Dataset Information
GPI-glycan structures of human Prion from a human brain
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Velos
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Brain
SUBMITTER: 
Tetsuya Hirata
LAB HEAD: Taroh Kinoshita
PROVIDER: PXD017656 | Pride | 2020-04-22
REPOSITORIES: Pride
Dataset's files
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Publications
α2,3 linkage of sialic acid to a GPI anchor and an unpredicted GPI attachment site in human prion protein.
The Journal of biological chemistry 20200422 22
Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrP<sup>Sc</sup>) after conversion of the cellular prion protein (PrP<sup>C</sup>). The glycosylphosphatidylinositol (GPI) anchor of PrP<sup>C</sup> is involved in prion disease pathogenesis, and especially sialic acid in a GPI side chain reportedly affects PrP<sup>C</sup> conversion. Thus, it is important to define the location and structure of the GPI ...[more]