about
Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's DiseasePrPC Undergoes Basal to Apical Transcytosis in Polarized Epithelial MDCK CellsInhibition of the FKBP family of peptidyl prolyl isomerases induces abortive translocation and degradation of the cellular prion protein.Neuroprotective properties of the PrP-like Shadoo glycoprotein assessed in the middle cerebral artery occlusion model of ischemiaPrion Protein and Stage Specific Embryo Antigen 1 as Selection Markers to Enrich the Fraction of Murine Embryonic Stem Cell-Derived CardiomyocytesRoles of endoproteolytic α-cleavage and shedding of the prion protein in neurodegeneration.The GPI-anchoring of PrP: implications in sorting and pathogenesis.Endoproteolytic processing of the mammalian prion glycoprotein family.Prions amplify through degradation of the VPS10P sorting receptor sortilin.New insights into structural determinants of prion protein folding and stabilityShedding light on prion disease.Biological and biochemical characterization of M2B cells: Classical BSE prion is conserved in transgenic mice overexpressing bovine prion protein gene.Cellular Prion Protein Enhances Drug Resistance of Colorectal Cancer Cells via Regulation of a Survival Signal Pathway.Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein.
P2860
Q26823798-7820F74D-2977-4D00-9CFC-E713C36B2AB0Q27341885-65521D03-A4C3-4998-B1F7-F3C286077DB3Q28254943-36397439-8044-4AE8-86C6-03AC60F3B500Q36070581-96915CAE-8189-4F82-959F-6CF42EF88446Q36716367-31C971CD-B2D3-42CD-928F-56E27E0E30CAQ37135556-F868B0EB-3034-4AD8-9456-CE0E543690A1Q37150756-C39C2C2A-4AA9-4BA1-A082-EF425EC89C46Q38081918-FC5C44A4-30FF-40B0-8A15-3EE2759D5AD0Q38186552-F989CFEF-7D93-4C46-BC21-930C9B52F165Q39052720-97F4F006-1A14-4832-9FC6-071464DF15BAQ40151988-C783E3BD-CA87-4D1A-8295-5170D3462C73Q41445983-F3B5FB24-8366-4CAF-8ACB-5F1F5C309065Q43226637-9AE16B20-A9B9-496E-97DC-0FEE9B9F6F94Q47446061-303BE904-6B7C-48F4-84B7-620A6C17E288Q47931139-50668CFA-FFD1-4F8D-BF05-AFF54769A952Q52602016-75DA63C9-4EFC-4299-BAE1-D2D2197BB918
P2860
description
2012 nî lūn-bûn
@nan
2012 թուականին հրատարակուած գիտական յօդուած
@hyw
2012 թվականին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
α-Cleavage of cellular prion protein
@ast
α-Cleavage of cellular prion protein
@en
α-Cleavage of cellular prion protein
@nl
type
label
α-Cleavage of cellular prion protein
@ast
α-Cleavage of cellular prion protein
@en
α-Cleavage of cellular prion protein
@nl
prefLabel
α-Cleavage of cellular prion protein
@ast
α-Cleavage of cellular prion protein
@en
α-Cleavage of cellular prion protein
@nl
P2860
P921
P356
P1433
P1476
α-Cleavage of cellular prion protein
@en
P2093
Jingjing Liang
Qingzhong Kong
P2860
P304
P356
10.4161/PRI.22511
P407
P577
2012-01-01T00:00:00Z
2012-10-10T00:00:00Z