The DOI matches its Crossref record; 155 of the 155 references it cites were found in a registry or an index.
The Androgen Receptor in Health and Disease
Abstract
Androgens play pivotal roles in the regulation of male development and physiological processes, particularly in the male reproductive system. Most biological effects of androgens are mediated by the action of nuclear androgen receptor (AR). AR acts as a master regulator of downstream androgen-dependent signaling pathway networks. This ligand-dependent transcriptional factor modulates gene expression through the recruitment of various coregulator complexes, the induction of chromatin reorganization, and epigenetic histone modifications at target genomic loci. Dysregulation of androgen/AR signaling perturbs normal reproductive development and accounts for a wide range of pathological conditions such as androgen-insensitive syndrome, prostate cancer, and spinal bulbar muscular atrophy. In this review we summarize recent advances in understanding of the epigenetic mechanisms of AR action as well as newly recognized aspects of AR-mediated androgen signaling in both men and women. In addition, we offer a perspective on the use of animal genetic model systems aimed at eventually developing novel therapeutic AR ligands.
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Cites
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Cited by
The Molecular Signatures Database Hallmark Gene Set Collection
Liberzon, A., Birger, C., Thorvaldsdóttir, H., Ghandi, M., Mesirov, J. P., & Tamayo, P. (2015) · Cell Systems · doi:10.1016/j.cels.2015.12.004 · Cited by 13,807
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“This ligand-dependent transcription factormodulates gene expression through direct DNA binding and the recruitment of several coregulators to form complexes, which are necessary to induce epigenetic histone modifications and chromatin remodeling at target genetic loci (20, 21).”
BackgroundCoregulator control of androgen receptor action by a novel nuclear receptor-binding motif
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“In addition, favorable electrostatic interactions appear to occur between the G(1), A(2), R(3), R(4), and R(6) of the peptide core with amino acids Arg-726, Asn-727, Gly-724, Glu-829, and Glu-837 that form the BF-3 pocket (Fig.”
BackgroundMethodInfluentialPeinetti, N., Cuello Rubio, M. M., Sosa, L. D. V., Scalerandi, M. V., Alasino, R. V., Peyret, V., Nicola, J. P., Beltramo, D. M., Quintar, A. A., & Maldonado, C. A. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.119985 · Cited by 7
Metadata
- Authors
- Matsumoto, T., Sakari, M., Okada, M., Yokoyama, A., Takahashi, S., Kouzmenko, A., & Kato, S.
- Venue
- Annual Review of Physiology
- Publisher
- Annual Reviews
- Published
- 2013-02-10
- Volume
- 75
- Issue
- 1
- Pages
- 201-224
- ISSN
- 0066-4278 (ISSN-L)
- 1545-1585
- OpenAlex
- W2164236134
- Cited by
- 266
- References
- 155
- FWCI
- 3.12
- Type
- journal article
- Language
- en
- Open access
- closed
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