NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works

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

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

The glucocorticoid receptor inhibits NFκB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain

Nissen, R. M., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.827900 · Cited by 559 · see citing works

A New Vector for High-Throughput, Ligation-Independent Cloning Encoding a Tobacco Etch Virus Protease Cleavage Site

Stols, L. M., Gu, M., Dieckman, L. J., Wilton, R., Collart, F., & Donnelly, M. I. (2002) · Protein Expression and Purification · doi:10.1006/prep.2001.1603 · Cited by 528 · see citing works

Partial Agonists Activate PPARγ Using a Helix 12 Independent Mechanism

Bruning, J. B., Chalmers, M. J., Prasad, S., Busby, S. A., Kamenecka, T. M., He, Y., Nettles, K. W., & Griffin, P. R. (2007) · Structure · doi:10.1016/j.str.2007.07.014 · Cited by 394 · see citing works

Structural insights into the mode of action of a pure antiestrogen.

Pike, A., Brzozowski, A., Walton, J., Hubbard, R., Thorsell, A., Li, Y.-L., Gustafsson, J.-Å., & Carlquist, M. (2001) · Structure · doi:10.1016/s0969-2126(01)00568-8 · Cited by 353 · see citing works

A fully dissociated compound of plant origin for inflammatory gene repression

Bosscher, K. D., Berghe, W. V., Beck, I. M. E., Molle, W. V., Hennuyer, N., Hapgood, J. P., Libert, C., Staels, B., Louw, A., & Haegeman, G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505554102 · Cited by 257 · see citing works

Constitutively active human estrogen receptors containing amino acid substitutions for tyrosine 537 in the receptor protein

Weis, K. E., Ekena, K., Thomas, J. A., Lazennec, G., & Katzenellenbogen, B. S. (1996) · Molecular Endocrinology · doi:10.1210/mend.10.11.8923465 · Cited by 236 · see citing works

Indazole Estrogens: Highly Selective Ligands for the Estrogen Receptor β

Angelis, M. D., Stossi, F., Carlson, K. A., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049223g · Cited by 216 · see citing works

Altered Ligand Binding Properties and Enhanced Stability of a Constitutively Active Estrogen Receptor: Evidence That an Open Pocket Conformation Is Required for Ligand Interaction

Carlson, K. E., Choi, I., Gee, A. C., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (1997) · Biochemistry · doi:10.1021/bi971746l · Cited by 202 · see citing works

Pyrazolo[1,5-a]pyrimidines: Estrogen Receptor Ligands Possessing Estrogen Receptor β Antagonist Activity

Compton, D. R., Sheng, S., Carlson, K. E., Rebacz, N. A., Lee, I. Y., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049631k · Cited by 184 · see citing works

Ligand-induced stabilization of PPARγ monitored by NMR spectroscopy: implications for nuclear receptor activation

Johnson, B. A., Wilson, E., Li, Y., Moller, D. E., Smith, R. G., & Zhou, G. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3636 · Cited by 165 · 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

Identification of pathway-selective estrogen receptor ligands that inhibit NF-κB transcriptional activity

Chadwick, C. C., Chippari, S. M., Matelan, E. M., Borges-Marcucci, L., Eckert, A. M., Keith, J. C., Albert, L. M., Leathurby, Y., Harris, H. A., Bhat, R. A., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405841102 · Cited by 137 · see citing works

Pyrazolo[1,5-a]pyrimidines: Estrogen Receptor Ligands Possessing Estrogen Receptor β Antagonist Activity.

Compton, D. R., Sheng, S., Carlson, K. E., Rebacz, N. A., Lee, I. Y., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm058162z · Cited by 137 · see citing works

Identification of Amino Acids in the Hormone Binding Domain of the Human Estrogen Receptor Important in Estrogen Binding

Ekena, K., Weis, K. E., Katzenellenbogen, J. A., & Katzenellenbogen, B. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.20053 · Cited by 113 · see citing works

Bridged Bicyclic Cores Containing a 1,1-Diarylethylene Motif Are High-Affinity Subtype-Selective Ligands for the Estrogen Receptor

Muthyala, R. S., Sheng, S., Carlson, K. E., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm0204800 · Cited by 94 · see citing works

Mechanistic Aspects of Estrogen Receptor Activation Probed with Constitutively Active Estrogen Receptors: Correlations with DNA and Coregulator Interactions and Receptor Conformational Changes

Lazennec, G., Ediger, T. R., Petz, L. N., Nardulli, A. M., & Katzenellenbogen, B. S. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.9.9983 · Cited by 90 · see citing works

Ligand-independent activation of the estrogen receptors alpha and beta by mutations of a conserved tyrosine can be abolished by antiestrogens.

Tremblay, G. B., Tremblay, A., Labrie, F., & Giguère, V. (1998) · PubMed · Cited by 75 · see citing works

Synthesis and Evaluation of Estrogen Receptor Ligands with Bridged Oxabicyclic Cores Containing a Diarylethylene Motif: Estrogen Antagonists of Unusual Structure

Zhou, H., Comninos, J. S., Stossi, F., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm0506773 · Cited by 74 · see citing works

Elemental Isomerism: A Boron-Nitrogen Surrogate for a Carbon-Carbon Double Bond Increases the Chemical Diversity of Estrogen Receptor Ligands

Zhou, H., Nettles, K. W., Bruning, J. B., Kim, Y., Joachimiak, A., Sharma, S., Carlson, K. E., Stossi, F., Katzenellenbogen, B. S., Greene, G. L., et al. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.04.009 · Cited by 73 · see citing works

Synthesis and Activity of Substituted 4-(Indazol-3-yl)phenols as Pathway-Selective Estrogen Receptor Ligands Useful in the Treatment of Rheumatoid Arthritis

Steffan, R. J., Matelan, E. M., Ashwell, M. A., Moore, W., Solvibile, W. R., Trybulski, E. J., Chadwick, C. C., Chippari, S. M., Kenney, T. F., Eckert, A., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049194+ · Cited by 70 · see citing works

The Flip Side

Schulman, I. G., & Heyman, R. A. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2003.12.021 · Cited by 67 · see citing works

Isocoumarins as estrogen receptor beta selective ligands: Isomers of isoflavone phytoestrogens and their metabolites

Angelis, M. D., Stossi, F., Waibel, M., Katzenellenbogen, B. S., & Katzenellenbogen, J. A. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.07.014 · Cited by 66 · see citing works

Function of Estrogen Receptor Tyrosine 537 in Hormone Binding, DNA Binding, and Transactivation

Yudt, M. R., Vorojeikina, D. P., Zhong, L., Skafar, D. F., Sasson, S., Gasiewicz, T. A., & Notides, A. C. (1999) · Biochemistry · doi:10.1021/bi9911132 · Cited by 65 · see citing works

Identification of Ligands with Bicyclic Scaffolds Provides Insights into Mechanisms of Estrogen Receptor Subtype Selectivity

Hsieh, R. W., Rajan, S. S., Sharma, S. K., Guo, Y., DeSombre, E. R., Mrksich, M., & Greene, G. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513684200 · Cited by 63 · see citing works

CBP Is a Dosage-Dependent Regulator of Nuclear Factor-κB Suppression by the Estrogen Receptor

Nettles, K. W., Gil, G. A., Nowak, J., Métivier, R., Sharma, V. B., & Greene, G. L. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0324 · Cited by 61 · see citing works

Hormone–PAMAM Dendrimer Conjugates: Polymer Dynamics and Tether Structure Affect Ligand Access to Receptors

Kim, S. H., & Katzenellenbogen, J. A. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200601923 · Cited by 53 · see citing works

Structure-Guided Optimization of Estrogen Receptor Binding Affinity and Antagonist Potency of Pyrazolopyrimidines with Basic Side Chains

Zhou, H., Sheng, S., Compton, D. R., Kim, Y., Joachimiak, A., Sharma, S., Carlson, K. E., Katzenellenbogen, B. S., Nettles, K. W., Greene, G. L., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm061035y · Cited by 43 · see citing works

PhIP Carcinogenicity in Breast Cancer: Computational and Experimental Evidence for Competitive Interactions with Human Estrogen Receptor

Bennion, B. J., Cosman, M., Lightstone, F. C., Knize, M. G., Montgomery, J. L., Bennett, L. M., Felton, J. S., & Kulp, K. S. (2005) · Chemical Research in Toxicology · doi:10.1021/tx0501031 · Cited by 34 · see citing works

Mutations of Tyrosine 537 in the Human Estrogen Receptor-α Selectively Alter the Receptor's Affinity for Estradiol and the Kinetics of the Interaction

Zhong, L., & Skafar, D. F. (2002) · Biochemistry · doi:10.1021/bi0121095 · Cited by 32 · see citing works

Nonpolar and Short Side Chain Groups at C-11β of Estradiol Result in Antiestrogens

Zhang, J., Labaree, D. C., & Hochberg, R. B. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm049352x · Cited by 29 · see citing works

ESR1 ligand-binding domain mutations in hormone-resistant breast cancer

Toy, W., Shen, Y., Won, H. H., Green, B., Sakr, R. A., Will, M., Li, Z., Gala, K. P., Fanning, S. W., King, T. A., et al. (2013) · Nature Genetics · doi:10.1038/ng.2822 · Cited by 1,252 · see citing works

ESR1 mutations—a mechanism for acquired endocrine resistance in breast cancer

Jeselsohn, R. M., Buchwalter, G., Angelis, C. D., Brown, M. A., & Schiff, R. (2015) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2015.117 · Cited by 718 · see citing works

Structural and Mechanistic Insights into Bisphenols Action Provide Guidelines for Risk Assessment and Discovery of Bisphenol A Substitutes

Delfosse, V., Grimaldi, M., Pons, J.-L., Boulahtouf, A., le Maire, A., Cavailles, V., Labesse, G., Bourguet, W., & Balaguer, P. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203574109 · Cited by 405 · see citing works

Activating ESR1 Mutations Differentially Affect the Efficacy of ER Antagonists

Toy, W., Weir, H. M., Razavi, P., Lawson, M., Goeppert, A. U., Mazzola, A. M., Smith, A., Wilson, J., Morrow, C. J., Wong, W. L., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-1523 · Cited by 371 · see citing works

Estrogen receptor alpha somatic mutations Y537S and D538G confer breast cancer endocrine resistance by stabilizing the activating function-2 binding conformation

Fanning, S. W., Mayne, C. G., Dharmarajan, V., Carlson, K. E., Martin, T. A., Novick, S. J., Toy, W., Green, B., Panchamukhi, S., Katzenellenbogen, B. S., et al. (2016) · eLife · doi:10.7554/elife.12792 · Cited by 317 · see citing works

Hydrocarbon Stapled Peptides as Modulators of Biological Function

Cromm, P. M., Spiegel, J., & Grossmann, T. N. (2015) · ACS Chemical Biology · doi:10.1021/cb501020r · Cited by 289 · see citing works

Allele-Specific Chromatin Recruitment and Therapeutic Vulnerabilities of ESR1 Activating Mutations

Jeselsohn, R. M., Bergholz, J. S., Pun, M. J., Cornwell, M., Liu, W., Nardone, A., Xiao, T., Li, W., Qiu, X., Buchwalter, G., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.01.004 · Cited by 278 · see citing works

Design and Structure of Stapled Peptides Binding to Estrogen Receptors

Phillips, C., Roberts, L. R., Schade, M., Bazin, R., Bent, A., Davies, N. L., Moore, R., Pannifer, A. D., Pickford, A. R., Prior, S. H., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja202946k · Cited by 247 · see citing works

Structural underpinnings of oestrogen receptor mutations in endocrine therapy resistance

Katzenellenbogen, J. A., Mayne, C. G., Katzenellenbogen, B. S., Greene, G. L., & Chandarlapaty, S. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0001-z · Cited by 219 · see citing works

Dual suppression of estrogenic and inflammatory activities for targeting of endometriosis

Zhao, Y., Gong, P., Chen, Y., Nwachukwu, J. C., Srinivasan, S., Ko, C., Bagchi, M. K., Taylor, R. N., Korach, K. S., Nettles, K. W., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.3010626 · Cited by 170 · see citing works

Intrinsically disordered proteins and multicellular organisms

Dunker, A. K., Bondos, S. E., Huang, F., & Oldfield, C. J. (2015) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.09.025 · Cited by 150 · see citing works

GDC-9545 (Giredestrant): A Potent and Orally Bioavailable Selective Estrogen Receptor Antagonist and Degrader with an Exceptional Preclinical Profile for ER+ Breast Cancer

Liang, J., Zbieg, J. R., Blake, R. A., Chang, J. H., Daly, S., DiPasquale, A. G., Friedman, L. S., Gelzleichter, T. R., Gill, M., Giltnane, J. M., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00847 · Cited by 155 · see citing works

Estradiol inhibits ongoing autoimmune neuroinflammation and NFκB-dependent CCL2 expression in reactive astrocytes

Giraud, S., Caron, C., Pham-Dinh, D., Kitabgi, P., & Nicot, A. (2010) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0910627107 · Cited by 147 · see citing works

Coupling of receptor conformation and ligand orientation determine graded activity

Bruning, J. B., Parent, A. A., Gil, G., Zhao, M., Nowak, J., Pace, M. C., Smith, C. L., Afonine, P. V., Adams, P. D., Katzenellenbogen, J. A., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.451 · Cited by 142 · 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

Resveratrol modulates the inflammatory response via an estrogen receptor-signal integration network

Nwachukwu, J. C., Srinivasan, S., Bruno, N. E., Parent, A. A., Hughes, T., Pollock, J. A., Gjyshi, O., Cavett, V. J., Nowak, J., Garcia-Ordoñez, R. D., et al. (2014) · eLife · doi:10.7554/elife.02057 · Cited by 137 · 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

The selective estrogen receptor downregulator GDC-0810 is efficacious in diverse models of ER+ breast cancer

Joseph, J. D., Darimont, B. D., Zhou, W. J., Arrazate, A., Young, A. E., Ingalla, E., Walter, K., Blake, R. A., Nonomiya, J., Guan, Z., et al. (2016) · eLife · doi:10.7554/elife.15828 · Cited by 122 · see citing works

Small Molecule Modulation of Nuclear Receptor Conformational Dynamics: Implications for Function and Drug Discovery

Kojetin, D. J., & Burris, T. P. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.079285 · Cited by 122 · see citing works

Discovery of Selective Estrogen Receptor Covalent Antagonists for the Treatment of ERαWT and ERαMUT Breast Cancer

Puyang, X., Furman, C., Zheng, G. Z., Wu, Z. J., Banka, D., Aithal, K. B., Agoulnik, S. I., Bolduc, D. M., Buonamici, S., Caleb, B. L., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-1229 · Cited by 120 · see citing works

The Evolving Role of the Estrogen Receptor Mutations in Endocrine Therapy-Resistant Breast Cancer

Jeselsohn, R. M., Angelis, C. D., Brown, M. A., & Schiff, R. (2017) · Current Oncology Reports · doi:10.1007/s11912-017-0591-8 · Cited by 115 · see citing works

A Blue-Absorbing Photolabile Protecting Group for in Vivo Chromatically Orthogonal Photoactivation

Fournier, L., Gauron, C., Xu, L., Aujard, I., Saux, T. L., Gagey‐Eilstein, N., Maurin, S., Dubruille, S., Baudin, J., Bensimon, D., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb400178m · Cited by 112 · see citing works

Estrogen receptor mutations and their role in breast cancer progression

Alluri, P. G., Speers, C. W., & Chinnaiyan, A. M. (2014) · Breast Cancer Research · doi:10.1186/s13058-014-0494-7 · Cited by 109 · 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

The SERM/SERD bazedoxifene disrupts ESR1 helix 12 to overcome acquired hormone resistance in breast cancer cells

Fanning, S. W., Jeselsohn, R. M., Dharmarajan, V., Mayne, C. G., Karimi, M., Buchwalter, G., Houtman, R., Toy, W., Fowler, C. E., Han, R., et al. (2018) · eLife · doi:10.7554/elife.37161 · Cited by 100 · see citing works

The atypical ubiquitin ligase RNF31 stabilizes estrogen receptor α and modulates estrogen-stimulated breast cancer cell proliferation

Zhu, J., Zhao, C., Razavirad, A., Zhuang, T., Jonsson, P., Liang, N., Williams, C., Lin, C.-Y., Qiao, Y., Zendehdel, K., et al. (2014) · Oncogene · doi:10.1038/onc.2013.573 · Cited by 99 · see citing works

A molecular switch regulating transcriptional repression and activation of PPARγ

Shang, J., Mosure, S. A., Zheng, J., Brust, R., Bass, J., Nichols, A., Solt, L. A., Griffin, P. R., & Kojetin, D. J. (2020) · Nature Communications · doi:10.1038/s41467-020-14750-x · Cited by 98 · see citing works

Stapled Peptides with γ‐Methylated Hydrocarbon Chains for the Estrogen Receptor/Coactivator Interaction

Speltz, T. E., Fanning, S. W., Mayne, C. G., Fowler, C. E., Tajkhorshid, E., Greene, G. L., & Moore, T. W. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201510557 · Cited by 89 · see citing works

Destabilizing Domains Derived from the Human Estrogen Receptor

Miyazaki, Y., Imoto, H., Chen, L., & Wandless, T. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja209933r · Cited by 86 · see citing works

Synthesis and Crystal Structure of a Phosphorylated Estrogen Receptor Ligand Binding Domain

Möcklinghoff, S., Rose, R., Carraz, M., Visser, A., Ottmann, C., & Brunsveld, L. (2010) · ChemBioChem · doi:10.1002/cbic.201000532 · Cited by 87 · see citing works

Nuclear Receptor Profiling of Bisphenol-A and Its Halogenated Analogues

Delfosse, V., Grimaldi, M., le Maire, A., Bourguet, W., & Balaguer, P. (2014) · Vitamins and hormones · doi:10.1016/b978-0-12-800095-3.00009-2 · Cited by 83 · see citing works

Structures of Endocrine-Disrupting Chemicals Determine Binding to and Activation of the Estrogen Receptor α and Androgen Receptor

Tan, H., Wang, X., Hong, H., Benfenati, E., Giesy, J. P., Gini, G. C., Kusko, R., Zhang, X., Yu, H., & Shi, W. F. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.0c02639 · Cited by 83 · see citing works

The 2010 Philip S. Portoghese Medicinal Chemistry Lectureship: Addressing the “Core Issue” in the Design of Estrogen Receptor Ligands

Katzenellenbogen, J. A. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200801h · Cited by 83 · see citing works

Competitive molecular docking approach for predicting estrogen receptor subtype α agonists and antagonists

Ng, H. W., Zhang, W., Shu, M., Luo, H., Ge, W., Perkins, R., Tong, W., & Hong, H. (2014) · BMC Bioinformatics · doi:10.1186/1471-2105-15-s11-s4 · Cited by 80 · see citing works

Antiestrogens: structure-activity relationships and use in breast cancer treatment

Traboulsi, T., Ezzy, M. E., Gleason, J., & Mader, S. (2016) · Journal of Molecular Endocrinology · doi:10.1530/jme-16-0024 · Cited by 64 · see citing works

Estrogen receptor mutations and functional consequences for breast cancer

Thomas, C. G., & Gustafsson, J.-Α. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.06.007 · Cited by 77 · see citing works

Identification by Molecular Docking of Homoisoflavones from Leopoldia comosa as Ligands of Estrogen Receptors

Grande, F., Rizzuti, B., Occhiuzzi, M. A., Ioele, G., Casacchia, T., Gelmini, F., Guzzi, R., Garofalo, A., & Statti, G. A. (2018) · Molecules · doi:10.3390/molecules23040894 · Cited by 72 · see citing works

Understanding the Molecular Basis for Differences in Responses of Fish Estrogen Receptor Subtypes to Environmental Estrogens

Tohyama, S., Miyagawa, S., Lange, A., Ogino, Y., Mizutani, T., Tatarazako, N., Katsu, Y., Ihara, M., Tanaka, H., Ishibashi, H., et al. (2015) · Environmental Science & Technology · doi:10.1021/acs.est.5b00704 · Cited by 72 · 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

ESR1 activating mutations: From structure to clinical application

Grinshpun, A., Chen, V. C., Sandusky, Z. M., Fanning, S. W., & Jeselsohn, R. M. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188830 · Cited by 69 · see citing works

Oral Selective Estrogen Receptor Degraders (SERDs) in Breast Cancer: Advances, Challenges, and Current Status

Downton, T. D., Zhou, F. H., Segara, D., Jeselsohn, R. M., & Lim, E. (2022) · Drug Design Development and Therapy · doi:10.2147/dddt.s380925 · Cited by 68 · see citing works

The X-ray Structure of RU486 Bound to the Progesterone Receptor in a Destabilized Agonistic Conformation

Raaijmakers, H. C. A., Versteegh, J. E., & Uitdehaag, J. C. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.007872 · Cited by 68 · see citing works

ESR1 mutations in HR+/HER2-metastatic breast cancer: Enhancing the accuracy of ctDNA testing

Venetis, K., Pepe, F., Pescia, C., Cursano, G., Criscitiello, C., Frascarelli, C., Mane, E., Russo, G., Salimbeni, B. T., Troncone, G., et al. (2023) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2023.102642 · Cited by 68 · see citing works

Full antagonism of the estrogen receptor without a prototypical ligand side chain

Srinivasan, S., Nwachukwu, J. C., Bruno, N. E., Dharmarajan, V., Goswami, D., Kastrati, I., Novick, S. J., Nowak, J., Cavett, V. J., Zhou, H., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2236 · Cited by 66 · see citing works

Implications of the binding of tamoxifen to the coactivator recognition site of the estrogen receptor

Kojetin, D. J., Burris, T. P., Jensen, E. V., & Khan, S. (2008) · Endocrine Related Cancer · doi:10.1677/erc-07-0281 · Cited by 65 · see citing works

Monitoring a Coordinated Exchange Process in a Four-Component Biological Interaction System: Development of a Time-Resolved Terbium-Based One-Donor/Three-Acceptor Multicolor FRET System

Kim, S. H., Gunther, J. R., & Katzenellenbogen, J. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100248q · Cited by 60 · see citing works

Structurally Novel Antiestrogens Elicit Differential Responses from Constitutively Active Mutant Estrogen Receptors in Breast Cancer Cells and Tumors

Zhao, Y., Laws, M. J., Guillen, V. S., Ziegler, Y., Min, J., Sharma, A., Kim, S. H., Chu, D. T. W., Park, B. H., Oesterreich, S., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1265 · Cited by 60 · see citing works

Stereospecific lasofoxifene derivatives reveal the interplay between estrogen receptor alpha stability and antagonistic activity in ESR1 mutant breast cancer cells

Hosfield, D. J., Weber, S., Li, N., Sauvage, M., Joiner, C., Hancock, G. R., Sullivan, E., Ndukwe, E. C., Han, R., Cush, S., et al. (2022) · eLife · doi:10.7554/elife.72512 · Cited by 59 · see citing works

Novel Dehydroepiandrosterone Derivatives with Antiapoptotic, Neuroprotective Activity

Calogeropoulou, T., Avlonitis, N., Minas, V., Alexi, X., Pantzou, A., Charalampopoulos, I., Zervoú, M., Vergou, V., Katsanou, E. S., Lazaridis, I., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900468p · Cited by 56 · see citing works

Effects of 7-O Substitutions on Estrogenic and Anti-Estrogenic Activities of Daidzein Analogues in MCF-7 Breast Cancer Cells

Jiang, Q., Payton‐Stewart, F., Elliott, S. G., Driver, J. L., Rhodes, L. V., Zhang, Q., Zheng, S., Bhatnagar, D., Boué, S. M., Collins‐Burow, B. M., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100610w · Cited by 55 · see citing works

Next-Generation ERα Inhibitors for Endocrine-Resistant ER+ Breast Cancer

Fanning, S. W., & Greene, G. L. (2019) · Endocrinology · doi:10.1210/en.2018-01095 · Cited by 54 · see citing works

Predictive features of ligand‐specific signaling through the estrogen receptor

Nwachukwu, J. C., Srinivasan, S., Zheng, Y., Wang, S., Min, J., Dong, C., Liao, Z., Nowak, J., Wright, N. A., Houtman, R., et al. (2016) · Molecular Systems Biology · doi:10.15252/msb.20156701 · Cited by 53 · see citing works

Binding of Androgen- and Estrogen-Like Flavonoids to Their Cognate (Non)Nuclear Receptors: A Comparison by Computational Prediction

D’Arrigo, G., Gianquinto, E., Rossetti, G., Cruciani, G., Lorenzetti, S., & Spyrakis, F. (2021) · Molecules · doi:10.3390/molecules26061613 · Cited by 51 · 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

Systematic Prioritization of Druggable Mutations in ∼5000 Genomes Across 16 Cancer Types Using a Structural Genomics-based Approach

Zhao, J., Cheng, F., Wang, Y., Arteaga, C. L., & Zhao, Z. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.053199 · Cited by 50 · 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

Unraveling the clinicopathological features driving the emergence of ESR1 mutations in metastatic breast cancer

Kuang, Y., Siddiqui, B. A., Hu, J., Pun, M. J., Cornwell, M., Buchwalter, G., Hughes, M. E., Wagle, N., Kirschmeier, P. T., Janne, P. A., et al. (2018) · npj Breast Cancer · doi:10.1038/s41523-018-0075-5 · Cited by 47 · see citing works

Distinct mechanisms of endocrine disruption of DDT-related pesticides toward estrogen receptor α and estrogen-related receptor γ

Zhuang, S., Zhang, J., Wen, Y., Zhang, C., & Liu, W. (2012) · Environmental Toxicology and Chemistry · doi:10.1002/etc.1986 · Cited by 47 · see citing works

Genome engineering for estrogen receptor mutations reveals differential responses to anti-estrogens and new prognostic gene signatures for breast cancer

Harrod, A., Lai, C., Goldsbrough, I., Simmons, G. M., Oppermans, N., Santos, D. B., Győrffy, B., Allsopp, R. C., Toghill, B. J., Balachandran, K., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02483-8 · Cited by 42 · see citing works

Endoxifen, 4-Hydroxytamoxifen and an Estrogenic Derivative Modulate Estrogen Receptor Complex Mediated Apoptosis in Breast Cancer

Maximov, P. Y., Abderrahman, B., Fanning, S. W., Sengupta, S., Fan, P., Curpan, R. F., Rincon, D. M. Q., Greenland, J. A., Rajan, S. S., Greene, G. L., et al. (2018) · Molecular Pharmacology · doi:10.1124/mol.117.111385 · Cited by 44 · see citing works

Systems Structural Biology Analysis of Ligand Effects on ERα Predicts Cellular Response to Environmental Estrogens and Anti-hormone Therapies

Nwachukwu, J. C., Srinivasan, S., Bruno, N. E., Nowak, J., Wright, N. A., Minutolo, F., Rangarajan, E. S., Izard, T., Yao, X.-Q., Grant, B. J., et al. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.11.014 · Cited by 43 · see citing works

Dual-mechanism estrogen receptor inhibitors

Min, J., Nwachukwu, J. C., Min, C. K., Njeri, J. W., Srinivasan, S., Rangarajan, E. S., Nettles, C. C., Guillen, V. S., Ziegler, Y., Yan, S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2101657118 · Cited by 43 · 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

Isoflavonoids from Erythrina poeppigiana: Evaluation of Their Binding Affinity for the Estrogen Receptor

Djiogue, S., Halabalaki, M., Alexi, X., Njamen, D., Fomum, Z. T., Alexis, Μ. N., & Skaltsounis, A. (2009) · Journal of Natural Products · doi:10.1021/np900271m · Cited by 41 · see citing works

Bicyclic core estrogens as full antagonists: synthesis, biological evaluation and structure–activity relationships of estrogen receptor ligands based on bridged oxabicyclic core arylsulfonamides

Zhu, M., Zhang, C., Nwachukwu, J. C., Srinivasan, S., Cavett, V. J., Zheng, Y., Carlson, K. E., Dong, C., Katzenellenbogen, J. A., Nettles, K. W., et al. (2012) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob26531a · Cited by 38 · see citing works

X-ray Structures of Progesterone Receptor Ligand Binding Domain in Its Agonist State Reveal Differing Mechanisms for Mixed Profiles of 11β-Substituted Steroids

Lusher, S. J., Raaijmakers, H. C. A., Vu‐Pham, D., Kazemier, B., Bosch, R., McGuire, R., Azevedo, R., Hamersma, H., Dechering, K. J., Oubrie, A., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308403 · Cited by 35 · see citing works

The Application of Ligand-Mapping Molecular Dynamics Simulations to the Rational Design of Peptidic Modulators of Protein–Protein Interactions

Tan, Y. S., Spring, D. R., Abell, C., & Verma, C. S. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/ct5010577 · Cited by 32 · see citing works

Development of Selective Estrogen Receptor Modulator (SERM)‐Like Activity Through an Indirect Mechanism of Estrogen Receptor Antagonism: Defining the Binding Mode of 7‐Oxabicyclo[2.2.1]hept‐5‐ene Scaffold Core Ligands

Zheng, Y., Zhu, M., Srinivasan, S., Nwachukwu, J. C., Cavett, V. J., Min, J., Carlson, K. E., Wang, P., Dong, C., Katzenellenbogen, J. A., et al. (2012) · ChemMedChem · doi:10.1002/cmdc.201200048 · Cited by 31 · see citing works

The cooked meat-derived mammary carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) elicits estrogenic-like microRNA responses in breast cancer cells

Papaioannou, M. D., Koufaris, C., & Gooderham, N. J. (2014) · Toxicology Letters · doi:10.1016/j.toxlet.2014.05.021 · Cited by 30 · see citing works

Triaryl-Substituted Schiff Bases Are High-Affinity Subtype-Selective Ligands for the Estrogen Receptor

Liao, Z.-Q., Dong, C., Carlson, K. E., Srinivasan, S., Nwachukwu, J. C., Chesnut, R. W., Sharma, A., Nettles, K. W., Katzenellenbogen, J. A., & Zhou, H. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500268j · Cited by 30 · see citing works

Designing modified polybrominated diphenyl ether BDE-47, BDE-99, BDE-100, BDE-183, and BDE-209 molecules with decreased estrogenic activities using 3D-QSAR, pharmacophore models coupled with resolution V of the 210-3 fractional factorial design and molecular docking

Chu, Z., & Li, Y. (2018) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2018.10.027 · Cited by 28 · see citing works

Estrogen Receptor Alpha Mutations, Truncations, Heterodimers, and Therapies

Hancock, G. R., Gertz, J., Jeselsohn, R. M., & Fanning, S. W. (2024) · Endocrinology · doi:10.1210/endocr/bqae051 · Cited by 27 · see citing works

Lignin-derived oak phenolics: a theoretical examination of additional potential health benefits of red wine

Setzer, W. N. (2010) · Journal of Molecular Modeling · doi:10.1007/s00894-010-0893-3 · Cited by 26 · see citing works

18F-Fluoroestradiol PET Imaging of Activating Estrogen Receptor-α Mutations in Breast Cancer

Kumar, M., Salem, K., Michel, C. J., Jeffery, J. J., Yan, Y., & Fowler, A. M. (2019) · Journal of Nuclear Medicine · doi:10.2967/jnumed.118.224667 · Cited by 25 · see citing works

A PROSS-designed extensively mutated estrogen receptor α variant displays enhanced thermal stability while retaining native allosteric regulation and structure

Kriegel, M., Wiederanders, H. J., Alkhashrom, S., Eichler, J., & Muller, Y. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-89785-1 · Cited by 25 · see citing works

A unifying biology of sex steroid-induced apoptosis in prostate and breast cancers

Maximov, P. Y., Abderrahman, B., Curpan, R. F., Hawsawi, Y. M., Fan, P., & Jordan, V. C. (2017) · Endocrine Related Cancer · doi:10.1530/erc-17-0416 · Cited by 25 · see citing works

Helix 12 Dynamics and Thyroid Hormone Receptor Activity: Experimental and Molecular Dynamics Studies of Ile280 Mutants

Souza, P. C. T., Barra, G. B., Velasco, L. F. R., Ribeiro, I. C. J., Simeoni, L. A., Togashi, M., Webb, P., Neves, F. D. A. R., Skaf, M. S., Martı́nez, L., et al. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.04.014 · Cited by 24 · see citing works

Endocrine therapy-resistant breast cancer model cells are inhibited by soybean glyceollin I through Eleanor non-coding RNA

Yamamoto, T., Sakamoto, C., Tachiwana, H., Kumabe, M., Matsui, T., Yamashita, T., Shinagawa, M., Ochiai, K., Saitoh, N., & Nakao, M. (2018) · Scientific Reports · doi:10.1038/s41598-018-33227-y · Cited by 24 · see citing works

The Structure-Function Relationship of Angular Estrogens and Estrogen Receptor Alpha to Initiate Estrogen-Induced Apoptosis in Breast Cancer Cells

Maximov, P. Y., Abderrahman, B., Hawsawi, Y. M., Chen, Y., Foulds, C. E., Jain, A., Malovannaya, A., Fan, P., Curpan, R. F., Han, R., et al. (2020) · Molecular Pharmacology · doi:10.1124/mol.120.119776 · Cited by 23 · see citing works

Design and synthesis of novel benzothiophene analogs as selective estrogen receptor covalent antagonists against breast cancer

Bai, C., Ren, S., Wu, S., Zhu, M., Luo, G., & Xiang, H. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113543 · Cited by 23 · see citing works

Unprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits

Ren, B., Peat, T. S., Streltsov, V. A., Pollard, M., Fernley, R. T., Grusovin, J., Seabrook, S. A., Pilling, P. A., Phan, T., Lu, L., et al. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714009626 · Cited by 22 · see citing works

Exploring Flexibility of Progesterone Receptor Ligand Binding Domain Using Molecular Dynamics

Zheng, L., Lin, V. C. L., & Mu, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165824 · Cited by 21 · see citing works

Hormone-Targeted Therapy and Resistance

Metcalfe, C., Friedman, L. S., & Hager, J. H. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030617-050512 · Cited by 21 · see citing works

5- and 4′-Hydroxylated flavonoids affect voltage gating of single alpha-hemolysin pore

Ostroumova, O. S., Efimova, S. S., & Schagina, L. V. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.04.005 · Cited by 20 · see citing works

Known and emerging factors modulating estrogenic effects of endocrine-disrupting chemicals

Zhang, W., Luo, Y., Zhang, L., Cai, Q., & Pan, X. (2013) · Environmental Reviews · doi:10.1139/er-2013-0047 · Cited by 20 · see citing works

Are We Ready to Use ESR1 Mutations in Clinical Practice

Jeselsohn, R. M. (2017) · Breast Care · doi:10.1159/000481428 · Cited by 19 · see citing works

Design, synthesis and biological evaluation of novel estrogen-derived steroid metal complexes

Zhang, X., Zuo, Z., Tang, J., Wang, K., Wang, C., Chen, W., Li, C., Xu, W. F., Xiong, X., Yuntai, K., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.04.088 · Cited by 19 · see citing works

Review of fluorescent steroidal ligands for the estrogen receptor 1995–2018

Gajadeera, N., & Hanson, R. N. (2019) · Steroids · doi:10.1016/j.steroids.2019.02.002 · Cited by 18 · see citing works

Stapled Peptides with γ‐Methylated Hydrocarbon Chains for the Estrogen Receptor/Coactivator Interaction

Speltz, T. E., Fanning, S. W., Mayne, C. G., Fowler, C. E., Tajkhorshid, E., Greene, G. L., & Moore, T. W. (2016) · Angewandte Chemie · doi:10.1002/ange.201510557 · Cited by 18 · see citing works

Structure and Function of Ecdysone Receptors—Interactions with Ecdysteroids and Synthetic Agonists

Hill, R. J., Graham, L. D., Turner, K. A., Howell, L., Tohidi‐Esfahani, D., Fernley, R. T., Grusovin, J., Ren, B., Pilling, P. A., Lu, L., et al. (2012) · Advances in insect physiology · doi:10.1016/b978-0-12-391500-9.00004-8 · Cited by 18 · see citing works

Nonclassical SNAPFL Analogue as a Cy5 Resonance Energy Transfer Partner

Kim, S. H., Gunther, J. R., & Katzenellenbogen, J. A. (2008) · Organic Letters · doi:10.1021/ol801907b · Cited by 18 · see citing works

Molecular dynamics simulation of the human estrogen receptor alpha: contribution to the pharmacophore of the agonists

Jereva, D., Fratev, F., Tsakovska, I., Alov, P., Pencheva, T., & Pajeva, I. K. (2015) · Mathematics and Computers in Simulation · doi:10.1016/j.matcom.2015.07.003 · Cited by 18 · see citing works

Exploring the Structural Compliancy versus Specificity of the Estrogen Receptor Using Isomeric Three-Dimensional Ligands

Sharma, N., Carlson, K. E., Nwachukwu, J. C., Srinivasan, S., Sharma, A., Nettles, K. W., & Katzenellenbogen, J. A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00918 · Cited by 18 · see citing works

Quantitative structure-activity relationship for estrogenic flavonoids from Psoralea corylifolia

Zhang, T., Zhong, S., Meng, Y., Deng, W., Hou, L., Wang, Y., Xing, X., Guan, T., Zhang, J., & Li, T. (2018) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2018.08.040 · Cited by 18 · see citing works

Cadmium activation of wild-type and constitutively active estrogen receptor alpha

Psaltis, J. B., Wang, Q., Yan, G., Gahtani, R. M., Huang, N., Haddad, B. R., & Martin, M. B. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1380047 · Cited by 17 · see citing works

Molecular basis and dual ligand regulation of tetrameric estrogen receptor α/14-3-3ζ protein complex

Somsen, B. A., Sijbesma, E., Leysen, S., Honzejková, K., Visser, E. J., Cossar, P. J., Obšil, T., Brunsveld, L., & Ottmann, C. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104855 · Cited by 17 · see citing works

Structural framework for the understanding spectroscopic and functional signatures of the cyanobacterial Orange Carotenoid Protein families

Sluchanko, N. N., Maksimov, E. G., Slonimskiy, Y. B., Varfolomeeva, L. A., Bukhanko, A. Y., Egorkin, N. A., Tsoraev, G. V., Khrenova, M. G., Ge, B., Qin, S., et al. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127874 · Cited by 18 · see citing works

Estrogen Receptor Alpha Phosphorylated at Tyrosine 537 is Associated with Poor Clinical Outcome in Breast Cancer Patients Treated with Tamoxifen

Skliris, G. P., Nugent, Z. J., Watson, P. H., & Murphy, L. C. (2010) · Hormones and Cancer · doi:10.1007/s12672-010-0049-z · Cited by 17 · see citing works

Computational insights on agonist and antagonist mechanisms of estrogen receptor α induced by bisphenol A analogues

Cao, H., Wang, L., Cao, M., Ye, T., & Sun, Y. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.02.058 · Cited by 16 · see citing works

Crystallographic comparison of the estrogen and progesterone receptor’s ligand binding domains

Tanenbaum, D. M., Wang, Y., Williams, S. P., & Sigler, P. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5998 · Cited by 742 · see citing works

Fast-tracking steroid receptor crystallization

Mader, S. (2008) · Nature Chemical Biology · doi:10.1038/nchembio0408-226

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

Steroid Hormone Structure, Receptor Binding and Activity: Empirical Drug Design

Duax, W. L., & Griffin, J. F. (1998) · Springer eBooks · doi:10.1007/978-94-015-9028-0_1 · Cited by 2 · see citing works

Crystallographic Studies of Steroid-Protein Interactions.

Monzingo, A. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-030-14265-0_2 · Cited by 2 · see citing works