An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity.
about
Amyloid beta precursor protein and prion protein have a conserved interaction affecting cell adhesion and CNS developmentMultifaceted Role of Sialylation in Prion DiseasesActivation of zebrafish Src family kinases by the prion protein is an amyloid-β-sensitive signal that prevents the endocytosis and degradation of E-cadherin/β-catenin complexes in vivo.The prion protein modulates A-type K+ currents mediated by Kv4.2 complexes through dipeptidyl aminopeptidase-like protein 6The N-terminus of the prion protein is a toxic effector regulated by the C-terminus.The N-terminal, polybasic region is critical for prion protein neuroprotective activity.The toxicity of a mutant prion protein is cell-autonomous, and can be suppressed by wild-type prion protein on adjacent cells.A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes.Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesionThe elusive role of the prion protein and the mechanism of toxicity in prion disease.A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation.Prion protein at the crossroads of physiology and disease.Ion channels induced by the prion protein: mediators of neurotoxicity.A Neuronal Culture System to Detect Prion Synaptotoxicity.The N-terminal, polybasic region of PrP(C) dictates the efficiency of prion propagation by binding to PrP(Sc).A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein.Expression of the Prion Protein Family Member Shadoo Causes Drug Hypersensitivity That Is Diminished by the Coexpression of the Wild Type Prion Protein.A mutant prion protein sensitizes neurons to glutamate-induced excitotoxicityThe prion protein family member Shadoo induces spontaneous ionic currents in cultured cells.Prion propagation, toxicity and degradation.An antipsychotic drug exerts anti-prion effects by altering the localization of the cellular prion protein.Identification of Anti-prion Compounds using a Novel Cellular Assay.A nine amino acid domain is essential for mutant prion protein toxicity.Domain-Specific Activation of Death-Associated Intracellular Signalling Cascades by the Cellular Prion Protein in Neuroblastoma Cells.Fate of pathological prion (PrP(sc)92-138) in soil and water: prion-clay nanoparticle molecular dynamics.Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2.An inter-domain regulatory mechanism controls toxic activities of PrPC.
P2860
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P2860
An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@ast
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@en
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@nl
type
label
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@ast
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@en
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@nl
prefLabel
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@ast
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@en
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@nl
P2093
P2860
P356
P1476
An N-terminal polybasic domain ...... mutant prion protein toxicity.
@en
P2093
David A Harris
Emiliano Biasini
Isaac H Solomon
James E Huettner
Natasha Khatri
Tania Massignan
P2860
P304
14724-14736
P356
10.1074/JBC.M110.214973
P407
P577
2011-03-08T00:00:00Z