The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that ensures cellular
proteostasis by maintaining the folding, stabilization, activation, and degradation of over 400 …

Malaria is still one of the major killer parasitic diseases in tropical settings, posing a public
health threat. The development of antimalarial drug resistance is reversing the gains made …

In a living cell, protein function is regulated in several ways, including post-translational
modifications (PTMs), protein-protein interaction, or by the global environment (eg crowding …

We report on a study that combines advanced fluorescence methods with molecular
dynamics (MD) simulations to cover timescales from nanoseconds to milliseconds for a large …

Hsp90, a crucial molecular chaperone, regulates diverse client proteins, impacting both
normal biology and disease. Central to its function is its conformational plasticity, driven by …

Cytochromes P450 are versatile enzymes that function in endobiotic and xenobiotic
metabolism and undergo meaningful structural changes that relate to their function …

The Hsp90 chaperone is an ATPase enzyme composed of two copies of a three-domain
subunit. Hsp90 stabilizes and activates a diverse array of regulatory proteins. Substrates are …

Protein turnover in cells is regulated by the ATP dependent activity of the Hsp90 chaperone.
In concert with accessory proteins, ATP hydrolysis drives the obligate Hsp90 dimer through …

Abstract Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that plays an
essential role in cellular homeostasis. It functions in the context of a structurally dynamic ATP …

To probe ligand-receptor binding at the atomic-level, a frequent approach involves
multidimensional nuclear magnetic resonance (NMR) spectroscopy experiments relying on …