Cargando…
The Toxicity of a Mutant Prion Protein Is Cell-Autonomous, and Can Be Suppressed by Wild-Type Prion Protein on Adjacent Cells
Insight into the normal function of PrP(C), and how it can be subverted to produce neurotoxic effects, is provided by PrP molecules carrying deletions encompassing the conserved central region. The most neurotoxic of these mutants, Δ105–125 (called ΔCR), produces a spontaneous neurodegenerative illn...
Autores principales: | Biasini, Emiliano, Turnbaugh, Jessie A., Massignan, Tania, Veglianese, Pietro, Forloni, Gianluigi, Bonetto, Valentina, Chiesa, Roberto, Harris, David A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3299791/ https://www.ncbi.nlm.nih.gov/pubmed/22428057 http://dx.doi.org/10.1371/journal.pone.0033472 |
Ejemplares similares
-
The N-Terminal, Polybasic Region Is Critical for Prion Protein Neuroprotective Activity
por: Turnbaugh, Jessie A., et al.
Publicado: (2011) -
Cell Type-Specific Neuroprotective Activity of Untranslocated Prion Protein
por: Restelli, Elena, et al.
Publicado: (2010) -
Oligomeropathies, inflammation and prion protein binding
por: Forloni, Gianluigi, et al.
Publicado: (2022) -
An antipsychotic drug exerts anti-prion effects by altering the localization of the cellular prion protein
por: Stincardini, Claudia, et al.
Publicado: (2017) -
Immunopurification of Pathological Prion Protein Aggregates
por: Biasini, Emiliano, et al.
Publicado: (2009)