File:Journal.pone.0001677.g006.png
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| Description | Formation of soluble oligomers occuring when apo WT SOD1 protein is kept close to physiological conditions for an extended period of time. In the absence of metal ions, SOD1 proteins form abnormal disulfide cross-links though the two free cysteines (Cys 6 and Cys 111) and noncovalent associations with other SOD1 monomers or dimers. |
| Date | |
| Source | SOD1 and Amyotrophic Lateral Sclerosis: Mutations and Oligomerization [1] |
| Author | Lucia Banci et al |
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| current | 23:04, 15 May 2008 | | 2,989 × 2,160 (1.72 MB) | Filip em (talk | contribs) | {{Information |Description=Formation of soluble oligomers occuring when apo WT SOD1 protein is kept close to physiological conditions for an extended period of time. In the absence of metal ions, SOD1 proteins form abnormal disulfide cross-links though th |
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