Evidence map›Paper›PMID 34385319›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Structure of autoinhibited Akt1 reveals mechanism of PIP

Linda Truebestein, Harald Hornegger, Dorothea Anrather, Markus Hartl, Kaelin D Fleming, Jordan T B Stariha, Els Pardon, Jan Steyaert, John E Burke, Thomas A Leonard

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

56 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. PHLPP is neither a Phosphatase nor a Tumor Suppressor.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The structural heterogeneity of AKT autoinhibition.Protein science : a publication of the Protein Society · 2026
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. mAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  18. PHLPP2 is a pseudophosphatase that lost activity in the metazoan ancestor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article
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

10 authors at 4 institutions in 3 countries.

Linda TruebesteinDepartment of Structural and Computational Biology, Max Perutz Labs, Vienna BioCenter, 1030 Vienna, Austria.ORCID 0000-0002-0596-201X
Harald HorneggerDepartment of Structural and Computational Biology, Max Perutz Labs, Vienna BioCenter, 1030 Vienna, Austria.ORCID 0000-0001-7703-9710
Dorothea AnratherMass Spectrometry Core Facility, Max Perutz Labs, Vienna BioCenter, 1030 Vienna, Austria.ORCID 0000-0003-1677-2403
Markus HartlMass Spectrometry Core Facility, Max Perutz Labs, Vienna BioCenter, 1030 Vienna, Austria.ORCID 0000-0002-4970-7336
Kaelin D FlemingDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 2Y2, Canada.ORCID 0000-0003-3063-7865
Jordan T B StarihaDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 2Y2, Canada.
Els PardonStructural Biology Brussels, Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium.ORCID 0000-0002-2466-0172
Jan SteyaertStructural Biology Brussels, Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium.ORCID 0000-0002-3825-874X
John E BurkeDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 2Y2, Canada.ORCID 0000-0001-7904-9859
Thomas A LeonardDepartment of Structural and Computational Biology, Max Perutz Labs, Vienna BioCenter, 1030 Vienna, Austria; thomas.leonard@meduniwien.ac.at.ORCID 0000-0001-6853-666X
Max Perutz Labs · ATUniversity of Victoria · CAVrije Universiteit Brussel · BEUniversity of British Columbia · CA

Funding

Austrian Science Fund FWF P 30584Austrian Science Fund FWF P 33066Austrian Science Fund FWF T 915
6 · The paper itself

Abstract

The protein kinase Akt is one of the primary effectors of growth factor signaling in the cell. Akt responds specifically to the lipid second messengers phosphatidylinositol-3,4,5-trisphosphate [PI(3,4,5)P

Indexed as

AnimalsBinding SitesHumansInsectaLipid MetabolismPhosphatidylinositol PhosphatesProtein BindingProtein ConformationProtein DomainsProto-Oncogene Proteins c-aktPyruvate Dehydrogenase Acetyl-Transferring KinaseSf9 CellsAKT1 protein, humanPDK1 protein, humanphosphatidylinositol 3,4,5-triphosphatephosphatidylinositol 3,4-diphosphatePhosphatidylinositol PhosphatesProto-Oncogene Proteins c-aktPyruvate Dehydrogenase Acetyl-Transferring KinaseAktkinaselipidPIP3signaling

Identifiers

PMID34385319
PMCPMC8379990
OpenAlexW3191332260

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.