Evidence map›Paper›PMID 32350110›Full record

ArticleThe Journal of biological chemistry2020

Phosphorylation-dependent substrate selectivity of protein kinase B (AKT1).

Nileeka Balasuriya, Norman E Davey, Jared L Johnson, Huadong Liu, Kyle K Biggar, Lewis C Cantley, Shawn Shun-Cheng Li, Patrick O'Donoghue

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

35 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Pinealectomy-Induced Neuroinflammation Varies with Age in Rats.International journal of molecular sciences · 2025
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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 3 institutions in 4 countries.

Nileeka BalasuriyaDepartment of Biochemistry, The University of Western Ontario, London, Ontario, Canada.
Norman E DaveyDivision of Cancer Biology, The Institute of Cancer Research, London, United Kingdom.
Jared L JohnsonMeyer Cancer Center, Department of Medicine, Weill Cornell Medical College, New York, New York, United States.ORCID 0000-0003-1802-6527
Huadong LiuDepartment of Biochemistry, The University of Western Ontario, London, Ontario, Canada.
Kyle K BiggarDepartment of Biochemistry, The University of Western Ontario, London, Ontario, Canada.
Lewis C CantleyMeyer Cancer Center, Department of Medicine, Weill Cornell Medical College, New York, New York, United States.
Shawn Shun-Cheng LiDepartment of Biochemistry, The University of Western Ontario, London, Ontario, Canada.
Patrick O'DonoghueDepartment of Biochemistry, The University of Western Ontario, London, Ontario, Canada patrick.odonoghue@uwo.ca.
Western University · CACornell University · USInstitute of Cancer Research · GB

Funding

CIHR 165985
6 · The paper itself

Abstract

Protein kinase B (AKT1) is a central node in a signaling pathway that regulates cell survival. The diverse pathways regulated by AKT1 are communicated in the cell via the phosphorylation of perhaps more than 100 cellular substrates. AKT1 is itself activated by phosphorylation at Thr-308 and Ser-473. Despite the fact that these phosphorylation sites are biomarkers for cancers and tumor biology, their individual roles in shaping AKT1 substrate selectivity are unknown. We recently developed a method to produce AKT1 with programmed phosphorylation at either or both of its key regulatory sites. Here, we used both defined and randomized peptide libraries to map the substrate selectivity of site-specific, singly and doubly phosphorylated AKT1 variants. To globally quantitate AKT1 substrate preferences, we synthesized three AKT1 substrate peptide libraries: one based on 84 "known" substrates and two independent and larger oriented peptide array libraries (OPALs) of ∼10

Indexed as

Amino Acid MotifsAmino Acid SequenceHumansPeptide LibraryPeptidesPhosphorylationPhosphoserineProto-Oncogene Proteins c-aktROC CurveSubstrate SpecificityAKT1 protein, humanPeptide LibraryPeptidesPhosphoserineProto-Oncogene Proteins c-aktAkt PKBcell signalinggenetic code expansionoriented peptide array librarypeptide arrayphosphoinositide-dependent kinase 1phosphoseryl-tRNA synthetasepost-translational modification (PTM)protein phosphorylationRNA metabolismserine/threonine protein kinasesubstrate specificitytRNASep

Identifiers

PMID32350110
PMCPMC7294097
OpenAlexW3023156490

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.