Evidence map›Paper›PMID 30348515›Full record

ReviewAdvances in biological regulation2019

Diacylglycerol kinases: Relationship to other lipid kinases.

Qianqian Ma, Sandra B Gabelli, Daniel M Raben

Abstract readReview
In one paragraph

Review in Advances in biological regulation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Involvement ofFrontiers in cell and developmental biology · 2025
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Kinase Inhibitors as Underexplored Antiviral Agents.Journal of medicinal chemistry · 2022
    Review
  11. Elusive structure of mammalian DGKs.Advances in biological regulation · 2022
    Review
  12. Article
  13. Review
  14. 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 at 1 institution in 1 country.

Qianqian MaThe Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Sandra B GabelliThe Department of Biophysics, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA; Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA; Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Daniel M RabenThe Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA. Electronic address: draben@jhmi.edu.
Johns Hopkins University · US

Funding

Tumor Antigens for Individual Signatures and TherapyP50CA062924 · NCI · JOHNS HOPKINS UNIVERSITY · PI THOMPSON, ELIZABETH D · 1993 to 2022
$54.6M
Biochemistry and Physiological Role of Diacylglycerol Kinase ThetaR01NS077923 · NINDS · JOHNS HOPKINS UNIVERSITY · PI RABEN, DANIEL M. · 2013 to 2016
$1.4M
NCI NIH HHS P50 CA062924NINDS NIH HHS R01 NS077923
6 · The paper itself

Abstract

Lipid kinases regulate a wide variety of cellular functions and have emerged as one the most promising targets for drug design. Diacylglycerol kinases (DGKs) are a family of enzymes that catalyze the ATP-dependent phosphorylation of diacylglycerol (DAG) to phosphatidic acid (PtdOH). Despite the critical role in lipid biosynthesis, both DAG and PtdOH have been shown as bioactive lipids mediating a number of signaling pathways. Although there is increasing recognition of their role in signaling systems, our understanding of the key enzyme which regulate the balance of these two lipid messages remain limited. Solved structures provide a wealth of information for understanding the function and regulation of these enzymes. Solving the structures of mammalian DGKs by traditional NMR and X-ray crystallography approaches have been challenging and so far, there are still no three-dimensional structures of these DGKs. Despite this, some insights may be gained by examining the similarities and differences between prokaryotic DGKs and other mammalian lipid kinases. This review focuses on summarizing and comparing the structure of prokaryotic and mammalian DGKs as well as two other lipid kinases: sphingosine kinase and phosphatidylinositol-3-kinase. How these known lipid kinases structures relate to mammalian DGKs will also be discussed.

Indexed as

Diacylglycerol KinaseDiglyceridesPhosphatidic AcidsSignal TransductionAnimalsCrystallography, X-RayHumansPhosphorylationProtein Domains1,2-diacylglycerolDiacylglycerol KinaseDiglyceridesPhosphatidic Acids

Identifiers

PMID30348515
PMCPMC6347529
OpenAlexW2894426672

What Socratic 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 Socratic graph.