The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.
The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor
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Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Experiments in molecular genetics
Miller, J. H. (1972) · Medical Entomology and Zoology · Cited by 27,157
Transformation of intact yeast cells treated with alkali cations
Ito, H., Fukuda, Y., Murata, K., & Kimura, A. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.163-168.1983 · Cited by 7,518
The Steroid and Thyroid Hormone Receptor Superfamily
Evans, R. M. (1988) · Science · doi:10.1126/science.3283939 · Cited by 7,439
Gene regulation by steroid hormones
Beato, M. (1989) · Cell · doi:10.1016/0092-8674(89)90237-7 · Cited by 3,383
The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer
Kumar, V., & Chambon, P. (1988) · Cell · doi:10.1016/0092-8674(88)90017-7 · Cited by 1,220
The human estrogen receptor has two independent nonacidic transcriptional activation functions
Tora, L., White, J., Brou, C., Tasset, D., Webster, N., Scheer, E., & Chambon, P. (1989) · Cell · doi:10.1016/0092-8674(89)90031-7 · Cited by 1,048
Determinants of target gene specificity for steroid/thyroid hormone receptors
Umesono, K., & Evans, R. M. (1989) · Cell · doi:10.1016/0092-8674(89)90051-2 · Cited by 948
Functional domains of the human glucocorticoid receptor
Giguère, V., Hollenberg, S. M., Rosenfeld, M. G., & Evans, R. M. (1986) · Cell · doi:10.1016/0092-8674(86)90339-9 · Cited by 918
Steroid Receptor Family: Structure and Functions
CARSON-JURICA, M. A., SCHRADER, W. T., & O'MALLEY, B. W. (1990) · Endocrine Reviews · doi:10.1210/edrv-11-2-201 · Cited by 811
Self-citation
Cited by
Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily
Oñate, S. A., Tsai, S. Y., Tsai, M.-J., & O'Malley, B. W. (1995) · Science · doi:10.1126/science.270.5240.1354 · Cited by 2,387
Self-citationThe 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
Nuclear Receptor Coregulators: Cellular and Molecular Biology*
McKenna, N. J., Lanz, R. B., & O’Malley, B. W. (1999) · Endocrine Reviews · doi:10.1210/edrv.20.3.0366 · Cited by 1,911
Self-citationSchoonjans, K., Staels, B., & Auwerx, J. (1996) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(96)00066-5 · Cited by 1,047
Coregulator Function: A Key to Understanding Tissue Specificity of Selective Receptor Modulators
Smith, C. L., & O’Malley, B. W. (2004) · Endocrine Reviews · doi:10.1210/er.2003-0023 · Cited by 931
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Metadata
- Authors
- Vegeto, E., Allan, G. F., Schrader, W. T., Tsai, M.-J., McDonnell, D. P., & O'Malley, B. W.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1992-05
- Volume
- 69
- Issue
- 4
- Pages
- 703-713
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2007048730
- Cited by
- 377
- References
- 64
- FWCI
- 16.90
- Type
- journal article
- Language
- en
- Open access
- closed
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- This page
- CoChat. (2026). Citation check: The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor. https://app.cochat.ai/papers/10.1016/0092-8674(92)90234-4
- The paper
- Vegeto, E., Allan, G. F., Schrader, W. T., Tsai, M.-J., McDonnell, D. P., & O'Malley, B. W. (1992). The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor. Cell. https://doi.org/10.1016/0092-8674(92)90234-4
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.