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Updated: May 6, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
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Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

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合成林-1调节了α-synuclein的组装,释放和吸收.

Diana F Lázaro1,2, Triana Amen3,4, Ellen Gerhardt5

  • 1Department of Pathology and Laboratory Medicine, Institute on Aging and Center for Neurodegenerative Disease Research, Perelman School of Medicine at the University of Pennsylvania, Pennsylvania, PA, USA. diana.lazaro@pennmedicine.upenn.edu.

NPJ Parkinson's disease
|November 20, 2025
PubMed
概括

研究人员使用synphilin-1 (Sph1) 在细胞中建模了α-synuclein (aSyn) 组件. 这揭示了明显的凝和固体类含,为帕金森病提供了新的洞察力.

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation09:16

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

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A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model08:24

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

Published on: November 25, 2022

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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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