Pub. Date : 2019 May 1
PMID : 30938419
3 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Here we report the inhibition of NMD by arginine-rich dipeptide repeats derived from C9orf72 hexanucleotide repeat expansion, the most common cause of familial amyotrophic lateral sclerosis. | Arginine | C9orf72-SMCR8 complex subunit | Homo sapiens |
| 2 | Using Drosophila as a model, we have validated that the C9orf72 hexanucleotide repeat expansion products could lead to the accumulation of the NMD substrates and identified arginine-rich dipeptide repeats, including poly glycine-arginine and poly proline-arginine, as the main culprits of NMD inhibition. | Arginine | C9orf72-SMCR8 complex subunit | Homo sapiens |
| 3 | Therefore, our study has revealed a cellular mechanism whereby arginine-rich C9orf72 dipeptide repeats could inhibit NMD activities by reducing the abundance of processing bodies. | Arginine | C9orf72-SMCR8 complex subunit | Homo sapiens |