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UnknownInteractome screening of C9orf72 dipeptide repeats reveals VCP sequestration and functional impairment by polyGA.
Not available
S-EPMC9014755 | biostudies-literature
ProteomicsInteractome screening of C9orf72 dipeptide repeats reveals sequestration and functional impairment of VCP by polyGA
Repeat expansions in the C9orf72 gene are a common cause of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), two devastating neurodegenerative disorders. One of the proposed mechanisms of GGGGCC repeat expansion is their translation to produce unnatural dipeptide rep...
ORGANISM(S): Homo sapiens (Human) 
2022-05-19 | PXD024120 | Pride
Proximity labeeling Proteomics Amyotrophic lateral sclerosis Als Valosin-containing protein Vcp Bioid Neurodegeneration Dipeptide repeats 
UnknownPolyGA targets the ER stress-adaptive response by impairing GRP75 function at the MAM in C9ORF72-ALS/FTD.
Not available
S-EPMC9547809 | biostudies-literature
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 
UnknownGlycine-alanine dipeptide repeats spread rapidly in a repeat length- and age-dependent manner in the fly brain.
Not available
S-EPMC6916080 | biostudies-literature
UnknownImmiscible inclusion 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.
Not available
S-EPMC7455042 | biostudies-literature
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 
UnknownRepeat length of C9orf72-associated glycine-alanine polypeptides affects their toxicity.
Not available
S-EPMC10463776 | biostudies-literature
ProteomicsRepeat length of the C9orf72-associated glycine-alanine polypeptides affects their toxicity
G4C2 hexanucleotide repeat expansions in a non-coding region of the C9orf72 gene are the most common cause of familial amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). G4C2 insertion length is variable, and patients can carry up to several thousand repeats. Dipeptide repeat pro...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2023-09-12 | PXD038900 | Pride
Toxicity Repeat length Drosophila C9orf72 Glycine-alanine 
UnknownReduced autophagy upon C9ORF72 loss synergizes with dipeptide repeat protein toxicity in G4C2 repeat expansion disorders.
Not available
S-EPMC7024836 | biostudies-literature
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