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Nucleocytoplasmic Shuttling of Estrogen Receptors is Blocked by “Pure Anti-Estrogens”

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Book cover Hormonal Carcinogenesis II

Abstract

The estrogen receptor belongs to a large family of nuclear receptors whose activity as a transcription factor depends on the binding of a hormonal ligand (1). As with other steroid receptors, in the absence of ligand the estrogen receptor is found in an oligomeric complex that is unable to bind to DNA (2–4). Following hormone binding, the complex is dissociated to allow receptor dimerization, high-affinity DNA binding, and transcriptional activation (5, 6). In the estrogen receptor, there are at least two regions called activation functions, or AFs, which are required to stimulate transcription (7, 8). The relative activities of AF-1, located in the N-terminal domain, and AF-2, in the C-terminal hormone binding domain, vary according to the responsive promoter and target cells.

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© 1996 Springer-Verlag New York, Inc.

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Dauvois, S., Parker, M.G. (1996). Nucleocytoplasmic Shuttling of Estrogen Receptors is Blocked by “Pure Anti-Estrogens”. In: Li, J.J., Li, S.A., Gustafsson, JÅ., Nandi, S., Sekely, L.I. (eds) Hormonal Carcinogenesis II. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-2332-0_8

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  • DOI: https://doi.org/10.1007/978-1-4612-2332-0_8

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-7506-0

  • Online ISBN: 978-1-4612-2332-0

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