Evidence map›Paper›PMID 31428612›Full record

ReviewFrontiers in cell and developmental biology2019

The Structure and Function of Acylglycerophosphate Acyltransferase 4/ Lysophosphatidic Acid Acyltransferase Delta (AGPAT4/LPAATδ).

Mikhail A Zhukovsky, Angela Filograna, Alberto Luini, Daniela Corda, Carmen Valente

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cell and developmental biology, 2019. 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
2.4field-weighted citation impact, top 13% 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, 38 citations in OpenAlex.

  1. Article
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  8. Transcriptomic and Proteomic Insights Into Buffalo Milk Fat Synthesis and the Role of IGFBP4 in BMECs.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
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  17. [The regulation of APGAT4 on the growth and lenvatinib resistance of hepatocellular carcinoma].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2023
    Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Mikhail A ZhukovskyInstitute of Biochemistry and Cell Biology and Institute of Protein Biochemistry, National Research Council, Naples, Italy.
Angela FilogranaInstitute of Biochemistry and Cell Biology and Institute of Protein Biochemistry, National Research Council, Naples, Italy.
Alberto LuiniInstitute of Biochemistry and Cell Biology and Institute of Protein Biochemistry, National Research Council, Naples, Italy.
Daniela CordaInstitute of Biochemistry and Cell Biology and Institute of Protein Biochemistry, National Research Council, Naples, Italy.
Carmen ValenteInstitute of Biochemistry and Cell Biology and Institute of Protein Biochemistry, National Research Council, Naples, Italy.
National Research Council · ITInstitute of Protein Biochemistry · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid-modifying enzymes serve crucial roles in cellular processes such as signal transduction (producing lipid-derived second messengers), intracellular membrane transport (facilitating membrane remodeling needed for membrane fusion/fission), and protein clustering (organizing lipid domains as anchoring platforms). The lipid products crucial in these processes can derive from different metabolic pathways, thus it is essential to know the localization, substrate specificity, deriving products (and their function) of all lipid-modifying enzymes. Here we discuss an emerging family of these enzymes, the lysophosphatidic acid acyltransferases (LPAATs), also known as acylglycerophosphate acyltransferases (AGPATs), that produce phosphatidic acid (PA) having as substrates lysophosphatidic acid (LPA) and acyl-CoA. Eleven LPAAT/AGPAT enzymes have been identified in mice and humans based on sequence homologies, and their localization, specific substrates and functions explored. We focus on one member of the family, LPAATδ, a protein expressed mainly in brain and in muscle (though to a lesser extent in other tissues); while at the cellular level it is localized at the

Indexed as

acyltransferaseAGPATBARSGolgi complexLPAATlysophosphatidic acidmembrane fissionphosphatidic acid

Identifiers

PMID31428612
PMCPMC6688108
OpenAlexW2958351069

What OpenQuestion holds

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LicenceCC BY
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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.