Young-Ho Lee

TL;DR: This work has developed a method called β-structure selection (BeStSel) for the secondary structure estimation that takes into account the twist of β-structures, and can predict the protein fold down to the topology level following the CATH classification from a single CD spectrum.

TL;DR: It is shown that the orientation and twisting of β-sheets account for the observed spectral diversity, and a new method to estimate accurately the secondary structure is developed, and the originality of BeStSel is that it carries out a detailed secondary structure analysis.

TL;DR: GQDs penetrate the blood–brain barrier and protect against dopamine neuron loss induced by α-syn preformed fibrils, Lewy body/Lewy neurite pathology and behavioural deficits, and can rescue neuronal death and synaptic loss.

TL;DR: By monitoring the kinetics of the formation of amyloid fibrils and glass-like amorphous aggregates, it is shown that solubility and supersaturation will be key factors for further understanding the aberrant aggregation of proteins.

TL;DR: In this article, the authors show that GQDs exhibit anti-amyloid activity via direct interaction with alpha-synuclein (α-syn) aggregates and demonstrate that they have notable potency in not only inhibiting fibrillization of α-syn but also disaggregating mature fibrils in a time-dependent manner.