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. 2010 Aug 25;1(10):655–660. doi: 10.1021/cn100067e

Figure 1.

Figure 1

Relative chymotrypsin-like activity of the h20S proteasome with or without the presence of 10 μM fibrillar, oligomeric, or monomeric Aβ(1−42). Statistically significant differences were found for all three assembly states of Aβ(1−42) compared with activity in the absence of Aβ peptide. Statistical significance denoted as *p < 0.01, **p < 0.001. Each data point represents the average from three independent runs.