The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Nuclear Hormone Receptors and Gene Expression
Abstract
The nuclear hormone receptor superfamily includes receptors for thyroid and steroid hormones, retinoids and vitamin D, as well as different “orphan” receptors of unknown ligand. Ligands for some of these receptors have been recently identified, showing that products of lipid metabolism such as fatty acids, prostaglandins, or cholesterol derivatives can regulate gene expression by binding to nuclear receptors. Nuclear receptors act as ligand-inducible transcription factors by directly interacting as monomers, homodimers, or heterodimers with the retinoid X receptor with DNA response elements of target genes, as well as by “cross-talking” to other signaling pathways. The effects of nuclear receptors on transcription are mediated through recruitment of coregulators. A subset of receptors binds corepressor factors and actively represses target gene expression in the absence of ligand. Corepressors are found within multicomponent complexes that contain histone deacetylase activity. Deacetylation leads to chromatin compactation and transcriptional repression. Upon ligand binding, the receptors undergo a conformational change that allows the recruitment of multiple coactivator complexes. Some of these proteins are chromatin remodeling factors or possess histone acetylase activity, whereas others may interact directly with the basic transcriptional machinery. Recruitment of coactivator complexes to the target promoter causes chromatin decompactation and transcriptional activation. The characterization of corepressor and coactivator complexes, in concert with the identification of the specific interaction motifs in the receptors, has demonstrated the existence of a general molecular mechanism by which different receptors elicit their transcriptional responses in target genes.
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Cites
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
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
Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase
Kato, S., Endoh, H., Masuhiro, Y., Kitamoto, T., Uchiyama, S., Sasaki, H., Masushige, S., Gotoh, Y., Nishida, E., Kawashima, H., et al. (1995) · Science · doi:10.1126/science.270.5241.1491 · Cited by 1,964
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Histone acetylation and transcriptional regulatory mechanisms
Struhl, K. (1998) · Genes & Development · doi:10.1101/gad.12.5.599 · Cited by 1,815
Crystallographic 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
Nuclear protein CBP is a coactivator for the transcription factor CREB
Kwok, R. P. S., Lundblad, J. R., Chrivia, J. C., Richards, J. P., Bächinger, H. P., Brennan, R. G., Roberts, S. G. E., Green, M. R., & Goodman, R. H. (1994) · Nature · doi:10.1038/370223a0 · Cited by 1,443
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
Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP
Petrif, F., Giles, R. H., Dauwerse, H. G., Saris, J. J., Hennekam, R. C. M., Masuno, M., Tommerup, N., van Ommen, G.-J. B., Goodman, R. H., Peters, D. J. M., et al. (1995) · Nature · doi:10.1038/376348a0 · Cited by 1,217
DNA binding of the glucocorticoid receptor is not essential for survival
Reichardt, H. M., Kaestner, K. H., Tuckermann, J., Kretz, O., Wessely, O., Bock, R., Gass, P., Schmid, W., Herrlich, P., Angel, P., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81183-6 · Cited by 1,068
The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand
Rochel, N., Wurtz, J. M., Mitschler, A., Klaholz, B., & Moras, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80413-x · Cited by 842
Three proteins define a class of human histone deacetylases related to yeast Hda1p
Grozinger, C. M., Hassig, C. A., & Schreiber, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4868 · Cited by 770
CDK-Independent Activation of Estrogen Receptor by Cyclin D1
Zwijsen, R. M. L., Wientjens, E., Klompmaker, R., van der Sman, J., Bernards, R., & Michalides, R. J. A. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81879-6 · Cited by 720
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
Phosphorylation of the Nuclear Receptor SF-1 Modulates Cofactor Recruitment
Hammer, G. D., Krylova, I., Zhang, Y., Darimont, B. D., Simpson, K., Weigel, N. L., & Ingraham, H. A. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80480-3 · Cited by 375
Durand, B., Saunders, M., Gaudon, C., Roy, B., Losson, R., & Chambon, P. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06872.x · Cited by 354
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
Drouin, J., Trifiro, M. A., Plante, R. K., Nemer, M., Eriksson, P., & Wrange, Ö. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.12.5305-5314.1989 · Cited by 283
Histone deacetylases: transcriptional repression with SINers and NuRDs
Ayer, D. E. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01536-6 · Cited by 274
Alen, P., Claessens, F., Verhoeven, G., Rombauts, W., & Peeters, B. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.9.6085 · Cited by 268
Neely, K. E., Hassan, A. H., Wallberg, A. E., Steger, D. J., Cairns, B. R., Wright, A. P. H., & Workman, J. L. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80216-6 · Cited by 245
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
Cited by
Preitner, N., Damiola, F., Luis-Lopez-Molina, Zakany, J., Duboule, D., Albrecht, U., & Schibler, U. (2002) · Cell · doi:10.1016/s0092-8674(02)00825-5 · Cited by 2,198
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
Estrogen receptor signaling mechanisms
(2019) · Advances in Protein Chemistry and Structural Biology · doi:10.1016/bs.apcsb.2019.01.001 · Cited by 988
Transcriptional Regulation of Metabolism
Desvergne, B., Michalik, L., & Wahli, W. (2006) · Physiological Reviews · doi:10.1152/physrev.00025.2005 · Cited by 892
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
Metadata
- Authors
- Aranda, A., & Pascual, A.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2001-07-01
- Volume
- 81
- Issue
- 3
- Pages
- 1269-1304
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W1919133853
- Cited by
- 1,570
- References
- 22
- FWCI
- 5.91
- Type
- journal article
- Language
- en
- Open access
- closed
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