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Fig. 3 | Experimental Hematology & Oncology

Fig. 3

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

Fig. 3

Different domains, mutants, and isoforms of p53 related to aggregation. Top: The sites of aggregation-related mutations are indicated by the corresponding residues. The bars above show the relative frequencies of missense mutations at the residues according to version R20 (July 2019) of the International Agency for Research on Cancer (IARC) tumor suppressor protein p53 (TP53) Database (http://www-p53.iarc.fr/). Middle: The frames show the different domains of p53 related to aggregation; the blue arrow shows the aggregation-nucleating segment. Bottom: The arrows indicate the start point (N-terminus) of the isoforms; the terminal arrows represent the C-terminal isoform variants. Transactivation domain I (TAD I); transactivation domain II (TAD II); proline rich domain (PRD); DNA-binding domain (DBD); oligomerization domain (OD); C-terminal domain (CTD)

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