Birgit Strodel

TL;DR: Simulations Complement Experimental Studies Jessica Nasica-Labouze, Phuong H. Nguyen, Fabio Sterpone,† Olivia Berthoumieu,‡ Nicolae-Viorel Buchete, Sebastien Cote, Alfonso De Simone, Andrew J. Doig, and Philippe Derreumaux are authors of this paper.

TL;DR: In this paper, the authors review what computer, in vitro, in vivo, and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (Aβ, tau), α-synuclein, IAPP, and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer's disease, Parkinson's disease (PD), type II diabetes (T2D), and amyotrophic lateral sclerosis (ALS) research.

TL;DR: The energy landscape of the monomer and dimer are explored for the amyloidogenic heptapeptide GNNQQNY from the N-terminal prion-determining domain of the yeast protein Sup35 to find a rapid fluctuation between four different conformations, where a geometry intermediate between compact and extended structures is the most thermodynamically favorable.

TL;DR: It is suggested that Aβ pores may consist of tetrameric and hexameric β-sheet subunits subunits, which are consistent with the results of biophysical and biochemical experiments.

TL;DR: The aim of this review is to document the progress in the research onAmyloid formation from a physicochemical perspective with a special focus on the physiological factors influencing the aggregation of the amyloid-β peptide, the islet amyloids polypeptide, α-synuclein, and the hungingtin protein.