Saeed Najafi

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: In this article, the role of polyethylene glycol (PEG) in complex coacervation driven liquid-liquid phase separation (LLPS) of biopolymers was investigated.

TL;DR: A structure-based coarse-grained model of the protein is introduced, where the information about the folded conformation is encoded in bonded angular interactions only, which do not favor the formation of native contacts.

TL;DR: In this paper, the authors show that subtle changes in solution conditions, including molecular crowding and the presence of binding partners, can lead to the formation of different types of Tau condensates with distinct micro-viscosity that can coexist as persistent and immiscible entities in solution.

TL;DR: The formation of membraneless organelles can be a proteotoxic stress control mechanism that locally condenses a set of components capable of mediating protein degradation decisions as mentioned in this paper .