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Fig. 1 | Experimental Hematology & Oncology

Fig. 1

From: p53 amyloid aggregation in cancer: function, mechanism, and therapy

Fig. 1

Illustration of p53 aggregation and the regulating factors. The scheme shows a potential route of aggregation, from the properly folded state, native state, to misfolded, aggregated forms of p53, including oligomers and amyloid fibrils. The main factors regulating p53 aggregation. (1) Some structural mutations, domains, and isoforms; (2) Chaperones, cochaperones, and some fiber stabilization factors are integrated into p53 amyloid aggregates, and abnormalities occur when they help p53-fold. (3) The protein state depends on the thermodynamic and kinetic factors in different environments. When the solution environment, such as Zn2+ concentration, pH, temperature, and pressure is changed, p53 may aggregate. (4) RNA molecules also modulate of p53 aggregation and seeding

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