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
APA
Chicago
ICMJE
MLA
NLM
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