Journal article icon

Journal article

Glycosylation and prion protein.

Abstract:

Recent advances have elucidated the detailed glycosylation of the prion protein and highlighted the size of the sugars, which shield large areas of the protein and confer some conformational stability on the normal cellular form. The reliability of SDS-PAGE banding patterns of different "glycoforms" as a diagnostics tool has been discussed. The possibility exists that the glycans may play a role in the location of the prion protein on the neuronal cell surface. Alternative topologies and teth...

Expand abstract
Publication status:
Published

Actions


Access Document


Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Journal:
Current opinion in structural biology
Volume:
12
Issue:
5
Pages:
578-586
Publication date:
2002-10-01
DOI:
EISSN:
1879-033X
ISSN:
0959-440X
Source identifiers:
99763
Language:
English
Keywords:
Pubs id:
pubs:99763
UUID:
uuid:cfbe0444-ef3b-4a17-b762-8e6ffc4331cc
Local pid:
pubs:99763
Deposit date:
2012-12-19

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP