The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
The steroid receptor superfamily: mechanisms of diversity
Abstract
The steroid receptor superfamily of ligand-dependent transcription factors is characterized by marked conservation of both structure and function between the various receptors. Despite their well-documented extensive similarities, these receptors respond to a diverse range of ligands, which results in an even more impressive diversity of function. A variety of strategies is used at each point in the pathway from ligand binding to gene expression to achieve this diversity. The nature of the ligand is important as are the tissue-specific patterns of receptor gene expression, the presence of binding proteins, and the effects of cell- or tissue-specific ligand-modifying enzymes. Once bound to the receptor, the nature of which may vary as a result of either differential splicing or gene duplication yielding multiple isoforms, the activated receptor may form hetero- or homodimers. A complex interplay then occurs between the receptor dimer, other nuclear proteins, the response element, and the promoter complex to regulate gene expression. These elements may vary as a function of the cell type, other stimuli, and the context and sequence of the response element (or elements) in a given gene. By these mechanisms diversity may even be achieved for a given ligand, receptor subtype, gene, or cell. The observations may help to explain certain phenomena in hormone biology that are difficult to reconcile with the previous, simple, univariant model of steroid hormone action.
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“Nr2e3 is part of the cellular and nuclear receptor family for steroid hormones and is involved in cone cell proliferation, maintenance of photoreceptor topography and intercellular interactions, and expression of rod photoreceptor cell-specific genes”
From Retinal ultrastructure of murine models of dry age-related macular degeneration (AMD) (2010) · cites this paper as Fuller, 1991
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Cites
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Webster, M. K., Goya, L., Ge, Y., Maiyar, A. C., & Firestone, G. L. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2031-2040.1993 · Cited by 581
Metadata
- Authors
- Fuller, P. J.
- Affiliations
- Prince Henry's Institute of Medical Research Prince Henry's Hospital Melbourne Victoria 3004 Australia
- Corresponding author
- Fuller, Peter J.
- ORCID
- Fuller, Peter J.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1991-12
- Volume
- 5
- Issue
- 15
- Pages
- 3092-3099
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1823225325
- Cited by
- 200
- References
- 66
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 4 · 2021: 2 · 2018: 2 · 2017: 1 · 2015: 2 · 2014: 1 · 2013: 3 · 2012: 3
- FWCI
- 10.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- steroid hormone receptors, ligand-dependent transcription factors, receptor diversity, ligand binding, tissue-specific gene expression, steroid binding proteins, differential splicing, gene duplication, receptor isoforms, receptor dimerization, response elements, promoter complex, hormone action
- MeSH terms
- Animals, Base Sequence, DNA-Binding Proteins, Drosophila, Multigene Family, Mammals, Molecular Sequence Data, Receptors, Steroid, Regulatory Sequences, Nucleic Acid, RNA Splicing, Genetic Variation, Transcriptional Activation
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