Functional Importance of Heat Shock Protein 90 Associated with Insulin Receptor on Insulin-Stimulated Mitogenesis
- 18 August 1997
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 237 (2), 345-347
- https://doi.org/10.1006/bbrc.1997.7116
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- The hsp90-binding Antibiotic Geldanamycin Decreases Raf Levels and Epidermal Growth Factor Signaling without Disrupting Formation of Signaling Complexes or Reducing the Specific Enzymatic Activity of Raf KinaseJournal of Biological Chemistry, 1997
- The dominant negative effect of a kinase-defective insulin receptor on insulin-like growth factor-I-stimulated signaling in Rat-1 fibroblastsMetabolism, 1996
- Functional Importance of Amino-terminal Domain of Shc for Interaction with Insulin and Epidermal Growth Factor Receptors in Phosphorylation-independent MannerPublished by Elsevier ,1996
- Hsp90 Mutants Disrupt Glucocorticoid Receptor Ligand Binding and Destabilize Aporeceptor ComplexesJournal of Biological Chemistry, 1995
- Possible Role for Serine/Threonine Phosphorylation in the Regulation of the Heteroprotein Complex between the hsp90 Stress Protein and the pp60v-src Tyrosine KinaseJournal of Biological Chemistry, 1995
- 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
- Heat shock proteins.Journal of Biological Chemistry, 1990
- The transformed glucocorticoid receptor has a lower steroid-binding affinity than the nontransformed receptorBiochemistry, 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
- Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins.Proceedings of the National Academy of Sciences, 1986