Altered prion protein glycosylation in the aging mouse brain.
about
Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivitySpecies and strain glycosylation patterns of PrPScSimultaneous characterization of glyco- and phosphoproteomes of mouse brain membrane proteome with electrostatic repulsion hydrophilic interaction chromatographyGene regulatory network analysis supports inflammation as a key neurodegeneration process in prion disease.Epigenetic control of agingPrion protein expression and functional importance in skeletal muscle.Developmental expression of the cellular prion protein (PrP(C) ) in bovine embryos.Prion strain discrimination in cell culture: the cell panel assaySelective vulnerability to neurodegenerative disease: the curious case of Prion Protein.The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling ModulesPrion protein and aging.Normal cellular prion protein is a ligand of selectins: binding requires Le(X) but is inhibited by sLe(X).Glycomic and Proteomic Changes in Aging Brain Nigrostriatal Pathway
P2860
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P2860
Altered prion protein glycosylation in the aging mouse brain.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Altered prion protein glycosylation in the aging mouse brain.
@en
type
label
Altered prion protein glycosylation in the aging mouse brain.
@en
prefLabel
Altered prion protein glycosylation in the aging mouse brain.
@en
P2093
P2860
P1476
Altered prion protein glycosylation in the aging mouse brain.
@en
P2093
Angeline Xi-Hua Goh
Boon-Seng Wong
Chaoyang Li
Man-Sun Sy
P2860
P304
P356
10.1111/J.1471-4159.2006.04268.X
P407
P577
2006-11-27T00:00:00Z