Cargando…
Morphological Differences between β(2)-Microglobulin in Fibrils and Inclusion Bodies
Autores principales: | Taylor, Garrick F, Wood, Stephen P, Mörs, Karsten, Glaubitz, Clemens, Werner, Jörn M, Williamson, Philip T F |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
WILEY-VCH Verlag
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3084992/ https://www.ncbi.nlm.nih.gov/pubmed/22238149 http://dx.doi.org/10.1002/cbic.201000582 |
Ejemplares similares
-
The residual structure of acid‐denatured β(2)‐microglobulin is relevant to an ordered fibril morphology
por: Tomiyama, Ryosuke, et al.
Publicado: (2023) -
Intermolecular Alignment in β(2)-Microglobulin Amyloid Fibrils
por: Debelouchina, Galia T., et al.
Publicado: (2010) -
Globular Tetramers of β(2)-Microglobulin Assemble into Elaborate Amyloid Fibrils
por: White, Helen E., et al.
Publicado: (2009) -
A Common β-Sheet Architecture Underlies in Vitro and in Vivo β(2)-Microglobulin Amyloid Fibrils
por: Jahn, Thomas R., et al.
Publicado: (2008) -
β(2)-microglobulin forms 3D domain-swapped amyloid fibrils with disulfide linkages
por: Liu, Cong, et al.
Publicado: (2010)