Cargando…
The prion-like RNA-processing protein HNRPDL forms inherently toxic amyloid-like inclusion bodies in bacteria
BACKGROUND: The formation of protein inclusions is connected to the onset of many human diseases. Human RNA binding proteins containing intrinsically disordered regions with an amino acid composition resembling those of yeast prion domains, like TDP-43 or FUS, are being found to aggregate in differe...
Autores principales: | Navarro, Susanna, Marinelli, Patrizia, Diaz-Caballero, Marta, Ventura, Salvador |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4498515/ https://www.ncbi.nlm.nih.gov/pubmed/26160665 http://dx.doi.org/10.1186/s12934-015-0284-7 |
Ejemplares similares
-
Yeast prions form infectious amyloid inclusion bodies in bacteria
por: Espargaró, Alba, et al.
Publicado: (2012) -
Amyloid Fibrils
Formed by Short Prion-Inspired Peptides
Are Metalloenzymes
por: Navarro, Susanna, et al.
Publicado: (2023) -
Characterization of Soft Amyloid Cores in Human Prion-Like Proteins
por: Batlle, Cristina, et al.
Publicado: (2017) -
Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria
por: Macedo, Bruno, et al.
Publicado: (2015) -
Functionalized Prion-Inspired Amyloids for Biosensor
Applications
por: Díaz-Caballero, Marta, et al.
Publicado: (2021)