Distinct C9orf72-Associated Dipeptide Repeat Structures Correlate with Neuronal Toxicity

@inproceedings{Flores2016DistinctCD,
  title={Distinct C9orf72-Associated Dipeptide Repeat Structures Correlate with Neuronal Toxicity},
  author={Brittany N. Flores and Mark E. Dulchavsky and Amy Krans and Michael R. Sawaya and Henry L. Paulson and Peter K. Todd and Sami J Barmada and Magdalena I. Ivanova},
  booktitle={PloS one},
  year={2016}
}
Hexanucleotide repeat expansions in C9orf72 are the most common inherited cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). The expansions elicit toxicity in part through repeat-associated non-AUG (RAN) translation of the intronic (GGGGCC)n sequence into dipeptide repeat-containing proteins (DPRs). Little is known, however, about the structural characteristics and aggregation propensities of the dipeptide units comprising DPRs. To address this question, we… CONTINUE READING
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