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

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

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Five Questions (with their Answers) on ER-Associated Degradation

Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling

Assessing the potential of atomistic molecular dynamics simulations to probe reversible protein-protein recognition and binding

N-linked sugar-regulated protein folding and quality control in the ER

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

Proteostasis: Bad news and good news from the endoplasmic reticulum

Real-Time Monitoring of Protein Conformational Changes Using a Nano-Mechanical Sensor

The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease

Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption

Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein