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Updated: May 24, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

人間の病気におけるタンパク質のアミロイド状態

David Eisenberg1, Mathias Jucker

  • 1Howard Hughes Medical Institute, Department of Biological Chemistry, University of California, Los Angeles, Los Angeles CA 90095-1570, USA. david@mbi.ucla.edu

Cell
|March 20, 2012
PubMed
まとめ

アミロイド繊維とオリゴマーは,アルツハイマー病のような人間の病気と関連しています. このレビューは,分子タンパク質の性質を疾患の病理学,毒性,および潜在的な介入と関連付けています.

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

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Amyloid Fibrils03:03

Amyloid Fibrils

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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, normally used to...
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