Cargando…
Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet Core
Amyloid deposits formed from islet amyloid polypeptide (IAPP) are a hallmark of type 2 diabetes mellitus and are known to be cytotoxic to pancreatic β-cells. The molecular structure of the fibrillar form of IAPP is subject of intense research, and to date, different models exist. We present results...
Autores principales: | Weirich, Franziska, Gremer, Lothar, Mirecka, Ewa A., Schiefer, Stephanie, Hoyer, Wolfgang, Heise, Henrike |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5015977/ https://www.ncbi.nlm.nih.gov/pubmed/27607147 http://dx.doi.org/10.1371/journal.pone.0161243 |
Ejemplares similares
-
β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor
por: Mirecka, Ewa A., et al.
Publicado: (2016) -
Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of β-wrapins
por: Orr, Asuka A., et al.
Publicado: (2018) -
Structural details of amyloid β oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
por: König, Anna S., et al.
Publicado: (2021) -
Sequence-Dependent Self-Assembly and Structural Diversity
of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils
por: Wang, Shih-Ting, et al.
Publicado: (2017) -
Amyloid fibril formation kinetics of low-pH denatured bovine PI3K-SH3 monitored by three different NMR techniques
por: Gardon, Luis, et al.
Publicado: (2023)