Evidence map›Paper›PMID 32271712›Full record

ArticleeLife2020

Cooperative enzymatic control of N-acyl amino acids by PM20D1 and FAAH.

Joon T Kim, Stephanie M Terrell, Veronica L Li, Wei Wei, Curt R Fischer, Jonathan Z Long

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-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

17 citing papers in PubMed, 23 citations in OpenAlex.

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  6. A human gutScience (New York, N.Y.) · 2024
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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

6 authors at 1 institution in 1 country.

Joon T KimDepartment of Pathology, Stanford University School of Medicine, Stanford, United States.ORCID 0000-0002-8663-1414
Stephanie M TerrellDepartment of Pathology, Stanford University School of Medicine, Stanford, United States.
Veronica L LiDepartment of Pathology, Stanford University School of Medicine, Stanford, United States.
Wei WeiDepartment of Pathology, Stanford University School of Medicine, Stanford, United States.
Curt R FischerStanford ChEM-H, Stanford University, Stanford, United States.ORCID 0000-0003-3386-9813
Jonathan Z LongDepartment of Pathology, Stanford University School of Medicine, Stanford, United States.ORCID 0000-0003-2631-7463
Stanford University · US

Funding

Stanford Islet Research CoreP30DK116074 · NIDDK · STANFORD UNIVERSITY · PI Seung K Kim · 2017 to 2026
$19.5M
Chemical control of energy metabolism by N-acyl amino acidsR01DK124265 · NIDDK · STANFORD UNIVERSITY · PI LONG, JONATHAN Z · 2020 to 2024
$2.0M
CIRCULATING FACTORS THAT REGULATE BROWN AND BEIGE FATR00DK105203 · NIDDK · STANFORD UNIVERSITY · PI LONG, JONATHAN Z · 2018 to 2020
$728k
Circulating Factors that Regulate Brown and Beige FatK99DK105203 · NIDDK · DANA-FARBER CANCER INST · PI LONG, JONATHAN Z · 2015 to 2016
$182k
NIDDK NIH HHS K99 DK105203NIDDK NIH HHS P30 DK116074NIDDK NIH HHS R00 DK105203NIDDK NIH HHS R01 DK124265
6 · The paper itself

Abstract

The N-acyl amino acids are a family of bioactive lipids with pleiotropic physiologic functions, including in energy homeostasis. Their endogenous levels are regulated by an extracellular mammalian N-acyl amino acid synthase/hydrolase called PM20D1 (peptidase M20 domain containing 1). Using an activity-guided biochemical approach, we report the molecular identification of fatty acid amide hydrolase (FAAH) as a second intracellular N-acyl amino acid synthase/hydrolase. In vitro, FAAH exhibits a more restricted substrate scope compared to PM20D1. In mice, genetic ablation or selective pharmacological inhibition of FAAH bidirectionally dysregulates intracellular, but not circulating, N-acyl amino acids. Dual blockade of both PM20D1 and FAAH reveals a dramatic and non-additive biochemical engagement of these two enzymatic pathways. These data establish FAAH as a second intracellular pathway for N-acyl amino acid metabolism and underscore enzymatic division of labor as an enabling strategy for the regulation of a structurally diverse bioactive lipid family.

Indexed as

AmidohydrolasesAmino AcidsAnimalsFatty Acid Amide HydrolasesMaleMiceMice, Inbred C57BLAmidohydrolasesAmino AcidsFatty Acid Amide HydrolasesPM20D1 protein, mousebiochemistrychemical biologyenzymeFAAHlipidsmouseN-acyl amino acidPM20D1signaling

Identifiers

PMID32271712
PMCPMC7145423
OpenAlexW3016200112

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.