Studies on Squalene Epoxidase of Rat Liver

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works

Evidence for Biochemically Different Types of Vesicles in the Hepatic Microsomal Fraction*

Imai, Y., Ito, A., & Sato, R. (1966) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a128453 · Cited by 749 · see citing works

Zur Kenntnis der Triterpene. 190. Mitteilung. Eine stereochemische Interpretation der biogenetischen Isoprenregel bei den Triterpenen

Eschenmoser, A., Růžička, L., Jeger, O., & Arigoni, D. (1955) · Helvetica Chimica Acta · doi:10.1002/hlca.19550380728 · Cited by 605 · see citing works

Mechanisms of Oxygen Metabolism

Mason, H. S. (1957) · Science · doi:10.1126/science.125.3259.1185 · Cited by 313 · see citing works

Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes

Oshino, N., Imai, Y., & Sato, R. (1966) · Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation · doi:10.1016/0926-6593(66)90137-8 · Cited by 285 · see citing works

Oxidases

Mason, H. S. (1965) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.34.070165.003115 · Cited by 238 · see citing works

2,3-Oxidosqualene, an Intermediate in the Biological Synthesis of Sterols from Squalene¹

Corey, E. J., Russey, W. E., & de Montellano, P. R. O. (1966) · Journal of the American Chemical Society · doi:10.1021/ja00972a056 · Cited by 225 · see citing works

Enzymic Conversion of Squalene 2,3-Oxide to Lanosterol and Cholesterol

Tamelen, E. E. V., Willett, J. D., Clayton, R. B., & Lord, K. E. (1966) · Journal of the American Chemical Society · doi:10.1021/ja00972a058 · Cited by 177 · see citing works

Studies on the Biosynthesis of Cholesterol

Popják, G. J., Goodman, D. S., Cornforth, J. W., Cornforth, R. H., & Ryhage, R. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64109-2 · Cited by 166 · see citing works

ON THE CONVERSION OF SQUALENE TO LANOSTEROL IN VITRO

Tchen, T. T., & Bloch, K. E. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70878-8 · Cited by 136 · see citing works

ON THE MECHANISM OF ENZYMATIC CYCLIZATION OF SQUALENE

Tchen, T. T., & Bloch, K. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70879-x · Cited by 84 · see citing works

A Soluble 2,3-Oxidosqualene Sterol Cyclase

DEAN, P. D. G., de Montellano, P. R. O., Bloch, K. E., & Corey, E. J. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99606-7 · Cited by 83 · see citing works

2,3-Iminosqualene, a potent inhibitor of the enzymic cyclization of 2,3-oxidosqualene to sterols

Corey, E. J., de Montellano, P. R. O., Lin, K., & DEAN, P. D. G. (1967) · Journal of the American Chemical Society · doi:10.1021/ja00987a089 · Cited by 77 · see citing works

Metabolic Fate of 10,11-Dihydrosqualene in Sterol-Producing Rat Liver Homogenate

Corey, E. J., & Russey, W. E. (1966) · Journal of the American Chemical Society · doi:10.1021/ja00972a057 · Cited by 59 · see citing works

SOME PROPERTIES OF THE MICROSOMAL 2,3-OXIDOSQUALENE STEROL CYCLASE

Yamamoto, S., Lin, K., & Bloch, K. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.63.1.110 · Cited by 49 · see citing works

Studies on the Conversion of Squalene to Sterol with Rat Liver Enzymes

Goodman, D. S. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64016-5 · Cited by 26 · see citing works

Relation of cholesterol synthesis and NADPH oxidation by microsomal electron transport system involving P-450

Wada, F., Hirata, K., & Sakamoto, Y. (1967) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(67)90131-4 · Cited by 18 · see citing works

Control of Cholesterol Biosynthesis by a Plasma Apo-lipoprotein

Boyd, G. S., & Onajobi, F. D. (1969) · Nature · doi:10.1038/221574b0 · Cited by 12 · see citing works

Epoxides in Polycyclic Aromatic Hydrocarbon Metabolism and Carcinogenesis

Sims, P. H., & Grover, P. L. (1974) · Advances in cancer research · doi:10.1016/s0065-230x(08)60111-6 · Cited by 724 · see citing works

Liver microsomal metabolism of aflatoxin B 1 to a reactive derivative toxic to Salmonella typhimurium TA 1530.

Garner, R. C., Miller, E. C., & MILLER, J. A. (1972) · PubMed · Cited by 410 · see citing works

Biochemistry of the violaxanthin cycle in higher plants

Yamamoto, H. Y. (1979) · Pure and Applied Chemistry · doi:10.1351/pac197951030639 · Cited by 372 · see citing works

Biodegradation of Natural Rubber and Related Compounds: Recent Insights into a Hardly Understood Catabolic Capability of Microorganisms

Rose, K., & Steinbüchel, A. (2005) · Applied and Environmental Microbiology · doi:10.1128/aem.71.6.2803-2812.2005 · Cited by 308 · see citing works

Cholesterol-Dependent Degradation of Squalene Monooxygenase, a Control Point in Cholesterol Synthesis beyond HMG-CoA Reductase

Gill, S., Stevenson, J., Kristiana, I., & Brown, A. J. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.01.015 · Cited by 304 · see citing works

Chemical and biological synthesis of chiral epoxides

Besse, P. B.-H. B.-H. P. P., & Veschambre, H. (1994) · Tetrahedron · doi:10.1016/s0040-4020(01)85362-x · Cited by 295 · see citing works

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

Spanova, M., & Daum, G. (2011) · European Journal of Lipid Science and Technology · doi:10.1002/ejlt.201100203 · Cited by 268 · see citing works

A genomics approach to the early stages of triterpene saponin biosynthesis in Medicago truncatula

Suzuki, H., Achnine, L., Xu, R., Matsuda, S. P. T., & Dixon, R. A. (2002) · The Plant Journal · doi:10.1046/j.1365-313x.2002.01497.x · Cited by 260 · see citing works

The human flavoproteome

Lienhart, W., Gudipati, V., & Macheroux, P. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.02.015 · Cited by 248 · see citing works

Purification and properties of sterol carrier protein2.

Noland, B. J., Arebalo, R. E., Hansbury, E., & Scallen, T. J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85664-8 · Cited by 238 · see citing works

A suppressor screen in Mecp2 mutant mice implicates cholesterol metabolism in Rett syndrome

Buchovecky, C. M., Turley, S. D., Brown, H. M., Kyle, S. M., McDonald, J. G., Liu, B., Pieper, A. A., Huang, W., Katz, D. M., Russell, D. W., et al. (2013) · Nature Genetics · doi:10.1038/ng.2714 · Cited by 234 · see citing works

Biochemical Characterization of StyAB from Pseudomonas sp. Strain VLB120 as a Two-Component Flavin-Diffusible Monooxygenase

Otto, K., Hofstetter, K., Röthlisberger, M., Witholt, B., & Schmid, A. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.16.5292-5302.2004 · Cited by 205 · see citing works

Regulation and deregulation of cholesterol homeostasis: The liver as a metabolic “power station”

Trapani, L. (2012) · World Journal of Hepatology · doi:10.4254/wjh.v4.i6.184 · Cited by 178 · see citing works

Inhibition of squalene epoxidase by allylamine antimycotic compounds. A comparative study of the fungal and mammalian enzymes

Ryder, N. S., & Dupont, M.-C. (1985) · Biochemical Journal · doi:10.1042/bj2300765 · Cited by 178 · see citing works

Metal-Catalyzed Oxidations of Organic Compounds in the Liquid Phase: A Mechanistic Approach

Sheldon, R. A., & Kochi, J. K. (1976) · Advances in catalysis · doi:10.1016/s0360-0564(08)60316-8 · Cited by 177 · see citing works

An epoxide is an intermediate in the microsomal metabolism of the chemical carcinogen, dibenz(a,h)anthracene

Selkirk, J. K., Huberman, E., & Heidelberger, C. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(71)90562-6 · Cited by 172 · see citing works

Solubilization and partial characterization of rat liver squalene epoxidase

Ono, T., & Bloch, K. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41847-4 · Cited by 157 · see citing works

Squalene epoxidase is a bona fide oncogene by amplification with clinical relevance in breast cancer

Brown, D. N., Caffa, I., Cirmena, G., Piras, D., Garuti, A., Gallo, M., Alberti, S., Nencioni, A., Ballestrero, A., & Zoppoli, G. M. (2016) · Scientific Reports · doi:10.1038/srep19435 · Cited by 146 · see citing works

Fish Nutrition

Cowey, C. B., & SARGENT, J. R. (1972) · Advances in marine biology · doi:10.1016/s0065-2881(08)60419-8 · Cited by 131 · see citing works

Molecular Cloning and Expression of Rat Squalene Epoxidase

Sakakibara, J., Watanabe, R., Kanai, Y., & Ono, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.1.17 · Cited by 128 · see citing works

In vitro metabolism of retinoic acid in hamster intestine and liver.

Roberts, A. B., Nichols, M. D., Newton, D. L., & Sporn, M. B. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50362-8 · Cited by 126 · see citing works

Detailed Mechanism of Squalene Epoxidase Inhibition by Terbinafine

Nowosielski, M., Hoffmann, M., Wyrwicz, L. S., Stępniak, P., Plewczyński, D., Łaźniewski, M., Ginalski, K., & Rychlewski, L. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci100403b · Cited by 125 · see citing works

Specificity and Role in Cholesterol Biosynthesis of a Squalene and Sterol Carrier Protein

Ritter, M. C., & Dempsey, M. E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77003-3 · Cited by 123 · see citing works

The Biosynthesis of Ergosterol

MERCER, E. I. (1984) · Pesticide Science · doi:10.1002/ps.2780150206 · Cited by 119 · see citing works

Formation and metabolism in vitro of 5,6-epoxides of cholesterol and β-sitosterol

Aringer, L., & Eneroth, P. H. E. (1974) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)36787-0 · Cited by 116 · see citing works

Evidence for a Noncatalytic Carrier Protein in Cholesterol Biosynthesis

Scallen, T. J., Schuster, M. W., & Dhar, A. K. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62553-0 · Cited by 116 · see citing works

Demonstrated and inferred metabolism associated with cytosolic lipid droplets

Goodman, J. M. (2009) · Journal of Lipid Research · doi:10.1194/jlr.r001446 · Cited by 116 · see citing works

Changes in phylloquinone epoxidase activity related to prothrombin synthesis and microsomal clotting activity in the rat

Willingham, A. K., & Matschiner, J. T. (1974) · Biochemical Journal · doi:10.1042/bj1400435 · Cited by 115 · see citing works

Squalene monooxygenase: a journey to the heart of cholesterol synthesis

Chua, N. K., Coates, H. W., & Brown, A. J. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101033 · Cited by 110 · see citing works

Squalene Epoxidase of Rat Liver

Tai, H., & Bloch, K. E. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45101-6 · Cited by 110 · see citing works

NB-598: a potent competitive inhibitor of squalene epoxidase.

Horie, M., Tsuchiya, Y., Hayashi, M., Iida, Y., Iwasawa, Y., Nagata, Y., Sawasaki, Y., Fukuzumi, H., Kitani, K., & Kamei, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44716-8 · Cited by 108 · see citing works

Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis

Shibata, N., Arita, M., Misaki, Y., Dohmae, N., Takio, K., Ono, T., Inoue, K., & Arai, H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041620398 · Cited by 108 · see citing works

Cloning, Heterologous Expression, and Enzymological Characterization of Human Squalene Monooxygenase

Laden, B. P., Tang, Y., & Porter, T. D. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1629 · Cited by 107 · see citing works

Ergosterol biosynthesis inSaccharomyces cerevisiae

Karst, F., & Lacroute, F. (1977) · Molecular and General Genetics MGG · doi:10.1007/bf00571282 · Cited by 107 · see citing works

Inhibitors of squalene biosynthesis and metabolism

Abe, I., Tomesch, J. C., Wattanasin, S., & Prestwich, G. D. (1994) · Natural Product Reports · doi:10.1039/np9941100279 · Cited by 101 · see citing works

Obesity Is Mediated by Differential Aryl Hydrocarbon Receptor Signaling in Mice Fed a Western Diet

Kerley-Hamilton, J. S., Trask, H. W., Ridley, C. J. A., DuFour, E., Ringelberg, C. S., Nurinova, N., Wong, D., Moodie, K. L., Shipman, S. L., Moore, J. H., et al. (2012) · Environmental Health Perspectives · doi:10.1289/ehp.1205003 · Cited by 98 · see citing works

Squalene epoxidase as a promising metabolic target in cancer treatment

Cirmena, G., Franceschelli, P., Isnaldi, E., Ferrando, L., Mariano, M. D., Ballestrero, A., & Zoppoli, G. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.03.034 · Cited by 98 · see citing works

Inhibition of human squalene monooxygenase by tellurium compounds: evidence of interaction with vicinal sulfhydryls

Laden, B. P., & Porter, T. D. (2001) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)31684-9 · Cited by 93 · see citing works

Cholesterol-rich intracellular membranes: a precursor to the plasma membrane.

Lange, Y., & Steck, T. L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36299-3 · Cited by 88 · see citing works

Purification and properties of a soluble protein activator of rat liver squalene epoxidase.

Ferguson, J. B., & Bloch, K. E. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63359-4 · Cited by 86 · see citing works

Purification and properties of sterol carrier protein1.

Srikantaiah, M. V., Hansbury, E., Loughran, E. D., & Scallen, T. J. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33087-9 · Cited by 86 · see citing works

Production of squalene by squalene synthases and their truncated mutants in Escherichia coli

Katabami, A., Li, L., Iwasaki, M., Furubayashi, M., Saito, K., & Umeno, D. (2014) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2014.07.013 · Cited by 73 · see citing works

Biosynthesis of hydroxyfatty acid polymers

Croteau, R., & Kolattukudy, P. E. (1975) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(75)90097-1 · Cited by 69 · see citing works

Crystal Structure of the Human Supernatant Protein Factor

Stocker, A., Tomizaki, T., Schulze‐Briese, C., & Baumann, U. (2002) · Structure · doi:10.1016/s0969-2126(02)00884-5 · Cited by 66 · see citing works

Cloning of cDNAs or genes encoding enzymes of sterol biosynthesis from plants and other eukaryotes: Heterologous expression and complementation analysis of mutations for functional characterization

Bach, T. J., & Benveniste, P. (1997) · Progress in Lipid Research · doi:10.1016/s0163-7827(97)00009-x · Cited by 65 · see citing works

α-Tocopherol transfer protein (α-TTP)

Arai, H., & Kono, N. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.09.021 · Cited by 63 · see citing works

Regulation of squalene epoxidase in HepG2 cells.

Hidaka, Y., Satoh, T., & Kamei, T. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42273-4 · Cited by 63 · see citing works

Supernatant protein factor facilitates intermembrane transfer of squalene.

Friedlander, E. J., Caras, I. W., Lin, L. F., & Bloch, K. E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70602-4 · Cited by 61 · see citing works

Isolation and partial characterization of a cholesterol-requiring mutant of Chinese hamster ovary cells.

Chang, T., Telakowski-Hopkins, C. A., Heuvel, W. V., Alberts, A. W., & Vagelos, P. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.3.832 · Cited by 61 · see citing works

Hypotheses for the origin and early evolution of triterpenoid cyclases

Fischer, W. W., & Pearson, A. (2007) · Geobiology · doi:10.1111/j.1472-4669.2007.00096.x · Cited by 61 · see citing works

Sterol Metabolism

Benveniste, P. (2002) · The Arabidopsis Book · doi:10.1199/tab.0004 · Cited by 58 · see citing works

Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system

Teruo, O., Shigeru, O., Fumihiko, H., & Imai, Y. (1977) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(77)90089-3 · Cited by 58 · see citing works

Effect of a supernatant protein on microsomal squalene epoxidase and 2,3-oxidosqualene-lanosterol cyclase.

Saat, Y. A., & Bloch, K. E. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33141-1 · Cited by 57 · see citing works

Spatial compartmentalization of lipid droplet biogenesis

Henne, W. M., Goodman, J. M., & Hariri, H. H. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.07.008 · Cited by 56 · see citing works

Lipidomics for Geochemistry

Pearson, A. (2013) · Treatise on Geochemistry · doi:10.1016/b978-0-08-095975-7.01022-6 · Cited by 55 · see citing works

Enzymatic epoxidation reactions

May, S. W. (1979) · Enzyme and Microbial Technology · doi:10.1016/0141-0229(79)90005-x · Cited by 53 · see citing works

New directions in the chemistry of natural products: The organic chemist as a pathfinder for biochemistry and medicine

Witkop, B. (1971) · Cellular and Molecular Life Sciences · doi:10.1007/bf02286882 · Cited by 53 · see citing works

Purification and partial characterization of squalene epoxidase from rat liver microsomes

Ono, T., Nakazono, K., & KOSAKA, H. (1982) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(82)90424-1 · Cited by 53 · see citing works

Effects of a supernatant protein activator on microsomal squalene-2,3-oxide-lanosterol cyclase.

Caras, I. W., & Bloch, K. E. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86390-1 · Cited by 49 · see citing works

Cytochrome P450 17α Hydroxylase/17,20 Lyase (CYP17) Function in Cholesterol Biosynthesis: Identification of Squalene Monooxygenase (Epoxidase) Activity Associated with CYP17 in Leydig Cells

Liu, Y., Yao, Z., & Papadopoulos, V. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0271 · Cited by 48 · see citing works

Mammalian cell mutant requiring cholesterol and unsaturated fatty acid for growth.

Limanek, J. S., Chin, J., & Chang, T. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.11.5452 · Cited by 48 · see citing works

Squalene monooxygenase – a target for hypercholesterolemic therapy

Belter, A., Skupińska, M., Giel-Pietraszuk, M., Grabarkiewicz, T., Rychlewski, L., & Barciszewski, J. (2011) · Biological Chemistry · doi:10.1515/bc.2011.195 · Cited by 46 · see citing works

Purification and characterization of recombinant squalene epoxidase

Nagumo, A., Kamei, T., Sakakibara, J., & Ono, T. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39736-4 · Cited by 46 · see citing works

Structural effects on the reactivity of substrates and inhibitors in the epoxidation system of Pseudomonas oleovorans

May, S. W., Schwartz, R. D., Abbott, B. J., & Zaborsky, O. R. (1975) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(75)90026-1 · Cited by 46 · see citing works

Squalene epoxidase as the target of antifungal allylamines

Ryder, N. S. (1987) · Pesticide Science · doi:10.1002/ps.2780210405 · Cited by 44 · see citing works

Intermembrane transfer of 5 alpha-cholest-7-en-3 beta-ol. Facilitation by supernatant protein (SCP).

Ishibashi, T., & Bloch, K. E. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42990-0 · Cited by 44 · see citing works

Isoprenoid Metabolism

Bramley, P. M. (1997) · Elsevier eBooks · doi:10.1016/b978-012214674-9/50012-6 · Cited by 42 · see citing works

Supernatant protein factor and tocopherol-associated protein: an unexpected link between cholesterol synthesis and vitamin E (review)

Porter, T. D. (2003) · The Journal of Nutritional Biochemistry · doi:10.1016/s0955-2863(02)00262-0 · Cited by 40 · see citing works

Properties of a particulate squalene epoxidase from Candida albicans

Ryder, N. S., & Dupont, M.-C. (1984) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(84)90013-4 · Cited by 40 · see citing works

Squalene mono-oxygenase, a key enzyme in cholesterol synthesis, is stabilized by unsaturated fatty acids

Stevenson, J., Luu, W., Kristiana, I., & Brown, A. J. (2014) · Biochemical Journal · doi:10.1042/bj20131404 · Cited by 39 · see citing works

Squalene Epoxidase and Oxidosqualene : Lanosterol Cyclase—Key Enzymes in Cholesterol Biosynthesis

Abe, I., & Prestwich, G. D. (1999) · Elsevier eBooks · doi:10.1016/b978-0-08-091283-7.00045-x · Cited by 39 · see citing works

Yeast mutant requiring only a sterol as growth supplement

Karst, F., & Lacroute, F. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80216-0 · Cited by 37 · see citing works

Regulation of squalene epoxidase activity in rat liver.

Satoh, T., Hidaka, Y., & Kamei, T. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42274-6 · Cited by 34 · see citing works

Microsomal Enzymes of Sterol Biosynthesis

Gaylor, J. L. (1972) · Advances in lipid research · doi:10.1016/b978-0-12-024910-7.50010-5 · Cited by 34 · see citing works

Purification of squalene epoxidase from rat liver microsomes

Ono, T., Takahashi, K., Odani, S., Konno, H., & Imai, Y. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)91245-0 · Cited by 33 · see citing works

Hypolipidemic effects of NB-598 in dogs

Horie, M., Sawasaki, Y., Fukuzumi, H., Watanabe, K., Iizuka, Y., Tsuchiya, Y., & Kamei, T. (1991) · Atherosclerosis · doi:10.1016/0021-9150(91)90080-m · Cited by 31 · see citing works

Effects of Historical Differences in Components of the Japanese Diet on the Risk of Obesity in Mice

Kitano, Y., Honma, T., Hatakeyama, Y., Jibu, Y., Kawakami, Y., Tsuduki, T., Nakagawa, K., & Miyazawa, T. (2014) · Nippon Eiyo Shokuryo Gakkaishi · doi:10.4327/jsnfs.67.73 · Cited by 29 · see citing works

Differential Inhibition of Fungal and Mammalian Squalene Epoxidases by the Benzylamine SDZ SBA 586 in Comparison with the Allylamine Terbinafine

Favre, B., & Ryder, N. S. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9908 · Cited by 28 · see citing works

Inhibition and activation of porcine squalene epoxidase

Bai, M., & Prestwich, G. D. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90400-q · Cited by 28 · see citing works

Altered Sensitivities to Potential Inhibitors of Cholesterol Biosynthesis in Niemann-Pick Type C Fibroblasts.

Ohno, K., Nanba, E., Nakano, T., Inui, K., Okada, S., & Takeshita, K. (1993) · Cell Structure and Function · doi:10.1247/csf.18.231 · Cited by 28 · see citing works

OXYGENASES IN FATTY ACID AND STEROID METABOLISM

Hámberg, M., Samuelsson, B. O., Björkhem, I., & Danielsson, H. (1974) · Elsevier eBooks · doi:10.1016/b978-0-12-333640-8.50007-1 · Cited by 28 · see citing works

Mammalian lipid droplets: structural, pathological, immunological and anti-toxicological roles

Hammoudeh, N., Soukkarieh, C., Murphy, D. J., & Hanano, A. (2023) · Progress in Lipid Research · doi:10.1016/j.plipres.2023.101233 · Cited by 27 · see citing works

Squalene epoxidase and oxidosqualene lanosterol-cyclase activities in cholesterogenic and non-cholesterogenic tissues

Astruc, M., Tabacik, C., Descomps, B., & de Paulet, A. C. (1977) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(77)90056-x · Cited by 27 · see citing works

The stereospecificity of biosynthesis of squalene and β-amyrin in Pisum sativum

Suga, T., & Shishibori, T. (1975) · Phytochemistry · doi:10.1016/0031-9422(75)80355-4 · Cited by 26 · see citing works

BIOCHEMISTRY OF THE VIOLAXANTHIN CYCLE IN HIGHER PLANTS

Yamamoto, H. Y. (1979) · Elsevier eBooks · doi:10.1016/b978-0-08-022359-9.50017-5 · Cited by 26 · see citing works

Role of supernatant protein factor and anionic phospholipid in squalene uptake and conversion by microsomes.

Chin, J., & Bloch, K. E. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)71272-x · Cited by 25 · see citing works

In vitro assay of squalene epoxidase of Saccharomyces cerevisiae

M'Baya, B., & Karst, F. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90967-3 · Cited by 25 · see citing works

[43] Squalene epoxidase from rat liver microsomes

Ono, T., & Imai, Y. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(85)10096-0 · Cited by 25 · see citing works

Structural insights on cholesterol endosynthesis: Binding of squalene and 2,3-oxidosqualene to supernatant protein factor

Christen, M., Marcaida, M. J., Lamprakis, C., Aeschimann, W., Vaithilingam, J., Schneider, P., Hilbert, M., Schneider, G., Cascella, M., & Stocker, A. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.05.001 · Cited by 24 · see citing works

Squalene Epoxidase — Enzymology and Inhibition

Ryder, N. S. (1990) · Springer eBooks · doi:10.1007/978-3-642-74215-6_13 · Cited by 24 · see citing works

Characterization of native sterol carrier protein

Scallen, T. J., Srikantaiah, M. V., Skrdlant, H. B., & Hansbury, E. (1972) · FEBS Letters · doi:10.1016/0014-5793(72)80491-5 · Cited by 24 · see citing works

Protein-facilitated intermembrane transfer of squalene. Demonstration by density gradient centrifugation.

Kojima, Y., Friedlander, E. J., & Bloch, K. E. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68952-0 · Cited by 23 · see citing works

Effect of triparanol and 3β-(β-dimethyl-aminoethoxy)-androst-5-en-17-one on growth and non-saponifiable lipids of saccharomyces cerevisiae

Fung, B., & Holmlund, C. E. (1976) · Biochemical Pharmacology · doi:10.1016/0006-2952(76)90086-1 · Cited by 23 · see citing works

Components of Sterol Biosynthesis Assembled on the Oxygen-Avid Hemoglobin of Ascaris

Sherman, D. R., Guinn, B., Perdok, M. M., & Goldberg, D. E. (1992) · Science · doi:10.1126/science.1470914 · Cited by 22 · see citing works

Repeated administration of diphenyl ditelluride induces hematological disorders in rats

Borges, V. C., da Rocha, J. B. T., Savegnago, L., & Nogueira, C. W. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.02.022 · Cited by 21 · see citing works

Photoaffinity Labeling and Site-Directed Mutagenesis of Rat Squalene Epoxidase

Lee, H.-K., Denner-Ancona, P., Sakakibara, J., Ono, T., & Prestwich, G. D. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1966 · Cited by 21 · see citing works

The roles of soluble factors in squalene epoxidation by rat liver microsomes

Nakamura, M., & Sato, R. (1979) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(79)91863-1 · Cited by 21 · see citing works

Intermediates in Drug Metabolism Reactions

Hucker, H. B. (1974) · Drug Metabolism Reviews · doi:10.3109/03602537409030004 · Cited by 21 · see citing works

Photoaffinity labeling identifies the substrate-binding site of mammalian squalene epoxidase

Lee, H.-K., Zheng, Y., Xiao, X.-Y., Bai, M., Sakakibara, J., Ono, T., & Prestwich, G. D. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.01.012 · Cited by 20 · see citing works

Metabolism in vitro of sulindac. Sulfoxide-reducing enzyme systems in guinea pig liver.

Kitamura, S., Tatsumi, K., & Yoshimura, H. (1980) · Journal of Pharmacobio-Dynamics · doi:10.1248/bpb1978.3.290 · Cited by 20 · see citing works

Squalene Epoxidase of Rat Liver

Tai, H., & Bloch, K. E. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45101-6 · Cited by 110 · see citing works

ChemInform Abstract: Epoxidation of 6,7‐ and 10,11‐Oxidosqualenes by the Squalene Epoxidase Present in Rat Liver Microsomes.

Abad, J. L., Casas, J., Abián, J., & Messeguer, Á. (1994) · ChemInform · doi:10.1002/chin.199427033

Epoxidation of squalene by rat liver microsomes

中村, 正. (1979)

[43] Squalene epoxidase from rat liver microsomes

Ono, T., & Imai, Y. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(85)10096-0 · Cited by 25 · see citing works

Solubilization and partial characterization of rat liver squalene epoxidase

Ono, T., & Bloch, K. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41847-4 · Cited by 157 · see citing works