Evidence map›Paper›PMID 23903585›Full record

ArticleScientific reports2013

Cadmium is a potent inhibitor of PPM phosphatases and targets the M1 binding site.

Chang Pan, Hong-Da Liu, Zheng Gong, Xiao Yu, Xu-Ben Hou, Di-Dong Xie, Xi-Bin Zhu, Hao-Wen Li, Jun-Yi Tang, Yun-Fei Xu and 9 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
  2. Article
  3. PHLPP2 is a pseudophosphatase that lost activity in the metazoan ancestor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. A comprehensive overview of PPM1A: From structure to disease.Experimental biology and medicine (Maywood, N.J.) · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Effects of lead and cadmium on the immune system and cancer progression.Journal of environmental health science & engineering · 2020
    Review
  15. Article
  16. Article
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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

19 authors at 6 institutions in 3 countries.

Chang PanKey Laboratory Experimental Teratology of the Ministry of Education and Department of Biochemistry and Molecular Biology, Shandong University, School of Medicine, Jinan, Shandong 250012, China.
Hong-Da Liu
Zheng Gong
Xiao Yu
Xu-Ben Hou
Di-Dong Xie
Xi-Bin Zhu
Hao-Wen Li
Jun-Yi Tang
Yun-Fei Xu
Jia-Qi Yu
Lian-Ying Zhang
Hao Fang
Kun-Hong Xiao
Yu-Guo Chen
Jiang-Yun Wang
Qi Pang
Wei Chen
Jin-Peng Sun
Shandong University · CNChinese Academy of Sciences · CNDuke Medical Center · USDuke University · USDuke University Hospital · USShandong Provincial Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The heavy metal cadmium is a non-degradable pollutant. By screening the effects of a panel of metal ions on the phosphatase activity, we unexpectedly identified cadmium as a potent inhibitor of PPM1A and PPM1G. In contrast, low micromolar concentrations of cadmium did not inhibit PP1 or tyrosine phosphatases. Kinetic studies revealed that cadmium inhibits PPM phosphatases through the M1 metal ion binding site. In particular, the negative charged D441 in PPM1G specific recognized cadmium. Our results suggest that cadmium is likely a potent inhibitor of most PPM family members except for PHLPPs. Furthermore, we demonstrated that cadmium inhibits PPM1A-regulated MAPK signaling and PPM1G-regulated AKT signaling potently in vivo. Cadmium reversed PPM1A-induced cell cycle arrest and cadmium insensitive PPM1A mutant rescued cadmium induced cell death. Taken together, these findings provide a better understanding of the effects of the toxicity of cadmium in the contexts of human physiology and pathology.

Indexed as

Models, ChemicalBinding SitesCadmiumComputer SimulationEnzyme ActivationHEK293 CellsHumansKineticsPhosphoprotein PhosphatasesProtein BindingProtein Phosphatase 2CCadmiumPhosphoprotein PhosphatasesPPM1A protein, humanPPM1G protein, humanProtein Phosphatase 2C

Identifiers

PMID23903585
PMCPMC3730172
OpenAlexW2005410560

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.