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Updated: Mar 26, 2026

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

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在哺乳动物细胞中存在单体α-synuclein的结构障碍

Francois-Xavier Theillet1, Andres Binolfi1, Beata Bekei1

  • 1In-Cell NMR Laboratory, Department of NMR-supported Structural Biology, Leibniz Institute of Molecular Pharmacology (FMP Berlin), Robert-Rössle Strasse 10, 13125 Berlin, Germany.

Nature
|January 26, 2016
PubMed
概括

错误折叠的α-synuclein蛋白质会导致帕金森病. 在细胞中,这种蛋白质保持无序,并采用紧的屏蔽形状,防止聚合.

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相关概念视频

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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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