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Updated: Jan 6, 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

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在α-Synuclein中的A30P和A30G突变促进了对EGCG具有明显结构反应的转移稳定的长寿聚合物

Santosh Devi1, Dushyant K Garg1, Rajiv Bhat1

  • 1School of Biotechnology, Jawaharlal Nehru University, New Delhi 110067, India.

Biochemistry
|November 7, 2025
PubMed
概括

同核蛋白病变中的α-synuclein突变可以减缓聚合,形成独特的,长寿的前纤维细胞物种. 这些转基因稳定对象受到像EGCG.这样的粉样蛋白调节剂的差异影响.

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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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