Evidence map›Paper›PMID 33277368›Full record

ArticleCancer research2021

MDMX Recruits UbcH5c to Facilitate MDM2 E3 Ligase Activity and Subsequent p53 Degradation

Jing Yang, Aiwen Jin, Jing Han, Xin Chen, Junnian Zheng, Yanping Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.5field-weighted citation impact, top 15% 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

31 citing papers in PubMed, 40 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Jing YangDepartment of Radiation Oncology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina. ypzhang@med.unc.edu jingyang@xzhmu.edu.cn zhengjunnian@sina.com.
Aiwen JinDepartment of Radiation Oncology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
Jing HanDepartment of Radiation Oncology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
Xin ChenDepartment of Radiation Oncology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
Junnian ZhengCenter of Clinical Oncology, Affiliated Hospital of Xuzhou Medical University, Xuzhou Medical University, Xuzhou, Jiangsu, China. ypzhang@med.unc.edu jingyang@xzhmu.edu.cn zhengjunnian@sina.com.
Yanping ZhangDepartment of Radiation Oncology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina. ypzhang@med.unc.edu jingyang@xzhmu.edu.cn zhengjunnian@sina.com.
University of North Carolina at Chapel Hill · USXuzhou Medical College · CN

Funding

In vivo regulation of p53 by MDM2 and MDMXR01CA212407 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YANPING · 2017 to 2021
$1.9M
Mitochondrial p32 regulation of the Mdm2-p53 tumor suppression signaling and apopR01CA155235 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YANPING · 2012 to 2016
$1.5M
The in vivo role of the Mdm2-MdmX interaction in p53 regulationR01CA167637 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YANPING · 2012 to 2016
$1.5M
In vivo function of Mdm2 E3 ubiquitin ligaseR01CA127770 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YANPING · 2008 to 2013
$1.5M
NCI NIH HHS R01 CA127770NCI NIH HHS R01 CA155235NCI NIH HHS R01 CA167637NCI NIH HHS R01 CA212407
6 · The paper itself

Abstract

MDM2 regulates p53 degradation by functioning as an E3 ubiquitin ligase. The role of MDMX, an MDM2 homolog that lacks E3 ligase activity, in the regulation of p53 degradation remains incompletely understood and sometime controversial. This confusion is due at least in part to studies of p53 degradation mainly carried out in

Indexed as

AnimalsCell Cycle ProteinsCells, CulturedEnzyme ActivationHumansMCF-7 CellsMiceMice, TransgenicProtein BindingProteolysisProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p53Ubiquitin-Conjugating EnzymesUbiquitin-Protein LigasesCell Cycle ProteinsMDM2 protein, humanMDM4 protein, humanProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2TP53 protein, humanTumor Suppressor Protein p53UBE2D3 protein, humanUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID33277368
PMCPMC8026549
OpenAlexW3108826619

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.