| Title |
Role of Disulfide Cross-Linking of Mutant SOD1 in the Formation of Inclusion-Body-Like Structures
|
|---|---|
| Published in |
PLOS ONE, October 2012
|
| DOI | 10.1371/journal.pone.0047838 |
| Pubmed ID | |
| Authors |
Brittany L. T. Roberts, Kinaree Patel, Hilda H. Brown, David R. Borchelt |
| Abstract |
Pathologic 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). |
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Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 1 | 100% |
Demographic breakdown
| Type | Count | As % |
|---|---|---|
| Members of the public | 1 | 100% |
Mendeley readers
The data shown below were compiled from readership statistics for 37 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 37 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 8 | 22% |
| Student > Bachelor | 5 | 14% |
| Student > Master | 5 | 14% |
| Student > Doctoral Student | 4 | 11% |
| Researcher | 4 | 11% |
| Other | 8 | 22% |
| Unknown | 3 | 8% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 17 | 46% |
| Biochemistry, Genetics and Molecular Biology | 6 | 16% |
| Neuroscience | 4 | 11% |
| Medicine and Dentistry | 3 | 8% |
| Chemistry | 2 | 5% |
| Other | 2 | 5% |
| Unknown | 3 | 8% |