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Updated: Jun 17, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

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在小鼠中经过后,A-synuclein prion菌株以差异化方式适应

Sara A M Holec1,2, Chase R Khedmatgozar1,2, Shelbe J Schure1

  • 1Department of Microbiology, Immunology, and Pathology, Prion Research Center, Colorado State University, Fort Collins, Colorado, United States of America.

PLoS pathogens
|December 6, 2024
PubMed
概括

像MSA这样的α-synuclein prion疾病在小鼠的初始传递过程中适应. 鼠标通过选择特定的α-synuclein形状,类似于蛋白 (PrP) 菌株.

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Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils

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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

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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, normally used to...