Propagation of pathological α-synuclein by a prion-like mechanism
Intercellular abnormal protein aggregates are a common feature of many neurodegenerative diseases. Misfolded proteins are accumulated in neurons and/or glial cells as a fibriller, phosphorylated and partially ubiquitinated forms. The distribution and spreading of these abnormal proteins in brains of patients are shown to correlate with clinical ...
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Prion-like propagation of alpha-synuclein in reconstructed neural networks
Neurodegenerative diseases such as Parkinsons’s or Alzheimer’s diseases are characterized by the aggregation of misfolded proteins in insoluble inclusions. These inclusions trigger cellular dysfnctions and are therefore thought to play an important role in the development of these pathologies.
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Interferon-Stimulated Gene-Mediated Defense Against Prion Infection: Noncanonical Function of Oas1a. [PDF]
Homma T, Ishibashi D.
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Prion-like Protein TDP-43: Mechanisms, Diagnosis, and Therapeutic Prospects. [PDF]
Shimamura MI, Satoh K.
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Evidence for multiple prion conformers in natural scrapie isolates. [PDF]
Imamura M +10 more
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Therapeutic strategies in prion disease: current evidence, translational challenges, and emerging directions. [PDF]
Zhu Y, Bradford BM, Mabbott NA.
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Deletion Analysis of Phase Separation, Amyloid Formation and Prion Propagation by the Intrinsically Disordered Region of Yeast Sup35 Protein. [PDF]
Grizel AV +6 more
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Cellular prion protein and its derived peptides: multifaceted roles in neurodegenerative diseases and potential as biomarkers. [PDF]
Mari E +9 more
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A scalable, dividing cell model for the robust propagation and quantification of human sporadic Creutzfeldt-Jakob disease prions. [PDF]
Nihat A +8 more
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