The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
The Role of Corepressors in Transcriptional Regulation by Nuclear Hormone Receptors
Abstract
▪ Abstract Nuclear receptors (also known as nuclear hormone receptors) are hormone-regulated transcription factors that control many important physiological and developmental processes in animals and humans. Defects in receptor function result in disease. The diverse biological roles of these receptors reflect their surprisingly versatile transcriptional properties, with many receptors possessing the ability to both repress and activate target gene expression. These bipolar transcriptional properties are mediated through the interactions of the receptors with two distinct classes of auxiliary proteins: corepressors and coactivators. This review focuses on how corepressors work together with nuclear receptors to repress gene transcription in the normal organism and on the aberrations in this process that lead to neoplasia and endocrine disorders. The actions of coactivators and the contributions of the same corepressors to the functions of nonreceptor transcription factors are also touched on.
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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
A decade of molecular biology of retinoic acid receptors
Chambon, P. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.9.8801176 · Cited by 2,889
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
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
CBP/p300 in cell growth, transformation, and development
Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778
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
Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00429-4 · Cited by 754
Cytokine Stimulation of Energy Expenditure through p38 MAP Kinase Activation of PPARγ Coactivator-1
Puigserver, P., Rhee, J., Lin, J., Wu, Z., Yoon, J. C., Zhang, C.-Y., Krauss, S., Mootha, V. K., Lowell, B. B., & Spiegelman, B. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00390-2 · Cited by 732
Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes.
Lavinsky, R. M., Jepsen, K., Heinzel, T., Torchia, J., Mullen, T.-M., Schiff, R., Del-Rio, A. L., Ricote, M., Ngo, S., Gemsch, J., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2920 · Cited by 660
Yoon, H., Chan, D. W., Huang, Z., Li, J., Fondell, J. D., Qin, J., & Wong, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg120 · Cited by 444
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
Lee, G., Elwood, F., McNally, J., Weiszmann, J., Lindstrom, M., Amaral, K., Nakamura, M., Miao, S., Cao, P., Learned, R. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200743200 · Cited by 319
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
Human HDAC7 Histone Deacetylase Activity Is Associated with HDAC3in Vivo
Fischle, W., Dequiedt, F., Fillion, M., Hendzel, M. J., Voelter, W., & Verdin, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104935200 · Cited by 232
Regulation of histone deacetylase 2 by protein kinase CK2
Tsai, S.-C., & Seto, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204149200 · Cited by 196
Receptor-interacting Protein 140 Directly Recruits Histone Deacetylases for Gene Silencing
Wei, L.-N., Hu, X., Chandra, D., Seto, E., & Farooqui, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004821200 · Cited by 150
Chakrabarti, S. R., & Nucifora, G. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1605 · Cited by 149
Cited by
The COSMIC Cancer Gene Census: describing genetic dysfunction across all human cancers
Sondka, Z., Bamford, S., Cole, C. G., Ward, S. A., Dunham, I., & Forbes, S. A. (2018) · Nature Reviews Cancer · doi:10.1038/s41568-018-0060-1 · Cited by 1,597
Transcriptional Regulatory Elements in the Human Genome
Maston, G. A., Evans, S. K., & Green, M. R. (2006) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.7.080505.115623 · Cited by 937
Rosenfeld, M. G., Lunyak, V. V., & Glass, C. K. (2006) · Genes & Development · doi:10.1101/gad.1424806 · Cited by 952
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
PPAR : a dagger in the heart of the metabolic syndrome
Barish, G. D. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27955 · Cited by 641
Metadata
- Authors
- Privalsky, M. L.
- Venue
- Annual Review of Physiology
- Publisher
- Annual Reviews
- Published
- 2004-03-01
- Volume
- 66
- Issue
- 1
- Pages
- 315-360
- ISSN
- 0066-4278 (ISSN-L)
- 1545-1585
- OpenAlex
- W2132613286
- Cited by
- 324
- References
- 18
- FWCI
- 2.90
- Type
- journal article
- Language
- en
- Open access
- closed
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