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Titel:

Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections.

Dokumenttyp:
Journal Article; Article
Autor(en):
Neuendorf, E; Weber, A; Saalmueller, A; Schätzl, H; Reifenberg, K; Pfaff, E; Groschup, MH
Abstract:
The conversion into abnormally folded prion protein (PrP) plays a key role in prion diseases. PrP(C) carries two N-linked glycan chains at amino acid residues 180 and 196 (mouse). Previous in vitro data indicated that the conversion process may not require glycosylation of PrP. However, it is conceivable that these glycans function as intermolecular binding sites during the de novo infection of cells on susceptible organisms and/or play a role for the interaction of both PrP isoforms. Such recep...     »
Zeitschriftentitel:
J Biol Chem
Jahr:
2004
Band / Volume:
279
Heft / Issue:
51
Seitenangaben Beitrag:
53306-16
Sprache:
eng
Volltext / DOI:
doi:10.1074/jbc.M410796200
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/15448157
Print-ISSN:
0021-9258
TUM Einrichtung:
Institut für Virologie
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