Yi Liang

TL;DR: Investigation of recombinant human Tau fragment Tau244–372 and its mutants shows that low micromolar zinc accelerates the fibrillization of human Tau protein via bridging Cys-291 and Cys -322 in physiological reducing conditions, providing clues to understanding the relationship between zinc dyshomeostasis and the etiology of neurodegenerative diseases.

TL;DR: The results presented here provide the first experimental evidence for the existence of competition between a repulsive excluded volume interaction between protein and polymer, which tends to enhance association of dilute protein, and an attractive interaction betweenprotein and polymer that tends to inhibit protein association.

TL;DR: In this paper, the wear behavior of a TiNi alloy after various heat treatments has been studied in three conditions: sliding wear, impact abrasion and sand-blasting erosion.

TL;DR: The data demonstrate that a crowded physiological environment could play an important role in the pathogenesis of neurodegenerative diseases by accelerating amyloidogenic protein misfolding and inducing human prion fibril fragmentation, which is considered to be an essential step in prion replication.

TL;DR: Both the ref folding yield and the refolding rate of MM-CK in mixtures of these agents are increased relative to the individual agents by themselves, indicating that mixed macromolecular crowding agents are more favorable to MM- CK folding and can be used to reflect the physiological environment more accurately than single crowding agent.