Heath W. Ecroyd

This study uses single-molecule techniques to show how Hsp90 helps Hsp70 release folding intermediates and remodel client proteins to enable proper refolding.

This study uses smFRET to visualize how Hsp70 remodels misfolded Fluc under chemical and heat stress, revealing conformational expansion and Hsp110-driven release for productive folding.

This paper shows that HspB1 and HspB5 differentially regulate TDP-43LCD condensation and aggregation, with HspB1 increasing dynamic exchange and HspB5 delaying pathological transition.

The paper compares proteostasis capacity in two neuronal cell lines by analyzing inclusion formation of an aggregation-prone protein, revealing differences in proteostasis machinery engagement.

This study investigates the interaction between sHsps and Hsp70 chaperones in α-synuclein disaggregation and aggregation, finding no synergy and potential antagonism between the chaperone classes.

This study uses single-molecule techniques to characterize how human sHsps bind to aggregation-prone client proteins and form complexes.

This paper introduces a flow cytometry-based method to quantify protein inclusions in C. elegans, demonstrating its applicability across multiple aggregation models and its ability to monitor inclusion dynamics under stress and aging.