Evidence map›Paper›PMID 25201201›Full record

ReviewSub-cellular biochemistry2014

Targeting p53-MDM2-MDMX loop for cancer therapy.

Qi Zhang, Shelya X Zeng, Hua Lu

Abstract readReview
In one paragraph

Review in Sub-cellular biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 1 pooled it
23.1field-weighted citation impact, top 1% of its field
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

54 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Development of MDM2-Targeting PROTAC for Advancing Bone Regeneration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Study ofMolecules (Basel, Switzerland) · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Qi ZhangDepartment of Biochemistry & Molecular Biology and Tulane Cancer Center, Tulane University School of Medicine, 1430 Tulane Ave, Louisiana, LA, 70112, USA.
Shelya X Zeng
Hua Lu
Tulane University · US

Funding

The Role of Ribosomal Proteins in the P53-MDM2 PathwayR01CA095441 · NCI · TULANE UNIVERSITY OF LOUISIANA · PI LU, HUA · 2002 to 2021
$5.1M
MOLECULAR DISSECTION OF A NOVEL P53 LIKE PROTEINR01CA079721 · NCI · OREGON HEALTH & SCIENCE UNIVERSITY · PI LU, HUA · 1999 to 2006
$1.8M
Role of ribosomal proteins in regulating c-MycR01CA129828 · NCI · TULANE UNIVERSITY OF LOUISIANA · PI LU, HUA · 2008 to 2012
$1.5M
Dual Targeting of the p53 pathway for development of anti-cancer therapyR01CA172468 · NCI · TULANE UNIVERSITY OF LOUISIANA · PI LU, HUA · 2012 to 2016
$1.5M
NCI NIH HHS CA079721NCI NIH HHS CA095441NCI NIH HHS CA172468NCI NIH HHS R01 CA079721NCI NIH HHS R01 CA095441NCI NIH HHS R01 CA129828NCI NIH HHS R01 CA172468
6 · The paper itself

Abstract

The tumor suppressor p53 plays a central role in anti-tumorigenesis and cancer therapy. It has been described as "the guardian of the genome", because it is essential for conserving genomic stability by preventing mutation, and its mutation and inactivation are highly related to all human cancers. Two important p53 regulators, MDM2 and MDMX, inactivate p53 by directly inhibiting its transcriptional activity and mediating its ubiquitination in a feedback fashion, as their genes are also the transcriptional targets of p53. On account of the importance of the p53-MDM2-MDMX loop in the initiation and development of wild type p53-containing tumors, intensive studies over the past decade have been aiming to identify small molecules or peptides that could specifically target individual protein molecules of this pathway for developing better anti-cancer therapeutics. In this chapter, we review the approaches for screening and discovering efficient and selective MDM2 inhibitors with emphasis on the most advanced synthetic small molecules that interfere with the p53-MDM2 interaction and are currently on Phase I clinical trials. Other therapeutically useful strategies targeting this loop, which potentially improve the prospects of cancer therapy and prevention, will also be discussed briefly.

Indexed as

Genes, p53Antineoplastic AgentsCell Cycle ProteinsHumansNeoplasmsNuclear ProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Antineoplastic AgentsCell Cycle ProteinsMDM2 protein, humanMDM4 protein, humanNuclear ProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2

Identifiers

PMID25201201
PMCPMC4472007
OpenAlexW25654050

What OpenQuestion holds

Textmetadata
LicenceTDM
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 OpenQuestion graph.