Cargando…
The C-terminal domain of the antiamyloid chaperone DNAJB6 binds to amyloid-β peptide fibrils and inhibits secondary nucleation
The DNAJB6 chaperone inhibits fibril formation of aggregation-prone client peptides through interaction with aggregated and oligomeric forms of the amyloid peptides. Here, we studied the role of its C-terminal domain (CTD) using constructs comprising either the entire CTD or the first two or all fou...
Autores principales: | Österlund, Nicklas, Frankel, Rebecca, Carlsson, Andreas, Thacker, Dev, Karlsson, Maja, Matus, Vanessa, Gräslund, Astrid, Emanuelsson, Cecilia, Linse, Sara |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10641233/ https://www.ncbi.nlm.nih.gov/pubmed/37797698 http://dx.doi.org/10.1016/j.jbc.2023.105317 |
Ejemplares similares
-
Amyloid-β oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation
por: Österlund, Nicklas, et al.
Publicado: (2020) -
Mass Spectrometry and Machine Learning Reveal Determinants of Client Recognition by Antiamyloid Chaperones
por: Österlund, Nicklas, et al.
Publicado: (2022) -
Interaction of the Molecular Chaperone DNAJB6 with Growing Amyloid-beta 42 (Aβ42) Aggregates Leads to Sub-stoichiometric Inhibition of Amyloid Formation
por: Månsson, Cecilia, et al.
Publicado: (2014) -
Cell-Penetrating Peptides with Unexpected Anti-Amyloid Properties
por: Österlund, Nicklas, et al.
Publicado: (2022) -
On the micelle formation of DNAJB6b
por: Carlsson, Andreas, et al.
Publicado: (2023)