Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37
Open Access
- 26 September 2008
- journal article
- Published by Elsevier BV in Molecular Cell
- Vol. 31 (6), 886-895
- https://doi.org/10.1016/j.molcel.2008.07.021
Abstract
No abstract availableThis publication has 45 references indexed in Scilit:
- Alteration of the Protein Kinase Binding Domain Enhances Function of the Saccharomyces cerevisiae Molecular Chaperone Cdc37Eukaryotic Cell, 2007
- Cdc37p Is Required for Stress-Induced High-Osmolarity Glycerol and Protein Kinase C Mitogen-Activated Protein Kinase Pathway Functionality by Interaction with Hog1p and Slt2p (Mpk1p)Eukaryotic Cell, 2007
- Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturationThe Journal of cell biology, 2007
- Regulation of the Raf–MEK–ERK pathway by protein phosphatase 5Nature, 2006
- Protein Phosphatase 5 Is a Negative Modulator of Heat Shock Factor 1Published by Elsevier BV ,2005
- Molecular Recognition via Coupled Folding and Binding in a TPR DomainJournal of Molecular Biology, 2005
- Definition of Protein Kinase Sequence Motifs That Trigger High Affinity Binding of Hsp90 and Cdc37Published by Elsevier BV ,2004
- Biochemical and Structural Studies of the Interaction of Cdc37 with Hsp90Journal of Molecular Biology, 2004
- Identification of a Conserved Sequence Motif That Promotes Cdc37 and Cyclin D1 Binding to Cdk4Online Journal of Public Health Informatics, 2004
- Development of a Bicistronic Vector Driven by the Human Polypeptide Chain Elongation Factor 1α Promoter for Creation of Stable Mammalian Cell Lines That Express Very High Levels of Recombinant ProteinsBiochemical and Biophysical Research Communications, 1998