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Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

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Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

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Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins

CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation

The Chaperone and Redox Properties of CnoX Chaperedoxins Are Tailored to the Proteostatic Needs of Bacterial Species

Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins

Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

Cytoplasmic Ubiquitin-Specific Protease 19 (USP19) Modulates Aggregation of Polyglutamine-Expanded Ataxin-3 and Huntingtin through the HSP90 Chaperone

Automated longitudinal monitoring of in vivo protein aggregation in neurodegenerative disease C. elegans models

Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein

Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones

Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs