Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.
Amyloidogenic proteins associated with a variety of unrelated diseases are typically capable of forming several distinct self-templating conformers. In prion diseases, these different structures, called prion strains (or variants), confer dramatic variation in disease pathology and transmission. Agg...
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| Main Authors: | , |
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| Format: | article |
| Language: | EN |
| Published: |
Public Library of Science (PLoS)
2014
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| Subjects: | |
| Online Access: | https://doaj.org/article/4ed89be211c245d1ab6bca0bc7f81b76 |
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