about
Prion hypothesis: the end of the controversy?Generating a prion with bacterially expressed recombinant prion protein.Cofactor molecules maintain infectious conformation and restrict strain properties in purified prionsCalcineurin inhibition at the clinical phase of prion disease reduces neurodegeneration, improves behavioral alterations and increases animal survivalThe physical relationship between infectivity and prion protein aggregates is strain-dependentDe novo generation of infectious prions in vitro produces a new disease phenotypeUltra-efficient PrP(Sc) amplification highlights potentialities and pitfalls of PMCA technologyCharge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Preclinical detection of variant CJD and BSE prions in blood.Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease.Human prion protein sequence elements impede cross-species chronic wasting disease transmission.Prion formation, but not clearance, is supported by protein misfolding cyclic amplification.High-resolution structure of infectious prion protein: the final frontierProtein misfolding cyclic amplification of infectious prions.Low density subcellular fractions enhance disease-specific prion protein misfolding.The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro.Coinfecting prion strains compete for a limiting cellular resource.Synthesis of high titer infectious prions with cofactor molecules.Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.Relationship between conformational stability and amplification efficiency of prions.De novo prions.Highly efficient amplification of chronic wasting disease agent by protein misfolding cyclic amplification with beads (PMCAb).Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C).Molecular modeling of prion transmission to humansReview: contribution of transgenic models to understanding human prion disease.Generation of a new form of human PrP(Sc) in vitro by interspecies transmission from cervid prionsStrain typing of classical scrapie by transgenic mouse bioassay using protein misfolding cyclic amplification to replace primary passage.Quantitative assessment of prion infectivity in tissues and body fluids by real-time quaking-induced conversion.Two misfolding routes for the prion protein around pH 4.5.Superparamagnetic nanoparticle capture of prions for amplification.Molecular biology and pathology of prion strains in sporadic human prion diseases.Epigenetic dominance of prion conformers.Red-backed vole brain promotes highly efficient in vitro amplification of abnormal prion protein from macaque and human brains infected with variant Creutzfeldt-Jakob disease agent.Initial fate of prions upon peripheral infection: half-life, distribution, clearance, and tissue uptake.Conformational transformation and selection of synthetic prion strains.Structural determinants of phenotypic diversity and replication rate of human prions.Prions on the move.Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions.A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.Rabbits are not resistant to prion infection
P2860
Q24599702-42A839F4-AE91-4562-92BC-1CD0888F03C0Q24626352-F67E1AC1-8ED7-48E1-B591-A49A50B66AB3Q24632206-DCB8F3DC-9B3C-431C-A611-286499FC6C78Q27313215-CBDC0CED-4CC9-4C3E-A3A9-B2B194B37D26Q27315010-EA32F360-4519-48D4-974C-E7AEDEC61591Q27317045-2D3A00C5-3994-4995-AC94-183E8DEA105CQ28478072-C92C1E07-8A0D-4A99-8641-3BC11CD76F76Q30368863-D0FFBBC6-BB36-44CA-A112-C3D0CD42EBB4Q30436588-277BD3A3-BABA-423C-AF72-FC718B5D3808Q30540027-B973FC43-E76C-4708-9928-3D74818E9151Q30639674-39B1F29D-876B-4279-A70F-7C02F5C3D57BQ30875331-64554F38-922B-412D-9F45-680DCDA391B4Q33725453-B1277AA1-CDC0-47D4-A934-CFD3C86402D4Q33725480-E697DB88-23C5-4CDC-9C44-60BECD71F45FQ33744702-FBFEA65E-542F-49C6-A1BC-8764830368FCQ33797815-98820E80-8765-40E0-A78C-FE26A523A62AQ33877386-9E1DF16C-2FF5-484D-9249-AD296DE37CE1Q33931086-362F1BFF-FA36-49EE-8F9A-8575E443A16CQ33967960-A742F4E9-53CD-465C-916F-F51F64CF3A3AQ33994890-58C063A9-3A6A-43D2-8C51-FB9FF2744482Q34175498-703F980A-1E4A-4C06-A29C-91EDCCA79439Q34238993-BD00E00D-8B3F-4D1E-93EB-5591C6B98F95Q34372311-87CEC768-C6D7-4B83-ACDB-97C41709DE58Q34423397-418BCBF7-9666-4BF7-9535-2C1565CCD961Q34474868-921C5A83-BEBB-4566-9A8B-6E6C9D3BD126Q34606377-088EF7A5-FA9F-4199-90E8-42F2620F5E89Q34614503-65C3B7D0-C135-48B2-9DB2-38D742B86BFFQ34720803-4E7D5B33-8883-41D2-AB00-689C0756B3BAQ34733523-93574623-B543-477A-854E-AC65AD93A0F5Q34742787-7E640BCF-168F-4452-B072-1DB7815A4D99Q34802620-EAF831BB-7535-4B11-AFD7-D8A9C54E4C58Q35034201-F60CA163-D5A7-44B6-B0E9-87D4F2166AE4Q35036649-EA7E4D39-9643-4608-AF22-957405EA5009Q35105375-7C6FEA80-87CE-4844-84CF-EE474A06CABCQ35376718-62792A80-F814-4D96-902C-8B1BA0DFE0E5Q35416860-ACB9459B-D5CC-460C-9481-149B5DE4DA50Q35512142-E0420074-D28A-48DB-BE3E-D1530C9D344AQ35585904-B36DD724-0F3F-4FAA-8993-500BE90C1DEBQ35678593-80D98297-AAA6-422E-ADAC-970232C1DBF0Q35882420-2AC6F1FA-2B53-427B-9D3F-11CC08A4A0D7
P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Cell-free propagation of prion strains.
@en
type
label
Cell-free propagation of prion strains.
@en
prefLabel
Cell-free propagation of prion strains.
@en
P2093
P2860
P356
P1433
P1476
Cell-free propagation of prion strains
@en
P2093
Claudio Soto
Marcelo Barria
Pierluigi Gambetti
Rodrigo Morales
P2860
P304
P356
10.1038/EMBOJ.2008.181
P407
P577
2008-09-18T00:00:00Z