TY - JOUR
T1 - Amyloid oligomers
T2 - A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis
AU - Nguyen, Phuong H.
AU - Ramamoorthy, Ayyalusamy
AU - Sahoo, Bikash R.
AU - Zheng, Jie
AU - Faller, Peter
AU - Straub, John E.
AU - Dominguez, Laura
AU - Shea, Joan Emma
AU - Dokholyan, Nikolay V.
AU - de Simone, Alfonso
AU - Ma, Buyong
AU - Nussinov, Ruth
AU - Najafi, Saeed
AU - Ngo, Son Tung
AU - Loquet, Antoine
AU - Chiricotto, Mara
AU - Ganguly, Pritam
AU - McCarty, James
AU - Li, Mai Suan
AU - Hall, Carol
AU - Wang, Yiming
AU - Miller, Yifat
AU - Melchionna, Simone
AU - Habenstein, Birgit
AU - Timr, Stepan
AU - Chen, Jiaxing
AU - Hnath, Brianna
AU - Strodel, Birgit
AU - Kayed, Rakez
AU - Lesné, Sylvain
AU - Wei, Guanghong
AU - Sterpone, Fabio
AU - Doig, Andrew J.
AU - Derreumaux, Philippe
N1 - Publisher Copyright:
© 2021 American Chemical Society
PY - 2021/2/24
Y1 - 2021/2/24
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85100615621&partnerID=8YFLogxK
U2 - 10.1021/acs.chemrev.0c01122
DO - 10.1021/acs.chemrev.0c01122
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C2 - 33543942
AN - SCOPUS:85100615621
SN - 0009-2665
VL - 121
SP - 2545
EP - 2647
JO - Chemical Reviews
JF - Chemical Reviews
IS - 4
ER -
