Unfolding of Metastable Linker Region Is at the Core of Hsp33 Activation as a Redox-regulated Chaperone

The mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity

(2010) Hongmei Yang et al.   PROTEIN SCIENCE

Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins

(2009) P. Tompa   FEBS Journal

Substrate binding site flexibility of the small heat shock protein molecular chaperones

(2009) N. Jaya et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding

(2009) T. L. Tapley et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Conserved amphiphilic feature is essential for periplasmic chaperone HdeA to support acid resistance in enteric bacteria

(2008) Ye E. Wu et al.   BIOCHEMICAL JOURNAL

Bleach Activates a Redox-Regulated Chaperone by Oxidative Protein Unfolding

(2008) J. Winter et al.   CELL

Activation of the Chaperone Hsp26 Is Controlled by the Rearrangement of Its Thermosensor Domain

(2008) Titus M. Franzmann et al.   MOLECULAR CELL

Quantifying changes in the thiol redox proteome upon oxidative stress in vivo

(2008) L. I. Leichert et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

On the Contribution of Water-Mediated Interactions to Protein-Complex Stability†

(2007) Dana Reichmann et al.   BIOCHEMISTRY