Evidence map›Paper›PMID 39916545›Full record

ArticleAngewandte Chemie (International ed. in English)2025

A Highly Selective and Versatile Probe Platform for Visualization of Monoacylglycerol Lipase.

Axel Hentsch, Mónica Guberman, Silke Radetzki, Sofia Kaushik, Mirjam Huizenga, Jerome Paul, Maria Schippers, Jörg Benz, Bernd Kuhn, Dominik Heer and 12 more

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. 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

22 authors.

Axel HentschLeibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Strasse 10, 13125, Berlin, GER.ORCID https://orcid.org/0000-0001-6968-1199
Mónica GubermanLeibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Strasse 10, 13125, Berlin, GER.ORCID https://orcid.org/0000-0002-2407-4771
Silke RadetzkiLeibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Strasse 10, 13125, Berlin, GER.ORCID https://orcid.org/0000-0003-2688-2868
Sofia KaushikLeibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Strasse 10, 13125, Berlin, GER.ORCID https://orcid.org/0000-0002-5757-764X
Mirjam HuizengaLeiden Institute of Chemistry (LIC), Universiteit Leiden, Einsteinweg 55, 2333 CC, Leiden, NL.
Jerome PaulLeibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Strasse 10, 13125, Berlin, GER.
Maria SchippersPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.
Jörg BenzPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.
Bernd KuhnPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.ORCID https://orcid.org/0000-0002-4301-562X
Dominik HeerPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.ORCID https://orcid.org/0009-0003-2089-4339
Andreas ToppPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.ORCID https://orcid.org/0009-0002-5511-2870
Ludivine Esteves GloriaPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.
Alexander WalterPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.
Remo HochstrasserPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.
Matthias B WittwerPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.ORCID https://orcid.org/0000-0003-1359-4795
Jens Peter von KriesLeibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Strasse 10, 13125, Berlin, GER.
Ludovic CollinPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.
Julie BlaisingPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.ORCID https://orcid.org/0000-0002-3367-6184
Mario van der SteltLeiden Institute of Chemistry (LIC), Universiteit Leiden, Einsteinweg 55, 2333 CC, Leiden, NL.
Noa LipsteinLeibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Strasse 10, 13125, Berlin, GER.ORCID https://orcid.org/0000-0002-0755-5899
Uwe GretherPharma Research & Early Development (pRED), F. Hoffmann-La Roche Ltd, Grenzacherstrasse 124, CH-4070, Basel, CH.ORCID https://orcid.org/0000-0002-3164-9270
Marc NazaréLeibniz Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Strasse 10, 13125, Berlin, GER.ORCID https://orcid.org/0000-0002-1602-2330

Funding

Deutsche Forschungsgemeinschaft CRC 1286Deutsche Forschungsgemeinschaft EXC-2049-390688087Volkswagen Foundation 9A867
6 · The paper itself

Abstract

Monoacylglycerol lipase (MAGL) is a key enzyme for signal termination in the endocannabinoid system (ECS). MAGL inhibition results in indirect activation of the cannabinoid receptors, which offers unique advantages for the treatment of, e.g., multiple sclerosis, epilepsy, and other neurological disorders. Molecular imaging techniques are valuable tools to overcome the current poor understanding of MAGL's distribution and role in patho- and physiological processes within ECS signaling. Herein, we report the design, synthesis, and validation of highly selective versatile fluorescent and click-chemistry probes for MAGL. Structure-based design combined with a reverse-design approach allowed the development of a structural unit that selectively and effectively recognizes MAGL while offering a versatile platform to attach different fluorophores and further reporter units. In this way, labeled probes with sub-nanomolar potency carrying diverse fluorescent dyes were obtained. Probe affinity and selectivity remained invariant to changes in the fluorophore subunit, showing the remarkable robustness of this platform in delivering tailor-made probes. Highly consistent inhibition across species supports pharmacological model translatability. Extensive profiling and validation in various cellular systems shows the ability of these highly potent and selective probes to elucidate the complex role of MAGL in ECS cellular signaling, inflammatory processes, and disease progression.

Indexed as

Fluorescent DyesMonoacylglycerol LipasesAnimalsClick ChemistryHumansMolecular StructureFluorescent DyesMonoacylglycerol Lipasesactivity-based protein profilingclick chemistryfluorescent probemicroscopymonoacylglycerol lipase

Identifiers

PMID39916545
PMCPMC11878344

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.