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Updated: Jun 23, 2025

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

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轻链突变有助于定义系统AL氨基粉症中的纤维状形态

Sara Karimi-Farsijani1, Peter Benedikt Pfeiffer2, Sambhasan Banerjee1

  • 1Institute of Protein Biochemistry, Ulm University, Ulm, Germany.

Nature communications
|June 15, 2024
PubMed
概括

免疫球蛋白轻链中的突变会导致全身AL氨基粉症. 不同的突变导致不同的纤维结构,影响致病剂.

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Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging10:04

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

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Characterization of Amyloid Structures in Aging C. Elegans Using Fluorescence Lifetime Imaging09:31

Characterization of Amyloid Structures in Aging C. Elegans Using Fluorescence Lifetime Imaging

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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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