Evidence map›Paper›PMID 16288287›Full record

ReviewOncogene2005

Regulation of the Akt kinase by interacting proteins.

Keyong Du, Philip N Tsichlis

Abstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
–field-weighted citation impact
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

72 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

12 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

2 authors.

Keyong DuMolecular Oncology Research Institute, Tufts-New England Medical Center, Boston, MA 02111, USA.
Philip N Tsichlis

Funding

Akt in T cell development and functionR01CA057436 · NCI · TUFTS MEDICAL CENTER · PI TSICHLIS, PHILIP N. · 1994 to 2011
$3.2M
NCI NIH HHS R01 CA57436
6 · The paper itself

Abstract

Ten years ago, it was observed that the Akt kinase is activated by phosphorylation via a phosphoinositide 3-kinase (PI-3K)-dependent process. This discovery generated enormous interest because it provided a link between PI-3K, an enzyme known to play a critical role in cellular physiology, and its downstream targets. Subsequently, it was shown that the activity of the core components of the 'PI-3K/Akt pathway' is modulated by a complex network of regulatory proteins and pathways. Some of the Akt-binding partners modulate its activation by external signals by interacting with different domains of the Akt protein. This review focuses on the Akt interacting proteins and the mechanisms by which they regulate Akt activation.

Indexed as

Protein BindingOncogene Protein v-aktPhosphatidylinositol 3-KinasesPhosphorylationSignal TransductionOncogene Protein v-aktPhosphatidylinositol 3-Kinases

Identifiers

PMID16288287

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.