Low density subcellular fractions enhance disease-specific prion protein misfolding

scientific article

Low density subcellular fractions enhance disease-specific prion protein misfolding is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M109.093484
P932PMC publication ID2843235
P698PubMed publication ID20106973

P2093author name stringTeresa J T Pinheiro
Dominic Kurian
Sonya Agarwal
Andrew C Gill
Louise Kirby
James F Graham
P2860cites workSelective incorporation of polyanionic molecules into hamster prionsQ24596538
PrionsQ24633319
Recombinant prion protein induces a new transmissible prion disease in wild-type animalsQ24645106
Formation of native prions from minimal components in vitroQ24676353
Chaperone-supervised conversion of prion protein to its protease-resistant formQ33736997
Scrapie strains maintain biological phenotypes on propagation in a cell line in cultureQ34080020
Synthetic mammalian prionsQ34337663
Aggregation and fibrillization of prions in lipid membranesQ36008637
Prions: protein only or something more? Overview of potential prion cofactorsQ36645420
Prion strain discrimination in cell culture: the cell panel assayQ36693359
Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteinsQ36919750
Cell-free propagation of prion strains.Q36936923
Amplification of purified prions in vitroQ37238143
Prion propagation by Hsp40 molecular chaperonesQ37266697
Influence of Hsp70s and their regulators on yeast prion propagationQ37266700
Synthesis and trafficking of prion proteins in cultured cellsQ37373585
Design and construction of diverse mammalian prion strainsQ37453512
Thoughts on mammalian prion strains.Q37556168
Structure and function of the molecular chaperone Hsp104 from yeastQ37600791
Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion proteinQ39673524
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 pathwayQ41608575
Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeastQ42119762
Stimulation of PrP(C) retrograde transport toward the endoplasmic reticulum increases accumulation of PrP(Sc) in prion-infected cellsQ44090721
Precursor ion scanning for detection and structural characterization of heterogeneous glycopeptide mixturesQ44152418
Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillizationQ44364889
Cellular heparan sulfate participates in the metabolism of prionsQ44519369
Binding of prion proteins to lipid membranesQ44707244
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 proteinQ45282297
Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrilsQ46318976
Expression and purification of full-length recombinant PrP of high purityQ46521631
In vitro cell-free conversion of bacterial recombinant PrP to PrPres as a model for conversionQ47564542
Molecular pathology of scrapie-associated fibril protein (PrP) in mouse brain affected by the ME7 strain of scrapieQ47590720
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 proteinQ48099698
Methods for conversion of prion protein into amyloid fibrilsQ48431467
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-sensitiveQ68318139
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
P4510describes a project that usesImageQuantQ112270642
P433issue13
P407language of work or nameEnglishQ1860
P921main subjectprion protein familyQ24724413
P304page(s)9868-9880
P577publication date2010-01-27
P1433published inJournal of Biological ChemistryQ867727
P1476titleLow density subcellular fractions enhance disease-specific prion protein misfolding
P478volume285

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cites work (P2860)
Q41048016Complement protein C1q forms a complex with cytotoxic prion protein oligomers
Q30380548Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein.
Q33977675Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties
Q33967960Dissociation of infectivity from seeding ability in prions with alternate docking mechanism
Q33862576In vitro amplification of misfolded prion protein using lysate of cultured cells
Q24630925Is tau ready for admission to the prion club?
Q34685395Monoacylated cellular prion protein modifies cell membranes, inhibits cell signaling, and reduces prion formation
Q34071628Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.
Q37256565PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions
Q37791785Structural requirements for efficient prion protein conversion: cofactors may promote a conversion-competent structure for PrP(C).
Q38297159The cellular prion protein with a monoacylated glycosylphosphatidylinositol anchor modifies cell membranes, inhibits cell signaling and reduces prion formation
Q35488786The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species

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