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Radical changes in beta-amyloid form and function.

Publication ,  Journal Article
Vitek, MP
Published in: Mol Chem Neuropathol
1996

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.

Duke Scholars

Published In

Mol Chem Neuropathol

DOI

ISSN

1044-7393

Publication Date

1996

Volume

28

Issue

1-3

Start / End Page

49 / 55

Location

United States

Related Subject Headings

  • Sequence Homology, Amino Acid
  • Rodentia
  • Protein Structure, Secondary
  • Prions
  • Neurology & Neurosurgery
  • Molecular Sequence Data
  • Humans
  • Glycation End Products, Advanced
  • Animals
  • Amyloid beta-Peptides
 

Citation

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MLA
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Vitek, M. P. (1996). Radical changes in beta-amyloid form and function. Mol Chem Neuropathol, 28(1–3), 49–55. https://doi.org/10.1007/BF02815204
Vitek, M. P. “Radical changes in beta-amyloid form and function.Mol Chem Neuropathol 28, no. 1–3 (1996): 49–55. https://doi.org/10.1007/BF02815204.
Vitek MP. Radical changes in beta-amyloid form and function. Mol Chem Neuropathol. 1996;28(1–3):49–55.
Vitek, M. P. “Radical changes in beta-amyloid form and function.Mol Chem Neuropathol, vol. 28, no. 1–3, 1996, pp. 49–55. Pubmed, doi:10.1007/BF02815204.
Vitek MP. Radical changes in beta-amyloid form and function. Mol Chem Neuropathol. 1996;28(1–3):49–55.

Published In

Mol Chem Neuropathol

DOI

ISSN

1044-7393

Publication Date

1996

Volume

28

Issue

1-3

Start / End Page

49 / 55

Location

United States

Related Subject Headings

  • Sequence Homology, Amino Acid
  • Rodentia
  • Protein Structure, Secondary
  • Prions
  • Neurology & Neurosurgery
  • Molecular Sequence Data
  • Humans
  • Glycation End Products, Advanced
  • Animals
  • Amyloid beta-Peptides