Glycosylation differences between the normal and pathogenic prion protein isoforms

Proceedings of the National Academy of Sciences of the United States of America

Volumn 96, Issue 23, 1999, Pages 13044-13049

  Rudd, Pauline M ^a   Endo, Tama ^b   Colominas, Cristina ^a   Groth, Darlene ^c   Wheeler, Susan F ^a   Harvey, David J ^a   Wormald, Mark R ^a   Serban, Hana ^c   Prusiner, Stanley B ^c   Kobata, Akira ^b   Dwek, Raymond A ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b TOKYO METROPOLITAN INSTITUTE OF GERONTOLOGY   (Japan)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

N acetylglucosaminyltransferase III scrapie

Indexed keywords

N ACETYLGLUCOSAMINYLTRANSFERASE; PRION PROTEIN;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN GLYCOSYLATION; PROTEIN PROCESSING; PROTEIN STRUCTURE; SIALYLATION; SYRIAN HAMSTER;

ANIMALS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CRICETINAE; GLYCOSYLATION; MESOCRICETUS; MODELS, MOLECULAR; PROTEIN ISOFORMS; PRP 27-30 PROTEIN; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ANIMALIA; CRICETINAE; MESOCRICETUS AURATUS;

EID: 0344239773     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.96.23.13044     Document Type: Article

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