Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency

Aggregate reactivation mediated by the Hsp100 chaperones

(2012) Michal Zolkiewski et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Orientation of the amino-terminal domain of ClpB affects the disaggregation of the protein

(2012) Sayaka Mizuno et al.   FEBS Journal

Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation

(2011) M. Miot et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Dynamic Allostery: Linkers Are Not Merely Flexible

(2011) Buyong Ma et al.   STRUCTURE

CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation

(2010) S. Lee et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface

(2009) Sergio P. Acebrón et al.   FEBS LETTERS

Developing force fields from the microscopic structure of solutions

(2009) Elizabeth A. Ploetz et al.   FLUID PHASE EQUILIBRIA

Synergistic Cooperation between Two ClpB Isoforms in Aggregate Reactivation

(2009) Maria Nagy et al.   JOURNAL OF MOLECULAR BIOLOGY

Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB

(2009) Maria Nagy et al.   PROTEIN SCIENCE

GROMACS 4:  Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

(2008) Berk Hess et al.   Journal of Chemical Theory and Computation

The Flexible Attachment of the N-Domains to the ClpA Ring Body Allows their Use On Demand

(2008) Susanne Cranz-Mileva et al.   JOURNAL OF MOLECULAR BIOLOGY