Title : Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer.

Pub. Date : 2016

PMID : 27271685






6 Functional Relationships(s)
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Protein Name
Organism
1 Expansion of the polyglutamine (polyQ) track of the Huntingtin (HTT) protein above 36 is associated with a sharply enhanced risk of Huntington"s disease (HD). polyglutamine huntingtin Rattus norvegicus
2 Expansion of the polyglutamine (polyQ) track of the Huntingtin (HTT) protein above 36 is associated with a sharply enhanced risk of Huntington"s disease (HD). polyglutamine huntingtin Rattus norvegicus
3 Expansion of the polyglutamine (polyQ) track of the Huntingtin (HTT) protein above 36 is associated with a sharply enhanced risk of Huntington"s disease (HD). polyglutamine huntingtin Rattus norvegicus
4 Expansion of the polyglutamine (polyQ) track of the Huntingtin (HTT) protein above 36 is associated with a sharply enhanced risk of Huntington"s disease (HD). polyglutamine huntingtin Rattus norvegicus
5 One hypothesis is that polyQ expansion induces an alternative, toxic conformation in the HTT exon1 monomer. polyglutamine huntingtin Rattus norvegicus
6 We find that, in vitro, mutant HTT exon1 peptides engage in polyQ repeat length dependent dimer and tetramer formation, followed by time dependent formation of diffusible spherical and fibrillar oligomers and finally by larger, sedimentable amyloid fibrils. polyglutamine huntingtin Rattus norvegicus