Journal
CELL
Volume 148, Issue 6, Pages 1188-1203Publisher
CELL PRESS
DOI: 10.1016/j.cell.2012.02.022
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIA NIH HHS [R01 AG029430] Funding Source: Medline
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Amyloid fibers and oligomers are associated with a great variety of human diseases including Alzheimer's disease and the prion conditions. Here we attempt to connect recent discoveries on the molecular properties of proteins in the amyloid state with observations about pathological tissues and disease states. We summarize studies of structure and nucleation of amyloid and relate these to observations on amyloid polymorphism, prion strains, coaggregation of pathogenic proteins in tissues, and mechanisms of toxicity and transmissibility. Molecular studies have also led to numerous strategies for biological and chemical interventions against amyloid diseases.
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