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

The Steroid and Thyroid Hormone Receptor Superfamily

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

Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A

Green, S., Walter, P., Kumar, V., Krust, A., Bornert, J., Argos, P., & Chambon, P. (1986) · Nature · doi:10.1038/320134a0 · Cited by 2,320 · 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

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

Primary structure and expression of a functional human glucocorticoid receptor cDNA

Hollenberg, S. M., Weinberger, C., Ong, E. S., Cerelli, G., Oro, A. E., Lebo, R. V., Thompson, E. B., Rosenfeld, M. G., & Evans, R. M. (1985) · Nature · doi:10.1038/318635a0 · Cited by 1,871 · see citing works

The importance of intrinsic disorder for protein phosphorylation

Iakoucheva, L. M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh253 · Cited by 1,429 · see citing works

Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept

Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.032807.125924 · Cited by 1,406 · see citing works

Chromosome-wide mapping of estrogen receptor binding reveals long-range regulation requiring the forkhead protein FoxA1

Carroll, J. S., Liu, X. S., Brodsky, A. S., Li, W., Meyer, C. A., Szary, A. J., Eeckhoute, J., Shao, W., Hestermann, E. V., Geistlinger, T. R., et al. (2005) · Cell · doi:10.1016/j.cell.2005.05.008 · Cited by 1,384 · see citing works

Genome-wide analysis of estrogen receptor binding sites

Carroll, J. S., Meyer, C. A., Song, J. S., Li, W., Geistlinger, T., Eeckhoute, J., Brodsky, A. S., Keeton, E. K., Fertuck, K. C., Hall, G., et al. (2006) · Nature Genetics · doi:10.1038/ng1901 · Cited by 1,368 · see citing works

Coupling of folding and binding for unstructured proteins

Dyson, H. J., & Wright, P. E. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00289-0 · Cited by 1,327 · see citing works

Sequence and Expression of Human Estrogen Receptor Complementary DNA

Greene, G. L., Gilna, P., Waterfield, M. D., BAKER, A. J., Hort, Y., & Shine, J. (1986) · Science · doi:10.1126/science.3753802 · Cited by 1,311 · see citing works

Principles for modulation of the nuclear receptor superfamily

Gronemeyer, H., Gustafsson, J.-Å., & Laudet, V. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1551 · Cited by 1,228 · see citing works

Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins

Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214 · see citing works

The human estrogen receptor has two independent nonacidic transcriptional activation functions

Tora, L., White, J. H., Brou, C., Tasset, D., Webster, N. J. G., Scheer, E., & Chambon, P. (1989) · Cell · doi:10.1016/0092-8674(89)90031-7 · Cited by 1,049 · see citing works

Mechanism of coupled folding and binding of an intrinsically disordered protein

Sugase, K., Dyson, H. J., & Wright, P. E. (2007) · Nature · doi:10.1038/nature05858 · Cited by 1,040 · see citing works

Linking folding and binding

Wright, P. E., & Dyson, H. J. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.12.003 · Cited by 1,012 · see citing works

GlobPlot: exploring protein sequences for globularity and disorder

Linding, R. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg519 · Cited by 985 · see citing works

Speeding molecular recognition by using the folding funnel: The fly-casting mechanism

Shoemaker, B. A., Portman, J. J., & Wolynes, P. G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160259697 · Cited by 971 · see citing works

Function and structure of inherently disordered proteins

Dunker, A. K., Silman, I., Uversky, V. N., & Sussman, J. L. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.002 · Cited by 963 · 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

Coregulator Function: A Key to Understanding Tissue Specificity of Selective Receptor Modulators

Smith, C. L., & O’Malley, B. W. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0023 · Cited by 931 · 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

FoldIndex(C): a simple tool to predict whether a given protein sequence is intrinsically unfolded

Prilusky, J., Felder, C. E., Zeev‐Ben‐Mordehai, T., Rydberg, E. H., Man, O., Beckmann, J. S., Silman, I., & Sussman, J. L. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti537 · Cited by 913 · see citing works

Molecular Cloning of Human and Rat Complementary DNA Encoding Androgen Receptors

Chang, C. S., Kokontis, J. M., & Liao, S. (1988) · Science · doi:10.1126/science.3353726 · Cited by 891 · see citing works

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

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

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

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

The glucocorticoid receptor: rapid exchange with regulatory sites in living cells

McNally, J. G., Müller, W. G., Walker, D., Wolford, R., & Hager, G. L. (2000) · Science · doi:10.1126/science.287.5456.1262 · Cited by 802 · see citing works

Intrinsic Disorder in Transcription Factors

Liu, J., Perumal, N. B., Oldfield, C. J., Su, E. W., Uversky, V. N., & Dunker, A. K. (2006) · Biochemistry · doi:10.1021/bi0602718 · Cited by 792 · see citing works

Reduced levels of hsp90 compromise steroid receptor action in vivo

Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787 · see citing works

Role of the two activating domains of the oestrogen receptor in the cell‐type and promoter‐context dependent agonistic activity of the anti‐oestrogen 4‐hydroxytamoxifen.

Berry, M., METZGER, D., & Chambon, P. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07469.x · Cited by 760 · see citing works

The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements

Schwabe, J. W. R., Chapman, L., Finch, J. T., & Rhodes, D. (1993) · Cell · doi:10.1016/0092-8674(93)90390-c · Cited by 750 · see citing works

The metazoan Mediator co-activator complex as an integrative hub for transcriptional regulation

Malik, S., & Roeder, R. G. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2901 · Cited by 730 · see citing works

Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components

Timasheff, S. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122225399 · Cited by 718 · see citing works

Structural Biology of the Tumor Suppressor p53

Joerger, A. C., & Fersht, A. R. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.060806.091238 · Cited by 699 · see citing works

Nuclear receptor coactivators

Glass, C. K., Rose, D. W., & Rosenfeld, M. G. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80066-x · Cited by 690 · see citing works

A Hierarchical Network of Transcription Factors Governs Androgen Receptor-Dependent Prostate Cancer Growth

Wang, Q., Li, W., Liu, X. S., Carroll, J. S., Jänne, O. A., Keeton, E. K., Chinnaiyan, A. M., Pienta, K. J., & Brown, M. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.041 · Cited by 689 · see citing works

Multiple and cooperative trans-activation domains of the human glucocorticoid receptor

Hollenberg, S. M., & Evans, R. M. (1988) · Cell · doi:10.1016/0092-8674(88)90145-6 · Cited by 685 · see citing works

DNA binding site sequence directs glucocorticoid receptor structure and activity

Meijsing, S. H., Pufall, M. A., So, A. Y., Bates, D. L., Chen, L., & Yamamoto, K. R. (2009) · Science · doi:10.1126/science.1164265 · Cited by 673 · see citing works

Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions

Tzukerman, M., Esty, A., Santiso‐Mere, D., Danielian, P. S., Parker, M. G., Stein, R. B., Pike, J. W., & McDonnell, D. P. (1994) · Molecular Endocrinology · doi:10.1210/mend.8.1.8152428 · Cited by 671 · see citing works

A molecular mechanism for osmolyte-induced protein stability

Street, T. O., Bolen, D. W., & Rose, G. D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606236103 · Cited by 670 · see citing works

RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins

Yang, Z., Thomson, R., McNeil, P., & Esnouf, R. M. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti534 · Cited by 642 · see citing works

Transcriptional activation and nuclear targeting signals of the human androgen receptor.

Simental, J. A., Sar, M., Lane, M. V., French, F. S., & Wilson, E. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52466-2 · Cited by 631 · see citing works

Solution Structure of the Glucocorticoid Receptor DNA-Binding Domain

Härd, T., Kellenbach, E. R., Boelens, R., Maler, B. A., Dahlman, K., Freedman, L. P., Carlstedt‐Duke, J., Yamamoto, K. R., Gustafsson, J.-Α., & Kaptein, R. (1990) · Science · doi:10.1126/science.2115209 · Cited by 601 · see citing works

Intrinsically disordered proteins: regulation and disease

Babu, M. M., van der Lee, R., de Groot, N. S., & Gsponer, J. A. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.011 · Cited by 597 · see citing works

Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor

Fawell, S. E. (1990) · Cell · doi:10.1016/0092-8674(90)90343-d · Cited by 590 · see citing works

The Human Androgen Receptor: Complementary Deoxyribonucleic Acid Cloning, Sequence Analysis and Gene Expression in Prostate

Lubahn, D. B., JOSEPH, D. R., Sar, M., Tan, J.-A., Higgs, H. N., Larson, R. E., French, F. S., & Wilson, E. M. (1988) · Molecular Endocrinology · doi:10.1210/mend-2-12-1265 · Cited by 570 · see citing works

Net charge per residue modulates conformational ensembles of intrinsically disordered proteins

Mao, A. H., Crick, S. L., Vitalis, A., Chicoine, C. L., & Pappu, R. V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911107107 · Cited by 554 · see citing works

Widespread negative response elements mediate direct repression by agonist-liganded glucocorticoid receptor

Surjit, M., Ganti, K. P., Mukherji, A., Ye, T., Hua, G., Metzger, D., Li, M., & Chambon, P. (2011) · Cell · doi:10.1016/j.cell.2011.03.027 · Cited by 551 · see citing works

Comparing and Combining Predictors of Mostly Disordered Proteins

Oldfield, C. J., Cheng, Y., Cortese, M. S., Brown, C. J., Uversky, V. N., & Dunker, A. K. (2005) · Biochemistry · doi:10.1021/bi047993o · Cited by 544 · see citing works

Structural Overview of the Nuclear Receptor Superfamily: Insights into Physiology and Therapeutics

Huang, P., Chandra, V., & Rastinejad, F. (2010) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021909-135917 · Cited by 530 · see citing works

Regression of castrate-recurrent prostate cancer by a small-molecule inhibitor of the amino-terminus domain of the androgen receptor.

Andersen, R. J., Mawji, N. R., Wang, J., Wang, G., Haile, S., Myung, J.-K., Watt, K., Tam, T., Yang, Y. C., Bañuelos, C. A., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.04.027 · Cited by 503 · see citing works

Allosteric effects of DNA on transcriptional regulators

Lefstin, J. A., & Yamamoto, K. R. (1998) · Nature · doi:10.1038/31860 · Cited by 488 · see citing works

Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family

Xu, J., Wu, R., & O’Malley, B. W. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2695 · Cited by 487 · see citing works

Characterization of Molecular Recognition Features, MoRFs, and Their Binding Partners

Vacic, V., Oldfield, C. J., Mohan, A., Predrag Radivojac, A., Cortese, M. S., Uversky, V. N., & Dunker, A. K. (2007) · Journal of Proteome Research · doi:10.1021/pr0701411 · Cited by 483 · see citing works

Solution structure of the DNA-binding domain of the oestrogen receptor

Schwabe, J. W. R., Neuhaus, D., & Rhodes, D. (1990) · Nature · doi:10.1038/348458a0 · Cited by 462 · see citing works

Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators

Demarest, S. J., Martinez‐Yamout, M. A., Chung, J., Chen, H.-W., Xu, W., Dyson, H. J., Evans, R. M., & Wright, P. E. (2002) · Nature · doi:10.1038/415549a · Cited by 452 · see citing works

FXXLF and WXXLF Sequences Mediate the NH2-terminal Interaction with the Ligand Binding Domain of the Androgen Receptor

He, B., Kemppainen, J., & Wilson, E. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002807200 · Cited by 441 · see citing works

Intrinsically disordered proteins from A to Z

Uversky, V. N. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.04.001 · Cited by 434 · see citing works

The structure of the nuclear hormone receptors

Kumar, R., & Thompson, E. B. (1999) · Steroids · doi:10.1016/s0039-128x(99)00014-8 · Cited by 433 · see citing works

The AF1 and AF2 Domains of the Androgen Receptor Interact with Distinct Regions of SRC1

Bevan, C. L., Hoare, S., Claessens, F., Heery, D. M., & Parker, M. G. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8383 · Cited by 424 · see citing works

Identification of two transcription activation units in the N-terminal domain of the human androgen receptor

Jenster, G., van der Korput, H. A. G. M., Trapman, J., & Brinkmann, A. O. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7341 · Cited by 419 · see citing works

The Steroid Receptor Coactivator-1 Contains Multiple Receptor Interacting and Activation Domains That Cooperatively Enhance the Activation Function 1 (AF1) and AF2 Domains of Steroid Receptors

Oñate, S. A., Boonyaratanakornkit, V., Spencer, T. E., Tsai, S. Y., Tsai, M., Edwards, D. P., & O’Malley, B. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.20.12101 · Cited by 416 · see citing works

Rapid non-genomic effects of corticosteroids and their role in the central stress response

Groeneweg, F. L., Karst, H., de Kloet, E. R., & Joëls, M. (2011) · Journal of Endocrinology · doi:10.1530/joe-10-0472 · Cited by 414 · see citing works

Estrogen receptor (ER) modulators each induce distinct conformational changes in ER α and ER β

Paige, L. A., Christensen, D. J., Grøn, H., Norris, J. D., Gottlin, E. B., Padilla, K. M., Chang, C., Ballas, L. M., Hamilton, P. T., McDonnell, D. P., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3999 · Cited by 410 · see citing works

p300 and p300/cAMP-response Element-binding Protein-associated Factor Acetylate the Androgen Receptor at Sites Governing Hormone-dependent Transactivation

Fu, M., Wang, C., Reutens, A. T., Wang, J., Angeletti, R. H., Siconolfi-Baez, L., Ogryzko, V. V., Avantaggiati, M. L., & Pestell, R. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000660200 · Cited by 409 · 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

Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins

Hilser, V. J., & Thompson, E. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700329104 · Cited by 406 · see citing works

Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones

Freeman, B. C., & Yamamoto, K. R. (2002) · Science · doi:10.1126/science.1073051 · Cited by 400 · see citing works

Structural basis of androgen receptor binding to selective androgen response elements

Shaffer, P. L., Jivan, A., Dollins, D. E., Claessens, F., & Gewirth, D. T. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401123101 · Cited by 400 · see citing works

27-Hydroxycholesterol is an endogenous SERM that inhibits the cardiovascular effects of estrogen

Umetani, M., Domoto, H., Gormley, A. K., Yuhanna, I. S., Cummins, C. L., Javitt, N. B., Korach, K. S., Shaul, P. W., & Mangelsdorf, D. J. (2007) · Nature Medicine · doi:10.1038/nm1641 · Cited by 397 · see citing works

FRAP reveals that mobility of oestrogen receptor-α is ligand- and proteasome-dependent

Stenoien, D. L., Patel, K. N., Mancini, M. G., Dutertre, M., Smith, C. L., O’Malley, B. W., & Mancini, M. A. (2000) · Nature Cell Biology · doi:10.1038/35050515 · Cited by 396 · see citing works

Cellular processing of the glucocorticoid receptor gene and protein: New mechanisms for generating tissue-specific actions of glucocorticoids

Oakley, R. H., & Cidlowski, J. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.179325 · Cited by 373 · see citing works

Cell- and gene-specific regulation of primary target genes by the androgen receptorPreprint

Bolton, E. C., So, A. Y., Chaivorapol, C., Haqq, C. M., Li, H., & Yamamoto, K. R. (2007) · Genes & Development · doi:10.1101/gad.1564207 · Cited by 348 · see citing works

Transcriptional regulation and the role of diverse coactivators in animal cells

Roeder, R. G. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.007 · Cited by 340 · see citing works

Aldosterone: effects on the kidney and cardiovascular system

Briet, M. B., & Schiffrin, E. L. (2010) · Nature Reviews Nephrology · doi:10.1038/nrneph.2010.30 · Cited by 337 · see citing works

Stress, sex, and neural adaptation to a changing environment: mechanisms of neuronal remodeling

McEwen, B. S. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05568.x · Cited by 335 · see citing works

Deciphering the Phosphorylation “Code” of the Glucocorticoid Receptor in Vivo

Wang, Z., Frederick, J., & Garabedian, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110530200 · Cited by 321 · see citing works

A surface on the androgen receptor that allosterically regulates coactivator binding

Estébanez-Perpiñá, E., Arnold, L. A., Nguyen, P., Rodrigues, E. D., Mar, E., Bateman, R., Pallai, P., Shokat, K. M., Baxter, J. D., Guy, R. K., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708036104 · Cited by 307 · see citing works

Determinants of Cell- and Gene-Specific Transcriptional Regulation by the Glucocorticoid Receptor

So, A. Y., Chaivorapol, C., Bolton, E. C., Li, H., & Yamamoto, K. R. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030094 · Cited by 304 · see citing works

Dynamics of heat shock protein 90–progesterone receptor binding and the disactivation loop model for steroid receptor complexes

Smith, D. F. (1993) · Molecular Endocrinology · doi:10.1210/me.7.11.1418 · Cited by 300 · see citing works

Crosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatases

Beck, I. M. E., Vanden Berghe, W., Vermeulen, L., Yamamoto, K. R., Haegeman, G., & De Bosscher, K. (2009) · Endocrine Reviews · doi:10.1210/er.2009-0013 · Cited by 298 · see citing works

Activation of Estrogen Receptor α by S118 Phosphorylation Involves a Ligand-Dependent Interaction with TFIIH and Participation of CDK7

Chen, D., Riedl, T., Washbrook, E., Pace, P. E., Coombes, R. C., Egly, J., & Ali, S. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00004-3 · Cited by 293 · see citing works

Unstructural biology coming of age

Tompa, P. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.012 · Cited by 292 · see citing works

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

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

Glucocorticoid Receptor Phosphorylation Differentially Affects Target Gene Expression

Chen, W., Dang, T., Blind, R. D., Wang, Z., Cavasotto, C. N., Hittelman, A. B., Rogatsky, I., Logan, S. K., & Garabedian, M. J. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0219 · Cited by 280 · see citing works

Evidence for an anti-parallel orientation of the ligand-activated human androgen receptor dimer

Langley, E., Zhou, Z.-X., & Wilson, E. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.50.29983 · Cited by 280 · see citing works

Identification of Human Glucocorticoid Receptor Complementary DNA Clones by Epitope Selection

Weinberger, C., Hollenberg, S. M., Ong, E. S., et al. (1985) · Science · doi:10.1126/science.2581314 · Cited by 275 · see citing works

The N‐terminal DNA‐binding ‘zinc finger’ of the oestrogen and glucocorticoid receptors determines target gene specificity.

Green, S., Kumar, V., Theulaz, I., Wahli, W., & Chambon, P. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03168.x · Cited by 270 · see citing works

Multiple glucocorticoid receptor isoforms and mechanisms of post-translational modification

Duma, D., Jewell, C. M., & Cidlowski, J. A. (2006) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.09.009 · Cited by 267 · see citing works

Separation of the hormone- and DNA-binding sites of the hepatic glucocorticoid receptor by means of proteolysis.

Wränge, Ö., & Gustafsson, J.-Α. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38183-8 · Cited by 259 · see citing works

New androgen receptor genomic targets show an interaction with the ETS1 transcription factor

Massie, C. E., Adryan, B., Barbosa‐Morais, N. L., Lynch, A. G., Tran, M. G., Neal, D. E., & Mills, I. G. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401046 · Cited by 259 · see citing works

Molecular Cloning of the Chicken Progesterone Receptor

Conneely, O. M., Sullivan, W. P., Toft, D. O., Birnbaumer, M., Cook, R. G., Maxwell, B. L., Zarucki-Schulz, T., Greene, G. L., Schrader, W. T., & O’Malley, B. W. (1986) · Science · doi:10.1126/science.2426779 · Cited by 242 · see citing works

p38 Mitogen-Activated Protein Kinase (MAPK) Is a Key Mediator in Glucocorticoid-Induced Apoptosis of Lymphoid Cells: Correlation between p38 MAPK Activation and Site-Specific Phosphorylation of the Human Glucocorticoid Receptor at Serine 211

Miller, A. L., Webb, M. S., Copik, A. J., Wang, Y., Johnson, B. H., Kumar, P., & Thompson, E. B. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0528 · Cited by 241 · see citing works

Target-specific utilization of transcriptional regulatory surfaces by the glucocorticoid receptor

Rogatsky, I., Wang, J.-C., Derynck, M. K., Nonaka, D. F., Khodabakhsh, D. B., Haqq, C. M., Darimont, B. D., Garabedian, M. J., & Yamamoto, K. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2336092100 · Cited by 239 · see citing works

Rapid Periodic Binding and Displacement of the Glucocorticoid Receptor during Chromatin Remodeling

Nagaich, A. K., Walker, D. A., Wolford, R. G., & Hager, G. L. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00178-9 · Cited by 239 · see citing works

Recognition and Accommodation at the Androgen Receptor Coactivator Binding Interface

Hur, E., Pfaff, S. J., Payne, E. S., Grøn, H., Buehrer, B. M., & Fletterick, R. J. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020274 · Cited by 235 · see citing works

Intermolecular NH2-/carboxyl-terminal interactions in androgen receptor dimerization revealed by mutations that cause androgen insensitivity

Langley, E., Kemppainen, J. A., & Wilson, E. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.1.92 · Cited by 233 · see citing works

Characterization of the Amino-terminal Transcriptional Activation Function of the Human Estrogen Receptor in Animal and Yeast Cells

METZGER, D., Ali, S., Bornert, J., & Chambon, P. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9535 · Cited by 228 · see citing works

Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations

Lavery, D. N., & Mcewan, I. J. (2005) · Biochemical Journal · doi:10.1042/bj20050872 · Cited by 227 · see citing works

Alternate surfaces of transcriptional coregulator GRIP1 function in different glucocorticoid receptor activation and repression contexts

Rogatsky, I., Luecke, H. F., Leitman, D. C., & Yamamoto, K. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262671599 · Cited by 226 · see citing works

Selective androgen receptor modulators as function promoting therapies

Bhasin, S., & Jasuja, R. (2009) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e32832a3d79 · Cited by 223 · see citing works

Different Regions in Activation Function-1 of the Human Estrogen Receptor Required for Antiestrogen- and Estradiol-dependent Transcription Activation

McInerney, E. M., & Katzenellenbogen, B. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.39.24172 · Cited by 222 · see citing works

Non-genomic progesterone actions in female reproduction

Gellersen, B., Fernandes, M. S., & Brosens, J. J. (2008) · Human Reproduction Update · doi:10.1093/humupd/dmn044 · Cited by 221 · see citing works

Structural basis for the nuclear import of the human androgen receptor

Cutress, M. L., Whitaker, H. C., Mills, I. G., Stewart, M., & Neal, D. E. (2008) · Journal of Cell Science · doi:10.1242/jcs.022103 · Cited by 219 · see citing works

The evolution of the nuclear receptor superfamily

Escrivá, H., Bertrand, S., & Laudet, V. (2004) · Essays in Biochemistry · doi:10.1042/bse0400011 · Cited by 214 · see citing works

Transactivation Functions of the N-Terminal Domains of Nuclear Hormone Receptors: Protein Folding and Coactivator Interactions

Kumar, R., & Thompson, E. B. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0258 · Cited by 210 · see citing works

Functional in Vivo Interaction between the Amino-Terminal, Transactivation Domain and the Ligand Binding Domain of the Androgen Receptor

Doesburg, P., Kuil, C. W., Berrevoets, C., Steketee, K., Faber, P. W., Mulder, E., Brinkmann, A. O., & Trapman, J. (1997) · Biochemistry · doi:10.1021/bi961775g · Cited by 209 · see citing works

Ligand-dependent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor.

Kraus, W. L., McInerney, E. M., & Katzenellenbogen, B. S. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.26.12314 · Cited by 208 · see citing works

DNA binding alters coactivator interaction surfaces of the intact VDR–RXR complex

Zhang, J., Chalmers, M. J., Stayrook, K. R., Burris, L. L., Wang, Y.-J., Busby, S. A., Pascal, B. D., Garcia-Ordoñez, R. D., Bruning, J. B., Istrate, M. A., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2046 · Cited by 203 · see citing works

Structural determinants of DNA-binding specificity by steroid receptors

Zilliacus, J., Wright, A. P. H., Carlstedt‐Duke, J., & Gustafsson, J. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.4.7659083 · Cited by 199 · see citing works

Steroid Receptor Phosphorylation: A Key Modulator of Multiple Receptor Functions

Weigel, N. L., & Moore, N. L. T. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0101 · Cited by 196 · see citing works

Common architecture of nuclear receptor heterodimers on DNA direct repeat elements with different spacings

Rochel, N., Ciesielski, F., Godet, J., Momán, E., Roessle, M. W., Peluso‐Iltis, C., Moulin, M., Haertlein, M., Callow, P., Mély, Y., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2054 · Cited by 193 · see citing works

A majority of the cancer/testis antigens are intrinsically disordered proteins

Rajagopalan, K., Mooney, S. M., Parekh, N., Getzenberg, R. H., & Kulkarni, P. (2011) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23252 · Cited by 188 · see citing works

Genomic Analyses of Transcription Factor Binding, Histone Acetylation, and Gene Expression Reveal Mechanistically Distinct Classes of Estrogen-Regulated Promoters

Kininis, M., Chen, B. S., Diehl, A. G., Isaacs, G. D., Zhang, T., Siepel, A. C., Clark, A. G., & Kraus, W. L. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00083-07 · Cited by 186 · see citing works

A Lifetime of Aldosterone Excess: Long-Term Consequences of Altered Regulation of Aldosterone Production for Cardiovascular Function

Connell, J. M. C., MacKenzie, S. M., Freel, E. M., Fraser, R., & Davies, E. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0030 · Cited by 182 · see citing works

Cloning of the chicken progesterone receptor.

Jeltsch, J., Krozowski, Z. S., Quirin‐Stricker, C., Gronemeyer, H., Simpson, R. J., Garnier, J., Krust, A., Jacob, F., & Chambon, P. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.15.5424 · Cited by 180 · see citing works

Drugs for ‘protein clouds’: targeting intrinsically disordered transcription factors

Dunker, A. K., & Uversky, V. N. (2010) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2010.09.005 · Cited by 178 · see citing works

Immunochemical analysis of the glucocorticoid receptor: identification of a third domain separate from the steroid-binding and DNA-binding domains.

Carlstedt‐Duke, J., Okret, S., Wränge, Ö., & Gustafsson, J.-Å. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.14.4260 · Cited by 178 · see citing works

Hormone-Dependent Interaction between the Amino- and Carboxyl-Terminal Domains of Progesterone Receptor in Vitro and in Vivo

Tetel, M. J., Giangrande, P. H., Leonhardt, S. A., McDonnell, D. P., & Edwards, D. P. (1999) · Molecular Endocrinology · doi:10.1210/mend.13.6.0300 · Cited by 172 · see citing works

Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP

Kjærgaard, M., Teilum, K., & Poulsen, F. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001693107 · Cited by 171 · see citing works

Compartmentalization of androgen receptor protein–protein interactions in living cells

van Royen, M. E., Cunha, S. M. P. R. M., Brink, M. C., Mattern, K. A., Nigg, A. L., Dubbink, H. J., Verschure, P. J., Trapman, J., & Houtsmuller, A. B. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609178 · Cited by 170 · see citing works

Androgen Receptor Acetylation Governs trans Activation and MEKK1-Induced Apoptosis without Affecting In Vitro Sumoylation and trans-Repression Function

Fu, M., Wang, C., Wang, J., Zhang, X., Sakamaki, T., Yeung, Y. G., Chang, C., Hopp, T., Fuqua, S. A. W., Jaffray, E., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3373-3388.2002 · Cited by 170 · see citing works

Roles of Phosphorylation and Helix Propensity in the Binding of the KIX Domain of CREB-binding Protein by Constitutive (c-Myb) and Inducible (CREB) Activators

Zor, T., Mayr, B. M., Dyson, H. J., Montminy, M., & Wright, P. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207361200 · Cited by 169 · see citing works

Dependence of Selective Gene Activation on the Androgen Receptor NH2- and COOH-terminal Interaction

He, B., Lee, L. W., Minges, J. T., & Wilson, E. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202809200 · Cited by 168 · see citing works

Trimethylamine N-Oxide-induced Cooperative Folding of an Intrinsically Unfolded Transcription-activating Fragment of Human Glucocorticoid Receptor

Baskakov, I. V., Kumar, P., Srinivasan, G., Ji, Y., Bolen, D. W., & Thompson, E. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10693 · Cited by 163 · see citing works

Glucocorticoid Receptor Homodimers and Glucocorticoid-Mineralocorticoid Receptor Heterodimers Form in the Cytoplasm through Alternative Dimerization Interfaces

Savory, J. G. A., Préfontaine, G. G., Lamprecht, C., Liao, M., Walther, R. F., Lefebvre, Y. A., & Haché, R. J. G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.3.781-793.2001 · Cited by 163 · see citing works

Structural characterization of a minimal functional transactivation domain from the human glucocorticoid receptor.

Dahlman‐Wright, K., Baumann, H., McEwan, I. J., Almlöf, T., Wright, A. P. H., Gustafsson, J.-Α., & Härd, T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1699 · Cited by 162 · see citing works

Role of naturally occurring osmolytes in protein folding and stability

Kumar, R. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.09.007 · Cited by 161 · see citing works

Evolution of steroid receptors from an estrogen-sensitive ancestral receptor

Eick, G. N., & Thornton, J. W. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.09.003 · Cited by 161 · see citing works

Synergism Between ER Transactivation Function 1 (AF-1) and AF-2 Mediated by Steroid Receptor Coactivator Protein-1: Requirement for the AF-1 -Helical Core and for a Direct Interaction Between the N- and C-Terminal Domains

Métivier, R., Penot, G., Flouriot, G., & Pakdel, F. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.11.0727 · Cited by 158 · see citing works

A structural biologist's view of the oestrogen receptor

Pike, A. C. W., Brzozowski, A. M., & Hubbard, R. E. (2000) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(00)00102-3 · Cited by 156 · see citing works

Signal transduction via unstructured protein conduits

Dunker, A. K., & Uversky, V. N. (2008) · Nature Chemical Biology · doi:10.1038/nchembio0408-229 · Cited by 152 · see citing works

The Hsp90 Chaperone Machinery Regulates Signaling by Modulating Ligand Binding Clefts

Pratt, W. B., Morishima, Y., & Osawa, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800023200 · Cited by 151 · see citing works

Synergy between estrogen receptor α activation functions AF1 and AF2 mediated by transcription intermediary factor TIF2

Benecke, A., Chambon, P., & Gronemeyer, H. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd028 · Cited by 151 · see citing works

Minireview: The Contribution of Different Androgen Receptor Domains to Receptor Dimerization and Signaling

Centenera, M. M., Harris, J. M., Tilley, W. D., & Butler, L. M. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0017 · Cited by 146 · see citing works

Nuclear Receptors: One Big Family

McEwan, I. J. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-575-0_1 · Cited by 144 · see citing works

Conformational Analysis of the Androgen Receptor Amino-terminal Domain Involved in Transactivation

Reid, J., Kelly, S. M., Watt, K., Price, N. C., & McEwan, I. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201003200 · Cited by 143 · see citing works

An Androgen Receptor NH2-terminal Conserved Motif Interacts with the COOH Terminus of the Hsp70-interacting Protein (CHIP)

He, B., Bai, S., Hnat, A. T., Kalman, R. I., Minges, J. T., Patterson, C., & Wilson, E. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403117200 · Cited by 137 · see citing works

The N-terminal Regions of Estrogen Receptor α and β Are Unstructured in Vitro and Show Different TBP Binding Properties

Wärnmark, A., Wikström, A., Wright, A. P. H., Gustafsson, J.-Α., & Härd, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107875200 · Cited by 135 · see citing works

The Conformation of the Glucocorticoid Receptor AF1/tau1 Domain Induced by Osmolyte Binds Co-regulatory Proteins

Kumar, R., Lee, J. C., Bolen, D. W., & Thompson, E. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100825200 · Cited by 133 · see citing works

Differences in DNA Binding Characteristics of the Androgen and Glucocorticoid Receptors Can Determine Hormone-specific Responses

Schoenmakers, E., Verrijdt, G., Peeters, B. P. H., Verhoeven, G., Rombauts, W., & Claessens, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.12290 · Cited by 132 · see citing works

Regulation of the androgen receptor by SET9-mediated methylation.

Gaughan, L., Stockley, J., Wang, N., McCracken, S. R. C., Treumann, A., Armstrong, K., Shaheen, F., Watt, K., McEwan, I. J., Wang, C., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq861 · Cited by 127 · see citing works

Comparative Analyses of Mechanistic Differences Among Antiestrogens1.

Wijayaratne, A., Nagel, S., Paige, L. A., Christensen, D., Norris, J., Fowlkes, D., & McDonnell, D. (1999) · Endocrinology · doi:10.1210/endo.140.12.7164 · Cited by 126 · see citing works

Mechanisms of estrogen receptor antagonism toward p53 and its implications in breast cancer therapeutic response and stem cell regulation

Konduri, S. D., Medisetty, R., Liu, W., Kaipparettu, B. A., Srivastava, P., Brauch, H. B., Fritz, P., Swetzig, W. M., Gardner, A. E., Khan, S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009575107 · Cited by 123 · see citing works

6 Mineralocorticoid resistance

Komesaroff, P. A., Funder, J. W., & Fuller, P. J. (1994) · Baillière s Clinical Endocrinology and Metabolism · doi:10.1016/s0950-351x(05)80256-3 · Cited by 122 · see citing works

Differential recruitment of glucocorticoid receptor phospho-isoforms to glucocorticoid-induced genes

Blind, R. D., & Garabedian, M. J. (2008) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2008.01.002 · Cited by 120 · see citing works

The transactivating function 1 of estrogen receptor α is dispensable for the vasculoprotective actions of 17β-estradiol

Billon-Galés, A., Fontaine, C., Filipe, C., Douin‐Echinard, V., Fouque, M.-J., Flouriot, G., Gourdy, P., Lenfant, F., Laurell, H., Krust, A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808742106 · Cited by 120 · see citing works

Domain structure of the glucocorticoid receptor protein.

Carlstedt‐Duke, J., Strömstedt, P. E., Wränge, Ö., Bergman, T., Gustafsson, J.-Α., & Jörnvall, H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.13.4437 · Cited by 119 · see citing works

Distinct recognition modes of FXXLF and LXXLL motifs by the androgen receptor

Dubbink, H. J., Hersmus, R., Verma, C. S., van der Korput, H. A. G. M., Berrevoets, C. A., van Tol, J., Ziel-van der Made, A. C. J., Brinkmann, A. O., Pike, A. C. W., & Trapman, J. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0375 · Cited by 118 · see citing works

Three Amino Acid Substitutions Selectively Disrupt the Activation but Not the Repression Function of the Glucocorticoid Receptor N Terminus

Iñiguez-Lluhı́, J. A., Lou, D. Y., & Yamamoto, K. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4149 · Cited by 116 · see citing works

Allosteric Modulation of Estrogen Receptor Conformation by Different Estrogen Response Elements

Wood, J. R., Likhite, V. S., Loven, M. A., & Nardulli, A. M. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.7.0671 · Cited by 116 · see citing works

Estrogen Signaling via Estrogen Receptor β*

Zhao, C.-Y., Dahlman-Wright, K., & Gustafsson, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.180109 · Cited by 114 · see citing works

Nuclear receptor coactivators: structural and functional biochemistry

Bulynko, Y. A., & O’Malley, B. W. (2011) · Biochemistry · doi:10.1021/bi101762x · Cited by 113 · see citing works

Delineation of Two Distinct Type 1 Activation Functions in the Androgen Receptor Amino-terminal Domain

Chamberlain, N. L., Whitacre, D. C., & Miesfeld, R. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.26772 · Cited by 113 · see citing works

Ligand-Specific Dynamics of the Progesterone Receptor in Living Cells and during Chromatin Remodeling In Vitro

Rayasam, G. V., Elbi, C., Walker, D. A., Wolford, R. G., Fletcher, T. M., Edwards, D. P., & Hager, G. L. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.6.2406-2418.2005 · Cited by 111 · see citing works

Estrogen Response Elements Function as Allosteric Modulators of Estrogen Receptor Conformation

Wood, J. R., Greene, G. L., & Nardulli, A. M. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.4.1927 · Cited by 110 · see citing works

Functional Interaction of the c-Myc Transactivation Domain with the TATA Binding Protein: Evidence for an Induced Fit Model of Transactivation Domain Folding

McEwan, I. J., Dahlman‐Wright, K., Ford, J., & Wright, A. P. H. (1996) · Biochemistry · doi:10.1021/bi960793v · Cited by 110 · see citing works

DNA recognition by nuclear receptors

Claessens, F., & Gewirth, D. T. (2004) · Essays in Biochemistry · doi:10.1042/bse0400059 · Cited by 108 · see citing works

Ligand–protein interactions in nuclear receptors of hormones

Egea, P. F., Klaholz, B. P., & Moras, D. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01672-0 · Cited by 108 · see citing works

Induced α-Helix Structure in AF1 of the Androgen Receptor upon Binding Transcription Factor TFIIF

Kumar, R., Betney, R., Li, J., Thompson, E. B., & McEwan, I. J. (2004) · Biochemistry · doi:10.1021/bi035934p · Cited by 107 · see citing works

Role of Acidic and Phosphorylated Residues in Gene Activation by the Glucocorticoid Receptor

Almlöf, T., Wright, A. P. H., & Gustafsson, J.-Α. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17535 · Cited by 106 · see citing works

Phosphorylation-Dependent Sumoylation Regulates Estrogen-Related Receptor-α and -γ Transcriptional Activity through a Synergy Control Motif

Tremblay, A., Wilson, B. J., Yang, X., & Giguère, V. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0357 · Cited by 105 · see citing works

Non-competitive androgen receptor inhibition in vitro and in vivo

Jones, J. O., Bolton, E. C., Huang, Y., Féau, C., Guy, R. K., Yamamoto, K. R., Hann, B. C., & Diamond, M. I. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807282106 · Cited by 104 · see citing works

Interdomain Signaling in a Two-domain Fragment of the Human Glucocorticoid Receptor*

Kumar, R., Baskakov, I., Srinivasan, G., Bolen, D., Lee, C. J., & Thompson, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.35.24737 · Cited by 103 · see citing works

Jun Dimerization Protein 2 Functions as a Progesterone Receptor N-Terminal Domain Coactivator

Wardell, S. E., Boonyaratanakornkit, V., Adelman, J. S., Aronheim, A., & Edwards, D. P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5451-5466.2002 · Cited by 103 · see citing works

Modulation of Steroid Hormone Receptor Activity

Stanišić, V., Lonard, D. M., & O’Malley, B. W. (2010) · Progress in brain research · doi:10.1016/s0079-6123(08)81009-6 · Cited by 102 · see citing works

Roles of transactivating functions 1 and 2 of estrogen receptor-α in bone

Börjesson, A., Windahl, S. H., Lagerquist, M. K., Engdahl, C., Frenkel, B., Movérare‐Skrtic, S., Sjögren, K., Kindblom, J. M., Stubelius, A., Islander, U., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100454108 · Cited by 100 · see citing works

Delineation of a small region within the majortransactivation domain of the human glucocorticoid receptor that mediatestransactivation of gene expression.

Dahlman‐Wright, K., Almlöf, T., McEwan, I. J., Gustafsson, J.-Α., & Wright, A. P. H. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.5.1619 · Cited by 99 · see citing works

Allosteric Control of Ligand Selectivity between Estrogen Receptors α and β

Nettles, K. W., Sun, J., Radek, J. T., Sheng, S., Rodriguez, A. L., Katzenellenbogen, J. A., Katzenellenbogen, B. S., & Greene, G. L. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00054-1 · Cited by 99 · see citing works

Lysine Methylation and Functional Modulation of Androgen Receptor by Set9 Methyltransferase

Ko, S., Ahn, J., Song, C. S., Kim, S.-Y., Knapczyk‐Stwora, K., & Chatterjee, B. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0482 · Cited by 97 · see citing works

Site-Specific Phosphorylation Induces Functionally Active Conformation in the Intrinsically Disordered N-Terminal Activation Function (AF1) Domain of the Glucocorticoid Receptor

Garza, A. S., Khan, S. H., & Kumar, P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00552-09 · Cited by 97 · see citing works

Simulating disorder–order transitions in molecular recognition of unstructured proteins: Where folding meets binding

Verkhivker, G. M., Bouzida, D., Gehlhaar, D. K., Rejto, P. A., Freer, S. T., & Rose, P. W. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0531373100 · Cited by 97 · see citing works

Characterization of transactivational property and coactivator mediation of rat mineralocorticoid receptor activation function-1 (AF-1).

Fuse, H., Kitagawa, H., & Kato, S. (2000) · Molecular Endocrinology · doi:10.1210/mend.14.6.0467 · Cited by 95 · see citing works

Structural Characterization of the Native NH2-Terminal Transactivation Domain of the Human Androgen Receptor: A Collapsed Disordered Conformation Underlies Structural Plasticity and Protein-Induced Folding

Lavery, D. N., & McEwan, I. J. (2008) · Biochemistry · doi:10.1021/bi702221e · Cited by 93 · see citing works

Mechanisms of androgen receptor signalling via steroid receptor coactivator-1 in prostate.

Powell, S. M., Christiaens, V., Voulgaraki, D., Waxman, J., Claessens, F., & Bevan, C. L. (2004) · Endocrine Related Cancer · doi:10.1677/erc.0.0110117 · Cited by 90 · see citing works

Intrinsic disorder in the androgen receptor: identification, characterisation and drugability

McEwan, I. J. (2011) · Molecular BioSystems · doi:10.1039/c1mb05249g · Cited by 87 · see citing works

Nuclear Receptors, Metabolism, and the Circadian ClockPreprint

Yang, X., Lamia, K. A., & Evans, R. M. (2007) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2007.72.058 · Cited by 87 · see citing works

Mineralocorticoid resistance

Zennaro, M., & Lombès, M. (2004) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2004.06.003 · Cited by 87 · see citing works

Receptor mechanisms of rapid extranuclear signalling initiated by steroid hormones

Boonyaratanakornkit, V., & Edwards, D. P. (2004) · Essays in Biochemistry · doi:10.1042/bse0400105 · Cited by 86 · see citing works

Alternative O-GlcNAcylation/O-Phosphorylation of Ser16 Induce Different Conformational Disturbances to the N Terminus of Murine Estrogen Receptor β

Chen, Y., Du, J., Zhou, L., Liu, X.-H., Zhao, Y., Nakanishi, H., & Li, Y. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.06.017 · Cited by 86 · see citing works

Structure of the Progesterone Receptor-Deoxyribonucleic Acid Complex: Novel Interactions Required for Binding to Half-Site Response Elements

Roemer, S. C., Donham, D. C., Sherman, L., Pon, V. H., Edwards, D. P., & Churchill, M. E. A. (2006) · Molecular Endocrinology · doi:10.1210/me.2005-0511 · Cited by 85 · see citing works

TATA box binding protein induces structure in the recombinant glucocorticoid receptor AF1 domain

Kumar, P., Volk, D. E., Li, J., Lee, J. C., Gorenstein, D. G., & Thompson, E. B. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407160101 · Cited by 84 · see citing works

The Relative Contribution Exerted by AF-1 and AF-2 Transactivation Functions in Estrogen Receptor α Transcriptional Activity Depends upon the Differentiation Stage of the Cell

Mérot, Y., Métivier, R., Penot, G., Manu, D., Saligaut, C., Gannon, F., Pakdel, F., Kah, O., & Flouriot, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402148200 · Cited by 84 · see citing works

The Androgen Receptor Acetylation Site Regulates cAMP and AKT but Not ERK-induced Activity

Fu, M., Rao, M., Wu, K., Wang, C., Zhang, X., Hessien, M., Yeung, Y.-G., Gioeli, D. G., Weber, M. J., & Pestell, R. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313466200 · Cited by 83 · see citing works

Conservation analysis predicts in vivo occupancy of glucocorticoid receptor-binding sequences at glucocorticoid-induced genes

So, A. Y., Cooper, S., Feldman, B. J., Manuchehri, M., & Yamamoto, K. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801551105 · Cited by 82 · see citing works

Natural Disordered Sequences in the Amino Terminal Domain of Nuclear Receptors: Lessons from the Androgen and Glucocorticoid Receptors

McEwan, I. J., Lavery, D. N., Fischer, K., & Watt, K. (2007) · Nuclear Receptor Signaling · doi:10.1621/nrs.05001 · Cited by 80 · see citing works

Estrogen Response Elements Alter Coactivator Recruitment through Allosteric Modulation of Estrogen Receptor β Conformation

Loven, M. A., Likhite, V. S., Choi, I., & Nardulli, A. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106211200 · Cited by 79 · see citing works

Role of Important Hydrophobic Amino Acids in the Interaction between the Glucocorticoid Receptor τ1-Core Activation Domain and Target Factors

Almlöf, T., Wallberg, A. E., Gustafsson, J.-Α., & Wright, A. P. H. (1998) · Biochemistry · doi:10.1021/bi973029x · Cited by 78 · see citing works

Role of intrinsically disordered protein regions/domains in transcriptional regulation

Garza, A. S., Ahmad, N., & Kumar, R. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.12.002 · Cited by 78 · see citing works

The Cochaperone Bag-1L Enhances Androgen Receptor Action via Interaction with the NH2-Terminal Region of the Receptor

Shatkina, L., Mink, S., Rogatsch, H., Klocker, H., Langer, G., Nestl, A., & Cato, A. C. B. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7189-7197.2003 · Cited by 78 · see citing works

Functional properties of the N-terminal region of progesterone receptors and their mechanistic relationship to structure

Takimoto, G. S., Tung, L. W., Abdel-Hafiz, H. A., Abel, M. G., Sartorius, C. A., Richer, J. K., Jacobsen, B. M., Bain, D. L., & Horwitz, K. B. (2003) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(03)00197-3 · Cited by 75 · see citing works

The Progesterone Receptor Hinge Region Regulates the Kinetics of Transcriptional Responses Through Acetylation, Phosphorylation, and Nuclear Retention

Daniel, A. R., Gaviglio, A. L., Czaplicki, L. M., et al. (2010) · Molecular Endocrinology · doi:10.1210/me.2010-0170 · Cited by 74 · see citing works

Hydrogen Bonding Progressively Strengthens upon Transfer of the Protein Urea-Denatured State to Water and Protecting Osmolytes

Holthauzen, L. M. F., Rösgen, J., & Bolen, D. W. (2010) · Biochemistry · doi:10.1021/bi9015499 · Cited by 74 · see citing works

Proteome-wide evidence for enhanced positive Darwinian selection within intrinsically disordered regions in proteins

Nilsson, J., Grahn, M., & Wright, A. P. H. (2011) · Genome biology · doi:10.1186/gb-2011-12-7-r65 · Cited by 74 · see citing works

Mechanism of Transcription Factor Recruitment by Acidic Activators

Ferreira, M. E., Hermann, S., Prochasson, P., Workman, J. L., Berndt, K. D., & Wright, A. P. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502627200 · Cited by 71 · see citing works

The nuclear BAG-1 isoform, BAG-1L, enhances oestrogen-dependent transcription

Cutress, R., Townsend, P. A., Sharp, A., Maison, A., Wood, L., Lee, R., Brimmell, M., Mullee, M., Johnson, P., Royle, G. T., et al. (2003) · Oncogene · doi:10.1038/sj.onc.1206688 · Cited by 71 · see citing works

Consequences of poly-glutamine repeat length for the conformation and folding of the androgen receptor amino-terminal domain

Davies, P., Watt, K., Kelly, S. M., Clark, C., Price, N. C., & McEwan, I. J. (2008) · Journal of Molecular Endocrinology · doi:10.1677/jme-08-0042 · 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

Conformation of the Mineralocorticoid Receptor N-terminal Domain: Evidence for Induced and Stable Structure

Fischer, K., Kelly, S. M., Watt, K., Price, N. C., & McEwan, I. J. (2010) · Molecular Endocrinology · doi:10.1210/me.2010-0005 · Cited by 68 · see citing works

Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions

Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057 · see citing works

Estrogen deficiency and the origin of obesity during menopause

Lizcano, F., & Guzmán, G. (2014) · BioMed Research International · doi:10.1155/2014/757461 · Cited by 586 · see citing works

Retinoic acid receptors: From molecular mechanisms to cancer therapy

di Masi, A., Leboffe, L., De Marinis, E., Pagano, F., Cicconi, L., Rochette-Egly, C., Lo-Coco, F., Ascenzi, P., & Nervi, C. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.12.003 · Cited by 403 · see citing works

Minireview: Dynamic Structures of Nuclear Hormone Receptors: New Promises and Challenges

Simons, S. S., Edwards, D. P., & Kumar, R. (2014) · Molecular Endocrinology · doi:10.1210/me.2013-1334 · Cited by 88 · see citing works

Evidence of androgen action in endometrial and ovarian cancers

Gibson, D. A., Simitsidellis, I., Collins, F., & Saunders, P. T. K. (2014) · Endocrine-Related Cancer · doi:10.1530/erc-13-0551 · Cited by 73 · see citing works

[Steroid receptors and hormonal receptivity. New pharmacological and therapeutic approaches applicable to the control of fertility].

Baulieu, É.-É. (1976) · PubMed

[Receptor mechanisms of action of sex hormones. Can the receptor work without a ligand?]

Бабичев, В. Н. (2006) · PubMed · doi:10.14341/probl200652132-38

Binding of hydrocortisone to rat liver histones

Sluyser, M. (1966) · Journal of Molecular Biology · doi:10.1016/s0022-2836(66)80029-3 · Cited by 49 · see citing works

Steroids Receptors in the Genital Tract and the Monitoring of Steroid Hormone Action

Jungblut, P. W. (1982) · Springer eBooks · doi:10.1007/978-3-642-67890-5_13

Plasma Membrane Receptors for Steroid Hormones in Cell Signaling and Nuclear Function

Pietras, R. J., & Szego, C. M. (2007) · Humana Press eBooks · doi:10.1007/978-1-59259-829-8_5 · Cited by 3 · see citing works