| Literature DB >> 30213863 |
John Douglas Cleary1,2,3, Amrutha Pattamatta1,2,3, Laura P W Ranum4,2,3,5,6.
Abstract
Microsatellite expansions cause more than 40 neurological disorders, including Huntington's disease, myotonic dystrophy, and C9ORF72 amyotrophic lateral sclerosis/frontotemporal dementia (ALS/FTD). These repeat expansion mutations can produce repeat-associated non-ATG (RAN) proteins in all three reading frames, which accumulate in disease-relevant tissues. There has been considerable interest in RAN protein products and their downstream consequences, particularly for the dipeptide proteins found in C9ORF72 ALS/FTD. Understanding how RAN translation occurs, what cellular factors contribute to RAN protein accumulation, and how these proteins contribute to disease should lead to a better understanding of the basic mechanisms of gene expression and human disease.Entities:
Keywords: C9ORF72 ALS/FTD; Huntington's disease; RAN translation; amyotrophic lateral sclerosis (ALS) (Lou Gehrig disease); mouse models; myotonic dystrophy; nucleocytoplasmic transport; spinocerebellar ataxia; translation; translation initiation; trinucleotide repeat disease
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Year: 2018 PMID: 30213863 PMCID: PMC6200949 DOI: 10.1074/jbc.R118.003237
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157