about
Large-scale approaches for glycobiology.Multifaceted Role of Sialylation in Prion DiseasesThe diverse roles of mononuclear phagocytes in prion disease pathogenesisSialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivityMapping of possible prion protein self-interaction domains using peptide arraysThe intriguing prion disorders.Prions on the move.Sialylation of the prion protein glycans controls prion replication rate and glycoform ratioThe prion protein preference of sporadic Creutzfeldt-Jakob disease subtypes.Prion strain discrimination in cell culture: the cell panel assayThe Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling ModulesPrion protein self-interaction in prion disease therapy approaches.Altered prion protein glycosylation in the aging mouse brain.N-glycoprotein macroheterogeneity: biological implications and proteomic characterization.Prion protein "gamma-cleavage": characterizing a novel endoproteolytic processing event.Cerebellar compartmentation of prion pathogenesis.Lysosomal Quality Control in Prion Diseases.Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.A New Approach for Detection Improvement of the Creutzfeldt-Jakob Disorder through a Specific Surface Chemistry Applied onto Titration Well.Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion.Evidence for distinct chronic wasting disease (CWD) strains in experimental CWD in ferrets.Increased proportions of C1 truncated prion protein protect against cellular M1000 prion infection.Structural conservation of prion strain specificities in recombinant prion protein fibrils in real-time quaking-induced conversion.Investigation of the effect of glycosylation on human prion protein by molecular dynamics.Analysis of Cellular Prion Protein Endoproteolytic Processing.Identification of new molecular alterations in fatal familial insomnia.Glycosylation Significantly Inhibits the Aggregation of Human Prion Protein and Decreases Its Cytotoxicity
P2860
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P2860
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Prion protein glycosylation.
@ast
Prion protein glycosylation.
@en
type
label
Prion protein glycosylation.
@ast
Prion protein glycosylation.
@en
prefLabel
Prion protein glycosylation.
@ast
Prion protein glycosylation.
@en
P2860
P1476
Prion protein glycosylation
@en
P2093
Colin L Masters
Steven J Collins
P2860
P304
P356
10.1111/J.1471-4159.2005.03104.X
P407
P577
2005-05-01T00:00:00Z