Yimei Lu

NMR studies reveal that protein dynamics critically mediate aggregation of the well-folded and very soluble E. coli S1 ribosomal protein

This study uses NMR and spectroscopy to show that dynamic inter-domain interactions and domain-level motions in E. coli S1 protein contribute to its aggregation propensity despite being well-folded and soluble.

RRM domain of ALS/FTD-causing FUS interacts with membrane: an anchor of membraneless organelles to membranes?

The paper investigates whether the RRM domain of FUS interacts with membranes, finding that it dynamically binds bicelles, suggesting a mechanism for organizing membraneless organelles with membranes.

Unlocked capacity of proteins to attack membranes characteristic of aggregation: the evil for diseases and aging from Pandora’s box

The paper investigates how protein aggregation in aging and disease unlocks membrane-interacting capacities, revealing that disrupted protein folds in E. coli and ALS-causing mutations expose hydrophobic regions that interact abnormally with membranes.

Mechanisms of self-assembly and fibrillization of the prion-like domains

This study investigates the self-assembly and fibrillization of prion-like domains, showing that these processes are sequence-dependent and not primarily governed by electrostatic interactions.