Evidence map›Paper›PMID 30077006›Full record

ReviewBiochimica et biophysica acta. Molecular and cell biology of lipids2019

Lysosomal phospholipase A2.

James A Shayman, John J G Tesmer

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 70 citations in OpenAlex.

  1. The Phospholipase AJournal of lipid and atherosclerosis · 2026
    Review
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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 2 institutions in 1 country.

James A ShaymanDepartment of Internal Medicine, University of Michigan Medical School, University of Michigan, Ann Arbor, MI, USA. Electronic address: jshayman@umich.edu.
John J G TesmerDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA.
Purdue University West Lafayette · USUniversity of Michigan–Ann Arbor · US

Funding

Structure and Function of the LPLA2/LCAT Acyltransferase FamilyR01HL122416 · NHLBI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI TESMER, JOHN · 2015 to 2018
$1.9M
Lysosomal Phospholipase A2 in Autoimmune DiseaseR01AR056991 · NIAMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHAYMAN, JAMES ALAN · 2010 to 2014
$1.6M
The Development of Small Molecule Inhibitors for Gaucher Disease Type 3UH3NS092981 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LARSEN, SCOTT D, SHAYMAN, JAMES ALAN · 2016 to 2019
$1.5M
Mechanisms of Drug Induced PhospholipidosisI01BX002021 · VA · VETERANS HEALTH ADMINISTRATION · PI SHAYMAN, JAMES ALAN · 2013 to 2016
–
BLRD VA I01 BX002021NHLBI NIH HHS R01 HL122416NIAMS NIH HHS R01 AR056991NINDS NIH HHS UH3 NS092981
6 · The paper itself

Abstract

Lysosomal phospholipase A2 (PLA2G15) is a ubiquitous enzyme uniquely characterized by a subcellular localization to the lysosome and late endosome. PLA2G15 has an acidic pH optimum, is calcium independent, and acts as a transacylase in the presence of N-acetyl-sphingosine as an acceptor. Recent studies aided by the delineation of the crystal structure of PLA2G15 have clarified further the catalytic mechanism, sn-1 versus sn-2 specificity, and the basis whereby cationic amphiphilic drugs inhibit its activity. PLA2G15 has recently been shown to hydrolyze short chain oxidized phospholipids which access the catalytic site directly based on their aqueous solubility. Studies on the PLA2G15 null mouse suggest a role for the enzyme in the catabolism of pulmonary surfactant. PLA2G15 may also have a role in host defense and in the processing of lipid antigens for presentation by CD1 proteins. This article is part of a Special Issue entitled Novel functions of phospholipase A2 Guest Editors: Makoto Murakami and Gerard Lambeau.

Indexed as

AnimalsHumansHydrolysisLysosomesOxidation-ReductionPhospholipases A2PhospholipidsPhospholipases A2PhospholipidsAntigen presentationCeramideLysosomePhospholipase A2PhospholipidosisTuberculosis

Identifiers

PMID30077006
PMCPMC6361722
OpenAlexW2885284144

What OpenQuestion 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 OpenQuestion graph.