Evidence map›Paper›PMID 35682605›Full record

ReviewInternational journal of molecular sciences2022

Monoubiquitination in Homeostasis and Cancer.

Yujie Chen, Dandan Zhou, Yinan Yao, Yutong Sun, Fan Yao, Li Ma

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-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

22 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. USP40 protects podocytes by deubiquitylating integrin β1.Biochemical and biophysical research communications · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Artificial selection of two antagonistic E3 ubiquitin ligases finetunes soybean photoperiod adaptation and grain yield.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. mTORC1 phosphorylates and stabilizes LST2 to negatively regulate EGFR.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Ubiquitination in the regulation of autophagy.Acta biochimica et biophysica Sinica · 2023
    Article
  19. Article
  20. Review
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

6 authors at 3 institutions in 2 countries.

Yujie ChenHubei Hongshan Laboratory, College of Biomedicine and Health, Huazhong Agricultural University, Wuhan 430070, China.
Dandan ZhouHubei Hongshan Laboratory, College of Biomedicine and Health, Huazhong Agricultural University, Wuhan 430070, China.
Yinan YaoHubei Hongshan Laboratory, College of Biomedicine and Health, Huazhong Agricultural University, Wuhan 430070, China.
Yutong SunDepartment of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
Fan YaoHubei Hongshan Laboratory, College of Biomedicine and Health, Huazhong Agricultural University, Wuhan 430070, China.ORCID 0000-0002-4393-7296
Li MaDepartment of Experimental Radiation Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.ORCID 0000-0001-9965-989X
Huazhong Agricultural University · CNThe University of Texas MD Anderson Cancer Center · USHubei University of Medicine · CN

Funding

Regulation of metastasis and epithelial-mesenchymal transition by microRNAsR01CA166051 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI MA, LI · 2012 to 2023
$3.4M
Cancer Prevention and Research Institute of Texas RP190029National Natural Science Foundation of China 31900935NCI NIH HHS R01 CA166051NIH HHS R01CA166051
6 · The paper itself

Abstract

Monoubiquitination is a post-translational modification (PTM), through which a single ubiquitin molecule is covalently conjugated to a lysine residue of the target protein. Monoubiquitination regulates the activity, subcellular localization, protein-protein interactions, or endocytosis of the substrate. In doing so, monoubiquitination is implicated in diverse cellular processes, including gene transcription, endocytosis, signal transduction, cell death, and DNA damage repair, which in turn regulate cell-cycle progression, survival, proliferation, and stress response. In this review, we summarize the functions of monoubiquitination and discuss how this PTM modulates homeostasis and cancer.

Indexed as

NeoplasmsUbiquitinHomeostasisHumansLysineProtein Processing, Post-TranslationalUbiquitinationLysineUbiquitincancerhomeostasismonoubiquitination

Identifiers

PMID35682605
PMCPMC9180643
OpenAlexW4281480732

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.