Cargando…
Distinct Annular Oligomers Captured along the Assembly and Disassembly Pathways of Transthyretin Amyloid Protofibrils
BACKGROUND: Defects in protein folding may lead to severe degenerative diseases characterized by the appearance of amyloid fibril deposits. Cytotoxicity in amyloidoses has been linked to poration of the cell membrane that may involve interactions with amyloid intermediates of annular shape. Although...
Autores principales: | Pires, Ricardo H., Karsai, Árpád, Saraiva, Maria J., Damas, Ana M., Kellermayer, Miklós S. Z. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3440338/ https://www.ncbi.nlm.nih.gov/pubmed/22984597 http://dx.doi.org/10.1371/journal.pone.0044992 |
Ejemplares similares
-
Amyloid
Oligomers and Protofibrils, but Not Filaments,
Self-Replicate from Native Lysozyme
por: Mulaj, Mentor, et al.
Publicado: (2014) -
Considerably Unfolded Transthyretin Monomers Preceed and Exchange with Dynamically Structured Amyloid Protofibrils
por: Groenning, Minna, et al.
Publicado: (2015) -
Amyloid Beta Annular Protofibrils in Cell Processes and Synapses Accumulate with Aging and Alzheimer-Associated Genetic Modification
por: Kokubo, Hideko, et al.
Publicado: (2009) -
Transthyretin Aggregation Pathway toward the Formation of Distinct Cytotoxic Oligomers
por: Dasari, Anvesh K. R., et al.
Publicado: (2019) -
Amyloid-β Protofibrils: Size, Morphology and Synaptotoxicity of an Engineered Mimic
por: Dubnovitsky, Anatoly, et al.
Publicado: (2013)