A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells.
about
Glycosylation influences cross-species formation of protease-resistant prion protein.Specific biarsenical labeling of cell surface proteins allows fluorescent- and biotin-tagging of amyloid precursor protein and prion proteins.New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products.Clearance and prevention of prion infection in cell culture by anti-PrP antibodies.Mapping of possible prion protein self-interaction domains using peptide arraysPrion protein amino acid determinants of differential susceptibility and molecular feature of prion strains in mice and volesBank Vole Prion Protein As an Apparently Universal Substrate for RT-QuIC-Based Detection and Discrimination of Prion StrainsCellular biology of prion diseases.Prion diseases and their biochemical mechanisms.A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence.Identification of two prion protein regions that modify scrapie incubation time.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.A molecular switch controls interspecies prion disease transmission in mice.Strain specific resistance to murine scrapie associated with a naturally occurring human prion protein polymorphism at residue 171.Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation.Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie.Influence of Mabs on PrP(Sc) formation using in vitro and cell-free systemsMultiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoformIncreased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion proteinEvidence for the role of PrP(C) helix 1 in the hydrophilic seeding of prion aggregates.Interactions between heterologous forms of prion protein: binding, inhibition of conversion, and species barriersThe Distribution of Prion Protein Allotypes Differs Between Sporadic and Iatrogenic Creutzfeldt-Jakob Disease PatientsMouse prion protein (PrP) segment 100 to 104 regulates conversion of PrP(C) to PrP(Sc) in prion-infected neuroblastoma cells.Integrity of helix 2-helix 3 domain of the PrP protein is not mandatory for prion replication.Structure of the β2-α2 loop and interspecies prion transmissionPrion protein NMR structure and familial human spongiform encephalopathies.Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation.Prion protein NMR structure and species barrier for prion diseasesMotif-grafted antibodies containing the replicative interface of cellular PrP are specific for PrPScScrapie susceptibility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms.How do amino acid substitutions affect the amyloidogenic properties and seeding efficiency of prion peptidesPrion protein misfolding and disease.Prion transmission prevented by modifying the β2-α2 loop structure of host PrPCCaprine PrP variants harboring Asp-146, His-154 and Gln-211 alleles display reduced convertibility upon interaction with pathogenic murine prion protein in scrapie infected cells.Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein.Identifying key components of the PrPC-PrPSc replicative interface.Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting diseaseIn Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.
P2860
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P2860
A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
A single hamster PrP amino aci ...... ted mouse neuroblastoma cells.
@ast
A single hamster PrP amino aci ...... ted mouse neuroblastoma cells.
@en
type
label
A single hamster PrP amino aci ...... ted mouse neuroblastoma cells.
@ast
A single hamster PrP amino aci ...... ted mouse neuroblastoma cells.
@en
prefLabel
A single hamster PrP amino aci ...... ted mouse neuroblastoma cells.
@ast
A single hamster PrP amino aci ...... ted mouse neuroblastoma cells.
@en
P2860
P1433
P1476
A single hamster PrP amino aci ...... cted mouse neuroblastoma cells
@en
P2093
P2860
P304
P407
P577
1995-12-01T00:00:00Z