scholarly article | Q13442814 |
P2093 | author name string | Surachai Supattapone | |
P2860 | cites work | Non-genetic propagation of strain-specific properties of scrapie prion protein. | Q54170124 |
Infectivity versus Seeding in Neurodegenerative Diseases Sharing a Prion-Like Mechanism | Q21284823 | ||
Selective incorporation of polyanionic molecules into hamster prions | Q24596538 | ||
Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids | Q24614859 | ||
Generating a prion with bacterially expressed recombinant prion protein | Q24626352 | ||
Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions | Q24632206 | ||
Prions | Q24633319 | ||
Formation of native prions from minimal components in vitro | Q24676353 | ||
Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor | Q27316451 | ||
De novo generation of infectious prions in vitro produces a new disease phenotype | Q27317045 | ||
The dominant-negative effect of the Q218K variant of the prion protein does not require protein X. | Q30493219 | ||
Attempts to convert the cellular prion protein into the scrapie isoform in cell-free systems | Q33719644 | ||
Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein | Q33803953 | ||
Iatrogenic Creutzfeldt-Jakob disease at the millennium. | Q33924749 | ||
Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding | Q34084209 | ||
Dominant-negative inhibition of prion replication in transgenic mice | Q34191612 | ||
Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein | Q34294957 | ||
Species specificity in the cell-free conversion of prion protein to protease-resistant forms: a model for the scrapie species barrier | Q34393434 | ||
In vitro generation of infectious scrapie prions. | Q34413661 | ||
Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro | Q34491356 | ||
Conversion of bacterially expressed recombinant prion protein | Q34629119 | ||
Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation | Q36581272 | ||
Cell-free propagation of prion strains. | Q36936923 | ||
Changes in prion replication environment cause prion strain mutation | Q37118769 | ||
Prion protein glycosylation is not required for strain-specific neurotropism. | Q37191812 | ||
Strain-specific role of RNAs in prion replication | Q38457828 | ||
Scrapie strain variation and mutation | Q40729976 | ||
Prion strains | Q40954190 | ||
In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups | Q44393768 | ||
In vitro prion protein conversion in detergent-solubilized membranes | Q44781715 | ||
Human spongiform encephalopathy: the National Institutes of Health series of 300 cases of experimentally transmitted disease | Q48126727 | ||
The stoichiometry of host PrPC glycoforms modulates the efficiency of PrPSc formation in vitro. | Q51802051 | ||
Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. | Q51816912 | ||
Cell-free formation of protease-resistant prion protein. | Q53204380 | ||
P433 | issue | 1 | |
P921 | main subject | prion protein family | Q24724413 |
P304 | page(s) | 100-105 | |
P577 | publication date | 2014-01-01 | |
P1433 | published in | Prion | Q26842757 |
P1476 | title | Elucidating the role of cofactors in mammalian prion propagation | |
P478 | volume | 8 |
Q36143652 | Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice |
Q92150816 | Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Terminal Domain, a Review |
Q61817665 | Neuroinflammation, Microglia, and Cell-Association during Prion Disease |
Q30399619 | Post-translational modifications in PrP expand the conformational diversity of prions in vivo |
Q35979953 | Prion Strain Differences in Accumulation of PrPSc on Neurons and Glia Are Associated with Similar Expression Profiles of Neuroinflammatory Genes: Comparison of Three Prion Strains |
Q26827209 | Prion strains and amyloid polymorphism influence phenotypic variation |
Q39097864 | Protein aggregation, misfolding and consequential human neurodegenerative diseases. |
Q91705222 | Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases |
Q47294251 | Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies. |
Q43226637 | Shedding light on prion disease. |
Q26795754 | Techniques to elucidate the conformation of prions |
Q39004351 | The activities of amyloids from a structural perspective |
Q38718288 | Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo. |
Q38288126 | Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids |
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