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Analysis of carboxy-terminal peptides derived from endoproteinase Lys-C digests of the scrapie isoform of the hamster prion protein revealed that the majority of the molecules are glycoinositol phospholipid linked through ethanolamine attached at serin-231. However, approximately 15% of PrPSc had a carboxy-terminal peptide that ends at glycine-228. It is intriguing that this glycine is part of the PrP sequence Gly-Arg-Arg, which is an established target sequence for the proteolysis and release of bioactive peptides from larger precursors. The mechanism of formation, as well as the role of the truncated carboxy terminus in the dissemination and neuropathology of scrapie, remains to be determined.
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
August 1993,
Glycobiology,
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
March 2015,
Biophysical journal,
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
August 1995,
The Journal of biological chemistry,
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
May 1997,
Proceedings of the National Academy of Sciences of the United States of America,
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
January 1985,
Nature,
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
January 2016,
Prion,
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
June 1990,
Biochemistry,
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
December 1982,
Science (New York, N.Y.),
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
January 2015,
Prion,
N Stahl, and
M A Baldwin, and
A L Burlingame, and
S B Prusiner
January 1989,
Methods in cell biology,
