The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Binding of Ligands and Activation of Transcription by Nuclear Receptors
Abstract
▪ Abstract Nuclear receptors (NRs) form a superfamily of ligand-inducible transcription factors composed of several domains. Recent structural studies focused on domain E, which harbors the ligand-binding site and the ligand-dependent transcription activation function AF-2. Structures of single representatives in an increasing number of various complexes as well as new structures of further NRs addressed issues such as discrimination of ligands, superagonism, isotype specificity, and partial agonism. Until today, one unique transcriptionally active form of domain E was determined; however, divergent tertiary structures of apo-forms and transcriptionally inactive forms are known. Thus, recent results link the transformation of NRs upon ligand binding to principles of protein folding. Furthermore, the ensemble of NR structures, including those of DNA-binding domains, provides one of the foundations for the understanding of interactions with transcription intermediary factors up to the characterization of the link between NR complexes and the basal transcriptional machinery at the structural level.
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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
Molecular recognition of fatty acids by peroxisome proliferator-activated receptors
Xu, H. E., Lambert, M. H., Montana, V. G., Parks, D. J., Blanchard, S. G., Brown, P. J., Sternbach, D. D., Lehmann, J. M., Wisely, G. B., Willson, T. M., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80467-0 · Cited by 1,169
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
Self-citationRochette-Egly, C., Adam, S., Rossignol, M., Egly, J.-M., & Chambon, P. (1997) · Cell · doi:10.1016/s0092-8674(00)80317-7 · Cited by 308
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Structure and mechanism of the Hsp90 molecular chaperone machinery
Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142738 · Cited by 1,103
Vecsey, C. G., Hawk, J. D., Lattal, K. M., Stein, J. M., Fabian, S. A., Attner, M. A., Cabrera, S. M., McDonough, C. B., Brindle, P. K., Abel, T., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0296-07.2007 · Cited by 831
The Aryl Hydrocarbon Receptor Complex and the Control of Gene Expression
Beischlag, T. V., Morales, J. L., Hollingshead, B. D., & Perdew, G. H. (2008) · Critical Reviews™ in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v18.i3.20 · Cited by 727
Jetten, A. M. (2009) · Nuclear Receptor Signaling · doi:10.1621/nrs.07003 · Cited by 673
Willson, T. M., & Kliewer, S. A. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd753 · Cited by 503
Metadata
- Authors
- Steinmetz, A. C. U., Renaud, J.-P., & Moras, D.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 2001-06
- Volume
- 30
- Issue
- 1
- Pages
- 329-359
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2121416807
- Cited by
- 205
- References
- 5
- FWCI
- 7.06
- Type
- journal article
- Language
- en
- Open access
- closed
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- Steinmetz, A. C. U., Renaud, J.-P., & Moras, D. (2001). Binding of Ligands and Activation of Transcription by Nuclear Receptors. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.30.1.329
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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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