Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity
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Title
Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity
Authors
Keywords
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Journal
MOLECULAR MICROBIOLOGY
Volume 91, Issue 1, Pages 66-78
Publisher
Wiley
Online
2013-10-29
DOI
10.1111/mmi.12444
References
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Related references
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- AAA+ Proteases: ATP-Fueled Machines of Protein Destruction
- (2011) Robert T. Sauer et al. Annual Review of Biochemistry
- Stepwise Unfolding of a β Barrel Protein by the AAA+ ClpXP Protease
- (2011) Andrew R. Nager et al. JOURNAL OF MOLECULAR BIOLOGY
- Protein unfolding and degradation by the AAA+ Lon protease
- (2011) Eyal Gur et al. PROTEIN SCIENCE
- Structure of the N-terminal fragment ofEscherichia coliLon protease
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- Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber
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- Crystal Structures of Bacillus subtilis Lon Protease
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- (2010) R. M. Vabulas et al. Cold Spring Harbor Perspectives in Biology
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- Protein unfolding by a AAA+ protease is dependent on ATP-hydrolysis rates and substrate energy landscapes
- (2008) Andreas Martin et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
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