Structural and molecular basis of cross-seeding barriers in amyloids.
amyloid
cross-seeding
nuclear magnetic resonance
prion
sequence to fold
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
05 01 2021
05 01 2021
Historique:
entrez:
14
1
2021
pubmed:
15
1
2021
medline:
15
5
2021
Statut:
ppublish
Résumé
Neurodegenerative disorders are frequently associated with β-sheet-rich amyloid deposits. Amyloid-forming proteins can aggregate under different structural conformations known as strains, which can exhibit a prion-like behavior and distinct pathophenotypes. Precise molecular determinants defining strain specificity and cross-strain interactions (cross-seeding) are currently unknown. The HET-s prion protein from the fungus
Identifiants
pubmed: 33443172
pii: 2014085118
doi: 10.1073/pnas.2014085118
pmc: PMC7817211
pii:
doi:
Substances chimiques
Amyloid
0
Amyloidogenic Proteins
0
Fungal Proteins
0
HET-S protein, Podospora anserina
0
Prions
0
Protein Aggregates
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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