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. 2016 Mar 2;6:22298. doi: 10.1038/srep22298

Figure 4. PKUMDL-YC-1205 blocks the interaction between c-Myc370–409 and Max.

Figure 4

(a) PKUMDL-YC-1205 abolished cMyc370–409 binding to Max in the SPR competitive assay at the indicated concentrations. (b) PKUMDL-YC-1205 disrupted the Max-Max/c-Myc-Max dimerization equilibrium. Chemical cross-linking and anti-Max western blotting results are shown (left). Blackness integrals of the GST-Max homodimer percentage are shown as a histogram (right). Data represent the mean ± standard deviation of two independent experiments. *p < 0.05.