IndraLab

Statements


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"Exogenous expression of human wild-type ataxin-3 in Drosophila suppressed polyglutamine related neurodegeneration in vivo, in a manner that was dependent on its Ub binding and chain cleaving properties [XREF_BIBR]."

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"Recently, ataxin-3, a polyubiquitin-binding protein with deubiquitination activity, was shown to suppress polyglutamine-mediated neurodegeneration in a proteasome-dependent manner [11] ."

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"Parkin can also target polyglutamine proteins ataxin-2 and ataxin-3 for ubiquitination to negatively control their levels and reduce these polyglutamine proteins induced cytotoxicity [XREF_BIBR, XREF_BIBR]."

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"In Drosophila, ataxin-3 suppresses the toxicity of expanded polyglutamine proteins in a manner that requires the catalytic activity of the Josephin domain XREF_BIBR."

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"Like CHIP, ataxin-3 suppresses polyglutamine toxicity and does so in a manner linked to its ubiquitin associated activities."

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"The findings suggested that JM17 ameliorated oxidative stress in SCA3 by improving mitochondrial function and reducing polyglutamine neurotoxicity."

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"Strikingly, it was found that ATXN3 suppresses polyglutamine neurodegeneration in Drosophila, and this suppressing activity is dependent on its interaction with ubiquitin and on its protease activity [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In contrast, full-length expanded ataxin-3 with an even longer repeat caused a much milder, selectively neurotoxic phenotype, and normal ataxin-3 actually suppressed the toxicity of other polyglutamine disease proteins."

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"Ataxin-3 suppresses polyglutamine neurodegeneration in Drosophila by a ubiquitin associated mechanism."