A single amino acid exchange abolishes dimerization of the androgen receptor and causes Reifenstein syndrome
- 28 April 1995
- journal article
- Published by Elsevier in Molecular and Cellular Endocrinology
- Vol. 111 (1), 93-98
- https://doi.org/10.1016/0303-7207(95)03554-k
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptorsNature, 1992
- Amino acid substitutions in the DNA-binding domain of the human androgen receptor are a frequent cause of receptor-binding positive androgen resistanceMolecular Endocrinology, 1992
- Androgen Resistance — The Clinical and Molecular SpectrumNew England Journal of Medicine, 1992
- Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signallingNature, 1992
- Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficientlyCell, 1992
- RXRβ: A coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elementsCell, 1991
- Crystallographic analysis of the interaction of the glucocorticoid receptor with DNANature, 1991
- The orientation and spacing of core DNA-binding motifs dictate selective transcriptional responses to three nuclear receptorsCell, 1991
- The scanning model for translation: an update.The Journal of cell biology, 1989
- Gene regulation by steroid hormonesCell, 1989