| Literature DB >> 33543942 |
Phuong H Nguyen1, Ayyalusamy Ramamoorthy2, Bikash R Sahoo2, Jie Zheng3, Peter Faller4, John E Straub5, Laura Dominguez6, Joan-Emma Shea7, Nikolay V Dokholyan8,9, Alfonso De Simone10,11, Buyong Ma12,13, Ruth Nussinov12,14, Saeed Najafi7, Son Tung Ngo15, Antoine Loquet16, Mara Chiricotto17, Pritam Ganguly7, James McCarty18, Mai Suan Li19,20, Carol Hall21, Yiming Wang21, Yifat Miller22, Simone Melchionna23, Birgit Habenstein16, Stepan Timr1, Jiaxing Chen8, Brianna Hnath8, Birgit Strodel24, Rakez Kayed25, Sylvain Lesné26, Guanghong Wei27, Fabio Sterpone1, Andrew J Doig28, Philippe Derreumaux1,29,30.
Abstract
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 many years.Entities:
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Year: 2021 PMID： 33543942 PMCID： PMC8836097 DOI： 10.1021/acs.chemrev.0c01122
Source DB: PubMed Journal: Chem Rev ISSN： 0009-2665 Impact factor: 60.622