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Updated: May 24, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
The amyloid state of proteins in human diseases
David Eisenberg1, Mathias Jucker
1Howard 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.
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