The ClpXP Protease Unfolds Substrates Using a Constant Rate of Pulling but Different Gears
Abstract
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This publication has 40 references indexed in Scilit:
- ClpXP, an ATP-powered unfolding and protein-degradation machineBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2012
- Stepwise Unfolding of a β Barrel Protein by the AAA+ ClpXP ProteaseJournal of Molecular Biology, 2011
- The nuts and bolts of ring-translocase structure and mechanismCurrent Opinion in Structural Biology, 2011
- ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein SubstratesCell, 2011
- Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic MachineCell, 2011
- Structures of Asymmetric ClpX Hexamers Reveal Nucleotide-Dependent Motions in a AAA+ Protein-Unfolding MachineCell, 2009
- Running in Reverse: The Structural Basis for Translocation Polarity in Hexameric HelicasesCell, 2009
- Intersubunit coordination in a homomeric ring ATPaseNature, 2009
- Distinct Static and Dynamic Interactions Control ATPase-Peptidase Communication in a AAA+ ProteaseMolecular Cell, 2007
- ATP-dependent proteases of bacteria: recognition logic and operating principlesTrends in Biochemical Sciences, 2006