An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function
- 12 January 2007
- journal article
- research article
- Published by Elsevier BV in Molecular Cell
- Vol. 25 (1), 151-159
- https://doi.org/10.1016/j.molcel.2006.12.008
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complexNature, 2006
- Chaperoning Checkpoint Kinase 1 (Chk1), an Hsp90 Client, with Purified ChaperonesOnline Journal of Public Health Informatics, 2006
- A yeast-based assay reveals a functional defect of the Q488H polymorphism in human Hsp90αBiochemical and Biophysical Research Communications, 2005
- Activity of Suberoylanilide Hydroxamic Acid Against Human Breast Cancer Cells with Amplification of Her-2Clinical Cancer Research, 2005
- Inhibition of Histone Deacetylase 6 Acetylates and Disrupts the Chaperone Function of Heat Shock Protein 90Online Journal of Public Health Informatics, 2005
- Structures of the N-Terminal and Middle Domains of E. coli Hsp90 and Conformation Changes upon ADP BindingStructure, 2005
- Identification and Characterization of a Novel p300-mediated p53 Acetylation Site, Lysine 305Online Journal of Public Health Informatics, 2003
- Hsp90 Regulates a von Hippel Lindau-independent Hypoxia-inducible Factor-1α-degradative PathwayOnline Journal of Public Health Informatics, 2002
- Domain Structures and Immunogenic Regions of the 90-kDa Heat-shock Protein (HSP90)Online Journal of Public Health Informatics, 1997
- Hsp90 Regulates Androgen Receptor Hormone Binding Affinity in VivoOnline Journal of Public Health Informatics, 1996