Evidence map›Paper›PMID 27571266›Full record

ArticleACS chemical biology2016

Bile Acid Recognition by NAPE-PLD.

Eleonora Margheritis, Beatrice Castellani, Paola Magotti, Sara Peruzzi, Elisa Romeo, Francesca Natali, Serena Mostarda, Antimo Gioiello, Daniele Piomelli, Gianpiero Garau

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

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  14. Symmetrically substituted dichlorophenes inhibitThe Journal of biological chemistry · 2020
    Article
  15. Article
  16. Review
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  19. Metabolic Effects of Bile Acids: Potential Role in Bariatric Surgery.Cellular and molecular gastroenterology and hepatology · 2019
    Review
  20. Secondary Unconjugated Bile Acids Induce Hepatic Stellate Cell Activation.International journal of molecular sciences · 2018
    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

10 authors at 4 institutions in 3 countries.

Eleonora MargheritisCenter for Nanotechnology Innovation@NEST, Istituto Italiano di Tecnologia , Piazza San Silvestro 12, 56127 Pisa, Italy.
Beatrice CastellaniDepartment of Drug Discovery-Validation, Istituto Italiano di Tecnologia , Via Morego 30, 16163 Genoa, Italy.
Paola MagottiDepartment of Drug Discovery-Validation, Istituto Italiano di Tecnologia , Via Morego 30, 16163 Genoa, Italy.
Sara PeruzziCenter for Nanotechnology Innovation@NEST, Istituto Italiano di Tecnologia , Piazza San Silvestro 12, 56127 Pisa, Italy.
Elisa RomeoDepartment of Drug Discovery-Validation, Istituto Italiano di Tecnologia , Via Morego 30, 16163 Genoa, Italy.
Francesca NataliInstitute Laue-Langevin (ILL) and CNR-IOM , 71 avenue des Martyrs, 38042 Grenoble, France.
Serena MostardaDepartment of Pharmaceutical Sciences, University of Perugia , Via del Liceo 1, 06125 Perugia, Italy.
Antimo GioielloDepartment of Pharmaceutical Sciences, University of Perugia , Via del Liceo 1, 06125 Perugia, Italy.
Daniele PiomelliDepartment of Drug Discovery-Validation, Istituto Italiano di Tecnologia , Via Morego 30, 16163 Genoa, Italy.
Gianpiero GarauCenter for Nanotechnology Innovation@NEST, Istituto Italiano di Tecnologia , Piazza San Silvestro 12, 56127 Pisa, Italy.
Italian Institute of Technology · ITCenter for Nanotechnology Innovation · ITUniversity of Perugia · ITInstitut Langevin · FR

Funding

Characterization of Anandamide Transport in BrainR01DA012413 · NIDA · UNIVERSITY OF CALIFORNIA-IRVINE · PI PIOMELLI, DANIELE · 1998 to 2016
$4.7M
Role of oleoylethanolamide in the control of food intakeR01DK073955 · NIDDK · UNIVERSITY OF CALIFORNIA-IRVINE · PI PIOMELLI, DANIELE · 2007 to 2010
$1.3M
NIDA NIH HHS R01 DA012413NIDDK NIH HHS R01 DK073955
6 · The paper itself

Abstract

The membrane-associated enzyme NAPE-PLD (N-acyl phosphatidylethanolamine specific-phospholipase D) generates the endogenous cannabinoid arachidonylethanolamide and other lipid signaling amides, including oleoylethanolamide and palmitoylethanolamide. These bioactive molecules play important roles in several physiological pathways including stress and pain response, appetite, and lifespan. Recently, we reported the crystal structure of human NAPE-PLD and discovered specific binding sites for the bile acid deoxycholic acid. In this study, we demonstrate that in the presence of this secondary bile acid, the stiffness of the protein measured by elastic neutron scattering increases, and NAPE-PLD is ∼7 times faster to catalyze the hydrolysis of the more unsaturated substrate N-arachidonyl-phosphatidylethanolamine, compared with N-palmitoyl-phosphatidylethanolamine. Chenodeoxycholic acid and glyco- or tauro-dihydroxy conjugates can also bind to NAPE-PLD and drive its activation. The only natural monohydroxy bile acid, lithocholic acid, shows an affinity of ∼20 μM and acts instead as a reversible inhibitor (IC

Indexed as

Bile Acids and SaltsCrystallography, X-RayHumansKineticsPhospholipase DProtein ConformationStructure-Activity RelationshipSubstrate SpecificityBile Acids and SaltsNAPEPLD protein, humanPhospholipase D

Identifiers

PMID27571266
PMCPMC5074845
OpenAlexW2512565177

What OpenQuestion holds

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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.