scholarly article | Q13442814 |
P2093 | author name string | Teresa J T Pinheiro | |
Dominic Kurian | |||
Sonya Agarwal | |||
Andrew C Gill | |||
Louise Kirby | |||
James F Graham | |||
P2860 | cites work | Selective incorporation of polyanionic molecules into hamster prions | Q24596538 |
Prions | Q24633319 | ||
Recombinant prion protein induces a new transmissible prion disease in wild-type animals | Q24645106 | ||
Formation of native prions from minimal components in vitro | Q24676353 | ||
Chaperone-supervised conversion of prion protein to its protease-resistant form | Q33736997 | ||
Scrapie strains maintain biological phenotypes on propagation in a cell line in culture | Q34080020 | ||
Synthetic mammalian prions | Q34337663 | ||
Aggregation and fibrillization of prions in lipid membranes | Q36008637 | ||
Prions: protein only or something more? Overview of potential prion cofactors | Q36645420 | ||
Prion strain discrimination in cell culture: the cell panel assay | Q36693359 | ||
Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins | Q36919750 | ||
Cell-free propagation of prion strains. | Q36936923 | ||
Amplification of purified prions in vitro | Q37238143 | ||
Prion propagation by Hsp40 molecular chaperones | Q37266697 | ||
Influence of Hsp70s and their regulators on yeast prion propagation | Q37266700 | ||
Synthesis and trafficking of prion proteins in cultured cells | Q37373585 | ||
Design and construction of diverse mammalian prion strains | Q37453512 | ||
Thoughts on mammalian prion strains. | Q37556168 | ||
Structure and function of the molecular chaperone Hsp104 from yeast | Q37600791 | ||
Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein | Q39673524 | ||
Disease-related prion protein forms aggresomes in neuronal cells leading to caspase activation and apoptosis. | Q40374572 | ||
Heparan sulfate is a cellular receptor for purified infectious prions. | Q40466338 | ||
Evidence for synthesis of scrapie prion proteins in the endocytic pathway | Q41608575 | ||
Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast | Q42119762 | ||
Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cells | Q44090721 | ||
Precursor ion scanning for detection and structural characterization of heterogeneous glycopeptide mixtures | Q44152418 | ||
Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization | Q44364889 | ||
Cellular heparan sulfate participates in the metabolism of prions | Q44519369 | ||
Binding of prion proteins to lipid membranes | Q44707244 | ||
Mitochondrial localization of cellular prion protein (PrPC) invokes neuronal apoptosis in aged transgenic mice overexpressing PrPC. | Q45219808 | ||
Strain-dependent differences in beta-sheet conformations of abnormal prion protein | Q45282297 | ||
Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils | Q46318976 | ||
Expression and purification of full-length recombinant PrP of high purity | Q46521631 | ||
In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversion | Q47564542 | ||
Molecular pathology of scrapie-associated fibril protein (PrP) in mouse brain affected by the ME7 strain of scrapie | Q47590720 | ||
Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. | Q47843274 | ||
In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). | Q47845633 | ||
Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein | Q48099698 | ||
Methods for conversion of prion protein into amyloid fibrils | Q48431467 | ||
Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking. | Q51790930 | ||
Protease-resistant prion protein amplification reconstituted with partially purified substrates and synthetic polyanions. | Q51816912 | ||
Cell-free formation of protease-resistant prion protein. | Q53204380 | ||
The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive | Q68318139 | ||
A novel, resistance-linked ovine PrP variant and its equivalent mouse variant modulate the in vitro cell-free conversion of rPrP to PrP(res) | Q79349997 | ||
P4510 | describes a project that uses | ImageQuant | Q112270642 |
P433 | issue | 13 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | prion protein family | Q24724413 |
P304 | page(s) | 9868-9880 | |
P577 | publication date | 2010-01-27 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Low density subcellular fractions enhance disease-specific prion protein misfolding | |
P478 | volume | 285 |
Q41048016 | Complement protein C1q forms a complex with cytotoxic prion protein oligomers |
Q30380548 | Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein. |
Q33977675 | Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties |
Q33967960 | Dissociation of infectivity from seeding ability in prions with alternate docking mechanism |
Q33862576 | In vitro amplification of misfolded prion protein using lysate of cultured cells |
Q24630925 | Is tau ready for admission to the prion club? |
Q34685395 | Monoacylated cellular prion protein modifies cell membranes, inhibits cell signaling, and reduces prion formation |
Q34071628 | Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction. |
Q37256565 | PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions |
Q37791785 | Structural requirements for efficient prion protein conversion: cofactors may promote a conversion-competent structure for PrP(C). |
Q38297159 | The cellular prion protein with a monoacylated glycosylphosphatidylinositol anchor modifies cell membranes, inhibits cell signaling and reduces prion formation |
Q35488786 | The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species |
Search more.