Fig. 8: Model of the oxidation-induced amyloid formation and disassembly mechanism of p16. | Nature Communications

Fig. 8: Model of the oxidation-induced amyloid formation and disassembly mechanism of p16.

From: Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism

Fig. 8

Helices in blue represent the native fold of p16 and the orange represents refolded fibrillar β-sheets with the stabilizing intermolecular disulfide bond. In the amyloid state, p16 is unable to inhibit CDK4/6 (green). Reduction of disulfide bonds triggers amyloid disassembly and refolding to the active p16 monomer which is capable of inhibiting CDK4/6 (red).

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