Evidence map›Paper›PMID 24708409›Full record

ReviewJournal of biomedical science2014

Diacylglycerol kinase as a possible therapeutic target for neuronal diseases.

Yasuhito Shirai, Naoaki Saito

Open access · diamondAbstract readReview
In one paragraph

Review in Journal of biomedical science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Momordicine I alleviates isoproterenol-induced cardiomyocyte hypertrophy through suppression of PLA2G6 and DGK-ζ.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Changes in lipid profiles of epileptic mouse model.Metabolomics : Official journal of the Metabolomic Society · 2020
    Article
  13. Molecular Signature of Pruriceptive MrgprA3The Journal of investigative dermatology · 2020
    Article
  14. Review
  15. Review
  16. Effect of Heavy IonMolecules (Basel, Switzerland) · 2020
    Article
  17. Diacylglycerol kinases regulate TRPV1 channel activity.The Journal of biological chemistry · 2020
    Article
  18. Review
  19. Article
  20. Roles of DGKs in neurons: Postsynaptic functions?Advances in biological regulation · 2020
    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

2 authors at 1 institution in 1 country.

Yasuhito ShiraiLaboratory of Chemistry and Utilization of Animal Production Resources, Applied Chemistry in Bioscience Division, Graduate School of Agricultural Science, Kobe University, Rokkodai-cho 1-1, Nada-ku, 657-8501 Kobe, Japan. shirai@kobe-u.ac.jp.
Naoaki Saito
Kobe University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diacylglycerol kinase (DGK) is a lipid kinase converting diacylglycerol to phosphatidic acid, and regulates many enzymes including protein kinase C, phosphatidylinositol 4-phosphate 5-kinase, and mTOR. To date, ten mammalian DGK subtypes have been cloned and divided into five groups, and they show subtype-specific tissue distribution. Therefore, each DGK subtype is thought to be involved in respective cellular responses by regulating balance of the two lipid messengers, diacylglycerol and phosphatidic acid. Indeed, the recent researches using DGK knockout mice have clearly demonstrated the importance of DGK in the immune system and its pathophysiological roles in heart and insulin resistance in diabetes. Especially, most subtypes show high expression in brain with subtype specific regional distribution, suggesting that each subtype has important and unique functions in brain. Recently, neuronal functions of some DGK subtypes have accumulated. Here, we introduce DGKs with their structural motifs, summarize the enzymatic properties and neuronal functions, and discuss the possibility of DGKs as a therapeutic target of the neuronal diseases.

Indexed as

AnimalsBrainDiacylglycerol KinaseHumansMiceMolecular Targeted TherapyNeuronsPhosphotransferases (Alcohol Group Acceptor)Protein Kinase CSignal TransductionTissue DistributionTOR Serine-Threonine Kinases1-phosphatidylinositol-4-phosphate 5-kinaseDiacylglycerol KinaseMTOR protein, humanPhosphotransferases (Alcohol Group Acceptor)Protein Kinase CTOR Serine-Threonine Kinases

Identifiers

PMID24708409
PMCPMC4005014
OpenAlexW2164694144

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.