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ProteomicsInclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation
Poly(glycine-alanine) (polyGA) is one of the dipolypeptides expressed in Motor Neuron Disease caused by C9ORF72 mutations and accumulates as inclusion bodies in the brain of patients. Superficially these inclusions are similar to those formed by polyglutamine (polyQ) in Huntington’s disease and bot...
ORGANISM(S): Mus musculus (Mouse) 
2020-08-18 | PXD018505 | Pride
Huntington C9orf72 Chaperones Proteosome Inclusions 
ProteomicsInclusion bodies formed by polyglutamine and poly(glycine-alanine) are enriched with distinct proteomes but converge in proteins that are risk factors for disease and involved in protein degradation
Poly(glycine-alanine) (polyGA) is one of the dipolypeptides expressed in Motor Neuron Disease caused by C9ORF72 mutations and accumulates as inclusion bodies in the brain of patients. Superficially these inclusions are similar to those formed by polyglutamine (polyQ) in Huntington’s disease and both...
ORGANISM(S): Mus musculus (Mouse) 
2020-08-18 | PXD018824 | Pride
Huntington Aggregates C9prf72 Polyga 
ProteomicsArginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that transmits multiple modes of toxicity
Motor Neuron Disease patients with the C9ORF72 hexanucleotide expansion mutations feature abnormal expression of 5 different dipeptide repeat polymers (DPRs). Two of these, poly-GR and poly-PR, have proven highly toxic to cell and animal models. To investigate the mechanisms, we defined the interact...
ORGANISM(S): Mus musculus (Mouse) 
2020-02-25 | PXD015177 | Pride
Ran-translation  amyotrophic lateral sclerosis (als)  proteotoxicity  protein aggregation  abce1  methylosome  prmt1  prmt5 
ProteomicsArginine valency in C9ORF72 dipolypeptides mediates promiscuous proteome binding that transmits multiple modes of toxicity
C9ORF72-associated Motor Neuron Disease patients feature abnormal expression of 5 dipeptide repeat (DPR) polymers. Here we used quantitative proteomics in a mouse neuronal-like cell line (Neuro2a) to demonstrate that the valency of Arg in the most toxic DPRS, PR and GR, drives promiscuous binding to...
ORGANISM(S): Mus musculus (Mouse) 
2020-02-25 | PXD015180 | Pride
Ran-translation  amyotrophic lateral sclerosis (als)  proteotoxicity  protein aggregation  abce1  methylosome  prmt1  prmt5 
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