Pharmacological chaperone for the structured domain of human prion protein. - Wikidata - wikimedia - TriplyDB

Pharmacological chaperone for the structured domain of human prion protein.

Pharmacological chaperone for the structured domain of human prion protein.

http://www.wikidata.org/entity/Q34199756

about

Emerging novel concept of chaperone therapies for protein misfolding diseases The prion protein binds thiamine Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Characterizing antiprion compounds based on their binding properties to prion proteins: implications as medical chaperones.A survey of antiprion compounds reveals the prevalence of non-PrP molecular targets.Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites Abrogation of complex glycosylation by swainsonine results in strain- and cell-specific inhibition of prion replication.A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein.Structural plasticity of the cellular prion protein and implications in health and disease.Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein Quinacrine promotes replication and conformational mutation of chronic wasting disease prions.Identification of Anti-prion Compounds using a Novel Cellular Assay.Mammalian prions and their wider relevance in neurodegenerative diseases.The Medical Research Council prion disease rating scale: a new outcome measure for prion disease therapeutic trials developed and validated using systematic observational studies.Synthesis of an (11) C-labeled antiprion GN8 derivative and evaluation of its brain uptake by positron emission tomography.Identification of a Compound That Disrupts Binding of Amyloid-β to the Prion Protein Using a Novel Fluorescence-based Assay.Prediction of antiprion activity of therapeutic agents with structure-activity models.Soluble Aβ aggregates can inhibit prion propagation.Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Targeting the cellular prion protein to treat neurodegeneration.Pharmacological Agents Targeting the Cellular Prion Protein.

P2860

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P2860

Pharmacological chaperone for the structured domain of human prion protein.

http://www.wikidata.org/entity/Q34199756

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

Pharmacological chaperone for the structured domain of human prion protein.

@ast

Pharmacological chaperone for the structured domain of human prion protein.

@en

Pharmacological chaperone for the structured domain of human prion protein.

@nl

type

label

Pharmacological chaperone for the structured domain of human prion protein.

@ast

Pharmacological chaperone for the structured domain of human prion protein.

@en

Pharmacological chaperone for the structured domain of human prion protein.

@nl

prefLabel

Pharmacological chaperone for the structured domain of human prion protein.

@ast

Pharmacological chaperone for the structured domain of human prion protein.

@en

Pharmacological chaperone for the structured domain of human prion protein.

@nl

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PNAS.1009062107

P1433

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

P1476

Pharmacological chaperone for the structured domain of human prion protein

@en

P2093

Amaurys Avila Ibarra

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

Andrew J Nicoll

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Anthony R Clarke

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Clare R Trevitt

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Connor Wright

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

Emma Quarterman

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

Emmanuel Risse

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

John Collinge

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M Howard Tattum

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

Mark Farrow

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

P2860

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers

Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation

Safety and efficacy of quinacrine in human prion disease (PRION-1 study): a patient-preference trial

Hot spots in prion protein for pathogenic conversion

NMR solution structure of the human prion protein

Targeted rescue of a destabilized mutant of p53 by an in silico screened drug

Crystal structure of human prion protein bound to a therapeutic antibody

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

Mice devoid of PrP are resistant to scrapie

A general model of prion strains and their pathogenicity

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17610-17615

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scholarly article

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10.1073/PNAS.1009062107

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P433

41

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107

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Graham S Jackson

Jonathan P Waltho

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2010-09-27T00:00:00Z

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46578329

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20876144

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Prion protein family

molecular chaperones

protein structure

P932

2955083

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