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ProteomicsDistinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N
We expressed and purified recombinant full-length wild-type human SOD1 and its G93A and D101N variants in Expi293F cells where the initiating Met was removed and the N-terminus at Ala1 was acetylated, and identified N-terminal acetylation of the mammalian cell–purified G93A , D101N , and wild-type S...
ORGANISM(S): Homo sapiens (Human) 
2025-10-20 | PXD066116 | Pride
Amyotrophic lateral sclerosis (als)  sod1 mutants  amyloid fibrils  cryo-em structure  toxicity. 
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 
ProteomicsAmyotrophic Lateral Sclerosis-Associated Mutants of SOD1 Perturb mRNA Splicing through Aberrant Interactions with SRSF2
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder that impacts neurons in the brain and spinal cord. Although a substantial number of studies have been conducted, much remains to be learned about the cellular mechanisms underlying ALS. In this study, we employed an engineered ascor...
ORGANISM(S): Homo sapiens (Human) 
2025-06-16 | PXD050785 | Pride
Sod1 Als Affinity pulldown Lc-msms 
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 
UnknownDistinct amyloid fibril structures formed by ALS-causing SOD1 mutants G93A and D101N.
Not available
S-EPMC12508129 | biostudies-literature
UnknownHuntingtin fragments and SOD1 mutants form soluble oligomers in the cell.
Not available
S-EPMC3386994 | biostudies-literature
UnknownAmyotrophic Lateral Sclerosis-Associated Mutants of SOD1 Perturb mRNA Splicing through Aberrant Interactions with SRSF2.
Not available
S-EPMC11412154 | biostudies-literature
ProteomicsPost-translational modification analysis of VDAC1 in ALS-SOD1 model cells reveals specific asparagine and glutamine deamination
Mitochondria from affected tissues of Amyotrophic Lateral Sclerosis (ALS) patients show morphological and biochemical abnormalities. The impairment of mitochondrial functions causes oxidative damage and accumulation of ROS and represents one of the major features that lead to the selective death of ...
ORGANISM(S): Mus musculus (Mouse) 
2020-12-10 | PXD022598 | Pride
Deamidation  amyotrophic lateral sclerosis  voltage dependent anion channel  post-translational modifications  mitochondria  ros  mass spectrometry analysis  orbitrap fusion tribrid  neurodegeneration  sod1 
UnknownAmyotrophic Lateral Sclerosis-Associated Mutants of SOD1 Modulate miRNA Biogenesis through Aberrant Interactions with Exportin 5.
Not available
S-EPMC9867941 | biostudies-literature
UnknownALS-causing SOD1 mutants generate vascular changes prior to motor neuron degeneration.
Not available
S-EPMC2895310 | biostudies-literature
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