ATP Binding to PAN or the 26S ATPases Causes Association with the 20S Proteasome, Gate Opening, and Translocation of Unfolded Proteins
- 1 December 2005
- journal article
- research article
- Published by Elsevier in Molecular Cell
- Vol. 20 (5) , 687-698
- https://doi.org/10.1016/j.molcel.2005.10.019
Abstract
No abstract availableKeywords
This publication has 60 references indexed in Scilit:
- A Ratchet Mechanism of Transcription Elongation and Its ControlCell, 2005
- Interstitial Collagenase Is a Brownian Ratchet Driven by Proteolysis of CollagenScience, 2004
- An unstructured initiation site is required for efficient proteasome-mediated degradationNature Structural & Molecular Biology, 2004
- Protein unfolding — an important process in vivo?Current Opinion in Structural Biology, 2003
- Chemomechanical coupling of the forward and backward steps of single kinesin moleculesNature Cell Biology, 2002
- ATP Binding, but Not Its Hydrolysis, Is Required for Assembly and Proteolytic Activity of the HslVU Protease inEscherichia coliBiochemical and Biophysical Research Communications, 1997
- Structure of 20S proteasome from yeast at 2.4Å resolutionNature, 1997
- The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasomeNature Structural & Molecular Biology, 1997
- Protein Sorting: Pulling in the proteinsCurrent Biology, 1995
- Can Hsp70 proteins act as force-generating motors?Cell, 1995