Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. - Wikidata - wikimedia - TriplyDB

Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion.

Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion.

http://www.wikidata.org/entity/Q31151988

about

A mathematical analysis of SELEX Prion protein-specific antibodies that detect multiple TSE agents with high sensitivity Anti-prion activity of an RNA aptamer and its structural basis RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity Immunodetection of disease-associated mutant PrP, which accelerates disease in GSS transgenic mice.Protection of HIV neutralizing aptamers against rectal and vaginal nucleases: implications for RNA-based therapeutics.Human prions and plasma lipoproteins.Generation of neutralizing aptamers against herpes simplex virus type 2: potential components of multivalent microbicides.Recent advances in prion chemotherapeutics.Current progress of RNA aptamer-based therapeutics.Inhibition of Aggregation of Mutant Huntingtin by Nucleic Acid Aptamers In Vitro and in a Yeast Model of Huntington's Disease Current and future molecular diagnostics for prion diseases.Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation.Anti-bovine prion protein RNA aptamer containing tandem GGA repeat interacts both with recombinant bovine prion protein and its beta isoform with high affinity PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions Human Norovirus Aptamer Exhibits High Degree of Target Conformation-Dependent Binding Similar to That of Receptors and Discriminates Particle Functionality A computationally designed DNA aptamer template with specific binding to phosphatidylserine.Delivery systems for in vivo use of nucleic Acid drugs.The role of RNA in mammalian prion protein conversion.Molecular diagnosis of human prion disease.Characterisation of aptamers for therapeutic studies.Small RNA drugs for prion disease: a new frontier.Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids.Cell-specific aptamers as emerging therapeutics.Distinguishing closely related amyloid precursors using an RNA aptamer.Selection of a DNA aptamer for cadmium detection based on cationic polymer mediated aggregation of gold nanoparticles.RNA aptamers selectively modulate protein recruitment to the cytoplasmic domain of beta-secretase BACE1 in vitro.Optimized light-directed synthesis of aptamer microarrays.Selection of aptamers for amyloid beta-protein, the causative agent of Alzheimer's disease.Aptamer and its applications in neurodegenerative diseases.Charge neutralization as the major factor for the assembly of nucleocapsid-like particles from C-terminal truncated hepatitis C virus core protein.Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Prion protein complexed to N2a cellular RNAs through its N-terminal domain forms aggregates and is toxic to murine neuroblastoma cells Binding of recombinant but not endogenous prion protein to DNA causes DNA internalization and expression in mammalian cells.Rapid formation of amyloid from alpha-monomeric recombinant human PrP in vitro.Screening of DNA aptamer against mouse prion protein by competitive selection.Structural determinants of conformationally selective, prion-binding aptamers.Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant: implications for disease susceptibility to Creutzfeldt-Jakob disease.Investigation of the interactions between aptamer and misfolded proteins: From monomer and oligomer to fibril by single-molecule force spectroscopy.

P2860

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P2860

Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion.

http://www.wikidata.org/entity/Q31151988

description

2003 nî lūn-bûn

@nan

2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի օգոստոսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

@zh-tw

2003年论文

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name

Characterization of 2'-fluoro- ...... rotein and inhibit conversion.

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Characterization of 2'-fluoro- ...... rotein and inhibit conversion.

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type

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Characterization of 2'-fluoro- ...... rotein and inhibit conversion.

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Characterization of 2'-fluoro- ...... rotein and inhibit conversion.

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prefLabel

Characterization of 2'-fluoro- ...... rotein and inhibit conversion.

@ast

Characterization of 2'-fluoro- ...... rotein and inhibit conversion.

@en

P1433

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P2860

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P1433

Journal of Biological Chemistry

P1476

Characterization of 2'-fluoro- ...... protein and inhibit conversion

@en

P2093

Abdessamad Tahiri-Alaoui

http://www.w3.org/2001/XMLSchema#string

Alexandre Rhie

http://www.w3.org/2001/XMLSchema#string

Ian Sylvester

http://www.w3.org/2001/XMLSchema#string

James Hope

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Louise Kirby

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Natalie Sayer

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Rosanna Wellesley

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P2860

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

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

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

NMR solution structure of the human prion protein

NMR structure of the bovine prion protein

Crystal structure of the human prion protein reveals a mechanism for oligomerization

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

Solution structure of Syrian hamster prion protein rPrP(90-231).

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

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39697-39705

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scholarly article

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10.1074/JBC.M305297200

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41

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278

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2003-08-05T00:00:00Z

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12902353

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P921

Prion protein family