Activity-based protein profiling reveals off-target proteins of the FAAH inhibitor BIA 10-2474

Isolation and Structure of a Brain Constituent That Binds to the Cannabinoid Receptor

Devane, W. A., Hanuš, L., Breuer, A., Pertwee, R. G., Stevenson, L. A., Griffin, G., Gibson, D., Mandelbaum, A., Etinger, A., & Mechoulam, R. (1992) · Science · doi:10.1126/science.1470919 · Cited by 5,633 · see citing works

Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides

Cravatt, B. F., Giang, D. K., Mayfield, S. P., Boger, D. L., Lerner, R. A., & Gilula, N. B. (1996) · Nature · doi:10.1038/384083a0 · Cited by 2,125 · see citing works

Modulation of anxiety through blockade of anandamide hydrolysis

Kathuria, S., Gaetani, S., Fegley, D., Valiño, F., Duranti, A., Tontini, A., Mor, M., Tarzia, G., Rana, G. L., Calignano, A., et al. (2003) · Nature Medicine · doi:10.1038/nm803 · Cited by 1,293 · see citing works

Activity-based protein profiling: The serine hydrolases

Liu, Y., Patricelli, M. P., & Cravatt, B. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14694 · Cited by 1,133 · see citing works

Dual blockade of FAAH and MAGL identifies behavioral processes regulated by endocannabinoid crosstalk in vivo

Long, J. Z., Nomura, D. K., Vann, R. E., Walentiny, D. M., Booker, L., Jin, X., Burston, J. J., Sim‐Selley, L. J., Lichtman, A. H., Wiley, J. L., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909411106 · Cited by 393 · see citing works

An efficient randomised, placebo-controlled clinical trial with the irreversible fatty acid amide hydrolase-1 inhibitor PF-04457845, which modulates endocannabinoids but fails to induce effective analgesia in patients with pain due to osteoarthritis of the knee

Huggins, J. P., Smart, T. S., Langman, S., Taylor, L., & Young, T. (2012) · Pain · doi:10.1016/j.pain.2012.04.020 · Cited by 375 · see citing works

Enzyme Inhibitor Discovery by Activity-Based Protein Profiling

Niphakis, M. J., & Cravatt, B. F. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035708 · Cited by 366 · see citing works

A road map to evaluate the proteome-wide selectivity of covalent kinase inhibitors

Lanning, B. R., Whitby, L. R., Dix, M. M., Douhan, J., Gilbert, A. M., Hett, E. C., Johnson, T., Joslyn, C. M., Kath, J. C., Niessen, S., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1582 · Cited by 356 · see citing works

Superfamily-wide portrait of serine hydrolase inhibition achieved by library-versus-library screening

Bachovchin, D. A., Ji, T., Li, W., Simon, G. M., Blankman, J. L., Adibekian, A., Hoover, H. S., Niessen, S., & Cravatt, B. F. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011663107 · Cited by 275 · see citing works

Anandamide acts as an intracellular messenger amplifying Ca2+ influx via TRPV1 channels

van der Stelt, M., Trevisani, M., Vellani, V., PETROCELLIS, L. D., Moriello, A. S., Campi, B., McNaughton, P. A., Geppetti, P., & Marzo, V. D. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600784 · Cited by 243 · see citing works

Mechanistic and Pharmacological Characterization of PF-04457845: A Highly Potent and Selective Fatty Acid Amide Hydrolase Inhibitor That Reduces Inflammatory and Noninflammatory Pain

Ahn, K., Smith, S. E., Liimatta, M. B., Beidler, D. R., Sadagopan, N., Dudley, D. T., Young, T., Wren, P. B., Zhang, Y., Swaney, S. M., et al. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.111.180257 · Cited by 229 · see citing works

Dual Effects of Anandamide on NMDA Receptor‐Mediated Responses and Neurotransmission

Hampson, A. J., Bornheim, L. M., Scanziani, M., Yost, C. S., Gray, A. T., Hansen, B. M., Leonoudakis, D., & Bickler, P. E. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70020671.x · Cited by 209 · see citing works

Discovery of PF-04457845: A Highly Potent, Orally Bioavailable, and Selective Urea FAAH Inhibitor

Johnson, D. S., Stiff, C. M., Lazerwith, S. E., Kesten, S. R., Fay, L. K., Morris, M. J., Beidler, D. R., Liimatta, M. B., Smith, S. E., Dudley, D. T., et al. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100190t · Cited by 200 · see citing works

The hereditary spastic paraplegia-related enzyme DDHD2 is a principal brain triglyceride lipase

Inloes, J. M., Hsu, K., Dix, M. M., Viader, A., Masuda, K. R., Takei, T., Wood, M. R., & Cravatt, B. F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413706111 · Cited by 175 · see citing works

RPLC-Ion-Trap-FTMS Method for Lipid Profiling of Plasma: Method Validation and Application to p53 Mutant Mouse Model

Hu, C., van Dommelen, J., van der Heijden, R., Spijksma, G. K., Reijmers, T. H., Wang, M., Slee, E. A., Lü, X., Xu, G., van der Greef, J., et al. (2008) · Journal of Proteome Research · doi:10.1021/pr800373m · Cited by 172 · see citing works

Acute Neurologic Disorder from an Inhibitor of Fatty Acid Amide Hydrolase

Kerbrat, A., Ferré, J.-C., Fillatre, P., Ronzière, T., Vannier, S., Carsin-Nicol, B., Lavoué, S., Vérin, M., Gauvrit, J.-Y., Le Tulzo, Y., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1604221 · Cited by 171 · see citing works

Rapid and profound rewiring of brain lipid signaling networks by acute diacylglycerol lipase inhibition

Ogasawara, D., Deng, H., Viader, A., Baggelaar, M. P., Breman, A. C., den Dulk, H., van den Nieuwendijk, A. M. C. H., Soethoudt, M., van der Wel, T., Zhou, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522364112 · Cited by 157 · see citing works

The Serine Hydrolase ABHD6 Is a Critical Regulator of the Metabolic Syndrome

Thomas, G., Betters, J. L., Lord, C. C., Brown, A. L., Marshall, S., Ferguson, D., Sawyer, J. K., Davis, M. A., Melchior, J., Blume, L. C., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.047 · Cited by 129 · see citing works

Assessment of the pharmacology and tolerability of PF‐04457845, an irreversible inhibitor of fatty acid amide hydrolase‐1, in healthy subjects

Li, G. L., Winter, H. R., Arends, R., Jay, G. W., Le, V., Young, T., & Huggins, J. P. (2011) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2011.04137.x · Cited by 125 · see citing works

Neuropathy target esterase impairments cause Oliver–McFarlane and Laurence–Moon syndromes

Hufnagel, R. B., Arno, G., Hein, N. D., Hersheson, J., Prasad, M. K., Anderson, Y. C., Krueger, L. A., Gregory, L. C., Stoetzel, C., Jaworek, T. J., et al. (2014) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2014-102856 · Cited by 123 · see citing works

Neuropathy target esterase (NTE): overview and future

Richardson, R. J., Hein, N. D., Wijeyesakere, S. J., Fink, J. K., & Махаева, Г. Ф. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.10.024 · Cited by 115 · see citing works

Loss-of-Function Mutations inPNPLA6Encoding Neuropathy Target Esterase Underlie Pubertal Failure and Neurological Deficits in Gordon Holmes Syndrome

Topaloglu, A. K., Lomniczi, A., Kretzschmar, D., Dissen, G. A., Kotan, L. D., McArdle, C. A., Koç, A., Hamel, B. C. J., Güçlü, M., Çakır, E. D. P., et al. (2014) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2014-1836 · Cited by 103 · see citing works

Neuropathy Target Esterase Is Required for Adult Vertebrate Axon Maintenance

Read, D. J., Li, Y., Chao, M. V., Cavanagh, J. B., & Glynn, P. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3007-09.2009 · Cited by 99 · see citing works

The novel, orally available and peripherally restricted selective cannabinoid CB2 receptor agonist LEI‐101 prevents cisplatin‐induced nephrotoxicity

Mukhopadhyay, P., Baggelaar, M. P., Erdélyi, K., Cao, Z., Çınar, R., Fezza, F., Ignatowska-Jankowska, B. M., Wilkerson, J. L., van Gils, N., Hansen, T. R., et al. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13338 · Cited by 86 · see citing works

Scientists in the dark after French clinical trial proves fatal

Butler, D., & Callaway, E. (2016) · Nature · doi:10.1038/nature.2016.19189 · Cited by 77 · see citing works

Development of an Activity‐Based Probe and In Silico Design Reveal Highly Selective Inhibitors for Diacylglycerol Lipase‐α in Brain

Baggelaar, M. P., Janssen, F. J., van Esbroeck, A. C. M., den Dulk, H., Allarà, M., Hoogendoorn, S., McGuire, R., Florea, B. I., Meeuwenoord, N. J., van den Elst, H., et al. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201306295 · Cited by 75 · see citing works

Molecular Characterization of Off-Target Activities of Telithromycin: a Potential Role for Nicotinic Acetylcholine Receptors

Bertrand, D., Bertrand, S., Neveu, E., & FERNANDES, P. B. (2010) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00840-10 · Cited by 74 · see citing works

Implications of the BIA‐102474‐101 study for review of first‐into‐human clinical trials

Eddleston, M., Cohen, A. F., & Webb, D. J. (2016) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.12920 · Cited by 66 · see citing works

Selective N-Hydroxyhydantoin Carbamate Inhibitors of Mammalian Serine Hydrolases

Cognetta, A. B., Niphakis, M. J., Lee, H., Martini, M. L., Hulce, J. J., & Cravatt, B. F. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.05.018 · Cited by 65 · see citing works

Highly Selective, Reversible Inhibitor Identified by Comparative Chemoproteomics Modulates Diacylglycerol Lipase Activity in Neurons

Baggelaar, M. P., Chameau, P. J. P., Kantae, V., Hummel, J. J. A., Hsu, K., Janssen, F. J., van der Wel, T., Soethoudt, M., Deng, H., den Dulk, H., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b04883 · Cited by 62 · see citing works

Cloning and expression of the murine sws/NTE gene

Moser, M., Stempfl, T., Li, Y., Glynn, P., Büttner, R., & Kretzschmar, D. (2000) · Mechanisms of Development · doi:10.1016/s0925-4773(99)00239-7 · Cited by 61 · see citing works

Enol Carbamates as Inhibitors of Fatty Acid Amide Hydrolase (FAAH) Endowed with High Selectivity for FAAH over the Other Targets of the Endocannabinoid System

Gattinoni, S., Simone, C. D., Dallavalle, S., Fezza, F., Nannei, R., Amadio, D., Minetti, P., Quattrociocchi, G., Caprioli, A., Borsini, F., et al. (2010) · ChemMedChem · doi:10.1002/cmdc.200900472 · Cited by 44 · see citing works

Synthesis, Biological Evaluation, and Molecular Modeling of 1-Benzyl-1H-imidazoles as Selective Inhibitors of Aldosterone Synthase (CYP11B2)

Roumen, L., Peeters, J. W., Emmen, J. M. A., Beugels, I. P. E., Custers, E. M. G., de Gooyer, M. E., Plate, R., Pieterse, K., Hilbers, P. A. J., Smits, J. F. M., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901356d · Cited by 41 · see citing works

Prostamide F2 α receptor antagonism combined with inhibition of FAAH may block the pro‐inflammatory mediators formed following selective FAAH inhibition

Ligresti, A., Martos, J. L., Wang, J. W., Guida, F., Allarà, M., Palmieri, V., Luongo, L., Woodward, D. F., & Marzo, V. D. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12410 · Cited by 35 · see citing works

Neuropathy target esterase: An essential enzyme for neural development and axonal maintenance

Chang, P., & Wu, Y. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.12.007 · Cited by 35 · see citing works

Discovery of Glycine Sulfonamides as Dual Inhibitors ofsn-1-Diacylglycerol Lipase α and α/β-Hydrolase Domain 6

Janssen, F. J., Deng, H., Baggelaar, M. P., Allarà, M., van der Wel, T., den Dulk, H., Ligresti, A., van Esbroeck, A. C. M., McGuire, R., Marzo, V. D., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500681z · Cited by 33 · see citing works

Fast Halogenation of Some N‐Heterocycles by Means of N,N′‐Dihalo‐5,5‐dimethylhydantoin

Sandtorv, A. H., & Bjørsvik, H. (2013) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201200723 · Cited by 31 · see citing works

A natural substrate-based fluorescence assay for inhibitor screening on diacylglycerol lipase α

van der Wel, T., Janssen, F. J., Baggelaar, M. P., Deng, H., den Dulk, H., Overkleeft, H. S., & van der Stelt, M. (2015) · Journal of Lipid Research · doi:10.1194/jlr.d056390 · Cited by 29 · see citing works

A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective ligation of azides and terminal alkynes

Rostovtsev, V. V., Green, L. G., Fokin, V. V., & Sharpless, K. B. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020715)41:14

Cannabinoid Receptors and the Endocannabinoid System: Signaling and Function in the Central Nervous System

Zou, S., & Kumar, U. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030833 · Cited by 1,362 · see citing works

Bioorthogonal chemistry

Scinto, S. L., Bilodeau, D. A., Hincapie, R., Lee, W., Nguyen, S. S., Xu, M., Ende, C. W. A., Finn, M. G., Lang, K., Lin, Q., et al. (2021) · Nature Reviews Methods Primers · doi:10.1038/s43586-021-00028-z · Cited by 620 · see citing works

New approaches and challenges to targeting the endocannabinoid system

Marzo, V. D. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.115 · Cited by 480 · see citing works

Is it possible to overcome issues of external validity in preclinical animal research? Why most animal models are bound to fail

Pound, P., & Ritskes-Hoitinga, M. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1678-1 · Cited by 419 · see citing works

Click Chemistry in Proteomic Investigations

Parker, C. G., & Pratt, M. R. (2020) · Cell · doi:10.1016/j.cell.2020.01.025 · Cited by 386 · see citing works

Bioactive lipids, inflammation and chronic diseases

Leuti, A., Fazio, D., Fava, M., Piccoli, A., Oddi, S., & Maccarrone, M. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.06.028 · Cited by 368 · see citing works

Chemotherapy-induced peripheral neuropathy: where are we now?

Colvin, L. (2019) · Pain · doi:10.1097/j.pain.0000000000001540 · Cited by 402 · see citing works

The emerging role of mass spectrometry-based proteomics in drug discovery

Meissner, F., Geddes‐McAlister, J., Mann, M., & Bantscheff, M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00409-3 · Cited by 355 · see citing works

The endogenous cannabinoid system: a budding source of targets for treating inflammatory and neuropathic pain

Donvito, G., Nass, S. R., Wilkerson, J. L., Curry, Z. A., Schurman, L. D., Kinsey, S. G., & Lichtman, A. H. (2018) · Neuropsychopharmacology · doi:10.1038/npp.2017.204 · Cited by 301 · see citing works

Organophosphorus Compounds at 80: Some Old and New Issues

Costa, L. G. (2017) · Toxicological Sciences · doi:10.1093/toxsci/kfx266 · Cited by 280 · see citing works

Novel pharmacological targets in drug development for the treatment of anxiety and anxiety-related disorders

Sartori, S. B., & Singewald, N. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107402 · Cited by 236 · see citing works

Recent advances in activity-based probes (ABPs) and affinity-based probes (A f BPs) for profiling of enzymes

Fang, H., Peng, B., Ong, S. Y., Wu, Q., Li, L., & Yao, S. Q. (2021) · Chemical Science · doi:10.1039/d1sc01359a · Cited by 210 · see citing works

Cannabinoid Signaling in the Skin: Therapeutic Potential of the “C(ut)annabinoid” System

Tóth, K. F., Ádám, D., Bı́ró, T., & Oláh, A. (2019) · Molecules · doi:10.3390/molecules24050918 · Cited by 209 · see citing works

The Molecular Industrial Revolution: Automated Synthesis of Small Molecules

Trobe, M., & Burke, M. D. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201710482 · Cited by 194 · see citing works

Efficacy and safety of a fatty acid amide hydrolase inhibitor (PF-04457845) in the treatment of cannabis withdrawal and dependence in men: a double-blind, placebo-controlled, parallel group, phase 2a single-site randomised controlled trial

D’Souza, D. C., Cortes-Briones, J., Creatura, G. M., Bluez, G., Thurnauer, H., Deaso, E., Forselius-Bielen, K., Surti, T. S., Radhakrishnan, R., Gupta, A., et al. (2018) · The Lancet Psychiatry · doi:10.1016/s2215-0366(18)30427-9 · Cited by 195 · see citing works

Therapeutic Potential of Cannabidiol (CBD) for Skin Health and Disorders

Baswan, S. M., Klosner, A. E., Glynn, K. M., Rajgopal, A., Malik, K. A., Yim, S., & Stern, N. (2020) · Clinical Cosmetic and Investigational Dermatology · doi:10.2147/ccid.s286411 · Cited by 194 · see citing works

Monoacylglycerol lipase inhibitors: modulators for lipid metabolism in cancer malignancy, neurological and metabolic disorders

Deng, H., & Li, W. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.10.006 · Cited by 182 · see citing works

Commentary on the <scp>EMA Guideline</scp> on strategies to identify and mitigate risks for first‐in‐human and early clinical trials with investigational medicinal products

van Gerven, J., & Bonelli, M. (2018) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.13550 · Cited by 174 · see citing works

Anandamide and other N-acylethanolamines: A class of signaling lipids with therapeutic opportunities

Mock, E. D., Gagestein, B., & van der Stelt, M. (2022) · Progress in Lipid Research · doi:10.1016/j.plipres.2022.101194 · Cited by 158 · see citing works

The endocannabinoid system and its therapeutic exploitation in multiple sclerosis: Clues for other neuroinflammatory diseases

Chiurchiù, V., van der Stelt, M., Centonze, D., & Maccarrone, M. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.10.007 · Cited by 140 · see citing works

Advances and Challenges in Computational Target Prediction

Sydow, D., Burggraaff, L., Szengel, A., van Vlijmen, H., IJzerman, A. P., van Westen, G. J. P., & Volkamer, A. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00832 · Cited by 127 · see citing works

Targeting Endocannabinoid Signaling: FAAH and MAG Lipase Inhibitors

van Egmond, N., Straub, V. M., & van der Stelt, M. (2020) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-030220-112741 · Cited by 129 · see citing works

Targeting Cannabinoid Signaling in the Immune System: “High”-ly Exciting Questions, Possibilities, and Challenges

Oláh, A., Szekanecz, Z., & Bı́ró, T. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01487 · Cited by 123 · see citing works

Solvent-Induced Protein Precipitation for Drug Target Discovery on the Proteomic Scale

Zhang, X., Wang, Q., Li, Y., Ruan, C., Wang, S., Hu, L., & Ye, M. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b04531 · Cited by 119 · see citing works

Activity-based protein profiling: Recent advances in medicinal chemistry

Deng, H., Lei, Q., Wu, Y., He, Y., & Li, W. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112151 · Cited by 119 · see citing works

Neurobiology of cannabinoid receptor signaling

Lutz, B. (2020) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2020.22.3/blutz · Cited by 112 · see citing works

The effects of inhibition of fatty acid amide hydrolase (FAAH) by JNJ-42165279 in social anxiety disorder: a double-blind, randomized, placebo-controlled proof-of-concept study

Schmidt, M. E., Liebowitz, M. R., Stein, M. B., Grunfeld, J. A., Hove, I. V., Simmons, W. K., van der Ark, P. D., Palmer, J. A., Saad, Z. S., Pemberton, D. J., et al. (2020) · Neuropsychopharmacology · doi:10.1038/s41386-020-00888-1 · Cited by 105 · see citing works

Enhanced endocannabinoid tone as a potential target of pharmacotherapy

Toczek, M., & Malinowska, B. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.04.054 · Cited by 104 · see citing works

Emerging targetome and signalome landscape of gut microbial metabolites

Zheng, X., Cai, X., & Hao, H. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2021.12.011 · Cited by 100 · see citing works

Photoaffinity labelling strategies for mapping the small molecule–protein interactome

Burton, N. R., Kim, P., & Backus, K. M. (2021) · Organic & Biomolecular Chemistry · doi:10.1039/d1ob01353j · Cited by 101 · see citing works

Covalent Small Molecules as Enabling Platforms for Drug Discovery

Dalton, S. E., & Campos, S. (2019) · ChemBioChem · doi:10.1002/cbic.201900674 · Cited by 98 · see citing works

A perspective review on fatty acid amide hydrolase (FAAH) inhibitors as potential therapeutic agents

Tripathi, R. K. P. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111953 · Cited by 95 · see citing works

Discovery of a NAPE-PLD inhibitor that modulates emotional behavior in mice

Mock, E. D., Mustafa, M. A., Gunduz‐Cinar, O., Çınar, R., Petrie, G. N., Kantae, V., Di, X., Ogasawara, D., Varga, Z. V., Pálóczi, J., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0528-7 · Cited by 95 · see citing works

Targeting the Endocannabinoid System in the Treatment of Posttraumatic Stress Disorder: A Promising Case of Preclinical-Clinical Translation?

Mayo, L. M., Rabinak, C. A., Hill, M. N., & Heilig, M. A. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2021.07.019 · Cited by 93 · see citing works

Cannabinoids: from pot to lab

Papaseit, E., Pérez‐Mañá, C., Pérez-Acevedo, A. P., Hladun, O., Torres-Moreno, M. C., Muga, R., Torrens, M., & Farré, M. (2018) · International Journal of Medical Sciences · doi:10.7150/ijms.27087 · Cited by 84 · see citing works

A quantitative thiol reactivity profiling platform to analyze redox and electrophile reactive cysteine proteomes

Fu, L., Li, Z., Liu, K., Tian, C., He, J.-X., He, J., He, F., Xu, P., & Yang, J. H. (2020) · Nature Protocols · doi:10.1038/s41596-020-0352-2 · Cited by 84 · see citing works

Selective Photoaffinity Probe That Enables Assessment of Cannabinoid CB2 Receptor Expression and Ligand Engagement in Human Cells

Soethoudt, M., Stolze, S. C., Westphal, M. V., van Stralen, L., Martella, A., van Rooden, E. J., Guba, W., Varga, Z. V., Deng, H., van Kasteren, S. I., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.7b11281 · Cited by 80 · see citing works

Importance of Quantifying Drug-Target Engagement in Cells

Stefaniak, J., & Huber, K. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00570 · Cited by 78 · see citing works

Chemoproteomic methods for covalent drug discovery

Chan, W. C., Sharifzadeh, S., Buhrlage, S. J., & Marto, J. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00231g · Cited by 78 · see citing works

Cannabinoid interventions for PTSD: Where to next?

Ney, L. J., Matthews, A. J., Bruno, R., & Felmingham, K. L. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.03.017 · Cited by 76 · see citing works

Advancing Covalent Ligand and Drug Discovery beyond Cysteine

Kim, G., Grams, R. J., & Hsu, K. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.5c00001 · Cited by 77 · see citing works

The selective reversible FAAH inhibitor, SSR411298, restores the development of maladaptive behaviors to acute and chronic stress in rodents

Griebel, G., Stemmelin, J., Lopez‐Grancha, M., Fauchey, V., Slowinski, F., Pichat, P., Dargazanli, G., Abouabdellah, A., Cohen, C., & Bergis, O. E. (2018) · Scientific Reports · doi:10.1038/s41598-018-20895-z · Cited by 76 · see citing works

In situ identification of cellular drug targets in mammalian tissue

Pang, Z., Schafroth, M. A., Ogasawara, D., Wang, Y., Nudell, V., Lal, N. K., Yang, D. U., Wang, K., Herbst, D. M., Ha, J., et al. (2022) · Cell · doi:10.1016/j.cell.2022.03.040 · Cited by 71 · see citing works

Small-molecule probes from bench to bedside: advancing molecular analysis of drug–target interactions toward precision medicine

Pan, S., Ding, A., Li, Y., Sun, Y., Zhan, Y., Ye, Z., Song, N., Peng, B., Li, L., Huang, W., et al. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00056g · Cited by 71 · see citing works

Targeted Covalent Modification Strategies for Drugging the Undruggable Targets

Tamura, T., Kawano, M., & Hamachi, I. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00745 · Cited by 71 · see citing works

Drug Target Identification in Tissues by Thermal Proteome Profiling

Mateus, A., Kurzawa, N., Perrin, J., Bergamini, G., & Savitski, M. M. (2021) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-052120-013205 · Cited by 69 · see citing works

Emerging Approaches for the Identification of Protein Targets of Small Molecules - A Practitioners’ Perspective

Comess, K. M., McLoughlin, S. M., Oyer, J. A., Richardson, P. L., Stöckmann, H., Vasudevan, A., & Warder, S. E. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01921 · Cited by 66 · see citing works

Impaired anandamide/palmitoylethanolamide signaling in hippocampal glutamatergic neurons alters synaptic plasticity, learning, and emotional responses

Zimmermann, T., Bartsch, J., Beer, A., Lomazzo, E., Guggenhuber, S., Lange, M. D., Bîndilă, L., Pape, H., & Lutz, B. (2018) · Neuropsychopharmacology · doi:10.1038/s41386-018-0274-7 · Cited by 66 · see citing works

Potential of Cannabinoid Receptor Ligands as Treatment for Substance Use Disorders

Galaj, E., & Xi, Z. (2019) · CNS Drugs · doi:10.1007/s40263-019-00664-w · Cited by 65 · see citing works

Mapping in vivo target interaction profiles of covalent inhibitors using chemical proteomics with label-free quantification

van Rooden, E. J., Florea, B. I., Deng, H., Baggelaar, M. P., van Esbroeck, A. C. M., Zhou, J., Overkleeft, H. S., & van der Stelt, M. (2018) · Nature Protocols · doi:10.1038/nprot.2017.159 · Cited by 63 · see citing works

Machine learning for target discovery in drug development

Rodrigues, T., & Bernardes, G. J. L. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.10.003 · Cited by 60 · see citing works

In vivo inactivation of glycosidases by conduritol B epoxide and cyclophellitol as revealed by activity‐based protein profiling

Kuo, C. J., Kallemeijn, W. W., Lelieveld, L. T., Mirzaian, M., Zoutendijk, I., Vardi, A., Futerman, A. H., Meijer, A. H., Spaink, H. P., Overkleeft, H. S., et al. (2019) · FEBS Journal · doi:10.1111/febs.14744 · Cited by 61 · see citing works

A practical guide to secondary pharmacology in drug discovery

Jenkinson, S. G., Schmidt, F., Ribeiro, L. R., Delaunois, A. G., & Valentin, J. (2020) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/j.vascn.2020.106869 · Cited by 61 · see citing works

The Chemistry of Cannabis and Cannabinoids

Duggan, P. J. (2021) · Australian Journal of Chemistry · doi:10.1071/ch21006 · Cited by 61 · see citing works

Epoxy Fatty Acids Are Promising Targets for Treatment of Pain, Cardiovascular Disease and Other Indications Characterized by Mitochondrial Dysfunction, Endoplasmic Stress and Inflammation

McReynolds, C. B., Morisseau, C. H. P., Wagner, K. M., & Hammock, B. D. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-50621-6_5 · Cited by 59 · see citing works

A monoacylglycerol lipase inhibitor showing therapeutic efficacy in mice without central side effects or dependence

Jiang, M., Huizenga, M. C. W., Wirt, J. L., Pálóczi, J., Amedi, A., van den Berg, R. J. B. H. N., Benz, J., Collin, L., Deng, H., Di, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43606-3 · Cited by 59 · see citing works

Research progress of mechanisms and drug therapy for neuropathic pain

Yan, Y., Li, C.-Y., Zhou, L., Ao, L., Fang, W., & Li, Y. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.09.033 · Cited by 57 · see citing works

α/β-Hydrolase Domain (ABHD) Inhibitors as New Potential Therapeutic Options against Lipid-Related Diseases

Bononi, G., Tuccinardi, T., Rizzolio, F., & Granchi, C. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00624 · Cited by 56 · see citing works

The state of the art in secondary pharmacology and its impact on the safety of new medicines

Brennan, R., Jenkinson, S. G., Brown, A. J., Delaunois, A. G., Dumotier, B. M., Pannirselvam, M., Rao, M., Ribeiro, L. R., Schmidt, F., Sibony, A., et al. (2024) · Nature Reviews Drug Discovery · doi:10.1038/s41573-024-00942-3 · Cited by 57 · see citing works

The endocannabinoid system in cardiovascular function: novel insights and clinical implications

Sierra, S., Luquin, N., & Navarro‐Otano, J. (2017) · Clinical Autonomic Research · doi:10.1007/s10286-017-0488-5 · Cited by 56 · see citing works

Combination treatment with FAAH inhibitors/URB597 and ferroptosis inducers significantly decreases the growth and metastasis of renal cell carcinoma cells via the PI3K-AKT signaling pathway

Hao, J., Chen, Q., Feng, Y., Jiang, Q., Sun, H., Deng, B., Huang, X., Guan, J., Chen, Q., Liu, X., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05779-z · Cited by 53 · see citing works

Chemoproteomics, A Broad Avenue to Target Deconvolution

Gao, Y., Ma, M., Li, W., & Lei, X. (2023) · Advanced Science · doi:10.1002/advs.202305608 · Cited by 52 · see citing works

Recent efforts to elucidate the scientific validity of animal-based drug tests by the pharmaceutical industry, pro-testing lobby groups, and animal welfare organisations

Bailey, J., & Balls, M. (2019) · BMC Medical Ethics · doi:10.1186/s12910-019-0352-3 · Cited by 51 · see citing works

Targeting Peripherally Restricted Cannabinoid Receptor 1, Cannabinoid Receptor 2, and Endocannabinoid-Degrading Enzymes for the Treatment of Neuropathic Pain Including Neuropathic Orofacial Pain

Hossain, M. Z., Ando, H., Unno, S., & Kitagawa, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041423 · Cited by 52 · see citing works

Reviewing the role of healthy volunteer studies in drug development

Karakunnel, J. J., Bui, N. Q., Palaniappan, L. P., Schmidt, K. T., Mahaffey, K. W., Morrison, B. W., Figg, W. D., & Kummar, S. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1710-5 · Cited by 50 · see citing works

The role of fatty acid amide hydrolase enzyme inhibitors in Alzheimer's disease

Jain, S., Bisht, A., Verma, K., Negi, S., Paliwal, S., & Sharma, S. K. (2021) · Cell Biochemistry and Function · doi:10.1002/cbf.3680 · Cited by 51 · see citing works

FAAH inhibition as a preventive treatment for migraine: A pre-clinical study

Greco, R., Demartini, C., Zanaboni, A. M., Tumelero, E., Reggiani, A. M., Misto, A., Piomelli, D., & Tassorelli, C. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104624 · Cited by 49 · see citing works

Therapeutic potential and safety considerations for the clinical use of synthetic cannabinoids

Sholler, D. J., Huestis, M. A., Amendolara, B., Vandrey, R. G., & Cooper, Z. D. (2020) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2020.173059 · Cited by 48 · see citing works

Recent Advances in the Potential of Cannabinoids for Neuroprotection in Alzheimer’s, Parkinson’s, and Huntington’s Diseases

Pérez-Olives, C., Rivas‐Santisteban, R., Lillo, J., Navarro, G., & Franco, R. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-57369-0_6 · Cited by 46 · see citing works

Global Portrait of Protein Targets of Metabolites of the Neurotoxic Compound BIA 10–2474

Huang, Z., Ogasawara, D., Seneviratne, U. I., Cognetta, A. B., Ende, C. W. A., Nason, D. M., Lapham, K., Litchfield, J., Johnson, D. S., & Cravatt, B. F. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01097 · Cited by 46 · see citing works

Synthesis of green benzamide-decorated UiO-66-NH2 for biomedical applications

Rabiee, N., Ghadiri, A. M., Alinezhad, V., Sedaghat, A., Ahmadi, S., Fatahi, Y., Makvandi, P., Saeb, M. R., Bagherzadeh, M., Asadnia, M., et al. (2022) · Chemosphere · doi:10.1016/j.chemosphere.2022.134359 · Cited by 46 · see citing works

Endocannabinoids in Body Weight Control

Horn, H., Böhme, B., Dietrich, L., & Koch, M. (2018) · Pharmaceuticals · doi:10.3390/ph11020055 · Cited by 46 · see citing works

Development of a Multiplexed Activity-Based Protein Profiling Assay to Evaluate Activity of Endocannabinoid Hydrolase Inhibitors

Janssen, A. P. A., van der Vliet, D., Bakker, A. T., Jiang, M., Grimm, S. H., Campiani, G., Butini, S., & van der Stelt, M. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00534 · Cited by 45 · see citing works

Monitoring protein communities and their responses to therapeutics

Budayeva, H. G., & Kirkpatrick, D. S. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0063-y · Cited by 41 · see citing works

Covalent binders in drug discovery

Vasudevan, A., Argiriadi, M. A., Baranczak, A., Friedman, M., Gavrilyuk, J. I., Hobson, A. D., Hulce, J. J., Osman, S., & Wilson, N. S. (2019) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2018.12.002 · Cited by 42 · see citing works

A Systematic Review With Meta-Analysis of the Efficacy of Cannabis and Cannabinoids for Inflammatory Bowel Disease

Doeve, B. H., van de Meeberg, M. M., van Schaik, F. D. M., & Fidder, H. H. (2020) · Journal of Clinical Gastroenterology · doi:10.1097/mcg.0000000000001393 · Cited by 43 · see citing works

Development and biological applications of sulfur–triazole exchange (SuTEx) chemistry

Borne, A. L., Brulet, J. W., Yuan, K., & Hsu, K. (2021) · RSC Chemical Biology · doi:10.1039/d0cb00180e · Cited by 42 · see citing works

Re-Evaluating the Mechanism of Action of α,β-Unsaturated Carbonyl DUB Inhibitors b-AP15 and VLX1570: A Paradigmatic Example of Unspecific Protein Cross-linking with Michael Acceptor Motif-Containing Drugs

Ward, J., Pinto-Fernández, A., Cornelissen, L., Bonham, S., Saez, L. D., Riant, O., Huber, K., Kessler, B. M., Féron, O., & Tate, E. W. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00144 · Cited by 41 · see citing works

Inner Engineering Practices and Advanced 4‐day Isha Yoga Retreat Are Associated with Cannabimimetic Effects with Increased Endocannabinoids and Short‐Term and Sustained Improvement in Mental Health: A Prospective Observational Study of Meditators

Sadhasivam, S., Alankar, S., Maturi, R. K., Vishnubhotla, R. V., Mudigonda, M., Pawale, D., Narayanan, S., Hariri, S., Ram, C., Chang, T. F. H., et al. (2020) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2020/8438272 · Cited by 41 · see citing works

Recent Advances in Activity-Based Protein Profiling of Proteases

Chakrabarty, S., Kahler, J. P., van de Plassche, M. A. T., Vanhoutte, R., & Verhelst, S. H. L. (2018) · Current topics in microbiology and immunology · doi:10.1007/82_2018_138 · Cited by 40 · see citing works

Activity-Based Protein Profiling Delivers Selective Drug Candidate ABX-1431, a Monoacylglycerol Lipase Inhibitor, To Control Lipid Metabolism in Neurological Disorders

Jiang, M., & van der Stelt, M. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01405 · Cited by 40 · see citing works

Phosphorus-Based Probes as Molecular Tools for Proteome Studies: Recent Advances in Probe Development and Applications

Joachimiak, Ł., & Błażewska, K. M. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00249 · Cited by 39 · see citing works

Endocannabinoid System in the Airways

Bozkurt, T. E. (2019) · Molecules · doi:10.3390/molecules24244626 · Cited by 40 · see citing works

The endocannabinoid system – current implications for drug development

Fowler, C. J. (2020) · Journal of Internal Medicine · doi:10.1111/joim.13229 · Cited by 38 · see citing works

Novel approaches and current challenges with targeting the endocannabinoid system

Morales, P., & Jagerovic, N. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1752178 · Cited by 38 · see citing works

Antidepressant-like effects of URB597 and JZL184 in male and female rats exposed to early life stress

Alteba, S., Zer‐Aviv, T. M., Tenenhaus, A., David, G. B., Adelman, J. W., Hillard, C. J., Doron, R., & Akirav, I. (2020) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2020.08.005 · Cited by 37 · see citing works

The endocannabinoid system in the amygdala and modulation of fear

Gunduz‐Cinar, O. (2020) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2020.110116 · Cited by 38 · see citing works

The Endocannabinoid System as a Pharmacological Target for New Cancer Therapies

Ramer, R., Wittig, F., & Hinz, B. (2021) · Cancers · doi:10.3390/cancers13225701 · Cited by 38 · see citing works

Profiling the Protein Targets of Unmodified Bio‐Active Molecules with Drug Affinity Responsive Target Stability and Liquid Chromatography/Tandem Mass Spectrometry

Hwang, H., Kim, T. Y., Szász, M. A., Döme, B., Malm, J., Marko‐Varga, G., & Kwon, H. J. (2020) · PROTEOMICS · doi:10.1002/pmic.201900325 · Cited by 36 · see citing works

Chemical Proteomics Reveals Antibiotic Targets of Oxadiazolones in MRSA

Bakker, A. T., Kotsogianni, I., Mirenda, L., Straub, V. M., Ávalos, M., van den Berg, R. J. B. H. N., Florea, B. I., van Wezel, G. P., Janssen, A. P. A., Martin, N. I., et al. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c10819 · Cited by 36 · see citing works

Catalytic asymmetric synthesis of meta benzene isosteres

Zhang, M., Chapman, M., Sarode, B. R., Xiong, B., Liang, H., Chen, J., Weerapana, E., & Morken, J. P. (2024) · Nature · doi:10.1038/s41586-024-07865-4 · Cited by 35 · see citing works

Design and Potency of Dual Soluble Epoxide Hydrolase/Fatty Acid Amide Hydrolase Inhibitors

Kodani, S. D., Wan, D., Wagner, K. M., Hwang, S. H., Morisseau, C. H. P., & Hammock, B. D. (2018) · ACS Omega · doi:10.1021/acsomega.8b01625 · Cited by 35 · see citing works

The Potential of Cannabinoid-Based Treatments in Tourette Syndrome

Artukoglu, B. B., & Bloch, M. H. (2019) · CNS Drugs · doi:10.1007/s40263-019-00627-1 · Cited by 37 · see citing works

Cannabinoids: Revealing their complexity and role in central networks of fear and anxiety

Murkar, A., Koninck, J. D., & Merali, Z. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.09.002 · Cited by 34 · see citing works

A Medicinal Chemistry Perspective on FDA-Approved Small Molecule Drugs with a Covalent Mechanism of Action

Dalton, S. E., Pietro, O. D., & Hennessy, E. T. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02661 · Cited by 34 · see citing works

In vitro secondary pharmacological profiling: An IQ-DruSafe industry survey on current practices

Valentin, J., Guillon, J.-M., Jenkinson, S. G., Kadambi, V. J., Peri, R., Roberts, S., Ribeiro, L. R., Schmidt, F., & Armstrong, D. (2018) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/j.vascn.2018.07.001 · Cited by 33 · see citing works

Can preclinical drug development help to predict adverse events in clinical trials?

Chi, L. H., Burrows, A. D., & Anderson, R. L. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.08.010 · Cited by 34 · see citing works

AI-empowered perturbation proteomics for complex biological systems

Qian, L., Sun, R., Aebersold, R. H., Bühlmann, P., Sander, C., & Guo, T. (2024) · Cell Genomics · doi:10.1016/j.xgen.2024.100691 · Cited by 31 · see citing works

Anticancer Potential of Small‐Molecule Inhibitors of Fatty Acid Amide Hydrolase and Monoacylglycerol Lipase

Jaiswal, S., & Ayyannan, S. R. (2021) · ChemMedChem · doi:10.1002/cmdc.202100120 · Cited by 33 · see citing works

Role of palmitoylethanolamide (PEA) in depression: Translational evidence

Gregorio, D. D., Manchia, M., Carpiniello, B., Valtorta, F., Nobile, M., Gobbi, G., & Comai, S. (2018) · Journal of Affective Disorders · doi:10.1016/j.jad.2018.10.117 · Cited by 32 · see citing works

A clue to a drug's neurotoxicity?

Kiberstis, P. A. (2017) · Science · doi:10.1126/science.356.6342.1040-h

Tracking off-targets

Farrell, A. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2445 · Cited by 2 · see citing works

Global Portrait of Protein Targets of Metabolites of the Neurotoxic Compound BIA 10–2474

Huang, Z., Ogasawara, D., Seneviratne, U. I., Cognetta, A. B., Ende, C. W. A., Nason, D. M., Lapham, K., Litchfield, J., Johnson, D. S., & Cravatt, B. F. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.8b01097 · Cited by 46 · see citing works

Preclinical pharmacological evaluation of the fatty acid amide hydrolase inhibitor BIA 10‐2474

Bonifácio, M. J., Sousa, F., Aires, C. C. P., Loureiro, A. I., Fernandes‐Lopes, C., Pires, N. M., Palma, P. N., Moser, P. C., & Soares-da-Silva, P. (2020) · British Journal of Pharmacology · doi:10.1111/bph.14973 · Cited by 16 · see citing works

EVALUATION OF THE POTENCY AND SELECTIVITY OF THE NOVEL FAAH INHIBITOR BIA 10‐2474 IN COMPARISON WITH PF‐04457845 AND JNJ‐42165279

Bonifácio, M. J., Sousa, F., Aires, C. C. P., Loureiro, A. I., Fernandes‐Lopes, C., Palma, P. N., Moser, P. C., & Soares-da-Silva, P. (2018) · The FASEB Journal · doi:10.1096/fasebj.2018.32.1_supplement.692.14 · Cited by 2 · see citing works