Evidence map›Paper›PMID 21436840›Full record

ReviewLeukemia2011

Targeting the translational apparatus to improve leukemia therapy: roles of the PI3K/PTEN/Akt/mTOR pathway.

A M Martelli, C Evangelisti, W Chappell, S L Abrams, J Bäsecke, F Stivala, M Donia, P Fagone, F Nicoletti, M Libra and 5 more

Abstract readReview
PubMed Publisher
In one paragraph

Review in Leukemia, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

112 citing papers in PubMed, 203 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. The Question of Survival or Death: What Is the Role of Autophagy in Acute Myeloid Leukemia (AML)?International journal of hematology-oncology and stem cell research · 2022
    Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

52 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

15 authors at 5 institutions in 3 countries.

A M MartelliDipartimento di Scienze Anatomiche Umane e Fisiopatologia dell'Apparato Locomotore, Università di Bologna, Bologna, Italy.
C Evangelisti
W Chappell
S L Abrams
J Bäsecke
F Stivala
M Donia
P Fagone
F Nicoletti
M Libra
V Ruvolo
P Ruvolo
C R Kempf
L S Steelman
J A McCubrey
East Carolina University · USUniversity of Catania · ITThe University of Texas MD Anderson Cancer Center · USUniversity of Bologna · ITUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It has become apparent that regulation of protein translation is an important determinant in controlling cell growth and leukemic transformation. The phosphoinositide 3-kinase (PI3K)/phosphatase and tensin homologue deleted on chromosome ten (PTEN)/Akt/mammalian target of rapamycin (mTOR) pathway is often implicated in sensitivity and resistance to therapy. Dysregulated signaling through the PI3K/PTEN/Akt/mTOR pathway is often the result of genetic alterations in critical components in this pathway as well as mutations at upstream growth factor receptors. Furthermore, this pathway is activated by autocrine transformation mechanisms. PTEN is a critical tumor suppressor gene and its dysregulation results in the activation of Akt. PTEN is often mutated, silenced and is often haploinsufficient. The mTOR complex1 (mTORC1) regulates the assembly of the eukaryotic initiation factor4F complex, which is critical for the translation of mRNAs that are important for cell growth, prevention of apoptosis and transformation. These mRNAs have long 5'-untranslated regions that are G+C rich, rendering them difficult to translate. Elevated mTORC1 activity promotes the translation of these mRNAs via the phosphorylation of 4E-BP1. mTORC1 is a target of rapamycin and novel active-site inhibitors that directly target the TOR kinase activity. Although rapamycin and novel rapalogs are usually cytostatic and not cytotoxic for leukemic cells, novel inhibitors that target the kinase activities of PI3K and mTOR may prove more effective for leukemia therapy.

Indexed as

Molecular Targeted TherapyAntineoplastic AgentsApoptosisDrug DesignDrug Resistance, NeoplasmGene Expression Regulation, LeukemicHumansLeukemiaMechanistic Target of Rapamycin Complex 1MicroRNAsMultiprotein ComplexesNeoplasm ProteinsNeoplastic Stem CellsPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphorylationAKT1 protein, humanAntineoplastic AgentsCRTC2 protein, humanMechanistic Target of Rapamycin Complex 1MicroRNAsMTOR protein, humanMultiprotein ComplexesNeoplasm ProteinsPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsProteinsProto-Oncogene Proteins c-aktPTEN PhosphohydrolasePTEN protein, humanRNA, MessengerRNA, NeoplasmTOR Serine-Threonine KinasesTranscription Factors

Identifiers

PMID21436840
OpenAlexW1569244981

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.