Evidence map›Paper›PMID 34843683›Full record

ArticleJournal of lipid research2022

Selective measurement of NAPE-PLD activity via a PLA

Jonah E Zarrow, Jianhua Tian, Brendan Dutter, Kwangho Kim, Amanda C Doran, Gary A Sulikowski, Sean S Davies

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of lipid research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 26% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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

7 authors at 2 institutions in 1 country.

Jonah E ZarrowChemical and Physical Biology Program, Vanderbilt University, Nashville, TN, USA; Department of Pharmacology, Vanderbilt University, Nashville, TN, USA.
Jianhua TianVanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN, USA.
Brendan DutterVanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN, USA.
Kwangho KimVanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN, USA; Department of Chemistry, Vanderbilt University, Nashville, TN, USA.
Amanda C DoranDivision of Cardiovascular Medicine, Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA.
Gary A SulikowskiDepartment of Pharmacology, Vanderbilt University, Nashville, TN, USA; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN, USA; Department of Chemistry, Vanderbilt University, Nashville, TN, USA.
Sean S DaviesDepartment of Pharmacology, Vanderbilt University, Nashville, TN, USA; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN, USA. Electronic address: sean.davies@vanderbilt.edu.
Vanderbilt University · USVanderbilt University Medical Center · US

Funding

Non-coding RNA & Bioinformatics CoreP01HL116263 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI LINTON, MACRAE F · 2014 to 2025
$24.7M
Chemistry-Biology Interface Training GrantT32GM065086 · NIGMS · VANDERBILT UNIVERSITY · PI BACHMANN, BRIAN O, SULIKOWSKI, GARY ALLEN · 2002 to 2022
$7.0M
Critical Mediators of Inflammation Resolution and Immune Memory in AtherosclerosisR01HL159487 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DORAN, AMANDA C · 2021 to 2025
$3.2M
NHLBI NIH HHS P01 HL116263NHLBI NIH HHS R01 HL159487NIGMS NIH HHS T32 GM065086
6 · The paper itself

Abstract

N-acyl-phosphatidylethanolamine (NAPE)-hydrolyzing phospholipase D (NAPE-PLD) is a zinc metallohydrolase enzyme that converts NAPEs to bioactive N-acyl-ethanolamides. Altered NAPE-PLD activity may contribute to pathogenesis of obesity, diabetes, atherosclerosis, and neurological diseases. Selective measurement of NAPE-PLD activity is challenging, however, because of alternative phospholipase pathways for NAPE hydrolysis. Previous methods to measure NAPE-PLD activity involved addition of exogenous NAPE followed by TLC or LC/MS/MS, which are time and resource intensive. Recently, NAPE-PLD activity in cells has been assayed using the fluorogenic NAPE analogs PED-A1 and PED6, but these substrates also detect the activity of serine hydrolase-type lipases PLA

Indexed as

PhosphatidylethanolaminesPhospholipases A2Fluorescent DyesHumansHydrolysisPhospholipase DPhospholipases A1Fluorescent DyesN-acylphosphatidylethanolaminePhosphatidylethanolaminesPhospholipase DPhospholipases A1Phospholipases A2atherosclerosisbiothionoldiabetesfluorescenceN-acylethanolamideN-acylphosphatidylethanolamideNAPE-PLDnociceptionphospholipase A1tetrahydrolipstatin

Identifiers

PMID34843683
PMCPMC8953660
OpenAlexW3216582622

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.