Evidence map›Paper›PMID 30901610›Full record

ReviewCurrent opinion in structural biology2019

AKTivation mechanisms.

Philip A Cole, Nam Chu, Antonieta L Salguero, Hwan Bae

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. The structural heterogeneity of AKT autoinhibition.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. The Flavonoid Extract ofAntioxidants (Basel, Switzerland) · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. AKT kinases as therapeutic targets.Journal of experimental & clinical cancer research : CR · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  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

4 authors at 2 institutions in 1 country.

Philip A ColeDivision of Genetics, Department of Medicine Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, United States. Electronic address: pacole@bwh.harvard.edu.
Nam ChuDivision of Genetics, Department of Medicine Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, United States.
Antonieta L SalgueroDivision of Genetics, Department of Medicine Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, United States; Department of Pharmacology and Molecular Sciences, Johns Hopkins School of Medicine, Baltimore, MD 21205, United States.
Hwan BaeDivision of Genetics, Department of Medicine Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, United States.
Brigham and Women's Hospital · USJohns Hopkins University · US

Funding

Chemical Approaches to Protein PhosphorylationR01CA074305 · NCI · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2002 to 2025
$8.0M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
ENZYMATIC STUDIES ON PROTEIN TYROSINE KINASE CSKR29CA074305 · NCI · ROCKEFELLER UNIVERSITY · PI COLE, PHILIP A · 1997 to 2001
$188k
NCI NIH HHS R01 CA074305NCI NIH HHS R29 CA074305NIGMS NIH HHS T32 GM080189
6 · The paper itself

Abstract

Akt1-3 (Akt) are a subset of the AGC protein Ser/Thr kinase family and play important roles in cell growth, metabolic regulation, cancer, and other diseases. We describe some of the roles of Akt in cell signaling and the biochemical and structural mechanisms of the regulation of Akt catalysis by the phospholipid PIP3 and by phosphorylation. Recent findings highlight a diverse set of strategies to control Akt catalytic activity to ensure its normal biological functions.

Indexed as

AnimalsCatalysisHumansPhosphatidylinositol 3-KinasesPhosphorylationProtein BindingProtein Interaction Domains and MotifsProto-Oncogene Proteins c-aktSignal TransductionStructure-Activity RelationshipSubstrate SpecificityPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-akt

Identifiers

PMID30901610
PMCPMC6752985
OpenAlexW4243480466

What OpenQuestion holds

Textmetadata
LicenceTDM
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.