 145
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang FL, Casey PJ. Protein prenylation: Molecular mechanisms and functional consequences. Annu Rev Biochem 65:241-269, 1996.
    • (1996) Annu Rev Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 146
    • 0030992130 scopus 로고    scopus 로고
    • Protein prenylation, et cetera: Signal transduction in two dimensions
    • Gelb MH. Protein prenylation, et cetera: Signal transduction in two dimensions. Science 275:1750-1751, 1997.
    • (1997) Science , vol.275 , pp. 1750-1751
    • Gelb, M.H.1
  • 147
    • 0028587430 scopus 로고
    • Weaving a pattern from disparate threads: Lamin function in nuclear assembly and DNA replication
    • Hutchinson CJ, Bridger JM, Cox CS, Kill IR. Weaving a pattern from disparate threads: Lamin function in nuclear assembly and DNA replication. J Cell Sci 107:3259-3269, 1994.
    • (1994) J Cell Sci , vol.107 , pp. 3259-3269
    • Hutchinson, C.J.1    Bridger, J.M.2    Cox, C.S.3    Kill, I.R.4
  • 148
    • 0028274845 scopus 로고
    • The role of isoprenylation in membrane attachment of nuclear lamins: A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties
    • Hennekes H, Nigg EA. The role of isoprenylation in membrane attachment of nuclear lamins: A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J Cell Sci 107:1019-1029, 1994.
    • (1994) J Cell Sci , vol.107 , pp. 1019-1029
    • Hennekes, H.1    Nigg, E.A.2
  • 149
    • 0029198668 scopus 로고
    • The dynamic properties and possible functions of nuclear lamins
    • Moir RD, Spann TP, Goldman RD. The dynamic properties and possible functions of nuclear lamins. Int Rev Cytol 162:141-182, 1995.
    • (1995) Int Rev Cytol , vol.162 , pp. 141-182
    • Moir, R.D.1    Spann, T.P.2    Goldman, R.D.3
  • 151
    • 0030962347 scopus 로고    scopus 로고
    • The potential of farnesyltransferase inhibitors as cancer chemotherapeutics
    • Gibbs JB, Oliff A. The potential of farnesyltransferase inhibitors as cancer chemotherapeutics. Annu Rev Pharmacol Toxicol 37:143-166, 1997.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 143-166
    • Gibbs, J.B.1    Oliff, A.2
  • 153
    • 0031849288 scopus 로고    scopus 로고
    • Pre-clinical development of farnesyltransferase inhibitors
    • Lobell RB, Kohl NE. Pre-clinical development of farnesyltransferase inhibitors. Cancer Metastasis Rev 17:203-210, 1998.
    • (1998) Cancer Metastasis Rev , vol.17 , pp. 203-210
    • Lobell, R.B.1    Kohl, N.E.2
  • 154
    • 0025952954 scopus 로고
    • Selective inhibition of isoprenylation of 21-26-kDa proteins by the anticarcinogen d-limonene and its metabolites
    • Crowell PL, Chang RR, Ren Z, Elson CE, Gould MN. Selective inhibition of isoprenylation of 21-26-kDa proteins by the anticarcinogen d-limonene and its metabolites. J Biol Chem 266:17679-17685, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 17679-17685
    • Crowell, P.L.1    Chang, R.R.2    Ren, Z.3    Elson, C.E.4    Gould, M.N.5
  • 155
    • 0026497014 scopus 로고
    • Identification of circulating metabolites of the antitumor agent d-limonene capable of inhibiting protein isoprenylation and cell growth
    • Crowell PL, Lin S, Vedejs E, Gould MN. Identification of circulating metabolites of the antitumor agent d-limonene capable of inhibiting protein isoprenylation and cell growth. Cancer Chemother Pharmacol 31:205-212, 1992.
    • (1992) Cancer Chemother Pharmacol , vol.31 , pp. 205-212
    • Crowell, P.L.1    Lin, S.2    Vedejs, E.3    Gould, M.N.4
  • 156
    • 0028343655 scopus 로고
    • Structure-activity relationships among monoterpene inhibitors of protein isoprenylation and cell proliferation
    • Crowell PL, Ren Z, Lin S, Vedejs E, Gould MN. Structure-activity relationships among monoterpene inhibitors of protein isoprenylation and cell proliferation. Biochem Pharmacol 47:1405-1415, 1994.
    • (1994) Biochem Pharmacol , vol.47 , pp. 1405-1415
    • Crowell, P.L.1    Ren, Z.2    Lin, S.3    Vedejs, E.4    Gould, M.N.5
  • 158
    • 0030757145 scopus 로고    scopus 로고
    • Inhibition of type I and type II geranylgeranyl-protein transferases by the monoterpene perillyl alcohol in NIH3T3 cells
    • Ren Z, Elson CE, Gould MN. Inhibition of type I and type II geranylgeranyl-protein transferases by the monoterpene perillyl alcohol in NIH3T3 cells. Biochem Pharmacol 54:113-120, 1997.
    • (1997) Biochem Pharmacol , vol.54 , pp. 113-120
    • Ren, Z.1    Elson, C.E.2    Gould, M.N.3
  • 159
    • 0029814832 scopus 로고    scopus 로고
    • Monoterpenes as regulators of malignant cell proliferation
    • American Institute for Cancer Research, Eds. New York: Plenum Press
    • Hohl RJ. Monoterpenes as regulators of malignant cell proliferation. In: American Institute for Cancer Research, Eds. Dietary Phytochemicals in Cancer Prevention and Treatment. New York: Plenum Press, pp 137-146, 1996.
    • (1996) Dietary Phytochemicals in Cancer Prevention and Treatment , pp. 137-146
    • Hohl, R.J.1
  • 160
    • 33749812853 scopus 로고    scopus 로고
    • National Cancer Institute (NCI). Cancer Trials [On-line]. Available: http://cancertrials.nci.nih.gov, 1999.
    • (1999) Cancer Trials
  • 161
    • 0001921354 scopus 로고    scopus 로고
    • Oral limonene: Combined prenylation inhibitor therapy of cancer
    • Nagourney RA. Oral limonene: Combined prenylation inhibitor therapy of cancer. J Med Foods 1:83-88, 1998.
    • (1998) J Med Foods , vol.1 , pp. 83-88
    • Nagourney, R.A.1
  • 162
    • 0017894322 scopus 로고
    • Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts incubated with compactin (ML-236B), a competitive inhibitor of the reductase
    • Brown MS, Faust JR, Goldstein JL, Kaneko I, Endo A. Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts incubated with compactin (ML-236B), a competitive inhibitor of the reductase. J Biol Chem 253:1121-1128, 1978.
    • (1978) J Biol Chem , vol.253 , pp. 1121-1128
    • Brown, M.S.1    Faust, J.R.2    Goldstein, J.L.3    Kaneko, I.4    Endo, A.5
  • 163
    • 0021799463 scopus 로고
    • Defective macromolecule biosynthesis and cell cycle progression in a mammalian cell starved for mevalonate
    • Sinenski M, Logel J. Defective macromolecule biosynthesis and cell cycle progression in a mammalian cell starved for mevalonate. Proc Natl Acad Sci USA 82:3257-3261, 1985.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 3257-3261
    • Sinenski, M.1    Logel, J.2
  • 164
    • 0023275949 scopus 로고
    • Cell cycle-specific requirement for mevalonate but not for cholesterol, for DNA synthesis in glial primary cultures
    • Langan TJ, Volpe JJ. Cell cycle-specific requirement for mevalonate but not for cholesterol, for DNA synthesis in glial primary cultures. J Neurochem 49:513-521, 1987.
    • (1987) J Neurochem , vol.49 , pp. 513-521
    • Langan, T.J.1    Volpe, J.J.2
  • 165
    • 0023749122 scopus 로고
    • Requirement for mevalonate in cycling cells: Quantitative and temporal aspects
    • Doyle JW, Kandutsche AA. Requirement for mevalonate in cycling cells: Quantitative and temporal aspects. J Cell Physiol 137:133-140, 1988.
    • (1988) J Cell Physiol , vol.137 , pp. 133-140
    • Doyle, J.W.1    Kandutsche, A.A.2
  • 167
    • 0023604660 scopus 로고
    • Isoprenylated proteins in cultured cells: Subcellular distribution and changes related to altered morphology and growth arrest induced by mevalonate deprivation
    • Maltese WA, Sheridan KM. Isoprenylated proteins in cultured cells: Subcellular distribution and changes related to altered morphology and growth arrest induced by mevalonate deprivation. J Cell Physiol 133:471-481, 1987.
    • (1987) J Cell Physiol , vol.133 , pp. 471-481
    • Maltese, W.A.1    Sheridan, K.M.2
  • 168
    • 0024328138 scopus 로고
    • Sterol-independent regulation of 3-hydroxy-3-methylglutaryl-CoA reductase by mevalonate in Chinese hamster ovary cells
    • Panini SR, Schnitzer-Polokoff R, Spencer TA, Sinenski M. Sterol-independent regulation of 3-hydroxy-3-methylglutaryl-CoA reductase by mevalonate in Chinese hamster ovary cells. J Biol Chem 264:11044-11052, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 11044-11052
    • Panini, S.R.1    Schnitzer-Polokoff, R.2    Spencer, T.A.3    Sinenski, M.4
  • 169
    • 0027153578 scopus 로고
    • Lovastatin 5-year safety and efficacy study. Lovastatin Study Groups I through IV
    • Anonymous. Lovastatin 5-year safety and efficacy study. Lovastatin Study Groups I through IV. Arch Intern Med 153:1079-1087, 1993.
    • (1993) Arch Intern Med , vol.153 , pp. 1079-1087
  • 172
    • 0030027536 scopus 로고    scopus 로고
    • Lipid metabolism as a target for brain cancer therapy: Synergistic activity of lovastatin and sodium phenylacetate against human glioma cells
    • Prasanna P, Thibault A, Liu L, Samid D. Lipid metabolism as a target for brain cancer therapy: Synergistic activity of lovastatin and sodium phenylacetate against human glioma cells. J Neurochem 66:710-716, 1996.
    • (1996) J Neurochem , vol.66 , pp. 710-716
    • Prasanna, P.1    Thibault, A.2    Liu, L.3    Samid, D.4
  • 174
    • 12944261766 scopus 로고    scopus 로고
    • A phase I study of the differentiating agent phenylbutyrate in patients with cancer
    • Thibault A, Figg WD, Samid D. A phase I study of the differentiating agent phenylbutyrate in patients with cancer. Proc Am Soc Clin Oncol 15:A1539, 1996.
    • (1996) Proc Am Soc Clin Oncol , vol.15
    • Thibault, A.1    Figg, W.D.2    Samid, D.3
  • 176
  • 177
    • 0030749232 scopus 로고    scopus 로고
    • Regulation of proliferation and ras localization in transformed cells by products of mevalonate metabolism
    • Cuthbert JA, Lipsky PE. Regulation of proliferation and ras localization in transformed cells by products of mevalonate metabolism. Cancer Res 57:3498-3505, 1997.
    • (1997) Cancer Res , vol.57 , pp. 3498-3505
    • Cuthbert, J.A.1    Lipsky, P.E.2
  • 179
    • 0029892886 scopus 로고    scopus 로고
    • Phenylacetate inhibits protein isoprenylation and growth of the androgen-independent LNCaP prostate cancer cells transfected with the T24 Ha-ras oncogene
    • Danesi R, Nardini D, Basolo F, Del Tacca M, Samid D, Myers CE. Phenylacetate inhibits protein isoprenylation and growth of the androgen-independent LNCaP prostate cancer cells transfected with the T24 Ha-ras oncogene. Mol Pharmacol 49:972-979, 1996.
    • (1996) Mol Pharmacol , vol.49 , pp. 972-979
    • Danesi, R.1    Nardini, D.2    Basolo, F.3    Del Tacca, M.4    Samid, D.5    Myers, C.E.6
  • 181
    • 0028314862 scopus 로고
    • Growth inhibition of rat liver epithelial tumor cells does not involve ras plasma membrane association
    • Ruch RJ, Sigler K. Growth inhibition of rat liver epithelial tumor cells does not involve ras plasma membrane association. Carcinogenesis 15:787-789, 1994.
    • (1994) Carcinogenesis , vol.15 , pp. 787-789
    • Ruch, R.J.1    Sigler, K.2
  • 182
    • 0030568077 scopus 로고    scopus 로고
    • Inhibition of lung tumor cell growth in vitro and mouse lung tumor formation by lovastatin
    • Hawk MA, Cesen KT, Siglin JC, Stoner GD, Ruch RJ. Inhibition of lung tumor cell growth in vitro and mouse lung tumor formation by lovastatin. Cancer Lett 109:217-222, 1996.
    • (1996) Cancer Lett , vol.109 , pp. 217-222
    • Hawk, M.A.1    Cesen, K.T.2    Siglin, J.C.3    Stoner, G.D.4    Ruch, R.J.5
  • 184
    • 13144260677 scopus 로고    scopus 로고
    • Lovastatin inhibits proliferation of pancreatic cancer cell lines with mutant as well as wild-type K-ras oncogene but with different effects on protein phosphorylation and induction of apoptosis
    • Muller C, Bockhorn AG, Klusmeier G, Kiehl M, Roeder C, Kalthoff H, Koch OM. Lovastatin inhibits proliferation of pancreatic cancer cell lines with mutant as well as wild-type K-ras oncogene but with different effects on protein phosphorylation and induction of apoptosis. Int J Oncol 12:717-723, 1998.
    • (1998) Int J Oncol , vol.12 , pp. 717-723
    • Muller, C.1    Bockhorn, A.G.2    Klusmeier, G.3    Kiehl, M.4    Roeder, C.5    Kalthoff, H.6    Koch, O.M.7
  • 186
    • 0030808048 scopus 로고    scopus 로고
    • Mevalonate-regulated mechanisms in cell growth control: Role of dolichyl phosphate in expression of the insulin-like growth factor-1 receptor (IGF-1R) in comparison to ras prenylation and expression of c-myc
    • Drieu A, Wang M, Hjertman M, Malec M, Biegen H, Wejde J, Carlberg M, Larsson O. Mevalonate-regulated mechanisms in cell growth control: Role of dolichyl phosphate in expression of the insulin-like growth factor-1 receptor (IGF-1R) in comparison to ras prenylation and expression of c-myc. Glycobiology 7:625-633, 1997.
    • (1997) Glycobiology , vol.7 , pp. 625-633
    • Drieu, A.1    Wang, M.2    Hjertman, M.3    Malec, M.4    Biegen, H.5    Wejde, J.6    Carlberg, M.7    Larsson, O.8
  • 187
    • 0028307941 scopus 로고
    • Inhibition of isoprenoid biosynthesis induces apoptosis in human promyelocytic HL-60 cells
    • Perez-Sala D, Mollinedo F. Inhibition of isoprenoid biosynthesis induces apoptosis in human promyelocytic HL-60 cells. Biochem Biophys Res Commun 199:1209-1215, 1994.
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 1209-1215
    • Perez-Sala, D.1    Mollinedo, F.2
  • 192
    • 0029054750 scopus 로고
    • Drug-induced apoptosis is not necessarily dependent on macromolecular synthesis or proliferation in the p53-negative human prostate cancer cell line PC-3
    • Borner MM, Myers CE, Sartor O, Sei Y, Toko T, Trepel JB, Schneider E. Drug-induced apoptosis is not necessarily dependent on macromolecular synthesis or proliferation in the p53-negative human prostate cancer cell line PC-3. Cancer Res 55:2122-2128, 1995.
    • (1995) Cancer Res , vol.55 , pp. 2122-2128
    • Borner, M.M.1    Myers, C.E.2    Sartor, O.3    Sei, Y.4    Toko, T.5    Trepel, J.B.6    Schneider, E.7
  • 194
    • 0032562711 scopus 로고    scopus 로고
    • Inhibition of the 3-hydroxy-3-methylglutaryl-coenzyme A reductase pathway induces p53-independent transcriptional regulation of p21 (WAF1/CIP1) in human prostate carcinoma cells
    • Lee SJ, Ha MJ, Lee J, Nguyen P, Choi YH, Pirnia F, Kang WK, Wang XF, Kim SJ, Trepel JB. Inhibition of the 3-hydroxy-3-methylglutaryl-coenzyme A reductase pathway induces p53-independent transcriptional regulation of p21 (WAF1/CIP1) in human prostate carcinoma cells. J Biol Chem 273:10618-10623, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 10618-10623
    • Lee, S.J.1    Ha, M.J.2    Lee, J.3    Nguyen, P.4    Choi, Y.H.5    Pirnia, F.6    Kang, W.K.7    Wang, X.F.8    Kim, S.J.9    Trepel, J.B.10
  • 195
    • 0025754857 scopus 로고
    • Nuclear lamin proteins: Domains required for nuclear targeting, assembly, and cell cycle-regulated dynamics
    • McKeon F. Nuclear lamin proteins: Domains required for nuclear targeting, assembly, and cell cycle-regulated dynamics. Curr Opin Cell Biol 3:82-86, 1991.
    • (1991) Curr Opin Cell Biol , vol.3 , pp. 82-86
    • McKeon, F.1
  • 196
    • 0026699171 scopus 로고
    • The type B receptor for tumor necrosis factor-a mediates DNA fragmentation in HL-60 and U937 cells and differentiation in HL-60 cells
    • Greenblatt MS, Elias L. The type B receptor for tumor necrosis factor-a mediates DNA fragmentation in HL-60 and U937 cells and differentiation in HL-60 cells. Blood 80:1339-1346, 1992.
    • (1992) Blood , vol.80 , pp. 1339-1346
    • Greenblatt, M.S.1    Elias, L.2
  • 197
    • 0028261732 scopus 로고
    • Flow cytometric detection of apoptosis: Comparison of the assays of in situ DNA degradation and chromatin changes
    • Hotz MA, Gong J, Traganos F, Darzynkiewicz Z. Flow cytometric detection of apoptosis: Comparison of the assays of in situ DNA degradation and chromatin changes. Cytometry 15:237-244, 1994.
    • (1994) Cytometry , vol.15 , pp. 237-244
    • Hotz, M.A.1    Gong, J.2    Traganos, F.3    Darzynkiewicz, Z.4
  • 198
    • 0028323164 scopus 로고
    • A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry
    • Gong J, Traganos F, Darzynkiewicz Z. A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry. Anal Biochem 218:314-319, 1994.
    • (1994) Anal Biochem , vol.218 , pp. 314-319
    • Gong, J.1    Traganos, F.2    Darzynkiewicz, Z.3
  • 199
    • 0028285272 scopus 로고
    • Nonsterol compounds that regulate cholesterogenesis: Analogues of farnesyl pyrophosphate reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels
    • Bradfute DL, Simoni RD. Nonsterol compounds that regulate cholesterogenesis: Analogues of farnesyl pyrophosphate reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels. J Biol Chem 269:6645-6650, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 6645-6650
    • Bradfute, D.L.1    Simoni, R.D.2
  • 201
    • 0028281429 scopus 로고
    • Inhibitors of cholesterol biosynthesis. 2. Hypocholesterolemic and antioxidant activities of benzopyran and tetrahydronaphthalene analogues of the tocotrienols
    • Pearce BC, Parker RA, Deason ME, Dischino DD, Gillespie E, Qureshi AA, Volk K, Wright JJ. Inhibitors of cholesterol biosynthesis. 2. Hypocholesterolemic and antioxidant activities of benzopyran and tetrahydronaphthalene analogues of the tocotrienols. J Med Chem 37:526-541, 1994.
    • (1994) J Med Chem , vol.37 , pp. 526-541
    • Pearce, B.C.1    Parker, R.A.2    Deason, M.E.3    Dischino, D.D.4    Gillespie, E.5    Qureshi, A.A.6    Volk, K.7    Wright, J.J.8
  • 204
    • 0031589211 scopus 로고    scopus 로고
    • Hypocholesterolemic effect of lycopene and β-carotene is related to suppression of cholesterol synthesis and augmentation of LDL receptor activity in macrophages
    • Fuhrman B, Elis A, Aviram M. Hypocholesterolemic effect of lycopene and β-carotene is related to suppression of cholesterol synthesis and augmentation of LDL receptor activity in macrophages. Biochem Biophys Res Commun 233:658-662, 1997.
    • (1997) Biochem Biophys Res Commun , vol.233 , pp. 658-662
    • Fuhrman, B.1    Elis, A.2    Aviram, M.3
  • 205
    • 0026742161 scopus 로고
    • Feedback-type inhibition of activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase by ubiquinone
    • Omkumar RV, Gaikwad AS, Ramasarma T. Feedback-type inhibition of activity of 3-hydroxy-3-methylglutaryl coenzyme A reductase by ubiquinone. Biochem Biophys Res Commun 184:1280-1287, 1982.
    • (1982) Biochem Biophys Res Commun , vol.184 , pp. 1280-1287
    • Omkumar, R.V.1    Gaikwad, A.S.2    Ramasarma, T.3
  • 206
    • 0030064856 scopus 로고    scopus 로고
    • Dietary α-tocopherol attenuates the impact of γ-tocotrienol on hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in chickens
    • Qureshi AA, Pearce BC, Nor RM, Gapor A, Peterson DM, Elson CE. Dietary α-tocopherol attenuates the impact of γ-tocotrienol on hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in chickens. J Nutr 126:389-394, 1996.
    • (1996) J Nutr , vol.126 , pp. 389-394
    • Qureshi, A.A.1    Pearce, B.C.2    Nor, R.M.3    Gapor, A.4    Peterson, D.M.5    Elson, C.E.6
  • 207
    • 0027439650 scopus 로고
    • Differences in the plasma transport and tissue concentrations of tocopherols and tocotrienols: Observations in humans and hamsters
    • Hayes KC, Pronczuk A, Liang JS. Differences in the plasma transport and tissue concentrations of tocopherols and tocotrienols: Observations in humans and hamsters. Proc Soc Exp Biol Med 202:353-359, 1993.
    • (1993) Proc Soc Exp Biol Med , vol.202 , pp. 353-359
    • Hayes, K.C.1    Pronczuk, A.2    Liang, J.S.3
  • 209
    • 0028934149 scopus 로고
    • Induction of geranylpyrophosphate pyrophosphatase activity by cholesterol-suppressive isoprenoids
    • Case GL, He L, Mo H, Elson CE. Induction of geranylpyrophosphate pyrophosphatase activity by cholesterol-suppressive isoprenoids. Lipids 30:357-359, 1995.
    • (1995) Lipids , vol.30 , pp. 357-359
    • Case, G.L.1    He, L.2    Mo, H.3    Elson, C.E.4
  • 210
    • 0007555171 scopus 로고    scopus 로고
    • Functional consequences of the modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity by isoprenoids
    • Peffley DM, Mo H, Gayen AK, Elson CE. Functional consequences of the modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity by isoprenoids. Proc Am Assoc Cancer Res 39:312A, 1998.
    • (1998) Proc Am Assoc Cancer Res , vol.39
    • Peffley, D.M.1    Mo, H.2    Gayen, A.K.3    Elson, C.E.4
  • 213
    • 0028861784 scopus 로고
    • Coupling the cholesterol- and tumor-suppressive actions of palm oil to the impact of its minor constituents on 3-hydroxy-3-methylglutaryl coenzyme A reductase activity
    • Elson CE, Qureshi AA. Coupling the cholesterol- and tumor-suppressive actions of palm oil to the impact of its minor constituents on 3-hydroxy-3-methylglutaryl coenzyme A reductase activity. Prostaglandins Leukot Essent Fatty Acids 52:205-208, 1995.
    • (1995) Prostaglandins Leukot Essent Fatty Acids , vol.52 , pp. 205-208
    • Elson, C.E.1    Qureshi, A.A.2
  • 214
    • 0026623497 scopus 로고
    • Increased expression of protein kinase Ca plays a key role retinoic acid-induced melanoma differentiation
    • Gruber JR, Ohno S, Niles RM. Increased expression of protein kinase Ca plays a key role retinoic acid-induced melanoma differentiation. J Biol Chem 267:13356-13360, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 13356-13360
    • Gruber, J.R.1    Ohno, S.2    Niles, R.M.3
  • 215
    • 0025035766 scopus 로고
    • Responses of a murine B16 melanoma to pharmacotherapy studied and compared with different assay systems
    • Kuwashima Y, Matsubara O, Kasuga T. Responses of a murine B16 melanoma to pharmacotherapy studied and compared with different assay systems. J Cancer Res Clin Oncol 116:173-178, 1990.
    • (1990) J Cancer Res Clin Oncol , vol.116 , pp. 173-178
    • Kuwashima, Y.1    Matsubara, O.2    Kasuga, T.3
  • 217
    • 0026247761 scopus 로고
    • Malignant melanoma: Relationship to parameters of differentiation
    • Tsukamoto K, Gersten DM, Law LW, Hearing VJ. Malignant melanoma: Relationship to parameters of differentiation. Melanoma Res 1:223-230, 1991.
    • (1991) Melanoma Res , vol.1 , pp. 223-230
    • Tsukamoto, K.1    Gersten, D.M.2    Law, L.W.3    Hearing, V.J.4
  • 218
  • 219
    • 0017704436 scopus 로고
    • Metastasis results from preexisting variant cells within a malignant tumor
    • Fidler IJ, Kripke ML. Metastasis results from preexisting variant cells within a malignant tumor. Science 197:893-895, 1977.
    • (1977) Science , vol.197 , pp. 893-895
    • Fidler, I.J.1    Kripke, M.L.2
  • 221
    • 0030897729 scopus 로고    scopus 로고
    • Inhibition of proliferation of estrogen receptor-negative MDA-MB-435 and -positive MCF-7 human breast cancer cells by palm oil tocotrienols and tamoxifen, alone and in combination
    • Guthric N, Gapor A, Chambers AF, Carroll KK. Inhibition of proliferation of estrogen receptor-negative MDA-MB-435 and -positive MCF-7 human breast cancer cells by palm oil tocotrienols and tamoxifen, alone and in combination. J Nutr 127:S544-S548, 1997.
    • (1997) J Nutr , vol.127
    • Guthric, N.1    Gapor, A.2    Chambers, A.F.3    Carroll, K.K.4
  • 223
    • 0000512125 scopus 로고
    • Potential anticarcinogenic natural products isolated from lemongrass oil and galanga root oil
    • Zheng G, Kenney PM, Lam LK. Potential anticarcinogenic natural products isolated from lemongrass oil and galanga root oil. J Agric Food Chem 41:153-156, 1983.
    • (1983) J Agric Food Chem , vol.41 , pp. 153-156
    • Zheng, G.1    Kenney, P.M.2    Lam, L.K.3
  • 225
    • 0026666172 scopus 로고
    • Anethofuran, carvone, and d-limonene: Potential cancer chemopreventive agents from dill weed oil and caraway oil
    • Zheng G, Kenney PM, Lam LK. Anethofuran, carvone, and d-limonene: Potential cancer chemopreventive agents from dill weed oil and caraway oil. Planta Med 58:338-341, 1992.
    • (1992) Planta Med , vol.58 , pp. 338-341
    • Zheng, G.1    Kenney, P.M.2    Lam, L.K.3
  • 228
  • 229
    • 0024519869 scopus 로고
    • The prevention of nitrosomethylurea-induced mammary tumors by d-limonene and orange oil
    • Maltzman TH, Hurt LM, Elson CE, Tanner MA, Gould MN. The prevention of nitrosomethylurea-induced mammary tumors by d-limonene and orange oil. Carcinogenesis 10:781-783, 1989.
    • (1989) Carcinogenesis , vol.10 , pp. 781-783
    • Maltzman, T.H.1    Hurt, L.M.2    Elson, C.E.3    Tanner, M.A.4    Gould, M.N.5
  • 230
    • 0028225147 scopus 로고
    • Inhibition of tumor promotion by various palm oil tocotrienols
    • Goh SH, Hew NF, Norhanom AW, Yadav M. Inhibition of tumor promotion by various palm oil tocotrienols. Int J Cancer 57:529-531, 1994.
    • (1994) Int J Cancer , vol.57 , pp. 529-531
    • Goh, S.H.1    Hew, N.F.2    Norhanom, A.W.3    Yadav, M.4
  • 231
    • 0028984650 scopus 로고
    • Induction of differentiation in neuro-2A cells by the monoterpene perillyl alcohol
    • Shi W, Gould MN. Induction of differentiation in neuro-2A cells by the monoterpene perillyl alcohol. Cancer Lett 95:1-6, 1995.
    • (1995) Cancer Lett , vol.95 , pp. 1-6
    • Shi, W.1    Gould, M.N.2
  • 232
    • 0029125753 scopus 로고
    • Differential effects of monoterpenes and lovastatin on ras processing
    • Hohl RJ, Lewis K. Differential effects of monoterpenes and lovastatin on ras processing. J Biol Chem 270:17508-17512, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 17508-17512
    • Hohl, R.J.1    Lewis, K.2
  • 233
    • 0028959539 scopus 로고
    • Farnesyl derivatives of rigid carboxylic acids inhibitors of raj-dependent cell growth
    • Marciano D, Ben-Baruch G, Marom M, Egozi Y, Haklai R, Kloog Y. Farnesyl derivatives of rigid carboxylic acids inhibitors of raj-dependent cell growth. J Med Chem 38:1267-1272, 1995.
    • (1995) J Med Chem , vol.38 , pp. 1267-1272
    • Marciano, D.1    Ben-Baruch, G.2    Marom, M.3    Egozi, Y.4    Haklai, R.5    Kloog, Y.6
  • 234
    • 0029089680 scopus 로고
    • Farnesyl acetate, a derivative of an isoprenoid of the mevalonate pathway, inhibits DNA replication in hamster and human cells
    • Meigs TE, Sherwood SW, Simoni RD. Farnesyl acetate, a derivative of an isoprenoid of the mevalonate pathway, inhibits DNA replication in hamster and human cells. Exp Cell Res 219:461-470, 1995.
    • (1995) Exp Cell Res , vol.219 , pp. 461-470
    • Meigs, T.E.1    Sherwood, S.W.2    Simoni, R.D.3
  • 235
    • 0027362493 scopus 로고
    • Farnesylamine: An inhibitor of farnesylation and growth of ras-transformed cells
    • Kothapalli R, Guthrie N, Chambers AF, Carroll KK. Farnesylamine: An inhibitor of farnesylation and growth of ras-transformed cells. Lipids 28:969-973, 1993.
    • (1993) Lipids , vol.28 , pp. 969-973
    • Kothapalli, R.1    Guthrie, N.2    Chambers, A.F.3    Carroll, K.K.4
  • 236
    • 17344391028 scopus 로고    scopus 로고
    • Citrus auraptene exerts dose-dependent chemopreventive activity in rat large bowel tumorigenesis: The inhibition correlates with suppression of cell proliferation and lipid peroxidation and the induction of phase II drug-metabolizing enzymes
    • Tanaka T, Kawabata K, Kakumoto M, Hara A, Murakami A, Kuki W, Takahashi Y, Yonei H, Maeda M, Ota T, Odashima A, Yamane T, Koshimizy K, Ohigashi H. Citrus auraptene exerts dose-dependent chemopreventive activity in rat large bowel tumorigenesis: The inhibition correlates with suppression of cell proliferation and lipid peroxidation and the induction of phase II drug-metabolizing enzymes. Cancer Res 58:2550-2556, 1998.
    • (1998) Cancer Res , vol.58 , pp. 2550-2556
    • Tanaka, T.1    Kawabata, K.2    Kakumoto, M.3    Hara, A.4    Murakami, A.5    Kuki, W.6    Takahashi, Y.7    Yonei, H.8    Maeda, M.9    Ota, T.10    Odashima, A.11    Yamane, T.12    Koshimizy, K.13    Ohigashi, H.14
  • 237
    • 0345420419 scopus 로고    scopus 로고
    • Tiglate, anthranilate and benzoate esters of geraniol and farnesol suppress the proliferation of B16 and HL-60 cells
    • Elson CE, Mo H. Tiglate, anthranilate and benzoate esters of geraniol and farnesol suppress the proliferation of B16 and HL-60 cells. AACR Proceed 40:396, 1999.
    • (1999) AACR Proceed , vol.40 , pp. 396
    • Elson, C.E.1    Mo, H.2
  • 238
    • 0031943302 scopus 로고    scopus 로고
    • Synthesis and biological activity of β-ion-one-derived alcohols for cancer chemoprevention
    • Jung M, Mo H, Elson CE. Synthesis and biological activity of β-ion-one-derived alcohols for cancer chemoprevention. Anticancer Res 18:189-192, 1998.
    • (1998) Anticancer Res , vol.18 , pp. 189-192
    • Jung, M.1    Mo, H.2    Elson, C.E.3
  • 239
    • 0020444890 scopus 로고
    • A study of the influence of mevalonic acid and its metabolites on the morphology of Swiss 3T3 cells
    • Schmidt RA, Glomset JA, Wright TN, Habenicht AJR, Ross R. A study of the influence of mevalonic acid and its metabolites on the morphology of Swiss 3T3 cells. J Cell Biol 95:144-153, 1982.
    • (1982) J Cell Biol , vol.95 , pp. 144-153
    • Schmidt, R.A.1    Glomset, J.A.2    Wright, T.N.3    Habenicht, A.J.R.4    Ross, R.5
  • 240
    • 0028928294 scopus 로고
    • Induction of apoptosis in liver tumors by the monoterpene perillyl alcohol
    • Mills JJ, Chari RS, Boyer IJ, Gould MN, Jirtle RL. Induction of apoptosis in liver tumors by the monoterpene perillyl alcohol. Cancer Res 55:979-983, 1995.
    • (1995) Cancer Res , vol.55 , pp. 979-983
    • Mills, J.J.1    Chari, R.S.2    Boyer, I.J.3    Gould, M.N.4    Jirtle, R.L.5
  • 241
    • 0032502793 scopus 로고    scopus 로고
    • Lamin B phosphorylation by protein kinase C and proteolysis during apoptosis in human leukemia HL-60 cells
    • Shimizu T, Cao CX, Shao RG, Pommier Y. Lamin B phosphorylation by protein kinase C and proteolysis during apoptosis in human leukemia HL-60 cells. J Biol Chem 273:8669-8674, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 8669-8674
    • Shimizu, T.1    Cao, C.X.2    Shao, R.G.3    Pommier, Y.4
  • 242
    • 0029828909 scopus 로고    scopus 로고
    • Identifying differential gene expression in monoterpene-treated mammary carcinomas using subtractive display
    • Ariazi EA, Gould MN. Identifying differential gene expression in monoterpene-treated mammary carcinomas using subtractive display. J Biol Chem 271:29286-29294, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 29286-29294
    • Ariazi, E.A.1    Gould, M.N.2
  • 243
    • 0025228499 scopus 로고
    • Inhibition of transformation in cultured rat tracheal epithelial cells by potential chemopreventive agents
    • Steele VE, Kelloff GJ, Wilkinson BP, Arnold JT. Inhibition of transformation in cultured rat tracheal epithelial cells by potential chemopreventive agents. Cancer Res 50:2068-2074, 1990.
    • (1990) Cancer Res , vol.50 , pp. 2068-2074
    • Steele, V.E.1    Kelloff, G.J.2    Wilkinson, B.P.3    Arnold, J.T.4
  • 244
    • 0027199916 scopus 로고
    • Increased mannose-6-phosphate-insulin-like growth factor II receptor and transforming growth factor β-1 levels during monoterpene-induced regression of mammary tumors
    • Jirtle RL, Haag JD, Ariazi EA, Gould MN. Increased mannose-6-phosphate-insulin-like growth factor II receptor and transforming growth factor β-1 levels during monoterpene-induced regression of mammary tumors. Cancer Res 53:3849-3852, 1993.
    • (1993) Cancer Res , vol.53 , pp. 3849-3852
    • Jirtle, R.L.1    Haag, J.D.2    Ariazi, E.A.3    Gould, M.N.4
  • 245
    • 0024947834 scopus 로고
    • Why are secondary metabolites (natural products) biosynthesized?
    • Williams DH, Stone MJ, Hauck PR, Rahman SK. Why are secondary metabolites (natural products) biosynthesized? J Nat Prod 52:1189-1208, 1989.
    • (1989) J Nat Prod , vol.52 , pp. 1189-1208
    • Williams, D.H.1    Stone, M.J.2    Hauck, P.R.3    Rahman, S.K.4
  • 246
    • 0001176872 scopus 로고
    • Leaf chemistry as a defense against insects
    • Scriber JM, Ayres MP. Leaf chemistry as a defense against insects. Anim Plant Sci 1:117-123, 1988.
    • (1988) Anim Plant Sci , vol.1 , pp. 117-123
    • Scriber, J.M.1    Ayres, M.P.2
  • 248
    • 0023616187 scopus 로고
    • Antimicrobial activities of essential oils. A 1976-1986 literature review on possible applications
    • Janssen AM, Scheffer JJ, Baerheim Svendsen A. Antimicrobial activities of essential oils. A 1976-1986 literature review on possible applications. Pharm Weekbl (Sci) 9:193-197, 1987.
    • (1987) Pharm Weekbl (Sci) , vol.9 , pp. 193-197
    • Janssen, A.M.1    Scheffer, J.J.2    Baerheim Svendsen, A.3
  • 249
    • 0028603390 scopus 로고
    • Biological effects of prenylated hydroquinones: Structure-activity relationship studies in antimicrobial, brine shrimp, and fish lethality assays
    • De Rosa S, De Giulio A, Iodice C. Biological effects of prenylated hydroquinones: Structure-activity relationship studies in antimicrobial, brine shrimp, and fish lethality assays. J Nat Prod 57:1711-1716, 1994.
    • (1994) J Nat Prod , vol.57 , pp. 1711-1716
    • De Rosa, S.1    De Giulio, A.2    Iodice, C.3
  • 250
    • 0028467448 scopus 로고
    • Prenylated flavonoids in the roots of yellow lupin
    • Tahara S, Katagiri Y, Ingham JL, Mizutani J. Prenylated flavonoids in the roots of yellow lupin. Phytochem 36:1261-1271, 1994.
    • (1994) Phytochem , vol.36 , pp. 1261-1271
    • Tahara, S.1    Katagiri, Y.2    Ingham, J.L.3    Mizutani, J.4
  • 252
    • 0029824394 scopus 로고    scopus 로고
    • Combined chemical defenses against an insect-fungal complex
    • Klepzig KD, Smalley EB, Raffa KF. Combined chemical defenses against an insect-fungal complex. J Chem Ecol 22:1367-1388, 1996.
    • (1996) J Chem Ecol , vol.22 , pp. 1367-1388
    • Klepzig, K.D.1    Smalley, E.B.2    Raffa, K.F.3
  • 253
    • 0008375297 scopus 로고    scopus 로고
    • The biological properties of monoterpenes: Hypotensive effects on rats and antifungal activities on plant pathogenic fungi of monoterpenes
    • Saito K, Okabe T, Inamori Y, Tsujibo H, Miyake Y, Hiraoka K, Ishida N. The biological properties of monoterpenes: Hypotensive effects on rats and antifungal activities on plant pathogenic fungi of monoterpenes. Mokuzai Gakkaishi 42:677-680, 1996.
    • (1996) Mokuzai Gakkaishi , vol.42 , pp. 677-680
    • Saito, K.1    Okabe, T.2    Inamori, Y.3    Tsujibo, H.4    Miyake, Y.5    Hiraoka, K.6    Ishida, N.7
  • 254
    • 0031403751 scopus 로고    scopus 로고
    • De novo biosynthesis of volatiles induced by insect herbivory in cotton plants
    • Pare PW, Tumlinson JH. De novo biosynthesis of volatiles induced by insect herbivory in cotton plants. Plant Physiol 114:1161-1167, 1997.
    • (1997) Plant Physiol , vol.114 , pp. 1161-1167
    • Pare, P.W.1    Tumlinson, J.H.2
  • 255
    • 0030838586 scopus 로고    scopus 로고
    • Monoterpene composition of Pinus sylvestris varieties resistant and susceptible to Dioryctria zimmermani
    • Sadof CS, Grant GG. Monoterpene composition of Pinus sylvestris varieties resistant and susceptible to Dioryctria zimmermani. J Chem Ecol 23:1917-1927, 1997.
    • (1997) J Chem Ecol , vol.23 , pp. 1917-1927
    • Sadof, C.S.1    Grant, G.G.2
  • 256
    • 0027132256 scopus 로고
    • 2,3-Dihydrofarnesoic acid, a unique terpene from trichomes of Lycopersicon hirsutum, repels spider mites
    • Snyder JC, Guo Z, Thacker R, Goodman JP, St. Pyrek J. 2,3-Dihydrofarnesoic acid, a unique terpene from trichomes of Lycopersicon hirsutum, repels spider mites. J Chem Ecol 19:2981-2997, 1993.
    • (1993) J Chem Ecol , vol.19 , pp. 2981-2997
    • Snyder, J.C.1    Guo, Z.2    Thacker, R.3    Goodman, J.P.4    St. Pyrek, J.5
  • 258
    • 51249186164 scopus 로고
    • Effect of β-ionone on Aspergillus flavus and Aspergillus parasiticus growth, sporulation, morphology and aflatoxin production
    • Wilson DM, Gueldner RC, McKinney JK, Lievsay RH, Evans BD, Hill RA. Effect of β-ionone on Aspergillus flavus and Aspergillus parasiticus growth, sporulation, morphology and aflatoxin production. JAOCS 58:959A-961A, 1981.
    • (1981) JAOCS , vol.58
    • Wilson, D.M.1    Gueldner, R.C.2    McKinney, J.K.3    Lievsay, R.H.4    Evans, B.D.5    Hill, R.A.6
  • 259
    • 0000583994 scopus 로고
    • Effects of β-ionone and abscisic acid on the growth of tobacco and resistance to blue mold: Mimicry of effects of stem infection by Peronospora tabacina Adam
    • Salt SD, Tuzun S, Kuc J. Effects of β-ionone and abscisic acid on the growth of tobacco and resistance to blue mold: Mimicry of effects of stem infection by Peronospora tabacina Adam. Physiol Mol Plant Pathol 28:287-297, 1986.
    • (1986) Physiol Mol Plant Pathol , vol.28 , pp. 287-297
    • Salt, S.D.1    Tuzun, S.2    Kuc, J.3
  • 260
    • 10544245502 scopus 로고
    • Inhibitory effect of β-ionone on growth and aflatoxin production by Aspergillus parasiticus on peanuts
    • Wei CI, Tan H, Fernando S, Ko NJ. Inhibitory effect of β-ionone on growth and aflatoxin production by Aspergillus parasiticus on peanuts. J Food Protect 49:515-518, 1986.
    • (1986) J Food Protect , vol.49 , pp. 515-518
    • Wei, C.I.1    Tan, H.2    Fernando, S.3    Ko, N.J.4
  • 261
    • 0029971797 scopus 로고    scopus 로고
    • Camptothecin and taxol: From discovery to clinic
    • Wall ME, Wani MC. Camptothecin and taxol: From discovery to clinic. J Ethnopharmacol 51:239-254, 1996.
    • (1996) J Ethnopharmacol , vol.51 , pp. 239-254
    • Wall, M.E.1    Wani, M.C.2
  • 263
    • 0031255282 scopus 로고    scopus 로고
    • Phytochemicals: Guardians of our health
    • Craig WJ. Phytochemicals: Guardians of our health. J Am Diet Assoc 97:S199-S204, 1997.
    • (1997) J Am Diet Assoc , vol.97
    • Craig, W.J.1
  • 264
    • 0031446103 scopus 로고    scopus 로고
    • Monoterpenes in breast cancer chemoprevention
    • Crowell PL. Monoterpenes in breast cancer chemoprevention. Breast Cancer Res Treat 46:191-197, 1997.
    • (1997) Breast Cancer Res Treat , vol.46 , pp. 191-197
    • Crowell, P.L.1
  • 265
    • 0030867207 scopus 로고    scopus 로고
    • Cancer chemoprevention and therapy by monoterpenes
    • Gould MN. Cancer chemoprevention and therapy by monoterpenes. Environ Health Perspect 105(Suppl 4):977-979, 1997.
    • (1997) Environ Health Perspect , vol.105 , Issue.4 SUPPL. , pp. 977-979
    • Gould, M.N.1
  • 268
    • 33749747829 scopus 로고
    • Trace components in flavours
    • Tong ST. Trace components in flavours. Int Flav Food Addit 6:350-355, 1975.
    • (1975) Int Flav Food Addit , vol.6 , pp. 350-355
    • Tong, S.T.1
  • 269
    • 84986516339 scopus 로고
    • GLC-MS analysis of volatile constituents in rabbiteye blueberries
    • Horvat RJ, Senter SD, Dekazos ED. GLC-MS analysis of volatile constituents in rabbiteye blueberries. J Food Sci 48:278-279, 1983.
    • (1983) J Food Sci , vol.48 , pp. 278-279
    • Horvat, R.J.1    Senter, S.D.2    Dekazos, E.D.3
  • 270
    • 84972896065 scopus 로고
    • Citrus carotenoids. VI. The redder carotenoid group contained in the peel of Citrus unshiu var. Benidobashi
    • Umeda K, Tanaka Y, Sato S. Citrus carotenoids. VI. The redder carotenoid group contained in the peel of Citrus unshiu var. Benidobashi. J Food Sci Technol 18:482-487, 1971.
    • (1971) J Food Sci Technol , vol.18 , pp. 482-487
    • Umeda, K.1    Tanaka, Y.2    Sato, S.3
  • 271
    • 0000903324 scopus 로고
    • Generation of oxidation artifacts during the hydrolysis of norisoprenoid glycosides by fungal enzyme preparations
    • Sefton MA, Williams PJ. Generation of oxidation artifacts during the hydrolysis of norisoprenoid glycosides by fungal enzyme preparations. J Agric Food Chem 39:1994-1997, 1991.
    • (1991) J Agric Food Chem , vol.39 , pp. 1994-1997
    • Sefton, M.A.1    Williams, P.J.2
  • 272
    • 84986835477 scopus 로고
    • The flavor of muscat wine: The sensory contribution of some volatile compounds
    • Etievant PX, Issanchou SN, Bayonove CL. The flavor of muscat wine: The sensory contribution of some volatile compounds. J Sci Food Agric 34:497-504, 1983.
    • (1983) J Sci Food Agric , vol.34 , pp. 497-504
    • Etievant, P.X.1    Issanchou, S.N.2    Bayonove, C.L.3
  • 273
    • 0000958549 scopus 로고
    • Glycosidically bound aroma compounds in the fruits of Prunus spp.: Apricot (Prunus armeniaca L.), peach (Prunus persica, L.), yellow plum (Prunus domestica ssp. syriaca)
    • Krammer G, Winterhalter P, Schwab M, Schreier P. Glycosidically bound aroma compounds in the fruits of Prunus spp.: Apricot (Prunus armeniaca L.), peach (Prunus persica, L.), yellow plum (Prunus domestica ssp. syriaca). J Agric Food Chem 39:778-781, 1991.
    • (1991) J Agric Food Chem , vol.39 , pp. 778-781
    • Krammer, G.1    Winterhalter, P.2    Schwab, M.3    Schreier, P.4
  • 274
    • 84948780444 scopus 로고
    • Relations between the content of aroma compounds and the sensory evaluation of 10 raspberry varieties (Rubus idacus L)
    • Larsen M, Poll L, Callensen O, Lewis M. Relations between the content of aroma compounds and the sensory evaluation of 10 raspberry varieties (Rubus idacus L). Acta Agric Scand 41:447-454, 1991.
    • (1991) Acta Agric Scand , vol.41 , pp. 447-454
    • Larsen, M.1    Poll, L.2    Callensen, O.3    Lewis, M.4
  • 275
    • 0344899024 scopus 로고
    • A 4-hydroxy-β-ionone disaccharide glycoside from raspberry fruits
    • Pabst A, Barron D, Semon E, Schreier P. A 4-hydroxy-β-ionone disaccharide glycoside from raspberry fruits. Phytochem 31:3105-3107, 1992.
    • (1992) Phytochem , vol.31 , pp. 3105-3107
    • Pabst, A.1    Barron, D.2    Semon, E.3    Schreier, P.4
  • 276
    • 0027134080 scopus 로고
    • Sensory, chemical and gas, chromatographic evaluation of five raspberry cultivars
    • Shamaila M, Skura B, Daubeny H, Anderson A. Sensory, chemical and gas, chromatographic evaluation of five raspberry cultivars. Food Res Int 26:443-449, 1993.
    • (1993) Food Res Int , vol.26 , pp. 443-449
    • Shamaila, M.1    Skura, B.2    Daubeny, H.3    Anderson, A.4
  • 277
    • 0015946449 scopus 로고
    • Essential oils of strawberries and their effect on aroma
    • Vereshchagin PV. Essential oils of strawberries and their effect on aroma. Prikl Biokhim Mikrobiol 10:166-169, 1974.
    • (1974) Prikl Biokhim Mikrobiol , vol.10 , pp. 166-169
    • Vereshchagin, P.V.1
  • 278
    • 84954970365 scopus 로고
    • Volatile components of ripe tomatoes and their juices, purees and pastes
    • Chung TY, Kato HH, Hayase F. Volatile components of ripe tomatoes and their juices, purees and pastes. J Agric Biol Chem 47:343-352, 1983.
    • (1983) J Agric Biol Chem , vol.47 , pp. 343-352
    • Chung, T.Y.1    Kato, H.H.2    Hayase, F.3
  • 281
    • 0028042606 scopus 로고
    • Occurrence of a growth inhibitor, 3-hydroxy-β-ionone, in seven cultivars of Phaseolus vulgaris and its role in light-induced growth inhibition
    • Kato-Noguchi H. Occurrence of a growth inhibitor, 3-hydroxy-β-ionone, in seven cultivars of Phaseolus vulgaris and its role in light-induced growth inhibition. Phytochem 36:273-275, 1994.
    • (1994) Phytochem , vol.36 , pp. 273-275
    • Kato-Noguchi, H.1
  • 282
    • 0000544204 scopus 로고
    • Broccoli storage under low-oxygen atmosphere: Identification of higher boiling volatiles
    • Hansen M, Buttery RG, Stern DJ, Cantwell MI, Ling LC. Broccoli storage under low-oxygen atmosphere: Identification of higher boiling volatiles. J Agric Food Chem 40:850-852, 1992.
    • (1992) J Agric Food Chem , vol.40 , pp. 850-852
    • Hansen, M.1    Buttery, R.G.2    Stern, D.J.3    Cantwell, M.I.4    Ling, L.C.5
  • 283
    • 84981588512 scopus 로고
    • Behavioral responses of the carrot fly larva, Psila rosae, to carrot root volatiles
    • Ryan MF, Guerin PM. Behavioral responses of the carrot fly larva, Psila rosae, to carrot root volatiles. Physiol Entomol 7:315-324, 1982.
    • (1982) Physiol Entomol , vol.7 , pp. 315-324
    • Ryan, M.F.1    Guerin, P.M.2
  • 285
    • 0001124906 scopus 로고
    • Analysis of the volatile constituents of baked, Jewel sweet potatoes
    • Purcell AE, Later DW, Lee ML. Analysis of the volatile constituents of baked, Jewel sweet potatoes. J Agric Food Chem 28:939-941, 1980.
    • (1980) J Agric Food Chem , vol.28 , pp. 939-941
    • Purcell, A.E.1    Later, D.W.2    Lee, M.L.3
  • 286
    • 0004582695 scopus 로고
    • 3S-(+)-3,7-dimethyl-1,5-octadiene-3,7-diol and ionone derivatives from tea
    • Etoh H, Ina K, Iguchi M. 3S-(+)-3,7-dimethyl-1,5-octadiene-3,7-diol and ionone derivatives from tea. Agric Biochem 44:2999-3000, 1990.
    • (1990) Agric Biochem , vol.44 , pp. 2999-3000
    • Etoh, H.1    Ina, K.2    Iguchi, M.3
  • 287
    • 0004616616 scopus 로고
    • Cytotoxicity of green tea flavor compounds against two solid tumor cells
    • Kubo I, Morimitsu Y. Cytotoxicity of green tea flavor compounds against two solid tumor cells. J Agric Food Chem 43:1626-1628, 1995.
    • (1995) J Agric Food Chem , vol.43 , pp. 1626-1628
    • Kubo, I.1    Morimitsu, Y.2
  • 288
    • 0007753389 scopus 로고
    • Evaluation of potent odorants in parsley leaves (Petroselinum crispum ssp. crispum) by aroma extract dilution analysis
    • Jung HP, Sen A, Grosch W. Evaluation of potent odorants in parsley leaves (Petroselinum crispum ssp. crispum) by aroma extract dilution analysis. Leb Wissen Technol 25:55-60, 1992.
    • (1992) Leb Wissen Technol , vol.25 , pp. 55-60
    • Jung, H.P.1    Sen, A.2    Grosch, W.3
  • 289
    • 0001527606 scopus 로고
    • Genotype and environment effects on tocols of barley and oats
    • Peterson DM, Qureshi AA. Genotype and environment effects on tocols of barley and oats. Cereal Chem 70:157-162, 1993.
    • (1993) Cereal Chem , vol.70 , pp. 157-162
    • Peterson, D.M.1    Qureshi, A.A.2
  • 290
    • 0027559892 scopus 로고
    • Identification and quantitation of γ-oryzanol components and simultaneous assessment of tocols in rice bran oil
    • Rogers EJ, Rice SM, Nicolosi RJ, Carpenter DR, McClelland CA, Romanczyk LJ Jr. Identification and quantitation of γ-oryzanol components and simultaneous assessment of tocols in rice bran oil. JAOCS 70:301-307, 1993.
    • (1993) JAOCS , vol.70 , pp. 301-307
    • Rogers, E.J.1    Rice, S.M.2    Nicolosi, R.J.3    Carpenter, D.R.4    McClelland, C.A.5    Romanczyk Jr., L.J.6
  • 291
    • 10544246347 scopus 로고
    • Nutrient composition of selected wheats and wheat products. III. Tocopherols
    • Slover HT, Lehmann J, Valis RJ. Nutrient composition of selected wheats and wheat products. III. Tocopherols. Cereal Chem 46:635-641, 1969.
    • (1969) Cereal Chem , vol.46 , pp. 635-641
    • Slover, H.T.1    Lehmann, J.2    Valis, R.J.3
  • 292
  • 293
    • 0028214765 scopus 로고
    • Effect of processing upon the tocopherol and tocotrienol composition of table olives
    • Hassapidou MN, Balatsouras GD, Manoukas AG. Effect of processing upon the tocopherol and tocotrienol composition of table olives. Food Chem 50:111-114, 1994.
    • (1994) Food Chem , vol.50 , pp. 111-114
    • Hassapidou, M.N.1    Balatsouras, G.D.2    Manoukas, A.G.3
  • 294
    • 0345542068 scopus 로고
    • Variations in the tocopherol and tocotrienol content during refining and hydrogenation of edible oils
    • Hernandez-Rabascall N, Boatella-Riera J. Variations in the tocopherol and tocotrienol content during refining and hydrogenation of edible oils. Grasas Aceites 38:145-148, 1987.
    • (1987) Grasas Aceites , vol.38 , pp. 145-148
    • Hernandez-Rabascall, N.1    Boatella-Riera, J.2
  • 295
    • 0002934819 scopus 로고
    • Determination of tocopherols in vegetable oils by HPLC
    • Micali G, Curro P. Determination of tocopherols in vegetable oils by HPLC. Rivista Ital Sostanze Grasse 61:95-98, 1984.
    • (1984) Rivista Ital Sostanze Grasse , vol.61 , pp. 95-98
    • Micali, G.1    Curro, P.2
  • 296
    • 51249172900 scopus 로고
    • Minor constituents of palm oil
    • Goh SH, Choo YM, Ong ASH. Minor constituents of palm oil. JAOCS 62:237-240, 1985.
    • (1985) JAOCS , vol.62 , pp. 237-240
    • Goh, S.H.1    Choo, Y.M.2    Ong, A.S.H.3
  • 297
    • 0026701521 scopus 로고
    • Fruit, vegetables, and cancer prevention: A review of the epidemiological evidence
    • Block G, Patterson B, Subar A. Fruit, vegetables, and cancer prevention: A review of the epidemiological evidence. Nutr Cancer 18:1-29, 1992.
    • (1992) Nutr Cancer , vol.18 , pp. 1-29
    • Block, G.1    Patterson, B.2    Subar, A.3
  • 298
    • 0026246632 scopus 로고
    • Vegetables, fruit, and cancer. II. Mechanisms
    • Steinmetz KA, Potter JD. Vegetables, fruit, and cancer. II. Mechanisms. Cancer Causes Control 2:427-442, 1991.
    • (1991) Cancer Causes Control , vol.2 , pp. 427-442
    • Steinmetz, K.A.1    Potter, J.D.2
  • 299
    • 0028305595 scopus 로고
    • Diet and health: What should we eat?
    • Willet WC. Diet and health: What should we eat? Science 64:532-537, 1994.
    • (1994) Science , vol.64 , pp. 532-537
    • Willet, W.C.1
  • 300
    • 0024445622 scopus 로고
    • Effect of wheat fiber and vitamins C and e on rectal polyps in patients with familial adenomatous polypsis
    • DeCosse JJ, Miller HH, Lesser ML. Effect of wheat fiber and vitamins C and E on rectal polyps in patients with familial adenomatous polypsis. J Natl Cancer Inst 81:1290-1297, 1989.
    • (1989) J Natl Cancer Inst , vol.81 , pp. 1290-1297
    • DeCosse, J.J.1    Miller, H.H.2    Lesser, M.L.3
  • 302
    • 0028303234 scopus 로고
    • A randomized trial of a low-fat, high-fibre diet in the recurrence of colorectal polyps: Toronto Polyp Prevention Group
    • McKeown-Eyssen GE, Bright-See E, Bruce WR, Jazmaji VA. A randomized trial of a low-fat, high-fibre diet in the recurrence of colorectal polyps: Toronto Polyp Prevention Group. J Clin Epidemiol 47:525-536, 1994.
    • (1994) J Clin Epidemiol , vol.47 , pp. 525-536
    • McKeown-Eyssen, G.E.1    Bright-See, E.2    Bruce, W.R.3    Jazmaji, V.A.4
  • 304
    • 0030013268 scopus 로고    scopus 로고
    • Vitamin E and vitamin C supplement use and risk of all-cause and coronary heart disease mortality in older persons: The established populations for epidemiologic studies of the elderly
    • Losonoczy KG, Harris TB, Havlik RJ. Vitamin E and vitamin C supplement use and risk of all-cause and coronary heart disease mortality in older persons: The established populations for epidemiologic studies of the elderly. Am J Clin Nutr 64:190-196, 1996.
    • (1996) Am J Clin Nutr , vol.64 , pp. 190-196
    • Losonoczy, K.G.1    Harris, T.B.2    Havlik, R.J.3
  • 308
    • 0010607277 scopus 로고
    • The effect of vitamin E and β-carotene on the incidence of lung cancer and other cancers in male smokers
    • The α-Tocopherol, β-Carotene Cancer Prevention Study Group. The effect of vitamin E and β-carotene on the incidence of lung cancer and other cancers in male smokers. N Engl J Med 330:1029-1035, 1994.
    • (1994) N Engl J Med , vol.330 , pp. 1029-1035
  • 311
    • 0030018520 scopus 로고    scopus 로고
    • Intake of vitamins A, C, and E and postmenopausal breast cancer: The Iowa Women's Health Study
    • Kushi LH, Fee RM, Sellers TA, Zheng W, Folsom AR. Intake of vitamins A, C, and E and postmenopausal breast cancer: The Iowa Women's Health Study. Am J Epidemiol 144:165-174, 1996.
    • (1996) Am J Epidemiol , vol.144 , pp. 165-174
    • Kushi, L.H.1    Fee, R.M.2    Sellers, T.A.3    Zheng, W.4    Folsom, A.R.5
  • 312
    • 0028807592 scopus 로고
    • Epidemiologic evidence for vitamin C and vitamin E in cancer prevention
    • Byers T, Guerrero N. Epidemiologic evidence for vitamin C and vitamin E in cancer prevention. Am J Clin Nutr 62:S1385-S1392, 1995.
    • (1995) Am J Clin Nutr , vol.62
    • Byers, T.1    Guerrero, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.