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Cell. 2012 Mar 16;148(6):1188-203. doi: 10.1016/j.cell.2012.02.022.

The amyloid state of proteins in human diseases.

Author information

1
Howard Hughes Medical Institute, Department of Biological Chemistry, University of California, Los Angeles, Los Angeles CA 90095-1570, USA. david@mbi.ucla.edu

Abstract

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.

PMID:
22424229
PMCID:
PMC3353745
DOI:
10.1016/j.cell.2012.02.022
[Indexed for MEDLINE]
Free PMC Article

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