Prion efficiently replicates in α-synuclein knockout mice
E Bistaffa, M Rossi, CMG De Luca, F Cazzaniga… - Molecular …, 2019 - Springer
Prion diseases are a group of neurodegenerative disorders associated with the
conformational conversion of the cellular prion protein (PrP C) into an abnormal misfolded …
conformational conversion of the cellular prion protein (PrP C) into an abnormal misfolded …
PrP meets alpha‐synuclein: Molecular mechanisms and implications for disease
TCRG Vieira, CA Barros, R Domingues… - Journal of …, 2024 - Wiley Online Library
The discovery of prions has challenged dogmas and has revolutionized our understanding
of protein‐misfolding diseases. The concept of self‐propagation via protein conformational …
of protein‐misfolding diseases. The concept of self‐propagation via protein conformational …
[HTML][HTML] α-Synuclein amyloids hijack prion protein to gain cell entry, facilitate cell-to-cell spreading and block prion replication
The precise molecular mechanism of how misfolded α-synuclein (α-Syn) accumulates and
spreads in synucleinopathies is still unknown. Here, we show the role of the cellular prion …
spreads in synucleinopathies is still unknown. Here, we show the role of the cellular prion …
[HTML][HTML] α-Synuclein strain propagation is independent of cellular prion protein expression in a transgenic synucleinopathy mouse model
RWL So, G Amano, E Stuart, A Ebrahim Amini… - PLoS …, 2024 - journals.plos.org
The cellular prion protein, PrPC, has been postulated to function as a receptor for α-
synuclein, potentially facilitating cell-to-cell spreading and/or toxicity of α-synuclein …
synuclein, potentially facilitating cell-to-cell spreading and/or toxicity of α-synuclein …
Calling α-synuclein a prion is scientifically justifiable
JC Watts - Acta Neuropathologica, 2019 - Springer
For more than a decade, the “prion-like” hypothesis for Parkinson's disease (PD) has
remained one of the most controversial topics in neurodegenerative disease research [21 …
remained one of the most controversial topics in neurodegenerative disease research [21 …
Alpha-synuclein-immunoreactive deposits in human and animal prion diseases
Prion related disorders are associated with the accumulation of a misfolded isoform (PrPsc)
of the host-encoded prion protein, PrP. There is strong evidence for the involvement of …
of the host-encoded prion protein, PrP. There is strong evidence for the involvement of …
The role of the prion protein in the internalization of α-synuclein amyloids
E De Cecco, G Legname - Prion, 2018 - Taylor & Francis
Synucleinopathies are a group of neurodegenerative diseases characterized by the
accumulation of α-synuclein amyloids in several regions of the brain. α-Synuclein fibrils are …
accumulation of α-synuclein amyloids in several regions of the brain. α-Synuclein fibrils are …
[HTML][HTML] Involvement of cellular prion protein in α-synuclein transport in neurons
L Urrea, M Segura-Feliu, M Masuda-Suzukake… - Molecular …, 2018 - Springer
The cellular prion protein, encoded by the gene Prnp, has been reported to be a receptor of
β-amyloid. Their interaction is mandatory for neurotoxic effects of β-amyloid oligomers. In …
β-amyloid. Their interaction is mandatory for neurotoxic effects of β-amyloid oligomers. In …
The cellular prion protein (PrPC) as neuronal receptor for α-synuclein
L Urrea, I Ferrer, R Gavín, JA Del Río - Prion, 2017 - Taylor & Francis
The term 'prion-like'is used to define some misfolded protein species that propagate
intercellularly, triggering protein aggregation in recipient cells. For cell binding, both direct …
intercellularly, triggering protein aggregation in recipient cells. For cell binding, both direct …
Accumulation of prion and abnormal prion protein induces hyperphosphorylation of α-synuclein in the brain tissues from prion diseases and in the cultured cells
DD Chen, LP Gao, YZ Wu, J Chen, C Hu… - ACS Chemical …, 2021 - ACS Publications
Prion disease (PrD) and Parkinson's disease (PD) are neurodegenerative diseases
characterized by aggregation of misfolded proteins in brain tissues, including protease …
characterized by aggregation of misfolded proteins in brain tissues, including protease …
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