Crystal Structure of the Glucocorticoid Receptor Ligand Binding Domain Reveals a Novel Mode of Receptor Dimerization and Coactivator Recognition
Top Cited Papers
- 1 July 2002
- journal article
- Published by Elsevier BV in Cell
- Vol. 110 (1), 93-105
- https://doi.org/10.1016/s0092-8674(02)00817-6
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Glucocorticoid Receptor Homodimers and Glucocorticoid-Mineralocorticoid Receptor Heterodimers Form in the Cytoplasm through Alternative Dimerization InterfacesMolecular and Cellular Biology, 2001
- Ligand binding and nuclear receptor evolutionBioEssays, 2000
- Stepwise Assembly of a Glucocorticoid Receptor·hsp90 Heterocomplex Resolves Two Sequential ATP-dependent Events Involving First hsp70 and Then hsp90 in Opening of the Steroid Binding PocketPublished by Elsevier BV ,2000
- Comparison of Chromatin Remodeling and Transcriptional Activation of the Mouse Mammary Tumor Virus Promoter by the Androgen and Glucocorticoid ReceptorExperimental Cell Research, 1999
- Structure and specificity of nuclear receptor–coactivator interactionsGenes & Development, 1998
- Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acidNature, 1995
- Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor SuperfamilyScience, 1995
- A transcriptional co-repressor that interacts with nuclear hormone receptorsNature, 1995
- Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressorNature, 1995
- Solvent-Accessible Surfaces of Proteins and Nucleic AcidsScience, 1983