Evidence map›Paper›PMID 29295817›Full record

ArticleEMBO reports2018

Regulation of the Mdm2-p53 pathway by the ubiquitin E3 ligase MARCH7.

Kailiang Zhao, Yang Yang, Guang Zhang, Chenfeng Wang, Decai Wang, Mian Wu, Yide Mei

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in EMBO reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.5field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Long noncoding RNAs in ubiquitination, protein degradation, and human diseases.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  11. Review
  12. Review
  13. Article
  14. MLF2 Negatively Regulates P53 and Promotes Colorectal Carcinogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Ubiquitin ligases: guardians of mammalian development.Nature reviews. Molecular cell biology · 2022
    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

7 authors at 1 institution in 1 country.

Kailiang ZhaoCAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science & Technology of China, Hefei, Anhui, China.
Yang YangCAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science & Technology of China, Hefei, Anhui, China.
Guang ZhangCAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science & Technology of China, Hefei, Anhui, China.
Chenfeng WangCAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science & Technology of China, Hefei, Anhui, China.
Decai WangCAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science & Technology of China, Hefei, Anhui, China.
Mian WuCAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science & Technology of China, Hefei, Anhui, China wumian@ustc.edu.cn meiyide@ustc.edu.cn.ORCID 0000-0002-2714-0500
Yide MeiCAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science & Technology of China, Hefei, Anhui, China wumian@ustc.edu.cn meiyide@ustc.edu.cn.ORCID 0000-0002-8670-7394
University of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tumor suppressor p53 plays a prominent role in the protection against cancer. The activity of p53 is mainly controlled by the ubiquitin E3 ligase Mdm2, which targets p53 for proteasomal degradation. However, the regulation of Mdm2 remains not well understood. Here, we show that MARCH7, a RING domain-containing ubiquitin E3 ligase, physically interacts with Mdm2 and is essential for maintaining the stability of Mdm2. MARCH7 catalyzes Lys

Indexed as

AnimalsDNA DamageHCT116 CellsHEK293 CellsHumansMaleMiceMice, NudeProtein BindingProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p53UbiquitinationUbiquitin-Protein LigasesMARCHF7 protein, humanMDM2 protein, humanProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p53Ubiquitin-Protein LigasesMARCH7Mdm2p53ubiquitination

Identifiers

PMID29295817
PMCPMC5797962
OpenAlexW2781926636

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.