Two Creutzfeldt-Jakob disease agents reproduce prion protein-independent identities in cell cultures.
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Darwinian evolution of prions in cell cultureCells infected with scrapie and Creutzfeldt-Jakob disease agents produce intracellular 25-nm virus-like particlesCellular aspects of prion replication in vitroThe kuru infectious agent is a unique geographic isolate distinct from Creutzfeldt-Jakob disease and scrapie agents.Endogenous proteolytic cleavage of disease-associated prion protein to produce C2 fragments is strongly cell- and tissue-dependent.Agent-specific Shadoo responses in transmissible encephalopathies.Quantitative recovery of scrapie agent with minimal protein from highly infectious cultures.Continuous production of prions after infectious particles are eliminated: implications for Alzheimer's diseaseInfectious particles, stress, and induced prion amyloids: a unifying perspective.Transfer of a prion strain to different hosts leads to emergence of strain variants.Proteomic analysis of host brain components that bind to infectious particles in Creutzfeldt-Jakob disease.CJD and Scrapie Require Agent-Associated Nucleic Acids for Infection.Replication and spread of CJD, kuru and scrapie agents in vivo and in cell cultureHigh CJD infectivity remains after prion protein is destroyed.Persistent propagation of variant Creutzfeldt-Jakob disease agent in murine spleen stromal cell culture with features of mesenchymal stem cells.Disease-specific motifs can be identified in circulating nucleic acids from live elk and cattle infected with transmissible spongiform encephalopathies.The role of genetics in chronic wasting disease of North American cervids.Generation of Infectious Prions and Detection with the Prion-Infected Cell Assay.A prokaryotic viral sequence is expressed and conserved in mammalian brain.Rapid chemical decontamination of infectious CJD and scrapie particles parallels treatments known to disrupt microbes and biofilms.Transcytosis of murine-adapted bovine spongiform encephalopathy agents in an in vitro bovine M cell model.A rapid accurate culture assay for infectivity in Transmissible Encephalopathies.Isolation of Exosomes and Microvesicles from Cell Culture Systems to Study Prion Transmission.Biological and biochemical characteristics of prion strains conserved in persistently infected cell cultures.Proliferative arrest of neural cells induces prion protein synthesis, nanotube formation, and cell-to-cell contacts.Strain-specific viral properties of variant Creutzfeldt-Jakob disease (vCJD) are encoded by the agent and not by host prion proteinTransmissible encephalopathy agents: virulence, geography and clockwork.Increased proportions of C1 truncated prion protein protect against cellular M1000 prion infection.Nuclease resistant circular DNAs copurify with infectivity in scrapie and CJD.Human stem cell-derived astrocytes replicate human prions in a PRNP genotype-dependent manner.Biological and biochemical characterization of M2B cells: Classical BSE prion is conserved in transgenic mice overexpressing bovine prion protein gene.
P2860
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P2860
Two Creutzfeldt-Jakob disease agents reproduce prion protein-independent identities in cell cultures.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Two Creutzfeldt-Jakob disease ...... t identities in cell cultures.
@ast
Two Creutzfeldt-Jakob disease ...... t identities in cell cultures.
@en
type
label
Two Creutzfeldt-Jakob disease ...... t identities in cell cultures.
@ast
Two Creutzfeldt-Jakob disease ...... t identities in cell cultures.
@en
prefLabel
Two Creutzfeldt-Jakob disease ...... t identities in cell cultures.
@ast
Two Creutzfeldt-Jakob disease ...... t identities in cell cultures.
@en
P2093
P2860
P356
P1476
Two Creutzfeldt-Jakob disease ...... t identities in cell cultures.
@en
P2093
Alvaro Arjona
Florian Islinger
Laura Manuelidis
Laura Simarro
Noriyuki Nishida
P2860
P304
P356
10.1073/PNAS.0400158101
P407
P577
2004-05-25T00:00:00Z