Structural and functional insights into nuclear receptor signaling

The nuclear receptor superfamily: the second decade

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Molecular basis of agonism and antagonism in the oestrogen receptor

Brzozowski, A. M., Pike, A. C. W., Dauter, Z., Hubbard, R. E., Bonn, T., Engström, O., Öhman, L., Greene, G. L., Gustafsson, J.-Å., & Carlquist, M. (1997) · Nature · doi:10.1038/39645 · Cited by 3,355 · see citing works

The coregulator exchange in transcriptional functions of nuclear receptors

Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233 · see citing works

Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ

Nolte, R. T., Wisely, G. B., Westin, S. K., Cobb, J. E., Lambert, M. H., Kurokawa, R., Rosenfeld, M. G., Willson, T. M., Glass, C. K., & Milburn, M. V. (1998) · Nature · doi:10.1038/25931 · Cited by 1,955 · 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

An oxysterol signalling pathway mediated by the nuclear receptor LXRα

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Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α

Bourguet, W., Ruff, M., Chambon, P., Gronemeyer, H., & Moras, D. (1995) · Nature · doi:10.1038/375377a0 · Cited by 1,177 · see citing works

Molecular recognition of fatty acids by peroxisome proliferator-activated receptors

Xu, H. E., Lambert, M. H., Montana, V. G., Parks, D. J., Blanchard, S. G., Brown, P. J., Sternbach, D. D., Lehmann, J. M., Wisely, G. B., Willson, T. M., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80467-0 · Cited by 1,169 · see citing works

Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid

Renaud, J., Rochel, N., Ruff, M., Vivat, V., Chambon, P., Gronemeyer, H., & Moras, D. (1995) · Nature · doi:10.1038/378681a0 · Cited by 1,098 · see citing works

Structure of the ligand‐binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist

Pike, A. C. W., Brzozowski, A. M., Hubbard, R. E., Bonn, T., Thorsell, A., Engström, O., Ljunggren, J., Gustafsson, J., & Carlquist, M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.17.4608 · Cited by 987 · see citing works

A structural role for hormone in the thyroid hormone receptor

Wagner, R. L., Apriletti, J. W., McGrath, M. E., West, B. L., Baxter, J. D., & Fletterick, R. J. (1995) · Nature · doi:10.1038/378690a0 · Cited by 928 · see citing works

Structure and specificity of nuclear receptor–coactivator interactionsPreprint

Darimont, B. D., Wagner, R. L., Apriletti, J. W., Stallcup, M. R., Kushner, P. J., Baxter, J. D., Fletterick, R. J., & Yamamoto, K. R. (1998) · Genes & Development · doi:10.1101/gad.12.21.3343 · Cited by 921 · see citing works

Orphan Nuclear Receptors: From Gene to Function

Giguère, V. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.5.0378 · Cited by 848 · see citing works

The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand

Rochel, N., Wurtz, J. M., Mitschler, A., Klaholz, B., & Moras, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80413-x · Cited by 842 · see citing works

Crystal Structure of the Glucocorticoid Receptor Ligand Binding Domain Reveals a Novel Mode of Receptor Dimerization and Coactivator Recognition

Bledsoe, R. K., Montana, V. G., Stanley, T. B., Delves, C. J., Apolito, C. J., McKee, D. D., Consler, T. G., Parks, D. J., Stewart, E. L., Willson, T. M., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00817-6 · Cited by 818 · see citing works

Structure of the intact PPAR-γ–RXR-α nuclear receptor complex on DNA

Chandra, V., Huang, P., Hamuro, Y., Raghuram, S., Wang, Y., Burris, T. P., & Rastinejad, F. (2008) · Nature · doi:10.1038/nature07413 · Cited by 808 · see citing works

The Human Nuclear Xenobiotic Receptor PXR: Structural Determinants of Directed Promiscuity

Watkins, R. E., Wisely, G. B., Moore, L. B., Collins, J. L., Lambert, M. H., Williams, S. P., Willson, T. M., Kliewer, S. A., & Redinbo, M. R. (2001) · Science · doi:10.1126/science.1060762 · Cited by 760 · see citing works

Rev-erbα, a Heme Sensor That Coordinates Metabolic and Circadian Pathways

Yin, L., Wu, N., Curtin, J. C., Qatanani, M., Szwergold, N. R., Reid, R. A., Waitt, G. M., Parks, D. J., Pearce, K. H., Wisely, G. B., et al. (2007) · Science · doi:10.1126/science.1150179 · Cited by 707 · see citing works

Atomic structure of progesterone complexed with its receptor

Williams, S. P., & Sigler, P. B. (1998) · Nature · doi:10.1038/30775 · Cited by 659 · see citing works

Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARα

Xu, H. E., Stanley, T. B., Montana, V. G., Lambert, M. H., Shearer, B. G., Cobb, J. E., McKee, D. D., Galardi, C. M., Plunket, K. D., Nolte, R. T., et al. (2002) · Nature · doi:10.1038/415813a · Cited by 618 · see citing works

Wilms’ tumor 1 and Dax-1 modulate the orphan nuclear receptor SF-1 in sex-specific gene expression.

Nachtigal, M. W., Hirokawa, Y., Enyeart-VanHouten, D. L., Flanagan, J. N., Hammer, G. D., & Ingraham, H. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81172-1 · Cited by 591 · see citing works

Structure and function of Nurr1 identifies a class of ligand-independent nuclear receptors

Wang, Z., Benoit, G., Liu, J., Prasad, S., Aarnisalo, P., Liu, X., Xu, H., Walker, N. P. C., & Perlmann, T. (2003) · Nature · doi:10.1038/nature01645 · Cited by 583 · see citing works

Identification of heme as the ligand for the orphan nuclear receptors REV-ERBα and REV-ERBβ

Raghuram, S., Stayrook, K. R., Huang, P., Rogers, P. M., Nosie, A. K., McClure, D. B., Burris, L. L., Khorasanizadeh, S., Burris, T. P., & Rastinejad, F. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1344 · Cited by 560 · see citing works

Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors

Xu, H. E., Lambert, M. H., Montana, V. G., Plunket, K. D., Moore, L. B., Collins, J. L., Oplinger, J. A., Kliewer, S. A., Gampe, R. T., McKee, D. D., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241410198 · Cited by 541 · 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

Flexible ligand docking to multiple receptor conformations: a practical alternative

Totrov, M., & Abagyan, R. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.01.004 · Cited by 497 · see citing works

A New Orphan Member of the Nuclear Hormone Receptor Superfamily That Interacts with a Subset of Retinoic Acid Response Elements

Baes, M. I., Gulick, T., Choi, H.-S., Martinoli, M., Simha, D., & Moore, D. D. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.3.1544 · Cited by 492 · see citing works

Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone

Sack, J. S., Kish, K. F., Wang, C., Attar, R. M., Kiefer, S. E., An, Y., Wu, G. Y., Scheffler, J. E., Salvati, M. E., Krystek, S. R., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081565498 · Cited by 491 · see citing works

Nuclear Receptor Coregulators: Judges, Juries, and Executioners of Cellular Regulation

Lonard, D. M., & O’Malley, B. W. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.012 · Cited by 489 · see citing works

Peroxisome Proliferator-activated Receptor Coactivator-1α (PGC-1α) Coactivates the Cardiac-enriched Nuclear Receptors Estrogen-related Receptor-α and -γ

Huss, J. M., Kopp, R. P., & Kelly, D. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206324200 · Cited by 480 · see citing works

Orphan Nuclear Receptors: From Gene to Function

Giguère, V. (1999) · Endocrine Reviews · doi:10.1210/er.20.5.689 · Cited by 423 · see citing works

Crystal Structure of a Heterodimeric Complex of RAR and RXR Ligand-Binding Domains

Bourguet, W., Vivat, V., Wurtz, J., Chambon, P., Gronemeyer, H., & Moras, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80424-4 · Cited by 405 · see citing works

Structural Analyses Reveal Phosphatidyl Inositols as Ligands for the NR5 Orphan Receptors SF-1 and LRH-1

Krylova, I. N., Sablin, E. P., Moore, J. M. R., Xu, R. X., Waitt, G. M., MacKay, J. A., JUZUMIENE, D. I., Bynum, J. M., Madauss, K. P., Montana, V. G., et al. (2005) · Cell · doi:10.1016/j.cell.2005.01.024 · Cited by 405 · see citing works

A Chemical, Genetic, and Structural Analysis of the Nuclear Bile Acid Receptor FXR

Downes, M., Verdecia, M. A., Roecker, A. J., Hughes, R. O., Hogenesch, J. B., Kast-Woelbern, H. R., Bowman, M. E., Ferrer, J.-L., Anisfeld, A. M., Edwards, P. A., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00104-7 · Cited by 392 · see citing works

Cytosporone B is an agonist for nuclear orphan receptor Nur77

Zhan, Y.-Y., Du, X., Chen, H., Liu, J., Zhao, B., Huang, D., Li, G., Xu, Q., Zhang, M., Weimer, B. C., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.106 · Cited by 361 · see citing works

Interdomain communication regulating ligand binding by PPAR-γ

Shao, D., Rangwala, S. M., Bailey, S., Krakow, S. L., Reginato, M., & Lazar, M. (1998) · Nature · doi:10.1038/24634 · Cited by 347 · see citing works

Structural Basis for Bile Acid Binding and Activation of the Nuclear Receptor FXR

Mi, L.-Z., Devarakonda, S., Harp, J. M., Han, Q., Pellicciari, R., Willson, T. M., Khorasanizadeh, S., & Rastinejad, F. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00112-6 · Cited by 315 · see citing works

Hepatocyte nuclear factor 4 is a transcription factor that constitutively binds fatty acids

Wisely, G. B., Miller, A. B., Davis, R. G., Thornquest, A. D., Johnson, R., Spitzer, T., Sefler, A., Shearer, B., Moore, J. T., Miller, A. B., et al. (2002) · Structure · doi:10.1016/s0969-2126(02)00829-8 · Cited by 311 · see citing works

Nuclear Receptor Coregulators and Human Disease

Lonard, D. M., Lanz, R. B., & O’Malley, B. W. (2007) · Endocrine Reviews · doi:10.1210/er.2007-0012 · Cited by 303 · see citing works

X-Ray Structure of the hRORα LBD at 1.63 Å

Kallen, J. A., Schlaeppi, J.-M., Bitsch, F., Geisse, S., Geiser, M., Delhon, I., & Fournier, B. (2002) · Structure · doi:10.1016/s0969-2126(02)00912-7 · Cited by 300 · see citing works

Structural and Functional Evidence for Ligand-Independent Transcriptional Activation by the Estrogen-Related Receptor 3

Greschik, H., Wurtz, J., Cianférani, S., Bourguet, W., DORSSELAER, A. V., Moras, D., & Renaud, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00444-6 · Cited by 292 · see citing works

Structural Basis for Androgen Receptor Interdomain and Coactivator Interactions Suggests a Transition in Nuclear Receptor Activation Function Dominance

He, B., Gampe, R. T., Kole, A. J., Hnat, A. T., Stanley, T. B., An, G., Stewart, E. L., Kalman, R. I., Minges, J. T., & Wilson, E. M. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.036 · Cited by 291 · see citing works

Nuclear-receptor interactions on DNA-response elements

Khorasanizadeh, S., & Rastinejad, F. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01800-x · Cited by 288 · see citing works

The BRG1 transcriptional coregulator

Trotter, K. W., & Archer, T. (2008) · Nuclear Receptor Signaling · doi:10.1621/nrs.06004 · Cited by 287 · see citing works

Crystal Structure of the HNF4α Ligand Binding Domain in Complex with Endogenous Fatty Acid Ligand

Dhe‐Paganon, S., Duda, K. M., Iwamoto, M. A., Chi, Y., & Shoelson, S. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200420200 · Cited by 287 · see citing works

Ligand control of coregulator recruitment to nuclear receptors.

Nettles, K., & Greene, G. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.66.032802.154710 · Cited by 283 · see citing works

Crystal structure of the heterodimeric complex of LXRα and RXRβ ligand‐binding domains in a fully agonistic conformation

Svensson, S., Östberg, T., Jacobsson, M., Norström, C., Stefansson, K., Hallén, D., Johansson, I. C., Zachrisson, K., Ogg, D., & Jendeberg, L. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg456 · Cited by 281 · see citing works

Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor

Billas, I. M. L., Iwema, T., Garnier, J., Mitschler, A., Rochel, N., & Moras, D. (2003) · Nature · doi:10.1038/nature02112 · Cited by 254 · see citing works

Structural Basis for an Unexpected Mode of SERM-Mediated ER Antagonism

Wu, Y.-L., Yang, X., Ren, Z. M., McDonnell, D. P., Norris, J. D., Willson, T. M., & Greene, G. L. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.014 · Cited by 236 · see citing works

All-trans retinoic acid is a ligand for the orphan nuclear receptor RORβ

Stehlin-Gaon, C., Willmann, D., Zeyer, D., Sanglier, S., Van Dorsselaer, A., Renaud, J.-P., Moras, D., & Schüle, R. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb979 · Cited by 231 · see citing works

A Structural Basis for Constitutive Activity in the Human CAR/RXRα Heterodimer

Xu, R. X., Lambert, M. H., Wisely, B., Warren, E. N., Weinert, E. E., Waitt, G. M., Williams, J. D., Collins, J. L., Moore, L. B., Willson, T. M., et al. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.042 · Cited by 230 · see citing works

Evidence for Ligand-independent Transcriptional Activation of the Human Estrogen-related Receptor α (ERRα)

Kallen, J. A., Schlaeppi, J.-M., Bitsch, F., Filipuzzi, I., Schilb, A., Riou, V., Graham, A., Strauss, A., Geiser, M., & Fournier, B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407999200 · Cited by 218 · see citing works

X-ray Crystal Structure of the Liver X Receptor β Ligand Binding Domain

Williams, S. P., Bledsoe, R. K., Collins, J. L., Boggs, S. D., Lambert, M. H., Miller, A. B., Moore, J. T., McKee, D. D., Moore, L. B., Nichols, J. A., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302260200 · Cited by 216 · see citing works

A Ligand-mediated Hydrogen Bond Network Required for the Activation of the Mineralocorticoid Receptor

Bledsoe, R. K., Madauss, K. P., Holt, J. A., Apolito, C. J., Lambert, M. H., Pearce, K. H., Stanley, T. B., Stewart, E. L., Trump, R. P., Willson, T. M., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504098200 · Cited by 216 · see citing works

Structural Basis for Hydroxycholesterols as Natural Ligands of Orphan Nuclear Receptor RORγ

Jin, L., Martynowski, D., Zheng, S., Wada, T., Xie, W., & Li, Y. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0507 · Cited by 215 · see citing works

Identification of COUP-TFII Orphan Nuclear Receptor as a Retinoic Acid–Activated Receptor

Kruse, S. W., Suino-Powell, K. M., Zhou, X. E., Kretschman, J. E., Reynolds, R. A., Vonrhein, C., Xu, Y., Wang, L., Tsai, S. Y., Tsai, M., et al. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060227 · Cited by 208 · see citing works

Crystallographic Identification and Functional Characterization of Phospholipids as Ligands for the Orphan Nuclear Receptor Steroidogenic Factor-1

Li, Y., Choi, M., Cavey, G. S., Daugherty, J., Suino, K., Kovach, A., Bingham, N. C., Kliewer, S. A., & Xu, H. E. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.002 · Cited by 205 · see citing works

Genetic Modulation of PPARγ Phosphorylation Regulates Insulin Sensitivity

Rangwala, S. M., Rhoades, B., Shapiro, J. S., Rich, A. S., Kim, J. K., Shulman, G. I., Kaestner, K. H., & Lazar, M. A. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00274-0 · Cited by 204 · see citing works

Structural Disorder in the Complex of Human Pregnane X Receptor and the Macrolide Antibiotic Rifampicin

Chrencik, J., Orans, J., Moore, L. B., Xue, Y., Peng, L., Collins, J. L., Wisely, G. B., Lambert, M. H., Kliewer, S. A., & Redinbo, M. R. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0346 · Cited by 201 · see citing works

Activation of nuclear receptors: a perspective from structural genomics.

Li, Y., Lambert, M., & Xu, H.-E. (2003) · Structure · doi:10.1016/s0969-2126(03)00133-3 · Cited by 200 · see citing works

The FXXLF Motif Mediates Androgen Receptor-specific Interactions with Coregulators

He, B., Minges, J. T., Lee, L. W., & Wilson, E. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111975200 · Cited by 188 · see citing works

Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor.

Li, Y., Suino, K., Daugherty, J., & Xu, H. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2005.06.026 · Cited by 188 · see citing works

The Nuclear Xenobiotic Receptor CAR

Suino, K., Peng, L., Reynolds, R. A., Li, Y., Cha, J.-Y., Repa, J. J., Kliewer, S. A., & Xu, H. E. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.036 · Cited by 186 · see citing works

Molecular Recognition of Agonist Ligands by RXRs

Egea, P. F., Mitschler, A., & Moras, D. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.5.0823 · Cited by 175 · see citing works

Molecular recognition of nitrated fatty acids by PPARγ

Li, Y., Zhang, J., Schopfer, F. J., Martynowski, D., Garcia-Barrio, M. T., Kovach, A., Suino-Powell, K., Baker, P. R. S., Freeman, B. A., Chen, Y. E., et al. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1447 · Cited by 168 · see citing works

Structural Basis for Ligand-Independent Activation of the Orphan Nuclear Receptor LRH-1

Sablin, E. P., Krylova, I. N., Fletterick, R. J., & Ingraham, H. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00236-3 · Cited by 164 · see citing works

Scaffold-based discovery of indeglitazar, a PPAR pan-active anti-diabetic agent

Artis, D. R., Lin, J. J., Zhang, C., Wang, W., Mehra, U., Perreault, M., Erbe, D. V., Krupka, H. I., England, B. P., Arnold, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811325106 · Cited by 150 · see citing works

Structural plasticity in the oestrogen receptor ligand‐binding domain

Nettles, K. W., Bruning, J. B., Gil, G. A., O'Neill, E., Nowak, J., Hughs, A., Kim, Y., DeSombre, E. R., Dilis, R., Hanson, R. N., et al. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400963 · Cited by 138 · see citing works

Crystal structure of a mutant mineralocorticoid receptor responsible for hypertension

Fagart, J., Huyet, J., Pinon, G. M., Rochel, M., Mayer, C., & Rafestin-Oblin, M. E. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb939 · Cited by 136 · see citing works

The Structural Basis of Gas-Responsive Transcription by the Human Nuclear Hormone Receptor REV-ERBβ

Pardee, K., Xu, X., Reinking, J., Schuetz, A., Dong, A., Liu, S., Zhang, R., Tiefenbach, J., Lajoie, G., Plotnikov, A. N., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000043 · Cited by 133 · see citing works

X‐ray structure of the orphan nuclear receptor RORβ ligand‐binding domain in the active conformation

Stehlin, C., Wurtz, J., Steinmetz, A. C. U., Greiner, E. F., Schüle, R., Moras, D., & Renaud, J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.5822 · Cited by 125 · see citing works

Evolution of promiscuous nuclear hormone receptors: LXR, FXR, VDR, PXR, and CAR

Krasowski, M. D., Ni, A., Hagey, L. R., & Ekins, S. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.06.016 · Cited by 115 · see citing works

Evolution of the bile salt nuclear receptor FXR in vertebrates*

Reschly, E. J., Ai, N., Ekins, S., Welsh, W. J., Hagey, L. R., Hofmann, A. F., & Krasowski, M. D. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800138-jlr200 · Cited by 112 · see citing works

Doubling the Size of the Glucocorticoid Receptor Ligand Binding Pocket by Deacylcortivazol

Suino-Powell, K. M., Xu, Y., Zhang, C., Tao, Y., Tolbert, W. D., Simons, S. S., & Xu, H. E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01541-07 · Cited by 110 · see citing works

Structure of the Murine Constitutive Androstane Receptor Complexed to Androstenol

Li, S., Vincent, J. G., Brunzelle, J. S., Dussault, I., Lin, M., Ianculescu, I., Sherman, M. A., FORMAN, B. M., & Fernandez, E. J. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.037 · Cited by 107 · see citing works

The structure of corepressor Dax-1 bound to its target nuclear receptor LRH-1

Sablin, E. P., Woods, A., Krylova, I. N., Hwang, P. K., Ingraham, H. A., & Fletterick, R. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808936105 · Cited by 106 · see citing works

Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner

Li, Y., Choi, M., Suino, K., Kovach, A., Daugherty, J., Kliewer, S. A., & Xu, H. E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501204102 · Cited by 95 · see citing works

Crystal Structure of the Pregnane X Receptor-Estradiol Complex Provides Insights into Endobiotic Recognition

Xue, Y., Moore, L. B., Orans, J., Peng, L., Bencharit, S., Kliewer, S. A., & Redinbo, M. R. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0323 · Cited by 93 · see citing works

Rational design of RAR‐selective ligands revealed by RARβ crystal stucture

Germain, P., Kammerer, S., Pérez‐Santín, E., Peluso‐Iltis, C., Tortolani, D. R., Zusi, F. C., Starrett, J. E. J., Lapointe, P., Daris, J., Marinier, A., et al. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400235 · Cited by 91 · see citing works

The Nuclear Xenobiotic Receptor CARStructural Determinants of Constitutive Activation and Heterodimerization

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The use of phage display technique for the isolation of androgen receptor interacting peptides with (F/W)XXL(F/W) and FXXLY new signature motifs

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Predicting peroxisome proliferator-activated receptor gamma potency of small molecules: a synergistic consensus model and deep learning binding affinity approach powered by Enalos Cloud Platform

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Identification of Indoquinazoline Derivatives as Novel NR4A1 Agonists by Suppressing Adipocyte Lipogenesis for Treatment of Obesity

Hu, Y.-T., Luo, J.-C., Xu, S., Jiang, Z., Lin, Y.-W., Li, Y., Tan, J., Chen, S.-B., & Huang, Z. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00895 · Cited by 3 · see citing works

Molecular regulation of PGC-1α: from protein-protein interactions and post-translational modifications to pharmacological modulation

Rios, W. Q., Silva, C. M., Ferreira, R. M., & Gomes, J. R. B. (2026) · Journal of Molecular Medicine · doi:10.1007/s00109-026-02694-6 · Cited by 3 · see citing works

HR3/RORα-mediated cholesterol sensing regulates TOR signaling

Lassen, M., Pardee, K., Bradić, I., Pedersen, L. H., Kubrak, O. I., Ahrentløv, N., Clancy, S., Koyama, T., Necakov, A., Liu, S., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71059-x · Cited by 3 · see citing works

Nuclear orphan receptors: A novel therapeutic agent in neuroinflammation

Thakur, K., Khan, H., Grewal, A. K., & Singh, T. G. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110845 · Cited by 3 · see citing works

Mechanism of antagonist ligand binding to REV-ERBα

Rahman, M. H., & Hegazy, L. (2024) · Scientific Reports · doi:10.1038/s41598-024-58945-4 · Cited by 3 · see citing works

Retinoid Receptors

Bourguet, W., & Moras, D. (2015) · doi:10.1002/9781118628003.ch7 · Cited by 3 · see citing works

Hepatocyte nuclear factor 4 located in different developmental stages of Schistosoma japonicum and involved in important metabolic pathways

Wu, K., Huang, S., Zhao, Y., Umar, A., Chen, H., Yu, Z., & Huang, J. (2024) · Biomedical Journal · doi:10.1016/j.bj.2024.100726 · Cited by 2 · see citing works

Distinct REV-ERBα Conformational State Predicted by GaMD Simulations Leads to the Structure-Based Discovery of Novel REV-ERBα AntagonistPreprint

Hegazy, L., Valfort, A.-C., Burris, T. P., & Elgendy, B. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.26.445894 · Cited by 2 · see citing works

Decades old glitazones still find niche in drug discoveries as PPAR-γ agonists: medicinal chemistry perspective, structure-activity relationships and therapeutic implications

Archana, P., Kumar, T. D. A., Ganesh, N. V., Mohammed, M., Tavanoji, H. P., Deepikarani, R., & Kumar, B. R. P. (2025) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2025.118393 · Cited by 1 · see citing works

Characteristics of C4-Type Zinc Finger Proteins in Tardigrades and Their Responses in Extreme Environments

Duan, M., Zhou, Y., Li, Z., Shi, X., Hua, Z., Gao, Z., & Yang, D. C. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27041739 · Cited by 1 · see citing works

Nuclear receptors: a pandora of hope for metabolic syndrome.

Singh, S., & Agrawal, R. (2026) · Nucleosides, Nucleotides & Nucleic Acids · doi:10.1080/15257770.2026.2620694 · Cited by 1 · see citing works

Long Noncoding RNA Functions as a Regulator for Steroid Hormone Receptor-Related Breast and Prostate Cancers

Jin, C., & Rosenfeld, M. G. (2015) · Springer eBooks · doi:10.1007/978-4-431-55576-6_13 · Cited by 1 · see citing works

Molecular Dynamics: a Tool to Understand Nuclear Receptors

Spyrakis, F., Barril, X., & Luque, F. J. (2012) · Royal Society of Chemistry eBooks · doi:10.1039/9781849735353-00060 · Cited by 1 · see citing works

Membrane Proteins: Targets That Should Not Be Overlooked for Assessing Human and Ecological Health Effects of Chemicals

Zhang, H., Ihara, M., & Chen, J. (2025) · Environmental Science & Technology · doi:10.1021/acs.est.5c05367 · Cited by 1 · see citing works

The Chemical Defensome of Fish: Conservation and Divergence of Genes Involved in Sensing and Responding to Pollutants Among Five Model TeleostsPreprint

Eide, M., Zhang, X., Karlsen, O. A., Goldstone, J. V., Stegeman, J. J., Jonassen, I., & Goksøyr, A. (2021) · doi:10.21203/rs.3.rs-175531/v1 · Cited by 1 · see citing works

Molecular characterisation of DHR38: the Drosophila ortholog of NR4A family of nuclear receptors

Parnaik, T. R. (2024) · doi:10.32657/10356/176376 · Cited by 1 · see citing works

TGFbeta-Dependent ROS Regulates a Local Endocrine Communication Network Between Stromal and Epithelial Cells in the Prostate

Grubisha, M. J. (2011) · D-Scholarship@Pitt (University of Pittsburgh)

An ELIXIR for bone loss?

Ross, F. P. (2012) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.1799

The production and purification of functional steroid hormone receptor ligand binding domains towards the development of a biological endocrine disruptor detection system

Tait, T. (2015) · SUNScholar (Stellenbosch University)

Androgen Insensitivity Due to Mutations of the Androgen Receptor

McPhaul, M. J. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800892-8.00020-8

The role of neuronal peroxisome proliferator-activated receptor delta in diet-induced obesity and hypothalamic inflammation

Kocalis, H. E. (2012)

Effects of Na/K-ATPase and its ligands on bone marrow mesenchymal stem cell differentiation

Sayed, M. (2014) · OhioLink ETD Center (Ohio Library and Information Network)

The Experimental 3D Structure of Nuclear Receptors. A Starting Point for Computational Investigations?

Safo, M. K., Kellogg, G. E., & Cozzini, P. (2012) · Royal Society of Chemistry eBooks · doi:10.1039/9781849735353-00023

Can we ENERGISE our metabolic health? : a deeper look into players of lipid metabolism and the regulation of fasting and cold-induced browning

Defour, M. (2021) · doi:10.18174/548645

Bile Salt Transporters

Eloranta, J. J., Stieger, B., & Kullak-Ublick, G. A. (2014) · doi:10.1002/9781118705308.ch8

Pharmacological Activation of RXR-α Promotes Hematoma Absorption in a PPAR-γ-Dependent Pathway After Intracerebral HemorrhagePreprint

Xu, C., Chen, H., Zhou, S., Sun, C., Xia, X., Peng, Y., Zhuang, J., Fu, X., Zeng, H., Zhou, H., et al. (2021) · doi:10.21203/rs.3.rs-67854/v2

Unraveling the Allosteric Cross-Talk Between Coactivator Peptide and Ligand Binding Site in Glucocorticoid ReceptorPreprint

Sala, G. L., Gunnarsson, A., edman, K., Tyrchan, C., Hogner, A., & Frolov, A. I. (2021) · ChemRxiv · doi:10.26434/chemrxiv.14159162

Chemical biology approaches for nuclear receptors:molecular and structural insights

Fuchs, S. (2013) · TU/e Research Portal · doi:10.6100/ir750746

Nuclear-Receptor Ligands and Ligand-Binding Domains

Weatherman, R. V., Fletterick, R. J., & Scanlan, T. S. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.559 · Cited by 323 · see citing works

Increasing the Complexity Minireview of Coactivation in Nuclear Receptor Signaling

Freedman, L. P. (1999) · Cited by 7 · see citing works

The nuclear receptor ligand-binding domain: structure and function

Moras, D., & Gronemeyer, H. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80015-x · Cited by 838 · see citing works

Nuclear Receptor Coactivators

Stender, J. D., & Glass, C. K. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00244-8