Takimoto, G.S., Tasset, D.M., Eppert, A.C., et al. Hormone-induced progesterone receptor phosphorylation consists of sequential DNA-independent and DNA-dependent stages: Analysis with zinc finger mutants and the progesterone antagonist ZK98299. Proceedings of the National Academy of Sciences, USA 89:3050–3054, 1992.
Tasset, D., Tora, L., Fromental, C., et al. Distinct classes of transcriptional activating domains function by different mechanisms. Cell 62:1177–1187, 1990.
Tsai, S.Y., Tsai, M-J., and O'Malley, B.W. Cooperative binding of steroid hormone receptors contributes to transcriptional synergism at target enhancer elements. Cell 57:443–448, 1989.
Umesono, K., and Evans, R.M. Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell 57:1139–1146, 1989.
Vegeto, E., Allan, G.F., Schrader, W.T., et al. The mechanism of RU 486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor. Cell 69:703–713, 1992.
Weigel, N.L., Carter, T.H., Schrader, W.T., et al. Chicken progesterone receptor is phosphorylated by a DNA-dependent protein kinase during in vitro transcription assays. Molecular Endocrinology 6:8–14, 1992.
Weigel, N.L., Denner, L.A., Poletti, A., et al. Phosphorylation/dephosphorylation regulates the activity of progesterone receptors. Advances in Protein Phosphatases 7:237–269, 1993.
Yen, P.M., Sugawara, A., and Chin, W.W. Triiodothyronine (T3) differentially affects T3-receptor/retinoic acid receptor and T3-receptor/retinoid X receptor heterodimer binding to DNA. Journal of Biological Chemistry 267:23248–23252, 1992.