Evidence map›Paper›PMID 39799258›Full record

ReviewMolecular diversity2025

Small molecules that targeting p53 Y220C protein: mechanisms, structures, and clinical advances in anti-tumor therapy.

Jinglei Xu, Jiahao Yuan, Wenxin Wang, Xiaoning Zhu, Jialong Li, Yule Ma, Shaojie Liu, Jie Feng, Yadong Chen, Tao Lu and 1 more

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular diversity, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Jinglei XuSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Jiahao YuanSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Wenxin WangSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Xiaoning ZhuSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Jialong LiSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Yule MaSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Shaojie LiuSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Jie FengSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Yadong ChenSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China.
Tao LuSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China. lutao@cpu.edu.cn.
Hongmei LiSchool of Sciences, China Pharmaceutical University, 639 Longmian Avenue, Nanjing, 211198, People's Republic of China. lihongmei@cpu.edu.cn.

Funding

"Double First-Class" Young Talents Research and Innovation Team Project CPUQNJC22_06Jiangsu Province Natural Science Funds BK20242074National Natural Science Foundation of China 82173692
6 · The paper itself

Abstract

The p53 protein is regarded as the "Guardian of the Genome," but its mutation is tumor progression and present in more than half of malignant tumors. The pro-metastatic property of mutant p53 makes a strong argument for targeting mutant p53 with new therapeutic strategies. However, mutant p53 was considered as a challenging target for drug discovery due to the lack of small molecular binding pockets. Among them, mutant p53 Y220C creates a narrow crevice since the side chains dynamics on protein surface, which is suitable for designing small molecules to occupy the cavity and recovery the tumor suppressing function. Here, we describe the mechanism of p53 related signal pathway and how p53 Y220C regulate the tumorigenesis. We review the two types of p53 Y220C modulators including restoring the conformation of mutant p53 Y220C protein to wild-type p53 protein and recruiting histone acetyltransferase p300/CBP to acetylate p53 Y220C thus enables p53 Y220C dependent upregulation of apoptotic genes and downregulation of DNA damage response pathways. We also report clinical advances and challenges of these molecules in p53 Y220C medicated tumor therapy.

Indexed as

Antineoplastic AgentsNeoplasmsSmall Molecule LibrariesTumor Suppressor Protein p53AnimalsHumansMolecular Targeted TherapyMutationSignal TransductionAntineoplastic AgentsSmall Molecule LibrariesTumor Suppressor Protein p53p53 Y220CRestoration of conformationSmall molecule activatorsTumor

Identifiers

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.