Radical changes in beta-amyloid form and function.

Published

Journal Article (Review)

A growing body of evidence supports the nucleation hypothesis of fibrillar amyloid formation. In this article, it is hypothesized that the fibrils formed with human A beta, rodent A beta, and a mixture of the two peptides may form nearly identical physical structures with clearly different biological activities. Data is reported supporting the concept that a specific "strain" of nucleation seed could impart a new structure on a growing amyloid fibril, thereby changing its biological activity. The data that the biological activities of specific prion strains have a basis in strain-specific structure have been supported experimentally.

Full Text

Duke Authors

Cited Authors

  • Vitek, MP

Published Date

  • May 1996

Published In

Volume / Issue

  • 28 / 1-3

Start / End Page

  • 49 - 55

PubMed ID

  • 8871941

Pubmed Central ID

  • 8871941

International Standard Serial Number (ISSN)

  • 1044-7393

Digital Object Identifier (DOI)

  • 10.1007/BF02815204

Language

  • eng

Conference Location

  • United States