Structural highlights
Publication Abstract from PubMed
One of the least understood aspects of prion diseases is the structure of infectious prion protein aggregates. Here we report a high-resolution cryo-EM structure of amyloid fibrils formed by human prion protein with the Y145Stop mutation that is associated with a familial prion disease. This structural insight allows us not only to explain previous biochemical findings, but also provides direct support for the conformational adaptability model of prion transmissibility barriers.
Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.,Li Q, Jaroniec CP, Surewicz WK Nat Struct Mol Biol. 2022 Oct;29(10):962-965. doi: 10.1038/s41594-022-00833-4. , Epub 2022 Sep 12. PMID:36097290[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li Q, Jaroniec CP, Surewicz WK. Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers. Nat Struct Mol Biol. 2022 Oct;29(10):962-965. PMID:36097290 doi:10.1038/s41594-022-00833-4
