A linear lattice model for polyglutamine in CAG-expansion diseases - Wikidata - awgldk - TriplyDB

A linear lattice model for polyglutamine in CAG-expansion diseases

A linear lattice model for polyglutamine in CAG-expansion diseases

http://www.wikidata.org/entity/Q34153913

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Structural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography.A universal mechanism ties genotype to phenotype in trinucleotide diseases The structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice model 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 Linear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10 The Huntington's disease mutation impairs Huntingtin's role in the transport of NF-κB from the synapse to the nucleus.Amyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host protein Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment.Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions Differential hydrophobicity drives self-assembly in Huntington's disease.Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansion Perturbation with intrabodies reveals that calpain cleavage is required for degradation of huntingtin exon 1 TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence.Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool.polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation.Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides A structural model of polyglutamine determined from a host-guest method combining experiments and landscape theory.Fragments of HdhQ150 mutant huntingtin form a soluble oligomer pool that declines with aggregate deposition upon aging Mutational analysis of the structural organization of polyglutamine aggregates.Polyglutamine fibrillogenesis: the pathway unfolds The role of interruptions in polyQ in the pathology of SCA1.Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy Protein aggregation in motor neurone disorders.Identifying polyglutamine protein species in situ that best predict neurodegeneration Anti-PolyQ Antibodies Recognize a Short PolyQ Stretch in Both Normal and Mutant Huntingtin Exon 1.Quantitative characterization of intrinsic disorder in polyglutamine: insights from analysis based on polymer theories.Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer.The emerging role of the first 17 amino acids of huntingtin in Huntington's disease Structural features and domain organization of huntingtin fibrils.Conformation sensors that distinguish monomeric proteins from oligomers in live cells.ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions.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.

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A linear lattice model for polyglutamine in CAG-expansion diseases

http://www.wikidata.org/entity/Q34153913

description

2002 nî lūn-bûn

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2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

A linear lattice model for polyglutamine in CAG-expansion diseases

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A linear lattice model for polyglutamine in CAG-expansion diseases

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A linear lattice model for polyglutamine in CAG-expansion diseases

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type

label

A linear lattice model for polyglutamine in CAG-expansion diseases

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A linear lattice model for polyglutamine in CAG-expansion diseases

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A linear lattice model for polyglutamine in CAG-expansion diseases

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prefLabel

A linear lattice model for polyglutamine in CAG-expansion diseases

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A linear lattice model for polyglutamine in CAG-expansion diseases

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A linear lattice model for polyglutamine in CAG-expansion diseases

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

P1476

A linear lattice model for polyglutamine in CAG-expansion diseases

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P2093

Anthony P West

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

Kathryn E Huey-Tubman

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Melanie J Bennett

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Scott A Ross

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P2860

A huntingtin-associated protein enriched in brain with implications for pathology

Crystal structure and immunoglobulin G binding properties of the human major histocompatibility complex-related Fc receptor(,)

Calculation of protein extinction coefficients from amino acid sequence data

Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin

Huntingtin interacts with a family of WW domain proteins

Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice

Discovering high-affinity ligands for proteins: SAR by NMR

A structural approach to trinucleotide expansion diseases.

Fourteen and counting: unraveling trinucleotide repeat diseases.

An improved function for fitting sedimentation velocity data for low-molecular-weight solutes.

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11634-11639

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scholarly article

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10.1073/PNAS.182393899

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18

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99

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Pamela J. Bjorkman

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2002-08-22T00:00:00Z

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11193897

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12193654

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129321

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