The structure of the AXH domain of spinocerebellar ataxin-1 - sprookjes - yvandenbroek - TriplyDB

The structure of the AXH domain of spinocerebellar ataxin-1

The structure of the AXH domain of spinocerebellar ataxin-1

http://www.wikidata.org/entity/Q27642446

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Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1.Pathogenic mechanisms of a polyglutamine-mediated neurodegenerative disease, spinocerebellar ataxia type 1 Cell biology of spinocerebellar ataxia The unstable repeats--three evolving faces of neurological disease Polyglutamine neurodegeneration: expanded glutamines enhance native functions Structural basis of protein complex formation and reconfiguration by polyglutamine disease protein Ataxin-1 and Capicua Self-Assembly and Conformational Heterogeneity of the AXH Domain of Ataxin-1: An Unusual Example of a Chameleon Fold Protein-protein interactions as a strategy towards protein-specific drug design: the example of ataxin-1 Phosphorylation of S776 and 14-3-3 binding modulate ataxin-1 interaction with splicing factors Conformational fluctuations of the AXH monomer of Ataxin-1.Partial loss of Tip60 slows mid-stage neurodegeneration in a spinocerebellar ataxia type 1 (SCA1) mouse model.Characterization of the zebrafish atxn1/axh gene family Consensus paper: pathological mechanisms underlying neurodegeneration in spinocerebellar ataxias.Mapping the self-association domains of ataxin-1: identification of novel non overlapping motifs.Kaleidoscopic protein-protein interactions in the life and death of ataxin-1: new strategies against protein aggregation.Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.Nuclear ataxias.Cerebellar Transcriptome Profiles of ATXN1 Transgenic Mice Reveal SCA1 Disease Progression and Protection Pathways.SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal.Evolution and conservation of JmjC domain proteins in the green lineage.Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions.Polyglutamine spinocerebellar ataxias - from genes to potential treatments.Destabilizing the AXH Tetramer by Mutations: Mechanisms and Potential Antiaggregation Strategies.Characterization of the AXH domain of Ataxin-1 using enhanced sampling and functional mode analysis.

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P2860

The structure of the AXH domain of spinocerebellar ataxin-1

http://www.wikidata.org/entity/Q27642446

description

2004 nî lūn-bûn

@nan

2004 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հունվարին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

The structure of the AXH domain of spinocerebellar ataxin-1

@ast

The structure of the AXH domain of spinocerebellar ataxin-1

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The structure of the AXH domain of spinocerebellar ataxin-1

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type

label

The structure of the AXH domain of spinocerebellar ataxin-1

@ast

The structure of the AXH domain of spinocerebellar ataxin-1

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The structure of the AXH domain of spinocerebellar ataxin-1

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prefLabel

The structure of the AXH domain of spinocerebellar ataxin-1

@ast

The structure of the AXH domain of spinocerebellar ataxin-1

@en

The structure of the AXH domain of spinocerebellar ataxin-1

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P1433

Journal of Biological Chemistry

P1476

The structure of the AXH domain of spinocerebellar ataxin-1

@en

P2093

Jan Löwe

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

Mark Bycroft

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

Mark D Allen

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

Yu Wai Chen

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

P2860

A novel protein with RNA-binding motifs interacts with ataxin-2

The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract

USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product

p80 coilin, a coiled body-specific protein, interacts with ataxin-1, the SCA1 gene product

Identification of a self-association region within the SCA1 gene product, ataxin-1

HBP1: a HMG box transcriptional repressor that is targeted by the retinoblastoma family

Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures

Negative regulation of the Wnt-beta-catenin pathway by the transcriptional repressor HBP1

Functional evolution of two subtly different (similar) folds

Improved methods for building protein models in electron density maps and the location of errors in these models

P304

3758-65

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scholarly article

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10.1074/JBC.M309817200

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P433

5

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279

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Dmitry B Veprintsev

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2004-01-30T00:00:00Z

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14583607

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