Evidence map›Paper›PMID 30208623›Full record

ReviewInternational journal of molecular sciences2018

Protein Tyrosine Phosphatases as Potential Regulators of STAT3 Signaling.

Mihwa Kim, Liza D Morales, Ik-Soon Jang, Yong-Yeon Cho, Dae Joon Kim

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

103 citing papers in PubMed, 169 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. STAT3 axis in cancer and cancer stem cells: From oncogenesis to targeted therapies.Biochimica et biophysica acta. Reviews on cancer · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Inflammation in glomerular diseases.Frontiers in immunology · 2025
    Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

43 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

5 authors at 3 institutions in 2 countries.

Mihwa KimDepartment of Biomedical Sciences, School of Medicine, University of Texas Rio Grande Valley, Edinburg, TX 78539, USA. mihwa.kim@utrgv.edu.ORCID 0000-0001-8065-1513
Liza D MoralesDepartment of Human Genetics, School of Medicine, University of Texas Rio Grande Valley, Edinburg, TX 78539, USA. liza.moralessmith@utrgv.edu.
Ik-Soon JangDivision of Bioconvergence Analysis, Korea Basic Science Institute, Daejeon 305-333, Korea. jangiksn@kbsi.re.kr.ORCID 0000-0003-2092-6372
Yong-Yeon ChoIntegrated Research Institute of Pharmaceutical Science & BK21 PLUS Team for Creative Leader Program for Pharmacomics-based Future Pharmacy, College of Pharmacy, The Catholic University of Korea, Bucheon-si, Gyeonggi-do 420-743, Korea. yongyeon@catholic.ac.kr.
Dae Joon KimDepartment of Biomedical Sciences, School of Medicine, University of Texas Rio Grande Valley, Edinburg, TX 78539, USA. dae.kim@utrgv.edu.ORCID 0000-0002-7977-9955
The University of Texas Rio Grande Valley · USCatholic University of Korea · KRKorea Basic Science Institute · KR

Funding

The role of TC-PTP in skin carcinogenesisR01ES022250 · NIEHS · UNIVERSITY OF TEXAS RIO GRANDE VALLEY · PI KIM, DAE JOON · 2013 to 2017
$1.7M
National Institute of Environmental Health Sciences ES022250
6 · The paper itself

Abstract

The signal transducer and activator of transcription 3 (STAT3) protein is a major transcription factor involved in many cellular processes, such as cell growth and proliferation, differentiation, migration, and cell death or cell apoptosis. It is activated in response to a variety of extracellular stimuli including cytokines and growth factors. The aberrant activation of STAT3 contributes to several human diseases, particularly cancer. Consequently, STAT3-mediated signaling continues to be extensively studied in order to identify potential targets for the development of new and more effective clinical therapeutics. STAT3 activation can be regulated, either positively or negatively, by different posttranslational mechanisms including serine or tyrosine phosphorylation/dephosphorylation, acetylation, or demethylation. One of the major mechanisms that negatively regulates STAT3 activation is dephosphorylation of the tyrosine residue essential for its activation by protein tyrosine phosphatases (PTPs). There are seven PTPs that have been shown to dephosphorylate STAT3 and, thereby, regulate STAT3 signaling: PTP receptor-type D (PTPRD), PTP receptor-type T (PTPRT), PTP receptor-type K (PTPRK), Src homology region 2 (SH-2) domain-containing phosphatase 1(SHP1), SH-2 domain-containing phosphatase 2 (SHP2), MEG2/PTP non-receptor type 9 (PTPN9), and T-cell PTP (TC-PTP)/PTP non-receptor type 2 (PTPN2). These regulators have great potential as targets for the development of more effective therapies against human disease, including cancer.

Indexed as

Signal TransductionAnimalsHumansMutationNeoplasmsPhosphorylationProtein Processing, Post-TranslationalProtein Tyrosine PhosphatasesSTAT3 Transcription FactorProtein Tyrosine PhosphatasesSTAT3 Transcription FactorPTPRDPTPRTSHP1SHP2STAT3TC-PTP

Identifiers

PMID30208623
PMCPMC6164089
OpenAlexW2891416934

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.