ArticlePloS one2012
Role of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Impact of cysteine mutations on the structural dynamics and functional impairment of SOD1: insights into the pathogenicity of amyotrophic lateral sclerosis.Genomics & informatics · 2025Article
- Tryptophan residue 32 in human Cu-Zn superoxide dismutase modulates prion-like propagation and strain selection.PloS one · 2020Article
- Experimental Mutations in Superoxide Dismutase 1 Provide Insight into Potential Mechanisms Involved in Aberrant Aggregation in Familial Amyotrophic Lateral Sclerosis.G3 (Bethesda, Md.) · 2019Article
- Quantum chemical and molecular mechanics studies on the assessment of interactions between resveratrol and mutant SOD1 (G93A) protein.Journal of computer-aided molecular design · 2018Article
- Article
- Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43Scientific reports · 2017Article
- Parsing disease-relevant protein modifications from epiphenomena: perspective on the structural basis of SOD1-mediated ALS.Journal of mass spectrometry : JMS · 2017Article
- Relationship between mutant Cu/Zn superoxide dismutase 1 maturation and inclusion formation in cell models.Journal of neurochemistry · 2017Article
- Cellular Redox Systems Impact the Aggregation of Cu,Zn Superoxide Dismutase Linked to Familial Amyotrophic Lateral Sclerosis.The Journal of biological chemistry · 2016Article
- Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1.The Journal of biological chemistry · 2014Article
- Analysis of mutant SOD1 electrophoretic mobility by Blue Native gel electrophoresis; evidence for soluble multimeric assemblies.PloS one · 2014Article
- A structural modeling approach for the understanding of initiation and elongation of ALS-linked superoxide dismutase fibrils.Journal of molecular modeling · 2013Article
- Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins.International journal of cell biology · 2013Review
- Disulfide bonding in neurodegenerative misfolding diseases.International journal of cell biology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundPathologic aggregates of superoxide dismutase 1 (SOD1) harboring mutations linked to familial amyotrophic lateral sclerosis (fALS) have been shown to contain aberrant intermolecular disulfide cross-links. In prior studies, we observed that intermolecular bonding was not necessary in the formation of detergent- insoluble SOD1 complexes by mutant SOD1, but we were unable to assess whether this type of bonding may be important for pathologic inclusion formation. In the present study, we visually assess the formation of large inclusions by fusing mutant SOD1 to yellow fluorescent protein (YFP). METHODOLOGY/PRINCIPAL
findingsExperimental constructs possessing mutations at all cysteine residues in SOD1 (sites 6, 57, 111, and 146 to F,S,Y,R or G,S,Y,R, respectively) were shown to maintain a high propensity of inclusion formation despite the inability to form disulfide cross-links. Interestingly, although aggregates form when all cysteines were mutated, double mutants of the ALS mutation C6G with an experimental mutation C111S exhibited low aggregation propensity. CONCLUSIONS/SIGNIFICANCE: Overall, this study is an extension of previous work demonstrating that cysteine residues in mutant SOD1 play a role in modulating aggregation and that intermolecular disulfide bonds are not required to produce large intracellular inclusion-like structures.
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