Evidence map›Paper›PMID 24794538›Full record

ReviewAdvances in biological regulation2014

Signaling specificity in the Akt pathway in biology and disease.

Alex Toker, Sandra Marmiroli

Abstract readReview
In one paragraph

Review in Advances in biological regulation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing 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

100 citing papers in PubMed.

  1. Article
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  9. Review
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  11. Human Dendritic Cell Maturation Is Modulated byTropical medicine and infectious disease · 2024
    Article
  12. Review
  13. Article
  14. Article
  15. Article
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40 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

2 authors.

Alex TokerDepartment of Pathology and Cancer Center, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA. Electronic address: atoker@bidmc.harvard.edu.
Sandra MarmiroliDepartment of Surgery, Medicine, Dentistry and Morphology, University of Modena and Reggio Emilia, Italy. Electronic address: sandra.marmiroli@unimore.it.

Funding

Novel regulation of PI3K/Akt to direct targeted breast cancer therapiesR01CA177910 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WEI, WENYI · 2013 to 2023
$3.9M
The Akt and NFAT Pathway and the Regulaton of Cancer Cell MotilityR01CA122099 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI TOKER, ALEX · 2007 to 2011
$1.4M
NCI NIH HHS R01 CA122099NCI NIH HHS R01 CA177910
6 · The paper itself

Abstract

Akt/PKB is a key master regulator of a wide range of physiological functions including metabolism, proliferation, survival, growth, angiogenesis and migration and invasion. The Akt protein kinase family comprises three highly related isoforms encoded by different genes. The initial observation that the Akt isoforms share upstream activators as well as several downstream effectors, together with the high sequence homology suggested that their functions were mostly redundant. By contrast, an increasing body of evidence has recently uncovered the concept of Akt isoform signaling specificity, supported by distinct phenotypes displayed by animal strains genetically modified for each of the three genes, as well as by the identification of isoform-specific substrates and association with discrete subcellular locations. Given that Akt is regarded as a promising therapeutic target in a number of pathologies, it is essential to dissect the relative contributions of each isoform, as well as the degree of compensation in pathophysiological function. Here we summarize our view of how Akt selectivity is achieved in the context of subcellular localization, isoform-specific substrate phosphorylation and context-dependent functions in normal and pathophysiological settings.

Indexed as

AnimalsEnzyme ActivationHumansLamin Type AMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Multiprotein ComplexesNuclear ProteinsPhosphoprotein PhosphatasesPhosphorylationProtein IsoformsProtein Phosphatase 2Protein Structure, TertiaryProto-Oncogene Proteins c-aktSignal TransductionSubstrate SpecificityLamin Type AMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2Multiprotein ComplexesNuclear ProteinsPHLPP1 protein, humanPhosphoprotein PhosphatasesProtein IsoformsProtein Phosphatase 2Proto-Oncogene Proteins c-aktTOR Serine-Threonine KinasesAktCancerNucleusPI 3-KinaseProtein kinaseSignaling

Identifiers

PMID24794538
PMCPMC4062840

What OpenQuestion holds

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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.