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Autor:
Carol A. Lange
Publikováno v:
Molecular Endocrinology. 18:269-278
In classical models of nuclear steroid hormone receptor function, ligand binds receptor, heat shock proteins dissociate, and receptor dimers enter or are withheld in the nucleus and interact with coregulatory molecules to mediate changes in gene expr
Publikováno v:
Molecular Endocrinology. 15:1929-1940
Steroid hormone receptors and signal transducers and activators of transcription (STAT) factors constitute two distinct families of transcription factors activated by different signaling pathways. In previous reports, cross-talk between STAT5 and sev
Autor:
Olli A. Jänne, Paul M. Yen, Mark Trifiro, Jeannie Whang, William W. Chin, Ying Liu, Jorma J. Palvimo, Leonard Pinsky
Publikováno v:
Molecular Endocrinology. 11:162-171
Androgen, glucocorticoid, and progesterone receptors (ARs, GRs, and PRs) often can regulate transcription via composite hormone response elements in target genes. We have used artificial and natural mutant ARs from patients with androgen resistance t
Autor:
Joe S. Mymryk, Trevor K. Archer
Publikováno v:
Molecular Endocrinology. 9:1825-1834
Steroid hormones act via a group of high affinity receptors that regulate transcription by binding to hormone response elements located in the promoters of hormone-inducible genes. Our understanding of these processes has been greatly enhanced by the
Publikováno v:
Molecular Endocrinology. 8:189-196
The association of heat shock proteins (hsp) with steroid hormone receptors may have functional significance for steroid receptor action. The association of hsp90 with steroid receptors is thought to maintain the receptors in the nonactivated state u
Publikováno v:
Molecular Endocrinology. 3:1270-1278
Progesterone receptor-containing T47D human breast cancer cells are responsive to progestins but fail to respond to other steroid hormones, in particular dexamethasone, because they have no measurable levels of receptors for estrogens, androgens, or
Publikováno v:
Molecular Endocrinology. 3:356-362
Previous analyses have indicated that steroid hormone receptors undergo an allosteric change in structure upon binding by the steroid ligand. This structural change was envisioned as an intramolecular unmasking of the protein's DNA-binding domain, th