Evidence map›Paper›PMID 10051597›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Myogenic signaling of phosphatidylinositol 3-kinase requires the serine-threonine kinase Akt/protein kinase B.

B H Jiang, M Aoki, J Z Zheng, J Li, P K Vogt

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
6.7field-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

88 citing papers in PubMed, 262 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Forkhead box O proteins: steering the course of stem cell fate.Cell regeneration (London, England) · 2024
    Review
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  6. Article
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  8. Article
  9. A non-translational role of threonyl-tRNA synthetase in regulating JNK signaling during myogenic differentiation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Molecular Mechanisms Regulating Muscle Plasticity in Fish.Animals : an open access journal from MDPI · 2020
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

28 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 1 institution in 1 country.

B H JiangThe Scripps Research Institute, BCC-239, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
M Aoki
J Z Zheng
J Li
P K Vogt
Scripps Research Institute · US

Funding

P3K, RETROVIRAL ONCOGENE AND HOMOLOG OF PI 3-KINASER01CA078230 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI VOGT, PETER K · 1998 to 2013
$5.6M
ONCOGENES P3K AND AKT IN TUMORIGENESISF32CA077892 · NCI · SCRIPPS RESEARCH INSTITUTE · PI JIANG, BING-HUA · 1999 to 2000
$26k
ONCOGENES IN VIRUS AND CELLR35CA042564 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI VOGT, PETER K · 1986 to 1999
–
NCI NIH HHS CA 42564NCI NIH HHS CA 77892NCI NIH HHS CA 78230NCI NIH HHS F32 CA077892NCI NIH HHS R01 CA078230
6 · The paper itself

Abstract

The oncogene p3k, coding for a constitutively active form of phosphatidylinositol 3-kinase (PI 3-kinase), strongly activates myogenic differentiation. Inhibition of endogenous PI 3-kinase activity with the specific inhibitor LY294002, or with dominant-negative mutants of PI 3-kinase, interferes with myotube formation and with the expression of muscle-specific proteins. Here we demonstrate that a downstream target of PI 3-kinase, serine-threonine kinase Akt, plays an important role in myogenic differentiation. Expression of constitutively active forms of Akt dramatically enhances myotube formation and expression of the muscle-specific proteins MyoD, creatine kinase, myosin heavy chain, and desmin. Transdominant negative forms of Akt inhibit myotube formation and the expression of muscle-specific proteins. The inhibition of myotube formation and the reduced expression of muscle-specific proteins caused by the PI 3-kinase inhibitor LY294002 are completely reversed by constitutively active forms of Akt. Wild-type cellular Akt effects a partial reversal of LY294002-induced inhibition of myogenic differentiation. This result suggests that Akt can substitute for PI 3-kinase in the stimulation of myogenesis; Akt may be an essential downstream component of PI 3-kinase-induced muscle differentiation.

Indexed as

Cell DifferentiationAnimalsCells, CulturedChick EmbryoChromonesCreatine KinaseDesminEnzyme InhibitorsGene Expression RegulationMorpholinesMuscle ProteinsMuscle, SkeletalMyoD ProteinMyosin Heavy ChainsPhosphatidylinositol 3-KinasesProtein Serine-Threonine Kinases2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneChromonesCreatine KinaseDesminEnzyme InhibitorsMorpholinesMuscle ProteinsMyoD ProteinMyosin Heavy ChainsPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRecombinant Proteins

Identifiers

PMID10051597
PMCPMC26739
OpenAlexW2003965030

What OpenQuestion holds

Texttitle and abstract
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.