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

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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淀粉样低聚物:阿尔茨海默病、帕金森病、II型糖尿病和肌萎缩侧索硬化症的联合实验/计算观点。

DOI:
10.1021/acs.chemrev.0c01122
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发表时间:
2021-02-24
期刊:
影响因子:
62.1
通讯作者:
Derreumaux P
Derreumaux P
中科院分区:
化学1区
文献类型:
--
作者:
Nguyen PH;Ramamoorthy A;Sahoo BR;Zheng J;Faller P;Straub JE;Dominguez L;Shea JE;Dokholyan NV;De Simone A;Ma B;Nussinov R;Najafi S;Ngo ST;Loquet A;Chiricotto M;Ganguly P;McCarty J;Li MS;Hall C;Wang Y;Miller Y;Melchionna S;Habenstein B;Timr S;Chen J;Hnath B;Strodel B;Kayed R;Lesné S;Wei G;Sterpone F;Doig AJ;Derreumaux P

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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.
淀粉样蛋白生成被脯氨酸取代所消除,但通过脂质结合而增强。
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