Evidence map›Paper›PMID 30145641›Full record

ReviewMolecular biology reports2018

Regulation and modulation of PTEN activity.

Elahe Naderali, Amir Afshin Khaki, Jafar Soleymani Rad, Alireza Ali-Hemmati, Mohammad Rahmati, Hojjatollah Nozad Charoudeh

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular biology reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 73 citations in OpenAlex.

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  12. Pharmaceuticals (Basel, Switzerland) · 2024
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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

6 authors at 1 institution in 1 country.

Elahe NaderaliStem Cell Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.
Amir Afshin KhakiDepartment of Anatomical sciences, Faculty of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran.ORCID http://orcid.org/0000-0002-4678-4002
Jafar Soleymani RadDepartment of Anatomical sciences, Faculty of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran.
Alireza Ali-HemmatiDepartment of Anatomical sciences, Faculty of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran.ORCID http://orcid.org/0000-0002-2929-006X
Mohammad RahmatiDepartment of Clinical Biochemistry Sciences, Faculty of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran.ORCID http://orcid.org/0000-0001-7791-3287
Hojjatollah Nozad CharoudehStem Cell Research Center, Tabriz University of Medical Sciences, Tabriz, Iran. nozadh@tbzmed.ac.ir.ORCID http://orcid.org/0000-0003-4883-9924
Tabriz University of Medical Sciences · IR

Funding

Tabriz University of Medical Sciences (IR) 5/104/996
6 · The paper itself

Abstract

PTEN (Phosphatase and tensin homolog deleted on chromosome ten) is a tumor suppressor that is frequently mutated in most human cancers. PTEN is a lipid and protein phosphatase that antagonizes PI3K/AKT pathway through lipid phosphatase activity at the plasma membrane. More recent studies showed that, in addition to the putative role of PTEN as a PI(3,4,5)P3 3-phosphatase, it is a PI(3,4)P2 3-phosphatase during stimulation of class I PI3K signaling pathway by growth factor. Although PTEN tumor suppressor function via it's lipid phosphatase activity occurs primarily in the plasma membrane, it can also be found in the nucleus, in cytoplasmic organelles and extracellular space. PTEN has also shown phosphatase independent functions in the nucleus. PTEN can exit from the cell through exosomal export or secretion and has a tumor suppressor function in adjacent cells. PTEN has a critical role in growth, the cell cycle, protein synthesis, survival, DNA repair and migration. Understanding the regulation of PTEN function, activity, stability, localization and its dysregulation outcomes and also the intracellular and extracellular role of PTEN and paracrine role of PTEN-L in tumor cells as an exogenous therapeutic agent can help to improve clinical conceptualization and treatment of cancer.

Indexed as

AnimalsCell CycleCell NucleusCytoplasmGenes, Tumor SuppressorHumansPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePTEN protein, humanPost-transcriptional regulationPTENPTEN-LTranscriptional regulation

Identifiers

PMID30145641
OpenAlexW2887997618

What OpenQuestion holds

Textmetadata
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.