Allosteric Control of Ligand Selectivity between Estrogen Receptors α and β

The Structural Basis of Estrogen Receptor/Coactivator Recognition and the Antagonism of This Interaction by Tamoxifen

Shiau, A. K., Barstad, D., Loria, P. M., Cheng, L., Kushner, P. J., Agard, D. A., & Greene, G. L. (1998) · Cell · doi:10.1016/s0092-8674(00)81717-1 · Cited by 2,726 · 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

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

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

Pyrazole Ligands: Structure−Affinity/Activity Relationships and Estrogen Receptor-α-Selective Agonists

Stauffer, S. R., Coletta, C. J., Tedesco, R., Nishiguchi, G., Carlson, K. E., Sun, J., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm000170m · Cited by 760 · see citing works

Unique response pathways are established by allosteric interactions among nuclear hormone receptors

FORMAN, B. M., Umesono, K., Chen, J., & Evans, R. M. (1995) · Cell · doi:10.1016/0092-8674(95)90075-6 · Cited by 625 · see citing works

Sensitization of diabetic and obese mice to insulin by retinoid X receptor agonists

Mukherjee, R., Davies, P. J., Crombie, D. L., Bischoff, E. D., Cesario, R. M., Jow, L., Hamann, L. G., Boehm, M. F., Mondon, C. E., Nadzan, A. M., et al. (1997) · Nature · doi:10.1038/386407a0 · Cited by 598 · see citing works

Asymmetry in the PPARγ/RXRα Crystal Structure Reveals the Molecular Basis of Heterodimerization among Nuclear Receptors

Gampe, R. T., Montana, V. G., Lambert, M. H., Miller, A. B., Bledsoe, R. K., Milburn, M. V., Kliewer, S. A., Willson, T. M., & Xu, H. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80448-7 · Cited by 574 · 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

Estrogen receptor β

Lewandowski, S. A., Kalita, K. B., & Kaczmarek, L. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03015-6 · Cited by 378 · see citing works

Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism

Shiau, A. K., Barstad, D., Radek, J. T., Meyers, M. J., Nettles, K. W., Katzenellenbogen, B. S., Katzenellenbogen, J. A., Agard, D. A., & Greene, G. L. (2002) · Nature Structural Biology · doi:10.1038/nsb787 · Cited by 357 · see citing works

Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators

Westin, S. K., Kurokawa, R., Nolte, R. T., Wisely, G. B., McInerney, E. M., Rose, D. W., Milburn, M. V., Rosenfeld, M. G., & Glass, C. K. (1998) · Nature · doi:10.1038/26040 · Cited by 333 · see citing works

Novel Ligands that Function as Selective Estrogens or Antiestrogens for Estrogen Receptor-α or Estrogen Receptor-β*

Sun, J., Meyers, M. J., Fink, B. E., Rajendran, R. R., Katzenellenbogen, J. A., & Katzenellenbogen, B. S. (1999) · Endocrinology · doi:10.1210/endo.140.2.6480 · Cited by 315 · see citing works

Co-regulator recruitment and the mechanism of retinoic acid receptor synergy

Germain, P., Iyer, J., Zechel, C., & Gronemeyer, H. (2002) · Nature · doi:10.1038/415187a · Cited by 308 · see citing works

Peroxisome Proliferator-Activated Receptors and Retinoic Acid Receptors Differentially Control the Interactions of Retinoid X Receptor Heterodimers with Ligands, Coactivators, and Corepressors

DiRenzo, J., Söderström, M., Kurokawa, R., Ogliastro, M.-H., Ricote, M., Ingrey, S., Hörlein, A., Rosenfeld, M. G., & Glass, C. K. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.4.2166 · Cited by 281 · see citing works

Transcription Activation by the Human Estrogen Receptor Subtypeβ (ERβ) Studied with ERβ and ERα Receptor Chimeras1

McInerney, E. M., Weis, K. E., Sun, J., Mosselman, S., & Katzenellenbogen, B. S. (1998) · Endocrinology · doi:10.1210/endo.139.11.6298 · Cited by 269 · see citing works

Interaction of methoxychlor and related compounds with estrogen receptor alpha and beta, and androgen receptor: structure-activity studies.

Gaido, K. W., Maness, S. C., McDonnell, D. P., Dehal, S. S., Kupfer, D., & Safe, S. H. (2000) · PubMed · Cited by 223 · see citing works

Coactivator Binding Promotes the Specific Interaction Between Ligand and the Pregnane X Receptor

Watkins, R. E., Davis-Searles, P. R., Lambert, M. H., & Redinbo, M. R. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00795-2 · Cited by 222 · see citing works

Conformational Changes and Coactivator Recruitment by Novel Ligands for Estrogen Receptor-α and Estrogen Receptor-β: Correlations with Biological Character and Distinct Differences among SRC Coactivator Family Members*

Kraichely, D. M., Sun, J., Katzenellenbogen, J. A., & Katzenellenbogen, B. S. (2000) · Endocrinology · doi:10.1210/endo.141.10.7698 · Cited by 217 · see citing works

Target Genes of Peroxisome Proliferator-activated Receptor γ in Colorectal Cancer Cells

Gupta, R. A., Brockman, J. A., Sarraf, P., Willson, T. M., & DuBois, R. N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103779200 · Cited by 215 · see citing works

Binding of Ligands and Activation of Transcription by Nuclear Receptors

Steinmetz, A. C. U., Renaud, J., & Moras, D. (2001) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.30.1.329 · Cited by 207 · see citing works

Interaction of Methoxychlor and Related Compounds with Estrogen Receptor α and β, and Androgen Receptor: Structure-Activity Studies

Gaido, K. W., Maness, S. C., McDonnell, D. P., Dehal, S. S., Kupfer, D., & Safe, S. H. (2000) · Molecular Pharmacology · doi:10.1124/mol.58.4.852 · Cited by 199 · see citing works

Two distinct actions of retinoid-receptor ligands

Chen, J., Clifford, J. L., Zusi, C., Starrett, J. E. J., Tortolani, D. R., Ostrowski, J., Reczek, P. R., Chambon, P., & Gronemeyer, H. (1996) · Nature · doi:10.1038/382819a0 · Cited by 194 · see citing works

Differential Interaction of the Methoxychlor Metabolite 2,2-Bis-(p-Hydroxyphenyl)-1,1,1-Trichloroethane with Estrogen Receptors α and β1

Gaido, K. W., Leonard, L. S., Maness, S. C., Hall, J. M., McDonnell, D. P., Saville, B., & Safe, S. H. (1999) · Endocrinology · doi:10.1210/endo.140.12.7191 · Cited by 190 · see citing works

Mechanism of rescue of common p53 cancer mutations by second‐site suppressor mutations

Nikolova, P. V., Wong, K., DeDecker, B. S., Henckel, J., & Fersht, A. R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.3.370 · Cited by 173 · see citing works

A dynamic mechanism of nuclear receptor activation and its perturbation in a human disease

Kallenberger, B. C., Love, J. D., Chatterjee, K., & Schwabe, J. W. R. (2003) · Nature Structural Biology · doi:10.1038/nsb892 · Cited by 170 · see citing works

Activation of specific RXR heterodimers by an antagonist of RXR homodimers

Lala, D. S., Mukherjee, R., Schulman, I. G., Koch, S. S. C., Dardashti, L. J., Nadzan, A. M., Croston, G. E., Evans, R. M., & Heyman, R. A. (1996) · Nature · doi:10.1038/383450a0 · Cited by 164 · see citing works

Characterization of potent inhibitors of the Bcr-Abl and the c-kit receptor tyrosine kinases.

Wisniewski, D. J., Lambek, C. L., Liu, C., Strife, A., Veach, D. R., Nagar, B., Young, M. A., Schindler, T. H., Bornmann, W. G., Bertino, J. R., et al. (2002) · PubMed · Cited by 161 · see citing works

Estrogen Receptor Subtype-Selective Ligands: Asymmetric Synthesis and Biological Evaluation of cis- and trans-5,11-Dialkyl- 5,6,11,12-tetrahydrochrysenes

Meyers, M. J., Sun, J., Carlson, K. E., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (1999) · Journal of Medicinal Chemistry · doi:10.1021/jm990101b · Cited by 137 · see citing works

Activation and Repression by Nuclear Hormone Receptors: Hormone Modulates an Equilibrium between Active and Repressive States

Schulman, I. G., Juguilon, H., & Evans, R. M. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3807 · Cited by 131 · see citing works

Differential SERM Effects on Corepressor Binding Dictate ERα Activity in Vivo *

Webb, P., Nguyen, P., & Kushner, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208501200 · Cited by 129 · see citing works

Coactivator Peptides Have a Differential Stabilizing Effect on the Binding of Estrogens and Antiestrogens with the Estrogen Receptor

Gee, A. C., Carlson, K. E., Martini, P. G. V., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.11.0373 · Cited by 128 · see citing works

The phantom ligand effect: allosteric control of transcription by the retinoid X receptor.Preprint

Schulman, I. G., Li, C. W., Schwabe, J. W. R., & Evans, R. M. (1997) · Genes & Development · doi:10.1101/gad.11.3.299 · Cited by 127 · see citing works

Ligands Specify Coactivator Nuclear Receptor (NR) Box Affinity for Estrogen Receptor Subtypes

Bramlett, K. S., Wu, Y., & Burris, T. P. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.6.0649 · Cited by 120 · see citing works

Point mutations and sequence variability in proteins: Redistributions of preexisting populations

Sinha, N., & Nussinov, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051399098 · Cited by 110 · see citing works

Molecular Basis for the Subtype Discrimination of the Estrogen Receptor-β-Selective Ligand, Diarylpropionitrile

Sun, J., Baudry, J. Y., Katzenellenbogen, J. A., & Katzenellenbogen, B. S. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0341 · Cited by 91 · see citing works

The Structural Basis for the Specificity of Retinoid-X Receptor-selective Agonists: New Insights Into the Role of Helix H12

Love, J. D., Gooch, J. T., Benkő, S., Li, C., Nagy, L., Chatterjee, K., Evans, R. M., & Schwabe, J. W. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110869200 · Cited by 76 · see citing works

Structure/Function of the Human Glucocorticoid Receptor: Tyrosine 735 Is Important for Transactivation

Ray, D. W., Suen, C. S., Brass, A., Soden, J., & White, A. E. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.11.0376 · Cited by 62 · see citing works

Dissociation of Steroid Receptor Coactivator 1 and Nuclear Receptor Corepressor Recruitment to the Human Glucocorticoid Receptor by Modification of the Ligand-Receptor Interface: The Role of Tyrosine 735

Stevens, A., Garside, H., Berry, A. A., Waters, C. E., White, A. E., & Ray, D. W. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0320 · Cited by 60 · see citing works

DNA Shuffling Method for Generating Estrogen Receptor α and β Chimeras in Yeast

Sun, J., Katzenellenbogen, J. A., Zhao, H., & Katzenellenbogen, B. S. (2003) · BioTechniques · doi:10.2144/03342st02 · Cited by 9 · see citing works

Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response

Rosenfeld, M. G., Lunyak, V. V., & Glass, C. K. (2006) · Genes & Development · doi:10.1101/gad.1424806 · Cited by 952 · see citing works

Mechanism of the nuclear receptor molecular switch

Nagy, L. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.04.006 · Cited by 406 · see citing works

Nuclear Receptor Structure: Implications for Function

Bain, D. L., Heneghan, A. F., Connaghan, K. D., & Miura, M. T. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.160308 · Cited by 366 · see citing works

Estrogen receptor (ER)-β isoforms: A key to understanding ER-β signaling

Leung, Y., Mak, P., Hassan, S., & Ho, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605676103 · Cited by 357 · see citing works

Mechanisms of Mineralocorticoid Action

Fuller, P. J., & Young, M. J. (2005) · Hypertension · doi:10.1161/01.hyp.0000193502.77417.17 · Cited by 324 · 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

Design of selective nuclear receptor modulators: RAR and RXR as a case study

de Lera, Á. R., Bourguet, W., Altucci, L., & Gronemeyer, H. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2398 · Cited by 272 · 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

Bisphenol AF Is a Full Agonist for the Estrogen Receptor ERα but a Highly Specific Antagonist for ERβ

Matsushima, A., Liu, X., Okada, H., Shimohigashi, M., & Shimohigashi, Y. (2010) · Environmental Health Perspectives · doi:10.1289/ehp.0901819 · Cited by 214 · 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

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 Underappreciated Role of Allostery in the Cellular Network

Nussinov, R., Tsai, C., & Ma, B. (2013) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-083012-130257 · Cited by 174 · 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

Fulvestrant (ICI 182,780)-dependent Interacting Proteins Mediate Immobilization and Degradation of Estrogen Receptor-α

Long, X., & Nephew, K. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510809200 · Cited by 170 · see citing works

Dissecting Physiological Roles of Estrogen Receptor α and β with Potent Selective Ligands from Structure-Based Design

Hillisch, A., Peters, O., Kosemund, D., Müller, G. A., Walter, A., Schneider, B., Reddersen, G., Elger, W. A. G., & Fritzemeier, K. (2004) · Molecular Endocrinology · doi:10.1210/me.2004-0050 · Cited by 171 · see citing works

LARMD: integration of bioinformatic resources to profile ligand-driven protein dynamics with a case on the activation of estrogen receptor

Yang, J., Wang, F., Chen, Y., Hao, G., & Yang, G. (2019) · Briefings in Bioinformatics · doi:10.1093/bib/bbz141 · Cited by 136 · see citing works

A structural perspective on nuclear receptors as targets of environmental compounds

Delfosse, V., le Maire, A., Balaguer, P., & Bourguet, W. (2014) · Acta Pharmacologica Sinica · doi:10.1038/aps.2014.133 · Cited by 138 · see citing works

Allosteric Modulators of Steroid Hormone Receptors: Structural Dynamics and Gene Regulation

Kumar, R., & McEwan, I. J. (2012) · Endocrine Reviews · doi:10.1210/er.2011-1033 · Cited by 135 · see citing works

Soy isoflavone phyto-pharmaceuticals in interleukin-6 affections

Dijsselbloem, N., Berghe, W. V., Naeyer, A. D., & Haegeman, G. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.05.036 · Cited by 136 · see citing works

Lessons learnt from structural studies of the oestrogen receptor.

Pike, A. (2006) · Best practice & research. Clinical endocrinology & metabolism · doi:10.1016/j.beem.2005.09.002 · Cited by 126 · see citing works

Structural mechanism for signal transduction in RXR nuclear receptor heterodimers

Kojetin, D. J., Matta‐Camacho, E., Hughes, T., Srinivasan, S., Nwachukwu, J. C., Cavett, V. J., Nowak, J., Chalmers, M. J., Marciano, D. P., Kamenecka, T. M., et al. (2015) · Nature Communications · doi:10.1038/ncomms9013 · Cited by 130 · see citing works

A structural view of nuclear hormone receptor: endocrine disruptor interactions

le Maire, A., Bourguet, W., & Balaguer, P. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0249-2 · Cited by 130 · see citing works

Characterization of the Interaction between Retinoic Acid Receptor/Retinoid X Receptor (RAR/RXR) Heterodimers and Transcriptional Coactivators through Structural and Fluorescence Anisotropy Studies

Pogenberg, V., Guichou, J., Vivat, V., Kammerer, S., Pérez‐Santín, E., Germain, P., de Lera, Á. R., Gronemeyer, H., Royer, C. A., & Bourguet, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409302200 · Cited by 128 · see citing works

Differential Response of Estrogen Receptor Subtypes to 1,3-Diarylindene and 2,3-Diarylindene Ligands

Clegg, N. J., Paruthiyil, S., Leitman, D. C., & Scanlan, T. S. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050226i · Cited by 123 · see citing works

Insights into the Mechanism of Partial Agonism

Pochetti, G., Godio, C., Mitro, N., Caruso, D., Galmozzi, A., Scurati, S., Loiodice, F., Fracchiolla, G., Tortorella, P., Laghezza, A., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702316200 · Cited by 114 · 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

Structural and Functional Profiling of Environmental Ligands for Estrogen Receptors

Delfosse, V., Grimaldi, M., Cavaillès, V., Balaguer, P., & Bourguet, W. (2014) · Environmental Health Perspectives · doi:10.1289/ehp.1408453 · Cited by 105 · see citing works

Crystal Structure of the Peroxisome Proliferator-Activated Receptor γ (PPARγ) Ligand Binding Domain Complexed with a Novel Partial Agonist: A New Region of the Hydrophobic Pocket Could Be Exploited for Drug Design

Montanari, R., Saccoccia, F., Scotti, E., Crestani, M., Godio, C., Gilardi, F., Loiodice, F., Fracchiolla, G., Laghezza, A., Tortorella, P., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800733h · Cited by 100 · see citing works

Conformational Dynamics of the Estrogen Receptor α: Molecular Dynamics Simulations of the Influence of Binding Site Structure on Protein Dynamics

Celik, L., Lund, J. D. D., & Schiøtt, B. (2007) · Biochemistry · doi:10.1021/bi061656t · Cited by 98 · see citing works

Exploration of Dimensions of Estrogen Potency

Jeyakumar, M., Carlson, K. E., Gunther, J. R., & Katzenellenbogen, J. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.205112 · Cited by 90 · see citing works

Structural basis for a molecular allosteric control mechanism of cofactor binding to nuclear receptors

Osz, J., Brélivet, Y., Peluso-Iltis, C., Cura, V., Eiler, S., Ruff, M., Bourguet, W., Rochel, N., & Moras, D. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118192109 · Cited by 84 · see citing works

Exploring the Binding Site Structure of the PPARγ Ligand-Binding Domain by Computational Solvent Mapping

Sheu, S., Kaya, T., Waxman, D. J., & Vajda, S. (2004) · Biochemistry · doi:10.1021/bi048032c · Cited by 79 · see citing works

Subtle Side-Chain Modifications of the Hop Phytoestrogen 8-Prenylnaringenin Result in Distinct Agonist/Antagonist Activity Profiles for Estrogen Receptors α and β

Roelens, F., Heldring, N., Dhooge, W., Bengtsson, M., Comhaire, F. H., Gustafsson, J.-Α., Treuter, E., & Keukeleire, D. D. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060692n · Cited by 78 · see citing works

Structural and Biochemical Basis for the Binding Selectivity of Peroxisome Proliferator-activated Receptor γ to PGC-1α

Li, Y., Kovach, A., Suino-Powell, K. M., Martynowski, D., & Xu, H. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802040200 · Cited by 73 · see citing works

Versatility or Promiscuity: The Estrogen Receptors, Control of Ligand Selectivity and an Update on Subtype Selective Ligands

Ng, H. W., Perkins, R., Tong, W., & Hong, H. (2014) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph110908709 · Cited by 71 · see citing works

Ligand-binding dynamics rewire cellular signaling via estrogen receptor-α

Srinivasan, S., Nwachukwu, J. C., Parent, A. A., Cavett, V. J., Nowak, J., Hughes, T., Kojetin, D. J., Katzenellenbogen, J. A., & Nettles, K. W. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1214 · Cited by 70 · see citing works

A Conformational Switch in the Ligand-binding Domain Regulates the Dependence of the Glucocorticoid Receptor on Hsp90

Ricketson, D., Hostick, U., Fang, L., Yamamoto, K. R., & Darimont, B. D. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.057 · Cited by 69 · see citing works

Coevolution in defining the functional specificity

Chakrabarti, S., & Panchenko, A. R. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22239 · Cited by 66 · see citing works

Rapid Creation of a Novel Protein Function by in Vitro Coevolution

Chen, Z., & Zhao, H. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.070 · Cited by 60 · see citing works

Estrogens and the hair follicle

Conrad, F., & Paus, R. (2004) · JDDG Journal der Deutschen Dermatologischen Gesellschaft · doi:10.1046/j.1439-0353.2004.04037.x · Cited by 57 · see citing works

Ligand unbinding pathways from the vitamin D receptor studied by molecular dynamics simulations

Peräkylä, M. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0369-x · Cited by 56 · see citing works

Isolation and Identification of Cucurbitane-Type Triterpenoids with Partial Agonist/Antagonist Potential for Estrogen Receptors from Momordica charantia

Hsu, C., Hsieh, C., Kuo, Y., & Huang, C. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf200418g · Cited by 56 · see citing works

Directed Evolution of Human Estrogen Receptor Variants with Significantly Enhanced Androgen Specificity and Affinity

Chen, Z., Katzenellenbogen, B. S., Katzenellenbogen, J. A., & Zhao, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402118200 · Cited by 56 · see citing works

Vitamin D Receptor: Ligand Recognition and Allosteric Network

Yamamoto, K., Abe, D., Yoshimoto, N., Choi, M., Yamagishi, K., Tokiwa, H., Shimizu, M., Makishima, M., & Yamada, S. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm050795q · Cited by 56 · see citing works

Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases

Laughlin, J. D., Nwachukwu, J. C., Figuera-Losada, M., Cherry, L., Nettles, K. W., & LoGrasso, P. V. (2012) · Structure · doi:10.1016/j.str.2012.09.021 · Cited by 50 · see citing works

Role of ligand-dependent GR phosphorylation and half-life in determination of ligand-specific transcriptional activity

Avenant, C., Ronacher, K., Stubsrud, E., Louw, A., & Hapgood, J. P. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.06.007 · Cited by 49 · see citing works

Computational Insights into the Mechanism of Ligand Unbinding and Selectivity of Estrogen Receptors

Shen, J., Li, W., Liu, G., Tang, Y., & Jiang, H. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp903785h · Cited by 48 · see citing works

Identification and Structure–Activity Relationships of a Novel Series of Estrogen Receptor Ligands Based on 7-Thiabicyclo[2.2.1]hept-2-ene-7-oxide

Wang, P., Min, J., Nwachukwu, J. C., Cavett, V. J., Carlson, K. E., Guo, P., Zhu, M., Zheng, Y., Dong, C., Katzenellenbogen, J. A., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201556r · Cited by 42 · see citing works

Dynamic allosteric communication pathway directing differential activation of the glucocorticoid receptor

Köhler, C., Carlström, G., Gunnarsson, A., Weininger, U., Tångefjord, S., Ullah, V., Lepistö, M., Karlsson, U., Papavoine, T., Edman, K., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb5277 · Cited by 42 · see citing works

Cortisol resistance in the New World revisited

Fuller, P. J., Smith, B. J., & Rogerson, F. M. (2004) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2004.07.001 · Cited by 42 · see citing works

Discovery of Novel Quinoline-Based Estrogen Receptor Ligands Using Peptide Interaction Profiling

Hoekstra, W. J., Patel, H. S., Liang, X., Blanc, J.-B. E., Heyer, D. O., Willson, T. M., Iannone, M. A., Kadwell, S. H., Miller, L. A., Pearce, K. H., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm040154f · Cited by 42 · see citing works

A theoretical entropy score as a single value to express inhibitor selectivity

Uitdehaag, J. C. M., & Zaman, G. J. R. (2011) · BMC Bioinformatics · doi:10.1186/1471-2105-12-94 · Cited by 41 · see citing works

Communication between the ERRα Homodimer Interface and the PGC-1α Binding Surface via the Helix 8–9 Loop

Greschik, H., Althage, M., Flaig, R., Sato, Y., Chavant, V., Peluso‐Iltis, C., Choulier, L., Cronet, P., Rochel, N., Schüle, R., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801920200 · Cited by 41 · see citing works

A Family-based Approach Reveals the Function of Residues in the Nuclear Receptor Ligand-binding Domain

Folkertsma, S., van Noort, P., Durme, J. V., Joosten, H., Bettler, E., Fleuren, W. W. M., Oliveira, L., Horn, F., de Vlieg, J., & Vriend, G. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.075 · Cited by 41 · see citing works

A Critical Region in the Mineralocorticoid Receptor for Aldosterone Binding and Activation by Cortisol: Evidence for a Common Mechanism Governing Ligand Binding Specificity in Steroid Hormone Receptors

Rogerson, F. M., Yao, Y.-Z., Elsass, R. E., Dimopoulos, N., Smith, B. J., & Fuller, P. J. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0246 · Cited by 39 · see citing works

Synthesis and Evaluation of Estrogen Agonism of Diaryl 4,5-Dihydroisoxazoles, 3-Hydroxyketones, 3-Methoxyketones, and 1,3-Diketones: A Compound Set Forming a 4D Molecular Library

Pulkkinen, J. T., Honkakoski, P., Peräkylä, M., Berczi, I., & Laatikainen, R. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8001795 · Cited by 35 · see citing works

Ligand selectivity of estrogen receptors by a molecular dynamics study

Hu, G., & Wang, J. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.04.049 · Cited by 33 · see citing works

Towards accurate high-throughput ligand affinity prediction by exploiting structural ensembles, docking metrics and ligand similarity

Schneider, M., Pons, J.-L., Bourguet, W., & Labesse, G. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz538 · Cited by 33 · see citing works

Computational Screening of Phthalate Monoesters for Binding to PPARγ

Kaya, T., Mohr, S. C., Waxman, D. J., & Vajda, S. (2006) · Chemical Research in Toxicology · doi:10.1021/tx050301s · Cited by 30 · see citing works

Estrogen Receptors: Their Actions and Functional Roles in Health and Disease

Nilsson, S. V., & Gustafsson, J.-Α. (2010) · Springer eBooks · doi:10.1007/978-90-481-3303-1_5 · Cited by 29 · see citing works

Selective estrogen receptor α activation disrupts sex organ differentiation and induces expression of vitellogenin II and very low-density apolipoprotein II in Japanese quail embryos

Mattsson, A., Olsson, J., & Brunström, B. (2008) · Reproduction · doi:10.1530/rep-08-0100 · Cited by 29 · see citing works

Molecular characterization of a B-ring unsaturated estrogen: Implications for conjugated equine estrogen components of Premarin

Hsieh, R. W., Rajan, S. S., Sharma, S. K., & Greene, G. L. (2007) · Steroids · doi:10.1016/j.steroids.2007.08.014 · Cited by 29 · see citing works

Why Does Binding of Proteins to DNA or Proteins to Proteins Not Necessarily Spell Function?

Ma, B., Tsai, C., Pan, Y., & Nussinov, R. (2010) · ACS Chemical Biology · doi:10.1021/cb900293a · Cited by 28 · see citing works

Helix 11 Dynamics Is Critical for Constitutive Androstane Receptor Activity

Wright, E., Busby, S. A., Wisecarver, S. N., Vincent, J. G., Griffin, P. R., & Fernandez, E. J. (2011) · Structure · doi:10.1016/j.str.2010.11.008 · Cited by 27 · see citing works

The helix 1–3 loop in the glucocorticoid receptor LBD is a regulatory element for FKBP cochaperones

Cluning, C., Ward, B. K., Rea, S. L., Arulpragasam, A., Fuller, P. J., & Ratajczak, T. (2013) · Molecular Endocrinology · doi:10.1210/me.2012-1023 · Cited by 26 · see citing works

Classification of anti-estrogens according to intramolecular FRET effects on phospho-mutants of estrogen receptor α

Zwart, W. T., Griekspoor, A., Rondaij, M. G., Verwoerd, D., Neefjes, J., & Michalides, R. J. A. M. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0750 · Cited by 26 · see citing works

The estrogen receptor and polyphenols: molecular simulation studies of their interactions, a review

Lambrinidis, G., Halabalaki, M., Katsanou, E. S., Skaltsounis, A., Alexis, Μ. N., & Mikros, E. (2006) · Environmental Chemistry Letters · doi:10.1007/s10311-006-0065-y · Cited by 26 · see citing works

Revealing a natural marine product as a novel agonist for retinoic acid receptors with a unique binding mode and inhibitory effects on cancer cells

Wang, S., Wang, Z., Lin, S., Zheng, W., Wang, R., Jin, S., Chen, J., Jin, L., & Li, Y. (2012) · Biochemical Journal · doi:10.1042/bj20120726 · Cited by 24 · see citing works

Bisphenol AF: Halogen bonding effect is a major driving force for the dual ERα-agonist and ERβ-antagonist activities

Liu, X., Suyama, K., Shiki, J., Torikai, K., Nose, T., Shimohigashi, M., & Shimohigashi, Y. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.115274 · Cited by 23 · see citing works

Helix 8 of the ligand binding domain of the glucocorticoid receptor (GR) is essential for ligand binding

Deng, Q., Waxse, B. J., Riquelme, D., Zhang, J., & Aguilera, G. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.01.044 · Cited by 21 · see citing works

Functional characterization of somatic point mutations of the human estrogen receptor α (hERα) in adenomyosis uteri

Oehler, M. K., Greschik, H., Fischer, D., Tong, X., Schüle, R., & Kieback, D. (2004) · Molecular Human Reproduction · doi:10.1093/molehr/gah113 · Cited by 21 · see citing works

Dynamic correlation networks in human peroxisome proliferator-activated receptor-γ nuclear receptor protein

Fidelak, J., Ferrer, S., Oberlin, M., Moras, D., Dejaegere, A. P., & Stote, R. H. (2010) · European Biophysics Journal · doi:10.1007/s00249-010-0608-9 · Cited by 18 · see citing works

Network approach for capturing ligand-induced subtle global changes in protein structures

Sukhwal, A., Bhattacharyya, M., & Vishveshwara, S. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911007062 · Cited by 18 · see citing works

Bisphenol-C is the strongest bifunctional ERα-agonist and ERβ-antagonist due to magnified halogen bonding

Liu, X., Suyama, K., Nose, T., Shimohigashi, M., & Shimohigashi, Y. (2021) · PLoS ONE · doi:10.1371/journal.pone.0246583 · Cited by 18 · see citing works

Effect of heterodimer partner RXRα on PPARγ activation function-2 helix in solution

Lu, J., Chen, M., Stanley, S. E., & Li, E. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.10.143 · Cited by 17 · see citing works

Glucocorticoid Receptor Point Mutation V571M Facilitates Coactivator and Ligand Binding by Structural Rearrangement and Stabilization

Carlsson, P., Koehler, K. F., & Nilsson, L. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0203 · Cited by 16 · see citing works

Multiple‐Targeting and Conformational Selection in the Estrogen Receptor: Computation and Experiment

Yuan, P., Liang, K., Ma, B., Zheng, N., Nussinov, R., & Huang, J. (2011) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2011.01119.x · Cited by 15 · see citing works

CAR: Three new models for a problem child

Moore, D. D. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2004.12.006 · Cited by 13 · see citing works

Conformational dynamics of estrogen receptors α and β as revealed by intrinsic tryptophan fluorescence and circular dichroism

Nair, S. K., Thomas, T., Greenfield, N. J., Chen, A., He, H., & Thomas, T. (2005) · Journal of Molecular Endocrinology · doi:10.1677/jme.1.01830 · Cited by 13 · see citing works

Allostery and Coupled Sequence Variation in Nuclear Hormone Receptors

Kuriyan, J. (2004) · Cell · doi:10.1016/s0092-8674(04)00125-4 · Cited by 13 · see citing works

Analysis of the hormone-binding domain of steroid receptors using chimeras generated by homologous recombination

Martínez, E. D., Pattabiraman, N., & Danielsen, M. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.03.040 · Cited by 12 · see citing works

Effects of estradiol and 4-hydroxytamoxifen on the conformation, thermal stability, and DNA recognition of estrogen receptor β

Vijayanathan, V., Greenfield, N. J., Thomas, T., Ivanova, M. M., Tyulmenkov, V. V., Klinge, C. M., Gallo, M. A., & Thomas, T. (2007) · Biochemistry and Cell Biology · doi:10.1139/o06-144 · Cited by 11 · see citing works

Ligand-Induced Allosteric Effects Governing SR Signaling

Okafor, C. D., Colucci, J. K., & Ortlund, E. A. (2019) · Nuclear Receptor Research · doi:10.32527/2019/101382 · Cited by 10 · see citing works

Advances in the Administration of Vitamin D Analogues to Support Bone Health and Treat Chronic Diseases

Kanemoto, Y., Iwaki, M., Sawada, T., Nojiri, K., Kurokawa, T., Tsutsumi, R., Nagasawa, K., & Kato, S. (2023) · Journal of Bone Metabolism · doi:10.11005/jbm.2023.30.3.219 · Cited by 10 · see citing works

Effects on differentiation of reproductive organs and sexual behaviour in Japanese quail by excessive embryonic ERa activation

Mattsson, A., & Brunström, B. (2010) · Reproduction Fertility and Development · doi:10.1071/rd08293 · Cited by 9 · see citing works

Differential gene regulation by a synthetic vitamin D receptor ligand and active vitamin D in human cells

Iwaki, M., Kanemoto, Y., Sawada, T., Nojiri, K., Kurokawa, T., Tsutsumi, R., Nagasawa, K., & Kato, S. (2023) · PLoS ONE · doi:10.1371/journal.pone.0295288 · Cited by 7 · see citing works

In silico simulations and molecular descriptors to predict in vitro transactivation potencies of Baikal seal estrogen receptors by environmental contaminants

Nguyen, H. T., Yoshinouchi, Y., Hirano, M., Nomiyama, K., Nakata, H., Kim, E., & Iwata, H. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.115495 · Cited by 6 · see citing works

Dynamical probing of allosteric control in nuclear receptors

Cunningham, M. A. (2012) · Journal of Molecular Modeling · doi:10.1007/s00894-011-1330-y · Cited by 6 · see citing works

Androgen and estrogen receptors: Potential of crystallography in the fight against cancer

Nahoum, V., & Bourguet, W. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.01.001 · Cited by 6 · see citing works

Protein‐Structure‐Based Prediction of Animal Model Suitability for Pharmacodynamic Studies of Subtype‐Selective Estrogens

Toschi, L., Hilbig, J., Wintermantel, T. M., Engelhaupt, A., Walter, A., Fritzemeier, K., & Hillisch, A. (2006) · ChemMedChem · doi:10.1002/cmdc.200600183 · Cited by 4 · see citing works

Molecular Determinants of Per- and Polyfluoroalkyl Substances Binding to Estrogen Receptors

Mada, S., Jordan, S., Mathew, J., Loveranes, C., Moran, J., Ganesh, H., & Dakshanamurthy, S. (2025) · Toxics · doi:10.3390/toxics13110903 · Cited by 3 · see citing works

Role of conformational dynamics and flexibilities in the steroid receptor-coregulator protein complex formation

Kumar, R. (2021) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2021.113780 · Cited by 3 · see citing works

A Unified Deep Graph Model for Identifying the Molecular Categories of Ligands Targeting Nuclear Receptors

Yang, K., Jiang, D., Deng, Q., Xiang, S., Ge, J., Xu, K., Jiang, Z., Wang, Z.-H., Yin, C., Qian, Y., et al. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c00700 · Cited by 2 · see citing works

High-throughput screening of estrogen receptor activity in personalized mixtures of persistent organic pollutants detected in the blood of Swedish adults

Reis, L. T. C., Strand, D., Höglund, A., Lundgren, B., Bergdahl, I. A., Martin, J. W., & Karlsson, O. (2025) · Environmental Research · doi:10.1016/j.envres.2025.123388 · Cited by 2 · see citing works

Twenty-five Years of Nuclear Receptor Structure Analysis: From the Laboratory to the Clinic

McEwan, I. J., & Kumar, P. (2015) · Springer eBooks · doi:10.1007/978-3-319-18729-7_1 · Cited by 2 · see citing works

Nuclear Hormone Receptors: Insights for Drug Design from Structure and Modeling

Renaud, J., Moras, D., & Wurtz, J. (2007) · Elsevier eBooks · doi:10.1016/b0-08-045044-x/00273-x · Cited by 2 · see citing works

Differential role of estrogen receptor isoforms in the cardiovascular system of young and senescent rats

Jazbutyte, V. (2007)

Ligand modulation of allosteric networks in an ancestral steroid receptorPreprint

Okafor, C. D., & Ortlund, E. A. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/414375

Role of estrogen receptor signaling in the control of the hair follicle cycle

Conrad, F. (2004)

BindingDB Entry 3154: Insights into the mechanism of partial agonism: crystal structures of the peroxisome proliferator-activated receptor gamma ligand-binding domain in the complex with two enantiomeric ligands.

BindingDB (2009) · UC San Diego · doi:10.7270/q27m0682

Ligand-Selective Inhibition of the Interaction of Steroid Receptor Coactivators and Estrogen Receptor Isoforms

Geistlinger, T., McReynolds, A. C., & Guy, R. K. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.01.016 · Cited by 45 · see citing works

Structure−Function Evaluation of ER α and β Interplay with SRC Family Coactivators. ER Selective Ligands

Wong, C., Komm, B. S., & Cheskis, B. J. (2001) · Biochemistry · doi:10.1021/bi010379h · Cited by 103 · see citing works

Estrogen receptor subtype ligand selectivity: molecular structural characteristics

Agatonović-Kuštrin, S., & Turner, J. (2009) · RUNE (Research UNE)

The nature of the ligand-binding pocket of estrogen receptor alpha and beta: The search for subtype-selective ligands and implications for the prediction of estrogenic activity

Katzenellenbogen, J. A., Muthyala, R., & Katzenellenbogen, B. S. (2003) · Pure and Applied Chemistry · doi:10.1351/pac200375112397 · Cited by 43 · see citing works

Selective Recognition of Distinct Classes of Coactivators by a Ligand-Inducible Activation Domain

Acevedo, M. L., Lee, K. C., Stender, J. D., Katzenellenbogen, B. S., & Kraus, W. L. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00121-2 · Cited by 58 · see citing works