Evidence map›Paper›PMID 25336918›Full record

ReviewDrug design, development and therapy2014

Posttranslational regulation of phosphatase and tensin homolog (PTEN) and its functional impact on cancer behaviors.

Wenting Xu, Zhen Yang, Shu-Feng Zhou, Nonghua Lu

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Drug design, development and therapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Review
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  4. Article
  5. Article
  6. Review
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  11. Review
  12. Structural and Dynamic Effects of PTEN C-Terminal Tail Phosphorylation.Journal of chemical information and modeling · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
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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

4 authors.

Wenting XuDepartment of Gastroenterology, The First Affiliated Hospital of Nanchang University, Nanchang, Jiangxi, People's Republic of China.
Zhen YangDepartment of Gastroenterology, The First Affiliated Hospital of Nanchang University, Nanchang, Jiangxi, People's Republic of China.
Shu-Feng ZhouDepartment of Pharmaceutical Sciences, College of Pharmacy, University of South Florida, Tampa, FL, USA.
Nonghua LuDepartment of Gastroenterology, The First Affiliated Hospital of Nanchang University, Nanchang, Jiangxi, People's Republic of China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The incidence of cancer is increasing worldwide, but the biochemical mechanisms for the occurrence of cancer is not fully understood, and there is no cure for advanced tumors. Defects of posttranslational modifications of proteins are linked to a number of important diseases, such as cancer. This review will update our knowledge on the critical role of posttranscriptional regulation of phosphatase and tensin homolog (PTEN) and its activities and the functional impact on cancer behaviors. PTEN is a tumor suppressor gene that occupies a key position in regulating cell growth, proliferation, apoptosis, mobility, signal transduction, and other crucial cellular processes. The activity and function of PTEN are regulated by coordinated epigenetic, transcriptional, posttranscriptional, and posttranslational modifications. In particular, PTEN is subject to phosphorylation, ubiquitylation, somoylation, acetylation, and active site oxidation. Posttranslational modifications of PTEN can dynamically change its activity and function. Deficiency in the posttranslational regulation of PTEN leads to abnormal cell proliferation, apoptosis, migration, and adhesion, which are associated with cancer initiation, progression, and metastasis. With increasing information on how PTEN is regulated by multiple mechanisms and networked proteins, its exact role in cancer initiation, growth, and metastasis will be revealed. PTEN and its functionally related proteins may represent useful targets for the discovery of new anticancer drugs, and gene therapy and the therapeutic potentials should be fully explored.

Indexed as

Protein Processing, Post-TranslationalHumansNeoplasmsPTEN PhosphohydrolasePTEN PhosphohydrolasePTEN protein, humanacetylationoxidationphosphorylationPTENubiquitination

Identifiers

PMID25336918
PMCPMC4199979

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Registered trials

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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.