Prefibrillar huntingtin oligomers isolated from HD brain potently seed amyloid formation

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dc.contributor.author Morozova, Olga A.
dc.contributor.author Gupta, Sharad
dc.contributor.author Colby, David W.
dc.date.accessioned 2015-06-26T10:02:50Z
dc.date.available 2015-06-26T10:02:50Z
dc.date.issued 2015-07-08
dc.identifier.citation Morozova, Olga A.; Gupta, Sharad and Colby, David W., “Prefibrillar huntingtin oligomers isolated from HD brain potently seed amyloid formation”, FEBS Letters, DOI: 10.1016/j.febslet.2015.05.041, vol. 589, no. 15, pp. 1897-1903, 8, Jul.2015.
dc.identifier.issn 0014-5793
dc.identifier.uri http://dx.doi.org/10.1016/j.febslet.2015.05.041
dc.identifier.uri https://repository.iitgn.ac.in/handle/123456789/1789
dc.description.abstract Many neurodegenerative diseases are associated with deposits of aggregated protein in the brain. The molecular pathways through which soluble proteins misfold to form amyloids and large protein aggregates often include diverse oligomeric species, only some of which progress to the amyloid state. Here we show that prefibrillar huntingtin (HTT) oligomers, isolated from Huntington’s disease (HD) affected human brain samples or mouse models, stimulate polyglutamine amyloid formation. Fibrillar HTT oligomers have been shown to be unstable under denaturing conditions and appear not to lead to amyloid formation. Here we show that prefibrillar HTT oligomers are remarkably stable and are potent seeds of polyglutamine amyloid formation. Therefore, our findings help to dissect the complex molecular pathway of HTT misfolding. en_US
dc.description.statementofresponsibility by Olga A. Morozova, Sharad Gupta and David W. Colby
dc.format.extent vol. 589, no. 15, pp. 1897-1903
dc.language.iso en en_US
dc.publisher Science Direct en_US
dc.subject Amyloid en_US
dc.subject Huntington’s disease en_US
dc.subject Oligomer en_US
dc.subject Neurodegeneration en_US
dc.subject Polyglutamine en_US
dc.title Prefibrillar huntingtin oligomers isolated from HD brain potently seed amyloid formation en_US
dc.type Article en_US
dc.relation.journal FEBS Letters


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