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Apoprotein destabilisation is often considered insufficient to explain mutant SOD1 misfolding and aggregation, given mutant apoSOD1 stability is virtually unchanged (D101N, D125 H, S134N) or improved (H46R, D124V, V148I) for a number of WTL and MBR mutations compared with wildtype apo protein in vitro.[ 96a , 106 ] This conclusion, however, is based upon data derived from comparatively simple and tightly controlled experimental environments, where mutations are assumed to be the only destabilizing influence