Ask about this productRelated genes to: SOD1 antibody
- Gene:
- SOD1 NIH gene
- Name:
- superoxide dismutase 1
- Previous symbol:
- ALS, ALS1
- Synonyms:
- IPOA
- Chromosome:
- 21q22.11
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2019-04-23
Related products to: SOD1 antibody
Related articles to: SOD1 antibody
- Medicinal plants have been the most important component of agro-ecosystems and the natural environment from the very beginning of life. Air, water, and soil have been significantly contaminated, adversely affecting the production and development of plants. Homa therapy, based on traditional Vedic knowledge, purportedly restores balance to nature and eliminates environmental pollutants. However, this approach must be comprehended in light of current scientific findings. - Source: PubMed
Publication date: 2026/05/15
Sharad PriyaMasood ShireenMasood OsaidKumari AlkaBerk UlrichBanerjee Monisha - Amyotrophic lateral sclerosis (ALS) is a debilitating and fatal neurodegenerative disease characterised by the progressive loss of motor functions affecting both upper and lower motor neurons. Although considered multifactorial with an unclear aetiology, it is believed that the interplay between genetic and environmental factors, with neuroinflammation playing a key role in disease progression, contributes to its development. There is currently no effective treatment for ALS. Curcumin has been recently highlighted for its potential therapeutic role in treating neurodegenerative diseases. Curcumin phospholipids, a highly bioavailable form of curcumin that allow the curcumin to be absorbed into the bloodstream more effectively than standard curcumin extracts, is considered as a natural cytokine-suppressive anti-inflammatory compound (CSAID) that is well-known for its therapeutic properties and is considered safe for humans and rodents at low to moderate concentrations. In this study, we investigated whether a long-term feeding regimen incorporating curcuminoids phospholipids-enriched diet early in disease progression could mitigate motor deficits and affect the lifespan of the SOD1 mouse model of familial ALS (fALS). Our results indicate sex-differences regarding the effect of curcumin supplementation on motor deficits and anxiety-like behaviour. While long-term feeding with curcuminoids phospholipids enriched diet had a complex effect on SOD1 female mice expressed as reduced anxiety like behaviour and motor deficits at the walking beam test, it had no effect on SOD1 male mice. Moreover, curcuminoids supplementation had a limited effect on disease onset and progression in SOD1 mice model for fALS. - Source: PubMed
Publication date: 2026/05/13
Purushotham Sushmitha SomanahalliChesworth RoseKeembiyage NisalMünch GeraldGyengesi ErikaBuskila Yossi - Mitochondria divide and fuse, and the balance between these processes maintains mitochondrial morphology and function. Although the core fusion and division machinery is well established, how cells sense mitochondrial morphology and actively adjust it remains unclear. In this Opinion article, we propose a new conceptual framework, termed 'Mitochondrial Safeguard (MitoSafe)', in which cells monitor mitochondrial size and rebalance division and fusion through four branches: activation of fusion or inhibition of division in small mitochondria and activation of division or inhibition of fusion in enlarged mitochondria. Recent findings show that fusion is suppressed once mitochondria exceed a healthy size threshold. Dysregulation of this branch of MitoSafe, involving Parkin, PINK1, SLC25A3, SOD1, and cytochrome-c oxidase, causes mitochondrial enlargement, mitochondrial DNA release, and stimulator of interferon genes (STING)-mediated inflammation. - Source: PubMed
Publication date: 2026/05/13
Haggerty NoraNakamura KentaroSesaki HiromiIijima Miho - TDP43 inclusion bodies are widely present in the majority of patients with familial and sporadic amyotrophic lateral sclerosis (ALS). The mechanisms regulating TDP43 solubility remain incompletely understood. Here, we report that TDP43 undergoes S-acylation primarily at the Cys244 residue by the S-acyltransferase zDHHC23. This S-acylation maintains the liquid-like properties of TDP43 by reducing the aberrant interaction with poly(ADP-ribose) polymerase 1 (PARP1) and PARylated proteins, thereby countering the pathological condensation of TDP43. S-acylation-deficient TDP43 inclusions sequester the translational machinery and inhibit cytoplasmic protein translation, ultimately resulting in neurotoxicity. Importantly, TDP43 S-acylation is decreased in the familial ALS-associated TDP43 mutants as well as in SOD1-G93A mice and C9orf72-ALS induced pluripotent stem cell (iPSC)-derived neurons, suggesting the widespread involvement of TDP43 S-acylation in ALS pathogenesis. Our findings reveal an undescribed modification of TDP43 and provide deeper insight into the regulation of TDP43 pathological condensation in ALS. - Source: PubMed
Publication date: 2026/05/12
Xu WentaoLi HuinaZhang WeiBai GeShen ChengyongZhang Kejing - Aberrant protein oligomerization is a hallmark of neurodegenerative disorders, yet the conformational and kinetic underpinnings of early aggregation remain poorly understood due to the inability of structural techniques to capture transient, low-abundance oligomeric intermediates. This necessitates the development of a methodology that can characterize the conformational states related to protein unfolding and thus allow for the investigation of the molecular mechanism responsible for disease progression. Here, we demonstrate how temperature-controlled nanoelectrospray ionization (TC-nESI) combined with high-resolution ion mobility-mass spectrometry (IM-MS), surface-induced dissociation (SID), and limited proteolysis can be used to define the misfolding and oligomerization landscape of bovine Cu/Zn superoxide dismutase (SOD1). This integrative approach enables real-time detection of coexisting intermediates, and captures molecular events including metal-induced stability, monomer unfolding and assembly into heterogeneous soluble oligomers. Our results reveal that both holo- and apo-SOD1 undergo dimer dissociation followed by monomer misfolding and assembly into heterogeneous non-native oligomers, and that slow thermal ramping promotes the accumulation of misfolded monomers and higher-order complexes. Apo-SOD1 that lacks stabilizing metal cofactors, forms more compact and kinetically distinct oligomers via monomeric, dimeric and trimeric intermediates. Proteolysis and heat-induced fragmentation identify loops V, VI, VII, and the C-terminus as key labile regions contributing to oligomer interface formation, predominantly through hydrophobic interactions. Our findings establish a mechanistically rich model for early aggregation and demonstrate the capability of TC-nESI-IM-MS to temporally and structurally resolve misfolding transitions and oligomeric populations in a single experiment. This platform provides a framework to dissect oligomerization pathways relevant to neurodegenerative diseases. - Source: PubMed
Publication date: 2026/05/13
Svingou DespoinaMcAlary LukeHarrison Julian AlexanderZenobi Renato