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ProteomicsCNS-derived extracellular vesicles from superoxide dismutase 1 (SOD1)G93A ALS mice originate from astrocytes and neurons and carry misfolded SOD1
Extracellular vesicles (EVs) are secreted by myriad cells in culture and also by unicellular organisms, and their identification in mammalian fluids suggests that EV release also occurs at the organism level. However, although it is clearly important to better understand EVs' roles in organismal...
ORGANISM(S): Mus musculus (Mouse) 
2020-09-11 | PXD021396 | Pride
Exosome (vesicle) Secretion Mouse model Proteomics Protein homeostasis Amyotrophic lateral sclerosis (als) (lou gehrig disease) Extracellular vesicles Central nervous system (cns) Neurodegeneration Astrocyte 
TranscriptomicsProfiling wt SOD versus ALS SOD1(G93A) mutant
Whole-genome profiling of SH-SY5Y cells was done on neuroblastoma SH-SY5Y stably transfected with cDNAs coding for SOD1WT or the mutant SOD1(G93A) protein. Five wt SOD versus five mutant SOD
ORGANISM(S): Homo sapiens 
2010-12-22 | E-GEOD-21298 | biostudies-arrayexpress
TranscriptomicsTranscription profiling by array of E. coli BL21(DE3)::TN7T7 -SOD to analyze the cellular response of this plasmid-free expression system to high level expression of recombinant human super-oxide-dismutase
This transcription profiling time course experiment was conducted in order to analyze the cellular response of the plasmid-free expression system E.coli BL21(DE3)::TN7 to high level expression of recombinant human super-oxide-dismutase (SOD).Three biological replicates were generated by usi...
ORGANISM(S): Escherichia coli 
2013-05-31 | E-MARS-24 | biostudies-arrayexpress
Proteomicssuperoxide dismutase 1 (SOD1) trimer interactome from mouse brain, spinal cord, and muscle tissues
In this work, we aimed to discover the protein binding partners of SOD1 trimers in brain, spinal cord, and skeletal muscle of mice tissue lysate.
ORGANISM(S): Mus musculus (Mouse) 
2025-10-06 | PXD050873 | Pride
Oligomers Interactome Sod1 
TranscriptomicsTranscriptome Profiling following Neuronal and Glial Expression of ALS-linked SOD1 in Drosophila
Amyotrophic Lateral Sclerosis (ALS) is generally a late onset neurodegenerative disease. Mutations in the Cu/Zn superoxide dismutase 1 (SOD1) gene accounts for approximately 20% of familial ALS and 2% of all ALS cases. Although a number of hypothesis have been proposed to explain mutant SOD1 toxic...
ORGANISM(S): Drosophila melanogaster 
2012-06-30 | E-GEOD-37148 | biostudies-arrayexpress
ProteomicsMisfolded SOD1 binds the ubiquitin ligase TRAF6
Amyotrophic lateral sclerosis (ALS) is a fatal disease, characterized by the selective loss of motor neurons. Mutations in Cu/Zn superoxide dismutase (SOD1) are the second most common cause of ALS and it is now well accepted that they result in a gain of toxicity due to protein misfolding. We previo...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-02-24 | PXD015279 | Pride
Tnf receptor-associated factor 6 (traf6) Superoxide dismutase 1 (sod1) Mitochondria Protein misfolding Ubiquitin Amyotrophic lateral sclerosis (als) Aggregation 
TranscriptomicsLCMV infection of Sod1-/- vs. WT mice
Study of host-virus interaction in the liver of Superoxide dismutase 1 (Sod1) deficient mice vs. wildtype mice.
ORGANISM(S): Mus musculus 
2015-11-17 | E-MTAB-2351 | biostudies-arrayexpress
TranscriptomicsmiRNA expression in fast and slow skeletal muscle of wild type and SOD1-G93A mice
Amyotrophic lateral sclerosis (ALS) is a lethal motor neuron disease that progressively debilitates neuronal cells that control voluntary muscle activity. In a mouse model of ALS that expresses mutated human superoxide dismutase 1 (SOD1-G93A) skeletal muscle is one of the tissues affected early by m...
ORGANISM(S): Mus musculus 
2014-03-04 | E-GEOD-55507 | biostudies-arrayexpress
ProteomicsAmyotrophic Lateral Sclerosis-associated Mutants of SOD1 Modulate miRNA Biogenesis through Aberrant Interactions with Exportin 5
Mutations in SOD1 (Superoxide Dismutase 1) gene are associated with amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disease. By employing ascorbate peroxidase (APEX)-based proximity labeling, coupled with LC-MS/MS analysis, we uncovered 37 and 28 proteins exhibiting higher abundance i...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2024-01-26 | PXD035452 | Pride
Lc-ms affinity purification sod1 apex 
UnknownAcylation of Superoxide Dismutase 1 (SOD1) at K122 Governs SOD1-Mediated Inhibition of Mitochondrial Respiration.
Not available
S-EPMC5615182 | biostudies-literature
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