相关实验视频

Updated: Jun 6, 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

11.8K

碳酸无酶粉胺聚合的加速导致纤维的毒性降低

Liliia Fakhranurova1, Victor Marchenkov2, Anatoly Glukhov2

  • 1Branch of the Institute of Bioorganic Chemistry RAS, Prospekt Nauki, 6, Pushchino, 142290, Russia.

Biochemical and biophysical research communications
|December 2, 2024
PubMed
概括

加快粉样蛋白的形成可以降低蛋白质聚合物的毒性. 修改残留物疏水性会影响粉样蛋白结构和细胞毒性,提供对抗粉样蛋白疾病的策略.

关键词:
聚合率是指聚合率是指聚合率.粉样蛋白是什么 粉样蛋白是什么碳酸无水酶是一种碳酸无水酶.细胞毒性 细胞毒性寡合体是一种寡合体.

更多相关视频

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils00:15

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

5.9K
Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System09:52

Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System

Published on: December 28, 2017

10.6K

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,...
9.2K