The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes. - Wikidata - awgldk - TriplyDB

The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.

The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.

http://www.wikidata.org/entity/Q33390385

about

The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease Neurodegeneration and unfolded-protein response in mice expressing a membrane-tethered flexible tail of PrP Prion pathogenesis in the absence of NLRP3/ASC inflammasomes Prion protein-specific antibodies that detect multiple TSE agents with high sensitivity Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian Prion The crystal structure of an octapeptide repeat of the Prion protein in complex with a Fab fragment of the POM2 antibody The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein The octarepeat region of the prion protein is conformationally altered in PrP(Sc)Biochemical properties of highly neuroinvasive prion strains Defining the conformational features of anchorless, poorly neuroinvasive prions The prion protein is an agonistic ligand of the G protein-coupled receptor Adgrg6 Tetracysteine-tagged prion protein allows discrimination between the native and converted forms Post-translational modifications in PrP expand the conformational diversity of prions in vivo Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion Human prion protein sequence elements impede cross-species chronic wasting disease transmission.Functionally relevant domains of the prion protein identified in vivo Repetitive immunization enhances the susceptibility of mice to peripherally administered prions.Unexpected tolerance of alpha-cleavage of the prion protein to sequence variations Enhanced neuroinvasion by smaller, soluble prions.Liposome-siRNA-peptide complexes cross the blood-brain barrier and significantly decrease PrP on neuronal cells and PrP in infected cell cultures.A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.Experimental verification of a traceback phenomenon in prion infection.The N-terminus of the prion protein is a toxic effector regulated by the C-terminus.Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers.Engulfment of cerebral apoptotic bodies controls the course of prion disease in a mouse strain-dependent manner.Prion strain interactions are highly selective.Prion protein and Abeta-related synaptic toxicity impairment.Comparison of 2 synthetically generated recombinant prions.Lymphotoxin, but not TNF, is required for prion invasion of lymph nodes.Prion protein-specific antibodies-development, modes of action and therapeutics application Prion pathogenesis is faithfully reproduced in cerebellar organotypic slice cultures.The role of the NADPH oxidase NOX2 in prion pathogenesis.Biological effects and use of PrPSc- and PrP-specific antibodies generated by immunization with purified full-length native mouse prions.The sheddase ADAM10 is a potent modulator of prion disease.Characterization of four new monoclonal antibodies against the distal N-terminal region of PrP(c).Single-molecule imaging reveals that small amyloid-β1-42 oligomers interact with the cellular prion protein (PrP(C))Spongiform encephalopathy in transgenic mice expressing a point mutation in the β2-α2 loop of the prion protein.Crystallization and preliminary X-ray diffraction analysis of prion protein bound to the Fab fragment of the POM1 antibody Prion infections and anti-PrP antibodies trigger converging neurotoxic pathways.

P2860

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P2860

The POM monoclonals: a comprehensive set of antibodies to non-overlapping prion protein epitopes.

http://www.wikidata.org/entity/Q33390385

description

2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

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name

The POM monoclonals: a compreh ...... apping prion protein epitopes.

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The POM monoclonals: a compreh ...... apping prion protein epitopes.

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Graciela Garen

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Iva Hafner-Bratkovic

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Magdalini Polymenidou

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Martin Vey

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Michael N G James

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Mike Scott

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Nat Kav

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P2860

Selection, characterization and x-ray structure of anti-ampicillin single-chain Fv fragments from phage-displayed murine antibody libraries

Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy

Mapping the prion protein using recombinant antibodies.

Conservation of the cellular gene encoding the scrapie prion protein.

Prion protein expression in different species: analysis with a panel of new mAbs

Ectopic expression of prion protein (PrP) in T lymphocytes or hepatocytes of PrP knockout mice is insufficient to sustain prion replication.

Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies.

Molecular location of a species-specific epitope on the hamster scrapie agent protein.

Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein.

Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system.

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e3872

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10.1371/JOURNAL.PONE.0003872

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12

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3

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Simone Hornemann

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23628023

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19060956

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Prion protein family

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2592702

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