Pharmacological Analysis of Sterol Δ8-Δ7 Isomerase Proteins with [3H]Ifenprodil

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works

Simultaneous analysis of families of sigmoidal curves: application to bioassay, radioligand assay, and physiological dose-response curves.

DeLÉAN, A., Munson, P. J., & Rodbard, D. (1978) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1978.235.2.e97 · Cited by 2,384 · see citing works

Purification, molecular cloning, and expression of the mammalian sigma1-binding site.

Hanner, M., Moebius, F. F., Flandorfer, A., Knaus, H. G., Striessnig, J., Kempner, E. S., & Glossmann, H. H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.8072 · Cited by 906 · see citing works

Mutations in the Δ7-sterol reductase gene in patients with the Smith–Lemli–Opitz syndrome

Fitzky, B. U., Witsch-Baumgartner, M., Erdel, M., Lee, J. N., Paik, Y.-K., Glossmann, H., Utermann, G., & Moebius, F. F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.8181 · Cited by 384 · see citing works

Pharmacological properties of recombinant human N-methyl-D-aspartate receptors comprising NR1a/NR2A and NR1a/NR2B subunit assemblies expressed in permanently transfected mouse fibroblast cells.

Priestley, T., Laughton, P., Myers, J., Bourdellès, B. L., Kerby, J., & Whiting, P. J. (1995) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10541-5 · Cited by 262 · see citing works

Molecular cloning and expression of the human Δ7-sterol reductase

Moebius, F. F., Fitzky, B. U., Lee, J. N., Paik, Y., & Glossmann, H. H. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1899 · Cited by 221 · see citing works

Interactions between Ifenprodil and the NR2B Subunit of the N-Methyl-D-aspartate Receptor

Gallagher, M. J., Huang, H., Pritchett, D. B., & Lynch, D. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9603 · Cited by 160 · see citing works

Emopamil-binding Protein, a Mammalian Protein That Binds a Series of Structurally Diverse Neuroprotective Agents, Exhibits Δ8-Δ7 Sterol Isomerase Activity in Yeast

Silve, S., Dupuy, P.-H., Bouteiller, C. L., Kaghad, M., Chalon, P., Rahier, A., Taton, M., Lupker, J. H., Shire, D. J., & Loison, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22434 · Cited by 128 · see citing works

High affinity of sigma1‐binding sites for sterol isomerization inhibitors: evidence for a pharmacological relationship with the yeast sterol C8–C7 isomerase

Moebius, F. F., Reiter, R. J., Hanner, M., & Glossmann, H. H. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701079 · Cited by 113 · see citing works

Tamoxifen and toremifene lower serum cholesterol by inhibition of delta 8-cholesterol conversion to lathosterol in women with breast cancer.

Gylling, H., Pyrhönen, S., Mäntylä, E., Mäenpää, H., Kangas, L., & Miettinen, T. A. (1995) · Journal of Clinical Oncology · doi:10.1200/jco.1995.13.12.2900 · Cited by 112 · see citing works

Significance of slow-binding enzyme inhibition and its relationship to reaction-intermediate analogs

Schloss, J. V. (1988) · Accounts of Chemical Research · doi:10.1021/ar00153a005 · Cited by 110 · see citing works

Role of Multidrug Resistance P-glycoproteins in Cholesterol Biosynthesis

Metherall, J. E., Li, H., & Waugh, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2634 · Cited by 108 · see citing works

The mysteries of sigma receptors: new family members reveal a role in cholesterol synthesis

Moebius, F. F., Striessnig, J., & Glossmann, H. H. (1997) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(96)01037-1 · Cited by 106 · see citing works

Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol Δ24-reductase

Bae, S., & Paik, Y. (1997) · Biochemical Journal · doi:10.1042/bj3260609 · Cited by 93 · see citing works

Further characterization of [3H]ifenprodil binding to σ receptors in rat brain

Hashimoto, K., & London, E. D. (1993) · European Journal of Pharmacology · doi:10.1016/0014-2999(93)90241-9 · Cited by 93 · see citing works

Phenylalkylamine Ca2+ Antagonist Binding Protein

Hanner, M., Moebius, F. F., Weber, F., Grabner, M., Striessnig, J., & Glossmann, H. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7551 · Cited by 86 · see citing works

An aspartate residue in the extracellular loop of the N-methyl-D-aspartate receptor controls sensitivity to spermine and protons.

Kashiwagi, K., Fukuchi, J., Chao, J., Igarashi, K., & Williams, K. L. (1996) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09016-9 · Cited by 83 · see citing works

Spiropiperidines as high-affinity, selective .sigma. ligands.

Chambers, M. S., Baker, R., Billington, D. C., Knight, A. R., Middlemiss, D. N., & Wong, E. H. F. (1992) · Journal of Medicinal Chemistry · doi:10.1021/jm00089a013 · Cited by 78 · see citing works

Yeast Sterol C8−C7 Isomerase: Identification and Characterization of a High-Affinity Binding Site for Enzyme Inhibitors

Moebius, F. F., Bermoser, K., Reiter, R. J., Hanner, M., & Glossmann, H. H. (1996) · Biochemistry · doi:10.1021/bi961996m · Cited by 69 · see citing works

Calculating the dissociation constant of an unlabeled compound from the concentration required to displace radiolabel binding by 50%.

Linden, J. M. (1982) · PubMed · Cited by 63 · see citing works

Disorders of cholesterol biosynthesis

Clayton, P. T. (1998) · Archives of Disease in Childhood · doi:10.1136/adc.78.2.185 · Cited by 55 · see citing works

Microsomal enzymes of cholesterol biosynthesis from lanosterol. Solubilization and purification of steroid 8-isomerase.

Paik, Y., Billheimer, J. T., Magolda, R. L., & Gaylor, J. L. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84586-6 · Cited by 54 · see citing works

Inhibition of the conversion of 7-dehydrocholesterol to cholesterol by AY-9944

Kraml, M., Bagli, J. F., & Dvornik, D. (1964) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(64)90485-1 · Cited by 49 · see citing works

Inhibition of Cholesterol Synthesis and Cell Growth by 24(R, S),25-Iminolanosterol and Triparanol in Cultured Rat Hepatoma Cells

Popják, G. J., Meenan, A., Parish, E. J., & Nes, W. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83338-5 · Cited by 48 · see citing works

INHIBITION BY TRIPARANOL OF CHOLESTEROL FORMATION IN THE BRAIN OF THE NEWBORN MOUSE*

Scallen, T. J., Condie, R. M., & Schroepfer, G. J. (1962) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1962.tb11849.x · Cited by 37 · see citing works

The effects of enclomiphene and zuclomiphene citrates on mouse embryos fertilized in vitro and in vivo

Schmidt, G. E., Kim, M. H., Mansour, R., Torello, L. A., & Friedman, C. I. (1986) · American Journal of Obstetrics and Gynecology · doi:10.1016/0002-9378(86)90444-8 · Cited by 35 · see citing works

Sterol Biosynthesis: Strong Inhibition of Maize Δ5,7-Sterol Δ7-Reductase by Novel 6-Aza-B-homosteroids and Other Analogs of a Presumptive Carbocationic Intermediate of the Reduction Reaction

Rahier, A., & Taton, M. (1996) · Biochemistry · doi:10.1021/bi9528154 · Cited by 33 · see citing works

High affinity specific antiestrogen binding sites are concentrated in rough microsomal membranes of rat liver

Watts, C. K. W., & Sutherland, R. L. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91420-7 · Cited by 33 · see citing works

Biochemical characterization of a 22-kDa high affinity antiischemic drug-binding polypeptide in the endoplasmic reticulum of guinea pig liver: potential common target for antiischemic drug action.

Moebius, F. F., Burrows, G. G., Striessnig, J., & Glossmann, H. H. (1993) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13593-1 · Cited by 33 · see citing works

Ectodermal dysplasia and immunodeficiency.

Abinun, M. (1995) · Archives of Disease in Childhood · doi:10.1136/adc.73.2.185 · Cited by 31 · see citing works

Identification of Δ5,7-sterol-Δ7-reductase in higher plant microsomes

Taton, M., & Rahier, A. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81442-1 · Cited by 26 · see citing works

Pharmacological characterization of in vivo [3H]lfenprodil binding sites in the mouse brain.

Bénavidès, J., Peny, B., Allen, J. R., & Scatton, B. (1992) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)11380-3 · Cited by 23 · see citing works

L-Type Calcium Channels: Binding Domains for Dihydropyridines and Benzothiazepines Are Located in Close Proximity to Each Other

Brauns, T., Prinz, H., Kimball, S. D., Haugland, R. P., Striessnig, J., & Glossmann, H. H. (1997) · Biochemistry · doi:10.1021/bi9613584 · Cited by 21 · see citing works

High-affinity binding sites for oxygenated sterols in rat liver microsomes: possible identity with antiestrogen binding sites☆

HWANG, P. (1990) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(90)90006-i · Cited by 20 · see citing works

Cholesterol Biosynthesis from Lanosterol: Regulation and Purification of Rat Hepatic Sterol 8-Isomerase1

Kang, M.-K., Kim, C.-K., Johng, T.-N., & Paik, Y. (1995) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a124781 · Cited by 19 · see citing works

Calmodulin antagonists suppress cholesterol synthesis by inhibiting sterol Δ24 reductasereductase

Filipović, I., & Buddecke, E. (1987) · Lipids · doi:10.1007/bf02533989 · Cited by 12 · see citing works

EFFECT OF ZUCLOMIPHENE ON CHOLESTEROL FORMATION IN THE DEVELOPING CENTRAL NERVOUS SYSTEM OF THE RAT

Ramsey, R. B., Fredericks, M. R., & Fischer, V. W. (1977) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1977.tb12326.x · Cited by 11 · see citing works

Enzyme inhibition during the conversion of squalene to cholesterol

Lewis, D., Galczenski, H., Needle, S., Tang, S.-Y., Amin, D., Gleason, M. M., Bilder, G. E., Perrone, M. H., Merkel, L. A., & Rojas, C. J. (1995) · Steroids · doi:10.1016/0039-128x(95)00054-t · Cited by 10 · see citing works

Triphenylethylene antiestrogen binding sites (TABS) specificity

Clark, J. H., Mitchell, W. C., & Guthrie, S. C. (1987) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(87)90052-5 · Cited by 10 · see citing works

An embryotoxicity study of the fungicide tridemorph and its commercial formulation Calixin

Merkle, J., Schulz, V., & Gelbke, H. P. (1984) · Teratology · doi:10.1002/tera.1420290212 · Cited by 8 · see citing works

An alternative mechanism for the inhibition of cholesterol biosynthesis in HepG2 cells by N-[(1,5,9)-trimethyldecyl]-4 alpha,10-dimethyl-8-aza-trans-decal-3 beta-ol (MDL 28,815).

Sickle, W. A. V., Wilson, P. K., Wannamaker, M. W., Cooper, J. R., Flanagan, M. A., McCarthy, J. R., Bey, P., & Jackson, R. L. (1993) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)39564-9 · Cited by 7 · see citing works

Butyrophenones as Inhibitors of Cholesterol Biosynthesis

Braun, G. A. (1969) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-6866-7_38 · Cited by 4 · see citing works

Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms

Gordon, D. E., Hiatt, J. B., Bouhaddou, M., Rezelj, V. V., Ulferts, S., Braberg, H., Jureka, A. S., Obernier, K., Guo, J. Z., Batra, J., et al. (2020) · Science · doi:10.1126/science.abe9403 · Cited by 731 · see citing works

Accumulation of 8,9-unsaturated sterols drives oligodendrocyte formation and remyelination

Hubler, Z., Allimuthu, D., Bederman, I., Elitt, M. S., Madhavan, M., Allan, K. C., Shick, H. E., Garrison, E., T. Karl, M., Factor, D. C., et al. (2018) · Nature · doi:10.1038/s41586-018-0360-3 · Cited by 226 · see citing works

Cholesterol Synthesis Inhibitor U18666A and the Role of Sterol Metabolism and Trafficking in Numerous Pathophysiological Processes

Cenedella, R. J. (2009) · Lipids · doi:10.1007/s11745-009-3305-7 · Cited by 204 · see citing works

Amiodarone Has Intrinsic Anti- Trypanosoma c ruzi Activity and Acts Synergistically with Posaconazole

Benaím, G., Sanders, J. M., García-Marchán, Y., Colina, C., Lira, R., Caldera, A., Payares, G., Sanoja, C., Burgos, J. M., Leon-Rossell, A., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm050691f · Cited by 188 · see citing works

The Molecular Function of σ Receptors: Past, Present, and Future

Schmidt, H. R., & Kruse, A. C. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.07.006 · Cited by 176 · see citing works

Neuro(active)steroids actions at the neuromodulatory sigma1 (σ1) receptor: Biochemical and physiological evidences, consequences in neuroprotection

Maurice, T., Gregoire, C. J., & Espallergues, J. (2006) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2006.07.009 · Cited by 140 · see citing works

Identification and pharmacological characterization of cholesterol-5,6-epoxide hydrolase as a target for tamoxifen and AEBS ligands

de Medina, P., Paillasse, M. R., Segala, G., Poirot, M., & Silvente-Poirot, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002922107 · Cited by 128 · see citing works

Cholesterol and breast cancer development

Danilo, C., & Frank, P. G. (2012) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2012.07.009 · Cited by 128 · see citing works

Discovery of High-Affinity Ligands of σ1 Receptor, ERG2, and Emopamil Binding Protein by Pharmacophore Modeling and Virtual Screening

Laggner, C., Schieferer, C., Fiechtner, B., Poles, G., Hoffmann, R. D., Glossmann, H. H., Langer, T., & Moebius, F. F. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049073+ · Cited by 116 · see citing works

Molecular Characterization of the Microsomal Tamoxifen Binding Site

Kedjouar, B., de Médina, P., Oulad‐Abdelghani, M., Payré, B., Silvente‐Poirot, S., Favre, G., Faye, J., & Poirot, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405230200 · Cited by 103 · see citing works

Steroidal Triterpenes of Cholesterol Synthesis

Ačimovič, J., & Rozman, D. (2013) · Molecules · doi:10.3390/molecules18044002 · Cited by 76 · see citing works

Synthesis of New Alkylaminooxysterols with Potent Cell Differentiating Activities: Identification of Leads for the Treatment of Cancer and Neurodegenerative Diseases

de Médina, P., Paillasse, M. R., Payré, B., Silvente‐Poirot, S., & Poirot, M. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901063e · Cited by 71 · see citing works

Mechanism of the Synergistic Effect of Amiodarone and Fluconazole in <i>Candida albicans</i>

Gamarra, S., Rocha, E. M. F., Zhang, Y.-Q., Park, S., Rao, R., & Perlin, D. S. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01728-09 · Cited by 70 · see citing works

The dextromethorphan analog dimemorfan attenuates kainate‐induced seizures via σ1 receptor activation: comparison with the effects of dextromethorphan

Shin, E., Nah, S.-Y., Kim, W., Ko, K. H., Jhoo, W., Lim, Y. K., Cha, J. Y., Chen, C., & Kim, H. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705998 · Cited by 68 · see citing works

Molecular imaging of σ receptors: synthesis and evaluation of the potent σ1 selective radioligand [18F]fluspidine

Fischer, S., Wiese, C., Maestrup, E. G., Hiller, A., Deuther‐Conrad, W., Scheunemann, M., Schepmann, D., Steinbach, J., Wünsch, B., & Brust, P. (2010) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-010-1658-z · Cited by 67 · see citing works

4-(Tetralin-1-yl)- and 4-(Naphthalen-1-yl)alkyl Derivatives of 1-Cyclohexylpiperazine as σ Receptor Ligands with Agonist σ2 Activity

Berardi, F., Ferorelli, S., Abate, C., Colabufo, N. A., Contino, M., Perrone, R., & Tortorella, V. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm031026e · Cited by 67 · see citing works

Defects in cholesterol synthesis genes in mouse and in humans: lessons for drug development and safer treatments

Horvat, S., McWhir, J., & Rozman, D. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2010.540580 · Cited by 66 · see citing works

Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition

Long, T., Hassan, A., Thompson, B. M., McDonald, J. G., Wang, J., & Li, X. (2019) · Nature Communications · doi:10.1038/s41467-019-10279-w · Cited by 65 · see citing works

TM6SF2 and MAC30, new enzyme homologs in sterol metabolism and common metabolic disease

Sanchez-Pulido, L., & Ponting, C. P. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00439 · Cited by 63 · see citing works

Genetic Defects in Postsqualene Cholesterol Biosynthesis

Moebius, F. F., Fitzky, B. U., & Glossmann, H. H. (2000) · Trends in Endocrinology and Metabolism · doi:10.1016/s1043-2760(00)00235-6 · Cited by 60 · see citing works

Identification of Environmental Quaternary Ammonium Compounds as Direct Inhibitors of Cholesterol Biosynthesis

Herron, J. M., Reese, R. C., Tallman, K. A., Narayanaswamy, R., Porter, N. A., & Xu, L. (2016) · Toxicological Sciences · doi:10.1093/toxsci/kfw041 · Cited by 59 · see citing works

Analogues of σ Receptor Ligand 1-Cyclohexyl-4-[3-(5-methoxy-1,2,3,4-tetrahydronaphthalen-1-yl)propyl]piperazine (PB28) with Added Polar Functionality and Reduced Lipophilicity for Potential Use as Positron Emission Tomography Radiotracers

Abate, C., Niso, M., Lacivita, E., Mosier, P. D., Toscano, A., & Perrone, R. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm1013133 · Cited by 55 · see citing works

A multireceptorial binding reinvestigation on an extended class of σ ligands: N-[ω-(indan-1-yl and tetralin-1-yl)alkyl] derivatives of 3,3-dimethylpiperidine reveal high affinities towards σ1 and EBP sites

Berardi, F. (2001) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(01)00011-6 · Cited by 54 · see citing works

Improving the efficacy of hormone therapy in breast cancer: The role of cholesterol metabolism in SERM-mediated autophagy, cell differentiation and death

Leignadier, J., Dalenc, F., Poirot, M., & Silvente‐Poirot, S. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.06.120 · Cited by 52 · see citing works

Direct perturbation of lens membrane structure may contribute to cataracts caused by U18666A, an oxidosqualene cyclase inhibitor

Cenedella, R. J., Jacob, R. F., Borchman, D., Tang, D., Neely, A. R., Samadi, A. K., Mason, R. P., & Sexton, P. S. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m300469-jlr200 · Cited by 50 · see citing works

Amiodarone and Itraconazole: A Rational Therapeutic Approach for the Treatment of Chronic Chagas’ Disease

Paniz‐Mondolfi, A., Pérez-Álvarez, A. M., Lanza, G., Márquez, E., & Concepción, J. L. (2009) · Chemotherapy · doi:10.1159/000219436 · Cited by 47 · see citing works

Novel 4-(4-Aryl)cyclohexyl-1-(2-pyridyl)piperazines as Δ8−Δ7Sterol Isomerase (Emopamil Binding Protein) Selective Ligands with Antiproliferative Activity

Berardi, F., Abate, C., Ferorelli, S., de Robertis, A. F., Leopoldo, M., Colabufo, N. A., Niso, M., & Perrone, R. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800965b · Cited by 47 · see citing works

Exploring the Importance of Piperazine N-Atoms for σ2Receptor Affinity and Activity in a Series of Analogs of 1-Cyclohexyl-4-[3-(5-methoxy-1,2,3,4-tetrahydronaphthalen-1-yl)propyl]piperazine (PB28)

Berardi, F., Abate, C., Ferorelli, S., Uricchio, V., Colabufo, N. A., Niso, M., & Perrone, R. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9007505 · Cited by 47 · see citing works

Isolation of differentially expressed genes in NPM‐ALK‐positive anaplastic large cell lymphoma

Villalva, C., Trempat, P., Greenland, C., Thomas, C., Girard, J., Moebius, F. F., Delsol, G., & Brousset, P. (2002) · British Journal of Haematology · doi:10.1046/j.1365-2141.2002.03671.x · Cited by 47 · see citing works

1‐Cyclohexyl‐4‐(4‐arylcyclohexyl)piperazines: Mixed σ and Human Δ8–Δ7 Sterol Isomerase Ligands with Antiproliferative and P‐Glycoprotein Inhibitory Activity

Abate, C., Niso, M., Contino, M., Colabufo, N. A., Ferorelli, S., Perrone, R., & Berardi, F. (2010) · ChemMedChem · doi:10.1002/cmdc.201000371 · Cited by 43 · see citing works

Diverse Chemical Scaffolds Enhance Oligodendrocyte Formation by Inhibiting CYP51, TM7SF2, or EBP

Allimuthu, D., Hubler, Z. M. L., Najm, F. J., Tang, H., Bederman, I. R., Seibel, W. L., Tesar, P. J., & Adams, D. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.01.004 · Cited by 42 · see citing works

Selective Aster inhibitors distinguish vesicular and nonvesicular sterol transport mechanisms

Xu, X., Kim, Y.-J., Romartínez-Alonso, B., Sirvydis, K., Ory, D. S., Schwabe, J. W. R., Jung, M. E., & Tontonoz, P. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024149118 · Cited by 41 · see citing works

Use of Trifluoroperazine Isolates a [3H]Ifenprodil Binding Site in Rat Brain Membranes with the Pharmacology of the Voltage-Independent Ifenprodil Site onN-Methyl-d-aspartate Receptors Containing NR2B Subunits

Coughenour, L. L., & Barr, B. M. (2001) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)29675-0 · Cited by 37 · see citing works

Hormonal Therapies in Multiple Sclerosis: a Review of Clinical Data

Hsu, S., & Bove, R. M. (2023) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-023-01326-7 · Cited by 34 · see citing works

Molecular genetics of the Smith-Lemli-Opitz syndrome and postsqualene sterol metabolism

Fitzky, B. U., Glossmann, H. H., Utermann, G., & Moebius, F. F. (1999) · Current Opinion in Lipidology · doi:10.1097/00041433-199904000-00006 · Cited by 33 · see citing works

Structural enzymology of cholesterol biosynthesis and storage

Long, T., Debler, E., & Li, X. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102369 · Cited by 32 · see citing works

Dendrogenin A: A Mammalian Metabolite of Cholesterol with Tumor Suppressor and Neurostimulating Properties

Dalenc, F., Poirot, M., & Silvente‐Poirot, S. (2015) · Current Medicinal Chemistry · doi:10.2174/0929867322666150716114912 · Cited by 30 · see citing works

Design and Evaluation of Naphthol- and Carbazole-Containing Fluorescent σ Ligands as Potential Probes for Receptor Binding Studies

Ferorelli, S., Abate, C., Colabufo, N. A., Niso, M., Inglese, C., Berardi, F., & Perrone, R. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070373b · Cited by 30 · see citing works

Amiodarone Alters Cholesterol Biosynthesis through Tissue-Dependent Inhibition of Emopamil Binding Protein and Dehydrocholesterol Reductase 24

Allen, L. B., Genaro‐Mattos, T. C., Anderson, A. C., Porter, N. A., Mirnics, K., & Korade, Ž. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00042 · Cited by 28 · see citing works

Structural similitudes between cytotoxic antiestrogen-binding site (AEBS) ligands and cytotoxic sigma receptor ligands. evidence for a relationship between cytotoxicity and affinity for AEBS or sigma-2 receptor but not for sigma-1 receptor

Kedjouar, B., Daunes, S., Vilner, B. J., Bowen, W. D., Klaebe, A., Faye, J.-C., & Poirot, M. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00285-3 · Cited by 27 · see citing works

Cloning of an emopamil-binding protein (EBP)-like protein that lacks sterol Δ8-Δ7 isomerase activity

Moebius, F. F., Fitzky, B. U., Wietzorrek, G., Haidekker, A., Andrea, E. D. E. R., & Glossmann, H. H. (2003) · Biochemical Journal · doi:10.1042/bj20030465 · Cited by 26 · see citing works

18F-Labeled 1,4-Dioxa-8-azaspiro[4.5]decane Derivative: Synthesis and Biological Evaluation of a σ1Receptor Radioligand with Low Lipophilicity as Potent Tumor Imaging Agent

Xie, F., Bergmann, R., Knieß, T., Deuther‐Conrad, W., Mamat, C., Neuber, C., Liu, B., Steinbach, J., Brust, P., Pietzsch, J., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00593 · Cited by 26 · see citing works

The response strategies of Colletotrichum gloeosporioides s.s. due to the stress caused by biological control agent Bacillus amyloliquefaciens deciphered by transcriptome analyses

Wang, Q., Ji, Y., Qu, Y.-Y., Qi, Y.-K., Li, D., Liu, Z., & Wu, X. (2020) · Biological Control · doi:10.1016/j.biocontrol.2020.104372 · Cited by 25 · see citing works

Chemical Inhibition of Sterol Biosynthesis

Peeples, E. S., Mirnics, K., & Korade, Ž. (2024) · Biomolecules · doi:10.3390/biom14040410 · Cited by 24 · see citing works

Evolution, Expression Profile, Regulatory Mechanism, and Functional Verification of EBP-Like Gene in Cholesterol Biosynthetic Process in Chickens (Gallus Gallus)

Jiang, K., Ma, Z., Wang, Z., Li, H., Wang, Y., Tian, Y., Li, D., & Liu, X. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2020.587546 · Cited by 21 · see citing works

Purification, characterization and catalytic properties of human sterol 8-isomerase

Nes, W. D., Zhou, W., Dennis, A. L., Li, H., Jia, Z., Keith, R. A., Piser, T. M., & Furlong, S. T. (2002) · Biochemical Journal · doi:10.1042/bj20020551 · Cited by 21 · see citing works

Selective and brain-penetrant lanosterol synthase inhibitors target glioma stem-like cells by inducing 24(S),25-epoxycholesterol production

Nguyen, T. P., Wang, W., Sternisha, A. C., Corley, C. D., Wang, H.-Y. L., Wang, X., Ortiz, F., Lim, S.-K., Abdullah, K. G., Parada, L. F., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.01.005 · Cited by 20 · see citing works

Amiodarone disrupts cholesterol biosynthesis pathway and causes accumulation of circulating desmosterol by inhibiting 24‐dehydrocholesterol reductase

Simonen, P. P., Li, S., Chua, N. K., Lampi, A., Piironen, V. I., Lommi, J., Sinisalo, J. P., Brown, A. J., Ikonen, E., & Gylling, H. (2020) · Journal of Internal Medicine · doi:10.1111/joim.13095 · Cited by 20 · see citing works

Cholesterol biosynthesis from lanosterol: molecular cloning, chromosomal localization, functional expression and liver-specific gene regulation of rat sterol Δ8-isomerase, a cholesterogenic enzyme with multiple functions

Bae, S., Seong, J. K., & Paik, Y. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530689 · Cited by 19 · see citing works

Potential Use of the Cholesterol Transfer Inhibitor U18666A as a Potent Research Tool for the Study of Cholesterol Mechanisms in Neurodegenerative Disorders

Yasamineh, S., Mehrabani, F. J., Derafsh, E., Cosimi, R. D., Forood, A. M. K., Soltani, S., Hadi, M., & Gholizadeh, O. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03798-7 · Cited by 17 · see citing works

Identification of essential amino acid residues in a sterol 8,7-isomerase from Zea mays reveals functional homology and diversity with the isomerases of animal and fungal origin

Rahier, A., Pierre, S., Riveill, G., & Karst, F. (2008) · Biochemical Journal · doi:10.1042/bj20080292 · Cited by 17 · see citing works

Synthesis and biological evaluation of 18F labeled fluoro-oligo-ethoxylated 4-benzylpiperazine derivatives for sigma-1 receptor imaging

Wang, X., Li, Y., Deuther‐Conrad, W., Xie, F., Chen, X., Cui, M., Zhang, X., Zhang, J., Steinbach, J., Brust, P., et al. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.10.038 · Cited by 16 · see citing works

Enhancers of Human and Rodent Oligodendrocyte Formation Predominantly Induce Cholesterol Precursor Accumulation

Sax, J. L., Hershman, S. N., Hubler, Z. M. L., Allimuthu, D., Elitt, M. S., Bederman, I. R., & Adams, D. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00330 · Cited by 15 · see citing works

High-level heterologous expression of the human transmembrane sterol Δ8,Δ7-isomerase in Pichia pastoris

Cai, H., Yao, H., Li, T., Tang, Y., & Li, D. (2019) · Protein Expression and Purification · doi:10.1016/j.pep.2019.105463 · Cited by 14 · see citing works

Bridging from Brain to Tumor Imaging: (S)-(−)- and (R)-(+)-[18F]Fluspidine for Investigation of Sigma-1 Receptors in Tumor-Bearing Mice

Kranz, M., Bergmann, R., Knieß, T., Belter, B., Neuber, C., Cai, Z., Deng, G., Fischer, S., Zhou, J., Huang, Y. H., et al. (2018) · Molecules · doi:10.3390/molecules23030702 · Cited by 13 · see citing works

Re-evaluation of in vivo selectivity of [11C]SA4503 to σ1 receptors in the brain: Contributions of emopamil binding protein

Toyohara, J., Sakata, M., & Ishiwata, K. (2012) · Nuclear Medicine and Biology · doi:10.1016/j.nucmedbio.2012.03.002 · Cited by 12 · see citing works

Stereoselective synthesis of a new class of potent and selective inhibitors of human Δ8,7-sterol isomerase

König, M., Müller, C., & Bracher, F. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.01.041 · Cited by 12 · see citing works

Thermostabilization of Membrane Proteins by Consensus Mutation: A Case Study for a Fungal Δ8-7 Sterol Isomerase

Yao, H., Cai, H., & Li, D. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.015 · Cited by 12 · see citing works

Repurposing Clemastine to Target Glioblastoma Cell Stemness

Sun, M. A., Yang, R. R., Liu, H., Wang, W., Song, X., Hu, B., Reynolds, N., Roso, K., Chen, L. H., Greer, P. K., et al. (2023) · Cancers · doi:10.3390/cancers15184619 · Cited by 9 · see citing works

ABotrytis cinereaEmopamil Binding Domain Protein, Required for Full Virulence, Belongs to a Eukaryotic Superfamily Which Has Expanded in Euascomycetes

Gioti, Α., Pradier, J., Fournier, E., Pêcheur, P. L., Giraud‐Delville, C., Debieu, D., Bach, J., Leroux, P., & Levis, C. (2007) · Eukaryotic Cell · doi:10.1128/ec.00159-07 · Cited by 8 · see citing works

Steroidomimetic Aminomethyl Spiroacetals as Novel Inhibitors of the Enzyme Δ8,7‐ S terol Isomerase in Cholesterol Biosynthesis

Krojer, M., Müller, C., & Bracher, F. (2013) · Archiv der Pharmazie · doi:10.1002/ardp.201300296 · Cited by 7 · see citing works

Combined Machine Learning and Molecular Modelling Workflow for the Recognition of Potentially Novel Fungicides

Jović, O., & Šmuc, T. (2020) · Molecules · doi:10.3390/molecules25092198 · Cited by 6 · see citing works

The Compound U18666A Inhibits the Intoxication of Cells by Clostridioides difficile Toxins TcdA and TcdB

Papatheodorou, P., Kindig, S., Badilla-Lobo, A., Fischer, S., Durgun, E., Thuraisingam, T., Witte, A., Song, S., Aktories, K., Chaves‐Olarte, E., et al. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.784856 · Cited by 6 · see citing works

Microsomal epoxide hydrolase expression in the endometrial uterine corpus is regulated by progesterone during the menstrual cycle

Popp, S. L., Abele, I. S., Buck, M. B., Stope, M. B., Blok, L. J., Hanifi‐Moghaddam, P., Burger, C. W., Fritz, P., & Knabbe, C. (2010) · Journal of Molecular Histology · doi:10.1007/s10735-010-9266-6 · Cited by 6 · see citing works

AEBS inhibition in macrophages: Augmenting reality for SERMs repurposing against infections

Sfogliarini, C., Tran, L. H., Cesta, C. M., Allegretti, M., Locati, M., & Vegeto, E. (2024) · Biochemical Pharmacology · doi:10.1016/j.bcp.2024.116544 · Cited by 5 · see citing works

Species and Tissue Distribution of Proteins Binding 16α,17α-Cycloalkanoprogesterone Derivatives

Smirnov, A. N., Pokrovskaya, E. V., Шевченко, В. П., Nagaev, I. Y., Myasoedov, N. F., Levina, I. S., Куликова, Л. Е., & Kamernitsky, A. V. (2002) · Russian Journal of Bioorganic Chemistry · doi:10.1023/a:1015760421546 · Cited by 4 · see citing works

Amiodarone accumulates two cholesterol precursors in myocardium: A controlled clinical study

Simonen, P. P., Lommi, J., Lemström, K., Tolva, J., Sinisalo, J. P., & Gylling, H. (2023) · Journal of Internal Medicine · doi:10.1111/joim.13693 · Cited by 3 · see citing works

Cholesterol and desmosterol dancing to the beat of a different drug

Brown, A. J., & Gelissen, I. C. (2017) · Journal of Internal Medicine · doi:10.1111/joim.12710 · Cited by 3 · see citing works

Atypical Antipsychotics

Leysen, J. E. (2002) · Handbook of experimental pharmacology · doi:10.1007/978-3-662-06765-9_14 · Cited by 3 · see citing works

5,6-epoxycholestanols metabolism and functions: Defining the epoxycholestanoid (EChA) family

Buñay, J., Ayadi, S., Gressein, C., Boudani, M., Commerçon, R., Le, P., Pucheu, L., Record, M., de Médina, P., Silvente‐Poirot, S., et al. (2026) · Progress in Lipid Research · doi:10.1016/j.plipres.2026.101386 · Cited by 2 · see citing works

Gene regulation by morpholines and piperidines in the cardiac embryonic stem cell test

Mennen, R. H., Hallmark, N., Pallardy, M. J., Bars, R., Tinwell, H., & Piersma, A. H. (2021) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2021.115781 · Cited by 2 · see citing works

Menopause and neurological disorders: a roadmap for research

Bove, R. M., & Dobson, R. (2026) · Nature Reviews Neurology · doi:10.1038/s41582-026-01244-5 · Cited by 1 · see citing works

Sterol flux rewiring: Cholesterol biosynthesis as a dynamic signaling network

Poirot, M., de Médina, P., & Silvente‐Poirot, S. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113381 · Cited by 1 · see citing works

Sterols regulate ciliary membrane dynamics and hedgehog signaling in health and diseasePreprint

Lamazière, A., Kozlowski, L., Ayala‐Sanmartín, J., Farhat, M., Belaid, N., Certain, A., Isidor, B., Besnard, T., Trugnan, G., Pazour, G. J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.15.664899 · Cited by 1 · see citing works

Effect of Cholesterol Accumulation on the Metabolism of Amyloid Precursor Protein (APP) in Cultured N2a Cells

Chung, J.-Y. (2015) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r32h3s

O

von Bruchhausen, F., Ebel, S., Hackenthal, E., Holzgrabe, U., Albinus, M., Amschler, G., Angerer, E. V., Arras‐Reiter, C., Bauer, A., Bauer, P., et al. (1999) · Springer eBooks · doi:10.1007/978-3-642-58388-9_4

Sterol Isomerases

Moebius, F. F., Fitzky, B. U., & Glossmann, H. H. (2002) · Wiley eBooks · doi:10.1002/0471203076.emm1320

A two‐component ortholog of the Niemann‐Pick C 1 protein is essential for normal growth and sterol trafficking and signaling in Tetrahymena thermophila

Costa, J., Herrera‐Preval, Y., Puca, G., Nusblat, A. D., & Uttaro, A. D. (2026) · FEBS Journal · doi:10.1111/febs.70636

Rewiring cholesterol vulnerabilities with biomaterials: Mechanisms and opportunities for cancer therapy

Chen, X., Zou, M., Chen, Z., Wu, J., Wu, G., Zhou, Z., Xu, R., Li, N., Feng, W., Guo, Z., et al. (2026) · Materials Today Bio · doi:10.1016/j.mtbio.2026.103762

BindingDB Entry 50042323: Synthesis and biological evaluation of¹8F labeled fluoro-oligo-ethoxylated 4-benzylpiperazine derivatives for sigma-1 receptor imaging.

BindingDB (2013) · UC San Diego · doi:10.7270/q2vm4dkp

BindingDB Entry 50037518: Discovery of high-affinity ligands of sigma1 receptor, ERG2, and emopamil binding protein by pharmacophore modeling and virtual screening.

BindingDB (2012) · UC San Diego · doi:10.7270/q2639qhb

BindingDB Entry 50038741: Novel 4-(4-aryl)cyclohexyl-1-(2-pyridyl)piperazines as Delta(8)-Delta(7) sterol isomerase (emopamil binding protein) selective ligands with antiproliferative activity.

BindingDB (2012) · UC San Diego · doi:10.7270/q21837d3

BindingDB Entry 50038942: Exploring the importance of piperazine N-atoms for sigma(2) receptor affinity and activity in a series of analogs of 1-cyclohexyl-4-[3-(5-methoxy-1,2,3,4-tetrahydronaphthalen-1-yl)propyl]piperazine (PB28).

BindingDB (2012) · UC San Diego · doi:10.7270/q2cj8fdb

BindingDB Entry 50017388: Amiodarone has intrinsic anti-Trypanosoma cruzi activity and acts synergistically with posaconazole.

BindingDB (2009) · UC San Diego · doi:10.7270/q2183626

BindingDB Entry 50042757: Stereoselective synthesis of a new class of potent and selective inhibitors of human¿8,7-sterol isomerase.

BindingDB (2013) · UC San Diego · doi:10.7270/q2sj1n0h

BindingDB Entry 50014603: 4-(tetralin-1-yl)- and 4-(naphthalen-1-yl)alkyl derivatives of 1-cyclohexylpiperazine as sigma receptor ligands with agonist sigma2 activity.

BindingDB (2009) · UC San Diego · doi:10.7270/q2dn44hs

BindingDB Entry 50032929: Analogues ofs receptor ligand 1-cyclohexyl-4-[3-(5-methoxy-1,2,3,4-tetrahydronaphthalen-1-yl)propyl]piperazine (PB28) with added polar functionality and reduced lipophilicity for potential use as positron emission tomography radiotracers.

BindingDB (2011) · UC San Diego · doi:10.7270/q20v8d3k

BindingDB Entry 50037959: Design and evaluation of naphthol- and carbazole-containing fluorescent sigma ligands as potential probes for receptor binding studies.

BindingDB (2012) · UC San Diego · doi:10.7270/q2sq917z

Untitled work

(1999) · doi:10.1002/(sici)1096-8628(19990319)83:3

Untitled work

Rankin, K. A., Mei, F., Kim, K., Shen, Y. A., Sylvester, S., Fung, A., Gallo, V., Fancy, S. P. J., & Green, P. E. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1475-18.2019

High affinity of sigma1‐binding sites for sterol isomerization inhibitors: evidence for a pharmacological relationship with the yeast sterol C8–C7 isomerase

Moebius, F. F., Reiter, R. J., Hanner, M., & Glossmann, H. H. (1997) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0701079 · Cited by 113 · see citing works

Yeast Sterol C8−C7 Isomerase: Identification and Characterization of a High-Affinity Binding Site for Enzyme Inhibitors

Moebius, F. F., Bermoser, K., Reiter, R. J., Hanner, M., & Glossmann, H. H. (1996) · Biochemistry · doi:10.1021/bi961996m · Cited by 69 · see citing works

Emopamil-binding Protein, a Mammalian Protein That Binds a Series of Structurally Diverse Neuroprotective Agents, Exhibits Δ8-Δ7 Sterol Isomerase Activity in Yeast

Silve, S., Dupuy, P.-H., Bouteiller, C. L., Kaghad, M., Chalon, P., Rahier, A., Taton, M., Lupker, J. H., Shire, D. J., & Loison, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22434 · Cited by 128 · see citing works

Isolation and characterization of an Arabidopsis thaliana C-8,7 sterol isomerase: functional and structural similarities to mammalian C-8,7 sterol isomerase/emopamil-binding protein

Grebenok, R. J., Ohnmeiss, T. E., Yamamoto, A., Huntley, E. D., Galbraith, D. W., & Penna, D. D. (1998) · Plant Molecular Biology · doi:10.1023/a:1006028623875 · Cited by 31 · see citing works

Novel 4-(4-Aryl)cyclohexyl-1-(2-pyridyl)piperazines as Δ8−Δ7Sterol Isomerase (Emopamil Binding Protein) Selective Ligands with Antiproliferative Activity

Berardi, F., Abate, C., Ferorelli, S., de Robertis, A. F., Leopoldo, M., Colabufo, N. A., Niso, M., & Perrone, R. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800965b · Cited by 47 · see citing works