Evidence map›Paper›PMID 28330929›Full record

ReviewCancer research2017

The Role of PIAS SUMO E3-Ligases in Cancer.

Andrea Rabellino, Cristina Andreani, Pier Paolo Scaglioni

Abstract readReview
In one paragraph

Review in Cancer research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
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

65 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. SUMO modifies GβL and mediates mTOR signaling.The Journal of biological chemistry · 2024
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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

3 authors.

Andrea RabellinoDepartment of Internal Medicine, The University of Texas Southwestern Medical Center, Dallas, Texas.
Cristina AndreaniDepartment of Internal Medicine, The University of Texas Southwestern Medical Center, Dallas, Texas.
Pier Paolo ScaglioniDepartment of Internal Medicine, The University of Texas Southwestern Medical Center, Dallas, Texas. Pier.Scaglioni@utsouthwestern.edu.

Funding

UNIVERSITY OF TEXAS--SPORE IN LUNG CANCERP50CA070907 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI HEYMACH, JOHN V., MINNA, JOHN D. · 1996 to 2024
$57.4M
UT Southwestern Medical Center Simmons Comprehensive Cancer CenterP30CA142543 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI MELANIE H. COBB · 2010 to 2026
$53.7M
Characterization and drug targeting of the PML tumor suppressor in lung cancerR01CA137195 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI SCAGLIONI, PIER PAOLO · 2009 to 2013
$1.6M
NCI NIH HHS P30 CA142543NCI NIH HHS P50 CA070907NCI NIH HHS R01 CA137195
6 · The paper itself

Abstract

SUMOylation modifies the interactome, localization, activity, and lifespan of its target proteins. This process regulates several cellular machineries, including transcription, DNA damage repair, cell-cycle progression, and apoptosis. Accordingly, SUMOylation is critical in maintaining cellular homeostasis, and its deregulation leads to the corruption of a plethora of cellular processes that contribute to disease states. Among the proteins involved in SUMOylation, the protein inhibitor of activated STAT (PIAS) E3-ligases were initially described as transcriptional coregulators. Recent findings also indicate that they have a role in regulating protein stability and signaling transduction pathways. PIAS proteins interact with up to 60 cellular partners affecting several cellular processes, most notably immune regulation and DNA repair, but also cellular proliferation and survival. Here, we summarize the current knowledge about their role in tumorigenesis and cancer-related processes.

Indexed as

SumoylationAnimalsCell MovementEpithelial-Mesenchymal TransitionHumansNeoplasmsPhosphatidylinositol 3-KinasesProtein Inhibitors of Activated STATProto-Oncogene Proteins c-mycTumor Suppressor Protein p53Ubiquitin-Protein LigasesMYC protein, humanPhosphatidylinositol 3-KinasesProtein Inhibitors of Activated STATProto-Oncogene Proteins c-mycTumor Suppressor Protein p53Ubiquitin-Protein Ligases

Identifiers

PMID28330929
PMCPMC5380518

What OpenQuestion holds

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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.