相关实验视频

Updated: Jun 8, 2025

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

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探索生理C端切断对α-Synuclein形状的影响,揭示调节病理聚合的机制

Fengjuan Huang1, Jiajia Yan2, Huan Xu2

  • 1Ningbo Institute of Innovation for Combined Medicine and Engineering (NIIME), The Affiliated Lihuili Hospital of Ningbo University, Ningbo 315211, China.

Journal of chemical information and modeling
|November 6, 2024
PubMed
概括

在帕金森病中,α-synuclein (αS) 的C端切断通过暴露容易聚合的区域,促进了粉样蛋白聚合. 这项研究使用模拟来揭示切割如何改变αS形状并驱动病理过程.

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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

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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,...
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