ATP-dependent Proteases Differ Substantially in Their Ability to Unfold Globular Proteins
Open Access
- 1 July 2009
- journal article
- Published by Elsevier
- Vol. 284 (28) , 18674-18684
- https://doi.org/10.1074/jbc.m900783200
Abstract
No abstract availableKeywords
This publication has 105 references indexed in Scilit:
- Substrate selection by the proteasome during degradation of protein complexesNature Chemical Biology, 2008
- Evolution of the ssrA degradation tag in Mycoplasma : Specificity switch to a different proteaseProceedings of the National Academy of Sciences, 2008
- Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfoldingNature Structural & Molecular Biology, 2008
- Diverse Pore Loops of the AAA+ ClpX Machine Mediate Unassisted and Adaptor-Dependent Recognition of ssrA-Tagged SubstratesMolecular Cell, 2008
- Single-Turnover Kinetic Experiments Confirm the Existence of High- and Low-Affinity ATPase Sites in Escherichia coli Lon ProteaseBiochemistry, 2006
- Monitoring the Timing of ATP Hydrolysis with Activation of Peptide Cleavage in Escherichia coli Lon by Transient KineticsBiochemistry, 2005
- Broad yet high substrate specificity: the challenge of AAA+ proteinsJournal of Structural Biology, 2004
- Recognition of the polyubiquitin proteolytic signalThe EMBO Journal, 2000
- Structure of 20S proteasome from yeast at 2.4Å resolutionNature, 1997
- Poly-L-lysine Activates both Peptide and ATP Hydrolysis by the ATP-Dependent HslVU Protease inEscherichia coliBiochemical and Biophysical Research Communications, 1996