相关实验视频

Updated: Oct 5, 2025

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

12.1K

以结构为基础的合理设计对粉样β (1-42) 聚合和毒性进行动态调节

Dongjoon Im1,2,3, Chae Eun Heo1, Myung Kook Son1,2,3

  • 1Department of Chemistry, Korea University, Seoul 02841, Republic of Korea.

Journal of the American Chemical Society
|January 25, 2022
PubMed
概括

研究人员设计了突变蛋白来抑制粉样β纤维化,减少毒性. 这种基于结构的方法为调节神经退行性疾病中的蛋白质聚合提供了新的策略.

更多相关视频

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices04:41

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

23.4K
Modeling Amyloid-β42 Toxicity and Neurodegeneration in Adult Zebrafish Brain10:01

Modeling Amyloid-β42 Toxicity and Neurodegeneration in Adult Zebrafish Brain

Published on: October 25, 2017

11.4K

相关概念视频

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
10.5K