Molecular location of a species-specific epitope on the hamster scrapie agent protein.
about
Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteinsPrion uptake in the gut: identification of the first uptake and replication sitesGlycosylation influences cross-species formation of protease-resistant prion protein.The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.Bax deletion prevents neuronal loss but not neurological symptoms in a transgenic model of inherited prion disease.A novel, drug-based, cellular assay for the activity of neurotoxic mutants of the prion protein.PrP conformational transitions alter species preference of a PrP-specific antibody.Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155.Deletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform.Similar signature of the prion protein in natural sheep scrapie and bovine spongiform encephalopathy-linked diseases.Neurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cellsSpecies specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrierAn N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity.Fatal familial insomnia and familial Creutzfeldt-Jakob disease: different prion proteins determined by a DNA polymorphism.Preparation and characterization of antibodies against mouse prion protein (PrP) peptides.The extracellular regulated kinase-1 (ERK1) controls regulated alpha-secretase-mediated processing, promoter transactivation, and mRNA levels of the cellular prion protein.A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum.Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues.A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells.Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies.Using small molecule reagents to selectively modify epitopes based on their conformation.Purification and properties of the cellular prion protein from Syrian hamster brain.Inhibition of protease-resistant prion protein formation by porphyrins and phthalocyaninesHeterologous PrP molecules interfere with accumulation of protease-resistant PrP in scrapie-infected murine neuroblastoma cellsAblation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies.GFP-tagged mutant prion protein forms intra-axonal aggregates in transgenic miceAccumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation.Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent.Lack of prion infectivity in fixed heart tissue from patients with Creutzfeldt-Jakob disease or amyloid heart disease.Prion protein with an insertional mutation accumulates on axonal and dendritic plasmalemma and is associated with distinctive ultrastructural changes.Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform.Modifiers of prion protein biogenesis and recycling identified by a highly parallel endocytosis kinetics assay.An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy.Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state.Prion protein lacks robust cytoprotective activity in cultured cells.
P2860
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P2860
Molecular location of a species-specific epitope on the hamster scrapie agent protein.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Molecular location of a species-specific epitope on the hamster scrapie agent protein.
@ast
Molecular location of a species-specific epitope on the hamster scrapie agent protein.
@en
type
label
Molecular location of a species-specific epitope on the hamster scrapie agent protein.
@ast
Molecular location of a species-specific epitope on the hamster scrapie agent protein.
@en
prefLabel
Molecular location of a species-specific epitope on the hamster scrapie agent protein.
@ast
Molecular location of a species-specific epitope on the hamster scrapie agent protein.
@en
P2093
P2860
P1433
P1476
Molecular location of a species-specific epitope on the hamster scrapie agent protein.
@en
P2093
D C Bolton
G Bablanian
P E Bendheim
R J Kascsak
S J Seligman
P2860
P304
P407
P577
1991-07-01T00:00:00Z