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.
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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
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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
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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
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
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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