Coordinated ATP Hydrolysis by the Hsp90 Dimer
Open Access
- 1 September 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (36), 33689-33696
- https://doi.org/10.1074/jbc.m103832200
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Hsp90: Chaperoning signal transductionJournal of Cellular Physiology, 2001
- C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle 1 1Edited by R. HuberJournal of Molecular Biology, 2000
- Delimitation of Two Regions in the 90-kDa Heat Shock Protein (Hsp90) Able to Interact with the Glucocorticosteroid Receptor (GR)Experimental Cell Research, 1999
- Monomer Arrangement in HSP90 Dimer as Determined by Decoration with N and C-Terminal Region Specific AntibodiesJournal of Molecular Biology, 1999
- Hydrolysis of ATP at Only One GyrB Subunit Is Sufficient to Promote Supercoiling by DNA GyrasePublished by Elsevier ,1998
- Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding ReactionCell, 1996
- Dimerization Is Required for the Activity of the Protein Histidine Kinase CheA That Mediates Signal Transduction in Bacterial ChemotaxisPublished by Elsevier ,1996
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- Crystal structure of an N-terminal fragment of the DNA gyrase B proteinNature, 1991
- Molecular Properties of Lactic Dehydrogenase under the Conditions of the Enzymatic TestEuropean Journal of Biochemistry, 1973