Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.
glycosylphosphatidylinositol (GPI) anchor
membrane interaction
prion protein (PrP)
protein semisynthesis
Journal
Journal of peptide science : an official publication of the European Peptide Society
ISSN: 1099-1387
Titre abrégé: J Pept Sci
Pays: England
ID NLM: 9506309
Informations de publication
Date de publication:
Oct 2019
Oct 2019
Historique:
received:
01
08
2019
revised:
23
08
2019
accepted:
23
08
2019
entrez:
13
11
2019
pubmed:
13
11
2019
medline:
3
4
2020
Statut:
ppublish
Résumé
Deciphering the pathophysiologic events in prion diseases is challenging, and the role of posttranslational modifications (PTMs) such as glypidation and glycosylation remains elusive due to the lack of homogeneous protein preparations. So far, experimental studies have been limited in directly analyzing the earliest events of the conformational change of cellular prion protein (PrP
Identifiants
pubmed: 31713950
doi: 10.1002/psc.3216
pmc: PMC6899880
doi:
Substances chimiques
PrPC Proteins
0
PrPSc Proteins
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3216Subventions
Organisme : Wien Kultur
Informations de copyright
© 2019 The Authors. Journal of Peptide Science published by European Peptide Society and John Wiley & Sons Ltd.
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