Evidence map›Paper›PMID 7479742›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells.

N Bonnefoy-Bérard, Y C Liu, M von Willebrand, A Sung, C Elly, T Mustelin, H Yoshida, K Ishizaka, A Altman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.3field-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

37 citing papers in PubMed, 139 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. 14-3-3σ and Its Modulators in Cancer.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The role of stratifin in fibroblast-keratinocyte interaction.Molecular and cellular biochemistry · 2007
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Structural and functional hot spots in cytokine receptors.International journal of hematology · 2001
    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

9 authors at 1 institution in 1 country.

N Bonnefoy-BérardDivision of Cell Biology, La Jolla Institute for Allergy and Immunology, CA 92037, USA.
Y C Liu
M von Willebrand
A Sung
C Elly
T Mustelin
H Yoshida
K Ishizaka
A Altman
La Jolla Institute for Immunology · US

Funding

T CELLS AND THEIR LYMPHOKINES IN CANCER IMMUNOTHERAPYR01CA035299 · NCI · SCRIPPS RESEARCH INSTITUTE · PI ALTMAN, AMNON · 1985 to 2013
$3.8M
FUNCTION AND REGULATION OF VAV IN LYMPHOCYTE ACTIVATIONR01GM050819 · NIGMS · LA JOLLA INST FOR ALLERGY &IMMUNOLGY · PI ALTMAN, AMNON · 1994 to 2005
$2.2M
SRC FAMILY KINASES--FUNCTION AND REGULATION IN T-CELLSR29GM048960 · NIGMS · LA JOLLA INST FOR ALLERGY &IMMUNOLGY · PI MUSTELIN, TOMAS M · 1993 to 1997
–
NCI NIH HHS CA35299NIGMS NIH HHS GM48960NIGMS NIH HHS GM50819
6 · The paper itself

Abstract

Proteins of the 14-3-3 family can associate with, and/or modulate the activity of, several protooncogene and oncogene products and, thus, are implicated in regulation of signaling pathways. We report that 14-3-3 is associated with another important transducing enzyme, phosphatidylinositol 3-kinase (PI3-K). A recombinant 14-3-3 fusion protein bound several tyrosine-phosphorylated proteins from antigen receptor-stimulated T lymphocytes. PI3-K was identified by immunoblotting and enzymatic assays as one of the 14-3-3-binding proteins in resting or activated cells. Moreover, endogenous 14-3-3 and PI3-K were coimmunoprecipitated from intact T cells. Far-Western blots of gel-purified, immunoprecipitated PI3-K with a recombinant 14-3-3 fusion protein revealed direct binding of 14-3-3 to the catalytic subunit (p110) of PI3-K. Finally, anti-phosphotyrosine immunoprecipitates from activated, 14-3-3-overexpressing cells contained lower PI3-K enzymatic activity than similar immunoprecipitates from control cells. These findings suggest that association of 14-3-3 with PI3-K in hematopoietic (and possibly other) cells regulates the enzymatic activity of PI3-K during receptor-initiated signal transduction.

Indexed as

Tyrosine 3-Monooxygenase14-3-3 ProteinsBase SequenceBlotting, WesternCell LineDNA PrimersEnzyme InhibitorsGlutathione TransferaseHumansLeukemia, T-CellMolecular Sequence DataPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)Polymerase Chain ReactionProteins14-3-3 ProteinsDNA PrimersEnzyme InhibitorsGlutathione TransferasePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)ProteinsRecombinant Fusion ProteinsTyrosine 3-Monooxygenase

Identifiers

PMID7479742
PMCPMC40752
OpenAlexW2046943799

What Socratic 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 Socratic graph.