Structural, Morphological, and Functional Diversity of Amyloid Oligomers
Document Type
Article
Publication Date
2015
Keywords
Protein misfolding, Protein aggregation, Amyloid oligomer, Amyloid fibril, Cytotoxicity
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.febslet.2015.07.013
Abstract
Protein misfolding and aggregation are known to play a crucial role in a number of important human diseases (Alzheimer’s, Parkinson’s, prion, diabetes, cataracts, etc.) as well as in a multitude of physiological processes. Protein aggregation is a highly complex process resulting in a variety of aggregates with different structures and morphologies. Oligomeric protein aggregates (amyloid oligomers) are formed as both intermediates and final products of the aggregation process. They are believed to play an important role in many protein aggregation-related diseases, and many of them are highly cytotoxic. Due to their instability and structural heterogeneity, information about structure, mechanism of formation, and physiological effects of amyloid oligomers is sparse. This review attempts to summarize the existing information on the major properties of amyloid oligomers.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 589, issue 19, p. 2640-2648
Scholar Commons Citation
Breydo, Leonid and Uversky, Vladimir N., "Structural, Morphological, and Functional Diversity of Amyloid Oligomers" (2015). Molecular Medicine Faculty Publications. 401.
https://digitalcommons.usf.edu/mme_facpub/401
