Evidence map›Paper›PMID 23150760›Full record

ArticleGenes & cancer2012

The Roles of MDM2 and MDMX Phosphorylation in Stress Signaling to p53.

Jiandong Chen

Open access · bronzeAbstract read
In one paragraph

Article in Genes & cancer, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Therapeutics Targeting p53-MDM2 Interaction to Induce Cancer Cell Death.International journal of molecular sciences · 2022
    Review
  5. Article
  6. The MDM2/MDMX/p53 axis in the adaptive stress response.Translational cancer research · 2020
    Review
  7. Article
  8. MDMX acidic domain inhibits p53 DNA binding in vivo and regulates tumorigenesis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Inhibition of Mdmx (Mdm4)Oncotarget · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

1 author at 1 institution in 1 country.

Jiandong ChenMolecular Oncology Department, Moffitt Cancer Center, Tampa, FL, USA.
Moffitt Cancer Center · US

Funding

Mechanisms of p53 activation during stress response (MPI)R01CA141244 · NCI · H. LEE MOFFITT CANCER CTR & RES INST · PI JIANDONG CHEN, Gary W Daughdrill · 2009 to 2026
$5.3M
Function and Regulation of MDMXR01CA109636 · NCI · H. LEE MOFFITT CANCER CTR &RES INST · PI CHEN, JIANDONG · 2004 to 2014
$2.8M
NCI NIH HHS R01 CA109636NCI NIH HHS R01 CA141244
6 · The paper itself

Abstract

The p53 tumor suppressor is highly responsive to different physiological stresses such as abnormal cell proliferation, nutrient deprivation, and DNA damage. Distinct signaling mechanisms have evolved to activate p53, which in turn modulate numerous pathways to enhance fitness and survival of the organism. Elucidating the molecular mechanisms of these signaling events is critical for understanding tumor suppression by p53 and development of novel therapeutics. Studies in the past decade have established that MDM2 and MDMX are important targets of signaling input from different pathways. Here, we focus our discussion on MDM2 and MDMX phosphorylation, which is important for p53 activation by DNA damage. Investigations in this area have generated new insight into the inner workings of MDM2 and MDMX and underscore the importance of allosteric communication between different domains in achieving an efficient response to phosphorylation. It is likely that MDM2 and MDMX regulation by phosphorylation will share mechanistic similarities to other signaling hub molecules. Phosphorylation-independent p53 activators such as ARF and ribosomal proteins ultimately achieve the same outcome as phosphorylation, suggesting that they may induce similar changes in the structure and function of MDM2 and MDMX through protein-protein interactions.

Indexed as

MDM2MDMXp53phosphorylationubiquitination

Identifiers

PMID23150760
PMCPMC3494364
OpenAlexW2138187945

What OpenQuestion 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 OpenQuestion graph.