Engineering novel specificities for ligand-activated transcription in the nuclear hormone receptor RXR
- 1 January 1998
- journal article
- Published by Elsevier in Chemistry & Biology
- Vol. 5 (1) , 13-21
- https://doi.org/10.1016/s1074-5521(98)90083-7
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Different Residues of the Human Estrogen Receptor Are Involved in the Recognition of Structurally Diverse Estrogens and AntiestrogensJournal of Biological Chemistry, 1997
- Analysis of the Ligand-Binding Domain of Human Retinoic Acid Receptor α by Site-Directed MutagenesisMolecular and Cellular Biology, 1996
- Nuclear hormone receptors: ligand-activated regulators of transcription and diverse cell responsesChemistry & Biology, 1996
- Mutational analysis of the estrogen receptor ligand-binding domain: influence of ligand structure and stereochemistry on transactivationJournal of Molecular Endocrinology, 1996
- A canonical structure for the ligand-binding domain of nuclear receptorsNature Structural & Molecular Biology, 1996
- The nuclear receptor superfamily: The second decadeCell, 1995
- Mutagenesis of the Ligand Binding Domain of the Human Retinoic Acid Receptor α Identifies Critical Residues for 9-cis-Retinoic Acid BindingPublished by Elsevier ,1995
- Genetic dissection of thyroid hormone receptor β: identification of mutations that separate hormone binding and transcriptional activationMolecular and Cellular Biology, 1995
- A Single Amino Acid That Determines the Sensitivity of Progesterone Receptors to RU486Science, 1992
- 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