| Literature DB >> 21454545 |
Frank Shewmaker1, Ryan P McGlinchey, Reed B Wickner.
Abstract
Amyloid is traditionally viewed as a consequence of protein misfolding and aggregation and is most notorious for its association with debilitating and chronic human diseases. However, a growing list of examples of "functional amyloid" challenges this bad reputation and indicates that many organisms can employ the biophysical properties of amyloid for their benefit. Because of developments in the structural studies of amyloid, a clearer picture is emerging about what defines amyloid structure and the properties that unite functional and pathological amyloids. Here, we review various amyloids and place them within the framework of the latest structural models.Entities:
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Year: 2011 PMID: 21454545 PMCID: PMC3089495 DOI: 10.1074/jbc.R111.227108
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157