Multiple Conformations of E. coli Hsp90 in Solution: Insights into the Conformational Dynamics of Hsp90
- 1 May 2008
- Vol. 16 (5) , 755-765
- https://doi.org/10.1016/j.str.2008.01.021
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- The ATPase Cycle of the Endoplasmic Chaperone Grp94Journal of Biological Chemistry, 2007
- Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 ChaperonesMolecular Cell, 2007
- Molecular chaperones and protein kinase quality controlTrends in Cell Biology, 2007
- Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domainProceedings of the National Academy of Sciences, 2006
- Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complexNature, 2006
- Development of Purine-Scaffold Small Molecule Inhibitors of Hsp90Current Cancer Drug Targets, 2003
- Disassembly of Transcriptional Regulatory Complexes by Molecular ChaperonesScience, 2002
- GroEL–Substrate InteractionsCell, 2000
- An improved method for calculating the contribution of solvent to the X-ray diffraction pattern of biological moleculesJournal of Applied Crystallography, 1978
- Zerstreuung von RöntgenstrahlenAnnalen der Physik, 1915