Fig. 6: MIF inhibition of mutant SOD1 misfolding is independent of its enzymatic activities or its normal oligomeric transitions | Cell Death & Disease

Fig. 6: MIF inhibition of mutant SOD1 misfolding is independent of its enzymatic activities or its normal oligomeric transitions

From: MIF inhibits the formation and toxicity of misfolded SOD1 amyloid aggregates: implications for familial ALS

Fig. 6: MIF inhibition of mutant SOD1 misfolding is independent of its enzymatic activities or its normal oligomeric transitions

a Schematic diagram of the experiment. b The accumulation of misfolded SOD1 was determined by immunoblotting of immunoprecipitates with the A5C3 antibody after incubating recombinant hSOD1G85R (4 µg) with (+) or without (–) recombinant MIFWT, MIFC60S, MIFP2A, or MIFN110C (all at 2 µg). Immunoblotting was used to determine the levels of SOD1 and MIF that remained in the unbound fraction of each immunoprecipitation assay. This immunoblot is representative of three independent experiments.

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