Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteins.

@article{Saunders2009MultidomainMU,
  title={Multi-domain misfolding: understanding the aggregation pathway of polyglutamine proteins.},
  author={Helen M Saunders and Stephen P. Bottomley},
  journal={Protein engineering, design \& selection : PEDS},
  year={2009},
  volume={22 8},
  pages={
          447-51
        }
}
The polyglutamine (polyQ) diseases consist of nine neurodegenerative diseases in which a polyQ tract expansion leads to protein misfolding and subsequent aggregation. Even when the causative proteins have the same length polyQ tract, there are differences in the severity and age of disease onset which implicate the polyQ flanking sequences as modulators of disease. Recent studies on the polyQ proteins ataxin-1, ataxin-3 and huntingtin exon-1 have shown that the flanking domains have an… 
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Modeling the polyglutamine aggregation pathway in Huntington's disease: from basic studies to clinical applications.
  • K. Sugaya
  • Biology
    Sub-cellular biochemistry
  • 2012
TLDR
Two risk-based stochastic kinetic models that describe genotype-phenotype correlations in patients with polyQ diseases and reflect alternative pathways of polyQ aggregation are described, and a mathematical model by which the time course of neurodegeneration in HD can be precisely predicted is presented.
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