Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

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Nguyen, Phuong, H | Ramamoorthy, Ayyalusamy | Sahoo, Bikash, R | Zheng, Jie | Faller, Peter | Straub, John, E | Dominguez, Laura | Shea, Joan-Emma | Dokholyan, Nikolay, V | de Simone, Alfonso | Ma, Buyong | Nussinov, Ruth | Najafi, Saeed | Ngo, Son, Tung | Loquet, Antoine | Chiricotto, Mara | Ganguly, Pritam | Mccarty, James | Li, Mai, Suan | Hall, Carol | Wang, Yiming | Miller, Yifat | Melchionna, Simone | Habenstein, Birgit | Timr, Stepan | Chen, Jiaxing | Hnath, Brianna | Strodel, Birgit | Kayed, Rakez | Lesné, Sylvain | Wei, Guanghong | Sterpone, Fabio | Doig, Andrew, J | Derreumaux, Philippe

Edité par CCSD ; American Chemical Society -

International audience. Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural and dynamic characterization of all species along the pathways from monomers to fibrils is challenging by experimental and computational means because they involve intrinsically disordered proteins in most diseases. Yet understanding how amyloid species become toxic is the challenge in developing a treatment for these diseases. Here we 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 (AD), Parkinson's disease (PD), type II diabetes (T2D) and amyotrophic lateral sclerosis (ALS) research, respectively for over many years.

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