Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids - Test2 - elhamkhani - TriplyDB

Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids

Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids

http://www.wikidata.org/entity/Q24614859

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Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions Insights into Mechanisms of Chronic Neurodegeneration Yeast prions: structure, biology, and prion-handling systems Synthetic prions with novel strain-specified properties Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian Prion Efficient uptake and dissemination of scrapie prion protein by astrocytes and fibroblasts from adult hamster brain Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity Evidence that bank vole PrP is a universal acceptor for prions Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein Critical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion protein Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity Anti-prion activity of a panel of aromatic chemical compounds: in vitro and in silico approaches Shaking alone induces de novo conversion of recombinant prion proteins to β-sheet rich oligomers and fibrils Role of polysaccharide and lipid in lipopolysaccharide induced prion protein conversion Physical, chemical and kinetic factors affecting prion infectivity Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Prion Protein Prolines 102 and 105 and the Surrounding Lysine Cluster Impede Amyloid Formation.Lipid-dependent generation of dual topology for a membrane protein.The structure of the infectious prion protein: experimental data and molecular models.Heparin binding confers prion stability and impairs its aggregation.Gene expression profiling of brains from bovine spongiform encephalopathy (BSE)-infected cynomolgus macaques.Synthesis of high titer infectious prions with cofactor molecules.Comparison of 2 synthetically generated recombinant prions.Lipopolysaccharide induced conversion of recombinant prion protein.The importance of prions.A C-terminal membrane anchor affects the interactions of prion proteins with lipid membranes.Nucleic acid induced unfolding of recombinant prion protein globular fragment is pH dependent.Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins.Transgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease.Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion Protein A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.Requirements for mutant and wild-type prion protein misfolding in vitro.Antiprion Activity of DB772 and Related Monothiophene- and Furan-Based Analogs in a Persistently Infected Ovine Microglia Culture System Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice Stabilization of a prion strain of synthetic origin requires multiple serial passages Anti-Prion Screening for Acridine, Dextran, and Tannic Acid using Real Time-Quaking Induced Conversion: A Comparison with PrPSc-Infected Cell Screening Two alternative pathways for generating transmissible prion disease de novo.Secondary-structure prediction revisited: Theoretical β-sheet propensity and coil propensity represent structures of amyloids and aid in elucidating phenomena involved in interspecies transmission of prions.PrPSc formation and clearance as determinants of prion tropism.

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Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids

http://www.wikidata.org/entity/Q24614859

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2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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Isolation of phosphatidylethan ...... n the absence of nucleic acids

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Isolation of phosphatidylethan ...... n the absence of nucleic acids

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Isolation of phosphatidylethan ...... n the absence of nucleic acids

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Isolation of phosphatidylethan ...... n the absence of nucleic acids

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Isolation of phosphatidylethan ...... n the absence of nucleic acids

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Proceedings of the National Academy of Sciences of the United States of America

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Isolation of phosphatidylethan ...... n the absence of nucleic acids

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Daniel J Walsh

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Fei Wang

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James C Geoghegan

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Jiyan Ma

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Nathan R Deleault

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Surachai Supattapone

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P2860

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Generating a prion with bacterially expressed recombinant prion protein.

Formation of native prions from minimal components in vitro

Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders

A general model of prion strains and their pathogenicity

Prion propagation and toxicity in vivo occur in two distinct mechanistic phases

Novel proteinaceous infectious particles cause scrapie

Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors

Relationship between conformational stability and amplification efficiency of prions.

Biochemistry. What makes a prion infectious?

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109

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Prion protein family

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3365173

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