The DOI matches its Crossref record; 99 of the 99 references it cites were found in a registry or an index.
Activation Functions 1 and 2 of Nuclear Receptors: Molecular Strategies for Transcriptional Activation
Open accessAbstract
Nuclear receptors (NRs) comprise a family of ligand inducible transcription factors. To achieve transcriptional activation of target genes, DNA-bound NRs directly recruit general transcription factors (GTFs) to the preinitiation complex or bind intermediary factors, so-called coactivators. These coactivators often constitute subunits of larger multiprotein complexes that act at several functional levels, such as chromatin remodeling, enzymatic modification of histone tails, or modulation of the preinitiation complex via interactions with RNA polymerase II and GTFs. The binding of NR to coactivators is often mediated through one of its activation domains. Many NRs have at least two activation domains, the ligand-independent activation function (AF)-1, which resides in the N-terminal domain, and the ligand-dependent AF-2, which is localized in the C-terminal domain. In this review, we summarize and discuss current knowledge regarding the molecular mechanisms of AF-1- and AF-2-mediated gene activation, focusing on AF-1 and AF-2 conformation and coactivator binding.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“The transcriptional activation functions of the receptors reside in both the NTD (a constitutively active AF-1) and LBD (a ligand-dependent AF-2), through which essential coactivators usually are recruited with DNA-bound receptors to activate transcription (Warnmark et al., 2003).”
From Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes (2020) · cites this paper as Warnmark et al., 2003
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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 2,759
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
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
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 1,979
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 1,941
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*
Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791
Kastner, P., Krust, A., Turcotte, B., Stropp, U., Tora, L., Gronemeyer, H., & Chambon, P. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08280.x · Cited by 1,534
Functional domains of the human estrogen receptor
Kumar, V., Green, S., Stack, G., Berry, M., Jin, J.-R., & Chambon, P. (1987) · Cell · doi:10.1016/0092-8674(87)90581-2 · Cited by 1,316
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 1,192
Flagged first, then by citations
Cited by
Sorted by citations
Insel, T. R. (2010) · Neuron · doi:10.1016/j.neuron.2010.03.005 · Cited by 1,044
Pharmacology of anabolic steroids
Kicman, A. T. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.165 · Cited by 578
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
Vitamin A and retinoid signaling: genomic and nongenomic effects
Al Tanoury, Z., Piskunov, A., & Rochette-Egly, C. (2013) · Journal of Lipid Research · doi:10.1194/jlr.r030833 · Cited by 408
Hypothalamus‐Pituitary‐Thyroid Axis
Ortiga-Carvalho, T. M., Chiamolera, M. I., Pazos-Moura, C. C., & Wondisford, F. E. (2016) · Comprehensive physiology · doi:10.1002/cphy.c150027 · Cited by 485
Thyroid hormone receptors and resistance to thyroid hormone disorders
Ortiga-Carvalho, T. M., Sidhaye, A. R., & Wondisford, F. E. (2014) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2014.143 · Cited by 383
Hussain, Q., Asim, M., Zhang, R., Khan, R., Farooq, S., & Wu, J. (2021) · Biomolecules · doi:10.3390/biom11081159 · Cited by 300
Dynamic and combinatorial control of gene expression by nuclear retinoic acid receptors (RARs)
Rochette‐Egly, C., & Germain, P. (2009) · Nuclear Receptor Signaling · doi:10.1621/nrs.07005 · Cited by 263
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 242
Structural and functional consequences of glutamine tract variation in the androgen receptor
Buchanan, G. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh181 · Cited by 225
Schäcke, H., Berger, M., Rehwinkel, H., & Asadullah, K. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2007.05.014 · Cited by 223
Modulation of Androgen Receptor Activation Function 2 by Testosterone and Dihydrotestosterone
Askew, E. B., Gampe, R. T., Stanley, T. B., Faggart, J. L., & Wilson, E. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703268200 · Cited by 211
Estrogen receptor signaling during vertebrate development
Bondesson, M., Hao, R., Lin, C., Williams, C., & Gustafsson, J.-Α. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.06.005 · Cited by 221
Self-citationMolecular basis of bile acid-FXR-FGF15/19 signaling axis
Katafuchi, T., & Makishima, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116046 · Cited by 193
Structure of a Biologically Active Estrogen Receptor-Coactivator Complex on DNA
Yi, P., Wang, Z., Feng, Q. F., Pintilie, G. D., Foulds, C. E., Lanz, R. B., Ludtke, S. J., Schmid, M. F., Chiu, W., & O’Malley, B. W. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.025 · Cited by 196
Expanding functional diversity of the coactivators
Lonard, D. M., & O'Malley, B. W. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.01.001 · Cited by 172
Sex, Gender, and Sex Hormones in Pulmonary Hypertension and Right Ventricular Failure
Hester, J., Ventetuolo, C. E., & Lahm, T. (2019) · Comprehensive physiology · doi:10.1002/cphy.c190011 · Cited by 183
Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes
Yu, X., Yi, P., Hamilton, R. A., Shen, H., Chen, M., Foulds, C. E., Mancini, M. A., Ludtke, S. J., Wang, Z., & O’Malley, B. W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.031 · Cited by 154
Signals and ReceptorsPreprint
Heldin, C., Lu, B. C., Evans, R. M., & Gutkind, J. S. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005900 · Cited by 163
Marciano, D. P., Chang, M. R., Corzo, C. A., Goswami, D., Lam, V. Q., Pascal, B. D., & Griffin, P. R. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2013.12.009 · Cited by 126
Optimized glucocorticoid therapy: teaching old drugs new tricks
Strehl, C., & Buttgereit, F. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.01.026 · Cited by 118
Stossi, F., Likhite, V. S., Katzenellenbogen, J. A., & Katzenellenbogen, B. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513405200 · Cited by 118
Dehm, S. M., & Tindall, D. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605002200 · Cited by 111
The mineralocorticoid receptor and its coregulators
Yang, J., & Young, M. J. (2009) · Journal of Molecular Endocrinology · doi:10.1677/jme-09-0031 · Cited by 120
Malik, S., Guermah, M., Yuan, C., Wu, W., Yamamura, S., & Roeder, R. G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.18.8244-8254.2004 · Cited by 106
Tung, L. W., Abdel-Hafiz, H. A., Shen, T., Harvell, D. M. E., Nitao, L. K., Richer, J. K., Sartorius, C. A., Takimoto, G. S., & Horwitz, K. B. (2006) · Molecular Endocrinology · doi:10.1210/me.2006-0105 · Cited by 96
Velloso, F. J., Bianco, A. F. R., Farias, J. O., Torres, N., Ferruzo, P. Y. M., Anschau, V., Jesus-Ferreira, H. C., Chang, T., Sogayar, M. C., Zerbini, L. F., et al. (2017) · OncoTargets and Therapy · doi:10.2147/ott.s142154 · Cited by 94
Wadosky, K. M., & Willis, M. S. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00703.2011 · Cited by 93
Williams, C., & Lin, C. (2016) · ecancermedicalscience · doi:10.3332/ecancer.2013.370 · Cited by 87
A conserved surface on the ligand binding domain of nuclear receptors for allosteric control
Buzón, V., Carbó, L. R., Estruch, S. B., Fletterick, R. J., & Estébanez‐Perpiñá, E. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.08.012 · Cited by 90
Phosphorylation of Liver X Receptor α Selectively Regulates Target Gene Expression in Macrophages
Pineda‐Torra, I., Ismaı̈li, N., Feig, J. E., Xu, C., Cavasotto, C. N., Pancratov, R., Rogatsky, I., Neubert, T. A., Fisher, E. A. A., & Garabedian, M. J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01575-07 · Cited by 85
Structural and Functional Diversity of Estrogen Receptor Ligands
Farooq, A. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150413154841 · Cited by 81
Lempiäinen, J. K., Niskanen, E. A., Launonen, K., Lampinen, R., Göös, H., Varjosalo, M. T., & Palvimo, J. J. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m117.067488 · Cited by 82
Estrogen-Related Receptors in Breast Cancer and Prostate Cancer
Misawa, A., & Inoue, S. (2015) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00083 · Cited by 76
Zattarin, E., Leporati, R., Ligorio, F., Lobefaro, R., Vingiani, A., Pruneri, G., & Vernieri, C. (2020) · Cells · doi:10.3390/cells9122644 · Cited by 75
Abdullah‐Zawawi, M., Afiqah‐Aleng, N., Ikhwanuddin, M., Sung, Y. Y., Tola, S., Fazhan, H., & Waiho, K. (2021) · Reviews in Aquaculture · doi:10.1111/raq.12552 · Cited by 72
Li, X., Lee, S., & Safe, S. H. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.02.021 · Cited by 71
Bour, G., Lalevée, S., & Rochette‐Egly, C. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.04.003 · Cited by 76
Molecular mechanisms and genome-wide aspects of PPAR subtype specific transactivation
Bugge, A., & Mandrup, S. (2010) · PPAR Research · doi:10.1155/2010/169506 · Cited by 69
Kumar, R., & Litwack, G. (2009) · Steroids · doi:10.1016/j.steroids.2009.07.012 · Cited by 66
Activity of Zearalenone in the Porcine Intestinal Tract
Gajęcka, M., Zielonka, Ł., & Gajęcki, M. T. (2016) · Molecules · doi:10.3390/molecules22010018 · Cited by 66
Estébanez‐Perpiñá, E., Arnold, L. A., Jouravel, N., Togashi, M., Blethrow, J. D., Mar, E., Nguyen, P. T., Phillips, K. J., Baxter, J. D., Webb, P., et al. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0174 · Cited by 66
van de Wijngaart, D. J., van Royen, M. E., Hersmus, R., Pike, A. C. W., Houtsmuller, A. B., Jenster, G. W., Trapman, J., & Dubbink, H. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602567200 · Cited by 66
Schäcke, H., Rehwinkel, H., Asadullah, K., & Cato, A. C. B. (2006) · Experimental Dermatology · doi:10.1111/j.1600-0625.2006.00453.x · Cited by 65
Visualizing the Architectures and Interactions of Nuclear Receptors
Khorasanizadeh, S., & Rastinejad, F. (2016) · Endocrinology · doi:10.1210/en.2016-1559 · Cited by 65
Role of mineralocorticoid receptors on the hypothalamus–pituitary–adrenal axis in humans
Berardelli, R., Karamouzis, I., D’Angelo, V., Zichi, C., Fussotto, B., Giordano, R., Ghigo, E., & Arvat, E. (2012) · Endocrine · doi:10.1007/s12020-012-9750-8 · Cited by 62
In vivo role of the HNF4α AF‐1 activation domain revealed by exon swapping
Briançon, N., & Weiss, M. C. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601021 · Cited by 59
The PPARγ2 A/B-Domain Plays a Gene-Specific Role in Transactivation and Cofactor Recruitment
Bugge, A. K., Grøntved, L., Aagaard, M. M., Borup, R., & Mandrup, S. (2009) · Molecular Endocrinology · doi:10.1210/me.2008-0236 · Cited by 65
Nuclear Receptors as Multiple Regulators of NLRP3 Inflammasome Function
Alatshan, A., & Benkő, S. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.630569 · Cited by 58
Neurotoxic effects of androgens in spinal and bulbar muscular atrophy
Parodi, S., & Pennuto, M. (2011) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2011.06.003 · Cited by 59
Zaveri, N. T., & Murphy, B. J. (2007) · Elsevier eBooks · doi:10.1016/b0-08-045044-x/00063-8 · Cited by 59
Sex Hormones and Lung Inflammation
Reyes-García, J., Montaño, L. M., Carbajal-García, A., & Wang, Y.-X. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-68748-9_15 · Cited by 60
Interactions of the mineralocorticoid receptor – Within and without
Yang, J., & Fuller, P. J. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.07.001 · Cited by 59
Kumar, R., Moure, C. M., Khan, S. H., Callaway, C., Grimm, S. L., Goswami, D., Griffin, P. R., & Edwards, D. P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.491787 · Cited by 56
Non-genomic effects of the NR4A1/Nur77/TR3/NGFIB orphan nuclear receptor
Pawlak, A., Strządała, L., & Kałas, W. (2014) · Steroids · doi:10.1016/j.steroids.2014.12.020 · Cited by 53
Steroid Hormone Receptors: Links With Cell Cycle Machinery and Breast Cancer Progression
Saha, S., Dey, S., & Nath, S. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.620214 · Cited by 52
Lenaerts, C., Wielendaele, P. V., Peeters, P., Broeck, J. V., & Marchal, E. (2016) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2016.05.003 · Cited by 57
Bour, G., Plassat, J., Bauer, A., Lalevée, S., & Rochette‐Egly, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501344200 · Cited by 50
Retinoic acid receptor structures: the journey from single domains to full-length complex
Rastinejad, F. (2022) · Journal of Molecular Endocrinology · doi:10.1530/jme-22-0113 · Cited by 53
Understanding response and resistance to oestrogen deprivation in ER-positive breast cancer
Patani, N., & Martin, L. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.09.038 · Cited by 50
Oleanolic acid is a selective farnesoid X receptor modulator
Liu, W., & Wong, C. (2009) · Phytotherapy Research · doi:10.1002/ptr.2948 · Cited by 49
Regulation of the transcriptional activity of nuclear receptors by the MEK/ERK1/2 pathway
Zassadowski, F., Rochette‐Egly, C., Chomienne, C., & Cassinat, B. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.08.003 · Cited by 56
Jones, A., Kulozik, P., Ostertag, A., & Herzig, S. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0973 · Cited by 47
Dubbink, H. J., Hersmus, R., Pike, A. C. W., Molier, M., Brinkmann, A. O., Jenster, G., & Trapman, J. (2006) · Molecular Endocrinology · doi:10.1210/me.2005-0348 · Cited by 47
Nuclear receptors and chromatin: an inducible couple
Gadaleta, R. M., & Magnani, L. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0170 · Cited by 52
Wardell, S. E., Kwok, S. C., Sherman, L., Hodges, R. S., & Edwards, D. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.20.8792-8808.2005 · Cited by 47
Garapaty, S., Mahajan, M., & Samuels, H. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706986200 · Cited by 44
Nuclear and extranuclear effects of vitamin A
Iskakova, M., Karbyshev, M. S., Piskunov, A., & Rochette‐Egly, C. (2015) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2014-0522 · Cited by 47
SPBP Is a Phosphoserine-Specific Repressor of Estrogen Receptor α
Gburcik, V., Bot, N. L., Maggiolini, M., & Picard, D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.9.3421-3430.2005 · Cited by 43
Modulation of Androgen Receptor Transactivation by FoxH1
Chen, G., Nomura, M., Morinaga, H., Matsubara, E., Okabe, T., Goto, K., Yanase, T., Zheng, H., Lu, J., & Nawata, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506147200 · Cited by 43
Orphan nuclear receptors as drug targets for the treatment of prostate and breast cancers
Roshan‐Moniri, M., Hsing, M., Butler, M. S., Cherkasov, A. R., & Rennie, P. S. (2014) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2014.10.005 · Cited by 42
Watanabe, T., Takeuchi, H., & Kubo, T. (2010) · BMC Evolutionary Biology · doi:10.1186/1471-2148-10-40 · Cited by 42
Whitfield, G., Jurutka, P., Haussler, C., Hsieh, J.-C., Barthel, T., Jacobs, E. T., Dominguez, C. E., Thatcher, M. L., & Haussler, M. (2005) · Elsevier eBooks · doi:10.1016/b978-012252687-9/50016-4 · Cited by 48
Li, H., Zhang, W., Niu, C., Lin, C., Wu, X., Jian, Y., Li, Y., Ye, L., Dai, Y., Ouyang, Y., et al. (2019) · International Journal of Cancer · doi:10.1002/ijc.32293 · Cited by 40
Natural products as modulators of retinoic acid receptor-related orphan receptors (RORs)
Ladurner, A., Schwarz, P. F., & Dirsch, V. M. (2020) · Natural Product Reports · doi:10.1039/d0np00047g · Cited by 44
Dissociated non-steroidal glucocorticoid receptor modulators: an update on new compounds
Schäcke, H., Berger, M., Hansson, T. G., McKerrecher, D., & Rehwinkel, H. (2008) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.18.3.339 · Cited by 39
Kim, S. B., Awais, M., Sato, M., Umezawa, Y., & Tao, H. (2007) · Analytical Chemistry · doi:10.1021/ac061934u · Cited by 38
Use of Phage Display to Identify Novel Mineralocorticoid Receptor-Interacting Proteins
Yang, J., Fuller, P. J., Morgan, J., Shibata, H., McDonnell, D. P., Clyne, C. D., & Young, M. J. (2014) · Molecular Endocrinology · doi:10.1210/me.2014-1101 · Cited by 38
Nuclear Receptors: Small Molecule Sensors that Coordinate Growth, Metabolism and Reproduction
Pardee, K., Necakov, A., & Krause, H. M. (2011) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-9069-0_6 · Cited by 39
Orphan Nuclear Receptors and the Regulation of Nutrient Metabolism: Understanding Obesity
Pearen, M. A., & Muscat, G. E. O. (2012) · Physiology · doi:10.1152/physiol.00007.2012 · Cited by 34
Nuclear Compartmentalization of N-CoR and Its Interactions with Steroid Receptors
Wu, Y., Kawate, H., Ohnaka, K., Nawata, H., & Takayanagi, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01534-05 · Cited by 36
Nuclear and Extra-Nuclear Effects of Retinoid Acid Receptors: How They Are Interconnected
Piskunov, A., Tanoury, Z. A., & Rochette‐Egly, C. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9050-5_6 · Cited by 38
Feng, S., Xu, S. H., Wen, Z., & Zhu, Y. (2015) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2015.2155 · Cited by 33
Connaghan, K. D., Heneghan, A. F., Miura, M. T., & Bain, D. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608848104 · Cited by 34
Yamamoto, Y., Shibata, J., Yonekura, K., Sato, K., Hashimoto, A., Aoyagi, Y., Wierzba, K., Yano, S., Asao, T., Buzdar, A. U., et al. (2005) · PubMed · Cited by 34
Tennessen, J. M., Opperman, K. J., & Rougvie, A. E. (2010) · Development · doi:10.1242/dev.048850 · Cited by 33
Dominant negative factors in health and disease
Veitia, R. A. (2009) · The Journal of Pathology · doi:10.1002/path.2583 · Cited by 33
Heat Shock Proteins in Benign Prostatic Hyperplasia and Prostate Cancer
Ratajczak, W., Lubkowski, M., & Lubkowska, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020897 · Cited by 32
HNF4α isoforms: the fraternal twin master regulators of liver function
Radi, S. H., Vemuri, K., Martinez-Lomeli, J., & Sladek, F. M. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1226173 · Cited by 34
Deegan, B. J., Bona, A., Bhat, V. S., Mikles, D. C., McDonald, C. B., Seldeen, K. L., & Farooq, A. (2011) · Journal of Molecular Recognition · doi:10.1002/jmr.1148 · Cited by 31
Yamamoto, Y., Shibata, J., Yonekura, K., Sato, K., Hashimoto, A., Aoyagi, Y., Wierzba, K., Yano, S., Asao, T., Buzdar, A. U., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.315.11.1 · Cited by 32
Retinoic Acid Receptors: Structural Basis for Coregulator Interaction and Exchange
le Maire, A., & Bourguet, W. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9050-5_3 · Cited by 32
Pearce, K. H., Iannone, M. A., Simmons, C. A., & Gray, J. G. (2004) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03201-5 · Cited by 32
Pederick, J. L., Frkic, R. L., McDougal, D. P., & Bruning, J. B. (2024) · Chemosphere · doi:10.1016/j.chemosphere.2024.141723 · Cited by 31
Allosteric pathways in nuclear receptors — Potential targets for drug design
Fernandez, E. J. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.10.014 · Cited by 32
[Molecular aspects of glucocorticoid sensitivity].
Faria, C., & Longui, C. (2006) · Arquivos brasileiros de endocrinologia e metabologia · doi:10.1590/s0004-27302006000600003 · Cited by 19
Characterization of porcine pregnane X receptor, farnesoid X receptor and their splice variants
Gray, M. A., Pollock, C. B., Schook, L. B., & Squires, E. J. (2010) · Experimental Biology and Medicine · doi:10.1258/ebm.2010.009339 · Cited by 30
Digoxin, an Overlooked Agonist of RORγ/RORγT
Karaś, K., Sałkowska, A., Sobalska‐Kwapis, M., Walczak‐Drzewiecka, A., Strapagiel, D., Dastych, J., Bachorz, R. A., & Ratajewski, M. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01460 · Cited by 30
Function and Evolution of Nuclear Receptors in Environmental-Dependent Postembryonic Development
Taubenheim, J., Kortmann, C., & Fraune, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653792 · Cited by 28
Chung, H. H., Sze, S. K., Woo, A. R. E., Sun, Y., Sim, K. H., Dong, X., & Lin, V. C. L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.522839 · Cited by 30
Metadata
- Authors
- Wärnmark, A., Treuter, E., Wright, A. P. H., & Gustafsson, J.-A.
- Affiliations
- Departments of BioSciences (A.W., E.T., A.P.H.W., J.-Å.G.), S-141 89 Huddinge, Sweden
- Södertörn University (SE)
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2003-10-01
- Volume
- 17
- Issue
- 10
- Pages
- 1901-1909
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- OpenAlex
- W1964247670
- Cited by
- 308
- References
- 99
- Citations by year
- 2026: 3 · 2025: 13 · 2024: 10 · 2023: 16 · 2022: 20 · 2021: 10 · 2020: 16 · 2019: 14 · 2018: 7 · 2017: 14 · 2016: 11 · 2015: 11 · 2014: 20 · 2013: 12 · 2012: 17
- FWCI
- 1.33
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Karolinska Institutet
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
- Keywords
- nuclear receptors, activation functions, AF-2, transcriptional activation, transcriptional coactivator, general transcription factors, preinitiation complex, chromatin remodeling, histone modifications, RNA polymerase II, ligand-independent receptor activation, ligand-dependent activation
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Promoter Regions, Genetic, Protein Binding, Transcription Factors, Transcription, Genetic, Transcriptional Activation, Receptors, Cytoplasmic and Nuclear
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review