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

[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

PROCHECK: a program to check the stereochemical quality of protein structures

Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · see citing works

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works

The nuclear receptor superfamily: the second decade

Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schütz, G., Umesono, K., Blumberg, B., Kastner, P., Mark, M., Chambon, P., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90199-x · Cited by 6,964 · see citing works

AMoRe: an automated package for molecular replacement

Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941 · see citing works

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

A signature motif in transcriptional co-activators mediates binding to nuclear receptors

Heery, D. M., Kalkhoven, E., Hoare, S., & Parker, M. G. (1997) · Nature · doi:10.1038/42750 · Cited by 2,128 · 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

Nuclear Receptor Coregulators: Cellular and Molecular Biology

McKenna, N. J., Lanz, R. B., & O’Malley, B. W. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.3.0366 · Cited by 1,905 · see citing works

Structure-Function Relationships in the Vitamin D Endocrine System*

Bouillon, R., Okamura, W. H., & Norman, A. W. (1995) · Endocrine Reviews · doi:10.1210/edrv-16-2-200 · Cited by 1,237 · see citing works

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

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

A canonical structure for the ligand-binding domain of nuclear receptors

Wurtz, J., Bourguet, W., Renaud, J., Vivat, V., Chambon, P., Moras, D., & Gronemeyer, H. (1996) · Nature Structural Biology · doi:10.1038/nsb0196-87 · Cited by 986 · 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

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

Increasing the Complexity of Coactivation in Nuclear Receptor Signaling

Freedman, L. P. (1999) · Cell · doi:10.1016/s0092-8674(00)80708-4 · Cited by 445 · see citing works

Cloning, expression, and transcriptional properties of the human enhancer factor TEF-1

Xiao, J. H., Davidson, I., Matthes, H. W. D., Garnier, J., & Chambon, P. (1991) · Cell · doi:10.1016/0092-8674(91)90088-g · Cited by 417 · see citing works

Inhibition of Osf2/Cbfa1 expression and terminal osteoblast differentiation by PPAR?2

Lecka‐Czernik, B., Gubrij, I. B., Moerman, E. J., Kajkenova, O., Lipschitz, D. A., Manolagas, S. C., & Jilka, R. L. (1999) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19990901)74:3 · Cited by 403 · see citing works

A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free systemPreprint

Rachez, C., Suldan, Z., Ward, J. O., Chang, C.-P. B., Burakov, D., Erdjument‐Bromage, H., Tempst, P., & Freedman, L. P. (1998) · Genes & Development · doi:10.1101/gad.12.12.1787 · Cited by 402 · see citing works

Structure-function relationships in the vitamin D endocrine system

Bouillon, R. (1995) · Endocrine Reviews · doi:10.1210/er.16.2.200 · Cited by 248 · see citing works

A Nuclear Hormone Receptor Corepressor Mediates Transcriptional Silencing by Receptors with Distinct Repression Domains

Zamir, I., Harding, H. P., Atkins, G. B., Hörlein, A., Glass, C. K., Rosenfeld, M. G., & Lazar, M. A. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5458 · Cited by 227 · see citing works

Distinct Conformational Changes Induced by 20-epi Analogues of 1α,25-Dihydroxyvitamin D3 Are Associated with Enhanced Activation of the Vitamin D Receptor

Peleg, S., Sastry, M., Collins, E. D., Bishop, J. E., & Norman, A. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.18.10551 · Cited by 199 · see citing works

Selective Interaction of Vitamin D Receptor with Transcriptional Coactivators by a Vitamin D Analog

Takeyama, K., Masuhiro, Y., Fuse, H., Endoh, H., Murayama, A., Kitanaka, S., Suzawa, M., Yanagisawa, J., & Kato, S. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1049 · Cited by 198 · see citing works

Mechanisms and Functions of Vitamin D

DeLuca, H. F., & Zierold, C. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1998.tb01686.x · Cited by 188 · see citing works

Vitamin D receptor interaction with specific DNA. Association as a 1,25-dihydroxyvitamin D3-modulated heterodimer.

Sone, T., Kerner, S. A., & Pike, J. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54496-3 · Cited by 154 · see citing works

Two mutations in the hormone binding domain of the vitamin D receptor cause tissue resistance to 1,25 dihydroxyvitamin D3.

Kristjánsson, K., Rut, A. R., Hewison, M., O'Riordan, J. L. H., & Hughes, M. R. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116539 · Cited by 153 · see citing works

Novel nonsecosteroidal vitamin D mimics exert VDR-modulating activities with less calcium mobilization than 1,25-dihydroxyvitamin D3

Boehm, M. F., Fitzgerald, P., Zou, A., et al. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(99)80072-6 · Cited by 152 · see citing works

Conformational adaptation of agonists to the human nuclear receptor RARγ

Klaholz, B. P., Renaud, J., Mitschler, A., Zusi, C., Chambon, P., Gronemeyer, H., & Moras, D. (1998) · Nature Structural Biology · doi:10.1038/nsb0398-199 · Cited by 144 · see citing works

Generalized method of determining heavy-atom positions using the difference Patterson function

Terwilliger, T. C., Kim, S.-H., & Eisenberg, D. (1987) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767387099999 · Cited by 135 · see citing works

Vitamin D receptors from patients with resistance to 1,25- dihydroxyvitamin D3: point mutations confer reduced transactivation in response to ligand and impaired interaction with the retinoid X receptor heterodimeric partner

Whitfield, G. K., Selznick, S. H., Haussler, C. A., Hsieh, J., Galligan, M. A., Jurutka, P. W., Thompson, P. D., Lee, S. M., Zerwekh, J. E., & Haussler, M. R. (1996) · Molecular Endocrinology · doi:10.1210/mend.10.12.8961271 · Cited by 131 · see citing works

Comparison of 6-s-cis- and 6-s-trans-Locked Analogs of 1α,25-Dihydroxyvitamin D3 Indicates That the 6-s-cis Conformation Is Preferred for Rapid Nongenomic Biological Responses and That Neither 6-s-cis- nor 6-s-trans-Locked Analogs Are Preferred for Genomic Biological Responses

Norman, A. W., Okamura, W. H., Hammond, M. W., Bishop, J. E., Dormanen, M. C., Bouillon, R., BAELEN, H. V., Ridall, A. L., Daane, E., Khoury, R., et al. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.10.9993 · Cited by 123 · see citing works

Human vitamin D receptor phosphorylation by casein kinase II at Ser-208 potentiates transcriptional activation.

Jurutka, P. W., Hsieh, J., Nakajima, S., Haussler, C. A., Whitfield, G. K., & Haussler, M. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3519 · Cited by 104 · see citing works

The Biological Activity of Nonsteroidal Vitamin D Hormone Analogs Lacking Both the C- and D-Rings

Verstuyf, A., Verlinden, L., BAELEN, H. V., et al. (1998) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1998.13.4.549 · Cited by 71 · see citing works

Statistical test of models and computerised parameter estimation for aldosterone binding in rat kidney

Claire, M., Rafestin-Oblin, M. E., Michaud, A., & Corvol, P. L. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80197-5 · Cited by 52 · see citing works

Synthesis and biological activity of 2-methyl-20-epi analogues of 1α,25-dihydroxyvitamin D3

Fujishima, T., Liu, Z., Miura, D., et al. (1998) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(98)00363-1 · Cited by 34 · see citing works

Crystal and molecular structure of 1,25-dihydroxycholecalciferol

Suwinska, K., & Kutner, A. (1996) · Acta Crystallographica Section B Structural Science · doi:10.1107/s0108768195017071 · Cited by 26 · see citing works

Nuclear Receptor Co-regulators

Lonard, D. M., & O’Malley, B. W. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-416006-4.00024-7 · Cited by 21 · see citing works

Characterization of the activation function-2 domain of the human 1,25-dihydroxyvitamin D3 receptor

Nakajima, S., Yamagata, M., Sakai, N., et al. (1998) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(98)00077-x · Cited by 16 · see citing works

Vitamin D metabolism, mechanism of action, and clinical applications

Bikle, D. D. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.12.016 · Cited by 1,933 · see citing works

Molecular Mechanisms of Vitamin D Action

Haussler, M. R., Whitfield, G. K., Kaneko, I., Haussler, C. A., Hsieh, D., Hsieh, J.-C., & Jurutka, P. W. (2013) · Calcified Tissue International · doi:10.1007/s00223-012-9619-0 · Cited by 759 · see citing works

Structural Evidence for Ligand Specificity in the Binding Domain of the Human Androgen Receptor

Matias, P. M., Donner, P., Coelho, R., Thomaz, M., Peixoto, C., Macedo, S., Otto, N., Joschko, S., Scholz, P., Wegg, A., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004571200 · Cited by 608 · see citing works

Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model

Norman, A. W., Mizwicki, M. T., & Norman, D. P. G. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1283 · Cited by 569 · see citing works

The roles of vitamin D in skeletal muscle: form, function, and metabolism

Girgis, C. M., Clifton-Bligh, R. J., Hamrick, M. W., Holick, M. F., & Gunton, J. E. (2013) · Endocrine Reviews · doi:10.1210/er.2012-1012 · Cited by 567 · 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 receptors CAR and PXR: Molecular, functional, and biomedical aspects

di Masi, A., Marinis, E. D., Ascenzi, P., & Marino, M. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.04.002 · Cited by 288 · see citing works

The role of androgen receptor mutations in prostate cancer progression.

Brooke, G., & Bevan, C. (2009) · Current Genomics · doi:10.2174/138920209787581307 · Cited by 181 · see citing works

The role of CYP11A1 in the production of vitamin D metabolites and their role in the regulation of epidermal functions

Slominski, A. T., Kim, T.-K., Li, W., Yi, A.-K., Postlethwaite, A., & Tuckey, R. C. (2014) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.10.012 · Cited by 170 · see citing works

Products of vitamin D3 or 7-dehydrocholesterol metabolism by cytochrome P450scc show anti-leukemia effects, having low or absent calcemic activity

Slominski, A. T., Janjetovic, Z., Fuller, B. E., Zmijewski, M. A., Tuckey, R. C., Nguyen, M. N., Sweatman, T., Li, W., Zjawiony, J., Miller, D., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009907 · Cited by 149 · see citing works

Structural and functional insights into nuclear receptor signaling

Jin, L., & Li, Y. (2010) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2010.08.007 · Cited by 112 · see citing works

Correlation between secosteroid-induced vitamin D receptor activity in melanoma cells and computer-modeled receptor binding strength

Kim, T.-K., Wang, J., Janjetovic, Z., Chen, J., Tuckey, R. C., Nguyen, M. N., Tang, E. K. Y., Miller, D., Li, W., & Slominski, A. T. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.04.001 · Cited by 67 · see citing works

Ecdysteroid Structure-Activity Relationships

(2003) · Studies in natural products chemistry · doi:10.1016/s1572-5995(03)80004-2 · Cited by 35 · see citing works

Identification of domains of c-Jun mediating androgen receptor transactivation

Wise, S., Burmeister, L. A., Zhou, X., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1201697 · Cited by 37 · see citing works

Stress-induced c-Jun-dependent Vitamin D Receptor (VDR) Activation Dissects the Non-classical VDR Pathway from the Classical VDR Activity

Li, Q., Qi, X.-M., Pramanik, R., Pohl, N. M., Loesch, M., & Chen, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604052200 · Cited by 34 · see citing works

Culture serum-induced conversion from agonist to antagonist of a Vitamin D analog, TEI-9647

Yamaoka, K., Kim, M.-S., Takada, I., Takeyama, K.-I., Kamimura, T., & Kato, S. (2006) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.04.008 · Cited by 4 · see citing works

Mechanisms of transcription activation by nuclear receptors: studies on the human glucocorticoid receptor tau 1 transactivation domain.

McEwan, I. J., Dahlman-Wright, K., Amlöf, T., Ford, J., Wright, A. P. H., & Gustafsson, J.-Å. (1995) · Mutation research · doi:10.1016/0027-5107(95)00126-3 · Cited by 8 · see citing works

p32 is a negative regulator of p53 tetramerization and transactivation

Ghate, N. B., Kim, J., Shin, Y., et al. (2019) · Molecular Oncology · doi:10.1002/1878-0261.12543 · Cited by 17 · see citing works