ArticleJournal of biomolecular structure & dynamics2017
Effects of the enlargement of polyglutamine segments on the structure and folding of ataxin-2 and ataxin-3 proteins.
Article in Journal of biomolecular structure & dynamics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Modulation of the Stress Granule Component Carhsp1 Mitigates Disease-Associated Deficits in Spinocerebellar Ataxia Type 3 Mouse Models.Movement disorders : official journal of the Movement Disorder Society · 2026Article
- Cell death or survival: Insights into the role of mRNA translational control.Seminars in cell & developmental biology · 2024Review
- Theoretical study on the design of allosteric inhibitors of diabetes associated protein PTP1B.Frontiers in pharmacology · 2024Article
- Autophagy in Spinocerebellar ataxia type 2, a dysregulated pathway, and a target for therapy.Cell death & disease · 2021Article
- Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?Cell death & disease · 2021Review
- Big data and artificial intelligence discover novel drugs targeting proteins without 3D structure and overcome the undruggable targets.Stroke and vascular neurology · 2020Review
- Removal of the Polyglutamine Repeat of Ataxin-3 by Redirecting pre-mRNA Processing.International journal of molecular sciences · 2019Article
- Calcium interactions with Cx26 hemmichannel: Spatial association between MD simulations biding sites and variant pathogenicity.Computational biology and chemistry · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Spinocerebellar ataxia type 2 (SCA2) and type 3 (SCA3) are two common autosomal-dominant inherited ataxia syndromes, both of which are related to the unstable expansion of trinucleotide CAG repeats in the coding region of the related ATXN2 and ATXN3 genes, respectively. The poly-glutamine (poly-Q) tract encoded by the CAG repeats has long been recognized as an important factor in disease pathogenesis and progress. In this study, using the I-TASSER method for 3D structure prediction, we investigated the effect of poly-Q tract enlargement on the structure and folding of ataxin-2 and ataxin-3 proteins. Our results show good agreement with the known experimental structures of the Josephin and UIM domains providing credence to the simulation results presented here, which show that the enlargement of the poly-Q region not only affects the local structure of these regions but also affects the structures of functional domains as well as the whole protein. The changes observed in the predicted models of the UIM domains in ataxin-3 when the poly-Q track is enlarged provide new insights on possible pathogenic mechanisms.
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Registered trials
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