Evidence map›Paper›PMID 22108654›Full record

ArticleFEBS letters2011

Substrate specificity of diacylglycerol kinase-epsilon and the phosphatidylinositol cycle.

Yulia V Shulga, Matthew K Topham, Richard M Epand

Abstract read
In one paragraph

Article in FEBS letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Diacylglycerol Kinase Puts the Brakes on Airway Smooth Muscle Contraction.American journal of respiratory cell and molecular biology · 2021
    Article
  6. Article
  7. Article
  8. Roles of DGKs in neurons: Postsynaptic functions?Advances in biological regulation · 2020
    Review
  9. Diacylglycerol kinases: Relationship to other lipid kinases.Advances in biological regulation · 2019
    Review
  10. Article
  11. Article
  12. Review
  13. Diacylglycerol Kinase-ε: Properties and Biological Roles.Frontiers in cell and developmental biology · 2016
    Review
  14. Review
  15. Article
  16. Article
  17. 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

3 authors.

Yulia V ShulgaDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Matthew K Topham
Richard M Epand

Funding

Diacylglycerol Kinase Delta in Growth and DevelopmentR01CA095463 · NCI · UNIVERSITY OF UTAH · PI TOPHAM, MATTHEW KENT · 2002 to 2011
$2.4M
NCI NIH HHS R01 CA095463NCI NIH HHS R01CA095463
6 · The paper itself

Abstract

We show that diacylglycerol kinase-ε (DGKε) has less preference for the acyl chain at the sn-1 position of diacylglycerol (DAG) than the one at the sn-2 position. Although DGKε discriminates between 1-stearoyl-2-arachidonoyl-DAG and 1-palmitoyl-2-arachidonoyl-DAG, it has similar substrate preference for 1-stearoyl-2-arachidonoyl-DAG and 1,2-diarachidonoyl-DAG. We suggest that in addition to binding to the enzyme, the acyl chain at the sn-1 position may contribute to the depth of insertion of the DAG into the membrane. Thus, the DAG intermediate of the PI-cycle, 1-stearoyl-2-arachidonoyl-DAG, is not the only DAG that is a good substrate for DGKε, the DGK isoform involved in PI-cycling.

Indexed as

Diacylglycerol KinaseDiglyceridesEnzyme InhibitorsHumansKineticsPhosphatidylinositolsSubstrate SpecificityDGKE protein, humanDiacylglycerol KinaseDiglyceridesEnzyme InhibitorsPhosphatidylinositolsstearoylarachidonylglycerol

Identifiers

PMID22108654
PMCPMC3237191

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Registered trials

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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.