Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment. - Wikidata - awgldk - TriplyDB

Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.

Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.

http://www.wikidata.org/entity/Q30490726

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Type 1 fimbrial adhesin FimH elicits an immune response that enhances cell adhesion of Escherichia coli Mutant huntingtin gene-dose impacts on aggregate deposition, DARPP32 expression and neuroinflammation in HdhQ150 mice Secondary Structure of Huntingtin Amino-Terminal Region Beta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residues Disease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact Structure An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril Formation Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Intrabody gene therapy ameliorates motor, cognitive, and neuropathological symptoms in multiple mouse models of Huntington's disease.Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo.Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species.Quantitative relationships between huntingtin levels, polyglutamine length, inclusion body formation, and neuronal death provide novel insight into huntington's disease molecular pathogenesis.Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core Autoimmune antibody decline in Parkinson's disease and Multiple System Atrophy; a step towards immunotherapeutic strategies.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansion Huntingtin localisation studies - a technical review.TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.Hsp70 and Hsp40 functionally interact with soluble mutant huntingtin oligomers in a classic ATP-dependent reaction cycle Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.A compact beta model of huntingtin toxicity.Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein alpha-synuclein.Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria, and selective synaptic degeneration in Huntington's disease Identifying polyglutamine protein species in situ that best predict neurodegeneration The emerging role of the first 17 amino acids of huntingtin in Huntington's disease Structural features and domain organization of huntingtin fibrils.Identification of novel polyglutamine-expanded aggregation species in spinal and bulbar muscular atrophy Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core Aggregation formation in the polyglutamine diseases: protection at a cost?Identical oligomeric and fibrillar structures captured from the brains of R6/2 and knock-in mouse models of Huntington's disease.Protein aggregates in Huntington's disease.An Antibody to Detect Alanine-Expanded PABPN1: A New Tool to Study Oculopharyngeal Muscular Dystrophy Pharmacological protein targets in polyglutamine diseases: mutant polypeptides and their interactors.Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?Pathology and function of nuclear amyloid. Protein homeostasis matters.Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.Quantitative feature extraction reveals the status quo of protein fibrillation in the cell nucleus.Polyglutamine expansion affects huntingtin conformation in multiple Huntington's disease models.Polyglutamine dances the conformational cha-cha-cha.A toxic mutant huntingtin species is resistant to selective autophagy.Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

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P2860

Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.

http://www.wikidata.org/entity/Q30490726

description

2009 nî lūn-bûn

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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Monoclonal antibodies recogniz ...... a mutant huntingtin fragment.

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Monoclonal antibodies recogniz ...... a mutant huntingtin fragment.

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type

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Monoclonal antibodies recogniz ...... a mutant huntingtin fragment.

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Monoclonal antibodies recogniz ...... a mutant huntingtin fragment.

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prefLabel

Monoclonal antibodies recogniz ...... a mutant huntingtin fragment.

@ast

Monoclonal antibodies recogniz ...... a mutant huntingtin fragment.

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JBC.M109.016923

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Journal of Biological Chemistry

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Monoclonal antibodies recogniz ...... a mutant huntingtin fragment.

@en

P2093

Cheping Ng

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

Geneva L Williams

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

Gregor P Lotz

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

Jan Ko

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

Jason Miller

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

Justin Legleiter

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

Paul H Patterson

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Paul J Muchowski

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Steve Finkbeiner

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P2860

Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's disease

The structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice model

Protein misfolding, functional amyloid, and human disease

Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation

Protein aggregation and neurodegenerative disease

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Huntingtin bodies sequester vesicle-associated proteins by a polyproline-dependent interaction.

Using antibodies to analyze polyglutamine stretches.

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32

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284

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2009-06-02T00:00:00Z

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19491400

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