Evidence map›Paper›PMID 26216043›Full record

ReviewChemistry and physics of lipids2016

Monoglyceride lipase: Structure and inhibitors.

Laura Scalvini, Daniele Piomelli, Marco Mor

Open access · greenAbstract readReview
In one paragraph

Review in Chemistry and physics of lipids, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
5.6field-weighted citation impact, top 4% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 67 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. The biological functions of monoacylglycerol lipase (MAGL) in cancer.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2026
    Review
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  19. Effect of monoacylglycerol lipase on the tumor growth in endometrial cancer.The journal of obstetrics and gynaecology research · 2019
    Article
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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

3 authors at 2 institutions in 2 countries.

Laura ScalviniDipartimento di Farmacia, Università degli Studi di Parma, I-43124 Parma, Italy.
Daniele PiomelliDepartment of Anatomy and Neurobiology, University of California, Irvine, Irvine, CA 92697, United States; Department of Biological Chemistry, University of California, Irvine, Irvine, CA 92697, United States; Unit of Drug Discovery and Development, Istituto Italiano di Tecnologia, Genova, Italy. Electronic address: piomelli@uci.edu.
Marco MorDipartimento di Farmacia, Università degli Studi di Parma, I-43124 Parma, Italy. Electronic address: marco.mor@unipr.it.
University of Parma · ITItalian Institute of Technology · IT

Funding

Characterization of Anandamide Transport in BrainR01DA012413 · NIDA · UNIVERSITY OF CALIFORNIA-IRVINE · PI PIOMELLI, DANIELE · 1998 to 2016
$4.7M
Optimization and preclinical development of FAAH inhibitors for smoking cessationDP1DA031387 · NIDA · UNIVERSITY OF CALIFORNIA-IRVINE · PI PIOMELLI, DANIELE · 2010 to 2014
$3.7M
NIDA NIH HHS DP1 DA031387NIDA NIH HHS R01 DA012413
6 · The paper itself

Abstract

Monoglyceride lipase (MGL), the main enzyme responsible for the hydrolytic deactivation of the endocannabinoid 2-arachidonoyl-sn-glycerol (2-AG), is an intracellular serine hydrolase that plays critical roles in many physiological and pathological processes, such as pain, inflammation, neuroprotection and cancer. The crystal structures of MGL that are currently available provide valuable information about how this enzyme might function and interact with site-directed small-molecule inhibitors. On the other hand, its conformational equilibria and the contribution of regulatory cysteine residues present within the substrate-binding pocket or on protein surface remain open issues. Several classes of MGL inhibitors have been developed, from early reversible ones, such as URB602 and pristimerin, to carbamoylating agents that react with the catalytic serine, such as JZL184 and more recent O-hexafluoroisopropyl carbamates. Other inhibitors that modulate MGL activity by interacting with conserved regulatory cysteines act through mechanisms that deserve to be more thoroughly investigated.

Indexed as

Crystallography, X-RayEnzyme InhibitorsHumansModels, MolecularMonoacylglycerol LipasesProtein ConformationEnzyme InhibitorsMonoacylglycerol Lipases2-Arachidonoyl-sn-glycerol (2-AG)CysteinesEndocannabinoidsInhibitorsLid domainMonoglyceride lipase (MGL)

Identifiers

PMID26216043
PMCPMC4728057
OpenAlexW1005113303

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.