Cargando…
Production and Characterization of RNA Aptamers Specific for Amyloid Fibril Epitopes
One of the most fascinating features of amyloid fibrils is their generic cross-β architecture that can be formed from many different and completely unrelated proteins. Nonetheless, amyloid fibrils with diverse structural and phenotypic properties can form, both in vivo and in vitro, from the same pr...
Autores principales: | Bunka, David H.J., Mantle, Benjamin J., Morten, Isobel J., Tennent, Glenys A., Radford, Sheena E., Stockley, Peter G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8782670/ https://www.ncbi.nlm.nih.gov/pubmed/17878167 http://dx.doi.org/10.1074/jbc.M703679200 |
Ejemplares similares
-
A Common β-Sheet Architecture Underlies in Vitro and in Vivo β(2)-Microglobulin Amyloid Fibrils
por: Jahn, Thomas R., et al.
Publicado: (2008) -
Fibril Fragmentation Enhances Amyloid Cytotoxicity
por: Xue, Wei-Feng, et al.
Publicado: (2009) -
Stacked Sets of Parallel, In-register β-Strands of β(2)-Microglobulin in Amyloid Fibrils Revealed by Site-directed Spin Labeling and Chemical Labeling
por: Ladner, Carol L., et al.
Publicado: (2010) -
Comparisons with Amyloid-β Reveal an Aspartate Residue That Stabilizes Fibrils of the Aortic Amyloid Peptide Medin
por: Davies, Hannah A., et al.
Publicado: (2015) -
The role of the I(T)-state in D76N β(2)-microglobulin amyloid assembly: A crucial intermediate or an innocuous bystander?
por: Smith, Hugh I., et al.
Publicado: (2020)