TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes. - Test2 - elhamkhani - TriplyDB

TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.

TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.

http://www.wikidata.org/entity/Q33851150

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Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy Anti-PolyQ Antibodies Recognize a Short PolyQ Stretch in Both Normal and Mutant Huntingtin Exon 1.Polyglutamine expansion affects huntingtin conformation in multiple Huntington's disease models.A toxic mutant huntingtin species is resistant to selective autophagy.Suppression of MAPK11 or HIPK3 reduces mutant Huntingtin levels in Huntington's disease models.Phosphorylation of huntingtin at residue T3 is decreased in Huntington's disease and modulates mutant huntingtin protein conformation.Inhibition of PIP4Kγ ameliorates the pathological effects of mutant huntingtin protein.The COOH-terminal domain of huntingtin interacts with RhoGEF kalirin and modulates cell survival.

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TR-FRET assays of Huntingtin protein fragments reveal temperature and polyQ length-dependent conformational changes.

http://www.wikidata.org/entity/Q33851150

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2014 nî lūn-bûn

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2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2014 թվականի հուլիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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TR-FRET assays of Huntingtin p ...... endent conformational changes.

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TR-FRET assays of Huntingtin p ...... endent conformational changes.

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TR-FRET assays of Huntingtin p ...... endent conformational changes.

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TR-FRET assays of Huntingtin p ...... endent conformational changes.

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TR-FRET assays of Huntingtin p ...... endent conformational changes.

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TR-FRET assays of Huntingtin p ...... endent conformational changes.

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TR-FRET assays of Huntingtin p ...... endent conformational changes.

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Boxun Lu

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P2860

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

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes.

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

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

Development of a method for the high-throughput quantification of cellular proteins.

Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease.

A linear lattice model for polyglutamine in CAG-expansion diseases

Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation.

A screen for enhancers of clearance identifies huntingtin as a heat shock protein 90 (Hsp90) client protein.

Identifying polyglutamine protein species in situ that best predict neurodegeneration

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