Gerstmann-Sträussler-Scheinker disease revisited: accumulation of covalently-linked multimers of internal prion protein fragments.
Aggregate formation
Creutzfeldt-Jakob disease
Epitope mapping
Mass spectrometry
Multimers
Prion protein
Journal
Acta neuropathologica communications
ISSN: 2051-5960
Titre abrégé: Acta Neuropathol Commun
Pays: England
ID NLM: 101610673
Informations de publication
Date de publication:
29 05 2019
29 05 2019
Historique:
received:
22
04
2019
accepted:
09
05
2019
entrez:
31
5
2019
pubmed:
31
5
2019
medline:
22
4
2020
Statut:
epublish
Résumé
Despite their phenotypic heterogeneity, most human prion diseases belong to two broadly defined groups: Creutzfeldt-Jakob disease (CJD) and Gerstmann-Sträussler-Scheinker disease (GSS). While the structural characteristics of the disease-related proteinase K-resistant prion protein (resPrP
Identifiants
pubmed: 31142381
doi: 10.1186/s40478-019-0734-2
pii: 10.1186/s40478-019-0734-2
pmc: PMC6540574
doi:
Substances chimiques
PrPSc Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
85Subventions
Organisme : NIA NIH HHS
ID : P30 AG010133
Pays : United States
Organisme : NIAID NIH HHS
ID : P01 AI077774
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS083687
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS103848
Pays : United States
Organisme : NIAID NIH HHS
ID : P01 AI106705
Pays : United States
Commentaires et corrections
Type : ErratumIn
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