AAA+ ATPases: Achieving Diversity of Function with Conserved Machinery
Author:
Affiliation:
1. Department of Pathology, College of Physicians & Surgeons, Columbia University, New York, NY 10032, USA
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1600-0854.2007.00642.x
Reference89 articles.
1. A link between sequence conservation and domain motion within the AAA+ family
2. Crystal Structures of the HslVU Peptidase–ATPase Complex Reveal an ATP-Dependent Proteolysis Mechanism
3. Conserved Pore Residues in the AAA Protease FtsH Are Important for Proteolysis and Its Coupling to ATP Hydrolysis
4. Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates
5. Evidence for an Unfolding/Threading Mechanism for Protein Disaggregation by Saccharomyces cerevisiae Hsp104
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