Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination.
Creutzfeldt-Jakob disease
N-linked glycosylation
PRC7
bovine spongiform encephalopathy
chronic wasting disease
monoclonal antibody
neurodegeneration
prion
prion disease
prion strains
prions
protein misfolding
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
24 07 2020
24 07 2020
Historique:
received:
24
01
2020
revised:
31
05
2020
pubmed:
10
6
2020
medline:
14
1
2021
entrez:
10
6
2020
Statut:
ppublish
Résumé
The causative factors underlying conformational conversion of cellular prion protein (PrP
Identifiants
pubmed: 32513872
pii: S0021-9258(17)50147-7
doi: 10.1074/jbc.RA120.012796
pmc: PMC7383396
doi:
Substances chimiques
Antibodies, Monoclonal, Murine-Derived
0
Epitopes
0
PrPC Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
10420-10433Subventions
Organisme : NINDS NIH HHS
ID : R01 NS121682
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS103763
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS040334
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS109376
Pays : United States
Organisme : NIAID NIH HHS
ID : P01 AI077774
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS052609
Pays : United States
Informations de copyright
© 2020 Kang et al.
Déclaration de conflit d'intérêts
Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.
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