Arginine in C9ORF72 Dipolypeptides Mediates Promiscuous Proteome Binding and Multiple Modes of Toxicity期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Arginine in C9ORF72 Dipolypeptides Mediates Promiscuous Proteome Binding and Multiple Modes of Toxicity

Institution:	3. Department of Biochemistry and Molecular Biology; and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, VIC 3010, Australia;4. Bio21 Mass Spectrometry and Proteomics Facility, The University of Melbourne, Parkville, Victoria, Australia;5. School of Chemistry, The University of Melbourne, VIC 3010, Australia

Abstract:	Download : Download high-res image (208KB) Download : Download full-size image Highlights ?Quantitative proteome interactions with 5 different C9ORF72 dipolypeptides (DPRs). ?The arg-rich DPRs promiscuously bound to the proteome compared with the other DPRs. ?Long repeat lengths of arg-rich DPRs, but not short lengths, stalled ribosomes. ?The arg-rich DPRs also reduced arginine methylation and actin cytoskeleton assembly.

Keywords:	Neurodegenerative diseases protein-protein interactions methylation translation protein identification molecular biology networks amyotrophic lateral sclerosis (ALS) methylosome protein aggregation proteotoxicity RAN-translation
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