{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T12:47:02Z","timestamp":1792154822671,"version":"4.4.0"},"reference-count":177,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,6,1]],"date-time":"2021-06-01T00:00:00Z","timestamp":1622505600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical Pharmacology"],"published-print":{"date-parts":[[2022,2]]},"DOI":"10.1016\/j.bcp.2021.114611","type":"journal-article","created":{"date-parts":[[2021,5,16]],"date-time":"2021-05-16T17:39:53Z","timestamp":1621186793000},"page":"114611","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":14,"special_numbering":"C","title":["Unearthing the Janus-face cholesterogenesis pathways in cancer"],"prefix":"10.1016","volume":"196","author":[{"given":"Babita","family":"Madan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David M.","family":"Virshup","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"W. David","family":"Nes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David J.","family":"Leaver","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bcp.2021.114611_b0005","series-title":"Lipids in Evolution","first-page":"245","author":"Nes","year":"1980"},{"key":"10.1016\/j.bcp.2021.114611_b0010","doi-asserted-by":"crossref","first-page":"2548","DOI":"10.1093\/molbev\/msz167","article-title":"Evolution of cholesterol biosynthesis pathway in animals","volume":"36","author":"Zhang","year":"2019","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.bcp.2021.114611_b0015","first-page":"2179","article-title":"Cholesterol as an evolutionary response to living with oxygen","volume":"64","author":"Brown","year":"2010","journal-title":"Evolution"},{"key":"10.1016\/j.bcp.2021.114611_b0020","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1146\/annurev.nu.12.070192.002135","article-title":"Serum cholesterol and cancer risk: an epidemiologic perspective","volume":"12","author":"Kritchevsky","year":"1992","journal-title":"Annu. Rev. Nutr."},{"key":"10.1016\/j.bcp.2021.114611_b0025","doi-asserted-by":"crossref","first-page":"5884","DOI":"10.1073\/pnas.1802930115","article-title":"C4-Demethylation enzymes distinguish bacterial and eukaryotic sterol synthesis","volume":"115","author":"Lee","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.bcp.2021.114611_b0030","series-title":"Biochemistry of Steroids and Other Isopentenoids","first-page":"690","author":"Nes","year":"1977"},{"key":"10.1016\/j.bcp.2021.114611_b0035","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1194\/jlr.RA119000317","article-title":"A nematode sterol C4\u03b1-methyltransferase catalyzes a new methylation reaction responsible for sterol diversity","volume":"61","author":"Zhou","year":"2020","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bcp.2021.114611_b0040","series-title":"Lipids: Chemistry, Biochemistry and Nutrition","first-page":"295","article-title":"Biosynthesis of cholesterol and related substances","author":"Popjak","year":"1986"},{"key":"10.1016\/j.bcp.2021.114611_b0045","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/s12154-008-0010-6","article-title":"Sterol and membrane dynamics","volume":"1","author":"Dufourc","year":"2008","journal-title":"J. Chem. Biol."},{"key":"10.1016\/j.bcp.2021.114611_b0050","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1172\/JCI0216390","article-title":"Cholesterol, lipid rafts and disease","volume":"110","author":"Simons","year":"2002","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bcp.2021.114611_b0055","doi-asserted-by":"crossref","first-page":"6218","DOI":"10.1016\/S0021-9258(17)34602-1","article-title":"The functional importance of structural features of ergosterol in yeast","volume":"253","author":"Nes","year":"1978","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0060","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1006\/abbi.1993.1100","article-title":"The structural requirements of sterols for membrane function in Saccharomyces cerevisiae","volume":"300","author":"Nes","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bcp.2021.114611_b0065","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/0039-128X(89)90033-0","article-title":"Studies of the oxysterol inhibition of tumor cell growth","volume":"53","author":"Parish","year":"1989","journal-title":"Steroids"},{"key":"10.1016\/j.bcp.2021.114611_b0070","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/s42255-020-0174-0","article-title":"Cholesterol metabolism in cancer: mechanisms and therapeutic opportunities","volume":"2","author":"Huang","year":"2020","journal-title":"Nat. Metab."},{"key":"10.1016\/j.bcp.2021.114611_b0075","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/j.cmet.2015.01.004","article-title":"Identification of natural ROR\u03b3 ligands that regulate the development of lymphoid cells","volume":"21","author":"Santori","year":"2015","journal-title":"Cell Metab."},{"key":"10.1016\/j.bcp.2021.114611_b0080","article-title":"Neuro-oxysterols and neuro-sterols as ligands to nuclear receptors, GPCRs, ligand-gated ion channels and other protein receptors","author":"Wang","year":"2020","journal-title":"Br. J. Pharmacol. In Press"},{"key":"10.1016\/j.bcp.2021.114611_b0085","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.bcp.2013.02.029","article-title":"Oxysterols in cancer cell proliferation and death","volume":"86","author":"de Weille","year":"2013","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.bcp.2021.114611_b0090","doi-asserted-by":"crossref","first-page":"1","DOI":"10.11131\/2015\/101154","article-title":"LXR Inhibits Proliferation of Human Breast Cancer Cells through the PI3K-Akt Pathway","volume":"2","author":"Hassan","year":"2015","journal-title":"Nucl. Receptor Res."},{"key":"10.1016\/j.bcp.2021.114611_b0095","doi-asserted-by":"crossref","unstructured":"L. Vedin, S. A. Lewandowski, P. Parini, J. Gustafsson, K. R.Steffensen, The oxysterol receptor LXR inhibits proliferation of human breast cancer cells, Carcinogenesis 30 (2009) 575\u2013579.","DOI":"10.1093\/carcin\/bgp029"},{"key":"10.1016\/j.bcp.2021.114611_b0100","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.1126\/science.1252787","article-title":"Cholesterol, cancer, in the balance","volume":"28","author":"Silvente-Poirot","year":"2014","journal-title":"Science"},{"key":"10.1016\/j.bcp.2021.114611_b0105","doi-asserted-by":"crossref","first-page":"828","DOI":"10.3390\/cells9040828","article-title":"Cholesterol homeostasis modulates platinum sensitivity in human ovarian cancer","volume":"30","author":"Criscuolo","year":"2020","journal-title":"Cells"},{"key":"10.1016\/j.bcp.2021.114611_b0110","doi-asserted-by":"crossref","first-page":"4393","DOI":"10.1038\/ncomms5393","article-title":"Cholesterol selectively activates canonical Wnt signalling over non-canonical Wnt signalling","volume":"5","author":"Sheng","year":"2015","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0115","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1158\/1078-0432.CCR-17-2923","article-title":"Statins Synergize with Hedgehog Pathway Inhibitors for Treatment of Medulloblastoma","volume":"24","author":"Gordon","year":"2018","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.bcp.2021.114611_b0120","doi-asserted-by":"crossref","unstructured":"M. Kinnebrew, E. J. Iverson, B. B. Patel, G. V. Pusapati, J. H. Kong, K. A. Johnson, G. Luchetti, K. M. Eckert, J. G. McDonald, D. F. Covey, C. Siebold, A. Radhakrishnan, R. Rohatgi, Cholesterol accessibility at the ciliary membrane controls hedgehog signaling, eLife 8 (2019) e50051.","DOI":"10.7554\/eLife.50051"},{"key":"10.1016\/j.bcp.2021.114611_b0125","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/s41586-020-2295-8","article-title":"Structure of nevanimibe-bound tetrameric human ACAT1","volume":"581","author":"Long","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.bcp.2021.114611_b0130","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1126\/science.150.3692.19","article-title":"The biological synthesis of cholesterol","volume":"150","author":"Bloch","year":"1965","journal-title":"Science"},{"key":"10.1016\/j.bcp.2021.114611_b0135","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1016\/S0021-9258(18)64608-3","article-title":"Preputial gland tumor sterols. 3. A metabolic pathway from lanosterol to cholesterol","volume":"235","author":"Kandutsch","year":"1960","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0140","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1042\/bj3260609","article-title":"Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol \u039424-reductase","volume":"326","author":"Bae","year":"1997","journal-title":"Biochem. J."},{"key":"10.1016\/j.bcp.2021.114611_b0145","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1098\/rspb.1987.0074","article-title":"Effects of 2,3-iminosqualene on cultured cells","volume":"232","author":"Popjak","year":"1987","journal-title":"Proc. Royal Soc. Lond. B."},{"key":"10.1016\/j.bcp.2021.114611_b0150","doi-asserted-by":"crossref","first-page":"6230","DOI":"10.1016\/S0021-9258(18)83338-5","article-title":"Inhibition of cholesterol synthesis by cell growth by 24(R, S)-iminolanosterol and triparinol in cultured rat hepatoma cells","volume":"264","author":"Popjak","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0155","doi-asserted-by":"crossref","unstructured":"M. M. Mitsche, J. G. McDonald, H. H. Hobbs, J. C. Cohen, Flux analysis of cholesterol biosynthesis in vivo reveals multiple tissue and cell-type specific pathways, eLife (2015) e07999.","DOI":"10.7554\/eLife.07999.016"},{"key":"10.1016\/j.bcp.2021.114611_b0160","doi-asserted-by":"crossref","first-page":"5483","DOI":"10.1021\/acs.biochem.6b00342","article-title":"Cholesterol biosynthesis: A mechanistic overview","volume":"55","author":"Nuno","year":"2016","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2021.114611_b0165","doi-asserted-by":"crossref","first-page":"6423","DOI":"10.1021\/cr200021m","article-title":"Biosynthesis of cholesterol and other sterols","volume":"111","author":"Nes","year":"2011","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bcp.2021.114611_b0170","unstructured":"L. J. Gaylor, Formation of sterols in animals. In Biosynthesis of Isoprenoid Compounds. Vol. 1 (J. W. Porter and S. L. Spurgeon, Eds). Wiley, New York (1981) pp. 410-441."},{"key":"10.1016\/j.bcp.2021.114611_b0175","doi-asserted-by":"crossref","first-page":"2063","DOI":"10.1158\/0008-5472.CAN-15-2613","article-title":"The role of cholesterol in cancer","volume":"76","author":"Kuzu","year":"2016","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2021.114611_b0180","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.biochi.2018.04.023","article-title":"Importance of genetic background of oxysterol signaling in cancer","volume":"153","author":"Holy","year":"2018","journal-title":"Biochimie"},{"key":"10.1016\/j.bcp.2021.114611_b0185","doi-asserted-by":"crossref","unstructured":"W. D. Nes, W. Zhou, A. L. Dennis, H. Li, R. A. Keith, T. M. Piser, S. T. Furlong, Purification, Characterization, and Catalytic Properties of Human Sterol 8-Isomerase, Biochem. J. 367 (2002) 587-599.","DOI":"10.1042\/bj20020551"},{"key":"10.1016\/j.bcp.2021.114611_b0190","doi-asserted-by":"crossref","first-page":"26838","DOI":"10.1074\/jbc.M111.237099","article-title":"Substrate preferences and catalytic parameters determined by structural characteristics of sterol 14\u03b1-Demethylase CYP51 from Leishmania infantum","volume":"286","author":"Hargrove","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0195","doi-asserted-by":"crossref","first-page":"7150","DOI":"10.1073\/pnas.1915923117","article-title":"A key mammalian cholesterol synthesis enzyme, squalene monooxygenase, is allosterically stabilized by its substrate","volume":"117","author":"Yoshioka","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bcp.2021.114611_b0200","doi-asserted-by":"crossref","first-page":"17549","DOI":"10.1074\/jbc.REV120.010723","article-title":"Post-translational control of the long and winding road to cholesterol","volume":"295","author":"Sharpe","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0205","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1126\/science.3513311","article-title":"A receptor-mediated pathway for cholesterol homeostasis","volume":"232","author":"Brown","year":"1986","journal-title":"Science"},{"key":"10.1016\/j.bcp.2021.114611_b0210","first-page":"283","article-title":"Control of sterol biosynthesis and its importance to developmental regulation and evolution","volume":"24","author":"Nes","year":"1990","journal-title":"Rec. Adv. Phytochem."},{"key":"10.1016\/j.bcp.2021.114611_b0215","doi-asserted-by":"crossref","first-page":"3628","DOI":"10.1182\/blood-2002-07-2283","article-title":"Cholesterol-modulating agents kill acute myeloid leukemia cells and sensitize them to therapeutics by blocking adaptive cholesterol responses","volume":"101","author":"Li","year":"2003","journal-title":"Blood"},{"key":"10.1016\/j.bcp.2021.114611_b0220","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1007\/s10863-020-09846-4","article-title":"Lipid composition of the cancer cell membrane","volume":"52","author":"Szlasa","year":"2020","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.bcp.2021.114611_b0225","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1158\/2159-8290.CD-12-0031","article-title":"Targeting C4-demethylating genes in the cancer cholesterol pathway sensitizes cancer cells to EGF receptor inhibitors via increased EGF receptor degradation","volume":"3","author":"Sukhanova","year":"2012","journal-title":"Cancer Discov."},{"key":"10.1016\/j.bcp.2021.114611_b0230","doi-asserted-by":"crossref","first-page":"1673","DOI":"10.1038\/s41416-020-01085-z","article-title":"Genkwadaphnin inhibits growth and invasion in hepatocellular carcinoma by blocking DHCR24-mediated cholesterol biosynthesis and lipid rafts formation","volume":"123","author":"Wu","year":"2020","journal-title":"Brit. J. Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0235","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.canlet.2020.07.010","article-title":"Sterol synthesis pathway inhibition as a target for cancer treatment","volume":"493","author":"Feltrin","year":"2020","journal-title":"Cancer Lett."},{"key":"10.1016\/j.bcp.2021.114611_b0240","article-title":"Role of cholesterol metabolism in the anticancer pharmacology of selective estrogen receptor modulators","author":"G\u00f3mez-Coronado","year":"2020","journal-title":"Semin. Cancer Biol. In Press"},{"key":"10.1016\/j.bcp.2021.114611_b0245","doi-asserted-by":"crossref","first-page":"4305","DOI":"10.1021\/bi6026192","article-title":"Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function","volume":"46","author":"Haapalainen","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2021.114611_b0250","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.jmb.2010.03.034","article-title":"Crystal structures of human HMG-CoA synthase isoforms provide insights into inherited ketogenesis disorders and inhibitor design","volume":"398","author":"Shafqat","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bcp.2021.114611_b0255","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1126\/science.1059344","article-title":"Structural mechanism for statin inhibition of HMG-CoA reductase","volume":"292","author":"Istvan","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.bcp.2021.114611_b0260","doi-asserted-by":"crossref","first-page":"3715","DOI":"10.1021\/bi7024386","article-title":"Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism","volume":"47","author":"Fu","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bcp.2021.114611_b0265","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1002\/prot.22151","article-title":"Crystal structure of human phosphomavelonate kinase at 1.8 \u00c5 resolution","volume":"73","author":"Chang","year":"2008","journal-title":"Proteins Struct. Funct. Bioinform."},{"key":"10.1016\/j.bcp.2021.114611_b0270","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.abb.2008.08.024","article-title":"Human mevalonate diphosphate decarboxylase: Characterization, investigation of the mevalonate diphosphate binding site, and crystal structure","volume":"480","author":"Voynova","year":"2008","journal-title":"Arch. Biochem Biophys."},{"key":"10.1016\/j.bcp.2021.114611_b0275","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1016\/j.jmb.2006.12.055","article-title":"The crystal structure of human isopentenyl diphosphate isomerase at 1.7 \u00c5 resolution reveals its catalytic mechanism in isoprenoid biosynthesis","volume":"366","author":"Zheng","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bcp.2021.114611_b0280","doi-asserted-by":"crossref","first-page":"3201","DOI":"10.1021\/jm201657x","article-title":"Design and synthesis of active site inhibitors of the human farnesyl pyrophosphate synthase: apoptosis and inhibition of ERK phosphorylation in multiple myeloma cells","volume":"55","author":"Lin","year":"2012","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0285","first-page":"E2530","article-title":"Eric oldfield, taxodione and arenarone inhibit farnesyl diphosphate synthase by binding to the isopentenyl diphosphate site","volume":"111","author":"Liu","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.bcp.2021.114611_b0290","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1021\/ml500528x","article-title":"Farnesyl Diphosphate Synthase Inhibitors With Unique Ligand-Binding Geometries","volume":"6","author":"Liu","year":"2015","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.bcp.2021.114611_b0295","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1107\/S2053230X14002106","article-title":"Structure of human farnesyl pyrophosphate synthase in complex with an aminopyridine bisphosphonate and two molecules of inorganic phosphate","volume":"70","author":"Park","year":"2014","journal-title":"Acta Cryst. F"},{"key":"10.1016\/j.bcp.2021.114611_b0300","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/nchembio.421","article-title":"Allosteric non-bisphosphonate inhibitors identified by fragment-based discovery","volume":"6","author":"Jahnke","year":"2010","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bcp.2021.114611_b0305","doi-asserted-by":"crossref","first-page":"30610","DOI":"10.1074\/jbc.M004132200","article-title":"Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis","volume":"275","author":"Pandit","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0310","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1038\/s41467-018-07928-x","article-title":"Structure and inhibition mechanism of the catalytic domain of human squalene epoxidase","volume":"10","author":"Padyana","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0315","doi-asserted-by":"crossref","first-page":"18707","DOI":"10.1074\/jbc.R113.479808","article-title":"Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoAreductase (HMGCR)","volume":"288","author":"Sharpe","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0320","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.abb.2013.12.005","article-title":"Flavin dependent monooxygenases","volume":"544","author":"Huijbers","year":"2014","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bcp.2021.114611_b0325","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.cmet.2011.01.015","article-title":"Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase","volume":"13","author":"Gill","year":"2011","journal-title":"Cell Metab."},{"key":"10.1016\/j.bcp.2021.114611_b0330","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1042\/BJ20131404","article-title":"Squalene mono-oxygenase, a key enzyme in cholesterol synthesis, is stabilized by unsaturated fatty acids","volume":"461","author":"Stevenson","year":"2014","journal-title":"Biochem. J."},{"key":"10.1016\/j.bcp.2021.114611_b0335","article-title":"The E3 ubiquitin ligase MARCHF6 as a metabolic integrator in cholesterol synthesis and beyond","volume":"1866","author":"Scott","year":"2021","journal-title":"Biochim. Biophys. Acta. Mol. Cell Biol. Lipids"},{"key":"10.1016\/j.bcp.2021.114611_b0340","doi-asserted-by":"crossref","first-page":"888","DOI":"10.1038\/s41467-019-08866-y","article-title":"The shape of human squalene epoxidase expands the arsenal against cancer","volume":"10","author":"Brown","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0345","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/S0021-9258(19)69921-7","article-title":"Biosynthesis of 24,25-epoxycholesterol from squalene 2,3;22,23-dioxide","volume":"256","author":"Nelson","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0350","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.bbrc.2004.01.052","article-title":"The monotopic membrane protein human oxidosqualene cyclase is active as monomer","volume":"315","author":"Ruf","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0355","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1038\/nature02993","article-title":"Insight into steroid scaffold formation from the structure of human oxidosqualene cyclase","volume":"432","author":"Thoma","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.bcp.2021.114611_b0360","doi-asserted-by":"crossref","first-page":"2452","DOI":"10.1038\/s41467-019-10279-w","article-title":"Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition","volume":"10","author":"Long","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0365","unstructured":"E. J. Pavlik, K. Nelson, S. Srinivasan, D. E. Powell, D. E. Kenady, P. D. DePriest, H. H. Gallion, J. R. van Nagell Jr., Resistance to tamoxifen with persisting sensitivity to estrogen: possible mediation by excessive antiestrogen binding site activity, Cancer Res. 52 (1992) 4106\u20134112."},{"key":"10.1016\/j.bcp.2021.114611_b0370","doi-asserted-by":"crossref","first-page":"13520","DOI":"10.1073\/pnas.1002922107","article-title":"Identification and pharmacological characterization of cholesterol-5,6-epoxide hydrolase as a target for tamoxifen and AEBS ligands","volume":"107","author":"de Medina","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bcp.2021.114611_b0375","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1194\/jlr.M069229","article-title":"Human sterol 14-demethylase as a target for anticancer chemotherapy: towards structure-aided drug design","volume":"57","author":"Hargrove","year":"2016","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bcp.2021.114611_b0380","doi-asserted-by":"crossref","first-page":"1753","DOI":"10.3390\/molecules23071753","article-title":"Synthesis and biological activity of sterol 14 \u03b1-demethylase and sterol C24-methyltransferase inhibitors","volume":"23","author":"Leaver","year":"2018","journal-title":"Molecules"},{"key":"10.1016\/j.bcp.2021.114611_b0385","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1021\/jo00003a059","article-title":"Assessment of the active-site requirements of lanosterol 14-demethylase: evaluation of novel substrate analogues as competitive inhibitors","volume":"56","author":"Tuck","year":"1991","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0390","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1021\/jm00055a012","article-title":"32-methyl-32-oxylanosterols: dual-action inhibitors of cholesterol biosynthesis","volume":"36","author":"Frye","year":"1993","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0395","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1194\/jlr.M021865","article-title":"Structural complex of sterol 14 \u03b1-demethylase (CYP51) with 14 \u03b1-methylenecyclopropyl-7-24,25-dihydrolanosterol","volume":"53","author":"Hargrove","year":"2012","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bcp.2021.114611_b0400","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/j.jmb.2010.01.075","article-title":"Structural basis of human CYP51 inhibition by antifungal azoles","volume":"397","author":"Strushkevich","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bcp.2021.114611_b0405","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/j.ccell.2020.08.015","article-title":"Cholesterol pathway inhibition induces TGF-\u03b2 signaling to promote basal differentiation in pancreatic cancer","volume":"38","author":"Gabitova-Cornell","year":"2020","journal-title":"Cancer Cell"},{"key":"10.1016\/j.bcp.2021.114611_b0410","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1111\/j.1365-2133.1992.tb00001.x","article-title":"Terbinafine: mode of action and properties of the squalene epoxidase inhibition","volume":"126","author":"Ryder","year":"1992","journal-title":"Br. J. Dermatol."},{"key":"10.1016\/j.bcp.2021.114611_b0415","doi-asserted-by":"crossref","first-page":"19435","DOI":"10.1038\/srep19435","article-title":"Squalene epoxidase is a bona fide oncogene by amplification with clinical relevance in breast cancer","volume":"6","author":"Brown","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bcp.2021.114611_b0420","doi-asserted-by":"crossref","first-page":"18075","DOI":"10.1016\/S0021-9258(17)44716-8","article-title":"NB-598: a potent competitive inhibitor of squalene epoxidase","volume":"265","author":"Horie","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0425","doi-asserted-by":"crossref","first-page":"3207","DOI":"10.1021\/jm00017a004","article-title":"(Aryloxy)methylsilane derivatives as new cholesterol biosynthesis inhibitors: synthesis and hypocholesterolemic activity of a new class of squalene epoxidase inhibitors","volume":"38","author":"Gotteland","year":"1995","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0430","doi-asserted-by":"crossref","first-page":"2797","DOI":"10.1021\/ja00987a089","article-title":"2,3-Iminosqualene, a potent inhibitor of the enzymic cyclization of 2,3-oxidosqualene to sterols","volume":"89","author":"Corey","year":"1967","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bcp.2021.114611_b0435","doi-asserted-by":"crossref","first-page":"1727","DOI":"10.3892\/or.2014.3332","article-title":"Cholesterol synthesis inhibitor RO 48\u20138071 suppresses transcriptional activity of human estrogen and androgen receptor","volume":"32","author":"Mafuvadze","year":"2014","journal-title":"Oncol. Rep."},{"key":"10.1016\/j.bcp.2021.114611_b0440","doi-asserted-by":"crossref","first-page":"4990","DOI":"10.1021\/jm300256z","article-title":"Cytotoxic effects of combination of oxidosqualene cyclase inhibitors with atorvastatin in human cancer cells","volume":"55","author":"Staedler","year":"2012","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0445","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1007\/s10549-014-2996-5","article-title":"Cholesterol biosynthesis inhibitors as potent novel anti-cancer agents: suppression of hormone-dependent breast cancer by the oxidosqualene cyclase inhibitor RO 48\u20138071","volume":"146","author":"Liang","year":"2014","journal-title":"Breast Cancer Res. Treat."},{"key":"10.1016\/j.bcp.2021.114611_b0450","doi-asserted-by":"crossref","first-page":"487","DOI":"10.2147\/BCTT.S140265","article-title":"Cholesterol biosynthesis inhibitor RO 48\u20138071 reduces progesterone receptor expression and inhibits progestin-dependent stem cell-like cell growth in hormone-dependent human breast cancer cells","volume":"9","author":"Liang","year":"2017","journal-title":"Breast Cancer-Targets Ther."},{"key":"10.1016\/j.bcp.2021.114611_b0455","first-page":"3223","article-title":"Cholesterol biosynthesis inhibitor RO 48\u20138071 suppresses growth of hormone-dependent and castration-resistant prostate cancer cells","volume":"9","author":"Lian","year":"2016","journal-title":"OncoTargets and Therapy"},{"key":"10.1016\/j.bcp.2021.114611_b0460","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/s11745-009-3305-7","article-title":"Cholesterol synthesis inhibitor U18666A and the role of sterol metabolism and trafficking in numerous pathophysiological processes","volume":"44","author":"Cenedella","year":"2009","journal-title":"Lipids"},{"key":"10.1016\/j.bcp.2021.114611_b0465","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1038\/bjc.2017.200","article-title":"Modulating cancer cell survival by targeting intracellular cholesterol transport","volume":"117","author":"Kuzu","year":"2017","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0470","doi-asserted-by":"crossref","unstructured":"F. Lu, Q. Liang, L. Abi-Mosleh, A. Das, J. K. De Brabander, J. L. Goldstein, M. S. Brown, Identification of NPC1 as the target of U18666A, an inhibitor of lysosomal cholesterol export and Ebola infection, eLife 4 (2015) e12177.","DOI":"10.7554\/eLife.12177"},{"key":"10.1016\/j.bcp.2021.114611_b0475","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1111\/febs.12119","article-title":"Purification, kinetics, inhibitors and CD for recombinant \u03b2-amyrin synthase from Euphorbia tirucalli L and functional analysis of the DCTA motif, which is highly conserved among oxidosqualene cyclases","volume":"280","author":"Ito","year":"2013","journal-title":"FEBS J."},{"key":"10.1016\/j.bcp.2021.114611_b0480","doi-asserted-by":"crossref","first-page":"34048","DOI":"10.1074\/jbc.M405230200","article-title":"Molecular characterization of the microsomal tamoxifen binding site","volume":"279","author":"Kedjouar","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0485","doi-asserted-by":"crossref","first-page":"20070","DOI":"10.1016\/S0021-9258(18)54892-4","article-title":"Effects of a novel lanosterol 14\u03b1-demethylase inhibitor on the regulation of 3-hydroxy-3-methylglutaryl-coenzyme a reductase in hep G2 cells","volume":"266","author":"Mayer","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0490","doi-asserted-by":"crossref","first-page":"3379","DOI":"10.1158\/0008-5472.CAN-06-4093","article-title":"Cholesterol starvation induces differentiation of human leukemia HL-60 cells","volume":"67","author":"S\u00e1nchez-Mart\u00edn","year":"2007","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2021.114611_b0495","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1194\/jlr.M400407-JLR200","article-title":"Effects of distal cholesterol biosynthesis inhibitors on cell proliferation and cell cycle progression","volume":"46","author":"Fern\u00e1ndez","year":"2005","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bcp.2021.114611_b0500","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1002\/pros.21447","article-title":"Contemporary experience with ketoconazole in patients with metastatic castration-resistant prostate cancer: clinical factors associated with PSA response and disease progression","volume":"72","author":"Keizman","year":"2012","journal-title":"Prostate"},{"key":"10.1016\/j.bcp.2021.114611_b0505","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1038\/nrd1031","article-title":"Tamoxifen: a most unlikely pioneering medicine","volume":"2","author":"Jordan","year":"2003","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bcp.2021.114611_b0510","doi-asserted-by":"crossref","first-page":"1270S","DOI":"10.1093\/ajcn\/71.5.1270s","article-title":"Role of cholesterol in embryonic development","volume":"71","author":"Roux","year":"2000","journal-title":"Am. J. Clin. Nutr."},{"key":"10.1016\/j.bcp.2021.114611_b0515","doi-asserted-by":"crossref","first-page":"1098","DOI":"10.3390\/ijms19041098","article-title":"Hedgehog signals mediate anti-cancer drug resistance in three-dimensional primary colorectal cancer organoid culture","volume":"19","author":"Usui","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bcp.2021.114611_b0520","doi-asserted-by":"crossref","first-page":"13413","DOI":"10.1016\/S0021-9258(18)90710-6","article-title":"Microsomal enzymes of cholesterol biosynthesis from lanosterol. Characterization, solubilization, and partial purification of NADPH-dependent \u03948,14-steroid 14-reductase","volume":"259","author":"Paik","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0525","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1016\/0006-291X(84)91184-7","article-title":"Effects of AY9944 on low density lipoprotein metabolism in cultured human fibroblasts","volume":"122","author":"Mazi\u00e8re","year":"1984","journal-title":"Chem. Biophys. Res. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0530","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.taap.2018.04.029","article-title":"Dichlorophenyl piperazines, including a recently-approved atypical antipsychotic, are potent inhibitors of DHCR7, the last enzyme in cholesterol biosynthesis","volume":"349","author":"Genaro-Mattos","year":"2018","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.bcp.2021.114611_b0535","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1038\/tpj.2016.48","article-title":"Investigation of 7-dehydrocholesterol reductase pathway to elucidate off-target prenatal effects of pharmaceuticals: a systematic review","volume":"16","author":"Boland","year":"2016","journal-title":"Pharmacogenomics J."},{"key":"10.1016\/j.bcp.2021.114611_b0540","doi-asserted-by":"crossref","first-page":"5904","DOI":"10.1073\/pnas.1604984113","article-title":"Endogenous B-ring oxysterols inhibit the Hedgehog component Smoothened in a manner distinct from cyclopamine or side-chain oxysterols","volume":"113","author":"Sever","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.bcp.2021.114611_b0545","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.tips.2014.03.002","article-title":"Targeting of smoothened for therapeutic gain","volume":"35","author":"Ruat","year":"2014","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.bcp.2021.114611_b0550","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1172\/JCI0216386","article-title":"Malformation syndromes due to inborn errors of cholesterol synthesis","volume":"110","author":"Porter","year":"2002","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bcp.2021.114611_b0555","doi-asserted-by":"crossref","first-page":"2850","DOI":"10.1074\/jbc.RA119.011323","article-title":"Twin enzymes, divergent control: the cholesterogenic enzymes DHCR14 and LBR are differentially regulated transcriptionally and post-translationally","volume":"295","author":"Capell-Hattam","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0560","first-page":"361ra140","article-title":"Selective targeting of mutant adenomatous polyposis coli (APC) in colorectal cancer","volume":"19","author":"Zhang","year":"2016","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.bcp.2021.114611_b0565","doi-asserted-by":"crossref","first-page":"6128","DOI":"10.1021\/jacs.9b13407","article-title":"A medicinal chemistry-driven approach identified the sterol isomerase EBP as the molecular target of TASIN colorectal cancer toxins","volume":"142","author":"Theodoropoulos","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bcp.2021.114611_b0570","doi-asserted-by":"crossref","first-page":"5217","DOI":"10.1021\/acs.jmedchem.9b00532","article-title":"Design and synthesis of TASIN analogues specifically targeting colorectal cancer cell lines with mutant adenomatous polyposis coli (APC)","volume":"62","author":"Wang","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0575","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1016\/S0022-3565(24)37523-8","article-title":"Both the Immunosuppressant SR31747 and the antiestrogen tamoxifen bind to an emopamil-insensitive site of mammalian \u03948-\u03947 sterol isomerase","volume":"285","author":"Paul","year":"1998","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"10.1016\/j.bcp.2021.114611_b0580","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.bbrc.2014.06.118","article-title":"Genkwadaphnin induces reactive oxygen species (ROS)-mediated apoptosis of squamous cell carcinoma (SCC) cells","volume":"450","author":"Li","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0585","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/j.jep.2006.12.023","article-title":"Daphnane diterpene esters isolated from flower buds of Daphne genkwa induce apoptosis in human myelocytic HL-60 cells and suppress tumor growth in Lewis lung carcinoma (LLC)-inoculated mouse model","volume":"111","author":"Park","year":"2007","journal-title":"J. Ethnopharmacol."},{"key":"10.1016\/j.bcp.2021.114611_b0590","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1194\/jlr.TR119000439","article-title":"Lipid rafts as signaling hubs in cancer cell survival\/death and invasion: implications in tumor progression and therapy","volume":"61","author":"Mollinedo","year":"2020","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bcp.2021.114611_b0595","first-page":"494","article-title":"Cataracts produced by triparanol. (MER-29)","volume":"65","author":"Kirby","year":"1967","journal-title":"Trans. Am. Ophthalmol. Soc."},{"key":"10.1016\/j.bcp.2021.114611_b0600","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/j.bbrc.2012.07.136","article-title":"Triparanol suppresses human tumor growth in vitro and in vivo","volume":"425","author":"Bi","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0605","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1186\/1471-2407-10-103","article-title":"Lovastatin induces apoptosis of ovarian cancer cells and synergizes with doxorubicin: potential therapeutic relevance","volume":"10","author":"Martirosyan","year":"2010","journal-title":"BMC Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0610","doi-asserted-by":"crossref","first-page":"165968","DOI":"10.1016\/j.bbadis.2020.165968","article-title":"Pleiotropic effects of statins: a focus on cancer","volume":"1866","author":"Ahmadi","year":"2020","journal-title":"Biochim. Biophys. Acta. Mol. Basis Dis."},{"key":"10.1016\/j.bcp.2021.114611_b0615","first-page":"76","article-title":"Caspase-7 is activated during lovastatin-induced apoptosis of the prostate cancer cell line LNCaP","volume":"58","author":"Marcelli","year":"1998","journal-title":"Cancer Res."},{"key":"10.1016\/j.bcp.2021.114611_b0620","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1002\/ijc.21361","article-title":"Dramatic synergistic anticancer effect of clinically achievable doses of lovastatin and troglitazone","volume":"118","author":"Yao","year":"2006","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0625","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1111\/bjh.13035","article-title":"SWOG0919: a Phase 2 study of idarubicin and cytarabine in combination with pravastatin for relapsed acute myeloid leukaemia","volume":"167","author":"Advani","year":"2014","journal-title":"Br. J. Haematol."},{"key":"10.1016\/j.bcp.2021.114611_b0630","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/s40170-020-00231-8","article-title":"The effect of statin treatment on intratumoral cholesterol levels and LDL receptor expression: a window-of opportunity breast cancer trial","volume":"8","author":"Feldt","year":"2020","journal-title":"Cancer Metab."},{"key":"10.1016\/j.bcp.2021.114611_b0635","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1054\/bjoc.2000.1716","article-title":"Effect of pravastatin on survival in patients with advanced hepatocellular carcinoma. A randomized controlled trial","volume":"84","author":"Kawata","year":"2001","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0640","doi-asserted-by":"crossref","first-page":"3200","DOI":"10.1016\/j.ejca.2010.07.036","article-title":"The addition of pravastatin to chemotherapy in advanced gastric carcinoma: a randomised phase II trial","volume":"46","author":"Konings","year":"2010","journal-title":"Eur. J. Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0645","doi-asserted-by":"crossref","first-page":"1553","DOI":"10.1158\/1078-0432.CCR-10-2525","article-title":"A randomized phase II study of gefitinib plus simvastatin versus gefitinib alone in previously treated patients with advanced non-small cell lung cancer","volume":"17","author":"Han","year":"2011","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.bcp.2021.114611_b0650","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1007\/s00280-013-2328-1","article-title":"Randomized double-blinded, placebo-controlled phase II trial of simvastatin and gemcitabine in advanced pancreatic cancer patients","volume":"73","author":"Hong","year":"2014","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.bcp.2021.114611_b0655","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1038\/bjc.2015.371","article-title":"A randomised, double-blind, placebo-controlled multi-centre phase III trial of XELIRI\/FOLFIRI plus simvastatin for patients with metastatic colorectal cancer","volume":"113","author":"Lim","year":"2015","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0660","doi-asserted-by":"crossref","first-page":"325","DOI":"10.3390\/jcm7100325","article-title":"The effect of statin added to systemic anticancer therapy: a meta-analysis of randomized, controlled trials","volume":"7","author":"Jang","year":"2018","journal-title":"J. Clin. Med."},{"key":"10.1016\/j.bcp.2021.114611_b0665","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.leukres.2018.01.021","article-title":"Report of the relapsed\/refractory cohort of SWOG S0919: a phase 2 study of idarubicin and cytarabine in combination with pravastatin for acute myelogenous leukemia (AML)","volume":"67","author":"Advani","year":"2018","journal-title":"Leuk. Res."},{"key":"10.1016\/j.bcp.2021.114611_b0670","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1200\/JCO.2016.69.7391","article-title":"Multicenter, phase III, randomized, double-blind, placebo- controlled trial of pravastatin added to first-line standard chemotherapy in small-cell lung cancer (LUNGSTAR)","volume":"35","author":"Seckl","year":"2017","journal-title":"J. Clin. Oncol."},{"key":"10.1016\/j.bcp.2021.114611_b0675","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1002\/hon.869","article-title":"A phase II clinical trial does not show that high dose simvastatin has beneficial effect on markers of bone turnover in multiple myeloma","volume":"27","author":"Sondergaard","year":"2009","journal-title":"Hematol. Oncol."},{"key":"10.1016\/j.bcp.2021.114611_b0680","doi-asserted-by":"crossref","first-page":"eaap9840","DOI":"10.1126\/scitranslmed.aap9840","article-title":"Squalene epoxidase drives NAFLD-induced hepatocellular carcinoma and is a pharmaceutical target","volume":"10","author":"Liu","year":"2018","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.bcp.2021.114611_b0685","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1053\/j.gastro.2020.09.009","article-title":"Reduction of squalene epoxidase by cholesterol accumulation accelerates colorectal cancer progression and metastasis","volume":"160","author":"Jun","year":"2021","journal-title":"Gastroenterology"},{"key":"10.1016\/j.bcp.2021.114611_b0690","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/s41467-018-07959-4","article-title":"A chemical biology screen identifies a vulnerability of neuroendocrine cancer cells to SQLE inhibition","volume":"10","author":"Mahoney","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0695","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1111\/1759-7714.12944","article-title":"Squalene epoxidase promotes the proliferation and metastasis of lung squamous cell carcinoma cells though extracellular signal-regulated kinase signaling","volume":"10","author":"Ge","year":"2019","journal-title":"Thorac. Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0700","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1002\/(SICI)1097-010X(19991015)285:3<237::AID-JEZ6>3.0.CO;2-S","article-title":"Meiosis activating sterols (MAS) and fertility in mammals and man","volume":"285","author":"Byskov","year":"1999","journal-title":"J. Exp. Zool."},{"key":"10.1016\/j.bcp.2021.114611_b0705","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1007\/s001090050286","article-title":"Meiosis-activating sterols: background, discovery, and possible use","volume":"76","author":"Byskov","year":"1998","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.bcp.2021.114611_b0710","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1038\/374559a0","article-title":"Chemical structure of sterols that activate oocyte meiosis","volume":"374","author":"Byskov","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.bcp.2021.114611_b0715","doi-asserted-by":"crossref","first-page":"85","DOI":"10.4049\/jimmunol.1003804","article-title":"Lamin B receptor regulates the growth and maturation of myeloid progenitors via its sterol reductase domain: implications for cholesterol biosynthesis in regulating myelopoiesis","volume":"188","author":"Subramanian","year":"2012","journal-title":"J. Immunol."},{"key":"10.1016\/j.bcp.2021.114611_b0720","doi-asserted-by":"crossref","unstructured":"P.-L. Tsai, C. Zhao, E. Turner, C. Schlieker, The Lamin B receptor is essential for cholesterol synthesis and perturbed by disease-causing mutations, eLife 5 (2016) e16011.","DOI":"10.7554\/eLife.16011"},{"key":"10.1016\/j.bcp.2021.114611_b0725","doi-asserted-by":"crossref","unstructured":"I. Bellezza, R. Roberti, L. Gatticchi, R. Del Sordo, M. G. Rambotti, M. C. Marchetti, A. Sidoni, A. Minelli, A novel role for Tm7sf2 gene in regulating TNF\u03b1 expression, PLOS ONE 8 (2013) e68017.","DOI":"10.1371\/journal.pone.0068017"},{"key":"10.1016\/j.bcp.2021.114611_b0730","doi-asserted-by":"crossref","first-page":"9471","DOI":"10.1038\/srep09471","article-title":"The loss of Tm7sf gene accelerates skin papilloma formation in mice","volume":"5","author":"Bellezza","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bcp.2021.114611_b0735","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/S0303-7207(01)00707-9","article-title":"Role of meiosis activating sterols, MAS, in induced oocyte maturation","volume":"187","author":"Byskov","year":"2002","journal-title":"Mol. Cell Endocrinol."},{"key":"10.1016\/j.bcp.2021.114611_b0740","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1002\/mrd.20899","article-title":"Involvement of mitogen-activated protein kinase (MAPK) pathway in LH- and meiosis-activating sterol (MAS)-induced maturation in rat and mouse oocytes","volume":"75","author":"Motola","year":"2008","journal-title":"Mol. Reprod. Dev."},{"key":"10.1016\/j.bcp.2021.114611_b0745","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.mce.2006.01.008","article-title":"Meiosis activating sterol (MAS) regulate FSH-induced meiotic resumption of cumulus cell-enclosed porcine oocytes via PKC pathway","volume":"249","author":"Jin","year":"2006","journal-title":"Mol. Cell Endocrinol."},{"key":"10.1016\/j.bcp.2021.114611_b0750","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.theriogenology.2019.11.012","article-title":"Follicular fluid meiosis-activating sterol (FF-MAS) promotes meiotic resumption via the MAPK pathway in porcine oocytes","volume":"148","author":"Guo","year":"2020","journal-title":"Theriogenology"},{"key":"10.1016\/j.bcp.2021.114611_b0755","doi-asserted-by":"crossref","first-page":"2299","DOI":"10.1210\/en.2014-1884","article-title":"Oocyte induction of EGF responsiveness in somatic cells is associated with the acquisition of porcine oocyte developmental competence","volume":"156","author":"Ritter","year":"2015","journal-title":"Endocrinology"},{"key":"10.1016\/j.bcp.2021.114611_b0760","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.mce.2004.09.009","article-title":"Resumption of oocyte meiosis in mammals: On models, meiosis activating sterols, steroids and EGF-like factors","volume":"234","author":"Tsafriri","year":"2005","journal-title":"Mol. Cell. Endocrinol."},{"key":"10.1016\/j.bcp.2021.114611_b0765","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1016\/j.ajhg.2010.11.004","article-title":"Hypomorphic temperature-sensitive alleles of NSDHL cause CK syndrome","volume":"87","author":"McLarren","year":"2010","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bcp.2021.114611_b0770","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1186\/s12881-020-01094-y","article-title":"Novel variant in NSDHL gene associated with CHILD syndrome and syndactyly- a case report","volume":"21","author":"Hettiarachchi","year":"2020","journal-title":"BMC Med. Genet."},{"key":"10.1016\/j.bcp.2021.114611_b0775","doi-asserted-by":"crossref","first-page":"1372","DOI":"10.1038\/cdd.2009.62","article-title":"Ligands of the antiestrogen-binding site induce active cell death and autophagy in human breast cancer cells through the modulation of cholesterol metabolism","volume":"16","author":"de Medina","year":"2009","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.bcp.2021.114611_b0780","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1038\/s41467-017-01948-9","article-title":"Dendrogenin a drives LXR to trigger lethal autophagy in cancers","volume":"8","author":"Segala","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.bcp.2021.114611_b0785","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.4161\/auto.5.7.9820","article-title":"Tamoxifen and AEBS ligands induced apoptosis and autophagy in breast cancer cells through the stimulation of sterol accumulation","volume":"5","author":"de Medina","year":"2009","journal-title":"Autophagy"},{"key":"10.1016\/j.bcp.2021.114611_b0790","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1146\/annurev-genom-091212-153412","article-title":"Disorders of cholesterol metabolism and their unanticipated convergent mechanisms of disease","volume":"15","author":"Platt","year":"2014","journal-title":"Annu. Rev. Genomics Hum. Genet."},{"key":"10.1016\/j.bcp.2021.114611_b0795","first-page":"1431","article-title":"The sterol-based transcriptional control of human 7-dehydrocholesterol reductase (DHCR7): Evidence of a cooperative regulatory program in cholesterol synthesis","volume":"2014","author":"Prabhu","year":"1841","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bcp.2021.114611_b0800","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0022-2275(20)39757-1","article-title":"Markedly increased tissue concentrations of 7-dehydrocholesterol combined with low levels of cholesterol are characteristic of the Smith-Lemli-Opitz syndrome","volume":"36","author":"Tint","year":"1995","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bcp.2021.114611_b0805","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1194\/jlr.P048603","article-title":"On the formation of 7-ketocholesterol from 7-dehydrocholesterol in patients with CTX and SLO","volume":"55","author":"Bj\u00f6rkhem","year":"2014","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bcp.2021.114611_b0810","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1021\/acs.jmedchem.5b01696","article-title":"The effect of small molecules on sterol homeostasis: measuring 7-dehydrocholesterol in Dhcr7-deficient neuro2a cells and human fibroblasts","volume":"59","author":"Korade","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0815","doi-asserted-by":"crossref","first-page":"3259","DOI":"10.1194\/jlr.M009365","article-title":"Biological activities of 7-dehydrocholesterol-derived oxysterols: implications for Smith-Lemli-Opitz syndrome","volume":"51","author":"Korade","year":"2010","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.bcp.2021.114611_b0820","doi-asserted-by":"crossref","first-page":"2222","DOI":"10.1021\/ja9080265","article-title":"Oxysterols from free radical chain oxidation of 7-dehydrocholesterol: product and mechanistic studies","volume":"132","author":"Xu","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bcp.2021.114611_b0825","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1016\/j.nbd.2011.12.011","article-title":"DHCEO accumulation is a critical mediator of pathophysiology in a Smith-Lemli-Opitz syndrome model","volume":"45","author":"Xu","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.bcp.2021.114611_b0830","doi-asserted-by":"crossref","first-page":"3653","DOI":"10.1111\/cas.14587","article-title":"24-Dehydrocholesterol reductase promotes the growth of breast cancer stem-like cells through the Hedgehog pathway","volume":"111","author":"Qiu","year":"2020","journal-title":"Cancer Sci."},{"key":"10.1016\/j.bcp.2021.114611_b0835","doi-asserted-by":"crossref","first-page":"41404","DOI":"10.1038\/srep41404","article-title":"Cholesterol synthetase DHCR24 induced by insulin aggravates cancer invasion and progesterone resistance in endometrial carcinoma","volume":"7","author":"Dai","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bcp.2021.114611_b0840","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1016\/j.ejmech.2017.08.011","article-title":"New chemotype of selective and potent inhibitors of human delta 24-dehydrocholesterol reductase","volume":"140","author":"M\u00fcller","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0845","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1007\/s00018-020-03490-2","article-title":"Crystal structures of human NSDHL and development of its novel inhibitor with the potential to suppress EGFR activity","volume":"78","author":"Kim","year":"2021","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bcp.2021.114611_b0850","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1186\/s12885-020-06840-2","article-title":"NAD(P)-dependent steroid dehydrogenaselike is involved in breast cancer cell growth and metastasis","volume":"20","author":"Yoon","year":"2020","journal-title":"BMC Cancer"},{"key":"10.1016\/j.bcp.2021.114611_b0855","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1128\/MCB.01140-13","article-title":"The E3 ubiquitin ligase MARCH6 degrades squalene monooxygenase and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase and the cholesterol synthesis pathway","volume":"34","author":"Zelcer","year":"2014","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.bcp.2021.114611_b0860","doi-asserted-by":"crossref","first-page":"20503","DOI":"10.1073\/pnas.1112831108","article-title":"Sterolinduced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8","volume":"108","author":"Jo","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.bcp.2021.114611_b0865","doi-asserted-by":"crossref","unstructured":"S. A Menzies, N. Volkmar, D. J. H. van den Boomen, R. T. Timms, A. S. Dickson, J. A. Nathan, P. J. Lehner, The sterol-responsive RNF145 E3 ubiquitin ligase mediates the degradation of HMG-CoA reductase together with gp78 and Hrd1, eLife 7 (2018) e40009.","DOI":"10.7554\/eLife.40009"},{"key":"10.1016\/j.bcp.2021.114611_b0870","doi-asserted-by":"crossref","first-page":"4484","DOI":"10.1091\/mbc.e12-08-0631","article-title":"Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system","volume":"23","author":"Tsai","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.bcp.2021.114611_b0875","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.molcel.2020.07.009","article-title":"Quality control of ER membrane proteins by the RNF185\/membralin ubiquitin ligase complex","volume":"79","author":"van de Weijer","year":"2020","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bcp.2021.114611_b0880","doi-asserted-by":"crossref","first-page":"8363","DOI":"10.1074\/jbc.M115.699546","article-title":"Cholesterol mediated degradation of 7-dehydrocholesterol reductase switches the balance from cholesterol to vitamin D synthesis","volume":"291","author":"Prabhu","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bcp.2021.114611_b0885","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1194\/jlr.M043257","article-title":"Signaling regulates activity of DHCR24, the final enzyme in cholesterol synthesis","volume":"55","author":"Luu","year":"2014","journal-title":"J. Lipid Res."}],"container-title":["Biochemical Pharmacology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006295221002173?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006295221002173?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T13:26:19Z","timestamp":1757769979000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006295221002173"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,2]]},"references-count":177,"alternative-id":["S0006295221002173"],"URL":"https:\/\/doi.org\/10.1016\/j.bcp.2021.114611","relation":{},"ISSN":["0006-2952"],"issn-type":[{"value":"0006-2952","type":"print"}],"subject":[],"published":{"date-parts":[[2022,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Unearthing the Janus-face cholesterogenesis pathways in cancer","name":"articletitle","label":"Article Title"},{"value":"Biochemical Pharmacology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bcp.2021.114611","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Authors. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"114611"}}