Analysis of the Cooperative ATPase Cycle of the AAA+ Chaperone ClpB from Thermus thermophilus by Using Ordered Heterohexamers with an Alternating Subunit Arrangement
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference45 articles.
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1. Modular and coordinated activity of AAA+ active sites in the double-ring ClpA unfoldase of the ClpAP protease;Proceedings of the National Academy of Sciences;2020-10-05
2. ClpL is a functionally active tetradecameric AAA+ chaperone, distinct from hexameric/dodecameric ones;The FASEB Journal;2020-09-10
3. Observation of a Transient Reaction Intermediate Illuminates the Mechanochemical Cycle of the AAA-ATPase p97;Journal of the American Chemical Society;2020-08-13
4. Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation;Journal of Biological Chemistry;2018-12
5. Dynamic structural states of ClpB involved in its disaggregation function;Nature Communications;2018-06-01
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