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Updated: Jun 20, 2026

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein
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Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Published on: May 30, 2015

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空间转录学揭示了前进性和高级α-synucleinopathy的分子特征

Lin Lin1, Nanna M Jensen1,2, Alberto Delaidelli3,4

  • 1Department of Biomedicine, Aarhus University, Høegh-Guldbergs Gade 10, 8000 Aarhus, Denmark.

iScience
|February 25, 2026
PubMed
概括

空间转录学揭示了帕金森病 (PD) 的动物模型中能量代谢和mRNA翻译的改变. 异常的骨质疏松素信号和CREB结合蛋白被确定为PD大脑中的进展标志物.

关键词:
模型生物模型生物.分子神经科学分子神经科学蛋白质结构方面 蛋白质结构方面文字转录学 (Transcriptomics) 是一个学科.

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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. 
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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...