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Article

Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?

22 Oct 2014

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 25336039
DOI: 10.1007/s12035-014-8932-1

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Related research

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Polyglutamine Aggregation in Huntington Disease: Does Structure Determine Toxicity?PMID 25336039Read ↗

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The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensitySemantic proximity Read ↗

Monomeric, Oligomeric and Polymeric Proteins in Huntington Disease and Other Diseases of Polyglutamine ExpansionSemantic proximity Read ↗

Polyglutamine aggregation in Huntington and related diseases.Semantic proximity Read ↗

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Conformational studies of pathogenic expanded polyglutamine protein deposits from Huntington’s diseaseSemantic proximity Read ↗

Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In VivoSemantic proximity Read ↗

A Review On Huntington Protein: Insight Into Protein Aggregation and Therapeutic Interventions.Semantic proximity Read ↗

The structural basis of huntingtin (Htt) fibril polymorphism, revealed by cryo-EM of exon 1 Htt fibrilsSemantic proximity Read ↗

Subtyping monogenic disorders: Huntington disease.Semantic proximity Read ↗

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