The Ah Receptor Is a Sensitive Target of Geldanamycin-Induced Protein Turnover
- 1 December 1997
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 348 (1) , 190-198
- https://doi.org/10.1006/abbi.1997.0398
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Disruption of the Raf-1-Hsp90 Molecular Complex Results in Destabilization of Raf-1 and Loss of Raf-1-Ras AssociationJournal of Biological Chemistry, 1995
- Production and Characterization of Monoclonal Antibodies Directed against theAhReceptorHybridoma, 1995
- Distinct Roles of the Molecular Chaperone hsp90 in Modulating Dioxin Receptor Function via the Basic Helix-Loop-Helix and PAS DomainsMolecular and Cellular Biology, 1995
- Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.Proceedings of the National Academy of Sciences, 1994
- Hsp90 chaperones protein folding in vitroNature, 1992
- Interaction of hsp90 with steroid receptors: organizing some diverse observations and presenting the newest conceptsMolecular and Cellular Endocrinology, 1990
- Reduced levels of hsp90 compromise steroid receptor action in vivoNature, 1990
- Evidence that the 90-Kilodalton Heat Shock Protein is Associated with Tubulin-Containing Complexes in L Cell Cytosol and in Intact PtK CellsMolecular Endocrinology, 1988
- The 90-kilodalton peptide of the heme-regulated eIF-2.alpha. kinase has sequence homology with the 90-kilodalton heat shock proteinBiochemistry, 1987
- Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and speciesBiochemistry, 1985