Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
about
Glypican-1 mediates both prion protein lipid raft association and disease isoform formationHeparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seedsCellular aspects of prion replication in vitroPrion-like properties of Tau protein: the importance of extracellular Tau as a therapeutic targetIdentification of a gene regulatory network associated with prion replication.Live imaging of prions reveals nascent PrPSc in cell-surface, raft-associated amyloid strings and websRecent advances in prion chemotherapeutics.Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPres level disparity.Modulation of Glycosaminoglycans Affects PrPSc Metabolism but Does Not Block PrPSc Uptake.PrPc does not mediate internalization of PrPSc but is required at an early stage for de novo prion infection of Rov cells.Susceptibility of cell substrates to PrPSc infection and safety control measures related to biological and biotherapeutical products.Glypican-1 facilitates prion conversion in lipid rafts.Manipulating the extracellular matrix and its role in brain and spinal cord plasticity and repair.Prion strains depend on different endocytic routes for productive infection.Protein aggregates stimulate macropinocytosis facilitating their propagationInternalization, axonal transport and release of fibrillar forms of alpha-synuclein.Sulfated glycosaminoglycans in protein aggregation diseases.Prophylactic effect of dietary seaweed Fucoidan against enteral prion infection.Copper-dependent co-internalization of the prion protein and glypican-1.Glycosylation-related gene expression in prion diseases: PrPSc accumulation in scrapie infected GT1 cells depends on beta-1,4-linked GalNAc-4-SO4 hyposulfation.Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapie-associated fibrils.PrPSc incorporation to cells requires endogenous glycosaminoglycan expression.Vertebrate food products as a potential source of prion-like α-synuclein.Copaxone interferes with the PrP Sc-GAG interaction.
P2860
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P2860
Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
@ast
Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
@en
type
label
Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
@ast
Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
@en
prefLabel
Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
@ast
Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
@en
P2093
P1476
Novel heparan mimetics potently inhibit the scrapie prion protein and its endocytosis.
@en
P2093
Albert Taraboulos
Denis Barritault
Dulce Papy-Garcia
Lior Horonchik
Oshrat Schonberger
Ruth Gabizon
P304
P356
10.1016/J.BBRC.2003.10.150
P407
P577
2003-12-01T00:00:00Z