Cargando…
Methionine Oxidation Perturbs the Structural Core of the Prion Protein and Suggests a Generic Misfolding Pathway
Oxidative stress and misfolding of the prion protein (PrP(C)) are fundamental to prion diseases. We have therefore probed the effect of oxidation on the structure and stability of PrP(C). Urea unfolding studies indicate that H(2)O(2) oxidation reduces the thermodynamic stability of PrP(C) by as much...
Autores principales: | Younan, Nadine D., Nadal, Rebecca C., Davies, Paul, Brown, David R., Viles, John H. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3436581/ https://www.ncbi.nlm.nih.gov/pubmed/22654104 http://dx.doi.org/10.1074/jbc.M112.354779 |
Ejemplares similares
-
Overexpression of quality control proteins reduces prion conversion in prion-infected cells
por: Thapa, Simrika, et al.
Publicado: (2018) -
Disulfide-crosslink scanning reveals prion–induced conformational changes and prion strain–specific structures of the pathological prion protein PrP(Sc)
por: Taguchi, Yuzuru, et al.
Publicado: (2018) -
Chronic wasting disease (CWD) prion strains evolve via adaptive diversification of conformers in hosts expressing prion protein polymorphisms
por: Duque Velásquez, Camilo, et al.
Publicado: (2020) -
Autophagy regulates exosomal release of prions in neuronal cells
por: Abdulrahman, Basant A., et al.
Publicado: (2018) -
An astrocyte cell line that differentially propagates murine prions
por: Tahir, Waqas, et al.
Publicado: (2020)