Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein. - Wikidata - awgldk - TriplyDB

Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein.

Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein.

http://www.wikidata.org/entity/Q39673524

about

Glypican-1 mediates both prion protein lipid raft association and disease isoform formation Selective incorporation of polyanionic molecules into hamster prions.Formation of native prions from minimal components in vitro Cellular aspects of prion replication in vitro Structure of the Flexible Amino-Terminal Domain of Prion Protein Bound to a Sulfated Glycan A computational approach for identifying the chemical factors involved in the glycosaminoglycans-mediated acceleration of amyloid fibril formation In situ photodegradation of incorporated polyanion does not alter prion infectivity Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Production of cattle lacking prion protein.Prion protein self-peptides modulate prion interactions and conversion.The expanding universe of prion diseases.Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring Heparin binding confers prion stability and impairs its aggregation.Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion protein Sulfated dextrans enhance in vitro amplification of bovine spongiform encephalopathy PrP(Sc) and enable ultrasensitive detection of bovine PrP(Sc).Low density subcellular fractions enhance disease-specific prion protein misfolding.Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro Redox control of prion and disease pathogenesis.Synthesis of high titer infectious prions with cofactor molecules.Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.Biochemistry. What makes a prion infectious?The role of cofactors in prion propagation and infectivity Lipopolysaccharide induced conversion of recombinant prion protein.Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro.Potent antiscrapie activities of degenerate phosphorothioate oligonucleotides.Glycosylphosphatidylinositol anchor-dependent stimulation pathway required for generation of baculovirus-derived recombinant scrapie prion protein.Prion protein misfolding.Prion strain-dependent differences in conversion of mutant prion proteins in cell culture.In vitro detection of prionemia in TSE-infected cervids and hamsters.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.Amyloidogenesis: historical and modern observations point to heparan sulfate proteoglycans as a major culprit.Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans Recent advances in prion chemotherapeutics.Efficient in vitro amplification of chronic wasting disease PrPRES.Modulation of Glycosaminoglycans Affects PrPSc Metabolism but Does Not Block PrPSc Uptake.Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice In vitro amplification of scrapie and chronic wasting disease PrP(res) using baculovirus-expressed recombinant PrP as substrate Volume and energy folding landscape of prion protein revealed by pressure.The role of the 132-160 region in prion protein conformational transitions.

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P2860

Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein.

http://www.wikidata.org/entity/Q39673524

description

2001 nî lūn-bûn

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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2001年论文

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2001年论文

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name

Sulfated glycans and elevated temperature stimulate PrP

@nl

Sulfated glycans and elevated ...... tease-resistant prion protein.

@en

type

label

Sulfated glycans and elevated temperature stimulate PrP

@nl

Sulfated glycans and elevated ...... tease-resistant prion protein.

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Sulfated glycans and elevated temperature stimulate PrP

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Sulfated glycans and elevated ...... tease-resistant prion protein.

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P1433

The EMBO Journal

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Sulfated glycans and elevated ...... tease-resistant prion protein.

@en

P2093

Caughey B

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Chesebro B

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Horiuchi M

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Raymond L

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Wehrly K

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Wong C

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Xiong LW

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P2860

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

NMR structure of the mouse prion protein domain PrP(121-231)

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform

Novel proteinaceous infectious particles cause scrapie

Eight prion strains have PrP(Sc) molecules with different conformations

Glycosylation differences between the normal and pathogenic prion protein isoforms

Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

Chaperone-supervised conversion of prion protein to its protease-resistant form.

Opposite effects of dextran sulfate 500, the polyene antibiotic MS-8209, and Congo red on accumulation of the protease-resistant isoform of PrP in the spleens of mice inoculated intraperitoneally with the scrapie agent.

Self-replication and scrapie.

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377-386

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10.1093/EMBOJ/20.3.377

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3

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20

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232752229

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11157745

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Prion protein family

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133469

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