Cargando…
Protein misfolding in Dictyostelium: Using a freak of nature to gain insight into a universal problem
Prion-like proteins can undergo conformational rearrangements from an intrinsically disordered to a highly ordered amyloid state. This ability to change conformation is encoded in distinctive domains, termed prion domains (PrDs). Previous work suggests that PrDs change conformation to affect protein...
Autores principales: | Malinovska, Liliana, Alberti, Simon |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4964863/ https://www.ncbi.nlm.nih.gov/pubmed/26529309 http://dx.doi.org/10.1080/19336896.2015.1099799 |
Ejemplares similares
-
Molecular mechanisms of spatial protein quality control
por: Alberti, Simon
Publicado: (2012) -
Exosome-dependent and independent mechanisms are involved in prion-like transmission of propagated Cu/Zn superoxide dismutase misfolding
por: Grad, Leslie I, et al.
Publicado: (2014) -
Disease-associated protein seeding suggests a dissociation between misfolded protein accumulation and neurodegeneration in prion disease
por: Alibhai, James, et al.
Publicado: (2017) -
New insights into structural determinants of prion protein folding and stability
por: Benetti, Federico, et al.
Publicado: (2015) -
Saccharomyces cerevisiae: A sexy yeast with a prion problem
por: Kelly, Amy C., et al.
Publicado: (2013)