Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections.
Neuendorf
Erdmute
E
Institute for Novel and Emerging Infectious Diseases, Federal Research Centre for Virus Diseases of Animals, 17943 Greifswald, Isle of Riems, Germany.
Weber
Artur
A
Saalmueller
Armin
A
Schatzl
Hermann
H
Reifenberg
Kurt
K
Pfaff
Eberhardt
E
Groschup
Martin Hermann
MH
D000818:Animals; D001665:Binding Sites; D019921:Biotinylation; D015153:Blotting, Western; D001921:Brain / Q000473:pathology; D016466:CHO Cells; D002417:Cattle; D002460:Cell Line; D045744:Cell Line, Tumor; D002469:Cell Separation; D003001:Cloning, Molecular; D006224:Cricetinae; D004220:Disulfides / Q000737:chemistry; D016643:Encephalopathy, Bovine Spongiform / Q000378:metabolism*; D005434:Flow Cytometry; D006031:Glycosylation; D047468:Immunoprecipitation; D051379:Mice; D008810:Mice, Inbred C57BL; D008822:Mice, Transgenic; D009154:Mutation; D011134:Polysaccharides / Q000737:chemistry*; D017096:Prion Diseases / Q000378:metabolism; D011328:Prions / Q000737:chemistry*; D020033:Protein Isoforms; D012608:Scrapie / Q000378:metabolism*; D019076:Transgenes
D004220:Disulfides; D011134:Polysaccharides; D011328:Prions; D020033:Protein Isoforms