The Ligand Binding Domain of the Human Retinoic Acid Receptor γ Is Predominantly α-Helical with a Trp Residue in the Ligand Binding Site
Open Access
- 1 October 1995
- journal article
- Published by Elsevier
- Vol. 270 (42) , 24884-24890
- https://doi.org/10.1074/jbc.270.42.24884
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Retinoic acid receptors and retinoid X receptors: interactions with endogenous retinoic acids.Proceedings of the National Academy of Sciences, 1993
- 9-cis retinoic acid is a high affinity ligand for the retinoid X receptorCell, 1992
- 9-Cis retinoic acid stereoisomer binds and activates the nuclear receptor RXRαNature, 1992
- Characterization of an autoregulated response element in the mouse retinoic acid receptor type beta gene.Proceedings of the National Academy of Sciences, 1990
- Identification of a retinoic acid responsive element in the retinoic acid receptor & beta;geneNature, 1990
- A retinoic acid-responsive element is present in the 5' flanking region of the laminin B1 gene.Proceedings of the National Academy of Sciences, 1989
- Nuclear receptors enhance our understanding of transcription regulationTrends in Genetics, 1988
- The Steroid and Thyroid Hormone Receptor SuperfamilyScience, 1988
- Identification of a new class of steroid hormone receptorsNature, 1988
- Multiple functions of vitamin A.Physiological Reviews, 1984