Identification of a nuclear receptor that is activated by farnesol metabolites

The Steroid and Thyroid Hormone Receptor Superfamily

Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,442 · see citing works

Regulation of the mevalonate pathway

Goldstein, J. L., & Brown, M. S. (1990) · Nature · doi:10.1038/343425a0 · Cited by 5,394 · see citing works

Stimulation of adipogenesis in fibroblasts by PPARγ2, a lipid-activated transcription factor

Tontonoz, P., Hu, E., & Spiegelman, B. M. (1994) · Cell · doi:10.1016/0092-8674(94)90006-x · Cited by 3,533 · see citing works

Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators

Issemann, I., & Green, S. (1990) · Nature · doi:10.1038/347645a0 · Cited by 3,519 · see citing works

9-cis retinoic acid is a high affinity ligand for the retinoid X receptor

Heyman, R. A., Mangelsdorf, D. J., Dyck, J. A., Stein, R. B., Eichele, G., Evans, R. M., & Thaller, C. (1992) · Cell · doi:10.1016/0092-8674(92)90479-v · Cited by 1,780 · see citing works

Nuclear receptor that identifies a novel retinoic acid response pathway

Mangelsdorf, D. J., Ong, E. S., Dyck, J. A., & Evans, R. M. (1990) · Nature · doi:10.1038/345224a0 · Cited by 1,491 · see citing works

Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling

Kliewer, S. A., Umesono, K., Mangelsdorf, D. J., & Evans, R. M. (1992) · Nature · doi:10.1038/355446a0 · Cited by 1,489 · see citing works

9-Cis retinoic acid stereoisomer binds and activates the nuclear receptor RXRα

Levin, A. A., Sturzenbecker, L. J., Kazmer, S., Bosakowski, T., Huselton, C. A., Allenby, G., Speck, J., ratzeisen, C., Rosenberger, M., Lovey, A. J., et al. (1992) · Nature · doi:10.1038/355359a0 · Cited by 1,221 · see citing works

Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth.

Brown, M. S., & Goldstein, J. L. (1980) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42221-7 · Cited by 1,210 · see citing works

Characterization of three RXR genes that mediate the action of 9-cis retinoic acid.Preprint

Mangelsdorf, D. J., Borgmeyer, U., Heyman, R. A., Zhou, J. Y., Ong, E. S., Oro, A. E., Kakizuka, A., & Evans, R. M. (1992) · Genes & Development · doi:10.1101/gad.6.3.329 · Cited by 1,193 · see citing works

RXRβ: A coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements

Yu, V. C. K., Delsert, C., D, B. A. M., Holloway, J. M., Devary, O. V., Näär, A. M., Kim, S. Y., Boutin, J., Glass, C. K., & Rosenfeld, M. G. (1991) · Cell · doi:10.1016/0092-8674(91)90301-e · Cited by 1,183 · see citing works

Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently

Leid, M. E., Kastner, P., Lyons, R., Nakshatri, H., Saunders, M., Zacharewski, T. R., Chen, J.-Y., Staub, A., Garnier, J., Mader, S., et al. (1992) · Cell · doi:10.1016/0092-8674(92)90478-u · Cited by 1,166 · see citing works

SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis

Wang, X., Sato, R., Brown, M. S., Hua, X., & Goldstein, J. L. (1994) · Cell · doi:10.1016/0092-8674(94)90234-8 · Cited by 1,003 · see citing works

The drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily

Koelle, M. R., Talbot, W. S., Segraves, W. A., Bender, M. T., Cherbas, P. T., & Hogness, D. S. (1991) · Cell · doi:10.1016/0092-8674(91)90572-g · Cited by 978 · see citing works

Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors

Zhang, X.-K., Hoffmann, B., Tran, P., et al. (1992) · Nature · doi:10.1038/355441a0 · Cited by 963 · see citing works

Functional ecdysone receptor is the product of EcR and Ultraspiracle genes

Yao, T., FORMAN, B. M., Jiang, Z., Cherbas, L., Chen, J.-D., McKeown, M., Cherbas, P. T., & Evans, R. M. (1993) · Nature · doi:10.1038/366476a0 · Cited by 947 · see citing works

Fatty acids activate a chimera of the clofibric acid-activated receptor and the glucocorticoid receptor.

Göttlicher, M., Widmark, E., Li, Q., & Gustafsson, J.-Α. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4653 · Cited by 857 · see citing works

Multiplicity generates diversity in the retinoic acid signalling pathways

Leid, M., Kastner, P., & Chambon, P. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90014-z · Cited by 821 · see citing works

Differential Recognition of Target Genes by Nuclear Receptor Monomers, Dimers, and Heterodimers*

Glass, C. K. (1994) · Endocrine Reviews · doi:10.1210/edrv-15-3-391 · Cited by 820 · see citing works

Inhibition of purified p21 farnesyl:protein transferase by Cys-AAX tetrapeptides

Reiss, Y., Goldstein, J. L., Seabra, M. C., Casey, P. J., & Brown, M. S. (1990) · Cell · doi:10.1016/0092-8674(90)90242-7 · Cited by 815 · see citing works

Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation

Yao, T., Segraves, W. A., Oro, A. E., McKeown, M., & Evans, R. M. (1992) · Cell · doi:10.1016/0092-8674(92)90266-f · Cited by 716 · see citing works

Sequence dependence of protein isoprenylation

Moores, S. L., Schaber, M. D., Mosser, S. D., Rands, E., O'Hara, M. B., Garsky, V. M., Marshall, M. S., Pompliano, D. L., & Gibbs, W. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98729-6 · Cited by 574 · see citing works

Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle

Thomas, H. E., Stunnenberg, H. G., & Stewart, A. F. (1993) · Nature · doi:10.1038/362471a0 · Cited by 520 · see citing works

H‐2RIIBP (RXR beta) heterodimerization provides a mechanism for combinatorial diversity in the regulation of retinoic acid and thyroid hormone responsive genes.

Marks, M. S., Hallenbeck, P. L., Nagata, T., Segars, J. H., Appella, E., Nikodem, V. M., & Ozato, K. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05187.x · Cited by 451 · see citing works

Regulation of retinoid signalling by receptor polarity and allosteric control of ligand binding

Kurokawa, R., DiRenzo, J., Boehm, M., Sugarman, J., Gloss, B., Rosenfeld, M. G., Heyman, R. A., & Glass, C. K. (1994) · Nature · doi:10.1038/371528a0 · Cited by 429 · see citing works

MINIREVIEW: Interactions Among a Subfamily of Nuclear Hormone Receptors: The Regulatory Zipper Model

FORMAN, B. M., & Samuels, H. H. (1990) · Molecular Endocrinology · doi:10.1210/mend-4-9-1293 · Cited by 404 · see citing works

Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors

Seol, W., Choi, H.-S., & Moore, D. D. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.1.7760852 · Cited by 389 · see citing works

Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme.

Nakanishi, M., Goldstein, J. L., & Brown, M. S. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68397-8 · Cited by 335 · see citing works

RARs and RXRs: evidence for two autonomous transactivation functions (AF‐1 and AF‐2) and heterodimerization in vivo.

Nagpal, S., Friant, S., Nakshatri, H., & Chambon, P. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05889.x · Cited by 300 · see citing works

The Metabolic Code

Tomkins, G. M. (1975) · Science · doi:10.1126/science.169570 · Cited by 238 · see citing works

Alpha and beta thyroid hormone receptor (TR) gene expression during auditory neurogenesis: evidence for TR isoform-specific transcriptional regulation in vivo.

Bradley, D. J., Towle, H. C., & Young, W. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.2.439 · Cited by 213 · see citing works

Differential recognition of target genes by nuclear receptor monomers, dimers, and heterodimers

Glass, C. K. (1994) · Endocrine Reviews · doi:10.1210/er.15.3.391 · Cited by 201 · see citing works

Sterols and Bile Acids

(1985) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)x6035-1 · Cited by 188 · see citing works

Peroxisome proliferator-activated receptors: finding the orphan a home

Green, S., & Wahli, W. (1994) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(94)90294-1 · Cited by 157 · see citing works

Control of Neuronal Gene Expression

Sutcliffe, J. G., Milner, R. J., Gottesfeld, J. M., et al. (1984) · Science · doi:10.1126/science.6474179 · Cited by 126 · see citing works

cDNA cloning of MEV, a mutant protein that facilitates cellular uptake of mevalonate, and identification of the point mutation responsible for its gain of function

Kim, C. M., Goldstein, J. L., & Brown, M. S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50064-8 · Cited by 124 · see citing works

Heterodimerization of thyroid hormone (TH) receptor with H-2RIIBP (RXR beta) enhances DNA binding and TH-dependent transcriptional activation.

Hallenbeck, P. L., Marks, M. S., Lippoldt, R. E., Ozato, K., & Nikodem, V. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5572 · Cited by 83 · see citing works

Ras (CXXX) and Rab (CC/CXC) prenylation signal sequences are unique and functionally distinct.

Khosravi‐Far, R., Clark, G. J., Abe, K., et al. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35774-0 · Cited by 77 · see citing works

Editorial: Did Eucaryotic Steroid Receptors Evolve from Intracrine Gene Regulators?*

O’Malley, B. W. (1989) · Endocrinology · doi:10.1210/endo-125-3-1119 · Cited by 68 · see citing works

Biosynthesis of Cholesterol

Werthessen, N. T., & Schwenk, E. (1952) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1952.171.1.55 · Cited by 68 · see citing works

The in vitro metabolism of mevalonate by sterol and non-sterol pathways.

Righetti, M., Wiley, M. H., Murrill, P. A., et al. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33546-9 · Cited by 62 · see citing works

The quantitative role of the kidneys in the in vivo metabolism of mevalonate.

Wiley, M. H., Howton, M. M., & Siperstein, M. D. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32752-7 · Cited by 60 · see citing works

Mevalonate Metabolism: Role of Kidneys

Edmond, J., Fogelman, A. M., & Popják, G. J. (1976) · Science · doi:10.1126/science.935865 · Cited by 58 · see citing works

Purified yeast protein farnesyltransferase is structurally and functionally similar to its mammalian counterpart

Gomez, R. P., Goodman, L., Tripathy, S. K., et al. (1993) · Biochemical Journal · doi:10.1042/bj2890025 · Cited by 56 · see citing works

Synthesis of terpenes containing the bicyclo[3.1.1]heptane ring system by the intramolecular [2 + 2] cycloaddition reaction of vinylketenes with alkenes. Preparation of chrysanthenone, .beta.-pinene, .beta.-cis-bergamotene, .beta.-trans-bergamotene, .beta.-copaene, and .beta.-ylangene and lemnalol

Kulkarni, Y. S., Niwa, M., Ron, E., et al. (1987) · The Journal of Organic Chemistry · doi:10.1021/jo00384a035 · Cited by 53 · see citing works

Diversity and unity in the nuclear hormone receptors: a terpenoid receptor superfamily.

Dd, M. (1990) · PubMed · Cited by 37 · see citing works

Identification of a nuclear receptor for bile acids

Makishima, M., Okamoto, A. Y., Repa, J. J., Tu, H., Learned, R. M., Luk, A., Hull, M. V., Lustig, K. D., Mangelsdorf, D. J., & Shan, B. (1999) · Science · doi:10.1126/science.284.5418.1362 · Cited by 2,714 · see citing works

Hypolipidemic drugs, polyunsaturated fatty acids, and eicosanoids are ligands for peroxisome proliferator-activated receptors α and δ

Forman, B. M., Chen, J., & Evans, R. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4312 · Cited by 2,116 · see citing works

Obesity and inflammation: the linking mechanism and the complications

Ellulu, M. S., Patimah, I., Khaza’ai, H., Rahmat, A., & Abed, Y. (2017) · Archives of Medical Science · doi:10.5114/aoms.2016.58928 · Cited by 1,982 · see citing works

Bile acid-microbiota crosstalk in gastrointestinal inflammation and carcinogenesis

Jia, W., Xie, G., & Jia, W. (2018) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2017.119 · Cited by 1,924 · see citing works

A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis

Goodwin, B., Jones, S. A., Price, R. R., Watson, M. A., McKee, D. D., Moore, L. B., Galardi, C., Wilson, J. G., Lewis, M. C., Roth, M. E., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00051-4 · Cited by 1,940 · see citing works

Targeted Disruption of the Nuclear Receptor FXR/BAR Impairs Bile Acid and Lipid Homeostasis

Sinal, C. J., Tohkin, M., Miyata, M., Ward, J. M., Lambert, G., & Gonzalez, F. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00062-3 · Cited by 1,819 · see citing works

Role of Bile Acids and Bile Acid Receptors in Metabolic Regulation

Lefebvre, P., Cariou, B., Lien, F., Kuipers, F., & Staels, B. (2009) · Physiological Reviews · doi:10.1152/physrev.00010.2008 · Cited by 1,678 · see citing works

Endogenous Bile Acids Are Ligands for the Nuclear Receptor FXR/BAR

Wang, H., Chen, J., Hollister, K., Sowers, L. C., & Forman, B. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80348-2 · Cited by 1,636 · see citing works

Molecular Basis for Feedback Regulation of Bile Acid Synthesis by Nuclear Receptors

Lu, T. T., Makishima, M., Repa, J. J., Schoonjans, K., Kerr, T. A., Auwerx, J., & Mangelsdorf, D. J. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00050-2 · Cited by 1,487 · see citing works

From NASH to HCC: current concepts and future challenges

Anstee, Q. M., Reeves, H. L., Kotsiliti, E., Govaere, O., & Heikenwalder, M. (2019) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-019-0145-7 · Cited by 1,392 · see citing works

Targeting bile‐acid signalling for metabolic diseases

Thomas, C., Pellicciari, R., Pruzanski, M., Auwerx, J., & Schoonjans, K. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2619 · Cited by 1,422 · see citing works

Recent advances in 2D and 3D in vitro systems using primary hepatocytes, alternative hepatocyte sources and non-parenchymal liver cells and their use in investigating mechanisms of hepatotoxicity, cell signaling and ADME

Godoy, P., Hewitt, N. J., Albrecht, U., Andersen, M. E., Ansari, N., Bhattacharya, S., Bode, J. G., Bolleyn, J., Borner, C., Böttger, J., et al. (2013) · Archives of Toxicology · doi:10.1007/s00204-013-1078-5 · Cited by 1,280 · see citing works

Pleiotropic Roles of Bile Acids in Metabolism

de Aguiar Vallim, T. Q., Tarling, E. J., & Edwards, P. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.013 · Cited by 1,209 · see citing works

Regulation of antibacterial defense in the small intestine by the nuclear bile acid receptor

Inagaki, T., Moschetta, A., Lee, Y.-K., Peng, L., Zhao, G., Downes, M., Yu, R. T., Shelton, J. M., Richardson, J. A., Repa, J. J., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509592103 · Cited by 1,164 · see citing works

Bile acid signaling in metabolic disease and drug therapy

Li, T., & Chiang, J. Y. L. (2014) · Pharmacological Reviews · doi:10.1124/pr.113.008201 · Cited by 935 · see citing works

Regulation of multidrug resistance-associated protein 2 (ABCC2) by the nuclear receptors pregnane X receptor, farnesoid X-activated receptor, and constitutive androstane receptor

Kast, H. R., Goodwin, B., Tarr, P. T., Jones, S. A., Anisfeld, A. M., Stoltz, C. M., Tontonoz, P., Kliewer, S., Willson, T. M., & Edwards, P. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109326200 · Cited by 916 · see citing works

New insecticides with ecdysteroidal and juvenile hormone activity

Dhadialla, T. S., Carlson, G. R., & Le, D. P. (1998) · Annual Review of Entomology · doi:10.1146/annurev.ento.43.1.545 · Cited by 912 · see citing works

Dietary metabolism, the gut microbiome, and heart failure

Tang, W. H. W., Li, D. Y., & Hazen, S. L. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0108-7 · Cited by 789 · see citing works

Transcriptional integration of metabolism by the nuclear sterol-activated receptors LXR and FXR

Calkin, A. C., & Tontonoz, P. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3312 · Cited by 779 · see citing works

Intestinal FXR agonism promotes adipose tissue browning and reduces obesity and insulin resistance

Fang, S., Suh, J. M., Reilly, S. M., Yu, E., Osborn, O., Lackey, D., Yoshihara, E., Perino, A., Jacinto, S., Lukasheva, Y., et al. (2015) · Nature Medicine · doi:10.1038/nm.3760 · Cited by 738 · see citing works

Systemic gut microbial modulation of bile acid metabolism in host tissue compartments

Swann, J. R., Want, E. J., Geier, F. M., Spagou, K., Wilson, I. D., Sidaway, J. E., Nicholson, J. K., & Holmes, E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006734107 · Cited by 726 · see citing works

Bile acid receptors as targets for drug development

Schaap, F. G., Trauner, M., & Jansen, P. L. M. (2014) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2013.151 · Cited by 696 · see citing works

The bile acid receptor FXR is a modulator of intestinal innate immunity

Vavassori, P., Mencarelli, A., Renga, B., Distrutti, E., & Fiorucci, S. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803978 · Cited by 655 · see citing works

Evolution of the nuclear receptor superfamily: early diversification from an ancestral orphan receptor

Laudet, V (1997) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0190207 · Cited by 557 · see citing works

New paradigms in the treatment of hepatic cholestasis: from UDCA to FXR, PXR and beyond

Beuers, U., Trauner, M., Jansen, P., & Poupon, R. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.02.023 · Cited by 537 · see citing works

Orphan Nuclear Receptors: Shifting Endocrinology into Reverse

Kliewer, S. A., Lehmann, J. M., & Willson, T. M. (1999) · Science · doi:10.1126/science.284.5415.757 · Cited by 499 · see citing works

The nuclear receptor SHP mediates inhibition of hepatic stellate cells by FXR and protects against liver fibrosis

Fiorucci, S., Antonelli, E., Rizzo, G., Renga, B., Mencarelli, A., Riccardi, L., Orlandi, S., Pellicciari, R., & Morelli, A. (2004) · Gastroenterology · doi:10.1053/j.gastro.2004.08.001 · Cited by 472 · see citing works

Molecular physiology of bile acid signaling in health, disease, and aging

Perino, A., Demagny, H., Velazquez-Villegas, L., & Schoonjans, K. (2021) · Physiological Reviews · doi:10.1152/physrev.00049.2019 · Cited by 481 · see citing works

Interactions between Bacteria and Bile Salts in the Gastrointestinal and Hepatobiliary Tracts

Urdaneta, V., & Casadesús, J. (2017) · Frontiers in Medicine · doi:10.3389/fmed.2017.00163 · Cited by 449 · see citing works

The bile acid membrane receptor TGR5 as an emerging target in metabolism and inflammation

Pols, T. W. H., Noriega, L. G., Nomura, M., Auwerx, J., & Schoonjans, K. (2011) · Journal of Hepatology · doi:10.1016/j.jhep.2010.12.004 · Cited by 454 · see citing works

Bile Acids as Hormones: The FXR-FGF15/19 Pathway

Kliewer, S. A., & Mangelsdorf, D. J. (2015) · Digestive Diseases · doi:10.1159/000371670 · Cited by 424 · see citing works

Signalling cognition: The gut microbiota and hypothalamic-pituitary-adrenal axis

Rusch, J. A., Layden, B. T., & Dugas, L. R. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1130689 · Cited by 415 · see citing works

FXR: a metabolic regulator and cell protector

Wang, Y.-D., Chen, W.-D., Moore, D. D., & Huang, W. (2008) · Cell Research · doi:10.1038/cr.2008.289 · Cited by 389 · see citing works

Immune regulation by microbiome metabolites

Kim, C. H. (2018) · Immunology · doi:10.1111/imm.12930 · Cited by 375 · see citing works

FXR, a multipurpose nuclear receptor

Lee, F. Y., Lee, H., Hubbert, M. L., Edwards, P. A., & Zhang, Y. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.08.002 · Cited by 344 · see citing works

Complementary roles of farnesoid X receptor, pregnane X receptor, and constitutive androstane receptor in protection against bile acid toxicity

Guo, G. L., Lambert, G., Negishi, M., Ward, J. M., Brewer, H. B., Kliewer, S. A., Gonzalez, F. J., & Sinal, C. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307145200 · Cited by 312 · see citing works

Primary biliary cholangitis: pathogenesis and therapeutic opportunities

Gulamhusein, A. F., & Hirschfield, G. M. (2020) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-019-0226-7 · Cited by 308 · see citing works

Farnesoid X receptor agonist WAY-362450 attenuates liver inflammation and fibrosis in murine model of non-alcoholic steatohepatitis

Zhang, S., Wang, J., Liu, Q., & Harnish, D. C. (2009) · Journal of Hepatology · doi:10.1016/j.jhep.2009.03.025 · Cited by 290 · see citing works

Apolipoprotein C-III: understanding an emerging cardiovascular risk factor

Ooi, E. M. M., Barrett, P. H. R., Chan, D. C., & Watts, G. F. (2008) · Clinical Science · doi:10.1042/cs20070308 · Cited by 282 · see citing works

Coordinate transcriptional regulation of bile acid homeostasis and drug metabolism

Eloranta, J. J., & Kullak-Ublick, G. A. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.09.019 · Cited by 260 · see citing works

Cholic acid mediates negative feedback regulation of bile acid synthesis in mice

Li-Hawkins, J., Gåfvels, M., Olin, M., Lund, E. G., Andersson, U., Schuster, G., Björkhem, I., Russell, D. W., & Eggertsen, G. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216309 · Cited by 227 · see citing works

Metabolic Messengers: bile acids

Perino, A., & Schoonjans, K. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00559-z · Cited by 223 · see citing works

Intestinal absorption of bile acids in health and disease

Ticho, A. L., Malhotra, P., Dudeja, P. K., Gill, R. K., & Alrefai, W. A. (2019) · Comprehensive physiology · doi:10.1002/cphy.c190007 · Cited by 215 · see citing works

The Human Apolipoprotein AV Gene Is Regulated by Peroxisome Proliferator-activated Receptor-α and Contains a Novel Farnesoid X-activated Receptor Response Element

Prieur, X., Coste, H., & Rodríguez, J. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301302200 · Cited by 194 · see citing works

The bile acid membrane receptor TGR5: a valuable metabolic target

Pols, T. W. H., Noriega, L. G., Nomura, M., Auwerx, J., & Schoonjans, K. (2011) · Digestive Diseases · doi:10.1159/000324126 · Cited by 185 · see citing works

Molecular basis of bile acid-FXR-FGF15/19 signaling axis

Katafuchi, T., & Makishima, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116046 · Cited by 193 · see citing works

A farnesoid x receptor-small heterodimer partner regulatory cascade modulates tissue metalloproteinase inhibitor-1 and matrix metalloprotease expression in hepatic stellate cells and promotes resolution of liver fibrosis

Fiorucci, S., Rizzo, G., Antonelli, E., Renga, B., Mencarelli, A., Riccardi, L., Orlandi, S., Pruzanski, M., Morelli, A., & Pellicciari, R. (2005) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.084905 · Cited by 183 · see citing works

Bile acids and their receptors

Martinot, E., Sèdes, L., Baptissart, M., Lobaccaro, J.-M., Caira, F., Beaudoin, C., & Volle, D. H. (2017) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2017.01.006 · Cited by 162 · see citing works

Identification of Farnesoid X Receptor β as a Novel Mammalian Nuclear Receptor Sensing Lanosterol

Otte, K., Kranz, H., Kober, I., Thompson, P., Hoefer, M., Haubold, B., Remmel, B., Voss, H., Kaiser, C., Albers, M., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.864-872.2003 · Cited by 176 · see citing works

Cross-Talk between Farnesoid-X-Receptor (FXR) and Peroxisome Proliferator-Activated Receptor γ Contributes to the Antifibrotic Activity of FXR Ligands in Rodent Models of Liver Cirrhosis

Fiorucci, S., Rizzo, G., Antonelli, E., Renga, B., Mencarelli, A., Riccardi, L., Morelli, A., Pruzanski, M., & Pellicciari, R. (2005) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.085597 · Cited by 177 · see citing works

Farnesoid x receptor ligands inhibit vascular smooth muscle cell inflammation and migration

Li, Y. T. Y., Swales, K. E., Thomas, G. J., Warner, T. D., & Bishop-Bailey, D. (2007) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.107.152694 · Cited by 171 · see citing works

How bile acids and the microbiota interact to shape host immunity

Lee, M. H., Nuccio, S.-P., Mohanty, I., Hagey, L. R., Dorrestein, P. C., Chu, H., & Raffatellu, M. (2024) · Nature Reviews Immunology · doi:10.1038/s41577-024-01057-x · Cited by 143 · see citing works

The gut microbiota as a therapeutic target in IBD and metabolic disease: a role for the bile acid receptors FXR and TGR5

Baars, A., Oosting, A., Knol, J., Garssen, J., & Van Bergenhenegouwen, J. (2015) · Microorganisms · doi:10.3390/microorganisms3040641 · Cited by 135 · see citing works

Results from a new efficacy and safety analysis of the REGENERATE trial of obeticholic acid for treatment of pre-cirrhotic fibrosis due to non-alcoholic steatohepatitis

Sanyal, A. J., Ratziu, V., Loomba, R., Anstee, Q. M., Kowdley, K. V., Rinella, M. E., Sheikh, M. Y., Trotter, J. F., Knapple, W., Lawitz, E. J., et al. (2023) · Journal of Hepatology · doi:10.1016/j.jhep.2023.07.014 · Cited by 137 · see citing works

Short-chain fatty acids, secondary bile acids and indoles: gut microbial metabolites with effects on enteroendocrine cell function and their potential as therapies for metabolic disease

Masse, K. E., & Lu, V. B. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1169624 · Cited by 120 · see citing works

Identification of Novel Pathways That Control Farnesoid X Receptor-mediated Hypocholesterolemia

Zhang, Y., Yin, L., Anderson, J., Ma, H., Gonzalez, F. J., Willson, T. M., & Edwards, P. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083899 · Cited by 112 · see citing works

Deletion of mouse FXR gene disturbs multiple neurotransmitter systems and alters neurobehavior

Huang, F., Wang, T., Lan, Y., Yang, L., Pan, W., Zhu, Y., Lv, B., Wei, Y., Shi, H., Wu, H., et al. (2015) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2015.00070 · Cited by 109 · see citing works

Role of TGR5 (GPBAR1) in Liver Disease

Häussinger, D., & Keitel, V. (2018) · Seminars in Liver Disease · doi:10.1055/s-0038-1669940 · Cited by 106 · see citing works

Genome–microbiome interplay provides insight into the determinants of the human blood metabolome

Diener, C., Dai, C. L., Wilmanski, T., Baloni, P., Smith, B., Rappaport, N., Hood, L., Magis, A. T., & Gibbons, S. M. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00670-1 · Cited by 102 · see citing works

Nuclear receptors linking metabolism, inflammation, and fibrosis in nonalcoholic fatty liver disease

Puengel, T., Liu, H., Guillot, A., Heymann, F., Tacke, F., & Peiseler, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052668 · Cited by 95 · see citing works

Roles of microRNA-29a in the antifibrotic effect of farnesoid X receptor in hepatic stellate cells

Li, J., Zhang, Y., Kuruba, R., Gao, X., Gandhi, C. R., Xie, W., & Li, S. (2011) · Molecular Pharmacology · doi:10.1124/mol.110.068247 · Cited by 78 · see citing works

Role of bile acids in the regulation of the metabolic pathways

Taoka, H., Yokoyama, Y., Morimoto, K., Kitamura, N., Tanigaki, T., Takashina, Y., Tsubota, K., & Watanabe, M. (2016) · World Journal of Diabetes · doi:10.4239/wjd.v7.i13.260 · Cited by 80 · see citing works

FXR ligands protect against hepatocellular inflammation via SOCS3 induction

Xu, Z., Huang, G., Gong, W., Zhou, P., Zhao, Y., Zhang, Y., Zeng, Y., Gao, M., Pan, Z., & He, F. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.04.015 · Cited by 71 · see citing works

Nuclear Receptors in Nonalcoholic Fatty Liver Disease

López-Velázquez, J. A., Carrillo-Córdova, L. D., Chávez-Tapia, N. C., Uribe, M., & Méndez-Sánchez, N. (2012) · Journal of Lipids · doi:10.1155/2012/139875 · Cited by 48 · see citing works

Novel substituted isoxazole FXR agonists with cyclopropyl, hydroxycyclobutyl and hydroxyazetidinyl linkers: understanding and improving key determinants of pharmacological properties

Kinzel, O., Steeneck, C., Schlüter, T., Schulz, A., Gege, C., Hahn, U., Hambruch, E., Hornberger, M., Spalwisz, A., Frick, K., et al. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.05.070 · Cited by 35 · see citing works

Bacterial metabolites directly modulate farnesoid X receptor activity

Zhang, X., Osaka, T., & Tsuneda, S. (2015) · Nutrition & Metabolism · doi:10.1186/s12986-015-0045-y · Cited by 34 · see citing works

Bile acids and glucocorticoid metabolism in health and disease

Theiler-Schwetz, V., Zaufel, A., Schlager, H., Obermayer-Pietsch, B., Fickert, P., & Zollner, G. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.08.001 · Cited by 31 · see citing works

Untitled work

Berry (2007) · doi:10.1155/2007/73256 · Cited by 28 · see citing works

Therapeutic implications of obeticholic acid, a farnesoid X receptor agonist, in the treatment of liver fibrosis

Azizsoltani, A., Niknam, B., Taghizadeh-Teymorloei, M., Ghoodjani, E., Dianat-Moghadam, H., & Alizadeh, E. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118249 · Cited by 15 · see citing works

Advancing care in primary biliary cholangitis: emerging insights and novel therapies

Vögelin, M., & Kremer, A. E. (2025) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2025.2516622 · Cited by 5 · see citing works

Retinoid X receptor is an auxiliary protein for thyroid hormone and retinoic acid receptors

Zhang, X.-K., Hoffmann, B., Tran, P., et al. (1992) · Nature · doi:10.1038/355441a0 · Cited by 963 · see citing works

Mutations in Retinoid X Receptor That Impair Heterodimerization with Specific Nuclear Hormone Receptor

Lee, S., Lee, B., & Lee, J. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006418200 · Cited by 13 · see citing works

Retinoid X Receptor Regulates Nur77/Thyroid Hormone Receptor 3-Dependent Apoptosis by Modulating Its Nuclear Export and Mitochondrial Targeting

Cao, X., Liu, W., Lin, F., Li, H., Kolluri, S. K., Lin, B., Han, Y.-H., Dawson, M. I., & Zhang, X.-K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.22.9705-9725.2004 · Cited by 177 · see citing works

Retinoid X receptor isoforms a and p differentially regulate 3,5,3′‐triiodothyronine‐induced transcription

Rhee, M. (1998) · Korean Journal of Biological Sciences · doi:10.1080/12265071.1998.9647450

Retinoid X receptors: X-ploring their (patho)physiological functions

Szántó, A., Narkar, V. A., Shen, Q., Uray, I. P., Davies, P. J., & Nagy, L. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401533 · Cited by 304 · see citing works