Tamoxifen resistant breast cancer: coregulators determine the direction of transcription by antagonist-occupied steroid receptors

[1]  C. Allis,et al.  Steroid receptor coactivator-1 is a histone acetyltransferase , 1997, Nature.

[2]  K. Horwitz,et al.  The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT. , 1997, Molecular endocrinology.

[3]  C. Glass,et al.  Nuclear receptor coactivators. , 1997, Current opinion in cell biology.

[4]  K. Horwitz,et al.  Nuclear receptor coactivators and corepressors. , 1996, Molecular endocrinology.

[5]  U. Krawinkel,et al.  Mass Spectrometric Identification of Leucine Zipper-like Homodimer Complexes of the Autoantigen L7* , 1996, The Journal of Biological Chemistry.

[6]  P. Chambon,et al.  TIF2, a 160 kDa transcriptional mediator for the ligand‐dependent activation function AF‐2 of nuclear receptors. , 1996, The EMBO journal.

[7]  B. Hankey,et al.  Second cancers after adjuvant tamoxifen therapy for breast cancer. , 1996, Journal of the National Cancer Institute.

[8]  M. Stallcup,et al.  GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[9]  Thorsten Heinzel,et al.  A CBP Integrator Complex Mediates Transcriptional Activation and AP-1 Inhibition by Nuclear Receptors , 1996, Cell.

[10]  B. Wold,et al.  Know Your Neighbors: Three Phenotypes in Null Mutants of the Myogenic bHLH Gene MRF4 , 1996, Cell.

[11]  K. Umesono,et al.  The nuclear receptor superfamily: The second decade , 1995, Cell.

[12]  B. O’Malley,et al.  Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily , 1995, Science.

[13]  Thorsten Heinzel,et al.  Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor , 1995, Nature.

[14]  P. Kushner,et al.  Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor. , 1995, The EMBO journal.

[15]  J. Pike,et al.  Analysis of estrogen receptor function in vitro reveals three distinct classes of antiestrogens. , 1995, Molecular endocrinology.

[16]  K. Horwitz When tamoxifen turns bad. , 1995, Endocrinology.

[17]  U. Krawinkel,et al.  Characterization of eukaryotic protein L7 as a novel autoantigen which frequently elicits an immune response in patients suffering from systemic autoimmune disease. , 1994, Immunobiology.

[18]  K. Horwitz,et al.  A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform. , 1994, Molecular endocrinology.

[19]  K. Horwitz,et al.  New T47D breast cancer cell lines for the independent study of progesterone B- and A-receptors: only antiprogestin-occupied B-receptors are switched to transcriptional agonists by cAMP. , 1994, Cancer research.

[20]  T. Bourne,et al.  Effects of tamoxifen on uterus and ovaries of postmenopausal women in a randomised breast cancer prevention trial , 1994, The Lancet.

[21]  D. Edwards,et al.  The progesterone antagonist RU486 acquires agonist activity upon stimulation of cAMP signaling pathways. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[22]  P. Chambon,et al.  Type II antagonists impair the DNA binding of steroid hormone receptors without affecting dimerization , 1993, The Journal of Steroid Biochemistry and Molecular Biology.

[23]  R B Mazess,et al.  Effects of tamoxifen on bone mineral density in postmenopausal women with breast cancer. , 1992, The New England journal of medicine.

[24]  G. Ryffel,et al.  Two types of antiprogestins identified by their differential action in transcriptionally active extracts from T47D cells. , 1991, Nucleic acids research.

[25]  R. Evans,et al.  The steroid and thyroid hormone receptor superfamily. , 1988, Science.

[26]  K. Tsurugi,et al.  Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 60 S ribosomal subunit proteins L4, L5, L7, L9, L11, L12, L13, L21, L22, L23, L26, L27, L30, L33, L35', L37, and L39. , 1976, The Journal of biological chemistry.