相关实验视频

Updated: Jun 24, 2025

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

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纳米盘复制和特征化粉样β前体蛋白C9999的前体蛋白

Bankala Krishnarjuna1,2, Gaurav Sharma1,2, Volodymyr M Hiiuk1,3

  • 1Biophysics Program, University of Michigan, Ann Arbor, Michigan 48109, United States.

Analytical chemistry
|June 3, 2024
PubMed
概括

研究人员将粉样前体蛋白 (APP) 的C端域重组为聚合物纳米光盘. 这一突破使得研究近似原生膜环境中的APP结构和动态成为可能,这对于了解阿尔茨海默病 (AD) 至关重要.

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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

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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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