Evidence map›Paper›PMID 31548312›Full record

ArticleThe Journal of biological chemistry2019

Serine 474 phosphorylation is essential for maximal Akt2 kinase activity in adipocytes.

Alison L Kearney, Kristen C Cooke, Dougall M Norris, Armella Zadoorian, James R Krycer, Daniel J Fazakerley, James G Burchfield, David E James

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. The insulin signalling network.Nature metabolism · 2025
    Review
  4. Article
  5. Food for thought: Nutrient metabolism controlling early T cell development.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  6. Article
  7. The Impact of Pdcd4, a Translation Inhibitor, on Drug Resistance.Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. GLUT4 On the move.The Biochemical journal · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

8 authors at 1 institution in 1 country.

Alison L KearneyCharles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia.
Kristen C CookeCharles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia.
Dougall M NorrisCharles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia.
Armella ZadoorianCharles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia.
James R KrycerCharles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia.
Daniel J FazakerleyCharles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia djf72@cam.ac.uk.
James G BurchfieldCharles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia james.burchfield@sydney.edu.au.ORCID 0000-0002-6609-6151
David E JamesCharles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales 2006, Australia david.james@sydney.edu.au.ORCID 0000-0001-5946-5257
University of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Ser/Thr protein kinase Akt regulates essential biological processes such as cell survival, growth, and metabolism. Upon growth factor stimulation, Akt is phosphorylated at Ser

Indexed as

3T3-L1 CellsAdipocytesAnimalsCell NucleusForkhead Box Protein O1GlucoseGlucose Transporter Type 4Heterocyclic Compounds, 3-RingInsulinMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2MiceMutagenesis, Site-DirectedPhosphorylationProtein BiosynthesisProto-Oncogene Proteins c-aktAkt2 protein, mouseForkhead Box Protein O1Foxo1 protein, mouseGlucoseGlucose Transporter Type 4Heterocyclic Compounds, 3-RingInsulinMechanistic Target of Rapamycin Complex 1Mechanistic Target of Rapamycin Complex 2MK 2206Proto-Oncogene Proteins c-aktSerineTsc2 protein, mouseTuberous Sclerosis Complex 2 ProteinadipocyteAkt PKBAkt Ser474 phosphorylationAkt W80Acell signalingchemical geneticsglucose transportGLUT4insulinMK2206mTOR complex (mTORC)phosphorylationprotein synthesisserine/threonine protein kinasesubstrate specificity

Identifiers

PMID31548312
PMCPMC6851323
OpenAlexW2976828099

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.