Molecular Mechanism of Hsp70 Chaperones: Interactions with Cochaperones and Substrates

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Explores the molecular mechanism and client preference of chaperonin GroEL in protein folding and aggregation prevention.

Explores the role of mitochondrial Hsp70 in protein import and folding processes, stress response pathways, and experimental techniques.

Explores the interaction between hsp70 and the intrinsically disordered Ntail domain of the measles virus nucleoprotein.

Explores protein folding dynamics, focusing on chaperone-assisted non-equilibrium stabilization and its implications for biophysics and evolution.

Delves into mitochondrial Hsp70 and MBP folding dynamics from a single molecule perspective.

Delves into DNAJB6's chaperone action, relevance to protein aggregation diseases, and interactions with various proteins.

Delves into transcellular chaperone signalling in C. elegans, revealing how it activates organismal proteostasis beyond cellular boundaries.

Explores the molecular interactions shaping tau polymorphs and the role of Hsp40s in regulating tau aggregation.

Explores protein folding dynamics, chaperones, ATP hydrolysis, and DNA folding intricacies within the nucleus.

Explores the regulation of the ER chaperone BiP, including its interaction with substrates and the impact of Ca²+ levels on its function.