Cargando…
The Effect of Octapeptide Repeats on Prion Folding and Misfolding
Misfolding of prion protein (PrP) into amyloid aggregates is the central feature of prion diseases. PrP has an amyloidogenic C-terminal domain with three α-helices and a flexible tail in the N-terminal domain in which multiple octapeptide repeats are present in most mammals. The role of the octapept...
Autores principales: | Yu, Kun-Hua, Huang, Mei-Yu, Lee, Yi-Ru, Lin, Yu-Kie, Chen, Hau-Ren, Lee, Cheng-I |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7918816/ https://www.ncbi.nlm.nih.gov/pubmed/33670336 http://dx.doi.org/10.3390/ijms22041800 |
Ejemplares similares
-
Characterization of Prion Disease Associated with a Two-Octapeptide Repeat Insertion
por: Brennecke, Nicholas, et al.
Publicado: (2021) -
Biological and Biochemical Characterization of Mice Expressing Prion Protein Devoid of the Octapeptide Repeat Region after Infection with Prions
por: Yamaguchi, Yoshitaka, et al.
Publicado: (2012) -
Amino Acid Substitution within Seven-Octapeptide Repeat Insertions in the Prion Protein Gene Associated with Short-Term Course
por: Chen, Zhongyun, et al.
Publicado: (2022) -
Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein
por: Goluguri, Rama Reddy, et al.
Publicado: (2019) -
Case Report: Histopathology and Prion Protein Molecular Properties in Inherited Prion Disease With a De Novo Seven-Octapeptide Repeat Insertion
por: Cali, Ignazio, et al.
Publicado: (2020)