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Arginine valency in <i>C9ORF72</i> dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteins

2019-08-28

Abstract excerpt

<h4>ABSTRACT</h4> C9ORF72 -associated Motor Neuron Disease patients feature abnormal expression of 5 dipeptide repeat (DPR) polymers. Here we used quantitative proteomics in a Neuro2a cell model to demonstrate that the valency of Arg in the most toxic DPRS, PR and GR, drives promiscuous binding to the proteome, compared to a relative sparse binding of the more inert AP and GA. Notable targets included ribosomal p...

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Literature Corpus work
589f08cd-6c36-5733-ab89-6108c567053f
DOI
10.1101/749127
Open publication

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Arginine valency in <i>C9ORF72</i> dipolypeptides mediates promiscuous proteome binding that stalls ribosomes, disable actin cytoskeleton assembly and impairs arginine methylation of endogenous proteinsDOI 10.1101/749127
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