Cargando…
Polymorphic Aβ42 fibrils adopt similar secondary structure but differ in cross-strand side chain stacking interactions within the same β-sheet
Formation of polymorphic amyloid fibrils is a common feature in neurodegenerative diseases involving protein aggregation. In Alzheimer’s disease, different fibril structures may be associated with different clinical sub-types. Structural basis of fibril polymorphism is thus important for understandi...
Autores principales: | Wang, Hongsu, Duo, Lan, Hsu, Frederick, Xue, Christine, Lee, Yoon Kyung, Guo, Zhefeng |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7109039/ https://www.ncbi.nlm.nih.gov/pubmed/32235842 http://dx.doi.org/10.1038/s41598-020-62181-x |
Ejemplares similares
-
Site-specific structural order in Alzheimer's Aβ42 fibrils
por: Wang, Hongsu, et al.
Publicado: (2018) -
Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphism
por: Xue, Christine, et al.
Publicado: (2019) -
Key Residues for the Formation of Aβ42 Amyloid
Fibrils
por: Hsu, Frederick, et al.
Publicado: (2018) -
Distinguishing the Effect on the Rate and Yield of
Aβ42 Aggregation by Green Tea Polyphenol EGCG
por: Park, Giovanna, et al.
Publicado: (2020) -
pH-controlled stacking direction of the β-strands in peptide fibrils
por: Tseng, Wei-Hsuan, et al.
Publicado: (2020)