title: Structural insights into functional and pathological amyloid.
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.
authors: Department of Pharmacology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, USA. fshewmaker@usuhs.mil
authors: Frank
authors: F
authors: Shewmaker
authors: Ryan P
authors: RP
authors: McGlinchey
authors: Reed B
authors: RB
authors: Wickner
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism; D000596:Amino Acids / Q000737:chemistry; D000682:Amyloid / Q000737:chemistry* / Q000502:physiology*; D000818:Animals; D001703:Biophysics / Q000379:methods; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D046529:Microscopy, Electron, Transmission / Q000379:methods; D011108:Polymers / Q000737:chemistry; D011328:Prions / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D000596:Amino Acids; D000682:Amyloid; D011108:Polymers; D011328:Prions