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Updated: May 24, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
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一种有毒的粉样蛋白小寡合物的原子图

Arthur Laganowsky1, Cong Liu, Michael R Sawaya

  • 1Department of Biological Chemistry, University of California Los Angeles (UCLA), Howard Hughes Medical Institute (HHMI), Los Angeles, CA 90095, USA.

Science (New York, N.Y.)
|March 10, 2012
PubMed
概括

研究人员从αB晶体中确定了一种有毒的粉样蛋白寡合体结构,称为圆柱体,来自αB晶体. 这种结构丰富于β-sheet,模仿了阿尔茨海默氏症等神经退行性疾病中发现的有毒寡合体.

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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. 
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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...