Cryo-EM structure and polymorphism of Aβ amyloid fibrils …
2019年10月29日 · Transmission electron microscopy (TEM) analysis of negatively stained specimens reveals the elongated morphology of the fibrils in our samples (Supplementary Fig. 1a)....
Cryo-EM structures of amyloid-β 42 filaments from human brains
2022年1月13日 · Alzheimer’s disease is characterized by a loss of memory and other cognitive functions and the filamentous assembly of Aβ and tau in the brain. The assembly of Aβ peptides into filaments that end at residue 42 is a central event.
Molecular Structure of β-Amyloid Fibrils in Alzheimer’s ... - Cell Press
2013年9月12日 · Abeta (1-40) forms five distinct amyloid structures whose β-sheet contents and fibril stabilities are correlated
Cryo-EM of Aβ fibrils from mouse models find tg-APP - Nature
2023年11月16日 · We found novel Aβ fibril structures in the APP/PS1, ARTE10 and tg-SwDI models, whereas the human type II filament fold was found in the ARTE10, tg-APP Swe and APP23 models. The tg-APP ArcSwe mice...
Cryo-EM structures of amyloid-β 42 filaments from human brains
2022年1月14日 · Filament assembly of amyloid-β peptides ending at residue 42 (Aβ42) is a central event in Alzheimer’s disease. Here, we report the cryo–electron microscopy (cryo-EM) structures of Aβ42 filaments from human brains. Two structurally related S-shaped protofilament folds give rise to two types of filaments.
Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)
2024年2月13日 · Here we present the cryo-electron microscopy (cryo-EM) structures of six lipidic Aβ40 fibrils that assemble from three filament folds, providing structural insights into fibril–lipid interactions.
Human Amyloid Beta 1-42 Oligomers (SPR-488_
Our Aβ42 oligomers present as globular oligomers when observed under TEM and AFM, and have a unique dimer/trimer and oligomer signal on a Western Blot with an anti-amyloid beta antibody. Our Aβ42 oligomers were also demonstrated to be toxic to primary rat cortical neurons in a dose-dependent manner.
Science | 阿尔兹海默病相关蛋白Aβ42纤维结构被揭示 - 知乎
这篇Science研究解析了Aβ42细丝结构特征，将为神经退行性疾病的个体诊断、治疗和新型Aβ抗体治疗提供关键信息和证据。 为此， Science 刊发了 Michael Willem 和 Marcus Fändrich 教授的评述： A molecular view of human amyloid-β folds。 原文链接： doi.org/10.1126/science. 阿尔茨海默病（Alzheimer’s disease，AD）是一种以认知障碍和记忆能力损害为主的中枢神经系统原发性、退行性疾病，是失智症（dementia）中最常见的类型。 阿尔茨海默病人大脑中同时存在两种 …
(PDF) Imaging Abeta aggregation by liquid-phase ... - ResearchGate
2024年1月31日 · To achieve this goal, we apply liquid-phase transmission electron microscopy (LTEM) in combination with all-atom molecular dynamics simulations. Our results offer an initial...
TEM images of the morphology of Aβ1–42 aggregates at 0 h...
Our work provides valuable insights into the distinct reactivities of cobalt complexes towards Abeta peptides, which offers a novel strategy to control Abeta amyloidogenesis using transition...