Evidence map›Paper›PMID 28930429›Full record

ArticleACS chemical biology2017

Mapping Protein Targets of Bioactive Small Molecules Using Lipid-Based Chemical Proteomics.

Kenneth M Lum, Yoshiaki Sato, Brittney A Beyer, Warren C Plaisted, Justin L Anglin, Luke L Lairson, Benjamin F Cravatt

Abstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 31 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Kenneth M LumDepartment of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
Yoshiaki SatoDepartment of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
Brittney A BeyerDepartment of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
Warren C PlaistedCalifornia Institute for Biomedical Research , La Jolla, California 92037, United States.
Justin L AnglinCalifornia Institute for Biomedical Research , La Jolla, California 92037, United States.
Luke L LairsonDepartment of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
Benjamin F CravattDepartment of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.ORCID 0000-0001-5330-3492
Scripps Research Institute · USCalifornia Institute for Biomedical Research · US

Funding

Chemoproteomic Identification and Therapeutic Validation of Proteins of Metabolic SignificanceRC2DK114785 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F, SAEZ, ENRIQUE · 2017 to 2021
$8.2M
Chemical Probes for Metabolic Pathway Discovery in Human DiseaseR01CA132630 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2007 to 2018
$5.1M
NCI NIH HHS R01 CA132630NIDDK NIH HHS RC2 DK114785
6 · The paper itself

Abstract

Lipids play critical roles in cell biology, often through direct interactions with proteins. We recently described the use of photoreactive lipid probes combined with quantitative mass spectrometry to globally map lipid-protein interactions, and the effects of drugs on these interactions, in cells. Here, we investigate the broader potential of lipid-based chemical proteomic probes for determining the cellular targets of biologically active small molecules, including natural product derivatives and repurposed drugs of ill-defined mechanisms. We identify the prostaglandin-regulatory enzyme PTGR2 as a target of the antidiabetic hops derivative KDT501 and show that miconazole-an antifungal drug that attenuates disease severity in preclinical models of multiple sclerosis-inhibits SGPL1, an enzyme that degrades the signaling lipid sphingosine-1-phosphate, drug analogues of which are used to treat multiple sclerosis in humans. Our findings highlight the versatility of lipid-based chemical proteomics probes for mapping small molecule-protein interactions in human cells to gain mechanistic understanding of bioactive compounds.

Indexed as

Drug DesignDrug DiscoveryHEK293 CellsHumansLipidsMass SpectrometryProtein BindingProteinsProteomicsSmall Molecule LibrariesLipidsProteinsSmall Molecule Libraries

Identifiers

PMID28930429
PMCPMC5650530
OpenAlexW2755365362

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.