Abstract
Background: Despite structural reorganization during disease, conformational prion protein epitopes remain undefined. Results: We identify specific amino acids constituting novel conformational monoclonal antibody epitopes. Conclusion: Immunoreactivities of globular domain epitopes depend on maintenance of regional tertiary structure. Significance: Our studies address how denatured conformational epitopes remain functional, provide insights into normal and disease-related prion protein, and expand epitope tagging options.
Original language | English (US) |
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Pages (from-to) | 37219-37232 |
Number of pages | 14 |
Journal | Journal of Biological Chemistry |
Volume | 287 |
Issue number | 44 |
DOIs | |
State | Published - Oct 26 2012 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology