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. 2022 Sep 28;11:66. doi: 10.1186/s40164-022-00317-7

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© The Author(s) 2022

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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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)