| First Author | Karch CM | Year | 2010 |
| Journal | Arch Biochem Biophys | Volume | 503 |
| Issue | 2 | Pages | 175-82 |
| PubMed ID | 20682279 | Mgi Jnum | J:169271 |
| Mgi Id | MGI:4940175 | Doi | 10.1016/j.abb.2010.07.027 |
| Citation | Karch CM, et al. (2010) Aggregation modulating elements in mutant human superoxide dismutase 1. Arch Biochem Biophys 503(2):175-82 |
| abstractText | Mutations in superoxide dismutase 1 (SOD1) cause some forms of familial amyotrophic lateral sclerosis (fALS). Affected tissues of patients and transgenic mouse models of the disease accumulate misfolded and aggregated forms of the mutant protein. In the present study we have identified specific sequences in human SOD1 that modulate the aggregation of fALS mutant proteins. From our study of a panel of mutant proteins, we identify two sequence elements in human SOD1 (residues 42-50 and 109-123) that are critical in modulating the aggregation of the protein. These sequences are components of the 4th and 7th beta-strands of the protein, and in the native structure are normally juxtaposed as elements of the core beta-barrel. Our data suggest that some type of intermolecular interaction between these elements may occur in promoting mutant SOD1 aggregation. |
