Cargando…
A Common β-Sheet Architecture Underlies in Vitro and in Vivo β(2)-Microglobulin Amyloid Fibrils
Misfolding and aggregation of normally soluble proteins into amyloid fibrils and their deposition and accumulation underlies a variety of clinically significant diseases. Fibrillar aggregates with amyloid-like properties can also be generated in vitro from pure proteins and peptides, including those...
Autores principales: | Jahn, Thomas R., Tennent, Glenys A., Radford, Sheena E. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2427364/ https://www.ncbi.nlm.nih.gov/pubmed/18424782 http://dx.doi.org/10.1074/jbc.M710351200 |
Ejemplares similares
-
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) -
Production and Characterization of RNA Aptamers Specific for Amyloid Fibril Epitopes
por: Bunka, David H.J., et al.
Publicado: (2020) -
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) -
Fibril Fragmentation Enhances Amyloid Cytotoxicity
por: Xue, Wei-Feng, et al.
Publicado: (2009) -
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)