Evidence for an Anti-parallel Orientation of the Ligand-activated Human Androgen Receptor Dimer
Open Access
- 1 December 1995
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (50) , 29983-29990
- https://doi.org/10.1074/jbc.270.50.29983
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- The leucine zippers of c-fos and c-jun for progesterone receptor dimerization: A-dominance in the A/B heterodimerThe Journal of Steroid Biochemistry and Molecular Biology, 1994
- The human estrogen receptor hormone binding domain dimerizes independently of ligand activationThe Journal of Steroid Biochemistry and Molecular Biology, 1994
- The side chains responsible for the dimerization of the estradiol receptor by ionic bonds are lost in a 17 kDa fragment extending downstream from aa 303The Journal of Steroid Biochemistry and Molecular Biology, 1994
- Specific binding of progesterone receptor to progesterone‐responsive elements does not require prior dimerizationEuropean Journal of Biochemistry, 1993
- Protein-protein interactions between the DNA-binding domains of nuclear receptors: Influence on DNA-bindingThe Journal of Steroid Biochemistry and Molecular Biology, 1993
- The glucocorticoid receptor in homodimeric and monomeric form visualised by electron microscopyJournal of Structural Biology, 1991
- A mutation in the ligand binding domain of the androgen receptor of human INCaP cells affects steroid binding characteristics and response to anti-androgensBiochemical and Biophysical Research Communications, 1990
- Unusual specificity of the androgen receptor in the human prostate tumor cell line LNCaP: High affinity for progestagenic and estrogenic steroidsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1990
- A novel genetic system to detect protein–protein interactionsNature, 1989
- Cooperative binding of steroid hormone receptors contributes to transcriptional synergism at target enhancer elementsCell, 1989