Proteomics

Dataset Information

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GPI-glycan structures of human Prion from knock-in mice_LC-MSMS


ABSTRACT: To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins isolated from knock-in mice those express human prion protein instead of mouse one.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Brain

SUBMITTER: Tetsuya Hirata  

LAB HEAD: Taroh Kinoshita

PROVIDER: PXD017655 | Pride | 2020-04-22

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
181019_Prion_trp_WT_Hilic_HilicTip_8u.mgf Mgf
181019_Prion_trp_WT_Hilic_HilicTip_8u.pride.mgf.gz Mgf
181019_Prion_trp_WT_Hilic_HilicTip_8u.raw Raw
F067969.dat Other
F067969.mzid.pride.mztab.gz Mztab
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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.

Kobayashi Atsushi A   Hirata Tetsuya T   Nishikaze Takashi T   Ninomiya Akinori A   Maki Yuta Y   Takada Yoko Y   Kitamoto Tetsuyuki T   Kinoshita Taroh T  

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]

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