The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
The RXR heterodimers and orphan receptors
Open accessAbstract
The nuclear receptor superfamily is comprised of over 150 different proteins that have evolved to mediate a complex array of extracellular signals into transcriptional responses. Many, but not all, of these proteins directly bind to signaling molecules, which, because of their small lipophilic character, can easily enter the target cell. Thus, unlike membrane-bound receptors, the nuclear receptors are intracellular and function to control the activity of target genes directly. In aggregate, these target genes comprise a genetic network whose coordinate activity defines the physiologic response. The purpose of this review is to establish the historical links between the steroid and nonsteroid receptor signaling systems, to chart the explosive development of the retinoid X receptor (RXR) heterodimer and orphan receptor family, to explain the impact of these discoveries on our understanding of the mechanisms of hormonal signaling, and, finally, to present emerging issues and implications of these studies for animal development, physiology, and human disease.
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.
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
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
Self-citationActivation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
Issemann, I., & Green, S. (1990) · Nature · doi:10.1038/347645a0 · Cited by 3,519
A human retinoic acid receptor which belongs to the family of nuclear receptors
Petkovich, M., Brand, N. J., Krust, A., & Chambon, P. (1987) · Nature · doi:10.1038/330444a0 · Cited by 2,214
Identification of a receptor for the morphogen retinoic acid
Giguere, V., Ong, E. S., Segui, P., & Evans, R. M. (1987) · Nature · doi:10.1038/330624a0 · Cited by 1,965 · cited 1×
“Thus, the RAR was the first known orphan receptor for which a ligand (all-frans retinoic acid) was identified (Giguere et al., 1987; Petkovich et al., 1987).”
BackgroundSelf-citation9-cis retinoic acid is a high affinity ligand for the retinoid X receptor
Heyman, R. A., Mangelsdorf, D. J., Dyck, J. A., Stein, R. B., Eichele, G., Evans, R. M., & Thaller, C. (1992) · Cell · doi:10.1016/0092-8674(92)90479-v · Cited by 1,780 · cited 1×
“The hunt for its true ligand (retinoid X) led two groups working independently and using different techniques to the discovery that a stereoisomer of retinoic acid, 9-cis retinoic acid, is a high affinity RXR ligand (Heyman et al., 1992; Levin et al., 1992).”
BackgroundSelf-citationCrystallographic analysis of the interaction of the glucocorticoid receptor with DNA
Luisi, B. F., Xu, W. X., Otwinowski, Z., Freedman, L. P., Yamamoto, K. R., & Sigler, P. B. (1991) · Nature · doi:10.1038/352497a0 · Cited by 1,503
Zanaria, E., Muscatelli, F., Bardoni, B., Strom, T. M., Guioli, S., Guo, W., Lalli, E., Moser, C., Walker, A. P., McCabe, E. R. B., et al. (1994) · Nature · doi:10.1038/372635a0 · Cited by 858
Multiplicity generates diversity in the retinoic acid signalling pathways
Leid, M., Kastner, P., & Chambon, P. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90014-z · Cited by 821 · cited 2×
“The discovery of RAR and RXR as two retinoid signaling pathways has greatly contributed to our understanding of the developmental and physiologic networks governed by vitamin A (reviewed by Mangelsdorf et al., 1994; Leid et al., 1992a).”
BackgroundLala, D. S. (1992) · Molecular Endocrinology · doi:10.1210/me.6.8.1249 · Cited by 678
Regulation of retinoid signalling by receptor polarity and allosteric control of ligand binding
Kurokawa, R., DiRenzo, J., Boehm, M., Sugarman, J., Gloss, B., Rosenfeld, M. G., Heyman, R. A., & Glass, C. K. (1994) · Nature · doi:10.1038/371528a0 · Cited by 429
Cited by
Identification of a nuclear receptor for bile acids
Makishima, M., Okamoto, A. Y., Repa, J. J., Tu, H., Learned, R. M., Luk, A., Hull, M. V., Lustig, K. D., Mangelsdorf, D. J., & Shan, B. (1999) · Science · doi:10.1126/science.284.5418.1362 · Cited by 2,714
Self-citationThe 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
Forman, B. M., Chen, J., & Evans, R. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4312 · Cited by 2,116
Self-citationNuclear Receptors and Lipid Physiology: Opening the X-Files
Chawla, A., Repa, J. J., Evans, R. M., & Mangelsdorf, D. J. (2001) · Science · doi:10.1126/science.294.5548.1866 · Cited by 2,085
Self-citationA regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis
Goodwin, B., Jones, S. A., Price, R. R., Watson, M. A., McKee, D. D., Moore, L. B., Galardi, C., Wilson, J. G., Lewis, M. C., Roth, M. E., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00051-4 · Cited by 1,940
Differential Ligand Activation of Estrogen Receptors ERα and ERβ at AP1 Sites
Paech, K., Webb, P., Kuiper, G. G. J. M., Nilsson, S., Gustafsson, J.-Å., Kushner, P. J., & Scanlan, T. S. (1997) · Science · doi:10.1126/science.277.5331.1508 · Cited by 1,861
Endogenous Bile Acids Are Ligands for the Nuclear Receptor FXR/BAR
Wang, H., Chen, J., Hollister, K., Sowers, L. C., & Forman, B. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80348-2 · Cited by 1,636
Retinoic acid imprints gut-homing specificity on T cells
Iwata, M., Hirakiyama, A., Eshima, Y., Kagechika, H., Kato, C., & Song, S.-Y. (2004) · Immunity · doi:10.1016/j.immuni.2004.08.011 · Cited by 1,541
Khovidhunkit, W., Kim, M.-S., Memon, R. A., Shigenaga, J. K., Moser, A. H., Feingold, K. R., & Grunfeld, C. (2004) · Journal of Lipid Research · doi:10.1194/jlr.r300019-jlr200 · Cited by 1,481
Combinatorial Control of Gene Expression by Nuclear Receptors and Coregulators
McKenna, N. J., & O'Malley, B. W. (2002) · Cell · doi:10.1016/s0092-8674(02)00641-4 · Cited by 1,463
Nuclear Receptor Repression Mediated by a Complex Containing SMRT, mSin3A, and Histone Deacetylase
Nagy, L., Kao, H.-Y., Chakravarti, D., Lin, R. J., Hassig, C. A., Ayer, D. E., Schreiber, S. L., & Evans, R. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80218-4 · Cited by 1,230
Self-citationSchoonjans, K., Staels, B., & Auwerx, J. (1996) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42003-6 · Cited by 1,216
Bile salt transporters: molecular characterization, function, and regulation
Trauner, M., & Boyer, J. L. (2003) · Physiological Reviews · doi:10.1152/physrev.00027.2002 · Cited by 999
Rosenfeld, M. G., Lunyak, V. V., & Glass, C. K. (2006) · Genes & Development · doi:10.1101/gad.1424806 · Cited by 952
Bile acid signaling in metabolic disease and drug therapy
Li, T., & Chiang, J. Y. L. (2014) · Pharmacological Reviews · doi:10.1124/pr.113.008201 · Cited by 935
Nuclear retinoid receptors and the transcription of retinoid-target genes
Bastien, J., & Rochette-Egly, C. (2004) · Gene · doi:10.1016/j.gene.2003.12.005 · Cited by 773
Overview of nomenclature of nuclear receptors
Germain, P., Staels, B., Dacquet, C., Spedding, M., & Laudet, V. (2006) · Pharmacological Reviews · doi:10.1124/pr.58.4.2 · Cited by 688
Transcription Factors, Normal Myeloid Development, and Leukemia
Tenen, D. G., Hromas, R., Licht, J. D., & Zhang, D.-E. (1997) · Blood · doi:10.1182/blood.v90.2.489 · Cited by 735
Molecular determinants of crosstalk between nuclear receptors and toll-like receptors
Ogawa, S., Lozach, J., Benner, C., Pascual, G., Tangirala, R. K., Westin, S., Hoffmann, A., Subramaniam, S., David, M., Rosenfeld, M. G., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.029 · Cited by 647
Triterpenoids and rexinoids as multifunctional agents for the prevention and treatment of cancer
Liby, K. T., Yore, M. M., & Sporn, M. B. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2129 · Cited by 637
Ecdysone receptors and their biological actions
Riddiford, L. M., Cherbas, P., & Truman, J. W. (2000) · Vitamins & Hormones · doi:10.1016/s0083-6729(00)60016-x · Cited by 605
Zoeller, R. T., & Rovet, J. (2004) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2004.01243.x · Cited by 605
The casein kinase 1 family: participation in multiple cellular processes in eukaryotes
Knippschild, U., Gocht, A., Wolff, S., Huber, N., Löhler, J., & Stöter, M. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2004.12.011 · Cited by 601
Duester, G. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01497.x · Cited by 570
Intestine-selective farnesoid X receptor inhibition improves obesity-related metabolic dysfunction
Jiang, C., Xie, C., Lv, Y., Li, J., Krausz, K. W., Shi, J., Brocker, C. N., Desai, D., Amin, S. G., Bisson, W. H., et al. (2015) · Nature Communications · doi:10.1038/ncomms10166 · Cited by 559
Laudet, V (1997) · Journal of Molecular Endocrinology · doi:10.1677/jme.0.0190207 · Cited by 557
Niederreither, K., McCaffery, P., Dräger, U. C., Chambon, P., & Dollé, P. (1997) · Mechanisms of Development · doi:10.1016/s0925-4773(96)00653-3 · Cited by 523
Orphan Nuclear Receptors: Shifting Endocrinology into Reverse
Kliewer, S. A., Lehmann, J. M., & Willson, T. M. (1999) · Science · doi:10.1126/science.284.5415.757 · Cited by 499
Peroxisome proliferator-activated receptors: insight into multiple cellular functions
Escher, P., & Wahli, W. (2000) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/s0027-5107(99)00231-6 · Cited by 491
Gradin, K., McGuire, J., Wenger, R. H., Kvietikova, I., Whitelaw, M. L., Toftgård, R., Tora, L., Gassmann, M., & Poellinger, L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5221 · Cited by 470
Role of Hormones in Pilosebaceous Unit Development
Deplewski, D., & Rosenfield, R. L. (2000) · Endocrine Reviews · doi:10.1210/edrv.21.4.0404 · Cited by 443
Ding, X. F., Anderson, C. M., Ma, H., Hong, H., Uht, R. M., Kushner, P. J., & Stallcup, M. R. (1998) · Molecular Endocrinology · doi:10.1210/mend.12.2.0065 · Cited by 434
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
Identification of the Retinoic Acid-inducible All-trans-retinoic Acid 4-Hydroxylase
White, J. A., Guo, Y.-D., Baetz, K., Beckett-Jones, B., Bonasoro, J., Hsu, K. E., Dilworth, F. J., Jones, G., & Petkovich, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.47.29922 · Cited by 382
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
Wang, H., Liu, K., Geng, M., Gao, P., Wu, X., Hai, Y., Li, Y., Li, Y., Luo, L., Hayes, J. D., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3386 · Cited by 382
Li, X. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms108 · Cited by 360
Differentiation therapy of leukemia: 3 decades of development.
Nowak, D., Stewart, D., & Koeffler, H. P. (2009) · Blood · doi:10.1182/blood-2009-01-198911 · Cited by 348
The role of PPARs in inflammation and immunity
Clark, R. B. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.71.3.388 · Cited by 337
Kemper, J. K., Xiao, Z., Ponugoti, B., Miao, J., Fang, S., Kanamaluru, D., Tsang, S., Wu, S.-Y., Chiang, C.-M., & Veenstra, T. D. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.09.009 · Cited by 332
A constitutively active dioxin/aryl hydrocarbon receptor induces stomach tumors
Andersson, P., McGuire, J., Rubio, C., Gradin, K., Whitelaw, M. L., Pettersson, S., Hanberg, A., & Poellinger, L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152706299 · Cited by 310
Rochette-Egly, C., Adam, S., Rossignol, M., Egly, J.-M., & Chambon, P. (1997) · Cell · doi:10.1016/s0092-8674(00)80317-7 · Cited by 308
PPARδ is a very low-density lipoprotein sensor in macrophages
Chawla, A., Lee, C.-H., Barak, Y., He, W., Rosenfeld, J., Liao, D., Han, J., Kang, H., & Evans, R. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0337331100 · Cited by 305
Self-citationNuclear-receptor interactions on DNA-response elements
Khorasanizadeh, S., & Rastinejad, F. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01800-x · Cited by 288
Drosophila Ecdysone Receptor Mutations Reveal Functional Differences among Receptor Isoforms
Bender, M., Imam, F. B., Talbot, W. S., Ganetzky, B., & Hogness, D. S. (1997) · Cell · doi:10.1016/s0092-8674(00)80466-3 · Cited by 280
Ding, Y., Qiao, A., Wang, Z., Goodwin, J. S., Lee, E.-S., Block, M. L., Allsbrook, M., McDonald, M. P., & Fan, G.-H. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3153-08.2008 · Cited by 269
Phytochemicals as inhibitors of NF-κB for treatment of Alzheimer’s disease
Seo, E.-J., Fischer, N., & Efferth, T. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2017.11.030 · Cited by 265
McKay, R. M., McKay, J. P., Avery, L., & Graff, J. M. (2003) · Developmental Cell · doi:10.1016/s1534-5807(02)00411-2 · Cited by 269
Zhang, L., Ren, X.-M., & Guo, L.-H. (2013) · Environmental Science & Technology · doi:10.1021/es4026722 · Cited by 267
Nuclear Receptors in Liver Disease Δ
Wagner, M., Zollner, G., & Trauner, M. (2011) · Hepatology · doi:10.1002/hep.24148 · Cited by 260
Depew, M. J., Tucker, A. S., & Sharpe, P. T. (2002) · Mouse Development · doi:10.1016/b978-012597951-1/50023-8 · Cited by 259
Nuclear receptors in macrophage biology: at the crossroads of lipid metabolism and inflammation
Castrillo, A., & Tontonoz, P. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.012103.134432 · Cited by 260
A class B scavenger receptor mediates the cellular uptake of carotenoids in Drosophila
Kiefer, C., Sumser, E., Wernet, M. F., & von Lintig, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162182899 · Cited by 255
Coordination of inflammation and metabolism by PPAR and LXR nuclear receptors
Hong, C., & Tontonoz, P. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.07.016 · Cited by 253
Edwards (2002) · doi:10.1016/s1537-1891(02)00175-1 · Cited by 233
The Acute Phase Response Is Associated with Retinoid X Receptor Repression in Rodent Liver
Beigneux, A. P., Moser, A. H., Shigenaga, J. K., Grunfeld, C., & Feingold, K. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000953200 · Cited by 223
Akhmedov, N. B., Piriev, N. I., Chang, B., Rapoport, A. L., Hawes, N. L., Nishina, P. M., Nusinowitz, S., Heckenlively, J. R., Roderick, T. H., Kozak, C. A., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5551 · Cited by 221
Target Genes of Peroxisome Proliferator-activated Receptor γ in Colorectal Cancer Cells
Gupta, R. A., Brockman, J. A., Sarraf, P., Willson, T. M., & DuBois, R. N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103779200 · Cited by 215
Regulation of photoreceptor gene expression by Crx-associated transcription factor network
Hennig, A. K., Peng, G.-H., & Chen, S. (2008) · Brain Research · doi:10.1016/j.brainres.2007.06.036 · Cited by 214
Multidomain integration in the structure of the HNF-4α nuclear receptor complex
Chandra, V., Huang, P., Potluri, N., Wu, D., Kim, Y., & Rastinejad, F. (2013) · Nature · doi:10.1038/nature11966 · Cited by 206
Bouillet, P., Sapin, V., Chazaud, C., Messaddeq, N., Décimo, D., Dollé, P., & Chambon, P. (1997) · Mechanisms of Development · doi:10.1016/s0925-4773(97)00039-7 · Cited by 209
Delva, L., Bastie, J.-N., Rochette-Egly, C., Kraïba, R., Balitrand, N., Despouy, G., Chambon, P., & Chomienne, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.7158 · Cited by 208
Alcohol and aldehyde dehydrogenases: Retinoid metabolic effects in mouse knockout models
Kumar, S., Sandell, L. L., Trainor, P. A., Koentgen, F., & Duester, G. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.04.004 · Cited by 190
BOST, F., CARON, L., MARCHETTI, I., DANI, C., MARCHAND-BRUSTEL, Y. L., & BINÉTRUY, B. (2002) · Biochemical Journal · doi:10.1042/bj3610621 · Cited by 184
Mamontova, A., Séguret-Macé, S., Esposito, B., Chaniale, C., Bouly, M., Delhaye-Bouchaud, N., Luc, G., Staels, B., Duverger, N., Mariani, J., et al. (1998) · Circulation · doi:10.1161/01.cir.98.24.2738 · Cited by 172
Liang, Y., Lin, S., Beyer, T. P., Zhang, Y., Wu, X., Bales, K. R., DeMattos, R. B., May, P. C., Li, S. D., Jiang, X., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02183.x · Cited by 160
Mechanisms of Androgen Induction of Sebocyte Differentiation
Rosenfield, R. L., Deplewski, D., Kentsis, A., & Ciletti, N. (1998) · Dermatology · doi:10.1159/000017864 · Cited by 156
Giannì, M., Bauer, A., Garattini, E., Chambon, P., & Rochette‐Egly, C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf374 · Cited by 151
ROR nuclear receptors: Structures, related diseases, and drug discovery
Zhang, Y., Luo, X.-Y., Wu, D.-H., & Xu, Y. (2015) · Acta Pharmacologica Sinica · doi:10.1038/aps.2014.120 · Cited by 151
Verrijdt, G. (2003) · Molecular Genetics and Metabolism · doi:10.1016/s1096-7192(03)00003-9 · Cited by 148
Nuclear receptors as therapeutic targets in cholestatic liver diseases
Zollner, G., & Trauner, M. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2008.00030.x · Cited by 146
Vu-Dac, N., Gervois, P., Torra, I. P., Fruchart, J. C., Kosykh, V, Kooistra, T., Princen, H. M., Dallongeville, J., & Staels, B. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1581 · Cited by 143
Liver X receptors as regulators of macrophage inflammatory and metabolic pathways
A-González, N., & Castrillo, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.12.015 · Cited by 139
Retinoic acid-gated sequence-specific translational control by RARα
Poon, M. M., & Chen, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807740105 · Cited by 138
Retinoic acid in the immune system
Pino‐Lagos, K., Benson, M. J., & Noelle, R. J. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1443.017 · Cited by 138
Thyroid hormone action: a binding contract
Lazar, M. A. (2003) · Journal of Clinical Investigation · doi:10.1172/jci19479 · Cited by 143
Núñez, V., Alameda, D., Rico, D., Mota, R., Gonzalo, P., Cedenilla, M., Fischer, T., Boscá, L., Glass, C. K., Arroyo, A. G., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913545107 · Cited by 133
Nuclear receptors as therapeutic targets for Alzheimer's disease
Mandrekar-Colucci, S., & Landreth, G. E. (2011) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.594043 · Cited by 126
Doucas, V., Shi, Y., Miyamoto, S., West, A., Verma, I., & Evans, R. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220413297 · Cited by 125
Self-citationNitric oxide synthase 2 and cyclooxygenase 2 interactions in inflammation
Weinberg, J. B. (2000) · Immunologic Research · doi:10.1385/ir:22:2-3:319 · Cited by 121
Towards a better understanding of carotenoid metabolism in animals
von Lintig, J., Hessel, S., Isken, A., Kiefer, C., Lampert, J. M., Voolstra, O., & Vogt, K. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.11.010 · Cited by 116
The mechanism of phosphorylation‐inducible activation of the ETS‐domain transcription factor Elk‐1
Yang, S., Shore, P., Willingham, N., Lakey, J. H., & Sharrocks, A. D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.20.5666 · Cited by 112
Taneja, R., Rochette‐Egly, C., Plassat, J., Penna, L., Gaub, M., & Chambon, P. (1997) · The EMBO Journal · doi:10.1093/emboj/16.21.6452 · Cited by 113
Lan, Q., Hiruma, K., Hu, X., Jindra, M., & Riddiford, L. M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.4897 · Cited by 107
Bastien, J., Adam-Stitah, S., Riedl, T., Egly, J.-M., Chambon, P., & Rochette-Egly, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001985200 · Cited by 107
Hodin, J., & Riddiford, L. M. (1998) · Development Genes and Evolution · doi:10.1007/s004270050186 · Cited by 105
Functional Association between CBP and HNF4 inTrans-activation
Yoshida, E., Aratani, S., Itou, H., Miyagishi, M., Takiguchi, M., Osumu, T., Murakami, K., & Fukamizu, A. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7871 · Cited by 104
Jiang, Y., Feng, D., Ma, X., Fan, S., Gao, Y., Fu, K., Wang, Y., Sun, J., Yao, X., Liu, C., et al. (2019) · Hepatology · doi:10.1002/hep.30131 · Cited by 103
The hinge region in androgen receptor control
Clinckemalie, L., Vanderschueren, D., Boonen, S., & Claessens, F. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.02.019 · Cited by 104
Bile Acid Receptors and the Gut–Liver Axis in Nonalcoholic Fatty Liver Disease
Xue, R., Su, L., Lai, S., Wang, Y., Zhao, D., Fan, J., Chen, W., Hylemon, P. B., & Zhou, H. (2021) · Cells · doi:10.3390/cells10112806 · Cited by 95
Antonson, P., Schuster, G. U., Wang, L., Rozell, B., Holter, E., Flodby, P., Treuter, E., Holmgren, L., & Gustafsson, J.-Å. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.4.1260-1268.2003 · Cited by 95
Tamibarotene: A Candidate Retinoid Drug for Alzheimer’s Disease
Fukasawa, H., Nakagomi, M., Yamagata, N., Katsuki, H., Kawahara, K., Kitaoka, K., Miki, T., & Shudo, K. (2012) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b12-00314 · Cited by 91
Metabolic Effects of Rexinoids: Tissue-Specific Regulation of Lipoprotein Lipase Activity
Davies, P. J. A., Berry, S. A., Shipley, G. L., Eckel, R. H., Hennuyer, N., Crombie, D. L., Ogilvie, K. M., Peinado-Onsurbe, J., Fievet, C., Leibowitz, M. D., et al. (2001) · Molecular Pharmacology · doi:10.1124/mol.59.2.170 · Cited by 89
Regulation of RXR-RAR Heterodimers by RXR- and RAR-Specific Ligands and Their Combinations
le Maire, A., Teyssier, C., Balaguer, P., Bourguet, W., & Germain, P. (2019) · Cells · doi:10.3390/cells8111392 · Cited by 88
Pike, J. W., & Meyer, M. B. (2012) · Rheumatic Disease Clinics of North America · doi:10.1016/j.rdc.2012.03.004 · Cited by 86
Impacts of transcriptional regulation on aging and senescence
Roy, A. K., Oh, T., Rivera, O., Mubiru, J., Song, C. S., & Chatterjee, B. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(02)00006-5 · Cited by 72
Liu, Z., & R. Simpson, E. (1999) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(99)00036-2 · Cited by 71
Peroxisome Proliferator-Activated Receptors and Skin Development
Rosenfield, R. L., Deplewski, D., & Greene, M. E. (2000) · Hormone Research in Paediatrics · doi:10.1159/000053270 · Cited by 69
Srinivas, H., Juroske, D. M., Kalyankrishna, S., Cody, D. D., Price, R. E., Xu, X.-C., Narayanan, R., Weigel, N. L., & Kurie, J. M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.1054-1069.2005 · Cited by 68
The NR4A orphan nuclear receptors mediate transcription-dependent hippocampal synaptic plasticity
Bridi, M. S., & Abel, T. (2013) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2013.06.020 · Cited by 66
Metadata
- Authors
- Mangelsdorf, D. J., & Evans, R. M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 83
- Issue
- 6
- Pages
- 841-850
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1995754186
- Cited by
- 3,158
- References
- 10
- FWCI
- 64.29
- Type
- journal article
- Language
- en
- Open access
- bronze
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
