Genetic Dissection of p23, an Hsp90 Cochaperone, Reveals a Distinct Surface Involved in Estrogen Receptor Signaling
Open Access
- 1 September 2003
- journal article
- Published by Elsevier
- Vol. 278 (38) , 36547-36555
- https://doi.org/10.1074/jbc.m305960200
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- The Influence of ATP and p23 on the Conformation of hsp90Journal of Biological Chemistry, 2002
- Disassembly of Transcriptional Regulatory Complexes by Molecular ChaperonesScience, 2002
- Hsp90 as a capacitor of phenotypic variationNature, 2002
- The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model systemToxicology Letters, 2001
- Stable Association of hsp90 and p23, but Not hsp70, with Active Human TelomeraseJournal of Biological Chemistry, 2001
- Crystal Structure and Activity of Human p23, a Heat Shock Protein 90 Co-chaperoneJournal of Biological Chemistry, 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 ,2000
- An unstructured C-terminal region of the hsp90 co-chaperone p23 is important for its chaperone function 1 1Edited by R. HuberJournal of Molecular Biology, 1999
- Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone MachineryJournal of Biological Chemistry, 1997
- Three Amino Acid Substitutions Selectively Disrupt the Activation but Not the Repression Function of the Glucocorticoid Receptor N TerminusJournal of Biological Chemistry, 1997