Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation
Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation
About this item
Full title
Author / Creator
Lau, Agnes , McDonald, Alex , Daude, Nathalie , Mays, Charles E , Walter, Eric D , Aglietti, Robin , Mercer, Robert CC , Wohlgemuth, Serene , van der Merwe, Jacques , Yang, Jing , Gapeshina, Hristina , Kim, Chae , Grams, Jennifer , Shi, Beipei , Wille, Holger , Balachandran, Aru , Schmitt‐Ulms, Gerold , Safar, Jiri G , Millhauser, Glenn L and Westaway, David
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
The cellular prion protein (PrP
C
) comprises a natively unstructured N‐terminal domain, including a metal‐binding octarepeat region (OR) and a linker, followed by a C‐terminal domain that misfolds to form PrP
S
c
in Creutzfeldt‐Jakob disease. PrP
C
β‐endoproteolysis to the C2 fragment allows PrP
S
c
formation, while α...
Alternative Titles
Full title
Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation
Authors, Artists and Contributors
Author / Creator
McDonald, Alex
Daude, Nathalie
Mays, Charles E
Walter, Eric D
Aglietti, Robin
Mercer, Robert CC
Wohlgemuth, Serene
van der Merwe, Jacques
Yang, Jing
Gapeshina, Hristina
Kim, Chae
Grams, Jennifer
Shi, Beipei
Wille, Holger
Balachandran, Aru
Schmitt‐Ulms, Gerold
Safar, Jiri G
Millhauser, Glenn L
Westaway, David
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_5e77529f4279415d8aa0b5975d382b3d
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_5e77529f4279415d8aa0b5975d382b3d
Other Identifiers
ISSN
1757-4676
E-ISSN
1757-4684
DOI
10.15252/emmm.201404588
