Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor
Abstract
The vitamin A derivative, retinoic acid, can regulate morphogenesis and differentiation in vertebrates. Two different subfamilies of the steroid receptor superfamily of transcription factors, the retinoic acid receptors and the retinoid X receptor, mediate the effects of retinoic acid. As part of an analysis of the hormonal control of development, we have examined the Drosophila genome for retinoic acid receptor homologues. Here we describe one such gene, XR2C, which encodes a product with structural similarity to the human retinoic acid-responsive transcription factor, retinoid X receptor. This receptor-like protein is encoded by ultraspiracle (usp), a locus required both maternally and zygotically for pattern formation. The discovery that the usp product is a retinoid X receptor homologue suggests that similar chemical cues underlie morphogenic signalling in vertebrate and invertebrate systems.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
EcR must interact with USP/RXR to form a heterodimeric transcription complex, EcR/USP.
“EcR must interact with the ultraspiracle protein (USP), retinoid X receptor (RXR) in Hemimetabola, the ortholog of the retinoid X receptor in vertebrates, to form a heterodimeric transcription complex, EcR/USP [37].”
From G protein-coupled receptors function as cell membrane receptors for the steroid hormone 20-hydroxyecdysone (2020) · cites this paper as [37]
Nuclear receptors act by forming homodimers or heterodimers.
“Nuclear receptors act by forming homodimers or heterodimers. For example, the glucocorticoid receptor [1] and estrogen receptor [2] form a homodimer, and insect ecdysone receptor (EcR) forms a heterodimer with an ultraspiracle protein (USP), the ortholog of retinoid X receptor in vertebrates [3].”
From G-protein-coupled receptor participates in 20-hydroxyecdysone signaling on the plasma membrane (2014) · cites this paper as [3]
Cites
A comprehensive set of sequence analysis programs for the VAX
Devereux, J., Haeberli, P. E., & Smithies, O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.1part1.387 · Cited by 14,222 · see citing works
The Steroid and Thyroid Hormone Receptor Superfamily
Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,442 · see citing works
Self-citationThe Genetics and Biology of Drosophila
(1978) · Food and Cosmetics Toxicology · doi:10.1016/s0015-6264(78)80200-4 · Cited by 3,776 · see citing works
Genetic variations of Drosophila melanogaster.
Lindsley, D. L., & Grell, E. H. (1968) · Biodiversity Heritage Library (Smithsonian Institution) · doi:10.5281/zenodo.10755360 · Cited by 2,623 · see citing works
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 · see citing works
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 · see citing works
Self-citationArriza, J. L., Weinberger, C., Cerelli, G., Glaser, T. M., Handelin, B. L., Housman, D. E., & Evans, R. M. (1987) · Science · doi:10.1126/science.3037703 · Cited by 1,946 · see citing works
Self-citationPrimary 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
Self-citationNuclear receptor that identifies a novel retinoic acid response pathway
Mangelsdorf, D. J., Ong, E. S., Dyck, J. A., & Evans, R. M. (1990) · Nature · doi:10.1038/345224a0 · Cited by 1,491 · see citing works
Self-citationComparison of the consensus sequence flanking translational start sites inDrosophilaand vertebrates
Cavener, D. R. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.4.1353 · Cited by 965 · see citing works
Sequence, structure, and codon preference of theDrosophilaribosomal protein 49 gene
O'Connell, P., & Rosbash, M. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.13.5495 · Cited by 519 · see citing works
Segraves, W. A., & Hogness, D. S. (1990) · Genes & Development · doi:10.1101/gad.4.2.204 · Cited by 485 · see citing works
Sigma factors fromE. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins
Gribskov, M., & Burgess, R. R. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.16.6745 · Cited by 450 · see citing works
Boggs, R. T., Gregor, P., Idriss, S., Belote, J. M., & McKeown, M. (1987) · Cell · doi:10.1016/0092-8674(87)90332-1 · Cited by 413 · see citing works
Self-citationA transposable P vector that confers selectable G418 resistance to Drosophila larvae
Steller, H., & Pirrotta, V. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb02332.x · Cited by 286 · see citing works
Retinoids, homeobox genes, and limb morphogenesis
Brockes, J. P. (1989) · Neuron · doi:10.1016/0896-6273(89)90066-4 · Cited by 239 · see citing works
A molecular framework for the actions of glucocorticoid hormones in the nervous system
Evans, R. M., & Arriza, J. L. (1989) · Neuron · doi:10.1016/0896-6273(89)90177-3 · Cited by 196 · see citing works
Self-citationDura, J., Randsholt, N. B., Deatrick, J., Erk, I., Santamarı́a, P., Freeman, J., Freeman, S. J., Weddell, D., & Brock, H. W. (1987) · Cell · doi:10.1016/0092-8674(87)90106-1 · Cited by 124 · see citing works
DEVELOPMENTAL GENETICS OF THE 2C-D REGION OF THE DROSOPHILA X CHROMOSOME
Perrimon, N., Engstrom, L., & Mahowald, A. P. (1985) · Genetics · doi:10.1093/genetics/111.1.23 · Cited by 106 · see citing works
The Drosophila gene knirps-related is a member of the steroid-receptor gene superf amily
Oro, A. E., Ong, E. S., Margolis, J. S., Posakony, J. W., Evans, R. M., & McKeown, M. (1988) · Nature · doi:10.1038/336493a0 · Cited by 105 · see citing works
Self-citationLefevre, G. (1981) · Genetics · doi:10.1093/genetics/99.3-4.461 · Cited by 85 · see citing works
Steroid hormone receptor homologs in development
Oro, A. E., Umesono, K., & Evans, R. M. (1989) · Development · doi:10.1242/dev.107.supplement.133 · Cited by 11 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Yu, V. C. K., Delsert, C., D, B. A. M., Holloway, J. M., Devary, O. V., Näär, A. M., Kim, S. Y., Boutin, J., Glass, C. K., & Rosenfeld, M. G. (1991) · Cell · doi:10.1016/0092-8674(91)90301-e · Cited by 1,183 · see citing works
Characterization of three RXR genes that mediate the action of 9-cis retinoic acid.Preprint
Mangelsdorf, D. J., Borgmeyer, U., Heyman, R. A., Zhou, J. Y., Ong, E. S., Oro, A. E., Kakizuka, A., & Evans, R. M. (1992) · Genes & Development · doi:10.1101/gad.6.3.329 · Cited by 1,193 · see citing works
Self-citationNuclear Receptors, RXR, and the Big Bang
Evans, R. M., & Mangelsdorf, D. J. (2014) · Cell · doi:10.1016/j.cell.2014.03.012 · Cited by 1,200 · see citing works
Self-citationLeid, M. E., Kastner, P., Lyons, R., Nakshatri, H., Saunders, M., Zacharewski, T. R., Chen, J.-Y., Staub, A., Garnier, J., Mader, S., et al. (1992) · Cell · doi:10.1016/0092-8674(92)90478-u · Cited by 1,166 · see citing works
Koelle, M. R., Talbot, W. S., Segraves, W. A., Bender, M. T., Cherbas, P. T., & Hogness, D. S. (1991) · Cell · doi:10.1016/0092-8674(91)90572-g · Cited by 978 · see citing works
New insecticides with ecdysteroidal and juvenile hormone activity
Dhadialla, T. S., Carlson, G. R., & Le, D. P. (1998) · Annual Review of Entomology · doi:10.1146/annurev.ento.43.1.545 · Cited by 912 · see citing works
“The availability of cloned DNA sequences coding for EcRs and USPs from several dipteran and lepidopteran insects (20, 38, 60, 61, 64, 65, 90, 125, 129)”
BackgroundZanaria, 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 · see citing works
Orphan Nuclear Receptors: From Gene to Function
Giguère, V. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.5.0378 · Cited by 848 · see citing works
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 · see citing works
Differential Recognition of Target Genes by Nuclear Receptor Monomers, Dimers, and Heterodimers*
Glass, C. K. (1994) · Endocrine Reviews · doi:10.1210/edrv-15-3-391 · Cited by 820 · see citing works
Steroid Hormone Receptors: Interaction with Deoxyribonucleic Acid and Transcription Factors*
Truss, M., & Beato, M. (1993) · Endocrine Reviews · doi:10.1210/edrv-14-4-459 · Cited by 739 · see citing works
Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation
Yao, T., Segraves, W. A., Oro, A. E., McKeown, M., & Evans, R. M. (1992) · Cell · doi:10.1016/0092-8674(92)90266-f · Cited by 716 · see citing works
Self-citationEcdysone Control of Developmental Transitions: Lessons from Drosophila Research
Yamanaka, N., Rewitz, K., & O’Connor, M. B. (2012) · Annual Review of Entomology · doi:10.1146/annurev-ento-120811-153608 · Cited by 671 · see citing works
“The core complex working to transduce the ecdysone signal is a heterodimer of two nuclear receptors, EcR (61) and Ultraspiracle (USP) (85).”
BackgroundInfluentialEvolution of the nuclear receptor gene superfamily.
Laudet, V., Hänni, C., Coll, J., Catzeflis, F. M., & Stéhelin, D. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05139.x · Cited by 656 · see citing works
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 · see citing works
Duester, G. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01497.x · Cited by 570 · see citing works
Nissen, R. M., & Yamamoto, K. R. (2000) · Genes & Development · doi:10.1101/gad.827900 · Cited by 559 · see citing works
“As an additional negative control, the Drosophila RXR homolog , ultraspiracle (Oro et al. 1990), failed to interact with either RDD fusion (Fig.”
BackgroundStructural determinants of nuclear receptor assembly on DNA direct repeats
Rastinejad, F., Perlmann, T., Evans, R. M., & Sigler, P. B. (1995) · Nature · doi:10.1038/375203a0 · Cited by 563 · see citing works
Self-citationControl and biochemical nature of the ecdysteroidogenic pathway
Gilbert, L. I., Rybczynski, R., & Warren, J. T. (2002) · Annual Review of Entomology · doi:10.1146/annurev.ento.47.091201.145302 · Cited by 532 · see citing works
Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle
Thomas, H. E., Stunnenberg, H. G., & Stewart, A. F. (1993) · Nature · doi:10.1038/362471a0 · Cited by 520 · see citing works
Giguère, V., Tini, M., Flock, G. B., Ong, E. S., Evans, R. M., & Otulakowski, G. (1994) · Genes & Development · doi:10.1101/gad.8.5.538 · Cited by 488 · see citing works
Self-citationGoodman, W. G., & Cusson, M. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-384749-2.10008-1 · Cited by 471 · see citing works
Marks, M. S., Hallenbeck, P. L., Nagata, T., Segars, J. H., Appella, E., Nikodem, V. M., & Ozato, K. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05187.x · Cited by 451 · see citing works
Seol, W., Choi, H.-S., & Moore, D. D. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.1.7760852 · Cited by 389 · see citing works
The retinoid X receptors and their ligands
Dawson, M. I., & Xia, Z. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.09.014 · Cited by 389 · see citing works
Mangelsdorf, D. J., Kliewer, S. A., Kakizuka, A., Umesono, K., & Evans, R. M. (1993) · Elsevier eBooks · doi:10.1016/b978-0-12-571148-7.50008-7 · Cited by 356 · see citing works
Self-citationThummel, C. S. (1995) · Cell · doi:10.1016/0092-8674(95)90203-1 · Cited by 349 · see citing works
Chick Ovalbumin Upstream Promoter-Transcription Factors (COUP-TFs): Coming of Age
Tsai, S. Y., & Tsai, M. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.2.0294 · Cited by 334 · see citing works
Characterization of the ligand‐dependent transactivation domain of thyroid hormone receptor.
Barettino, D., Ruiz, M. M. V., & Stunnenberg, H. G. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06603.x · Cited by 321 · see citing works
Participation of Non-Zinc Finger Residues in DNA Binding by Two Nuclear Orphan Receptors
Wilson, T. E., Paulsen, R. E., Padgett, K. A., & Milbrandt, J. (1992) · Science · doi:10.1126/science.1314418 · Cited by 310 · see citing works
Retinoid X receptors: X-ploring their (patho)physiological functions
Szántó, A., Narkar, V. A., Shen, Q., Uray, I. P., Davies, P. J., & Nagy, L. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401533 · Cited by 304 · see citing works
Lee, M. S., Kliewer, S. A., Provencal, J., Wright, P. E., & Evans, R. M. (1993) · Science · doi:10.1126/science.8388124 · Cited by 292 · see citing works
Self-citationFTZ-F1, a Steroid Hormone Receptor-like Protein Implicated in the Activation of fushi tarazu
Lavorgna, G., Ueda, H., Clos, J., & Wu, C. (1991) · Science · doi:10.1126/science.1709303 · Cited by 286 · see citing works
Ultraspiracle: An invertebrate nuclear receptor for juvenile hormones
Jones, G., & Sharp, P. A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.25.13499 · Cited by 281 · see citing works
Ecdysone response genes govern egg chamber development during mid-oogenesis in Drosophila
Buszczak, M., Freeman, M. R., Carlson, J. R., Bender, M. T., Cooley, L., & Segraves, W. A. (1999) · Development · doi:10.1242/dev.126.20.4581 · Cited by 276 · see citing works
The Nuclear Receptor Superfamily: A Rosetta Stone for Physiology
Evans, R. M. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0046 · Cited by 262 · see citing works
“We tested RXR, but our initial experiments were flawed.”
InfluentialSelf-citationArthropod nuclear receptors and their role in molting
Nakagawa, Y., & Henrich, V. C. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07347.x · Cited by 255 · see citing works
The genome and transcriptome of Japanese flounder provide insights into flatfish asymmetry
Shao, C., Bao, B., Xie, Z., Chen, X., Li, B., Jia, X., Yao, Q., Ortı́, G., Li, W., Li, X., et al. (2016) · Nature Genetics · doi:10.1038/ng.3732 · Cited by 248 · see citing works
Activation of mammalian retinoid X receptors by the insect growth regulator methoprene.
Harmon, M. A., Boehm, M. F., Heyman, R. A., & Mangelsdorf, D. J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.13.6157 · Cited by 240 · see citing works
Autophagic programmed cell death in Drosophila
Baehrecke, E. H. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401280 · Cited by 226 · see citing works
The Drosophila ecdysone receptor (EcR) Gene Is Required Maternally for Normal Oogenesis
Carney, G. E., & Bender, M. T. (2000) · Genetics · doi:10.1093/genetics/154.3.1203 · Cited by 226 · see citing works
Nagy, L., Szántó, A., Szatmári, I., & Széles, L. (2012) · Physiological Reviews · doi:10.1152/physrev.00004.2011 · Cited by 215 · see citing works
Tissue-Specific Gene Expression and Ecdysone-Regulated Genomic Networks in Drosophila
Li, T.-R., & White, K. P. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00192-8 · Cited by 204 · see citing works
Practical uses for ecdysteroids in mammals including humans: and update
Lafont, R., & Dinan, L. (2003) · Journal of Insect Science · doi:10.1093/jis/3.1.7 · Cited by 196 · see citing works
“One of the most promiscuous heterodimeric partners for vertebrate nuclear receptors is RXR, of which the equivalent in insects is Ultraspiracle (USP; Oro et al., 1990).”
BackgroundPractical uses for ecdysteroids in mammals including humans: And update
Lafont, R., & Dinan, L. (2003) · Journal of Insect Science · doi:10.1673/031.003.0701 · Cited by 196 · see citing works
“One of the most promiscuous heterodimeric partners for vertebrate nuclear receptors is RXR, of which the equivalent in insects is Ultraspiracle (USP; Oro et al., 1990).”
COUP-TF orphan nuclear receptors in development and differentiation
Pereira, F. A., Tsai, M., & Tsai, S. Y. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000624 · Cited by 193 · see citing works
Mechanisms of complex transcriptional regulation: implications for brain development
He, X., & Rosenfeld, M. G. (1991) · Neuron · doi:10.1016/0896-6273(91)90257-z · Cited by 187 · see citing works
Sluder, A. E., Mathews, S. W., Hough, D., Yin, V. P., & Maina, C. V. (1999) · Genome Research · doi:10.1101/gr.9.2.103 · Cited by 187 · see citing works
“1991) and Ultraspiracle (Oro et al. 1990) proteins or of an ultraspiracle-related gene from the dog heartworm D.”
BackgroundMethylation at lysine 4 of histone H3 in ecdysone-dependent development of Drosophila
Sedkov, Y., Cho, E., Petruk, S., Cherbas, L., Smith, S. T., Jones, R. S., Cherbas, P. T., Canaani, E., Jaynes, J. B., & Mazo, A. (2003) · Nature · doi:10.1038/nature02080 · Cited by 176 · see citing works
“Ecdysone works by binding to a nuclear receptor, EcR, which heterodimerizes with the retinoid X receptor homologue Ultraspiracl”
The RXR homolog Ultraspiracle is an essential component of the Drosophila ecdysone receptor
Hall, B. L., & Thummel, C. S. (1998) · Development · doi:10.1242/dev.125.23.4709 · Cited by 177 · see citing works
Regulation of Body Size and Growth Control
Texada, M., Koyama, T., & Rewitz, K. (2020) · Genetics · doi:10.1534/genetics.120.303095 · Cited by 129 · see citing works
Perrimon, N., Lanjuin, A., Arnold, C., & Noll, E. (1996) · Genetics · doi:10.1093/genetics/144.4.1681 · Cited by 176 · see citing works
Sullivan, A. A., & Thummel, C. S. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0430 · Cited by 175 · see citing works
Molecular Recognition of Agonist Ligands by RXRs
Egea, P. F., Mitschler, A., & Moras, D. (2002) · Molecular Endocrinology · doi:10.1210/mend.16.5.0823 · Cited by 175 · see citing works
“0888-8809/02/$15.00/0 Molecular Endocrinology 16(5):987–997 Printed in U.S.A. Copyright © 2002 by The Endocrine Society 987Downloaded from https://academic.oup.com/mend/article-abstract/16/5/987/2741678 by guest on 26 July 2018 the ortholog of RXR in Arthropods (19).”
InfluentialInteraction between retinoic acid and vitamin D signaling pathways.
Schräder, M., Bendik, I., Becker-André, M., & Carlberg, C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46779-2 · Cited by 174 · see citing works
Goodman, W. G., & Granger, N. A. (2005) · Elsevier eBooks · doi:10.1016/b0-44-451924-6/00039-9 · Cited by 172 · see citing works
Olmstead, A. W., & LeBlanc, G. A. (2003) · Environmental Health Perspectives · doi:10.1289/ehp.5982 · Cited by 171 · see citing works
“Ultraspiracle is a retinoid X receptor ortholog found in insects and crustaceans (Chung et al. 1998; Oro et al. 1990).”
BackgroundCharacterization of the mouse HNF-4 gene and its expression during mouse embryogenesis
Taraviras, S. L., Monaghan, A. P., Schütz, G., & Kelsey, G. (1994) · Mechanisms of Development · doi:10.1016/0925-4773(94)90017-5 · Cited by 166 · see citing works
DHR3: a Drosophila steroid receptor homolog.
Koelle, M. R., Segraves, W. A., & Hogness, D. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.6167 · Cited by 163 · see citing works
Song, Y., Villeneuve, D. L., Toyota, K., Iguchi, T., & Tollefsen, K. E. (2017) · Environmental Science & Technology · doi:10.1021/acs.est.7b00480 · Cited by 158 · see citing works
Molecular Chaperones Activate the Drosophila Ecdysone Receptor, an RXR Heterodimer
Arbeitman, M. N., & Hogness, D. S. (2000) · Cell · doi:10.1016/s0092-8674(00)80624-8 · Cited by 154 · see citing works
Retinoic acid X receptor in the diploblast, Tripedalia cystophora
Kostrouch, Z., Kostrouchová, M., Love, W. K., Jannini, E. A., Piatigorsky, J., & Rall, J. E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13442 · Cited by 153 · see citing works
Clayton, G. M., Peak-Chew, S. Y., Evans, R. M., & Schwabe, J. W. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041611298 · Cited by 151 · see citing works
Self-citationNER, a new member of the gene family encoding the human steroid hormone nuclear receptor
SHINAR, D. M., Endo, N., Rutledge, S. J., Vogel, R., Rodan, G. A., & Schmidt, A. (1994) · Gene · doi:10.1016/0378-1119(94)90080-9 · Cited by 151 · see citing works
Blumberg, B., Mangelsdorf, D. J., Dyck, J. A., Bittner, D., Evans, R. M., & Robertis, E. M. D. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.6.2321 · Cited by 151 · see citing works
Self-citationOro, A. E., McKeown, M., & Evans, R. M. (1992) · Development · doi:10.1242/dev.115.2.449 · Cited by 149 · see citing works
Self-citationFahrbach, S. E., Smagghe, G. J., & Velarde, R. A. (2011) · Annual Review of Entomology · doi:10.1146/annurev-ento-120710-100607 · Cited by 147 · see citing works
Kapitskaya, M. Z., Wang, S.-F., Cress, D. E., Dhadialla, T. S., & Raikhel, A. S. (1996) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(96)03847-6 · Cited by 145 · see citing works
Chung, A. C.-K., Durica, D. S., Clifton, S. W., Roe, B. A., & Hopkins, P. M. (1998) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(98)00056-2 · Cited by 144 · see citing works
Competition for Overlapping Sites in the Regulatory Region of the Drosophila Gene Krüppel
Hoch, M., Gerwin, N., Taubert, H., & Jäckle, H. (1992) · Science · doi:10.1126/science.1348871 · Cited by 139 · see citing works
9-cis retinoic acid signaling: changing partners causes some excitement.Preprint
Leblanc, B. P., & Stunnenberg, H. G. (1995) · Genes & Development · doi:10.1101/gad.9.15.1811 · Cited by 141 · see citing works
Peptide Hormones, Steroid Hormones, and Puffs: Mechanisms and Models in Insect Development
Henrich, V. C., Rybczynski, R., & Gilbert, L. I. (1998) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60934-6 · Cited by 141 · see citing works
Huet, F., Ruiz, C., & Richards, G. (1995) · Development · doi:10.1242/dev.121.4.1195 · Cited by 134 · see citing works
Structural basis of RXR-DNA interactions 1 1Edited by P. E. Wright
Zhao, Q., Chasse, S., Devarakonda, S., Sierk, M. L., Ahvazi, B., & Rastinejad, F. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3457 · Cited by 133 · see citing works
Schubiger, M., & Truman, J. W. (2000) · Development · doi:10.1242/dev.127.6.1151 · Cited by 129 · see citing works
Ahuja, H. S., Szántó, A., Nagy, L., & Davies, P. J. (2003) · PubMed · Cited by 128 · see citing works
Zhong, W., Sladek, F. M., & Darnell, J. E., Jr. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05685.x · Cited by 128 · see citing works
Regulation of retinoid and thyroid hormone action through homodimeric and heterodimeric receptors
Zhang, X.-K., & Kahl, M. (1993) · Trends in Endocrinology and Metabolism · doi:10.1016/1043-2760(93)90105-n · Cited by 123 · see citing works
Christianson, A. M. K., King, D. L., Hatzivassiliou, E., Casas, J. E., Hallenbeck, P. L., Nikodem, V. M., Mitsialis, S. A., & Kafatos, F. C. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.23.11503 · Cited by 125 · see citing works
Insect nuclear receptors: A developmental and comparative perspective
Henrich, V. C., & Brown, N. E. (1995) · Insect Biochemistry and Molecular Biology · doi:10.1016/0965-1748(95)00030-y · Cited by 123 · see citing works
Palli, S. R., Hiruma, K., & Riddiford, L. M. (1992) · Developmental Biology · doi:10.1016/0012-1606(92)90244-b · Cited by 122 · see citing works
Vitellogenesis and Post-Vitellogenic Maturation of the Insect Ovarian Follicle
Swevers, L., Raikhel, A. S., Sappington, T. W., Shirk, P. D., & Iatrou, K. (2005) · Elsevier eBooks · doi:10.1016/b0-44-451924-6/00093-4 · Cited by 120 · see citing works
“Furthermore, both components of the ecdysone receptor heterodimer, EcR and USP, are expressed throughout oogenesis in both the germline (nurse cells and oocyte) and the soma (follicular epithelium cells) (Khoury-Christianson et al., 1992; Buszczak et al., 1999; Carney and Bender, 2000).”
BackgroundInfluentialKeaveney, M., & Stunnenberg, H. G. (1995) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4684-6837-3_7 · Cited by 120 · see citing works
Fisk, G. J., & Thummel, C. S. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.23.10604 · Cited by 118 · see citing works
The X-ray Structure of a Hemipteran Ecdysone Receptor Ligand-binding Domain
Carmichael, J. A., Lawrence, M. C., Graham, L. D., Pilling, P. A., Epa, V. C., Noyce, L., Lovrecz, G. O., Winkler, D. A., Pawlak-Skrzecz, A., Eaton, R. E., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500661200 · Cited by 116 · see citing works
Retnakaran, R. R., Flock, G. B., & Giguère, V. (1994) · Molecular Endocrinology · doi:10.1210/mend.8.9.7838156 · Cited by 116 · see citing works
RNAi studies reveal a conserved role for RXR in molting in the cockroach Blattella germanica
Martı́n, D., Maestro, Ó., Cruz, J., Mané‐Padrós, D., & Bellés, X. (2006) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2005.12.002 · Cited by 111 · see citing works
“In this particular insect, the EcR gene encodes three protein isoforms, EcR-A, EcR-B1 and EcR-B2 (Talbot et al., 1993), whereas USP encodes a single protein (Oro et al., 1990; Henrich et al., 1990; Shea et al., 1990).”
BackgroundSteroid regulation of programmed cell death during Drosophila development
Baehrecke, E. H. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400753 · Cited by 111 · see citing works
Regulation of Metabolism by Retinoic Acid and Its Nuclear Receptors
Pfahl, M., & Chytil, F. (1996) · Annual Review of Nutrition · doi:10.1146/annurev.nu.16.070196.001353 · Cited by 110 · see citing works
Stone, B. L., & Thummel, C. S. (1993) · Cell · doi:10.1016/0092-8674(93)80072-m · Cited by 111 · see citing works
Nuclear Gene Sequences for Higher Level Phylogenetic Analysis: 14 Promising Candidates
Friedlander, T. P., Regier, J. C., & Mitter, C. W. (1992) · Systematic Biology · doi:10.1093/sysbio/41.4.483 · Cited by 107 · see citing works
Durica, D. S., Wu, X., Anilkumar, G., Hopkins, P. M., & Chung, A. C.-K. (2002) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(01)00740-7 · Cited by 104 · see citing works
Antoniewski, C., Mugat, B., Delbac, F., & Lepesant, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.6.2977 · Cited by 104 · see citing works
Linney, E. A. (1992) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(08)60538-4 · Cited by 100 · see citing works
Seven-up Inhibits Ultraspiracle-Based Signaling Pathways In Vitro and In Vivo
Zelhof, A. C., Yao, T., Chen, J. D., Evans, R. M., & McKeown, M. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.12.6736 · Cited by 98 · see citing works
“Usp is the Drosophila homolog of the retinoid X receptor (RXR) (25, 29), and Svp is the Drosophila homolog of the chicken ovalbumin upstream promoter transcription factor (COUP-TF) (24).”
BackgroundSelf-citationThe Isolation of Two Juvenile Hormone-Inducible Genes in Drosophila melanogaster
Dubrovsky, E. B., Dubrovskaya, V. A., Bilderback, A. L., & Berger, E. M. (2000) · Developmental Biology · doi:10.1006/dbio.2000.9800 · Cited by 97 · see citing works
“The Drosophila USP is a uclear receptor and the only known insect homolog of the ertebrate RXR (Oro et al., 1990; Shea et al., 1990).”
BackgroundJuvenile hormone III-dependent conformational changes of the nuclear receptor ultraspiracle
Jones, G., Woźniak, M., Chu, Y., Dhar, S. K., & Jones, D. (2001) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(01)00077-7 · Cited by 97 · see citing works
Differential Expression and Regulation by 20-Hydroxyecdysone of Mosquito Ultraspiracle Isoforms
Wang, S.-F., Li, C., Zhu, J., Miura, K., Miksicek, R. J., & Raikhel, A. S. (2000) · Developmental Biology · doi:10.1006/dbio.1999.9575 · Cited by 93 · see citing works
“Unlike Drosophila USP, for which a single form of RNA has been identified (Shea et al., 1990; Henrich et al., 990; Oro et al., 1990), two USP isoforms are reported in the osquito Aedes aegypti (USP-A and USP-B; Kapitskaya et l., 1996) and in the moth, M. sexta (USP-1 and USP-2; indra et al., 1997).”
BackgroundBuilding up the Drosophila eggshell: First of all the eggshell genes must be transcribed
Cavaliere, V., Bernardi, F., Romani, P., Duchi, S., & Gargiulo, G. (2008) · Developmental Dynamics · doi:10.1002/dvdy.21625 · Cited by 91 · see citing works
Schubiger, M., Carré, C., Antoniewski, C., & Truman, J. W. (2005) · Development · doi:10.1242/dev.02093 · Cited by 89 · see citing works
- Authors
- Oro, A. E., McKeown, M., & Evans, R. M.
- Affiliations
- Howard Hughes Medical Institute (US)
- Salk Institute for Biological Studies (US)
- Venue
- Nature
- Published
- 1990-09
- Volume
- 347
- Issue
- 6290
- Pages
- 298-301
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1966843280
- Cited by
- 406
- References
- 22
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 2 · 2023: 2 · 2022: 7 · 2021: 7 · 2020: 6 · 2019: 2 · 2018: 8 · 2017: 5 · 2016: 1 · 2015: 9 · 2014: 9 · 2013: 8 · 2012: 10
- FWCI
- 9.13
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- ultraspiracle, retinoid X receptor, retinoic acid receptor, retinoic acid, steroid receptor superfamily, transcription factors, Drosophila, vertebrate-invertebrate comparison, morphogenesis, pattern formation, gene homology
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Carrier Proteins, DNA, Drosophila, Humans, Molecular Sequence Data, Mutation, Nucleic Acid Hybridization, Sequence Homology, Nucleic Acid, Restriction Mapping, Receptors, Retinoic Acid
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
