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. Author manuscript; available in PMC: 2011 Oct 20.
Published in final edited form as: ACS Chem Neurosci. 2010 Oct 20;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 state of Aβ(1–42) compared to 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.