The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Structure and Function of the Estrogen Receptor
Abstract
The hormone binding domain of the estrogen receptor is required not only for binding estradiol but also to form stable homodimers of the protein and mediate transcriptional activation by the receptor. Residues that are essential for estrogen binding are also involved in dimerization, suggesting that the hormone-binding pocket is at or near the dimer interface. Distinct hydrophobic and charged residues are essential for hormone-dependent transcriptional activation, and these appear to be conserved by other members of the nuclear receptor family. We have found that the pure antiestrogens ICI 164384 and ICI 182780 increase the turnover of the receptor compared with that in the presence of estradiol. Because it is likely that the pure antiestrogens bind to a similar region of the receptor as that of estradiol, we propose that they inhibit receptor dimerization by means of their 7 alpha alkyl-amide extension. It appears that as a consequence nuclear uptake is inhibited and the receptor more rapidly degraded in the cytoplasm.
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“Nuclear receptors act by forming homodimers or heterodimers. For example, the glucocorticoid receptor [1] and estrogen receptor [2] form a homodimer, and insect ecdysone receptor (EcR) forms a heterodimer with an ultraspiracle protein (USP), the ortholog of retinoid X receptor in vertebrates [3].”
From G-protein-coupled receptor participates in 20-hydroxyecdysone signaling on the plasma membrane (2014) · cites this paper as [2]
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Cites
Transcriptional Regulation in Mammalian Cells by Sequence-Specific DNA Binding Proteins
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The c-erb-A gene encodes a thyroid hormone receptor
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Functional domains of the human estrogen receptor
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The c-erb-A protein is a high-affinity receptor for thyroid hormone
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The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer
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Research works printed but not linked: 1
- Danielian P. S., 1992, Identification of residues in the estrogen receptor which confer differential sensitivity to estrogen and hydroxytamoxifen, Mol. Endocrinol.
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The oxytocin receptor system: structure, function, and regulation
Gimpl, G., & Fahrenholz, F. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.629 · Cited by 3,089
Overview of resistance to systemic therapy in patients with breast cancer
Gonzalez-Angulo, A. M., Morales-Vasquez, F., & Hortobagyi, G. N. (2007) · Advances in Experimental Medicine and Biology · doi:10.1007/978-0-387-74039-3_1 · Cited by 904
Blair, R. M. (2000) · Toxicological Sciences · doi:10.1093/toxsci/54.1.138 · Cited by 806
Basic Guide to the Mechanisms of Antiestrogen Action
MacGregor, J. I., & Jordan, V. C. (1998) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01358-9 · Cited by 698
Webb, P., Lopez, G. N., Uht, R. M., & Kushner, P. J. (1995) · Molecular Endocrinology · doi:10.1210/mend.9.4.7659088 · Cited by 694
Metadata
- Authors
- PARKER, M. G., ARBUCKLE, N., DAUVOIS, S., DANIELIAN, P., & WHITE, R.
- ORCID
- DANIELIAN, P.
- Venue
- Annals of the New York Academy of Sciences
- Publisher
- Wiley
- Published
- 1993-06
- Volume
- 684
- Issue
- 1
- Pages
- 119-126
- ISSN
- 0077-8923 (ISSN-L)
- 1749-6632
- OpenAlex
- W2138484074
- Cited by
- 129
- References
- 51
- Citations by year
- 2024: 2 · 2023: 2 · 2022: 2 · 2021: 4 · 2020: 1 · 2019: 2 · 2017: 2 · 2016: 1 · 2015: 4 · 2014: 3 · 2013: 1 · 2012: 5
- FWCI
- 0.76
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annals of the New York Academy of Sciences (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Physical Sciences › Environmental Science › Health, Toxicology and Mutagenesis › Effects and risks of endocrine disrupting chemicals
- Keywords
- estrogen receptor, hormone-binding domain, estradiol binding, receptor dimerization, transcriptional activation, nuclear receptors, antiestrogens, fulvestrant, receptor turnover, nuclear uptake, protein degradation
- MeSH terms
- Animals, Estrogen Antagonists, Hormones, Humans, Mutation, Receptors, Estrogen, Transcription, Genetic
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