2024:

Akefe, I. O., Saber, S. H., Matthews, B., Venkatesh, B. G., Gormal, R. S., Blackmore, D. G., Alexander, S., Sieriecki, E., Gambin, Y., Bertran-Gonzalez, J., Vitale, N., Humeau, Y., Gaudin, A., Ellis, S. A., Michaels, A. A., Xue, M., Cravatt, B., Joensuu, M., Wallis, T. P., & Meunier, F. A. (2024). The DDHD2-STXBP1 interaction mediates long-term memory via generation of saturated free fatty acids. EMBO J, 43(4), 533-567. https://doi.org/10.1038/s44318-024-00030-7 

Stanton, C., Sun, J., Nutsch, K., Rosarda, J. D., Nguyen, T., Li-Ma, C., Njomen, E., Melillo, B., Kutseikin, S., Saez, E., Cravatt, B. F., Teijaro, J. R., Wiseman, R. L., & Bollong, M. J. (2024). Covalent Targeting As a Common Mechanism for Inhibiting NLRP3 Inflammasome Assembly. ACS Chem Biol, 19(2), 254-265. https://doi.org/10.1021/acschembio.3c00330 

2023:

Tao, Y., Felber, J. G., Zou, Z., Njomen, E., Remsberg, J., Ogasawara, D., Ye, C., Melillo, B., Schreiber, S. L., He, C., Remillard, D., & Cravatt, B. (2023). Chemical proteomic discovery of isotype-selective covalent inhibitors of the RNA Methyltransferase NSUN2. Angew Chem Int Ed Engl, e202311924. https://doi.org/10.1002/anie.202311924 

Wichroski M, Benci J, Liu SQ, Chupak L, Fang J, Cao C, Wang C, Onorato J, Qiu H, Shan Y, Banas D, Powles R, Locke G, Witt A, Stromko C, Qi H, Zheng X, Martin S, Ding M, Gentles R, Meanwell N, Velaparthi U, Olson R, Wee S, Tenney D, Parker CG, Cravatt BF, Lawrence M, Borzilleri R, Lees E. (2023). DGKα/ζ inhibitors combine with PD-1 checkpoint therapy to promote T cell-mediated antitumor immunity. Sci Transl Med, 15(719), eadh1892. https://doi.org/10.1126/scitranslmed.adh1892 

Li, H., Ma, T., Remsberg, J. R., Won, S. J., DeMeester, K. E., Njomen, E., Ogasawara, D., Zhao, K. T., Huang, T. P., Lu, B., Simon, G. M., Melillo, B., Schreiber, S. L., Lykke-Andersen, J., Liu, D. R., & Cravatt, B. F. (2023). Assigning functionality to cysteines by base editing of cancer dependency genes. Nature Chemical Biology, 19(11), 1320-1330. https://doi.org/10.1038/s41589-023-01428-w 

Vozella, V., Cruz, B., Feldman, H. C., Bullard, R., Bianchi, P. C., Natividad, L. A., Cravatt, B. F., Zorrilla, E. P., Ciccocioppo, R., & Roberto, M. (2023). Sexually dimorphic effects of monoacylglycerol lipase inhibitor MJN110 on stress-related behaviors and drinking in Marchigian Sardinian alcohol-preferring rats. Br J Pharmacol. https://doi.org/10.1111/bph.16197 

Zhang, Y., Remillard, D., Onubogu, U., Karakyriakou, B., Asiaban, J. N., Ramos, A. R., Bowland, K., Bishop, T. R., Barta, P. A., Nance, S., Durbin, A. D., Ott, C. J., Janiszewska, M., Cravatt, B. F., & Erb, M. A. (2023). Collateral lethality between HDAC1 and HDAC2 exploits cancer-specific NuRD complex vulnerabilities. Nat Struct Mol Biol. https://doi.org/10.1038/s41594-023-01041-4 

Sharma, T., Zhang, Y., Zigrossi, A., Cravatt, B. F., & Kastrati, I. (2023). Dimethyl fumarate inhibits ZNF217 and can be beneficial in a subset of estrogen receptor positive breast cancers. Breast Cancer Res Treat. https://doi.org/10.1007/s10549-023-07037-4 

Cravatt, B. F. (2023). Activity-based protein profiling - finding general solutions to specific problems. Isr J Chem, 63(3-4). https://doi.org/10.1002/ijch.202300029 

Lazear, M. R., Remsberg, J. R., Jaeger, M. G., Rothamel, K., Her, H.-l., DeMeester, K. E., Njomen, E., Hogg, S. J., Rahman, J., Whitby, L. R., Won, S. J., Schafroth, M. A., Ogasawara, D., Yokoyama, M., Lindsey, G. L., Li, H., Germain, J., Barbas, S., Vaughan, J., . . . Cravatt, B. F. (2023) Proteomic discovery of chemical probes that perturb protein complexes in human cells. Molecular Cell. https://doi.org/10.1016/j.molcel.2023.03.026 

Kathman, S. G., Koo, S. J., Lindsey, G. L., Her, H. L., Blue, S. M., Li, H., Jaensch, S., Remsberg, J. R., Ahn, K., Yeo, G. W., Ghosh, B., & Cravatt, B. F. (2023). Remodeling oncogenic transcriptomes by small molecules targeting NONO. Nature Chemical Biology. https://doi.org/10.1038/s41589-023-01270-0 

Darabedian, N., Ji, W., Fan, M., Lin, S., Seo, H. S., Vinogradova, E. V., Yaron, T. M., Mills, E. L., Xiao, H., Senkane, K., Huntsman, E. M., Johnson, J. L., Che, J., Cantley, L. C., Cravatt, B. F., Dhe-Paganon, S., Stegmaier, K., Zhang, T., Gray, N. S., & Chouchani, E. T. (2023). Depletion of creatine phosphagen energetics with a covalent creatine kinase inhibitor. Nature Chemical Biology. https://doi.org/10.1038/s41589-023-01273-x 

Reed, A., Ware, T., Li, H., Fernando Bazan, J., & Cravatt, B. F. (2023). TMEM164 is an acyltransferase that forms ferroptotic C20:4 ether phospholipids. Nature Chemical Biology. https://doi.org/10.1038/s41589-022-01253-7

Asantewaa, G., Tuttle, E. T., Ward, N. P., Kang, Y. P., Kim, Y., Kavanagh, M. E., Girnius, N., Chen, Y., Duncan, R., Rodriguez, K., Hecht, F., Zocchi, M., Smorodintsev-Schiller, L., Scales, T. Q., Taylor, K., Alimohammadi, F., Sechrist, Z. R., Agostini-Vulaj, D., Schafer, X. L., . . . Harris, I. S. (2023). Glutathione supports lipid abundance in vivo. bioRxiv. https://doi.org/10.1101/2023.02.10.524960

2022:

Xu, C., Yadav-Samudrala, B. J., Xu, C., Nath, B., Mistry, T., Jiang, W., Niphakis, M. J., Cravatt, B. F., Mukhopadhyay, S., Lichtman, A. H., Ignatowska-Jankowska, B. M., & Fitting, S. (2022). Inhibitory Neurotransmission Is Sex-Dependently Affected by Tat Expression in Transgenic Mice and Suppressed by the Fatty Acid Amide Hydrolase Enzyme Inhibitor PF3845 via Cannabinoid Type-1 Receptor Mechanisms. Cells, 11(5). https://doi.org/10.3390/cells11050857

Tao, Y., Remillard, D., Vinogradova, E. V., Yokoyama, M., Banchenko, S., Schwefel, D., Melillo, B., Schreiber, S. L., Zhang, X., & Cravatt, B. F. (2022). Targeted Protein Degradation by Electrophilic PROTACs that Stereoselectively and Site-Specifically Engage DCAF1. J Am Chem Soc, 144(40), 18688-18699. https://doi.org/10.1021/jacs.2c08964

Rinschen, M. M., Palygin, O., El-Meanawy, A., Domingo-Almenara, X., Palermo, A., Dissanayake, L. V., Golosova, D., Schafroth, M. A., Guijas, C., Demir, F., Jaegers, J., Gliozzi, M. L., Xue, J., Hoehne, M., Benzing, T., Kok, B. P., Saez, E., Bleich, M., Himmerkus, N., . . . Staruschenko, A. (2022). Accelerated lysine metabolism conveys kidney protection in salt-sensitive hypertension. Nat Commun, 13(1), 4099. https://doi.org/10.1038/s41467-022-31670-0

Reed, A., Ichu, T. A., Milosevich, N., Melillo, B., Schafroth, M. A., Otsuka, Y., Scampavia, L., Spicer, T. P., & Cravatt, B. F. (2022). LPCAT3 Inhibitors Remodel the Polyunsaturated Phospholipid Content of Human Cells and Protect from Ferroptosis. ACS Chem Biol, 17(6), 1607-1618. https://doi.org/10.1021/acschembio.2c00317

Pang, Z., Schafroth, M. A., Ogasawara, D., Wang, Y., Nudell, V., Lal, N. K., Yang, D., Wang, K., Herbst, D. M., Ha, J., Guijas, C., Blankman, J. L., Cravatt, B. F., & Ye, L. (2022). In situ identification of cellular drug targets in mammalian tissue. Cell, 185(10), 1793-1805 e1717. https://doi.org/10.1016/j.cell.2022.03.040

Morimoto, K., Krahn, D., Kaschani, F., Hopkinson-Woolley, D., Gee, A., Buscaill, P., Mohammed, S., Sieber, S. A., Cravatt, B. F., Schofield, C. J., & van der Hoorn, R. A. L. (2022). Broad-range metalloprotease profiling in plants uncovers immunity provided by defence-related metalloenzyme. New Phytol, 235(3), 1287-1301. https://doi.org/10.1111/nph.18200

Li, M., Patel, H. V., Cognetta, A. B., 3rd, Smith, T. C., 2nd, Mallick, I., Cavalier, J. F., Previti, M. L., Canaan, S., Aldridge, B. B., Cravatt, B. F., & Seeliger, J. C. (2022). Identification of cell wall synthesis inhibitors active against Mycobacterium tuberculosis by competitive activity-based protein profiling. Cell Chem Biol, 29(5), 883-896 e885. https://doi.org/10.1016/j.chembiol.2021.09.002

Li, F. L., Fu, V., Liu, G., Tang, T., Konradi, A. W., Peng, X., Kemper, E., Cravatt, B. F., Franklin, J. M., Wu, Z., Mayfield, J., Dixon, J. E., Gerwick, W. H., & Guan, K. L. (2022). Hippo pathway regulation by phosphatidylinositol transfer protein and phosphoinositides. Nature Chemical Biology, 18(10), 1076-1086. https://doi.org/10.1038/s41589-022-01061-z

Kemper, E. K., Zhang, Y., Dix, M. M., & Cravatt, B. F. (2022). Global profiling of phosphorylation-dependent changes in cysteine reactivity. Nat Methods, 19(3), 341-352. https://doi.org/10.1038/s41592-022-01398-2

Kavanagh, M. E., Horning, B. D., Khattri, R., Roy, N., Lu, J. P., Whitby, L. R., Ye, E., Brannon, J. C., Parker, A., Chick, J. M., Eissler, C. L., Wong, A. J., Rodriguez, J. L., Rodiles, S., Masuda, K., Teijaro, J. R., Simon, G. M., Patricelli, M. P., & Cravatt, B. F. (2022). Selective inhibitors of JAK1 targeting an isoform-restricted allosteric cysteine. Nature Chemical Biology, 18(12), 1388-1398. https://doi.org/10.1038/s41589-022-01098-0

Kavanagh, M. E., Horning, B. D., Khattri, R., Roy, N., Lu, J. P., Whitby, L. R., Ye, E., Brannon, J. C., Parker, A., Chick, J. M., Eissler, C. L., Wong, A. J., Rodriguez, J. L., Rodiles, S., Masuda, K., Teijaro, J. R., Simon, G. M., Patricelli, M. P., & Cravatt, B. F. (2022). Author Correction: Selective inhibitors of JAK1 targeting an isoform-restricted allosteric cysteine. Nature Chemical Biology, 18(11), 1288. https://doi.org/10.1038/s41589-022-01181-6

Feldman, H. C., Merlini, E., Guijas, C., DeMeester, K. E., Njomen, E., Kozina, E. M., Yokoyama, M., Vinogradova, E., Reardon, H. T., Melillo, B., Schreiber, S. L., Loreto, A., Blankman, J. L., & Cravatt, B. F. (2022). Selective inhibitors of SARM1 targeting an allosteric cysteine in the autoregulatory ARM domain. Proc Natl Acad Sci U S A, 119(35), e2208457119. https://doi.org/10.1073/pnas.2208457119

Deng, L., Viray, K., Singh, S., Cravatt, B., & Stella, N. (2022). ABHD6 Controls Amphetamine-Stimulated Hyperlocomotion: Involvement of CB(1) Receptors. Cannabis Cannabinoid Res, 7(2), 188-198. https://doi.org/10.1089/can.2021.0066

Cheng, R., Fujinaga, M., Yang, J., Rong, J., Haider, A., Ogasawara, D., Van, R. S., Shao, T., Chen, Z., Zhang, X., Calderon Leon, E. R., Zhang, Y., Mori, W., Kumata, K., Yamasaki, T., Xie, L., Sun, S., Wang, L., Ran, C., . . . Liang, S. H. (2022). A novel monoacylglycerol lipase-targeted (18)F-labeled probe for positron emission tomography imaging of brown adipose tissue in the energy network. Acta Pharmacol Sin, 43(11), 3002-3010. https://doi.org/10.1038/s41401-022-00912-8

Carvalho, L. A. R., Ross, B., Fehr, L., Bolgi, O., Wohrle, S., Lum, K. M., Podlesainski, D., Vieira, A. C., Kiefersauer, R., Felix, R., Rodrigues, T., Lucas, S. D., Gross, O., Geiss-Friedlander, R., Cravatt, B. F., Huber, R., Kaiser, M., & Moreira, R. (2022). Chemoproteomics-Enabled Identification of 4-Oxo-beta-Lactams as Inhibitors of Dipeptidyl Peptidases 8 and 9. Angew Chem Int Ed Engl, 61(47), e202210498. https://doi.org/10.1002/anie.202210498

Bainbridge, M. N., Mazumder, A., Ogasawara, D., Abou Jamra, R., Bernard, G., Bertini, E., Burglen, L., Cope, H., Crawford, A., Derksen, A., Dure, L., Gantz, E., Koch-Hogrebe, M., Hurst, A. C. E., Mahida, S., Marshall, P., Micalizzi, A., Novelli, A., Peng, H., . . . Friedman, J. (2022). Endocannabinoid dysfunction in neurological disease: neuro-ocular DAGLA-related syndrome. Brain, 145(10), 3383-3390. https://doi.org/10.1093/brain/awac223

2021:

Zhang, X., Thielert, M., Li, H., & Cravatt, B. F. (2021). SPIN4 Is a Principal Endogenous Substrate of the E3 Ubiquitin Ligase DCAF16. Biochemistry, 60(9), 637-642. https://doi.org/10.1021/acs.biochem.1c00067

Zhang, X., Luukkonen, L. M., Eissler, C. L., Crowley, V. M., Yamashita, Y., Schafroth, M. A., Kikuchi, S., Weinstein, D. S., Symons, K. T., Nordin, B. E., Rodriguez, J. L., Wucherpfennig, T. G., Bauer, L. G., Dix, M. M., Stamos, D., Kinsella, T. M., Simon, G. M., Baltgalvis, K. A., & Cravatt, B. F. (2021). DCAF11 Supports Targeted Protein Degradation by Electrophilic Proteolysis-Targeting Chimeras. J Am Chem Soc, 143(13), 5141-5149. https://doi.org/10.1021/jacs.1c00990

Vinogradova, E. V., & Cravatt, B. F. (2021). Multiplexed proteomic profiling of cysteine reactivity and ligandability in human T cells. STAR Protoc, 2(2), 100458. https://doi.org/10.1016/j.xpro.2021.100458

Suciu, R. M., Luvaga, I. K., Hazeen, A., Weerasooriya, C., Richardson, S. K., Firestone, A. J., Shannon, K., Howell, A. R., & Cravatt, B. F. (2021). Chemical proteomic analysis of palmostatin beta-lactone analogs that affect N-Ras palmitoylation. Bioorg Med Chem Lett, 53, 128414. https://doi.org/10.1016/j.bmcl.2021.128414

Ruiz-Perez, G., Ruiz de Martin Esteban, S., Marques, S., Aparicio, N., Grande, M. T., Benito-Cuesta, I., Martinez-Relimpio, A. M., Arnanz, M. A., Tolon, R. M., Posada-Ayala, M., Cravatt, B. F., Esteban, J. A., Romero, J., & Palenzuela, R. (2021). Potentiation of amyloid beta phagocytosis and amelioration of synaptic dysfunction upon FAAH deletion in a mouse model of Alzheimer's disease. J Neuroinflammation, 18(1), 223. https://doi.org/10.1186/s12974-021-02276-y

Rosier, K., McDevitt, M. T., Smet, J., Floyd, B. J., Verschoore, M., Marcaida, M. J., Bingman, C. A., Lemmens, I., Dal Peraro, M., Tavernier, J., Cravatt, B. F., Gounko, N. V., Vints, K., Monnens, Y., Bhalla, K., Aerts, L., Rashan, E. H., Vanlander, A. V., Van Coster, R., . . . Creemers, J. W. M. (2021). Prolyl endopeptidase-like is a (thio)esterase involved in mitochondrial respiratory chain function. iScience, 24(12), 103460. https://doi.org/10.1016/j.isci.2021.103460

Rong, J., Mori, W., Xia, X., Schafroth, M. A., Zhao, C., Van, R. S., Yamasaki, T., Chen, J., Xiao, Z., Haider, A., Ogasawara, D., Hiraishi, A., Shao, T., Zhang, Y., Chen, Z., Pang, F., Hu, K., Xie, L., Fujinaga, M., . . . Liang, S. H. (2021). Novel Reversible-Binding PET Ligands for Imaging Monoacylglycerol Lipase Based on the Piperazinyl Azetidine Scaffold. J Med Chem, 64(19), 14283-14298. https://doi.org/10.1021/acs.jmedchem.1c00747

Remsberg, J. R., Suciu, R. M., Zambetti, N. A., Hanigan, T. W., Firestone, A. J., Inguva, A., Long, A., Ngo, N., Lum, K. M., Henry, C. L., Richardson, S. K., Predovic, M., Huang, B., Dix, M. M., Howell, A. R., Niphakis, M. J., Shannon, K., & Cravatt, B. F. (2021). ABHD17 regulation of plasma membrane palmitoylation and N-Ras-dependent cancer growth. Nature Chemical Biology, 17(8), 856-864. https://doi.org/10.1038/s41589-021-00785-8

Rayo, J., Gregor, R., Jacob, N. T., Dandela, R., Dubinsky, L., Yashkin, A., Aranovich, A., Thangaraj, M., Ernst, O., Barash, E., Malitsky, S., Florea, B. I., Krom, B. P., Wiemer, E. A. C., Kickhoefer, V. A., Rome, L. H., Mathison, J. C., Kaufmann, G. F., Overkleeft, H. S., . . . Meijler, M. M. (2021). Immunoediting role for major vault protein in apoptotic signaling induced by bacterial N-acyl homoserine lactones. Proc Natl Acad Sci U S A, 118(12). https://doi.org/10.1073/pnas.2012529118

Pavon, F. J., Polis, I. Y., Stouffer, D. G., Cravatt, B. F., Roberto, M., Martin-Fardon, R., Rodriguez de Fonseca, F., Parsons, L. H., & Serrano, A. (2021). Selective inhibition of monoacylglycerol lipase is associated with passive coping behavior and attenuation of stress-induced dopamine release in the medial prefrontal cortex. Neurobiol Stress, 14, 100293. https://doi.org/10.1016/j.ynstr.2021.100293

O'Brien, L. D., Smith, T. L., Donvito, G., Cravatt, B. F., Newton, J., Spiegel, S., Reeves, T. M., Phillips, L. L., & Lichtman, A. H. (2021). Diacylglycerol Lipase-beta Knockout Mice Display a Sex-Dependent Attenuation of Traumatic Brain Injury-Induced Mortality with No Impact on Memory or Other Functional Consequences. Cannabis Cannabinoid Res, 6(6), 508-521. https://doi.org/10.1089/can.2020.0175

Morena, M., Nastase, A. S., Santori, A., Cravatt, B. F., Shansky, R. M., & Hill, M. N. (2021). Sex-dependent effects of endocannabinoid modulation of conditioned fear extinction in rats. Br J Pharmacol, 178(4), 983-996. https://doi.org/10.1111/bph.15341

Litwin, K., Crowley, V. M., Suciu, R. M., Boger, D. L., & Cravatt, B. F. (2021). Chemical proteomic identification of functional cysteines with atypical electrophile reactivities. Tetrahedron Lett, 67. https://doi.org/10.1016/j.tetlet.2021.152861

League, A. F., Gorman, B. L., Hermes, D. J., Johnson, C. T., Jacobs, I. R., Yadav-Samudrala, B. J., Poklis, J. L., Niphakis, M. J., Cravatt, B. F., Lichtman, A. H., Ignatowska-Jankowska, B. M., & Fitting, S. (2021). Monoacylglycerol Lipase Inhibitor MJN110 Reduces Neuronal Hyperexcitability, Restores Dendritic Arborization Complexity, and Regulates Reward-Related Behavior in Presence of HIV-1 Tat. Front Neurol, 12, 651272. https://doi.org/10.3389/fneur.2021.651272

Kuljanin, M., Mitchell, D. C., Schweppe, D. K., Gikandi, A. S., Nusinow, D. P., Bulloch, N. J., Vinogradova, E. V., Wilson, D. L., Kool, E. T., Mancias, J. D., Cravatt, B. F., & Gygi, S. P. (2021). Reimagining high-throughput profiling of reactive cysteines for cell-based screening of large electrophile libraries. Nat Biotechnol, 39(5), 630-641. https://doi.org/10.1038/s41587-020-00778-3

Jing, H., Reed, A., Ulanovskaya, O. A., Grigoleit, J. S., Herbst, D. M., Henry, C. L., Li, H., Barbas, S., Germain, J., Masuda, K., & Cravatt, B. F. (2021). Phospholipase Cgamma2 regulates endocannabinoid and eicosanoid networks in innate immune cells. Proc Natl Acad Sci U S A, 118(41). https://doi.org/10.1073/pnas.2112971118

Hou, L., Rong, J., Haider, A., Ogasawara, D., Varlow, C., Schafroth, M. A., Mu, L., Gan, J., Xu, H., Fowler, C. J., Zhang, M. R., Vasdev, N., Ametamey, S., Cravatt, B. F., Wang, L., & Liang, S. H. (2021). Positron Emission Tomography Imaging of the Endocannabinoid System: Opportunities and Challenges in Radiotracer Development. J Med Chem, 64(1), 123-149. https://doi.org/10.1021/acs.jmedchem.0c01459

Hermes, D. J., Yadav-Samudrala, B. J., Xu, C., Paniccia, J. E., Meeker, R. B., Armstrong, M. L., Reisdorph, N., Cravatt, B. F., Mackie, K., Lichtman, A. H., Ignatowska-Jankowska, B. M., Lysle, D. T., & Fitting, S. (2021). GPR18 drives FAAH inhibition-induced neuroprotection against HIV-1 Tat-induced neurodegeneration. Exp Neurol, 341, 113699. https://doi.org/10.1016/j.expneurol.2021.113699

Grevengoed, T. J., Trammell, S. A., Svenningsen, J. S., Makarov, M. V., Nielsen, T. S., Jacobsen, J. C. B., Treebak, J. T., Calder, P. C., Migaud, M. E., Cravatt, B. F., & Gillum, M. P. (2021). An abundant biliary metabolite derived from dietary omega-3 polyunsaturated fatty acids regulates triglycerides. J Clin Invest, 131(6). https://doi.org/10.1172/JCI143861

Garnar-Wortzel, L., Bishop, T. R., Kitamura, S., Milosevich, N., Asiaban, J. N., Zhang, X., Zheng, Q., Chen, E., Ramos, A. R., Ackerman, C. J., Hampton, E. N., Chatterjee, A. K., Young, T. S., Hull, M. V., Sharpless, K. B., Cravatt, B. F., Wolan, D. W., & Erb, M. A. (2021). Chemical Inhibition of ENL/AF9 YEATS Domains in Acute Leukemia. ACS Cent Sci, 7(5), 815-830. https://doi.org/10.1021/acscentsci.0c01550

Gao, J., Liu, Y., Yang, F., Chen, X., Cravatt, B. F., & Wang, C. (2021). CIMAGE2.0: An Expanded Tool for Quantitative Analysis of Activity-Based Protein Profiling (ABPP) Data. J Proteome Res, 20(10), 4893-4900. https://doi.org/10.1021/acs.jproteome.1c00455

Filip, R., Desrochers, G. F., Lefebvre, D. M., Reed, A., Singaravelu, R., Cravatt, B. F., & Pezacki, J. P. (2021). Profiling of MicroRNA Targets Using Activity-Based Protein Profiling: Linking Enzyme Activity to MicroRNA-185 Function. Cell Chem Biol, 28(2), 202-212 e206. https://doi.org/10.1016/j.chembiol.2020.12.009

Crowley, V. M., Thielert, M., & Cravatt, B. F. (2021). Functionalized Scout Fragments for Site-Specific Covalent Ligand Discovery and Optimization. ACS Cent Sci, 7(4), 613-623. https://doi.org/10.1021/acscentsci.0c01336

Chen, Z., Mori, W., Rong, J., Schafroth, M. A., Shao, T., Van, R. S., Ogasawara, D., Yamasaki, T., Hiraishi, A., Hatori, A., Chen, J., Zhang, Y., Hu, K., Fujinaga, M., Sun, J., Yu, Q., Collier, T. L., Shao, Y., Cravatt, B. F., . . . Liang, S. H. (2021). Development of a highly-specific (18)F-labeled irreversible positron emission tomography tracer for monoacylglycerol lipase mapping. Acta Pharmaceutica Sinica B, 11(6), 1686-1695. https://doi.org/10.1016/j.apsb.2021.01.021

Bouffard, E., Zaro, B. W., Dix, M. M., Cravatt, B., & Wong, C. H. (2021). Refinement of Covalent EGFR Inhibitor AZD9291 to Eliminate Off-target Activity. Tetrahedron Lett, 74. https://doi.org/10.1016/j.tetlet.2021.153178

Bi, J., Khan, A., Tang, J., Armando, A. M., Wu, S., Zhang, W., Gimple, R. C., Reed, A., Jing, H., Koga, T., Wong, I. T., Gu, Y., Miki, S., Yang, H., Prager, B., Curtis, E. J., Wainwright, D. A., Furnari, F. B., Rich, J. N., . . . Mischel, P. S. (2021). Targeting glioblastoma signaling and metabolism with a re-purposed brain-penetrant drug. Cell Rep, 37(5), 109957. https://doi.org/10.1016/j.celrep.2021.109957

Abbasov, M. E., Kavanagh, M. E., Ichu, T. A., Lazear, M. R., Tao, Y., Crowley, V. M., Am Ende, C. W., Hacker, S. M., Ho, J., Dix, M. M., Suciu, R., Hayward, M. M., Kiessling, L. L., & Cravatt, B. F. (2021). A proteome-wide atlas of lysine-reactive chemistry. Nat Chem, 13(11), 1081-1092. https://doi.org/10.1038/s41557-021-00765-4

Abbasov, M. E., Kavanagh, M. E., Ichu, T. A., Lazear, M. R., Tao, Y., Crowley, V. M., Am Ende, C. W., Hacker, S. M., Ho, J., Dix, M. M., Suciu, R., Hayward, M. M., Kiessling, L. L., & Cravatt, B. F. (2021). Publisher Correction: A proteome-wide atlas of lysine-reactive chemistry. Nat Chem, 13(11), 1151. https://doi.org/10.1038/s41557-021-00823-x

2020:

Yamashita, Y., Vinogradova, E. V., Zhang, X., Suciu, R. M., & Cravatt, B. F. (2020). A Chemical Proteomic Probe for the Mitochondrial Pyruvate Carrier Complex. Angew Chem Int Ed Engl, 59(10), 3896-3899. https://doi.org/10.1002/anie.201914391

Xu, J. H., Eberhardt, J., Hill-Payne, B., Gonzalez-Paez, G. E., Castellon, J. O., Cravatt, B. F., Forli, S., Wolan, D. W., & Backus, K. M. (2020). Integrative X-ray Structure and Molecular Modeling for the Rationalization of Procaspase-8 Inhibitor Potency and Selectivity. ACS Chem Biol, 15(2), 575-586. https://doi.org/10.1021/acschembio.0c00019

Vinogradova, E. V., Zhang, X., Remillard, D., Lazar, D. C., Suciu, R. M., Wang, Y., Bianco, G., Yamashita, Y., Crowley, V. M., Schafroth, M. A., Yokoyama, M., Konrad, D. B., Lum, K. M., Simon, G. M., Kemper, E. K., Lazear, M. R., Yin, S., Blewett, M. M., Dix, M. M., . . . Cravatt, B. F. (2020). An Activity-Guided Map of Electrophile-Cysteine Interactions in Primary Human T Cells. Cell, 182(4), 1009-1026 e1029. https://doi.org/10.1016/j.cell.2020.07.001

Vaisar, T., Hu, J. H., Airhart, N., Fox, K., Heinecke, J., Nicosia, R. F., Kohler, T., Potter, Z. E., Simon, G. M., Dix, M. M., Cravatt, B. F., Gharib, S. A., & Dichek, D. A. (2020). Parallel Murine and Human Plaque Proteomics Reveals Pathways of Plaque Rupture. Circ Res, 127(8), 997-1022. https://doi.org/10.1161/CIRCRESAHA.120.317295

Thompson, A. L., Grenald, S. A., Ciccone, H. A., BassiriRad, N., Niphakis, M. J., Cravatt, B. F., Largent-Milnes, T. M., & Vanderah, T. W. (2020). The Endocannabinoid System Alleviates Pain in a Murine Model of Cancer-Induced Bone Pain. J Pharmacol Exp Ther, 373(2), 230-238. https://doi.org/10.1124/jpet.119.262337

Tang, M., Xie, Q., Gimple, R. C., Zhong, Z., Tam, T., Tian, J., Kidwell, R. L., Wu, Q., Prager, B. C., Qiu, Z., Yu, A., Zhu, Z., Mesci, P., Jing, H., Schimelman, J., Wang, P., Lee, D., Lorenzini, M. H., Dixit, D., . . . Rich, J. N. (2020). Three-dimensional bioprinted glioblastoma microenvironments model cellular dependencies and immune interactions. Cell Res, 30(10), 833-853. https://doi.org/10.1038/s41422-020-0338-1

Muldoon, P. P., Akinola, L. S., Schlosburg, J. E., Lichtman, A. H., Sim-Selley, L. J., Mahadevan, A., Cravatt, B. F., & Damaj, M. I. (2020). Inhibition of monoacylglycerol lipase reduces nicotine reward in the conditioned place preference test in male mice. Neuropharmacology, 176, 108170. https://doi.org/10.1016/j.neuropharm.2020.108170

Mock, E. D., Mustafa, M., Gunduz-Cinar, O., Cinar, R., Petrie, G. N., Kantae, V., Di, X., Ogasawara, D., Varga, Z. V., Paloczi, J., Miliano, C., Donvito, G., van Esbroeck, A. C. M., van der Gracht, A. M. F., Kotsogianni, I., Park, J. K., Martella, A., van der Wel, T., Soethoudt, M., . . . van der Stelt, M. (2020). Discovery of a NAPE-PLD inhibitor that modulates emotional behavior in mice. Nature Chemical Biology, 16(6), 667-675. https://doi.org/10.1038/s41589-020-0528-7

Mizrak, D., Bayin, N. S., Yuan, J., Liu, Z., Suciu, R. M., Niphakis, M. J., Ngo, N., Lum, K. M., Cravatt, B. F., Joyner, A. L., & Sims, P. A. (2020). Single-Cell Profiling and SCOPE-Seq Reveal Lineage Dynamics of Adult Ventricular-Subventricular Zone Neurogenesis and NOTUM as a Key Regulator. Cell Rep, 31(12), 107805. https://doi.org/10.1016/j.celrep.2020.107805

Laszlo, Z. I., Lele, Z., Zoldi, M., Miczan, V., Mogor, F., Simon, G. M., Mackie, K., Kacskovics, I., Cravatt, B. F., & Katona, I. (2020). ABHD4-dependent developmental anoikis safeguards the embryonic brain. Nat Commun, 11(1), 4363. https://doi.org/10.1038/s41467-020-18175-4

Kok, B. P., Ghimire, S., Kim, W., Chatterjee, S., Johns, T., Kitamura, S., Eberhardt, J., Ogasawara, D., Xu, J., Sukiasyan, A., Kim, S. M., Godio, C., Bittencourt, J. M., Cameron, M., Galmozzi, A., Forli, S., Wolan, D. W., Cravatt, B. F., Boger, D. L., & Saez, E. (2020). Discovery of small-molecule enzyme activators by activity-based protein profiling. Nature Chemical Biology, 16(9), 997-1005. https://doi.org/10.1038/s41589-020-0555-4

Kathman, S. G., & Cravatt, B. F. (2020). A masked zinger to block GPX4. Nature Chemical Biology, 16(5), 482-483. https://doi.org/10.1038/s41589-020-0511-3

Kathman, S. G., Boshart, J., Jing, H., & Cravatt, B. F. (2020). Blockade of the Lysophosphatidylserine Lipase ABHD12 Potentiates Ferroptosis in Cancer Cells. ACS Chem Biol, 15(4), 871-877. https://doi.org/10.1021/acschembio.0c00086

Ichu, T. A., Reed, A., Ogasawara, D., Ulanovskaya, O., Roberts, A., Aguirre, C. A., Bar-Peled, L., Gao, J., Germain, J., Barbas, S., Masuda, K., Conti, B., Tontonoz, P., & Cravatt, B. F. (2020). ABHD12 and LPCAT3 Interplay Regulates a Lyso-phosphatidylserine-C20:4 Phosphatidylserine Lipid Network Implicated in Neurological Disease. Biochemistry, 59(19), 1793-1799. https://doi.org/10.1021/acs.biochem.0c00292

Feja, M., Leigh, M. P. K., Baindur, A. N., McGraw, J. J., Wakabayashi, K. T., Cravatt, B. F., & Bass, C. E. (2020). The novel MAGL inhibitor MJN110 enhances responding to reward-predictive incentive cues by activation of CB1 receptors. Neuropharmacology, 162, 107814. https://doi.org/10.1016/j.neuropharm.2019.107814

Erikci Ertunc, M., Kok, B. P., Parsons, W. H., Wang, J. G., Tan, D., Donaldson, C. J., Pinto, A. F. M., Vaughan, J. M., Ngo, N., Lum, K. M., Henry, C. L., Coppola, A. R., Niphakis, M. J., Cravatt, B. F., Saez, E., & Saghatelian, A. (2020). AIG1 and ADTRP are endogenous hydrolases of fatty acid esters of hydroxy fatty acids (FAHFAs) in mice. J Biol Chem, 295(18), 5891-5905. https://doi.org/10.1074/jbc.RA119.012145

Dickson, P., Abegg, D., Vinogradova, E., Takaya, J., An, H., Simanski, S., Cravatt, B. F., Adibekian, A., & Kodadek, T. (2020). Physical and Functional Analysis of the Putative Rpn13 Inhibitor RA190. Cell Chem Biol, 27(11), 1371-1382 e1376. https://doi.org/10.1016/j.chembiol.2020.08.007

Carvalho, L. A. R., Almeida, V. T., Brito, J. A., Lum, K. M., Oliveira, T. F., Guedes, R. C., Goncalves, L. M., Lucas, S. D., Cravatt, B. F., Archer, M., & Moreira, R. (2020). 3-Oxo-beta-sultam as a Sulfonylating Chemotype for Inhibition of Serine Hydrolases and Activity-Based Protein Profiling. ACS Chem Biol, 15(4), 878-883. https://doi.org/10.1021/acschembio.0c00090

Asiaban, J. N., Milosevich, N., Chen, E., Bishop, T. R., Wang, J., Zhang, Y., Ackerman, C. J., Hampton, E. N., Young, T. S., Hull, M. V., Cravatt, B. F., & Erb, M. A. (2020). Cell-Based Ligand Discovery for the ENL YEATS Domain. ACS Chem Biol, 15(4), 895-903. https://doi.org/10.1021/acschembio.0c00124

2019:

Zhang, X., Crowley, V. M., Wucherpfennig, T. G., Dix, M. M., & Cravatt, B. F. (2019). Electrophilic PROTACs that degrade nuclear proteins by engaging DCAF16. Nature Chemical Biology, 15(7), 737-746. https://doi.org/10.1038/s41589-019-0279-5

Zaro, B. W., Vinogradova, E. V., Lazar, D. C., Blewett, M. M., Suciu, R. M., Takaya, J., Studer, S., de la Torre, J. C., Casanova, J. L., Cravatt, B. F., & Teijaro, J. R. (2019). Dimethyl Fumarate Disrupts Human Innate Immune Signaling by Targeting the IRAK4-MyD88 Complex. J Immunol, 202(9), 2737-2746. https://doi.org/10.4049/jimmunol.1801627

Wang, Y., Dix, M. M., Bianco, G., Remsberg, J. R., Lee, H. Y., Kalocsay, M., Gygi, S. P., Forli, S., Vite, G., Lawrence, R. M., Parker, C. G., & Cravatt, B. F. (2019). Expedited mapping of the ligandable proteome using fully functionalized enantiomeric probe pairs. Nat Chem, 11(12), 1113-1123. https://doi.org/10.1038/s41557-019-0351-5

Walsh, S. I., Peters, D. S., Smith, P. A., Craney, A., Dix, M. M., Cravatt, B. F., & Romesberg, F. E. (2019). Inhibition of Protein Secretion in Escherichia coli and Sub-MIC Effects of Arylomycin Antibiotics. Antimicrob Agents Chemother, 63(2). https://doi.org/10.1128/AAC.01253-18

Sticht, M. A., Lau, D. J., Keenan, C. M., Cavin, J. B., Morena, M., Vemuri, V. K., Makriyannis, A., Cravatt, B. F., Sharkey, K. A., & Hill, M. N. (2019). Endocannabinoid regulation of homeostatic feeding and stress-induced alterations in food intake in male rats. Br J Pharmacol, 176(10), 1524-1540. https://doi.org/10.1111/bph.14453

Senkane, K., Vinogradova, E. V., Suciu, R. M., Crowley, V. M., Zaro, B. W., Bradshaw, J. M., Brameld, K. A., & Cravatt, B. F. (2019). The Proteome-Wide Potential for Reversible Covalency at Cysteine. Angew Chem Int Ed Engl, 58(33), 11385-11389. https://doi.org/10.1002/anie.201905829

Schurman, L. D., Carper, M. C., Moncayo, L. V., Ogasawara, D., Richardson, K., Yu, L., Liu, X., Poklis, J. L., Liu, Q. S., Cravatt, B. F., & Lichtman, A. H. (2019). Diacylglycerol Lipase-Alpha Regulates Hippocampal-Dependent Learning and Memory Processes in Mice. J Neurosci, 39(30), 5949-5965. https://doi.org/10.1523/JNEUROSCI.1353-18.2019

Pentinmikko, N., Iqbal, S., Mana, M., Andersson, S., Cognetta, A. B., 3rd, Suciu, R. M., Roper, J., Luopajarvi, K., Markelin, E., Gopalakrishnan, S., Smolander, O. P., Naranjo, S., Saarinen, T., Juuti, A., Pietilainen, K., Auvinen, P., Ristimaki, A., Gupta, N., Tammela, T., . . . Katajisto, P. (2019). Notum produced by Paneth cells attenuates regeneration of aged intestinal epithelium. Nature, 571(7765), 398-402. https://doi.org/10.1038/s41586-019-1383-0

Pavon, F. J., Serrano, A., Stouffer, D. G., Polis, I., Roberto, M., Cravatt, B. F., Martin-Fardon, R., Rodriguez de Fonseca, F., & Parsons, L. H. (2019). Ethanol-induced alterations in endocannabinoids and relevant neurotransmitters in the nucleus accumbens of fatty acid amide hydrolase knockout mice. Addict Biol, 24(6), 1204-1215. https://doi.org/10.1111/adb.12695

Otrubova, K., Chatterjee, S., Ghimire, S., Cravatt, B. F., & Boger, D. L. (2019). N-Acyl pyrazoles: Effective and tunable inhibitors of serine hydrolases. Bioorg Med Chem, 27(8), 1693-1703. https://doi.org/10.1016/j.bmc.2019.03.020

Ogasawara, D., Ichu, T. A., Jing, H., Hulce, J. J., Reed, A., Ulanovskaya, O. A., & Cravatt, B. F. (2019). Discovery and Optimization of Selective and in Vivo Active Inhibitors of the Lysophosphatidylserine Lipase alpha/beta-Hydrolase Domain-Containing 12 (ABHD12). J Med Chem, 62(3), 1643-1656. https://doi.org/10.1021/acs.jmedchem.8b01958

Jacobs, I. R., Xu, C., Hermes, D. J., League, A. F., Xu, C., Nath, B., Jiang, W., Niphakis, M. J., Cravatt, B. F., Mackie, K., Mukhopadhyay, S., Lichtman, A. H., Ignatowska-Jankowska, B. M., & Fitting, S. (2019). Inhibitory Control Deficits Associated with Upregulation of CB(1)R in the HIV-1 Tat Transgenic Mouse Model of Hand. J Neuroimmune Pharmacol, 14(4), 661-678. https://doi.org/10.1007/s11481-019-09867-w

Huang, Z., Ogasawara, D., Seneviratne, U. I., Cognetta, A. B., 3rd, Am Ende, C. W., Nason, D. M., Lapham, K., Litchfield, J., Johnson, D. S., & Cravatt, B. F. (2019). Global Portrait of Protein Targets of Metabolites of the Neurotoxic Compound BIA 10-2474. ACS Chem Biol, 14(2), 192-197. https://doi.org/10.1021/acschembio.8b01097

Habib, A., Chokr, D., Wan, J., Hegde, P., Mabire, M., Siebert, M., Ribeiro-Parenti, L., Le Gall, M., Letteron, P., Pilard, N., Mansouri, A., Brouillet, A., Tardelli, M., Weiss, E., Le Faouder, P., Guillou, H., Cravatt, B. F., Moreau, R., Trauner, M., & Lotersztajn, S. (2019). Inhibition of monoacylglycerol lipase, an anti-inflammatory and antifibrogenic strategy in the liver. Gut, 68(3), 522-532. https://doi.org/10.1136/gutjnl-2018-316137

Guillamat Prats, R., Rami, M., Ring, L., Rinne, P., Lauer, E., Lenglet, S., Thomas, A., Pagano, S., Vuilleumier, N., Cravatt, B. F., Weber, C., Faussner, A., & Steffens, S. (2019). Deficiency of Monoacylglycerol Lipase Enhances IgM Plasma Levels and Limits Atherogenesis in a CB2-Dependent Manner. Thromb Haemost, 119(2), 348-351. https://doi.org/10.1055/s-0038-1676769

Grevengoed, T. J., Trammell, S. A. J., McKinney, M. K., Petersen, N., Cardone, R. L., Svenningsen, J. S., Ogasawara, D., Nexoe-Larsen, C. C., Knop, F. K., Schwartz, T. W., Kibbey, R. G., Cravatt, B. F., & Gillum, M. P. (2019). N-acyl taurines are endogenous lipid messengers that improve glucose homeostasis. Proc Natl Acad Sci U S A, 116(49), 24770-24778. https://doi.org/10.1073/pnas.1916288116

Galmozzi, A., Kok, B. P., Kim, A. S., Montenegro-Burke, J. R., Lee, J. Y., Spreafico, R., Mosure, S., Albert, V., Cintron-Colon, R., Godio, C., Webb, W. R., Conti, B., Solt, L. A., Kojetin, D., Parker, C. G., Peluso, J. J., Pru, J. K., Siuzdak, G., Cravatt, B. F., & Saez, E. (2019). PGRMC2 is an intracellular haem chaperone critical for adipocyte function. Nature, 576(7785), 138-142. https://doi.org/10.1038/s41586-019-1774-2

Chen, Z., Mori, W., Fu, H., Schafroth, M. A., Hatori, A., Shao, T., Zhang, G., Van, R. S., Zhang, Y., Hu, K., Fujinaga, M., Wang, L., Belov, V., Ogasawara, D., Giffenig, P., Deng, X., Rong, J., Yu, Q., Zhang, X., . . . Liang, S. H. (2019). Design, Synthesis, and Evaluation of (18)F-Labeled Monoacylglycerol Lipase Inhibitors as Novel Positron Emission Tomography Probes. J Med Chem, 62(19), 8866-8872. https://doi.org/10.1021/acs.jmedchem.9b00936

Chen, Z., Mori, W., Deng, X., Cheng, R., Ogasawara, D., Zhang, G., Schafroth, M. A., Dahl, K., Fu, H., Hatori, A., Shao, T., Zhang, Y., Yamasaki, T., Zhang, X., Rong, J., Yu, Q., Hu, K., Fujinaga, M., Xie, L., . . . Liang, S. H. (2019). Design, Synthesis, and Evaluation of Reversible and Irreversible Monoacylglycerol Lipase Positron Emission Tomography (PET) Tracers Using a "Tail Switching" Strategy on a Piperazinyl Azetidine Skeleton. J Med Chem, 62(7), 3336-3353. https://doi.org/10.1021/acs.jmedchem.8b01778

Chen, A. L., Lum, K. M., Lara-Gonzalez, P., Ogasawara, D., Cognetta, A. B., 3rd, To, A., Parsons, W. H., Simon, G. M., Desai, A., Petrascheck, M., Bar-Peled, L., & Cravatt, B. F. (2019). Pharmacological convergence reveals a lipid pathway that regulates C. elegans lifespan. Nature Chemical Biology, 15(5), 453-462. https://doi.org/10.1038/s41589-019-0243-4

Chefetz, I., Grimley, E., Yang, K., Hong, L., Vinogradova, E. V., Suciu, R., Kovalenko, I., Karnak, D., Morgan, C. A., Chtcherbinine, M., Buchman, C., Huddle, B., Barraza, S., Morgan, M., Bernstein, K. A., Yoon, E., Lombard, D. B., Bild, A., Mehta, G., . . . Buckanovich, R. J. (2019). A Pan-ALDH1A Inhibitor Induces Necroptosis in Ovarian Cancer Stem-like Cells. Cell Rep, 26(11), 3061-3075 e3066. https://doi.org/10.1016/j.celrep.2019.02.032

Bi, J., Ichu, T. A., Zanca, C., Yang, H., Zhang, W., Gu, Y., Chowdhry, S., Reed, A., Ikegami, S., Turner, K. M., Zhang, W., Villa, G. R., Wu, S., Quehenberger, O., Yong, W. H., Kornblum, H. I., Rich, J. N., Cloughesy, T. F., Cavenee, W. K., . . . Mischel, P. S. (2019). Oncogene Amplification in Growth Factor Signaling Pathways Renders Cancers Dependent on Membrane Lipid Remodeling. Cell Metab, 30(3), 525-538 e528. https://doi.org/10.1016/j.cmet.2019.06.014

Baillargeon, P., Fernandez-Vega, V., Sridharan, B. P., Brown, S., Griffin, P. R., Rosen, H., Cravatt, B., Scampavia, L., & Spicer, T. P. (2019). The Scripps Molecular Screening Center and Translational Research Institute. SLAS Discov, 24(3), 386-397. https://doi.org/10.1177/2472555218820809

2018:

Wilkerson, J. L., Curry, Z. A., Kinlow, P. D., Mason, B. L., Hsu, K. L., van der Stelt, M., Cravatt, B. F., & Lichtman, A. H. (2018). Evaluation of different drug classes on transient sciatic nerve injury-depressed marble burying in mice. Pain, 159(6), 1155-1165. https://doi.org/10.1097/j.pain.0000000000001199

Suciu, R. M., Cognetta, A. B., 3rd, Potter, Z. E., & Cravatt, B. F. (2018). Selective Irreversible Inhibitors of the Wnt-Deacylating Enzyme NOTUM Developed by Activity-Based Protein Profiling. ACS Med Chem Lett, 9(6), 563-568. https://doi.org/10.1021/acsmedchemlett.8b00191

Solis, G. M., Kardakaris, R., Valentine, E. R., Bar-Peled, L., Chen, A. L., Blewett, M. M., McCormick, M. A., Williamson, J. R., Kennedy, B., Cravatt, B. F., & Petrascheck, M. (2018). Translation attenuation by minocycline enhances longevity and proteostasis in old post-stress-responsive organisms. Elife, 7. https://doi.org/10.7554/eLife.40314

Serrano, A., Pavon, F. J., Buczynski, M. W., Schlosburg, J., Natividad, L. A., Polis, I. Y., Stouffer, D. G., Zorrilla, E. P., Roberto, M., Cravatt, B. F., Martin-Fardon, R., Rodriguez de Fonseca, F., & Parsons, L. H. (2018). Deficient endocannabinoid signaling in the central amygdala contributes to alcohol dependence-related anxiety-like behavior and excessive alcohol intake. Neuropsychopharmacology, 43(9), 1840-1850. https://doi.org/10.1038/s41386-018-0055-3

Pavon, F. J., Serrano, A., Sidhpura, N., Polis, I., Stouffer, D., de Fonseca, F. R., Cravatt, B. F., Martin-Fardon, R., & Parsons, L. H. (2018). Fatty acid amide hydrolase (FAAH) inactivation confers enhanced sensitivity to nicotine-induced dopamine release in the mouse nucleus accumbens. Addict Biol, 23(2), 723-734. https://doi.org/10.1111/adb.12531

Parker, C. G., & Cravatt, B. F. (2018). Chemistry Takes Center Stage for Identifying Cancer Targetability. Cell, 173(4), 815-817. https://doi.org/10.1016/j.cell.2018.04.020

Ogasawara, D., Ichu, T. A., Vartabedian, V. F., Benthuysen, J., Jing, H., Reed, A., Ulanovskaya, O. A., Hulce, J. J., Roberts, A., Brown, S., Rosen, H., Teijaro, J. R., & Cravatt, B. F. (2018). Selective blockade of the lyso-PS lipase ABHD12 stimulates immune responses in vivo. Nature Chemical Biology, 14(12), 1099-1108. https://doi.org/10.1038/s41589-018-0155-8

Mortenson, D. E., Brighty, G. J., Plate, L., Bare, G., Chen, W., Li, S., Wang, H., Cravatt, B. F., Forli, S., Powers, E. T., Sharpless, K. B., Wilson, I. A., & Kelly, J. W. (2018). "Inverse Drug Discovery" Strategy To Identify Proteins That Are Targeted by Latent Electrophiles As Exemplified by Aryl Fluorosulfates. J Am Chem Soc, 140(1), 200-210. https://doi.org/10.1021/jacs.7b08366

McReynolds, J. R., Doncheck, E. M., Li, Y., Vranjkovic, O., Graf, E. N., Ogasawara, D., Cravatt, B. F., Baker, D. A., Liu, Q. S., Hillard, C. J., & Mantsch, J. R. (2018). Stress Promotes Drug Seeking Through Glucocorticoid-Dependent Endocannabinoid Mobilization in the Prelimbic Cortex. Biol Psychiatry, 84(2), 85-94. https://doi.org/10.1016/j.biopsych.2017.09.024

Manterola, A., Bernal-Chico, A., Cipriani, R., Ruiz, A., Perez-Samartin, A., Moreno-Rodriguez, M., Hsu, K. L., Cravatt, B. F., Brown, J. M., Rodriguez-Puertas, R., Matute, C., & Mato, S. (2018). Re-examining the potential of targeting ABHD6 in multiple sclerosis: Efficacy of systemic and peripherally restricted inhibitors in experimental autoimmune encephalomyelitis. Neuropharmacology, 141, 181-191. https://doi.org/10.1016/j.neuropharm.2018.08.038

Manterola, A., Bernal-Chico, A., Cipriani, R., Canedo-Antelo, M., Moreno-Garcia, A., Martin-Fontecha, M., Perez-Cerda, F., Sanchez-Gomez, M. V., Ortega-Gutierrez, S., Brown, J. M., Hsu, K. L., Cravatt, B., Matute, C., & Mato, S. (2018). Deregulation of the endocannabinoid system and therapeutic potential of ABHD6 blockade in the cuprizone model of demyelination. Biochem Pharmacol, 157, 189-201. https://doi.org/10.1016/j.bcp.2018.07.042

Lee, H. Y., Suciu, R. M., Horning, B. D., Vinogradova, E. V., Ulanovskaya, O. A., & Cravatt, B. F. (2018). Covalent inhibitors of nicotinamide N-methyltransferase (NNMT) provide evidence for target engagement challenges in situ. Bioorg Med Chem Lett, 28(16), 2682-2687. https://doi.org/10.1016/j.bmcl.2018.04.017

Inloes, J. M., Kiosses, W. B., Wang, H., Walther, T. C., Farese, R. V., Jr., & Cravatt, B. F. (2018). Functional Contribution of the Spastic Paraplegia-Related Triglyceride Hydrolase DDHD2 to the Formation and Content of Lipid Droplets. Biochemistry, 57(5), 827-838. https://doi.org/10.1021/acs.biochem.7b01028

Inloes, J. M., Jing, H., & Cravatt, B. F. (2018). The Spastic Paraplegia-Associated Phospholipase DDHD1 Is a Primary Brain Phosphatidylinositol Lipase. Biochemistry, 57(39), 5759-5767. https://doi.org/10.1021/acs.biochem.8b00810

Hermes, D. J., Xu, C., Poklis, J. L., Niphakis, M. J., Cravatt, B. F., Mackie, K., Lichtman, A. H., Ignatowska-Jankowska, B. M., & Fitting, S. (2018). Neuroprotective effects of fatty acid amide hydrolase catabolic enzyme inhibition in a HIV-1 Tat model of neuroAIDS. Neuropharmacology, 141, 55-65. https://doi.org/10.1016/j.neuropharm.2018.08.013

Gavin, A. L., Huang, D., Huber, C., Martensson, A., Tardif, V., Skog, P. D., Blane, T. R., Thinnes, T. C., Osborn, K., Chong, H. S., Kargaran, F., Kimm, P., Zeitjian, A., Sielski, R. L., Briggs, M., Schulz, S. R., Zarpellon, A., Cravatt, B., Pang, E. S., . . . Nemazee, D. (2018). PLD3 and PLD4 are single-stranded acid exonucleases that regulate endosomal nucleic-acid sensing. Nat Immunol, 19(9), 942-953. https://doi.org/10.1038/s41590-018-0179-y

Gao, D. W., Vinogradova, E. V., Nimmagadda, S. K., Medina, J. M., Xiao, Y., Suciu, R. M., Cravatt, B. F., & Engle, K. M. (2018). Direct Access to Versatile Electrophiles via Catalytic Oxidative Cyanation of Alkenes. J Am Chem Soc, 140(26), 8069-8073. https://doi.org/10.1021/jacs.8b03704

Galmozzi, A., Parker, C. G., Kok, B. P., Cravatt, B. F., & Saez, E. (2018). Discovery of Modulators of Adipocyte Physiology Using Fully Functionalized Fragments. Methods Mol Biol, 1787, 115-127. https://doi.org/10.1007/978-1-4939-7847-2_9

Dandela, R., Mantin, D., Cravatt, B. F., Rayo, J., & Meijler, M. M. (2018). Proteome-wide mapping of PQS-interacting proteins in Pseudomonas aeruginosa. Chem Sci, 9(8), 2290-2294. https://doi.org/10.1039/c7sc04287f

Curry, Z. A., Wilkerson, J. L., Bagdas, D., Kyte, S. L., Patel, N., Donvito, G., Mustafa, M. A., Poklis, J. L., Niphakis, M. J., Hsu, K. L., Cravatt, B. F., Gewirtz, D. A., Damaj, M. I., & Lichtman, A. H. (2018). Monoacylglycerol Lipase Inhibitors Reverse Paclitaxel-Induced Nociceptive Behavior and Proinflammatory Markers in a Mouse Model of Chemotherapy-Induced Neuropathy. J Pharmacol Exp Ther, 366(1), 169-183. https://doi.org/10.1124/jpet.117.245704

Cheng, R., Mori, W., Ma, L., Alhouayek, M., Hatori, A., Zhang, Y., Ogasawara, D., Yuan, G., Chen, Z., Zhang, X., Shi, H., Yamasaki, T., Xie, L., Kumata, K., Fujinaga, M., Nagai, Y., Minamimoto, T., Svensson, M., Wang, L., . . . Liang, S. H. (2018). In Vitro and in Vivo Evaluation of (11)C-Labeled Azetidinecarboxylates for Imaging Monoacylglycerol Lipase by PET Imaging Studies. J Med Chem, 61(6), 2278-2291. https://doi.org/10.1021/acs.jmedchem.7b01400

Aparicio, N., Grande, M. T., Ruiz de Martin Esteban, S., Lopez, A., Ruiz-Perez, G., Amores, M., Vazquez, C., Martinez-Relimpio, A. M., Pazos, M. R., Cravatt, B. F., Tolon, R. M., & Romero, J. (2018). Role of interleukin 1-beta in the inflammatory response in a fatty acid amide hydrolase-knockout mouse model of Alzheimer's disease. Biochem Pharmacol, 157, 202-209. https://doi.org/10.1016/j.bcp.2018.09.009

Aebersold, R., Agar, J. N., Amster, I. J., Baker, M. S., Bertozzi, C. R., Boja, E. S., Costello, C. E., Cravatt, B. F., Fenselau, C., Garcia, B. A., Ge, Y., Gunawardena, J., Hendrickson, R. C., Hergenrother, P. J., Huber, C. G., Ivanov, A. R., Jensen, O. N., Jewett, M. C., Kelleher, N. L., . . . Zhang, B. (2018). How many human proteoforms are there? Nature Chemical Biology, 14(3), 206-214. https://doi.org/10.1038/nchembio.25762017:

2017:

Yun, B., Lee, H., Powell, R., Reisdorph, N., Ewing, H., Gelb, M. H., Hsu, K. L., Cravatt, B. F., & Leslie, C. C. (2017). Regulation of calcium release from the endoplasmic reticulum by the serine hydrolase ABHD2. Biochem Biophys Res Commun, 490(4), 1226-1231. https://doi.org/10.1016/j.bbrc.2017.06.195

Wilkerson, J. L., Ghosh, S., Mustafa, M., Abdullah, R. A., Niphakis, M. J., Cabrera, R., Maldonado, R. L., Cravatt, B. F., & Lichtman, A. H. (2017). The endocannabinoid hydrolysis inhibitor SA-57: Intrinsic antinociceptive effects, augmented morphine-induced antinociception, and attenuated heroin seeking behavior in mice. Neuropharmacology, 114, 156-167. https://doi.org/10.1016/j.neuropharm.2016.11.015

Wilkerson, J. L., Donvito, G., Grim, T. W., Abdullah, R. A., Ogasawara, D., Cravatt, B. F., & Lichtman, A. H. (2017). Investigation of Diacylglycerol Lipase Alpha Inhibition in the Mouse Lipopolysaccharide Inflammatory Pain Model. J Pharmacol Exp Ther, 363(3), 394-401. https://doi.org/10.1124/jpet.117.243808

Whitby, L. R., Obach, R. S., Simon, G. M., Hayward, M. M., & Cravatt, B. F. (2017). Quantitative Chemical Proteomic Profiling of the in Vivo Targets of Reactive Drug Metabolites. ACS Chem Biol, 12(8), 2040-2050. https://doi.org/10.1021/acschembio.7b00346

van Esbroeck, A. C. M., Janssen, A. P. A., Cognetta, A. B., 3rd, Ogasawara, D., Shpak, G., van der Kroeg, M., Kantae, V., Baggelaar, M. P., de Vrij, F. M. S., Deng, H., Allara, M., Fezza, F., Lin, Z., van der Wel, T., Soethoudt, M., Mock, E. D., den Dulk, H., Baak, I. L., Florea, B. I., . . . van der Stelt, M. (2017). Activity-based protein profiling reveals off-target proteins of the FAAH inhibitor BIA 10-2474. Science, 356(6342), 1084-1087. https://doi.org/10.1126/science.aaf7497

Touchette, M. H., Van Vlack, E. R., Bai, L., Kim, J., Cognetta, A. B., 3rd, Previti, M. L., Backus, K. M., Martin, D. W., Cravatt, B. F., & Seeliger, J. C. (2017). A Screen for Protein-Protein Interactions in Live Mycobacteria Reveals a Functional Link between the Virulence-Associated Lipid Transporter LprG and the Mycolyltransferase Antigen 85A. ACS Infect Dis, 3(5), 336-348. https://doi.org/10.1021/acsinfecdis.6b00179

Tan, J., Cognetta Iii, A. B., Diaz, D. B., Lum, K. M., Adachi, S., Kundu, S., Cravatt, B. F., & Yudin, A. K. (2017). Multicomponent mapping of boron chemotypes furnishes selective enzyme inhibitors. Nat Commun, 8(1), 1760. https://doi.org/10.1038/s41467-017-01319-4

Sousa-Valente, J., Varga, A., Torres-Perez, J. V., Jenes, A., Wahba, J., Mackie, K., Cravatt, B., Ueda, N., Tsuboi, K., Santha, P., Jancso, G., Tailor, H., Avelino, A., & Nagy, I. (2017). Inflammation of peripheral tissues and injury to peripheral nerves induce differing effects in the expression of the calcium-sensitive N-arachydonoylethanolamine-synthesizing enzyme and related molecules in rat primary sensory neurons. J Comp Neurol, 525(8), 1778-1796. https://doi.org/10.1002/cne.24154

Shimanaka, Y., Kono, N., Taketomi, Y., Arita, M., Okayama, Y., Tanaka, Y., Nishito, Y., Mochizuki, T., Kusuhara, H., Adibekian, A., Cravatt, B. F., Murakami, M., & Arai, H. (2017). Omega-3 fatty acid epoxides are autocrine mediators that control the magnitude of IgE-mediated mast cell activation. Nat Med, 23(11), 1287-1297. https://doi.org/10.1038/nm.4417

Schonhoft, J. D., Monteiro, C., Plate, L., Eisele, Y. S., Kelly, J. M., Boland, D., Parker, C. G., Cravatt, B. F., Teruya, S., Helmke, S., Maurer, M., Berk, J., Sekijima, Y., Novais, M., Coelho, T., Powers, E. T., & Kelly, J. W. (2017). Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients. Sci Transl Med, 9(407). https://doi.org/10.1126/scitranslmed.aam7621

Parker, C. G., Kuttruff, C. A., Galmozzi, A., Jorgensen, L., Yeh, C. H., Hermanson, D. J., Wang, Y., Artola, M., McKerrall, S. J., Josyln, C. M., Norremark, B., Dunstl, G., Felding, J., Saez, E., Baran, P. S., & Cravatt, B. F. (2017). Chemical Proteomics Identifies SLC25A20 as a Functional Target of the Ingenol Class of Actinic Keratosis Drugs. ACS Cent Sci, 3(12), 1276-1285. https://doi.org/10.1021/acscentsci.7b00420

Parker, C. G., Galmozzi, A., Wang, Y., Correia, B. E., Sasaki, K., Joslyn, C. M., Kim, A. S., Cavallaro, C. L., Lawrence, R. M., Johnson, S. R., Narvaiza, I., Saez, E., & Cravatt, B. F. (2017). Ligand and Target Discovery by Fragment-Based Screening in Human Cells. Cell, 168(3), 527-541 e529. https://doi.org/10.1016/j.cell.2016.12.029

Owens, R. A., Mustafa, M. A., Ignatowska-Jankowska, B. M., Damaj, M. I., Beardsley, P. M., Wiley, J. L., Niphakis, M. J., Cravatt, B. F., & Lichtman, A. H. (2017). Inhibition of the endocannabinoid-regulating enzyme monoacylglycerol lipase elicits a CB(1) receptor-mediated discriminative stimulus in mice. Neuropharmacology, 125, 80-86. https://doi.org/10.1016/j.neuropharm.2017.06.032

Niessen, S., Dix, M. M., Barbas, S., Potter, Z. E., Lu, S., Brodsky, O., Planken, S., Behenna, D., Almaden, C., Gajiwala, K. S., Ryan, K., Ferre, R., Lazear, M. R., Hayward, M. M., Kath, J. C., & Cravatt, B. F. (2017). Proteome-wide Map of Targets of T790M-EGFR-Directed Covalent Inhibitors. Cell Chem Biol, 24(11), 1388-1400 e1387. https://doi.org/10.1016/j.chembiol.2017.08.017

Matthews, M. L., He, L., Horning, B. D., Olson, E. J., Correia, B. E., Yates, J. R., 3rd, Dawson, P. E., & Cravatt, B. F. (2017). Chemoproteomic profiling and discovery of protein electrophiles in human cells. Nat Chem, 9(3), 234-243. https://doi.org/10.1038/nchem.2645

Lum, K. M., Sato, Y., Beyer, B. A., Plaisted, W. C., Anglin, J. L., Lairson, L. L., & Cravatt, B. F. (2017). Mapping Protein Targets of Bioactive Small Molecules Using Lipid-Based Chemical Proteomics. ACS Chem Biol, 12(10), 2671-2681. https://doi.org/10.1021/acschembio.7b00581

Kory, N., Grond, S., Kamat, S. S., Li, Z., Krahmer, N., Chitraju, C., Zhou, P., Frohlich, F., Semova, I., Ejsing, C., Zechner, R., Cravatt, B. F., Farese, R. V., Jr., & Walther, T. C. (2017). Mice lacking lipid droplet-associated hydrolase, a gene linked to human prostate cancer, have normal cholesterol ester metabolism. J Lipid Res, 58(1), 226-235. https://doi.org/10.1194/jlr.M072538

Kornahrens, A. F., Cognetta, A. B., 3rd, Brody, D. M., Matthews, M. L., Cravatt, B. F., & Boger, D. L. (2017). Design of Benzoxathiazin-3-one 1,1-Dioxides as a New Class of Irreversible Serine Hydrolase Inhibitors: Discovery of a Uniquely Selective PNPLA4 Inhibitor. J Am Chem Soc, 139(20), 7052-7061. https://doi.org/10.1021/jacs.7b02985

Hacker, S. M., Backus, K. M., Lazear, M. R., Forli, S., Correia, B. E., & Cravatt, B. F. (2017). Global profiling of lysine reactivity and ligandability in the human proteome. Nat Chem, 9(12), 1181-1190. https://doi.org/10.1038/nchem.2826

Guo, C. J., Chang, F. Y., Wyche, T. P., Backus, K. M., Acker, T. M., Funabashi, M., Taketani, M., Donia, M. S., Nayfach, S., Pollard, K. S., Craik, C. S., Cravatt, B. F., Clardy, J., Voigt, C. A., & Fischbach, M. A. (2017). Discovery of Reactive Microbiota-Derived Metabolites that Inhibit Host Proteases. Cell, 168(3), 517-526 e518. https://doi.org/10.1016/j.cell.2016.12.021

Deng, H., Kooijman, S., van den Nieuwendijk, A. M., Ogasawara, D., van der Wel, T., van Dalen, F., Baggelaar, M. P., Janssen, F. J., van den Berg, R. J., den Dulk, H., Cravatt, B. F., Overkleeft, H. S., Rensen, P. C., & van der Stelt, M. (2017). Triazole Ureas Act as Diacylglycerol Lipase Inhibitors and Prevent Fasting-Induced Refeeding. J Med Chem, 60(1), 428-440. https://doi.org/10.1021/acs.jmedchem.6b01482

Chen, Y. C., Backus, K. M., Merkulova, M., Yang, C., Brown, D., Cravatt, B. F., & Zhang, C. (2017). Covalent Modulators of the Vacuolar ATPase. J Am Chem Soc, 139(2), 639-642. https://doi.org/10.1021/jacs.6b12511

Bar-Peled, L., Kemper, E. K., Suciu, R. M., Vinogradova, E. V., Backus, K. M., Horning, B. D., Paul, T. A., Ichu, T. A., Svensson, R. U., Olucha, J., Chang, M. W., Kok, B. P., Zhu, Z., Ihle, N. T., Dix, M. M., Jiang, P., Hayward, M. M., Saez, E., Shaw, R. J., & Cravatt, B. F. (2017). Chemical Proteomics Identifies Druggable Vulnerabilities in a Genetically Defined Cancer. Cell, 171(3), 696-709 e623. https://doi.org/10.1016/j.cell.2017.08.051

2016:

Zaro, B. W., Whitby, L. R., Lum, K. M., & Cravatt, B. F. (2016). Metabolically Labile Fumarate Esters Impart Kinetic Selectivity to Irreversible Inhibitors. J Am Chem Soc, 138(49), 15841-15844. https://doi.org/10.1021/jacs.6b10589

Wills, K. L., Petrie, G. N., Millett, G., Limebeer, C. L., Rock, E. M., Niphakis, M. J., Cravatt, B. F., & Parker, L. A. (2016). Double Dissociation of Monoacylglycerol Lipase Inhibition and CB1 Antagonism in the Central Amygdala, Basolateral Amygdala, and the Interoceptive Insular Cortex on the Affective Properties of Acute Naloxone-Precipitated Morphine Withdrawal in Rats. Neuropsychopharmacology, 41(7), 1865-1873. https://doi.org/10.1038/npp.2015.356

Wilkerson, J. L., Niphakis, M. J., Grim, T. W., Mustafa, M. A., Abdullah, R. A., Poklis, J. L., Dewey, W. L., Akbarali, H., Banks, M. L., Wise, L. E., Cravatt, B. F., & Lichtman, A. H. (2016). The Selective Monoacylglycerol Lipase Inhibitor MJN110 Produces Opioid-Sparing Effects in a Mouse Neuropathic Pain Model. J Pharmacol Exp Ther, 357(1), 145-156. https://doi.org/10.1124/jpet.115.229971

Wilkerson, J. L., Ghosh, S., Bagdas, D., Mason, B. L., Crowe, M. S., Hsu, K. L., Wise, L. E., Kinsey, S. G., Damaj, M. I., Cravatt, B. F., & Lichtman, A. H. (2016). Diacylglycerol lipase beta inhibition reverses nociceptive behaviour in mouse models of inflammatory and neuropathic pain. Br J Pharmacol, 173(10), 1678-1692. https://doi.org/10.1111/bph.13469

Wiley, J. L., Lefever, T. W., Pulley, N. S., Marusich, J. A., Cravatt, B. F., & Lichtman, A. H. (2016). Just add water: cannabinoid discrimination in a water T-maze with FAAH(-/-) and FAAH(+/+) mice. Behav Pharmacol, 27(5), 479-484. https://doi.org/10.1097/FBP.0000000000000228

Wang, B., Rong, X., Duerr, M. A., Hermanson, D. J., Hedde, P. N., Wong, J. S., Vallim, T. Q., Cravatt, B. F., Gratton, E., Ford, D. A., & Tontonoz, P. (2016). Intestinal Phospholipid Remodeling Is Required for Dietary-Lipid Uptake and Survival on a High-Fat Diet. Cell Metab, 23(3), 492-504. https://doi.org/10.1016/j.cmet.2016.01.001

Villa, G. R., Hulce, J. J., Zanca, C., Bi, J., Ikegami, S., Cahill, G. L., Gu, Y., Lum, K. M., Masui, K., Yang, H., Rong, X., Hong, C., Turner, K. M., Liu, F., Hon, G. C., Jenkins, D., Martini, M., Armando, A. M., Quehenberger, O., . . . Mischel, P. S. (2016). An LXR-Cholesterol Axis Creates a Metabolic Co-Dependency for Brain Cancers. Cancer Cell, 30(5), 683-693. https://doi.org/10.1016/j.ccell.2016.09.008

Viader, A., Ogasawara, D., Joslyn, C. M., Sanchez-Alavez, M., Mori, S., Nguyen, W., Conti, B., & Cravatt, B. F. (2016). A chemical proteomic atlas of brain serine hydrolases identifies cell type-specific pathways regulating neuroinflammation. Elife, 5, e12345. https://doi.org/10.7554/eLife.12345

Tada, N., Jansen, D. J., Mower, M. P., Blewett, M. M., Umotoy, J. C., Cravatt, B. F., Wolan, D. W., & Shenvi, R. A. (2016). Synthesis and Sulfur Electrophilicity of the Nuphar Thiaspirane Pharmacophore. ACS Cent Sci, 2(6), 401-408. https://doi.org/10.1021/acscentsci.6b00113

Sticht, M. A., Limebeer, C. L., Rafla, B. R., Abdullah, R. A., Poklis, J. L., Ho, W., Niphakis, M. J., Cravatt, B. F., Sharkey, K. A., Lichtman, A. H., & Parker, L. A. (2016). Endocannabinoid regulation of nausea is mediated by 2-arachidonoylglycerol (2-AG) in the rat visceral insular cortex. Neuropharmacology, 102, 92-102. https://doi.org/10.1016/j.neuropharm.2015.10.039

Saghatelian, A., & Cravatt, B. (2016). Glucagon and Thyroid Hormone: A Championship Team. Cell, 167(3), 604-605. https://doi.org/10.1016/j.cell.2016.10.008

Parsons, W. H., Kolar, M. J., Kamat, S. S., Cognetta, A. B., 3rd, Hulce, J. J., Saez, E., Kahn, B. B., Saghatelian, A., & Cravatt, B. F. (2016). AIG1 and ADTRP are atypical integral membrane hydrolases that degrade bioactive FAHFAs. Nature Chemical Biology, 12(5), 367-372. https://doi.org/10.1038/nchembio.2051

Panlilio, L. V., Thorndike, E. B., Nikas, S. P., Alapafuja, S. O., Bandiera, T., Cravatt, B. F., Makriyannis, A., Piomelli, D., Goldberg, S. R., & Justinova, Z. (2016). Effects of fatty acid amide hydrolase (FAAH) inhibitors on working memory in rats. Psychopharmacology (Berl), 233(10), 1879-1888. https://doi.org/10.1007/s00213-015-4140-6

Owens, R. A., Ignatowska-Jankowska, B., Mustafa, M., Beardsley, P. M., Wiley, J. L., Jali, A., Selley, D. E., Niphakis, M. J., Cravatt, B. F., & Lichtman, A. H. (2016). Discriminative Stimulus Properties of the Endocannabinoid Catabolic Enzyme Inhibitor SA-57 in Mice. J Pharmacol Exp Ther, 358(2), 306-314. https://doi.org/10.1124/jpet.115.229492

Ogura, Y., Parsons, W. H., Kamat, S. S., & Cravatt, B. F. (2016). A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines. Nature Chemical Biology, 12(9), 669-671. https://doi.org/10.1038/nchembio.2127

Ogasawara, D., Deng, H., Viader, A., Baggelaar, M. P., Breman, A., den Dulk, H., van den Nieuwendijk, A. M., Soethoudt, M., van der Wel, T., Zhou, J., Overkleeft, H. S., Sanchez-Alavez, M., Mori, S., Nguyen, W., Conti, B., Liu, X., Chen, Y., Liu, Q. S., Cravatt, B. F., & van der Stelt, M. (2016). Rapid and profound rewiring of brain lipid signaling networks by acute diacylglycerol lipase inhibition. Proc Natl Acad Sci U S A, 113(1), 26-33. https://doi.org/10.1073/pnas.1522364112

Liu, X., Chen, Y., Vickstrom, C. R., Li, Y., Viader, A., Cravatt, B. F., & Liu, Q. S. (2016). Coordinated regulation of endocannabinoid-mediated retrograde synaptic suppression in the cerebellum by neuronal and astrocytic monoacylglycerol lipase. Sci Rep, 6, 35829. https://doi.org/10.1038/srep35829

Limebeer, C. L., Rock, E. M., Puvanenthirarajah, N., Niphakis, M. J., Cravatt, B. F., & Parker, L. A. (2016). Elevation of 2-AG by monoacylglycerol lipase inhibition in the visceral insular cortex interferes with anticipatory nausea in a rat model. Behav Neurosci, 130(2), 261-266. https://doi.org/10.1037/bne0000132

Kolar, M. J., Kamat, S. S., Parsons, W. H., Homan, E. A., Maher, T., Peroni, O. D., Syed, I., Fjeld, K., Molven, A., Kahn, B. B., Cravatt, B. F., & Saghatelian, A. (2016). Branched Fatty Acid Esters of Hydroxy Fatty Acids Are Preferred Substrates of the MODY8 Protein Carboxyl Ester Lipase. Biochemistry, 55(33), 4636-4641. https://doi.org/10.1021/acs.biochem.6b00565

Horning, B. D., Suciu, R. M., Ghadiri, D. A., Ulanovskaya, O. A., Matthews, M. L., Lum, K. M., Backus, K. M., Brown, S. J., Rosen, H., & Cravatt, B. F. (2016). Chemical Proteomic Profiling of Human Methyltransferases. J Am Chem Soc, 138(40), 13335-13343. https://doi.org/10.1021/jacs.6b07830

Gruner, B. M., Schulze, C. J., Yang, D., Ogasawara, D., Dix, M. M., Rogers, Z. N., Chuang, C. H., McFarland, C. D., Chiou, S. H., Brown, J. M., Cravatt, B. F., Bogyo, M., & Winslow, M. M. (2016). An in vivo multiplexed small-molecule screening platform. Nat Methods, 13(10), 883-889. https://doi.org/10.1038/nmeth.3992

Dugan, A., Majmudar, C. Y., Pricer, R., Niessen, S., Lancia, J. K., Fung, H. Y., Cravatt, B. F., & Mapp, A. K. (2016). Discovery of Enzymatic Targets of Transcriptional Activators via in Vivo Covalent Chemical Capture. J Am Chem Soc, 138(38), 12629-12635. https://doi.org/10.1021/jacs.6b07680

Chen, Y., Liu, X., Vickstrom, C. R., Liu, M. J., Zhao, L., Viader, A., Cravatt, B. F., & Liu, Q. S. (2016). Neuronal and Astrocytic Monoacylglycerol Lipase Limit the Spread of Endocannabinoid Signaling in the Cerebellum. eNeuro, 3(3). https://doi.org/10.1523/ENEURO.0048-16.2016

Chen, W., Dong, J., Plate, L., Mortenson, D. E., Brighty, G. J., Li, S., Liu, Y., Galmozzi, A., Lee, P. S., Hulce, J. J., Cravatt, B. F., Saez, E., Powers, E. T., Wilson, I. A., Sharpless, K. B., & Kelly, J. W. (2016). Arylfluorosulfates Inactivate Intracellular Lipid Binding Protein(s) through Chemoselective SuFEx Reaction with a Binding Site Tyr Residue. J Am Chem Soc, 138(23), 7353-7364. https://doi.org/10.1021/jacs.6b02960

Burston, J. J., Mapp, P. I., Sarmad, S., Barrett, D. A., Niphakis, M. J., Cravatt, B. F., Walsh, D. A., & Chapman, V. (2016). Robust anti-nociceptive effects of monoacylglycerol lipase inhibition in a model of osteoarthritis pain. Br J Pharmacol, 173(21), 3134-3144. https://doi.org/10.1111/bph.13574

Buczynski, M. W., Herman, M. A., Hsu, K. L., Natividad, L. A., Irimia, C., Polis, I. Y., Pugh, H., Chang, J. W., Niphakis, M. J., Cravatt, B. F., Roberto, M., & Parsons, L. H. (2016). Diacylglycerol lipase disinhibits VTA dopamine neurons during chronic nicotine exposure. Proc Natl Acad Sci U S A, 113(4), 1086-1091. https://doi.org/10.1073/pnas.1522672113

Briggs, K. J., Koivunen, P., Cao, S., Backus, K. M., Olenchock, B. A., Patel, H., Zhang, Q., Signoretti, S., Gerfen, G. J., Richardson, A. L., Witkiewicz, A. K., Cravatt, B. F., Clardy, J., & Kaelin, W. G., Jr. (2016). Paracrine Induction of HIF by Glutamate in Breast Cancer: EglN1 Senses Cysteine. Cell, 166(1), 126-139. https://doi.org/10.1016/j.cell.2016.05.042

Blewett, M. M., Xie, J., Zaro, B. W., Backus, K. M., Altman, A., Teijaro, J. R., & Cravatt, B. F. (2016). Chemical proteomic map of dimethyl fumarate-sensitive cysteines in primary human T cells. Sci Signal, 9(445), rs10. https://doi.org/10.1126/scisignal.aaf7694

Bilbao, A., Serrano, A., Cippitelli, A., Pavon, F. J., Giuffrida, A., Suarez, J., Garcia-Marchena, N., Baixeras, E., Gomez de Heras, R., Orio, L., Alen, F., Ciccocioppo, R., Cravatt, B. F., Parsons, L. H., Piomelli, D., & Rodriguez de Fonseca, F. (2016). Role of the satiety factor oleoylethanolamide in alcoholism. Addict Biol, 21(4), 859-872. https://doi.org/10.1111/adb.12276

Backus, K. M., Correia, B. E., Lum, K. M., Forli, S., Horning, B. D., Gonzalez-Paez, G. E., Chatterjee, S., Lanning, B. R., Teijaro, J. R., Olson, A. J., Wolan, D. W., & Cravatt, B. F. (2016). Proteome-wide covalent ligand discovery in native biological systems. Nature, 534(7608), 570-574. https://doi.org/10.1038/nature18002

2015:

Zhao, N., Darby, C. M., Small, J., Bachovchin, D. A., Jiang, X., Burns-Huang, K. E., Botella, H., Ehrt, S., Boger, D. L., Anderson, E. D., Cravatt, B. F., Speers, A. E., Fernandez-Vega, V., Hodder, P. S., Eberhart, C., Rosen, H., Spicer, T. P., & Nathan, C. F. (2015). Target-based screen against a periplasmic serine protease that regulates intrabacterial pH homeostasis in Mycobacterium tuberculosis. ACS Chem Biol, 10(2), 364-371. https://doi.org/10.1021/cb500746z

Zhang, Z., Wang, W., Zhong, P., Liu, S. J., Long, J. Z., Zhao, L., Gao, H. Q., Cravatt, B. F., & Liu, Q. S. (2015). Blockade of 2-arachidonoylglycerol hydrolysis produces antidepressant-like effects and enhances adult hippocampal neurogenesis and synaptic plasticity. Hippocampus, 25(1), 16-26. https://doi.org/10.1002/hipo.22344

Wiebelhaus, J. M., Grim, T. W., Owens, R. A., Lazenka, M. F., Sim-Selley, L. J., Abdullah, R. A., Niphakis, M. J., Vann, R. E., Cravatt, B. F., Wiley, J. L., Negus, S. S., & Lichtman, A. H. (2015). Delta9-tetrahydrocannabinol and endocannabinoid degradative enzyme inhibitors attenuate intracranial self-stimulation in mice. J Pharmacol Exp Ther, 352(2), 195-207. https://doi.org/10.1124/jpet.114.218677

Viader, A., Blankman, J. L., Zhong, P., Liu, X., Schlosburg, J. E., Joslyn, C. M., Liu, Q. S., Tomarchio, A. J., Lichtman, A. H., Selley, D. E., Sim-Selley, L. J., & Cravatt, B. F. (2015). Metabolic Interplay between Astrocytes and Neurons Regulates Endocannabinoid Action. Cell Rep, 12(5), 798-808. https://doi.org/10.1016/j.celrep.2015.06.075

Vazquez, C., Tolon, R. M., Pazos, M. R., Moreno, M., Koester, E. C., Cravatt, B. F., Hillard, C. J., & Romero, J. (2015). Endocannabinoids regulate the activity of astrocytic hemichannels and the microglial response against an injury: In vivo studies. Neurobiol Dis, 79, 41-50. https://doi.org/10.1016/j.nbd.2015.04.005

Vazquez, C., Tolon, R. M., Grande, M. T., Caraza, M., Moreno, M., Koester, E. C., Villaescusa, B., Ruiz-Valdepenas, L., Fernandez-Sanchez, F. J., Cravatt, B. F., Hillard, C. J., & Romero, J. (2015). Endocannabinoid regulation of amyloid-induced neuroinflammation. Neurobiol Aging, 36(11), 3008-3019. https://doi.org/10.1016/j.neurobiolaging.2015.08.003

Schreiber, S. L., Kotz, J. D., Li, M., Aube, J., Austin, C. P., Reed, J. C., Rosen, H., White, E. L., Sklar, L. A., Lindsley, C. W., Alexander, B. R., Bittker, J. A., Clemons, P. A., de Souza, A., Foley, M. A., Palmer, M., Shamji, A. F., Wawer, M. J., McManus, O., . . . Team, N. I. H. M. L. P. (2015). Advancing Biological Understanding and Therapeutics Discovery with Small-Molecule Probes. Cell, 161(6), 1252-1265. https://doi.org/10.1016/j.cell.2015.05.023

Sanchez-Alavez, M., Nguyen, W., Mori, S., Moroncini, G., Viader, A., Nomura, D. K., Cravatt, B. F., & Conti, B. (2015). Monoacylglycerol Lipase Regulates Fever Response. PLoS One, 10(8), e0134437. https://doi.org/10.1371/journal.pone.0134437

Rock, E. M., Limebeer, C. L., Ward, J. M., Cohen, A., Grove, K., Niphakis, M. J., Cravatt, B. F., & Parker, L. A. (2015). Interference with acute nausea and anticipatory nausea in rats by fatty acid amide hydrolase (FAAH) inhibition through a PPARalpha and CB1 receptor mechanism, respectively: a double dissociation. Psychopharmacology (Berl), 232(20), 3841-3848. https://doi.org/10.1007/s00213-015-4050-7

Parker, L. A., Niphakis, M. J., Downey, R., Limebeer, C. L., Rock, E. M., Sticht, M. A., Morris, H., Abdullah, R. A., Lichtman, A. H., & Cravatt, B. F. (2015). Effect of selective inhibition of monoacylglycerol lipase (MAGL) on acute nausea, anticipatory nausea, and vomiting in rats and Suncus murinus. Psychopharmacology (Berl), 232(3), 583-593. https://doi.org/10.1007/s00213-014-3696-x

Niphakis, M. J., Lum, K. M., Cognetta, A. B., 3rd, Correia, B. E., Ichu, T. A., Olucha, J., Brown, S. J., Kundu, S., Piscitelli, F., Rosen, H., & Cravatt, B. F. (2015). A Global Map of Lipid-Binding Proteins and Their Ligandability in Cells. Cell, 161(7), 1668-1680. https://doi.org/10.1016/j.cell.2015.05.045

Nass, S. R., Long, J. Z., Schlosburg, J. E., Cravatt, B. F., Lichtman, A. H., & Kinsey, S. G. (2015). Endocannabinoid Catabolic Enzymes Play Differential Roles in Thermal Homeostasis in Response to Environmental or Immune Challenge. J Neuroimmune Pharmacol, 10(2), 364-370. https://doi.org/10.1007/s11481-015-9593-1

Muldoon, P. P., Chen, J., Harenza, J. L., Abdullah, R. A., Sim-Selley, L. J., Cravatt, B. F., Miles, M. F., Chen, X., Lichtman, A. H., & Damaj, M. I. (2015). Inhibition of monoacylglycerol lipase reduces nicotine withdrawal. Br J Pharmacol, 172(3), 869-882. https://doi.org/10.1111/bph.12948

Lee, H. C., Simon, G. M., & Cravatt, B. F. (2015). ABHD4 regulates multiple classes of N-acyl phospholipids in the mammalian central nervous system. Biochemistry, 54(15), 2539-2549. https://doi.org/10.1021/acs.biochem.5b00207

Kohnz, R. A., Mulvihill, M. M., Chang, J. W., Hsu, K. L., Sorrentino, A., Cravatt, B. F., Bandyopadhyay, S., Goga, A., & Nomura, D. K. (2015). Activity-Based Protein Profiling of Oncogene-Driven Changes in Metabolism Reveals Broad Dysregulation of PAFAH1B2 and 1B3 in Cancer. ACS Chem Biol, 10(7), 1624-1630. https://doi.org/10.1021/acschembio.5b00053

Kamat, S. S., Camara, K., Parsons, W. H., Chen, D. H., Dix, M. M., Bird, T. D., Howell, A. R., & Cravatt, B. F. (2015). Immunomodulatory lysophosphatidylserines are regulated by ABHD16A and ABHD12 interplay. Nature Chemical Biology, 11(2), 164-171. https://doi.org/10.1038/nchembio.1721

Janssen, F. J., Baggelaar, M. P., Hummel, J. J., Overkleeft, H. S., Cravatt, B. F., Boger, D. L., & van der Stelt, M. (2015). Comprehensive Analysis of Structure-Activity Relationships of alpha-Ketoheterocycles as sn-1-Diacylglycerol Lipase alpha Inhibitors. J Med Chem, 58(24), 9742-9753. https://doi.org/10.1021/acs.jmedchem.5b01627

Ignatowska-Jankowska, B., Wilkerson, J. L., Mustafa, M., Abdullah, R., Niphakis, M., Wiley, J. L., Cravatt, B. F., & Lichtman, A. H. (2015). Selective monoacylglycerol lipase inhibitors: antinociceptive versus cannabimimetic effects in mice. J Pharmacol Exp Ther, 353(2), 424-432. https://doi.org/10.1124/jpet.114.222315

Hruba, L., Seillier, A., Zaki, A., Cravatt, B. F., Lichtman, A. H., Giuffrida, A., & McMahon, L. R. (2015). Simultaneous inhibition of fatty acid amide hydrolase and monoacylglycerol lipase shares discriminative stimulus effects with Delta9-tetrahydrocannabinol in mice. J Pharmacol Exp Ther, 353(2), 261-268. https://doi.org/10.1124/jpet.115.222836

Ghosh, S., Kinsey, S. G., Liu, Q. S., Hruba, L., McMahon, L. R., Grim, T. W., Merritt, C. R., Wise, L. E., Abdullah, R. A., Selley, D. E., Sim-Selley, L. J., Cravatt, B. F., & Lichtman, A. H. (2015). Full Fatty Acid Amide Hydrolase Inhibition Combined with Partial Monoacylglycerol Lipase Inhibition: Augmented and Sustained Antinociceptive Effects with Reduced Cannabimimetic Side Effects in Mice. J Pharmacol Exp Ther, 354(2), 111-120. https://doi.org/10.1124/jpet.115.222851

Gamage, T. F., Ignatowska-Jankowska, B. M., Muldoon, P. P., Cravatt, B. F., Damaj, M. I., & Lichtman, A. H. (2015). Differential effects of endocannabinoid catabolic inhibitors on morphine withdrawal in mice. Drug Alcohol Depend, 146, 7-16. https://doi.org/10.1016/j.drugalcdep.2014.11.015

Dincheva, I., Drysdale, A. T., Hartley, C. A., Johnson, D. C., Jing, D., King, E. C., Ra, S., Gray, J. M., Yang, R., DeGruccio, A. M., Huang, C., Cravatt, B. F., Glatt, C. E., Hill, M. N., Casey, B. J., & Lee, F. S. (2015). FAAH genetic variation enhances fronto-amygdala function in mouse and human. Nat Commun, 6, 6395. https://doi.org/10.1038/ncomms7395

Cravatt, B. F., & Kodadek, T. (2015). Editorial overview: Omics: Methods to monitor and manipulate biological systems: recent advances in 'omics'. Curr Opin Chem Biol, 24, v-vii. https://doi.org/10.1016/j.cbpa.2014.12.023

Craney, A., Dix, M. M., Adhikary, R., Cravatt, B. F., & Romesberg, F. E. (2015). An Alternative Terminal Step of the General Secretory Pathway in Staphylococcus aureus. mBio, 6(4). https://doi.org/10.1128/mBio.01178-15

Cognetta, A. B., 3rd, Niphakis, M. J., Lee, H. C., Martini, M. L., Hulce, J. J., & Cravatt, B. F. (2015). Selective N-Hydroxyhydantoin Carbamate Inhibitors of Mammalian Serine Hydrolases. Chem Biol, 22(7), 928-937. https://doi.org/10.1016/j.chembiol.2015.05.018

Chang, J. W., Zuhl, A. M., Speers, A. E., Niessen, S., Brown, S. J., Mulvihill, M. M., Fan, Y. C., Spicer, T. P., Southern, M., Scampavia, L., Fernandez-Vega, V., Dix, M. M., Cameron, M. D., Hodder, P. S., Rosen, H., Nomura, D. K., Kwon, O., Hsu, K. L., & Cravatt, B. F. (2015). Selective inhibitor of platelet-activating factor acetylhydrolases 1b2 and 1b3 that impairs cancer cell survival. ACS Chem Biol, 10(4), 925-932. https://doi.org/10.1021/cb500893q

Camara, K., Kamat, S. S., Lasota, C. C., Cravatt, B. F., & Howell, A. R. (2015). Combining cross-metathesis and activity-based protein profiling: new beta-lactone motifs for targeting serine hydrolases. Bioorg Med Chem Lett, 25(2), 317-321. https://doi.org/10.1016/j.bmcl.2014.11.038

Baggelaar, M. P., Chameau, P. J., Kantae, V., Hummel, J., Hsu, K. L., Janssen, F., van der Wel, T., Soethoudt, M., Deng, H., den Dulk, H., Allara, M., Florea, B. I., Di Marzo, V., Wadman, W. J., Kruse, C. G., Overkleeft, H. S., Hankemeier, T., Werkman, T. R., Cravatt, B. F., & van der Stelt, M. (2015). Highly Selective, Reversible Inhibitor Identified by Comparative Chemoproteomics Modulates Diacylglycerol Lipase Activity in Neurons. J Am Chem Soc, 137(27), 8851-8857. https://doi.org/10.1021/jacs.5b04883

Arrowsmith, C. H., Audia, J. E., Austin, C., Baell, J., Bennett, J., Blagg, J., Bountra, C., Brennan, P. E., Brown, P. J., Bunnage, M. E., Buser-Doepner, C., Campbell, R. M., Carter, A. J., Cohen, P., Copeland, R. A., Cravatt, B., Dahlin, J. L., Dhanak, D., Edwards, A. M., . . . Zuercher, W. J. (2015). The promise and peril of chemical probes. Nature Chemical Biology, 11(8), 536-541. https://doi.org/10.1038/nchembio.1867

Arrowsmith, C. H., Audia, J. E., Austin, C., Baell, J., Bennett, J., Blagg, J., Bountra, C., Brennan, P. E., Brown, P. J., Bunnage, M. E., Buser-Doepner, C., Campbell, R. M., Carter, A. J., Cohen, P., Copeland, R. A., Cravatt, B., Dahlin, J. L., Dhanak, D., Edwards, A. M., . . . Zuercher, W. J. (2015). Corrigendum: The promise and peril of chemical probes. Nature Chemical Biology, 11(11), 887. https://doi.org/10.1038/nchembio1115-887c

Adachi, S., Cognetta, A. B., 3rd, Niphakis, M. J., He, Z., Zajdlik, A., St Denis, J. D., Scully, C. C., Cravatt, B. F., & Yudin, A. K. (2015). Facile synthesis of borofragments and their evaluation in activity-based protein profiling. Chem Commun (Camb), 51(17), 3608-3611. https://doi.org/10.1039/c4cc09107h

2014:

Zhong, P., Wang, W., Pan, B., Liu, X., Zhang, Z., Long, J. Z., Zhang, H. T., Cravatt, B. F., & Liu, Q. S. (2014). Monoacylglycerol lipase inhibition blocks chronic stress-induced depressive-like behaviors via activation of mTOR signaling. Neuropsychopharmacology, 39(7), 1763-1776. https://doi.org/10.1038/npp.2014.24

Yun, B., Lee, H., Ghosh, M., Cravatt, B. F., Hsu, K. L., Bonventre, J. V., Ewing, H., Gelb, M. H., & Leslie, C. C. (2014). Serine hydrolase inhibitors block necrotic cell death by preventing calcium overload of the mitochondria and permeability transition pore formation. J Biol Chem, 289(3), 1491-1504. https://doi.org/10.1074/jbc.M113.497651

Wang, C., Weerapana, E., Blewett, M. M., & Cravatt, B. F. (2014). A chemoproteomic platform to quantitatively map targets of lipid-derived electrophiles. Nat Methods, 11(1), 79-85. https://doi.org/10.1038/nmeth.2759

Schlosburg, J. E., Kinsey, S. G., Ignatowska-Jankowska, B., Ramesh, D., Abdullah, R. A., Tao, Q., Booker, L., Long, J. Z., Selley, D. E., Cravatt, B. F., & Lichtman, A. H. (2014). Prolonged monoacylglycerol lipase blockade causes equivalent cannabinoid receptor type 1 receptor-mediated adaptations in fatty acid amide hydrolase wild-type and knockout mice. J Pharmacol Exp Ther, 350(2), 196-204. https://doi.org/10.1124/jpet.114.212753

Rajagopalan, S., Wang, C., Yu, K., Kuzin, A. P., Richter, F., Lew, S., Miklos, A. E., Matthews, M. L., Seetharaman, J., Su, M., Hunt, J. F., Cravatt, B. F., & Baker, D. (2014). Design of activated serine-containing catalytic triads with atomic-level accuracy. Nature Chemical Biology, 10(5), 386-391. https://doi.org/10.1038/nchembio.1498

Otrubova, K., Cravatt, B. F., & Boger, D. L. (2014). Design, synthesis, and characterization of alpha-ketoheterocycles that additionally target the cytosolic port Cys269 of fatty acid amide hydrolase. J Med Chem, 57(3), 1079-1089. https://doi.org/10.1021/jm401820q

Niphakis, M. J., & Cravatt, B. F. (2014). Enzyme inhibitor discovery by activity-based protein profiling. Annu Rev Biochem, 83, 341-377. https://doi.org/10.1146/annurev-biochem-060713-035708

Naydenov, A. V., Horne, E. A., Cheah, C. S., Swinney, K., Hsu, K. L., Cao, J. K., Marrs, W., Blankman, J. L., Tu, S., Cherry, A. E., Fung, S., Wen, A., Li, W., Saporito, M. S., Selley, D. E., Cravatt, B. F., Oakley, J. C., & Stella, N. (2014). ABHD6 blockade exerts antiepileptic activity in PTZ-induced seizures and in spontaneous seizures in R6/2 mice. Neuron, 83(2), 361-371. https://doi.org/10.1016/j.neuron.2014.06.030

Manna, J. D., Wepy, J. A., Hsu, K. L., Chang, J. W., Cravatt, B. F., & Marnett, L. J. (2014). Identification of the major prostaglandin glycerol ester hydrolase in human cancer cells. J Biol Chem, 289(49), 33741-33753. https://doi.org/10.1074/jbc.M114.582353

Lanning, B. R., Whitby, L. R., Dix, M. M., Douhan, J., Gilbert, A. M., Hett, E. C., Johnson, T. O., Joslyn, C., Kath, J. C., Niessen, S., Roberts, L. R., Schnute, M. E., Wang, C., Hulce, J. J., Wei, B., Whiteley, L. O., Hayward, M. M., & Cravatt, B. F. (2014). A road map to evaluate the proteome-wide selectivity of covalent kinase inhibitors. Nature Chemical Biology, 10(9), 760-767. https://doi.org/10.1038/nchembio.1582

Lajkiewicz, N. J., Cognetta, A. B., 3rd, Niphakis, M. J., Cravatt, B. F., & Porco, J. A., Jr. (2014). Remodeling natural products: chemistry and serine hydrolase activity of a rocaglate-derived beta-lactone. J Am Chem Soc, 136(6), 2659-2664. https://doi.org/10.1021/ja412431g

Kambe, T., Correia, B. E., Niphakis, M. J., & Cravatt, B. F. (2014). Mapping the protein interaction landscape for fully functionalized small-molecule probes in human cells. J Am Chem Soc, 136(30), 10777-10782. https://doi.org/10.1021/ja505517t

Inloes, J. M., Hsu, K. L., Dix, M. M., Viader, A., Masuda, K., Takei, T., Wood, M. R., & Cravatt, B. F. (2014). The hereditary spastic paraplegia-related enzyme DDHD2 is a principal brain triglyceride lipase. Proc Natl Acad Sci U S A, 111(41), 14924-14929. https://doi.org/10.1073/pnas.1413706111

Ignatowska-Jankowska, B. M., Ghosh, S., Crowe, M. S., Kinsey, S. G., Niphakis, M. J., Abdullah, R. A., Tao, Q., ST, O. N., Walentiny, D. M., Wiley, J. L., Cravatt, B. F., & Lichtman, A. H. (2014). In vivo characterization of the highly selective monoacylglycerol lipase inhibitor KML29: antinociceptive activity without cannabimimetic side effects. Br J Pharmacol, 171(6), 1392-1407. https://doi.org/10.1111/bph.12298

Hama, A. T., Germano, P., Varghese, M. S., Cravatt, B. F., Milne, G. T., Pearson, J. P., & Sagen, J. (2014). Fatty acid amide hydrolase (FAAH) inhibitors exert pharmacological effects, but lack antinociceptive efficacy in rats with neuropathic spinal cord injury pain. PLoS One, 9(5), e96396. https://doi.org/10.1371/journal.pone.0096396

Grim, T. W., Ghosh, S., Hsu, K. L., Cravatt, B. F., Kinsey, S. G., & Lichtman, A. H. (2014). Combined inhibition of FAAH and COX produces enhanced anti-allodynic effects in mouse neuropathic and inflammatory pain models. Pharmacol Biochem Behav, 124, 405-411. https://doi.org/10.1016/j.pbb.2014.07.008

Galmozzi, A., Sonne, S. B., Altshuler-Keylin, S., Hasegawa, Y., Shinoda, K., Luijten, I. H. N., Chang, J. W., Sharp, L. Z., Cravatt, B. F., Saez, E., & Kajimura, S. (2014). ThermoMouse: an in vivo model to identify modulators of UCP1 expression in brown adipose tissue. Cell Rep, 9(5), 1584-1593. https://doi.org/10.1016/j.celrep.2014.10.066

Galmozzi, A., Dominguez, E., Cravatt, B. F., & Saez, E. (2014). Application of activity-based protein profiling to study enzyme function in adipocytes. Methods Enzymol, 538, 151-169. https://doi.org/10.1016/B978-0-12-800280-3.00009-8

Dominguez, E., Galmozzi, A., Chang, J. W., Hsu, K. L., Pawlak, J., Li, W., Godio, C., Thomas, J., Partida, D., Niessen, S., O'Brien, P. E., Russell, A. P., Watt, M. J., Nomura, D. K., Cravatt, B. F., & Saez, E. (2014). Integrated phenotypic and activity-based profiling links Ces3 to obesity and diabetes. Nature Chemical Biology, 10(2), 113-121. https://doi.org/10.1038/nchembio.1429

Dix, M. M., Simon, G. M., & Cravatt, B. F. (2014). Global identification of caspase substrates using PROTOMAP (protein topography and migration analysis platform). Methods Mol Biol, 1133, 61-70. https://doi.org/10.1007/978-1-4939-0357-3_3

Deng, X., Liang, H., Ulanovskaya, O. A., Ji, Q., Zhou, T., Sun, F., Lu, Z., Hutchison, A. L., Lan, L., Wu, M., Cravatt, B. F., & He, C. (2014). Steady-state hydrogen peroxide induces glycolysis in Staphylococcus aureus and Pseudomonas aeruginosa. J Bacteriol, 196(14), 2499-2513. https://doi.org/10.1128/JB.01538-14

Dainese, E., De Fabritiis, G., Sabatucci, A., Oddi, S., Angelucci, C. B., Di Pancrazio, C., Giorgino, T., Stanley, N., Del Carlo, M., Cravatt, B. F., & Maccarrone, M. (2014). Membrane lipids are key modulators of the endocannabinoid-hydrolase FAAH. Biochem J, 457(3), 463-472. https://doi.org/10.1042/BJ20130960

Cravatt, B. F. (2014). TRP channels-Convergent sites of action for phytochemicals and endogenous lipid transmitters that regulate human sensation and physiology. ACS Chem Neurosci, 5(11), 1083. https://doi.org/10.1021/cn500263c

Chang, C. J., Cravatt, B. F., Johnson, D. S., & Lim, M. H. (2014). Molecular medicine and neurodegenerative diseases. Chem Soc Rev, 43(19), 6668-6671. https://doi.org/10.1039/c4cs90065k

Alpar, A., Tortoriello, G., Calvigioni, D., Niphakis, M. J., Milenkovic, I., Bakker, J., Cameron, G. A., Hanics, J., Morris, C. V., Fuzik, J., Kovacs, G. G., Cravatt, B. F., Parnavelas, J. G., Andrews, W. D., Hurd, Y. L., Keimpema, E., & Harkany, T. (2014). Endocannabinoids modulate cortical development by configuring Slit2/Robo1 signalling. Nat Commun, 5, 4421. https://doi.org/10.1038/ncomms5421

2013:

Ward, J., Spath, S. N., Pabst, B., Carpino, P. A., Ruggeri, R. B., Xing, G., Speers, A. E., Cravatt, B. F., & Ahn, K. (2013). Mechanistic characterization of a 2-thioxanthine myeloperoxidase inhibitor and selectivity assessment utilizing click chemistry--activity-based protein profiling. Biochemistry, 52(51), 9187-9201. https://doi.org/10.1021/bi401354d

Ulanovskaya, O. A., Zuhl, A. M., & Cravatt, B. F. (2013). NNMT promotes epigenetic remodeling in cancer by creating a metabolic methylation sink. Nature Chemical Biology, 9(5), 300-306. https://doi.org/10.1038/nchembio.1204

Thomas, G., Betters, J. L., Lord, C. C., Brown, A. L., Marshall, S., Ferguson, D., Sawyer, J., Davis, M. A., Melchior, J. T., Blume, L. C., Howlett, A. C., Ivanova, P. T., Milne, S. B., Myers, D. S., Mrak, I., Leber, V., Heier, C., Taschler, U., Blankman, J. L., . . . Brown, J. M. (2013). The serine hydrolase ABHD6 Is a critical regulator of the metabolic syndrome. Cell Rep, 5(2), 508-520. https://doi.org/10.1016/j.celrep.2013.08.047

Simon, G. M., Niphakis, M. J., & Cravatt, B. F. (2013). Determining target engagement in living systems. Nature Chemical Biology, 9(4), 200-205. https://doi.org/10.1038/nchembio.1211

Ramya, T. N., Weerapana, E., Cravatt, B. F., & Paulson, J. C. (2013). Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans. Glycobiology, 23(2), 211-221. https://doi.org/10.1093/glycob/cws144

Ramesh, D., Gamage, T. F., Vanuytsel, T., Owens, R. A., Abdullah, R. A., Niphakis, M. J., Shea-Donohue, T., Cravatt, B. F., & Lichtman, A. H. (2013). Dual inhibition of endocannabinoid catabolic enzymes produces enhanced antiwithdrawal effects in morphine-dependent mice. Neuropsychopharmacology, 38(6), 1039-1049. https://doi.org/10.1038/npp.2012.269

Pryce, G., Cabranes, A., Fernandez-Ruiz, J., Bisogno, T., Di Marzo, V., Long, J. Z., Cravatt, B. F., Giovannoni, G., & Baker, D. (2013). Control of experimental spasticity by targeting the degradation of endocannabinoids using selective fatty acid amide hydrolase inhibitors. Mult Scler, 19(14), 1896-1904. https://doi.org/10.1177/1352458513485982

Otrubova, K., Brown, M., McCormick, M. S., Han, G. W., O'Neal, S. T., Cravatt, B. F., Stevens, R. C., Lichtman, A. H., & Boger, D. L. (2013). Rational design of fatty acid amide hydrolase inhibitors that act by covalently bonding to two active site residues. J Am Chem Soc, 135(16), 6289-6299. https://doi.org/10.1021/ja4014997

Nomura, D. K., & Cravatt, B. F. (2013). Lipid metabolism in cancer. Biochim Biophys Acta, 1831(10), 1497-1498. https://doi.org/10.1016/j.bbalip.2013.08.001

Niphakis, M. J., Cognetta, A. B., 3rd, Chang, J. W., Buczynski, M. W., Parsons, L. H., Byrne, F., Burston, J. J., Chapman, V., & Cravatt, B. F. (2013). Evaluation of NHS carbamates as a potent and selective class of endocannabinoid hydrolase inhibitors. ACS Chem Neurosci, 4(9), 1322-1332. https://doi.org/10.1021/cn400116z

Nagano, J. M., Hsu, K. L., Whitby, L. R., Niphakis, M. J., Speers, A. E., Brown, S. J., Spicer, T., Fernandez-Vega, V., Ferguson, J., Hodder, P., Srinivasan, P., Gonzalez, T. D., Rosen, H., Bahnson, B. J., & Cravatt, B. F. (2013). Selective inhibitors and tailored activity probes for lipoprotein-associated phospholipase A(2). Bioorg Med Chem Lett, 23(3), 839-843. https://doi.org/10.1016/j.bmcl.2012.11.061

Molica, F., Burger, F., Thomas, A., Staub, C., Tailleux, A., Staels, B., Pelli, G., Zimmer, A., Cravatt, B., Matter, C. M., Pacher, P., & Steffens, S. (2013). Endogenous cannabinoid receptor CB1 activation promotes vascular smooth-muscle cell proliferation and neointima formation. J Lipid Res, 54(5), 1360-1368. https://doi.org/10.1194/jlr.M035147

Moellering, R. E., & Cravatt, B. F. (2013). Functional lysine modification by an intrinsically reactive primary glycolytic metabolite. Science, 341(6145), 549-553. https://doi.org/10.1126/science.1238327

Lowery, C. A., Matamouros, S., Niessen, S., Zhu, J., Scolnick, J., Lively, J. M., Cravatt, B. F., Miller, S. I., Kaufmann, G. F., & Janda, K. D. (2013). A chemical biology approach to interrogate quorum-sensing regulated behaviors at the molecular and cellular level. Chem Biol, 20(7), 903-911. https://doi.org/10.1016/j.chembiol.2013.05.009

Li, J., Cisar, J. S., Zhou, C. Y., Vera, B., Williams, H., Rodriguez, A. D., Cravatt, B. F., & Romo, D. (2013). Simultaneous structure-activity studies and arming of natural products by C-H amination reveal cellular targets of eupalmerin acetate. Nat Chem, 5(6), 510-517. https://doi.org/10.1038/nchem.1653

Lenglet, S., Thomas, A., Soehnlein, O., Montecucco, F., Burger, F., Pelli, G., Galan, K., Cravatt, B., Staub, C., & Steffens, S. (2013). Fatty acid amide hydrolase deficiency enhances intraplaque neutrophil recruitment in atherosclerotic mice. Arterioscler Thromb Vasc Biol, 33(2), 215-223. https://doi.org/10.1161/ATVBAHA.112.300275

Komatsu, T., Hanaoka, K., Adibekian, A., Yoshioka, K., Terai, T., Ueno, T., Kawaguchi, M., Cravatt, B. F., & Nagano, T. (2013). Diced electrophoresis gel assay for screening enzymes with specified activities. J Am Chem Soc, 135(16), 6002-6005. https://doi.org/10.1021/ja401792d

Kinsey, S. G., Wise, L. E., Ramesh, D., Abdullah, R., Selley, D. E., Cravatt, B. F., & Lichtman, A. H. (2013). Repeated low-dose administration of the monoacylglycerol lipase inhibitor JZL184 retains cannabinoid receptor type 1-mediated antinociceptive and gastroprotective effects. J Pharmacol Exp Ther, 345(3), 492-501. https://doi.org/10.1124/jpet.112.201426

Ismail, H. M., O'Neill, P. M., Hong, D. W., Finn, R. D., Henderson, C. J., Wright, A. T., Cravatt, B. F., Hemingway, J., & Paine, M. J. (2013). Pyrethroid activity-based probes for profiling cytochrome P450 activities associated with insecticide interactions. Proc Natl Acad Sci U S A, 110(49), 19766-19771. https://doi.org/10.1073/pnas.1320185110

Hulce, J. J., Cognetta, A. B., Niphakis, M. J., Tully, S. E., & Cravatt, B. F. (2013). Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat Methods, 10(3), 259-264. https://doi.org/10.1038/nmeth.2368

Hsu, K. L., Tsuboi, K., Whitby, L. R., Speers, A. E., Pugh, H., Inloes, J., & Cravatt, B. F. (2013). Development and optimization of piperidyl-1,2,3-triazole ureas as selective chemical probes of endocannabinoid biosynthesis. J Med Chem, 56(21), 8257-8269. https://doi.org/10.1021/jm400898x

Hsu, K. L., Tsuboi, K., Chang, J. W., Whitby, L. R., Speers, A. E., Pugh, H., & Cravatt, B. F. (2013). Discovery and optimization of piperidyl-1,2,3-triazole ureas as potent, selective, and in vivo-active inhibitors of alpha/beta-hydrolase domain containing 6 (ABHD6). J Med Chem, 56(21), 8270-8279. https://doi.org/10.1021/jm400899c

Holly, S. P., Chang, J. W., Li, W., Niessen, S., Phillips, R. M., Piatt, R., Black, J. L., Smith, M. C., Boulaftali, Y., Weyrich, A. S., Bergmeier, W., Cravatt, B. F., & Parise, L. V. (2013). Chemoproteomic discovery of AADACL1 as a regulator of human platelet activation. Chem Biol, 20(9), 1125-1134. https://doi.org/10.1016/j.chembiol.2013.07.011

Hill, M. N., Kumar, S. A., Filipski, S. B., Iverson, M., Stuhr, K. L., Keith, J. M., Cravatt, B. F., Hillard, C. J., Chattarji, S., & McEwen, B. S. (2013). Disruption of fatty acid amide hydrolase activity prevents the effects of chronic stress on anxiety and amygdalar microstructure. Mol Psychiatry, 18(10), 1125-1135. https://doi.org/10.1038/mp.2012.90

Gu, C., Shannon, D. A., Colby, T., Wang, Z., Shabab, M., Kumari, S., Villamor, J. G., McLaughlin, C. J., Weerapana, E., Kaiser, M., Cravatt, B. F., & van der Hoorn, R. A. (2013). Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases. Chem Biol, 20(4), 541-548. https://doi.org/10.1016/j.chembiol.2013.01.016

Ghosh, S., Wise, L. E., Chen, Y., Gujjar, R., Mahadevan, A., Cravatt, B. F., & Lichtman, A. H. (2013). The monoacylglycerol lipase inhibitor JZL184 suppresses inflammatory pain in the mouse carrageenan model. Life Sci, 92(8-9), 498-505. https://doi.org/10.1016/j.lfs.2012.06.020

French, J. B., Zhao, H., An, S., Niessen, S., Deng, Y., Cravatt, B. F., & Benkovic, S. J. (2013). Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome. Proc Natl Acad Sci U S A, 110(7), 2528-2533. https://doi.org/10.1073/pnas.1300173110

Deng, X., Weerapana, E., Ulanovskaya, O., Sun, F., Liang, H., Ji, Q., Ye, Y., Fu, Y., Zhou, L., Li, J., Zhang, H., Wang, C., Alvarez, S., Hicks, L. M., Lan, L., Wu, M., Cravatt, B. F., & He, C. (2013). Proteome-wide quantification and characterization of oxidation-sensitive cysteines in pathogenic bacteria. Cell Host Microbe, 13(3), 358-370. https://doi.org/10.1016/j.chom.2013.02.004

Chen, D. H., Naydenov, A., Blankman, J. L., Mefford, H. C., Davis, M., Sul, Y., Barloon, A. S., Bonkowski, E., Wolff, J., Matsushita, M., Smith, C., Cravatt, B. F., Mackie, K., Raskind, W. H., Stella, N., & Bird, T. D. (2013). Two novel mutations in ABHD12: expansion of the mutation spectrum in PHARC and assessment of their functional effects. Hum Mutat, 34(12), 1672-1678. https://doi.org/10.1002/humu.22437

Chang, J. W., Cognetta, A. B., 3rd, Niphakis, M. J., & Cravatt, B. F. (2013). Proteome-wide reactivity profiling identifies diverse carbamate chemotypes tuned for serine hydrolase inhibition. ACS Chem Biol, 8(7), 1590-1599. https://doi.org/10.1021/cb400261h

Cao, Z., Mulvihill, M. M., Mukhopadhyay, P., Xu, H., Erdelyi, K., Hao, E., Holovac, E., Hasko, G., Cravatt, B. F., Nomura, D. K., & Pacher, P. (2013). Monoacylglycerol lipase controls endocannabinoid and eicosanoid signaling and hepatic injury in mice. Gastroenterology, 144(4), 808-817 e815. https://doi.org/10.1053/j.gastro.2012.12.028

Blankman, J. L., Long, J. Z., Trauger, S. A., Siuzdak, G., & Cravatt, B. F. (2013). ABHD12 controls brain lysophosphatidylserine pathways that are deregulated in a murine model of the neurodegenerative disease PHARC. Proc Natl Acad Sci U S A, 110(4), 1500-1505. https://doi.org/10.1073/pnas.1217121110

Blankman, J. L., & Cravatt, B. F. (2013). Chemical probes of endocannabinoid metabolism. Pharmacol Rev, 65(2), 849-871. https://doi.org/10.1124/pr.112.006387

Bisogno, T., Mahadevan, A., Coccurello, R., Chang, J. W., Allara, M., Chen, Y., Giacovazzo, G., Lichtman, A., Cravatt, B., Moles, A., & Di Marzo, V. (2013). A novel fluorophosphonate inhibitor of the biosynthesis of the endocannabinoid 2-arachidonoylglycerol with potential anti-obesity effects. Br J Pharmacol, 169(4), 784-793. https://doi.org/10.1111/bph.12013

Beisner, D. R., Langerak, P., Parker, A. E., Dahlberg, C., Otero, F. J., Sutton, S. E., Poirot, L., Barnes, W., Young, M. A., Niessen, S., Wiltshire, T., Bodendorf, U., Martoglio, B., Cravatt, B., & Cooke, M. P. (2013). The intramembrane protease Sppl2a is required for B cell and DC development and survival via cleavage of the invariant chain. J Exp Med, 210(1), 23-30. https://doi.org/10.1084/jem.20121072

2012:

Zuhl, A. M., Mohr, J. T., Bachovchin, D. A., Niessen, S., Hsu, K. L., Berlin, J. M., Dochnahl, M., Lopez-Alberca, M. P., Fu, G. C., & Cravatt, B. F. (2012). Competitive activity-based protein profiling identifies aza-beta-lactams as a versatile chemotype for serine hydrolase inhibition. J Am Chem Soc, 134(11), 5068-5071. https://doi.org/10.1021/ja300799t

Yu, P. T., Babicky, M., Jaquish, D., French, R., Marayuma, K., Mose, E., Niessen, S., Hoover, H., Shields, D., Cheresh, D., Cravatt, B. F., & Lowy, A. M. (2012). The RON-receptor regulates pancreatic cancer cell migration through phosphorylation-dependent breakdown of the hemidesmosome. Int J Cancer, 131(8), 1744-1754. https://doi.org/10.1002/ijc.27447

Wiskerke, J., Irimia, C., Cravatt, B. F., De Vries, T. J., Schoffelmeer, A. N., Pattij, T., & Parsons, L. H. (2012). Characterization of the effects of reuptake and hydrolysis inhibition on interstitial endocannabinoid levels in the brain: an in vivo microdialysis study. ACS Chem Neurosci, 3(5), 407-417. https://doi.org/10.1021/cn300036b

Wise, L. E., Long, K. A., Abdullah, R. A., Long, J. Z., Cravatt, B. F., & Lichtman, A. H. (2012). Dual fatty acid amide hydrolase and monoacylglycerol lipase blockade produces THC-like Morris water maze deficits in mice. ACS Chem Neurosci, 3(5), 369-378. https://doi.org/10.1021/cn200130s

Tai, T., Tsuboi, K., Uyama, T., Masuda, K., Cravatt, B. F., Houchi, H., & Ueda, N. (2012). Endogenous molecules stimulating N-acylethanolamine-hydrolyzing acid amidase (NAAA). ACS Chem Neurosci, 3(5), 379-385. https://doi.org/10.1021/cn300007s

Stock, K., Kumar, J., Synowitz, M., Petrosino, S., Imperatore, R., Smith, E. S., Wend, P., Purfurst, B., Nuber, U. A., Gurok, U., Matyash, V., Walzlein, J. H., Chirasani, S. R., Dittmar, G., Cravatt, B. F., Momma, S., Lewin, G. R., Ligresti, A., De Petrocellis, L., . . . Glass, R. (2012). Neural precursor cells induce cell death of high-grade astrocytomas through stimulation of TRPV1. Nat Med, 18(8), 1232-1238. https://doi.org/10.1038/nm.2827

Sticht, M. A., Long, J. Z., Rock, E. M., Limebeer, C. L., Mechoulam, R., Cravatt, B. F., & Parker, L. A. (2012). Inhibition of monoacylglycerol lipase attenuates vomiting in Suncus murinus and 2-arachidonoyl glycerol attenuates nausea in rats. Br J Pharmacol, 165(8), 2425-2435. https://doi.org/10.1111/j.1476-5381.2011.01407.x

Skaddan, M. B., Zhang, L., Johnson, D. S., Zhu, A., Zasadny, K. R., Coelho, R. V., Kuszpit, K., Currier, G., Fan, K. H., Beck, E. M., Chen, L., Drozda, S. E., Balan, G., Niphakis, M., Cravatt, B. F., Ahn, K., Bocan, T., & Villalobos, A. (2012). The synthesis and in vivo evaluation of [18F]PF-9811: a novel PET ligand for imaging brain fatty acid amide hydrolase (FAAH). Nucl Med Biol, 39(7), 1058-1067. https://doi.org/10.1016/j.nucmedbio.2012.03.011

Seeliger, J. C., Holsclaw, C. M., Schelle, M. W., Botyanszki, Z., Gilmore, S. A., Tully, S. E., Niederweis, M., Cravatt, B. F., Leary, J. A., & Bertozzi, C. R. (2012). Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J Biol Chem, 287(11), 7990-8000. https://doi.org/10.1074/jbc.M111.315473

Saario, S. M., McKinney, M. K., Speers, A. E., Wang, C., & Cravatt, B. F. (2012). Clickable, photoreactive inhibitors to probe the active site microenvironment of fatty acid amide hydrolase(). Chem Sci, 3(1), 77-83. https://doi.org/10.1039/C1SC00336D

Rothmann, M., Niessen, S., Haushalter, R. W., Cravatt, B. F., & Burkart, M. D. (2012). Resin-based investigation of acyl carrier protein interaction networks in Escherichia coli. Bioorg Med Chem, 20(2), 667-671. https://doi.org/10.1016/j.bmc.2011.10.053

Palumbo-Zerr, K., Horn, A., Distler, A., Zerr, P., Dees, C., Beyer, C., Selvi, E., Cravatt, B. F., Distler, O., Schett, G., & Distler, J. H. (2012). Inactivation of fatty acid amide hydrolase exacerbates experimental fibrosis by enhanced endocannabinoid-mediated activation of CB1. Ann Rheum Dis, 71(12), 2051-2054. https://doi.org/10.1136/annrheumdis-2012-201823

Niphakis, M. J., Johnson, D. S., Ballard, T. E., Stiff, C., & Cravatt, B. F. (2012). O-hydroxyacetamide carbamates as a highly potent and selective class of endocannabinoid hydrolase inhibitors. ACS Chem Neurosci, 3(5), 418-426. https://doi.org/10.1021/cn200089j

Moellering, R. E., & Cravatt, B. F. (2012). How chemoproteomics can enable drug discovery and development. Chem Biol, 19(1), 11-22. https://doi.org/10.1016/j.chembiol.2012.01.001

Liu, X., Dix, M., Speers, A. E., Bachovchin, D. A., Zuhl, A. M., Cravatt, B. F., & Kodadek, T. J. (2012). Rapid development of a potent photo-triggered inhibitor of the serine hydrolase RBBP9. Chembiochem, 13(14), 2082-2093. https://doi.org/10.1002/cbic.201200445

Lim, S. K., Park, M. J., Lim, J. C., Kim, J. C., Han, H. J., Kim, G. Y., Cravatt, B. F., Woo, C. H., Ma, S. J., Yoon, K. C., & Park, S. H. (2012). Hyperglycemia induces apoptosis via CB1 activation through the decrease of FAAH 1 in retinal pigment epithelial cells. J Cell Physiol, 227(2), 569-577. https://doi.org/10.1002/jcp.22756

Li, Y., Martin, B. R., Cravatt, B. F., & Hofmann, S. L. (2012). DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells. J Biol Chem, 287(1), 523-530. https://doi.org/10.1074/jbc.M111.306183

Keow, J. Y., Pond, E. D., Cisar, J. S., Cravatt, B. F., & Crawford, B. D. (2012). Activity-based labeling of matrix metalloproteinases in living vertebrate embryos. PLoS One, 7(8), e43434. https://doi.org/10.1371/journal.pone.0043434

Kaschani, F., Nickel, S., Pandey, B., Cravatt, B. F., Kaiser, M., & van der Hoorn, R. A. (2012). Selective inhibition of plant serine hydrolases by agrochemicals revealed by competitive ABPP. Bioorg Med Chem, 20(2), 597-600. https://doi.org/10.1016/j.bmc.2011.06.040

Kaczocha, M., Lin, Q., Nelson, L. D., McKinney, M. K., Cravatt, B. F., London, E., & Deutsch, D. G. (2012). Anandamide externally added to lipid vesicles containing trapped fatty acid amide hydrolase (FAAH) is readily hydrolyzed in a sterol-modulated fashion. ACS Chem Neurosci, 3(5), 364-368. https://doi.org/10.1021/cn300001w

Hsu, K. L., Tsuboi, K., Adibekian, A., Pugh, H., Masuda, K., & Cravatt, B. F. (2012). DAGLbeta inhibition perturbs a lipid network involved in macrophage inflammatory responses. Nature Chemical Biology, 8(12), 999-1007. https://doi.org/10.1038/nchembio.1105

Dix, M. M., Simon, G. M., Wang, C., Okerberg, E., Patricelli, M. P., & Cravatt, B. F. (2012). Functional interplay between caspase cleavage and phosphorylation sculpts the apoptotic proteome. Cell, 150(2), 426-440. https://doi.org/10.1016/j.cell.2012.05.040

Dillon, M. B., Bachovchin, D. A., Brown, S. J., Finn, M. G., Rosen, H., Cravatt, B. F., & Mowen, K. A. (2012). Novel inhibitors for PRMT1 discovered by high-throughput screening using activity-based fluorescence polarization. ACS Chem Biol, 7(7), 1198-1204. https://doi.org/10.1021/cb300024c

Di Venere, A., Dainese, E., Fezza, F., Angelucci, B. C., Rosato, N., Cravatt, B. F., Finazzi-Agro, A., Mei, G., & Maccarrone, M. (2012). Rat and human fatty acid amide hydrolases: overt similarities and hidden differences. Biochim Biophys Acta, 1821(11), 1425-1433. https://doi.org/10.1016/j.bbalip.2012.07.021

Cisar, J. S., & Cravatt, B. F. (2012). Fully functionalized small-molecule probes for integrated phenotypic screening and target identification. J Am Chem Soc, 134(25), 10385-10388. https://doi.org/10.1021/ja304213w

Chang, J. W., Niphakis, M. J., Lum, K. M., Cognetta, A. B., 3rd, Wang, C., Matthews, M. L., Niessen, S., Buczynski, M. W., Parsons, L. H., & Cravatt, B. F. (2012). Highly selective inhibitors of monoacylglycerol lipase bearing a reactive group that is bioisosteric with endocannabinoid substrates. Chem Biol, 19(5), 579-588. https://doi.org/10.1016/j.chembiol.2012.03.009

Chang, J. W., Moellering, R. E., & Cravatt, B. F. (2012). An activity-based imaging probe for the integral membrane hydrolase KIAA1363. Angew Chem Int Ed Engl, 51(4), 966-970. https://doi.org/10.1002/anie.201107236

Brown, W. H., Gillum, M. P., Lee, H. Y., Camporez, J. P., Zhang, X. M., Jeong, J. K., Alves, T. C., Erion, D. M., Guigni, B. A., Kahn, M., Samuel, V. T., Cravatt, B. F., Diano, S., & Shulman, G. I. (2012). Fatty acid amide hydrolase ablation promotes ectopic lipid storage and insulin resistance due to centrally mediated hypothyroidism. Proc Natl Acad Sci U S A, 109(37), 14966-14971. https://doi.org/10.1073/pnas.1212887109

Booker, L., Kinsey, S. G., Abdullah, R. A., Blankman, J. L., Long, J. Z., Ezzili, C., Boger, D. L., Cravatt, B. F., & Lichtman, A. H. (2012). The fatty acid amide hydrolase (FAAH) inhibitor PF-3845 acts in the nervous system to reverse LPS-induced tactile allodynia in mice. Br J Pharmacol, 165(8), 2485-2496. https://doi.org/10.1111/j.1476-5381.2011.01445.x

Benjamin, D. I., Cravatt, B. F., & Nomura, D. K. (2012). Global profiling strategies for mapping dysregulated metabolic pathways in cancer. Cell Metab, 16(5), 565-577. https://doi.org/10.1016/j.cmet.2012.09.013

Benito, C., Tolon, R. M., Castillo, A. I., Ruiz-Valdepenas, L., Martinez-Orgado, J. A., Fernandez-Sanchez, F. J., Vazquez, C., Cravatt, B. F., & Romero, J. (2012). beta-Amyloid exacerbates inflammation in astrocytes lacking fatty acid amide hydrolase through a mechanism involving PPAR-alpha, PPAR-gamma and TRPV1, but not CB(1) or CB(2) receptors. Br J Pharmacol, 166(4), 1474-1489. https://doi.org/10.1111/j.1476-5381.2012.01889.x

Bashashati, M., Storr, M. A., Nikas, S. P., Wood, J. T., Godlewski, G., Liu, J., Ho, W., Keenan, C. M., Zhang, H., Alapafuja, S. O., Cravatt, B. F., Lutz, B., Mackie, K., Kunos, G., Patel, K. D., Makriyannis, A., Davison, J. S., & Sharkey, K. A. (2012). Inhibiting fatty acid amide hydrolase normalizes endotoxin-induced enhanced gastrointestinal motility in mice. Br J Pharmacol, 165(5), 1556-1571. https://doi.org/10.1111/j.1476-5381.2011.01644.x

Bachovchin, D. A., & Cravatt, B. F. (2012). The pharmacological landscape and therapeutic potential of serine hydrolases. Nat Rev Drug Discov, 11(1), 52-68. https://doi.org/10.1038/nrd3620

Adibekian, A., Martin, B. R., Chang, J. W., Hsu, K. L., Tsuboi, K., Bachovchin, D. A., Speers, A. E., Brown, S. J., Spicer, T., Fernandez-Vega, V., Ferguson, J., Hodder, P. S., Rosen, H., & Cravatt, B. F. (2012). Confirming target engagement for reversible inhibitors in vivo by kinetically tuned activity-based probes. J Am Chem Soc, 134(25), 10345-10348. https://doi.org/10.1021/ja303400u

2011:

Zhong, P., Pan, B., Gao, X. P., Blankman, J. L., Cravatt, B. F., & Liu, Q. S. (2011). Genetic deletion of monoacylglycerol lipase alters endocannabinoid-mediated retrograde synaptic depression in the cerebellum. J Physiol, 589(Pt 20), 4847-4855. https://doi.org/10.1113/jphysiol.2011.215509

Tsuboi, K., Bachovchin, D. A., Speers, A. E., Spicer, T. P., Fernandez-Vega, V., Hodder, P., Rosen, H., & Cravatt, B. F. (2011). Potent and selective inhibitors of glutathione S-transferase omega 1 that impair cancer drug resistance. J Am Chem Soc, 133(41), 16605-16616. https://doi.org/10.1021/ja2066972

Straiker, A., Wager-Miller, J., Hu, S. S., Blankman, J. L., Cravatt, B. F., & Mackie, K. (2011). COX-2 and fatty acid amide hydrolase can regulate the time course of depolarization-induced suppression of excitation. Br J Pharmacol, 164(6), 1672-1683. https://doi.org/10.1111/j.1476-5381.2011.01486.x

Rowland, M. M., Bostic, H. E., Gong, D., Speers, A. E., Lucas, N., Cho, W., Cravatt, B. F., & Best, M. D. (2011). Phosphatidylinositol 3,4,5-trisphosphate activity probes for the labeling and proteomic characterization of protein binding partners. Biochemistry, 50(51), 11143-11161. https://doi.org/10.1021/bi201636s

Rossi, S., Furlan, R., De Chiara, V., Muzio, L., Musella, A., Motta, C., Studer, V., Cavasinni, F., Bernardi, G., Martino, G., Cravatt, B. F., Lutz, B., Maccarrone, M., & Centonze, D. (2011). Cannabinoid CB1 receptors regulate neuronal TNF-alpha effects in experimental autoimmune encephalomyelitis. Brain Behav Immun, 25(6), 1242-1248. https://doi.org/10.1016/j.bbi.2011.03.017

Ramesh, D., Ross, G. R., Schlosburg, J. E., Owens, R. A., Abdullah, R. A., Kinsey, S. G., Long, J. Z., Nomura, D. K., Sim-Selley, L. J., Cravatt, B. F., Akbarali, H. I., & Lichtman, A. H. (2011). Blockade of endocannabinoid hydrolytic enzymes attenuates precipitated opioid withdrawal symptoms in mice. J Pharmacol Exp Ther, 339(1), 173-185. https://doi.org/10.1124/jpet.111.181370

Pan, B., Wang, W., Zhong, P., Blankman, J. L., Cravatt, B. F., & Liu, Q. S. (2011). Alterations of endocannabinoid signaling, synaptic plasticity, learning, and memory in monoacylglycerol lipase knock-out mice. J Neurosci, 31(38), 13420-13430. https://doi.org/10.1523/JNEUROSCI.2075-11.2011

Nomura, D. K., Morrison, B. E., Blankman, J. L., Long, J. Z., Kinsey, S. G., Marcondes, M. C., Ward, A. M., Hahn, Y. K., Lichtman, A. H., Conti, B., & Cravatt, B. F. (2011). Endocannabinoid hydrolysis generates brain prostaglandins that promote neuroinflammation. Science, 334(6057), 809-813. https://doi.org/10.1126/science.1209200

Nomura, D. K., Lombardi, D. P., Chang, J. W., Niessen, S., Ward, A. M., Long, J. Z., Hoover, H. H., & Cravatt, B. F. (2011). Monoacylglycerol lipase exerts dual control over endocannabinoid and fatty acid pathways to support prostate cancer. Chem Biol, 18(7), 846-856. https://doi.org/10.1016/j.chembiol.2011.05.009

Nicolaou, K. C., Sanchini, S., Sarlah, D., Lu, G., Wu, T. R., Nomura, D. K., Cravatt, B. F., Cubitt, B., de la Torre, J. C., Hessell, A. J., & Burton, D. R. (2011). Design, synthesis, and biological evaluation of a biyouyanagin compound library. Proc Natl Acad Sci U S A, 108(17), 6715-6720. https://doi.org/10.1073/pnas.1015258108

Mukhopadhyay, P., Horvath, B., Rajesh, M., Matsumoto, S., Saito, K., Batkai, S., Patel, V., Tanchian, G., Gao, R. Y., Cravatt, B. F., Hasko, G., & Pacher, P. (2011). Fatty acid amide hydrolase is a key regulator of endocannabinoid-induced myocardial tissue injury. Free Radic Biol Med, 50(1), 179-195. https://doi.org/10.1016/j.freeradbiomed.2010.11.002

Mukhopadhyay, B., Cinar, R., Yin, S., Liu, J., Tam, J., Godlewski, G., Harvey-White, J., Mordi, I., Cravatt, B. F., Lotersztajn, S., Gao, B., Yuan, Q., Schuebel, K., Goldman, D., & Kunos, G. (2011). Hyperactivation of anandamide synthesis and regulation of cell-cycle progression via cannabinoid type 1 (CB1) receptors in the regenerating liver. Proc Natl Acad Sci U S A, 108(15), 6323-6328. https://doi.org/10.1073/pnas.1017689108

Mileni, M., Garfunkle, J., Ezzili, C., Cravatt, B. F., Stevens, R. C., & Boger, D. L. (2011). Fluoride-mediated capture of a noncovalent bound state of a reversible covalent enzyme inhibitor: X-ray crystallographic analysis of an exceptionally potent alpha-ketoheterocycle inhibitor of fatty acid amide hydrolase. J Am Chem Soc, 133(11), 4092-4100. https://doi.org/10.1021/ja110877y

Meier, J. L., Patel, A. D., Niessen, S., Meehan, M., Kersten, R., Yang, J. Y., Rothmann, M., Cravatt, B. F., Dorrestein, P. C., Burkart, M. D., & Bafna, V. (2011). Practical 4'-phosphopantetheine active site discovery from proteomic samples. J Proteome Res, 10(1), 320-329. https://doi.org/10.1021/pr100953b

Martin, B. R., Wang, C., Adibekian, A., Tully, S. E., & Cravatt, B. F. (2011). Global profiling of dynamic protein palmitoylation. Nat Methods, 9(1), 84-89. https://doi.org/10.1038/nmeth.1769

Long, J. Z., LaCava, M., Jin, X., & Cravatt, B. F. (2011). An anatomical and temporal portrait of physiological substrates for fatty acid amide hydrolase. J Lipid Res, 52(2), 337-344. https://doi.org/10.1194/jlr.M012153

Long, J. Z., & Cravatt, B. F. (2011). The metabolic serine hydrolases and their functions in mammalian physiology and disease. Chem Rev, 111(10), 6022-6063. https://doi.org/10.1021/cr200075y

Long, J. Z., Cisar, J. S., Milliken, D., Niessen, S., Wang, C., Trauger, S. A., Siuzdak, G., & Cravatt, B. F. (2011). Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids. Nature Chemical Biology, 7(11), 763-765. https://doi.org/10.1038/nchembio.659

Lone, A. M., Bachovchin, D. A., Westwood, D. B., Speers, A. E., Spicer, T. P., Fernandez-Vega, V., Chase, P., Hodder, P. S., Rosen, H., Cravatt, B. F., & Saghatelian, A. (2011). A substrate-free activity-based protein profiling screen for the discovery of selective PREPL inhibitors. J Am Chem Soc, 133(30), 11665-11674. https://doi.org/10.1021/ja2036095

Kinsey, S. G., O'Neal, S. T., Long, J. Z., Cravatt, B. F., & Lichtman, A. H. (2011). Inhibition of endocannabinoid catabolic enzymes elicits anxiolytic-like effects in the marble burying assay. Pharmacol Biochem Behav, 98(1), 21-27. https://doi.org/10.1016/j.pbb.2010.12.002

Kinsey, S. G., Nomura, D. K., O'Neal, S. T., Long, J. Z., Mahadevan, A., Cravatt, B. F., Grider, J. R., & Lichtman, A. H. (2011). Inhibition of monoacylglycerol lipase attenuates nonsteroidal anti-inflammatory drug-induced gastric hemorrhages in mice. J Pharmacol Exp Ther, 338(3), 795-802. https://doi.org/10.1124/jpet.110.175778

Kinsey, S. G., Naidu, P. S., Cravatt, B. F., Dudley, D. T., & Lichtman, A. H. (2011). Fatty acid amide hydrolase blockade attenuates the development of collagen-induced arthritis and related thermal hyperalgesia in mice. Pharmacol Biochem Behav, 99(4), 718-725. https://doi.org/10.1016/j.pbb.2011.06.022

Johnson, D. S., Stiff, C., Lazerwith, S. E., Kesten, S. R., Fay, L. K., Morris, M., Beidler, D., Liimatta, M. B., Smith, S. E., Dudley, D. T., Sadagopan, N., Bhattachar, S. N., Kesten, S. J., Nomanbhoy, T. K., Cravatt, B. F., & Ahn, K. (2011). Discovery of PF-04457845: A Highly Potent, Orally Bioavailable, and Selective Urea FAAH Inhibitor. ACS Med Chem Lett, 2(2), 91-96. https://doi.org/10.1021/ml100190t

Jaquish, D. V., Yu, P. T., Shields, D. J., French, R. P., Maruyama, K. P., Niessen, S., Hoover, H., D, A. C., Cravatt, B., & Lowy, A. M. (2011). IGF1-R signals through the RON receptor to mediate pancreatic cancer cell migration. Carcinogenesis, 32(8), 1151-1156. https://doi.org/10.1093/carcin/bgr086

Hall, C. I., Reese, M. L., Weerapana, E., Child, M. A., Bowyer, P. W., Albrow, V. E., Haraldsen, J. D., Phillips, M. R., Sandoval, E. D., Ward, G. E., Cravatt, B. F., Boothroyd, J. C., & Bogyo, M. (2011). Chemical genetic screen identifies Toxoplasma DJ-1 as a regulator of parasite secretion, attachment, and invasion. Proc Natl Acad Sci U S A, 108(26), 10568-10573. https://doi.org/10.1073/pnas.1105622108

Ezzili, C., Mileni, M., McGlinchey, N., Long, J. Z., Kinsey, S. G., Hochstatter, D. G., Stevens, R. C., Lichtman, A. H., Cravatt, B. F., Bilsky, E. J., & Boger, D. L. (2011). Reversible competitive alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase containing additional conformational constraints in the acyl side chain: orally active, long-acting analgesics. J Med Chem, 54(8), 2805-2822. https://doi.org/10.1021/jm101597x

Chang, J. W., Nomura, D. K., & Cravatt, B. F. (2011). A potent and selective inhibitor of KIAA1363/AADACL1 that impairs prostate cancer pathogenesis. Chem Biol, 18(4), 476-484. https://doi.org/10.1016/j.chembiol.2011.02.008

Bowyer, P. W., Simon, G. M., Cravatt, B. F., & Bogyo, M. (2011). Global profiling of proteolysis during rupture of Plasmodium falciparum from the host erythrocyte. Mol Cell Proteomics, 10(5), M110 001636. https://doi.org/10.1074/mcp.M110.001636

Bachovchin, D. A., Zuhl, A. M., Speers, A. E., Wolfe, M. R., Weerapana, E., Brown, S. J., Rosen, H., & Cravatt, B. F. (2011). Discovery and optimization of sulfonyl acrylonitriles as selective, covalent inhibitors of protein phosphatase methylesterase-1. J Med Chem, 54(14), 5229-5236. https://doi.org/10.1021/jm200502u

Bachovchin, D. A., Mohr, J. T., Speers, A. E., Wang, C., Berlin, J. M., Spicer, T. P., Fernandez-Vega, V., Chase, P., Hodder, P. S., Schurer, S. C., Nomura, D. K., Rosen, H., Fu, G. C., & Cravatt, B. F. (2011). Academic cross-fertilization by public screening yields a remarkable class of protein phosphatase methylesterase-1 inhibitors. Proc Natl Acad Sci U S A, 108(17), 6811-6816. https://doi.org/10.1073/pnas.1015248108

Ahn, K., Smith, S. E., Liimatta, M. B., Beidler, D., Sadagopan, N., Dudley, D. T., Young, T., Wren, P., Zhang, Y., Swaney, S., Van Becelaere, K., Blankman, J. L., Nomura, D. K., Bhattachar, S. N., Stiff, C., Nomanbhoy, T. K., Weerapana, E., Johnson, D. S., & Cravatt, B. F. (2011). Mechanistic and pharmacological characterization of PF-04457845: a highly potent and selective fatty acid amide hydrolase inhibitor that reduces inflammatory and noninflammatory pain. J Pharmacol Exp Ther, 338(1), 114-124. https://doi.org/10.1124/jpet.111.180257

Adibekian, A., Martin, B. R., Wang, C., Hsu, K. L., Bachovchin, D. A., Niessen, S., Hoover, H., & Cravatt, B. F. (2011). Click-generated triazole ureas as ultrapotent in vivo-active serine hydrolase inhibitors. Nature Chemical Biology, 7(7), 469-478. https://doi.org/10.1038/nchembio.579

2010:

2009:

Wright, A. T., Song, J. D., & Cravatt, B. F. (2009). A suite of activity-based probes for human cytochrome P450 enzymes. J Am Chem Soc, 131(30), 10692-10700. https://doi.org/10.1021/ja9037609

Sun, X., Wang, H., Okabe, M., Mackie, K., Kingsley, P. J., Marnett, L. J., Cravatt, B. F., & Dey, S. K. (2009). Genetic loss of Faah compromises male fertility in mice. Biol Reprod, 80(2), 235-242. https://doi.org/10.1095/biolreprod.108.072736

Straiker, A., Hu, S. S., Long, J. Z., Arnold, A., Wager-Miller, J., Cravatt, B. F., & Mackie, K. (2009). Monoacylglycerol lipase limits the duration of endocannabinoid-mediated depolarization-induced suppression of excitation in autaptic hippocampal neurons. Mol Pharmacol, 76(6), 1220-1227. https://doi.org/10.1124/mol.109.059030

Speers, A. E., & Cravatt, B. F. (2009). Activity-Based Protein Profiling (ABPP) and Click Chemistry (CC)-ABPP by MudPIT Mass Spectrometry. Curr Protoc Chem Biol, 1, 29-41. https://doi.org/10.1002/9780470559277.ch090138

Simon, G. M., Dix, M. M., & Cravatt, B. F. (2009). Comparative assessment of large-scale proteomic studies of apoptotic proteolysis. ACS Chem Biol, 4(6), 401-408. https://doi.org/10.1021/cb900082q

Schlosburg, J. E., Carlson, B. L., Ramesh, D., Abdullah, R. A., Long, J. Z., Cravatt, B. F., & Lichtman, A. H. (2009). Inhibitors of endocannabinoid-metabolizing enzymes reduce precipitated withdrawal responses in THC-dependent mice. Aaps j, 11(2), 342-352. https://doi.org/10.1208/s12248-009-9110-7

Schlosburg, J. E., Boger, D. L., Cravatt, B. F., & Lichtman, A. H. (2009). Endocannabinoid modulation of scratching response in an acute allergenic model: a new prospective neural therapeutic target for pruritus. J Pharmacol Exp Ther, 329(1), 314-323. https://doi.org/10.1124/jpet.108.150136

Sabido, E., Tarrago, T., Niessen, S., Cravatt, B. F., & Giralt, E. (2009). Activity-based probes for monitoring postproline protease activity. Chembiochem, 10(14), 2361-2366. https://doi.org/10.1002/cbic.200900244

Pan, B., Wang, W., Long, J. Z., Sun, D., Hillard, C. J., Cravatt, B. F., & Liu, Q. S. (2009). Blockade of 2-arachidonoylglycerol hydrolysis by selective monoacylglycerol lipase inhibitor 4-nitrophenyl 4-(dibenzo[d][1,3]dioxol-5-yl(hydroxy)methyl)piperidine-1-carboxylate (JZL184) Enhances retrograde endocannabinoid signaling. J Pharmacol Exp Ther, 331(2), 591-597. https://doi.org/10.1124/jpet.109.158162

Nakai, R., Salisbury, C. M., Rosen, H., & Cravatt, B. F. (2009). Ranking the selectivity of PubChem screening hits by activity-based protein profiling: MMP13 as a case study. Bioorg Med Chem, 17(3), 1101-1108. https://doi.org/10.1016/j.bmc.2008.03.018

Naidu, P. S., Booker, L., Cravatt, B. F., & Lichtman, A. H. (2009). Synergy between enzyme inhibitors of fatty acid amide hydrolase and cyclooxygenase in visceral nociception. J Pharmacol Exp Ther, 329(1), 48-56. https://doi.org/10.1124/jpet.108.143487

Mileni, M., Garfunkle, J., DeMartino, J. K., Cravatt, B. F., Boger, D. L., & Stevens, R. C. (2009). Binding and inactivation mechanism of a humanized fatty acid amide hydrolase by alpha-ketoheterocycle inhibitors revealed from cocrystal structures. J Am Chem Soc, 131(30), 10497-10506. https://doi.org/10.1021/ja902694n

Meier, J. L., Niessen, S., Hoover, H. S., Foley, T. L., Cravatt, B. F., & Burkart, M. D. (2009). An orthogonal active site identification system (OASIS) for proteomic profiling of natural product biosynthesis. ACS Chem Biol, 4(11), 948-957. https://doi.org/10.1021/cb9002128

Martin, B. R., & Cravatt, B. F. (2009). Large-scale profiling of protein palmitoylation in mammalian cells. Nat Methods, 6(2), 135-138. https://doi.org/10.1038/nmeth.1293

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., & Cravatt, B. F. (2009). Dual blockade of FAAH and MAGL identifies behavioral processes regulated by endocannabinoid crosstalk in vivo. Proc Natl Acad Sci U S A, 106(48), 20270-20275. https://doi.org/10.1073/pnas.0909411106

Long, J. Z., Nomura, D. K., & Cravatt, B. F. (2009). Characterization of monoacylglycerol lipase inhibition reveals differences in central and peripheral endocannabinoid metabolism. Chem Biol, 16(7), 744-753. https://doi.org/10.1016/j.chembiol.2009.05.009

Long, J. Z., Li, W., Booker, L., Burston, J. J., Kinsey, S. G., Schlosburg, J. E., Pavon, F. J., Serrano, A. M., Selley, D. E., Parsons, L. H., Lichtman, A. H., & Cravatt, B. F. (2009). Selective blockade of 2-arachidonoylglycerol hydrolysis produces cannabinoid behavioral effects. Nature Chemical Biology, 5(1), 37-44. https://doi.org/10.1038/nchembio.129

Lever, I. J., Robinson, M., Cibelli, M., Paule, C., Santha, P., Yee, L., Hunt, S. P., Cravatt, B. F., Elphick, M. R., Nagy, I., & Rice, A. S. (2009). Localization of the endocannabinoid-degrading enzyme fatty acid amide hydrolase in rat dorsal root ganglion cells and its regulation after peripheral nerve injury. J Neurosci, 29(12), 3766-3780. https://doi.org/10.1523/JNEUROSCI.4071-08.2009

Kinsey, S. G., Long, J. Z., O'Neal, S. T., Abdullah, R. A., Poklis, J. L., Boger, D. L., Cravatt, B. F., & Lichtman, A. H. (2009). Blockade of endocannabinoid-degrading enzymes attenuates neuropathic pain. J Pharmacol Exp Ther, 330(3), 902-910. https://doi.org/10.1124/jpet.109.155465

Kaschani, F., Gu, C., Niessen, S., Hoover, H., Cravatt, B. F., & van der Hoorn, R. A. (2009). Diversity of serine hydrolase activities of unchallenged and botrytis-infected Arabidopsis thaliana. Mol Cell Proteomics, 8(5), 1082-1093. https://doi.org/10.1074/mcp.M800494-MCP200

Johnson, D. S., Ahn, K., Kesten, S., Lazerwith, S. E., Song, Y., Morris, M., Fay, L., Gregory, T., Stiff, C., Dunbar, J. B., Jr., Liimatta, M., Beidler, D., Smith, S., Nomanbhoy, T. K., & Cravatt, B. F. (2009). Benzothiophene piperazine and piperidine urea inhibitors of fatty acid amide hydrolase (FAAH). Bioorg Med Chem Lett, 19(10), 2865-2869. https://doi.org/10.1016/j.bmcl.2009.03.080

Hu, S. S., Bradshaw, H. B., Benton, V. M., Chen, J. S., Huang, S. M., Minassi, A., Bisogno, T., Masuda, K., Tan, B., Roskoski, R., Jr., Cravatt, B. F., Di Marzo, V., & Walker, J. M. (2009). The biosynthesis of N-arachidonoyl dopamine (NADA), a putative endocannabinoid and endovanilloid, via conjugation of arachidonic acid with dopamine. Prostaglandins Leukot Essent Fatty Acids, 81(4), 291-301. https://doi.org/10.1016/j.plefa.2009.05.026

Bradshaw, H. B., Rimmerman, N., Hu, S. S., Benton, V. M., Stuart, J. M., Masuda, K., Cravatt, B. F., O'Dell, D. K., & Walker, J. M. (2009). The endocannabinoid anandamide is a precursor for the signaling lipid N-arachidonoyl glycine by two distinct pathways. BMC Biochem, 10, 14. https://doi.org/10.1186/1471-2091-10-14

Bachovchin, D. A., Brown, S. J., Rosen, H., & Cravatt, B. F. (2009). Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes. Nat Biotechnol, 27(4), 387-394. https://doi.org/10.1038/nbt.1531

Ahn, K., Johnson, D. S., Mileni, M., Beidler, D., Long, J. Z., McKinney, M. K., Weerapana, E., Sadagopan, N., Liimatta, M., Smith, S. E., Lazerwith, S., Stiff, C., Kamtekar, S., Bhattacharya, K., Zhang, Y., Swaney, S., Van Becelaere, K., Stevens, R. C., & Cravatt, B. F. (2009). Discovery and characterization of a highly selective FAAH inhibitor that reduces inflammatory pain. Chem Biol, 16(4), 411-420. https://doi.org/10.1016/j.chembiol.2009.02.013

Ahn, K., Johnson, D. S., & Cravatt, B. F. (2009). Fatty acid amide hydrolase as a potential therapeutic target for the treatment of pain and CNS disorders. Expert Opin Drug Discov, 4(7), 763-784. https://doi.org/10.1517/17460440903018857

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Wise, L. E., Cannavacciulo, R., Cravatt, B. F., Martin, B. F., & Lichtman, A. H. (2008). Evaluation of fatty acid amides in the carrageenan-induced paw edema model. Neuropharmacology, 54(1), 181-188. https://doi.org/10.1016/j.neuropharm.2007.06.003

Weerapana, E., Simon, G. M., & Cravatt, B. F. (2008). Disparate proteome reactivity profiles of carbon electrophiles. Nature Chemical Biology, 4(7), 405-407. https://doi.org/10.1038/nchembio.91

Wang, P., Shim, E., Cravatt, B., Jacobsen, R., Schoeniger, J., Kim, A. C., Paetzel, M., & Dalbey, R. E. (2008). Escherichia coli signal peptide peptidase A is a serine-lysine protease with a lysine recruited to the nonconserved amino-terminal domain in the S49 protease family. Biochemistry, 47(24), 6361-6369. https://doi.org/10.1021/bi800657p

Turman, M. V., Kingsley, P. J., Rouzer, C. A., Cravatt, B. F., & Marnett, L. J. (2008). Oxidative metabolism of a fatty acid amide hydrolase-regulated lipid, arachidonoyltaurine. Biochemistry, 47(12), 3917-3925. https://doi.org/10.1021/bi702530z

Suarez, J., Bermudez-Silva, F. J., Mackie, K., Ledent, C., Zimmer, A., Cravatt, B. F., & de Fonseca, F. R. (2008). Immunohistochemical description of the endogenous cannabinoid system in the rat cerebellum and functionally related nuclei. J Comp Neurol, 509(4), 400-421. https://doi.org/10.1002/cne.21774

Slaymaker, I. M., Bracey, M., Mileni, M., Garfunkle, J., Cravatt, B. F., Boger, D. L., & Stevens, R. C. (2008). Correlation of inhibitor effects on enzyme activity and thermal stability for the integral membrane protein fatty acid amide hydrolase. Bioorg Med Chem Lett, 18(22), 5847-5850. https://doi.org/10.1016/j.bmcl.2008.06.086

Simon, G. M., & Cravatt, B. F. (2008). Anandamide biosynthesis catalyzed by the phosphodiesterase GDE1 and detection of glycerophospho-N-acyl ethanolamine precursors in mouse brain. J Biol Chem, 283(14), 9341-9349. https://doi.org/10.1074/jbc.M707807200

Simon, G. M., & Cravatt, B. F. (2008). Challenges for the 'chemical-systems' biologist. Nature Chemical Biology, 4(11), 639-642. https://doi.org/10.1038/nchembio1108-639

Salisbury, C. M., & Cravatt, B. F. (2008). Optimization of activity-based probes for proteomic profiling of histone deacetylase complexes. J Am Chem Soc, 130(7), 2184-2194. https://doi.org/10.1021/ja074138u

Rimmerman, N., Bradshaw, H. B., Hughes, H. V., Chen, J. S., Hu, S. S., McHugh, D., Vefring, E., Jahnsen, J. A., Thompson, E. L., Masuda, K., Cravatt, B. F., Burstein, S., Vasko, M. R., Prieto, A. L., O'Dell, D. K., & Walker, J. M. (2008). N-palmitoyl glycine, a novel endogenous lipid that acts as a modulator of calcium influx and nitric oxide production in sensory neurons. Mol Pharmacol, 74(1), 213-224. https://doi.org/10.1124/mol.108.045997

Ortega-Gutierrez, S., Leung, D., Ficarro, S., Peters, E. C., & Cravatt, B. F. (2008). Targeted disruption of the PME-1 gene causes loss of demethylated PP2A and perinatal lethality in mice. PLoS One, 3(7), e2486. https://doi.org/10.1371/journal.pone.0002486

Nyilas, R., Dudok, B., Urban, G. M., Mackie, K., Watanabe, M., Cravatt, B. F., Freund, T. F., & Katona, I. (2008). Enzymatic machinery for endocannabinoid biosynthesis associated with calcium stores in glutamatergic axon terminals. J Neurosci, 28(5), 1058-1063. https://doi.org/10.1523/JNEUROSCI.5102-07.2008

Nomura, D. K., Fujioka, K., Issa, R. S., Ward, A. M., Cravatt, B. F., & Casida, J. E. (2008). Dual roles of brain serine hydrolase KIAA1363 in ether lipid metabolism and organophosphate detoxification. Toxicol Appl Pharmacol, 228(1), 42-48. https://doi.org/10.1016/j.taap.2007.11.021

Nomura, D. K., Blankman, J. L., Simon, G. M., Fujioka, K., Issa, R. S., Ward, A. M., Cravatt, B. F., & Casida, J. E. (2008). Activation of the endocannabinoid system by organophosphorus nerve agents. Nature Chemical Biology, 4(6), 373-378. https://doi.org/10.1038/nchembio.86

Mileni, M., Johnson, D. S., Wang, Z., Everdeen, D. S., Liimatta, M., Pabst, B., Bhattacharya, K., Nugent, R. A., Kamtekar, S., Cravatt, B. F., Ahn, K., & Stevens, R. C. (2008). Structure-guided inhibitor design for human FAAH by interspecies active site conversion. Proc Natl Acad Sci U S A, 105(35), 12820-12824. https://doi.org/10.1073/pnas.0806121105

Maccarrone, M., Rossi, S., Bari, M., De Chiara, V., Fezza, F., Musella, A., Gasperi, V., Prosperetti, C., Bernardi, G., Finazzi-Agro, A., Cravatt, B. F., & Centonze, D. (2008). Anandamide inhibits metabolism and physiological actions of 2-arachidonoylglycerol in the striatum. Nat Neurosci, 11(2), 152-159. https://doi.org/10.1038/nn2042

Hoover, H. S., Blankman, J. L., Niessen, S., & Cravatt, B. F. (2008). Selectivity of inhibitors of endocannabinoid biosynthesis evaluated by activity-based protein profiling. Bioorg Med Chem Lett, 18(22), 5838-5841. https://doi.org/10.1016/j.bmcl.2008.06.091

Hegde, V. L., Hegde, S., Cravatt, B. F., Hofseth, L. J., Nagarkatti, M., & Nagarkatti, P. S. (2008). Attenuation of experimental autoimmune hepatitis by exogenous and endogenous cannabinoids: involvement of regulatory T cells. Mol Pharmacol, 74(1), 20-33. https://doi.org/10.1124/mol.108.047035

Gaultier, A., Arandjelovic, S., Niessen, S., Overton, C. D., Linton, M. F., Fazio, S., Campana, W. M., Cravatt, B. F., 3rd, & Gonias, S. L. (2008). Regulation of tumor necrosis factor receptor-1 and the IKK-NF-kappaB pathway by LDL receptor-related protein explains the antiinflammatory activity of this receptor. Blood, 111(11), 5316-5325. https://doi.org/10.1182/blood-2007-12-127613

Egertova, M., Simon, G. M., Cravatt, B. F., & Elphick, M. R. (2008). Localization of N-acyl phosphatidylethanolamine phospholipase D (NAPE-PLD) expression in mouse brain: A new perspective on N-acylethanolamines as neural signaling molecules. J Comp Neurol, 506(4), 604-615. https://doi.org/10.1002/cne.21568

Dix, M. M., Simon, G. M., & Cravatt, B. F. (2008). Global mapping of the topography and magnitude of proteolytic events in apoptosis. Cell, 134(4), 679-691. https://doi.org/10.1016/j.cell.2008.06.038

DeMartino, J. K., Garfunkle, J., Hochstatter, D. G., Cravatt, B. F., & Boger, D. L. (2008). Exploration of a fundamental substituent effect of alpha-ketoheterocycle enzyme inhibitors: Potent and selective inhibitors of fatty acid amide hydrolase. Bioorg Med Chem Lett, 18(22), 5842-5846. https://doi.org/10.1016/j.bmcl.2008.06.084

Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008). Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. Annu Rev Biochem, 77, 383-414. https://doi.org/10.1146/annurev.biochem.75.101304.124125

Cravatt, B. F. (2008). Tetrahedron young investigator award 2008. Bioorg Med Chem Lett, 18(22), 5837. https://doi.org/10.1016/j.bmcl.2008.10.059

Conn, E. M., Madsen, M. A., Cravatt, B. F., Ruf, W., Deryugina, E. I., & Quigley, J. P. (2008). Cell surface proteomics identifies molecules functionally linked to tumor cell intravasation. J Biol Chem, 283(39), 26518-26527. https://doi.org/10.1074/jbc.M803337200

Barglow, K. T., Saikatendu, K. S., Bracey, M. H., Huey, R., Morris, G. M., Olson, A. J., Stevens, R. C., & Cravatt, B. F. (2008). Functional proteomic and structural insights into molecular recognition in the nitrilase family enzymes. Biochemistry, 47(51), 13514-13523. https://doi.org/10.1021/bi801786y

Ahn, K., McKinney, M. K., & Cravatt, B. F. (2008). Enzymatic pathways that regulate endocannabinoid signaling in the nervous system. Chem Rev, 108(5), 1687-1707. https://doi.org/10.1021/cr0782067

2007:

Wright, A. T., & Cravatt, B. F. (2007). Chemical proteomic probes for profiling cytochrome p450 activities and drug interactions in vivo. Chem Biol, 14(9), 1043-1051. https://doi.org/10.1016/j.chembiol.2007.08.008

Wise, L. E., Shelton, C. C., Cravatt, B. F., Martin, B. R., & Lichtman, A. H. (2007). Assessment of anandamide's pharmacological effects in mice deficient of both fatty acid amide hydrolase and cannabinoid CB1 receptors. Eur J Pharmacol, 557(1), 44-48. https://doi.org/10.1016/j.ejphar.2006.11.002

Weerapana, E., Speers, A. E., & Cravatt, B. F. (2007). Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP)--a general method for mapping sites of probe modification in proteomes. Nat Protoc, 2(6), 1414-1425. https://doi.org/10.1038/nprot.2007.194

Wang, H., Xie, H., Sun, X., Kingsley, P. J., Marnett, L. J., Cravatt, B. F., & Dey, S. K. (2007). Differential regulation of endocannabinoid synthesis and degradation in the uterus during embryo implantation. Prostaglandins Other Lipid Mediat, 83(1-2), 62-74. https://doi.org/10.1016/j.prostaglandins.2006.09.009

Wan, Y., Saghatelian, A., Chong, L. W., Zhang, C. L., Cravatt, B. F., & Evans, R. M. (2007). Maternal PPAR gamma protects nursing neonates by suppressing the production of inflammatory milk. Genes Dev, 21(15), 1895-1908. https://doi.org/10.1101/gad.1567207

Vila, A., Rosengarth, A., Piomelli, D., Cravatt, B., & Marnett, L. J. (2007). Hydrolysis of prostaglandin glycerol esters by the endocannabinoid-hydrolyzing enzymes, monoacylglycerol lipase and fatty acid amide hydrolase. Biochemistry, 46(33), 9578-9585. https://doi.org/10.1021/bi7005898

Varvel, S. A., Wise, L. E., Niyuhire, F., Cravatt, B. F., & Lichtman, A. H. (2007). Inhibition of fatty-acid amide hydrolase accelerates acquisition and extinction rates in a spatial memory task. Neuropsychopharmacology, 32(5), 1032-1041. https://doi.org/10.1038/sj.npp.1301224

Salisbury, C. M., & Cravatt, B. F. (2007). Activity-based probes for proteomic profiling of histone deacetylase complexes. Proc Natl Acad Sci U S A, 104(4), 1171-1176. https://doi.org/10.1073/pnas.0608659104

Romero, F. A., Du, W., Hwang, I., Rayl, T. J., Kimball, F. S., Leung, D., Hoover, H. S., Apodaca, R. L., Breitenbucher, J. G., Cravatt, B. F., & Boger, D. L. (2007). Potent and selective alpha-ketoheterocycle-based inhibitors of the anandamide and oleamide catabolizing enzyme, fatty acid amide hydrolase. J Med Chem, 50(5), 1058-1068. https://doi.org/10.1021/jm0611509

Naidu, P. S., Varvel, S. A., Ahn, K., Cravatt, B. F., Martin, B. R., & Lichtman, A. H. (2007). Evaluation of fatty acid amide hydrolase inhibition in murine models of emotionality. Psychopharmacology (Berl), 192(1), 61-70. https://doi.org/10.1007/s00213-006-0689-4

Mei, G., Di Venere, A., Gasperi, V., Nicolai, E., Masuda, K. R., Finazzi-Agro, A., Cravatt, B. F., & Maccarrone, M. (2007). Closing the gate to the active site: effect of the inhibitor methoxyarachidonyl fluorophosphonate on the conformation and membrane binding of fatty acid amide hydrolase. J Biol Chem, 282(6), 3829-3836. https://doi.org/10.1074/jbc.M605653200

Macpherson, L. J., Xiao, B., Kwan, K. Y., Petrus, M. J., Dubin, A. E., Hwang, S., Cravatt, B., Corey, D. P., & Patapoutian, A. (2007). An ion channel essential for sensing chemical damage. J Neurosci, 27(42), 11412-11415. https://doi.org/10.1523/JNEUROSCI.3600-07.2007

Macpherson, L. J., Dubin, A. E., Evans, M. J., Marr, F., Schultz, P. G., Cravatt, B. F., & Patapoutian, A. (2007). Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines. Nature, 445(7127), 541-545. https://doi.org/10.1038/nature05544

List, K., Currie, B., Scharschmidt, T. C., Szabo, R., Shireman, J., Molinolo, A., Cravatt, B. F., Segre, J., & Bugge, T. H. (2007). Autosomal ichthyosis with hypotrichosis syndrome displays low matriptase proteolytic activity and is phenocopied in ST14 hypomorphic mice. J Biol Chem, 282(50), 36714-36723. https://doi.org/10.1074/jbc.M705521200

Li, W., Blankman, J. L., & Cravatt, B. F. (2007). A functional proteomic strategy to discover inhibitors for uncharacterized hydrolases. J Am Chem Soc, 129(31), 9594-9595. https://doi.org/10.1021/ja073650c

Karsak, M., Gaffal, E., Date, R., Wang-Eckhardt, L., Rehnelt, J., Petrosino, S., Starowicz, K., Steuder, R., Schlicker, E., Cravatt, B., Mechoulam, R., Buettner, R., Werner, S., Di Marzo, V., Tuting, T., & Zimmer, A. (2007). Attenuation of allergic contact dermatitis through the endocannabinoid system. Science, 316(5830), 1494-1497. https://doi.org/10.1126/science.1142265

Hardouin, C., Kelso, M. J., Romero, F. A., Rayl, T. J., Leung, D., Hwang, I., Cravatt, B. F., & Boger, D. L. (2007). Structure-activity relationships of alpha-ketooxazole inhibitors of fatty acid amide hydrolase. J Med Chem, 50(14), 3359-3368. https://doi.org/10.1021/jm061414r

Hanson, S. R., Hsu, T. L., Weerapana, E., Kishikawa, K., Simon, G. M., Cravatt, B. F., & Wong, C. H. (2007). Tailored glycoproteomics and glycan site mapping using saccharide-selective bioorthogonal probes. J Am Chem Soc, 129(23), 7266-7267. https://doi.org/10.1021/ja0724083

Fu, J., Astarita, G., Gaetani, S., Kim, J., Cravatt, B. F., Mackie, K., & Piomelli, D. (2007). Food intake regulates oleoylethanolamide formation and degradation in the proximal small intestine. J Biol Chem, 282(2), 1518-1528. https://doi.org/10.1074/jbc.M607809200

Everley, P. A., Gartner, C. A., Haas, W., Saghatelian, A., Elias, J. E., Cravatt, B. F., Zetter, B. R., & Gygi, S. P. (2007). Assessing enzyme activities using stable isotope labeling and mass spectrometry. Mol Cell Proteomics, 6(10), 1771-1777. https://doi.org/10.1074/mcp.M700057-MCP200

Evans, M. J., Morris, G. M., Wu, J., Olson, A. J., Sorensen, E. J., & Cravatt, B. F. (2007). Mechanistic and structural requirements for active site labeling of phosphoglycerate mutase by spiroepoxides. Mol Biosyst, 3(7), 495-506. https://doi.org/10.1039/b705113a

Cravatt, B. F., Simon, G. M., & Yates, J. R., 3rd. (2007). The biological impact of mass-spectrometry-based proteomics. Nature, 450(7172), 991-1000. https://doi.org/10.1038/nature06525

Chamero, P., Marton, T. F., Logan, D. W., Flanagan, K., Cruz, J. R., Saghatelian, A., Cravatt, B. F., & Stowers, L. (2007). Identification of protein pheromones that promote aggressive behaviour. Nature, 450(7171), 899-902. https://doi.org/10.1038/nature05997

Carlson, E. E., & Cravatt, B. F. (2007). Chemoselective probes for metabolite enrichment and profiling. Nat Methods, 4(5), 429-435. https://doi.org/10.1038/nmeth1038

Carlson, E. E., & Cravatt, B. F. (2007). Enrichment tags for enhanced-resolution profiling of the polar metabolome. J Am Chem Soc, 129(51), 15780-15782. https://doi.org/10.1021/ja0779506

Blednov, Y. A., Cravatt, B. F., Boehm, S. L., 2nd, Walker, D., & Harris, R. A. (2007). Role of endocannabinoids in alcohol consumption and intoxication: studies of mice lacking fatty acid amide hydrolase. Neuropsychopharmacology, 32(7), 1570-1582. https://doi.org/10.1038/sj.npp.1301274

Blankman, J. L., Simon, G. M., & Cravatt, B. F. (2007). A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol. Chem Biol, 14(12), 1347-1356. https://doi.org/10.1016/j.chembiol.2007.11.006

Batkai, S., Rajesh, M., Mukhopadhyay, P., Hasko, G., Liaudet, L., Cravatt, B. F., Csiszar, A., Ungvari, Z., & Pacher, P. (2007). Decreased age-related cardiac dysfunction, myocardial nitrative stress, inflammatory gene expression, and apoptosis in mice lacking fatty acid amide hydrolase. Am J Physiol Heart Circ Physiol, 293(2), H909-918. https://doi.org/10.1152/ajpheart.00373.2007

Barglow, K. T., & Cravatt, B. F. (2007). Activity-based protein profiling for the functional annotation of enzymes. Nat Methods, 4(10), 822-827. https://doi.org/10.1038/nmeth1092

Ahn, K., Johnson, D. S., Fitzgerald, L. R., Liimatta, M., Arendse, A., Stevenson, T., Lund, E. T., Nugent, R. A., Nomanbhoy, T. K., Alexander, J. P., & Cravatt, B. F. (2007). Novel mechanistic class of fatty acid amide hydrolase inhibitors with remarkable selectivity. Biochemistry, 46(45), 13019-13030. https://doi.org/10.1021/bi701378g

2006:

Wei, B. Q., Mikkelsen, T. S., McKinney, M. K., Lander, E. S., & Cravatt, B. F. (2006). A second fatty acid amide hydrolase with variable distribution among placental mammals. J Biol Chem, 281(48), 36569-36578. https://doi.org/10.1074/jbc.M606646200

Wang, H., Xie, H., Guo, Y., Zhang, H., Takahashi, T., Kingsley, P. J., Marnett, L. J., Das, S. K., Cravatt, B. F., & Dey, S. K. (2006). Fatty acid amide hydrolase deficiency limits early pregnancy events. J Clin Invest, 116(8), 2122-2131. https://doi.org/10.1172/JCI28621

Varvel, S. A., Cravatt, B. F., Engram, A. E., & Lichtman, A. H. (2006). Fatty acid amide hydrolase (-/-) mice exhibit an increased sensitivity to the disruptive effects of anandamide or oleamide in a working memory water maze task. J Pharmacol Exp Ther, 317(1), 251-257. https://doi.org/10.1124/jpet.105.095059

Simon, G. M., & Cravatt, B. F. (2006). Endocannabinoid biosynthesis proceeding through glycerophospho-N-acyl ethanolamine and a role for alpha/beta-hydrolase 4 in this pathway. J Biol Chem, 281(36), 26465-26472. https://doi.org/10.1074/jbc.M604660200

Siegmund, S. V., Seki, E., Osawa, Y., Uchinami, H., Cravatt, B. F., & Schwabe, R. F. (2006). Fatty acid amide hydrolase determines anandamide-induced cell death in the liver. J Biol Chem, 281(15), 10431-10438. https://doi.org/10.1074/jbc.M509706200

Sieber, S. A., Niessen, S., Hoover, H. S., & Cravatt, B. F. (2006). Proteomic profiling of metalloprotease activities with cocktails of active-site probes. Nature Chemical Biology, 2(5), 274-281. https://doi.org/10.1038/nchembio781

Sieber, S. A., & Cravatt, B. F. (2006). Analytical platforms for activity-based protein profiling--exploiting the versatility of chemistry for functional proteomics. Chem Commun (Camb)(22), 2311-2319. https://doi.org/10.1039/b600653c

Saghatelian, A., McKinney, M. K., Bandell, M., Patapoutian, A., & Cravatt, B. F. (2006). A FAAH-regulated class of N-acyl taurines that activates TRP ion channels. Biochemistry, 45(30), 9007-9015. https://doi.org/10.1021/bi0608008

Safo, P. K., Cravatt, B. F., & Regehr, W. G. (2006). Retrograde endocannabinoid signaling in the cerebellar cortex. Cerebellum, 5(2), 134-145. https://doi.org/10.1080/14734220600791477

Nomura, D. K., Durkin, K. A., Chiang, K. P., Quistad, G. B., Cravatt, B. F., & Casida, J. E. (2006). Serine hydrolase KIAA1363: toxicological and structural features with emphasis on organophosphate interactions. Chem Res Toxicol, 19(9), 1142-1150. https://doi.org/10.1021/tx060117m

Mulder, A. M., & Cravatt, B. F. (2006). Endocannabinoid metabolism in the absence of fatty acid amide hydrolase (FAAH): discovery of phosphorylcholine derivatives of N-acyl ethanolamines. Biochemistry, 45(38), 11267-11277. https://doi.org/10.1021/bi061122s

Milner, J. M., Kevorkian, L., Young, D. A., Jones, D., Wait, R., Donell, S. T., Barksby, E., Patterson, A. M., Middleton, J., Cravatt, B. F., Clark, I. M., Rowan, A. D., & Cawston, T. E. (2006). Fibroblast activation protein alpha is expressed by chondrocytes following a pro-inflammatory stimulus and is elevated in osteoarthritis. Arthritis Res Ther, 8(1), R23. https://doi.org/10.1186/ar1877

McKinney, M. K., & Cravatt, B. F. (2006). Structure-based design of a FAAH variant that discriminates between the N-acyl ethanolamine and taurine families of signaling lipids. Biochemistry, 45(30), 9016-9022. https://doi.org/10.1021/bi0608010

Madsen, M. A., Deryugina, E. I., Niessen, S., Cravatt, B. F., & Quigley, J. P. (2006). Activity-based protein profiling implicates urokinase activation as a key step in human fibrosarcoma intravasation. J Biol Chem, 281(23), 15997-16005. https://doi.org/10.1074/jbc.M601223200

Leung, D., Saghatelian, A., Simon, G. M., & Cravatt, B. F. (2006). Inactivation of N-acyl phosphatidylethanolamine phospholipase D reveals multiple mechanisms for the biosynthesis of endocannabinoids. Biochemistry, 45(15), 4720-4726. https://doi.org/10.1021/bi060163l

Evans, M. J., & Cravatt, B. F. (2006). Mechanism-based profiling of enzyme families. Chem Rev, 106(8), 3279-3301. https://doi.org/10.1021/cr050288g

Chiang, K. P., Niessen, S., Saghatelian, A., & Cravatt, B. F. (2006). An enzyme that regulates ether lipid signaling pathways in cancer annotated by multidimensional profiling. Chem Biol, 13(10), 1041-1050. https://doi.org/10.1016/j.chembiol.2006.08.008

Basavarajappa, B. S., Yalamanchili, R., Cravatt, B. F., Cooper, T. B., & Hungund, B. L. (2006). Increased ethanol consumption and preference and decreased ethanol sensitivity in female FAAH knockout mice. Neuropharmacology, 50(7), 834-844. https://doi.org/10.1016/j.neuropharm.2005.12.005

Barglow, K. T., & Cravatt, B. F. (2006). Substrate mimicry in an activity-based probe that targets the nitrilase family of enzymes. Angew Chem Int Ed Engl, 45(44), 7408-7411. https://doi.org/10.1002/anie.200603187

Balakrishnan, A., Patel, B., Sieber, S. A., Chen, D., Pachikara, N., Zhong, G., Cravatt, B. F., & Fan, H. (2006). Metalloprotease inhibitors GM6001 and TAPI-0 inhibit the obligate intracellular human pathogen Chlamydia trachomatis by targeting peptide deformylase of the bacterium. J Biol Chem, 281(24), 16691-16699. https://doi.org/10.1074/jbc.M513648200

Alexander, J. P., & Cravatt, B. F. (2006). The putative endocannabinoid transport blocker LY2183240 is a potent inhibitor of FAAH and several other brain serine hydrolases. J Am Chem Soc, 128(30), 9699-9704. https://doi.org/10.1021/ja062999h

Aguado, T., Palazuelos, J., Monory, K., Stella, N., Cravatt, B., Lutz, B., Marsicano, G., Kokaia, Z., Guzman, M., & Galve-Roperh, I. (2006). The endocannabinoid system promotes astroglial differentiation by acting on neural progenitor cells. J Neurosci, 26(5), 1551-1561. https://doi.org/10.1523/JNEUROSCI.3101-05.2006

2005:

Want, E. J., Cravatt, B. F., & Siuzdak, G. (2005). The expanding role of mass spectrometry in metabolite profiling and characterization. Chembiochem, 6(11), 1941-1951. https://doi.org/10.1002/cbic.200500151

Speers, A. E., & Cravatt, B. F. (2005). A tandem orthogonal proteolysis strategy for high-content chemical proteomics. J Am Chem Soc, 127(28), 10018-10019. https://doi.org/10.1021/ja0532842

Saghatelian, A., & Cravatt, B. F. (2005). Global strategies to integrate the proteome and metabolome. Curr Opin Chem Biol, 9(1), 62-68. https://doi.org/10.1016/j.cbpa.2004.12.004

Saghatelian, A., & Cravatt, B. F. (2005). Discovery metabolite profiling--forging functional connections between the proteome and metabolome. Life Sci, 77(14), 1759-1766. https://doi.org/10.1016/j.lfs.2005.05.019

Saghatelian, A., & Cravatt, B. F. (2005). Assignment of protein function in the postgenomic era. Nature Chemical Biology, 1(3), 130-142. https://doi.org/10.1038/nchembio0805-130

Patel, S., Cravatt, B. F., & Hillard, C. J. (2005). Synergistic interactions between cannabinoids and environmental stress in the activation of the central amygdala. Neuropsychopharmacology, 30(3), 497-507. https://doi.org/10.1038/sj.npp.1300535

Patel, S., Carrier, E. J., Ho, W. S., Rademacher, D. J., Cunningham, S., Reddy, D. S., Falck, J. R., Cravatt, B. F., & Hillard, C. J. (2005). The postmortal accumulation of brain N-arachidonylethanolamine (anandamide) is dependent upon fatty acid amide hydrolase activity. J Lipid Res, 46(2), 342-349. https://doi.org/10.1194/jlr.M400377-JLR200

Pacher, P., Batkai, S., Osei-Hyiaman, D., Offertaler, L., Liu, J., Harvey-White, J., Brassai, A., Jarai, Z., Cravatt, B. F., & Kunos, G. (2005). Hemodynamic profile, responsiveness to anandamide, and baroreflex sensitivity of mice lacking fatty acid amide hydrolase. Am J Physiol Heart Circ Physiol, 289(2), H533-541. https://doi.org/10.1152/ajpheart.00107.2005

Osei-Hyiaman, D., Depetrillo, M., Harvey-White, J., Bannon, A. W., Cravatt, B. F., Kuhar, M. J., Mackie, K., Palkovits, M., & Kunos, G. (2005). Cocaine- and amphetamine-related transcript is involved in the orexigenic effect of endogenous anandamide. Neuroendocrinology, 81(4), 273-282. https://doi.org/10.1159/000087925

Nomura, D. K., Leung, D., Chiang, K. P., Quistad, G. B., Cravatt, B. F., & Casida, J. E. (2005). A brain detoxifying enzyme for organophosphorus nerve poisons. Proc Natl Acad Sci U S A, 102(17), 6195-6200. https://doi.org/10.1073/pnas.0501915102

McKinney, M. K., & Cravatt, B. F. (2005). Structure and function of fatty acid amide hydrolase. Annu Rev Biochem, 74, 411-432. https://doi.org/10.1146/annurev.biochem.74.082803.133450

Lichtman, A. H., & Cravatt, B. F. (2005). Food for thought: endocannabinoid modulation of lipogenesis. J Clin Invest, 115(5), 1130-1133. https://doi.org/10.1172/JCI25076

Leung, D., Du, W., Hardouin, C., Cheng, H., Hwang, I., Cravatt, B. F., & Boger, D. L. (2005). Discovery of an exceptionally potent and selective class of fatty acid amide hydrolase inhibitors enlisting proteome-wide selectivity screening: concurrent optimization of enzyme inhibitor potency and selectivity. Bioorg Med Chem Lett, 15(5), 1423-1428. https://doi.org/10.1016/j.bmcl.2004.12.085

Jessani, N., Young, J. A., Diaz, S. L., Patricelli, M. P., Varki, A., & Cravatt, B. F. (2005). Class assignment of sequence-unrelated members of enzyme superfamilies by activity-based protein profiling. Angew Chem Int Ed Engl, 44(16), 2400-2403. https://doi.org/10.1002/anie.200463098

Jessani, N., Niessen, S., Wei, B. Q., Nicolau, M., Humphrey, M., Ji, Y., Han, W., Noh, D. Y., Yates, J. R., 3rd, Jeffrey, S. S., & Cravatt, B. F. (2005). A streamlined platform for high-content functional proteomics of primary human specimens. Nat Methods, 2(9), 691-697. https://doi.org/10.1038/nmeth778

Jessani, N., Niessen, S., Mueller, B. M., & Cravatt, B. F. (2005). Breast cancer cell lines grown in vivo: what goes in isn't always the same as what comes out. Cell Cycle, 4(2), 253-255. https://www.ncbi.nlm.nih.gov/pubmed/15655359

Hogestatt, E. D., Jonsson, B. A., Ermund, A., Andersson, D. A., Bjork, H., Alexander, J. P., Cravatt, B. F., Basbaum, A. I., & Zygmunt, P. M. (2005). Conversion of acetaminophen to the bioactive N-acylphenolamine AM404 via fatty acid amide hydrolase-dependent arachidonic acid conjugation in the nervous system. J Biol Chem, 280(36), 31405-31412. https://doi.org/10.1074/jbc.M501489200

Go, E. P., Apon, J. V., Luo, G., Saghatelian, A., Daniels, R. H., Sahi, V., Dubrow, R., Cravatt, B. F., Vertes, A., & Siuzdak, G. (2005). Desorption/ionization on silicon nanowires. Anal Chem, 77(6), 1641-1646. https://doi.org/10.1021/ac048460o

Evans, M. J., Saghatelian, A., Sorensen, E. J., & Cravatt, B. F. (2005). Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling. Nat Biotechnol, 23(10), 1303-1307. https://doi.org/10.1038/nbt1149

Drahl, C., Cravatt, B. F., & Sorensen, E. J. (2005). Protein-reactive natural products. Angew Chem Int Ed Engl, 44(36), 5788-5809. https://doi.org/10.1002/anie.200500900

Cravatt, B. F. (2005). Kinase chemical genomics--a new rule for the exceptions. Nat Methods, 2(6), 411-412. https://doi.org/10.1038/nmeth0605-411

Cravatt, B. F. (2005). Live chemical reports from the cell surface. Chem Biol, 12(9), 954-956; discussion 999-1006. https://doi.org/10.1016/j.chembiol.2005.09.001

Boger, D. L., Miyauchi, H., Du, W., Hardouin, C., Fecik, R. A., Cheng, H., Hwang, I., Hedrick, M. P., Leung, D., Acevedo, O., Guimaraes, C. R., Jorgensen, W. L., & Cravatt, B. F. (2005). Discovery of a potent, selective, and efficacious class of reversible alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase effective as analgesics. J Med Chem, 48(6), 1849-1856. https://doi.org/10.1021/jm049614v

Alexander, J. P., & Cravatt, B. F. (2005). Mechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymes. Chem Biol, 12(11), 1179-1187. https://doi.org/10.1016/j.chembiol.2005.08.011

Aguado, T., Monory, K., Palazuelos, J., Stella, N., Cravatt, B., Lutz, B., Marsicano, G., Kokaia, Z., Guzman, M., & Galve-Roperh, I. (2005). The endocannabinoid system drives neural progenitor proliferation. Faseb j, 19(12), 1704-1706. https://doi.org/10.1096/fj.05-3995fje

2004:

Weber, A., Ni, J., Ling, K. H., Acheampong, A., Tang-Liu, D. D., Burk, R., Cravatt, B. F., & Woodward, D. (2004). Formation of prostamides from anandamide in FAAH knockout mice analyzed by HPLC with tandem mass spectrometry. J Lipid Res, 45(4), 757-763. https://doi.org/10.1194/jlr.M300475-JLR200

Speers, A. E., & Cravatt, B. F. (2004). Chemical strategies for activity-based proteomics. Chembiochem, 5(1), 41-47. https://doi.org/10.1002/cbic.200300721

Speers, A. E., & Cravatt, B. F. (2004). Profiling enzyme activities in vivo using click chemistry methods. Chem Biol, 11(4), 535-546. https://doi.org/10.1016/j.chembiol.2004.03.012

Sieber, S. A., Mondala, T. S., Head, S. R., & Cravatt, B. F. (2004). Microarray platform for profiling enzyme activities in complex proteomes. J Am Chem Soc, 126(48), 15640-15641. https://doi.org/10.1021/ja044286+

Saghatelian, A., Trauger, S. A., Want, E. J., Hawkins, E. G., Siuzdak, G., & Cravatt, B. F. (2004). Assignment of endogenous substrates to enzymes by global metabolite profiling. Biochemistry, 43(45), 14332-14339. https://doi.org/10.1021/bi0480335

Saghatelian, A., Jessani, N., Joseph, A., Humphrey, M., & Cravatt, B. F. (2004). Activity-based probes for the proteomic profiling of metalloproteases. Proc Natl Acad Sci U S A, 101(27), 10000-10005. https://doi.org/10.1073/pnas.0402784101

Ortega-Gutierrez, S., Hawkins, E. G., Viso, A., Lopez-Rodriguez, M. L., & Cravatt, B. F. (2004). Comparison of anandamide transport in FAAH wild-type and knockout neurons: evidence for contributions by both FAAH and the CB1 receptor to anandamide uptake. Biochemistry, 43(25), 8184-8190. https://doi.org/10.1021/bi049395f

Massa, F., Marsicano, G., Hermann, H., Cannich, A., Monory, K., Cravatt, B. F., Ferri, G. L., Sibaev, A., Storr, M., & Lutz, B. (2004). The endogenous cannabinoid system protects against colonic inflammation. J Clin Invest, 113(8), 1202-1209. https://doi.org/10.1172/JCI19465

Lichtman, A. H., Shelton, C. C., Advani, T., & Cravatt, B. F. (2004). Mice lacking fatty acid amide hydrolase exhibit a cannabinoid receptor-mediated phenotypic hypoalgesia. Pain, 109(3), 319-327. https://doi.org/10.1016/j.pain.2004.01.022

Lichtman, A. H., Leung, D., Shelton, C. C., Saghatelian, A., Hardouin, C., Boger, D. L., & Cravatt, B. F. (2004). Reversible inhibitors of fatty acid amide hydrolase that promote analgesia: evidence for an unprecedented combination of potency and selectivity. J Pharmacol Exp Ther, 311(2), 441-448. https://doi.org/10.1124/jpet.104.069401

Jessani, N., Humphrey, M., McDonald, W. H., Niessen, S., Masuda, K., Gangadharan, B., Yates, J. R., 3rd, Mueller, B. M., & Cravatt, B. F. (2004). Carcinoma and stromal enzyme activity profiles associated with breast tumor growth in vivo. Proc Natl Acad Sci U S A, 101(38), 13756-13761. https://doi.org/10.1073/pnas.0404727101

Jessani, N., & Cravatt, B. F. (2004). The development and application of methods for activity-based protein profiling. Curr Opin Chem Biol, 8(1), 54-59. https://doi.org/10.1016/j.cbpa.2003.11.004

Huitron-Resendiz, S., Sanchez-Alavez, M., Wills, D. N., Cravatt, B. F., & Henriksen, S. J. (2004). Characterization of the sleep-wake patterns in mice lacking fatty acid amide hydrolase. Sleep, 27(5), 857-865. https://doi.org/10.1093/sleep/27.5.857

Gulyas, A. I., Cravatt, B. F., Bracey, M. H., Dinh, T. P., Piomelli, D., Boscia, F., & Freund, T. F. (2004). Segregation of two endocannabinoid-hydrolyzing enzymes into pre- and postsynaptic compartments in the rat hippocampus, cerebellum and amygdala. Eur J Neurosci, 20(2), 441-458. https://doi.org/10.1111/j.1460-9568.2004.03428.x

Egertova, M., Michael, G. J., Cravatt, B. F., & Elphick, M. R. (2004). Fatty acid amide hydrolase in brain ventricular epithelium: mutually exclusive patterns of expression in mouse and rat. J Chem Neuroanat, 28(3), 171-181. https://doi.org/10.1016/j.jchemneu.2004.07.001

Cravatt, B. F., Saghatelian, A., Hawkins, E. G., Clement, A. B., Bracey, M. H., & Lichtman, A. H. (2004). Functional disassociation of the central and peripheral fatty acid amide signaling systems. Proc Natl Acad Sci U S A, 101(29), 10821-10826. https://doi.org/10.1073/pnas.0401292101

Cravatt, B. F., & Lichtman, A. H. (2004). The endogenous cannabinoid system and its role in nociceptive behavior. J Neurobiol, 61(1), 149-160. https://doi.org/10.1002/neu.20080

Chiang, K. P., Gerber, A. L., Sipe, J. C., & Cravatt, B. F. (2004). Reduced cellular expression and activity of the P129T mutant of human fatty acid amide hydrolase: evidence for a link between defects in the endocannabinoid system and problem drug use. Hum Mol Genet, 13(18), 2113-2119. https://doi.org/10.1093/hmg/ddh216

Bracey, M. H., Cravatt, B. F., & Stevens, R. C. (2004). Structural commonalities among integral membrane enzymes. FEBS Lett, 567(2-3), 159-165. https://doi.org/10.1016/j.febslet.2004.04.084

Barglow, K. T., & Cravatt, B. F. (2004). Discovering disease-associated enzymes by proteome reactivity profiling. Chem Biol, 11(11), 1523-1531. https://doi.org/10.1016/j.chembiol.2004.08.023

Azad, S. C., Monory, K., Marsicano, G., Cravatt, B. F., Lutz, B., Zieglgansberger, W., & Rammes, G. (2004). Circuitry for associative plasticity in the amygdala involves endocannabinoid signaling. J Neurosci, 24(44), 9953-9961. https://doi.org/10.1523/JNEUROSCI.2134-04.2004

Adam, G. C., Burbaum, J., Kozarich, J. W., Patricelli, M. P., & Cravatt, B. F. (2004). Mapping enzyme active sites in complex proteomes. J Am Chem Soc, 126(5), 1363-1368. https://doi.org/10.1021/ja038441g

2003:

Speers, A. E., Adam, G. C., & Cravatt, B. F. (2003). Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J Am Chem Soc, 125(16), 4686-4687. https://doi.org/10.1021/ja034490h

McKinney, M. K., & Cravatt, B. F. (2003). Evidence for distinct roles in catalysis for residues of the serine-serine-lysine catalytic triad of fatty acid amide hydrolase. J Biol Chem, 278(39), 37393-37399. https://doi.org/10.1074/jbc.M303922200

Liu, J., Batkai, S., Pacher, P., Harvey-White, J., Wagner, J. A., Cravatt, B. F., Gao, B., & Kunos, G. (2003). Lipopolysaccharide induces anandamide synthesis in macrophages via CD14/MAPK/phosphoinositide 3-kinase/NF-kappaB independently of platelet-activating factor. J Biol Chem, 278(45), 45034-45039. https://doi.org/10.1074/jbc.M306062200

Leung, D., Hardouin, C., Boger, D. L., & Cravatt, B. F. (2003). Discovering potent and selective reversible inhibitors of enzymes in complex proteomes. Nat Biotechnol, 21(6), 687-691. https://doi.org/10.1038/nbt826

Kustedjo, K., Deechongkit, S., Kelly, J. W., & Cravatt, B. F. (2003). Recombinant expression, purification, and comparative characterization of torsinA and its torsion dystonia-associated variant Delta E-torsinA. Biochemistry, 42(51), 15333-15341. https://doi.org/10.1021/bi0349569

Egertova, M., Cravatt, B. F., & Elphick, M. R. (2003). Comparative analysis of fatty acid amide hydrolase and cb(1) cannabinoid receptor expression in the mouse brain: evidence of a widespread role for fatty acid amide hydrolase in regulation of endocannabinoid signaling. Neuroscience, 119(2), 481-496. https://doi.org/10.1016/s0306-4522(03)00145-3

Cravatt, B. F., & Lichtman, A. H. (2003). Fatty acid amide hydrolase: an emerging therapeutic target in the endocannabinoid system. Curr Opin Chem Biol, 7(4), 469-475. https://doi.org/10.1016/s1367-5931(03)00079-6

Clement, A. B., Hawkins, E. G., Lichtman, A. H., & Cravatt, B. F. (2003). Increased seizure susceptibility and proconvulsant activity of anandamide in mice lacking fatty acid amide hydrolase. J Neurosci, 23(9), 3916-3923. https://doi.org/10.1523/JNEUROSCI.23-09-03916.2003

Adam, G. C., Vanderwal, C. D., Sorensen, E. J., & Cravatt, B. F. (2003). (-)-FR182877 is a potent and selective inhibitor of carboxylesterase-1. Angew Chem Int Ed Engl, 42(44), 5480-5484. https://doi.org/10.1002/anie.200352576

2002:

Waleh, N. S., Cravatt, B. F., Apte-Deshpande, A., Terao, A., & Kilduff, T. S. (2002). Transcriptional regulation of the mouse fatty acid amide hydrolase gene. Gene, 291(1-2), 203-210. https://doi.org/10.1016/s0378-1119(02)00598-x

Sipe, J. C., Chiang, K., Gerber, A. L., Beutler, E., & Cravatt, B. F. (2002). A missense mutation in human fatty acid amide hydrolase associated with problem drug use. Proc Natl Acad Sci U S A, 99(12), 8394-8399. https://doi.org/10.1073/pnas.082235799

Lichtman, A. H., Hawkins, E. G., Griffin, G., & Cravatt, B. F. (2002). Pharmacological activity of fatty acid amides is regulated, but not mediated, by fatty acid amide hydrolase in vivo. J Pharmacol Exp Ther, 302(1), 73-79. https://doi.org/10.1124/jpet.302.1.73

Jessani, N., Liu, Y., Humphrey, M., & Cravatt, B. F. (2002). Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness. Proc Natl Acad Sci U S A, 99(16), 10335-10340. https://doi.org/10.1073/pnas.162187599

Cravatt, B. F., & Lichtman, A. H. (2002). The enzymatic inactivation of the fatty acid amide class of signaling lipids. Chem Phys Lipids, 121(1-2), 135-148. https://doi.org/10.1016/s0009-3084(02)00147-0

Bracey, M. H., Hanson, M. A., Masuda, K. R., Stevens, R. C., & Cravatt, B. F. (2002). Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling. Science, 298(5599), 1793-1796. https://doi.org/10.1126/science.1076535

Aebersold, R., & Cravatt, B. F. (2002). Proteomics--advances, applications and the challenges that remain. Trends Biotechnol, 20(12 Suppl), S1-2. https://doi.org/10.1016/s1471-1931(02)00206-9

Adam, G. C., Sorensen, E. J., & Cravatt, B. F. (2002). Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype. Nat Biotechnol, 20(8), 805-809. https://doi.org/10.1038/nbt714

Adam, G. C., Sorensen, E. J., & Cravatt, B. F. (2002). Chemical strategies for functional proteomics. Mol Cell Proteomics, 1(10), 781-790. https://doi.org/10.1074/mcp.r200006-mcp200

Adam, G. C., Sorensen, E. J., & Cravatt, B. F. (2002). Trifunctional chemical probes for the consolidated detection and identification of enzyme activities from complex proteomes. Mol Cell Proteomics, 1(10), 828-835. https://doi.org/10.1074/mcp.t200007-mcp200

2001:

Patricelli, M. P., & Cravatt, B. F. (2001). Proteins regulating the biosynthesis and inactivation of neuromodulatory fatty acid amides. Vitam Horm, 62, 95-131. https://doi.org/10.1016/s0083-6729(01)62002-8

Patricelli, M. P., & Cravatt, B. F. (2001). Characterization and manipulation of the acyl chain selectivity of fatty acid amide hydrolase. Biochemistry, 40(20), 6107-6115. https://doi.org/10.1021/bi002578r

Larsen, N. A., Heine, A., Crane, L., Cravatt, B. F., Lerner, R. A., & Wilson, I. A. (2001). Structural basis for a disfavored elimination reaction in catalytic antibody 1D4. J Mol Biol, 314(1), 93-102. https://doi.org/10.1006/jmbi.2001.5112

Kidd, D., Liu, Y., & Cravatt, B. F. (2001). Profiling serine hydrolase activities in complex proteomes. Biochemistry, 40(13), 4005-4015. https://doi.org/10.1021/bi002579j

Huitron-Resendiz, S., Gombart, L., Cravatt, B. F., & Henriksen, S. J. (2001). Effect of oleamide on sleep and its relationship to blood pressure, body temperature, and locomotor activity in rats. Exp Neurol, 172(1), 235-243. https://doi.org/10.1006/exnr.2001.7792

Cravatt, B. F., Demarest, K., Patricelli, M. P., Bracey, M. H., Giang, D. K., Martin, B. R., & Lichtman, A. H. (2001). Supersensitivity to anandamide and enhanced endogenous cannabinoid signaling in mice lacking fatty acid amide hydrolase. Proc Natl Acad Sci U S A, 98(16), 9371-9376. https://doi.org/10.1073/pnas.161191698

Adam, G. C., Cravatt, B. F., & Sorensen, E. J. (2001). Profiling the specific reactivity of the proteome with non-directed activity-based probes. Chem Biol, 8(1), 81-95. https://doi.org/10.1016/s1074-5521(00)90060-7

2000:

Wang, E. W., Kessler, B. M., Borodovsky, A., Cravatt, B. F., Bogyo, M., Ploegh, H. L., & Glas, R. (2000). Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity. Proc Natl Acad Sci U S A, 97(18), 9990-9995. https://doi.org/10.1073/pnas.180328897

Patricelli, M. P., & Cravatt, B. F. (2000). Clarifying the catalytic roles of conserved residues in the amidase signature family. J Biol Chem, 275(25), 19177-19184. https://doi.org/10.1074/jbc.M001607200

Kustedjo, K., Bracey, M. H., & Cravatt, B. F. (2000). Torsin A and its torsion dystonia-associated mutant forms are lumenal glycoproteins that exhibit distinct subcellular localizations. J Biol Chem, 275(36), 27933-27939. https://doi.org/10.1074/jbc.M910025199

Egertova, M., Cravatt, B. F., & Elphick, M. R. (2000). Fatty acid amide hydrolase expression in rat choroid plexus: possible role in regulation of the sleep-inducing action of oleamide. Neurosci Lett, 282(1-2), 13-16. https://doi.org/10.1016/s0304-3940(00)00841-7

Cravatt, B. F., & Sorensen, E. J. (2000). Chemical strategies for the global analysis of protein function. Curr Opin Chem Biol, 4(6), 663-668. https://doi.org/10.1016/s1367-5931(00)00147-2

Boger, D. L., Sato, H., Lerner, A. E., Hedrick, M. P., Fecik, R. A., Miyauchi, H., Wilkie, G. D., Austin, B. J., Patricelli, M. P., & Cravatt, B. F. (2000). Exceptionally potent inhibitors of fatty acid amide hydrolase: the enzyme responsible for degradation of endogenous oleamide and anandamide. Proc Natl Acad Sci U S A, 97(10), 5044-5049. https://doi.org/10.1073/pnas.97.10.5044

Boger, D. L., Fecik, R. A., Patterson, J. E., Miyauchi, H., Patricelli, M. P., & Cravatt, B. F. (2000). Fatty acid amide hydrolase substrate specificity. Bioorg Med Chem Lett, 10(23), 2613-2616. https://doi.org/10.1016/s0960-894x(00)00528-x

1999:

Thomas, E. A., Cravatt, B. F., & Sutcliffe, J. G. (1999). The endogenous lipid oleamide activates serotonin 5-HT7 neurons in mouse thalamus and hypothalamus. J Neurochem, 72(6), 2370-2378. https://doi.org/10.1046/j.1471-4159.1999.0722370.x

Patricelli, M. P., Lovato, M. A., & Cravatt, B. F. (1999). Chemical and mutagenic investigations of fatty acid amide hydrolase: evidence for a family of serine hydrolases with distinct catalytic properties. Biochemistry, 38(31), 9804-9812. https://doi.org/10.1021/bi990637z

Patricelli, M. P., & Cravatt, B. F. (1999). Fatty acid amide hydrolase competitively degrades bioactive amides and esters through a nonconventional catalytic mechanism. Biochemistry, 38(43), 14125-14130. https://doi.org/10.1021/bi991876p

Liu, Y., Patricelli, M. P., & Cravatt, B. F. (1999). Activity-based protein profiling: the serine hydrolases. Proc Natl Acad Sci U S A, 96(26), 14694-14699. https://doi.org/10.1073/pnas.96.26.14694

Boger, D. L., Sato, H., Lerner, A. E., Austin, B. J., Patterson, J. E., Patricelli, M. P., & Cravatt, B. F. (1999). Trifluoromethyl ketone inhibitors of fatty acid amide hydrolase: a probe of structural and conformational features contributing to inhibition. Bioorg Med Chem Lett, 9(2), 265-270. https://doi.org/10.1016/s0960-894x(98)00734-3

1998:

Wan, M., Cravatt, B. F., Ring, H. Z., Zhang, X., & Francke, U. (1998). Conserved chromosomal location and genomic structure of human and mouse fatty-acid amide hydrolase genes and evaluation of clasper as a candidate neurological mutation. Genomics, 54(3), 408-414. https://doi.org/10.1006/geno.1998.5597

Patricelli, M. P., Patterson, J. E., Boger, D. L., & Cravatt, B. F. (1998). An endogenous sleep-inducing compound is a novel competitive inhibitor of fatty acid amide hydrolase. Bioorg Med Chem Lett, 8(6), 613-618. https://doi.org/10.1016/s0960-894x(98)00073-0

Patricelli, M. P., Lashuel, H. A., Giang, D. K., Kelly, J. W., & Cravatt, B. F. (1998). Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization. Biochemistry, 37(43), 15177-15187. https://doi.org/10.1021/bi981733n

Giang, D. K., & Cravatt, B. F. (1998). A second mammalian N-myristoyltransferase. J Biol Chem, 273(12), 6595-6598. https://doi.org/10.1074/jbc.273.12.6595

Egertova, M., Giang, D. K., Cravatt, B. F., & Elphick, M. R. (1998). A new perspective on cannabinoid signalling: complementary localization of fatty acid amide hydrolase and the CB1 receptor in rat brain. Proc Biol Sci, 265(1410), 2081-2085. https://doi.org/10.1098/rspb.1998.0543

Boger, D. L., Patterson, J. E., Guan, X., Cravatt, B. F., Lerner, R. A., & Gilula, N. B. (1998). Chemical requirements for inhibition of gap junction communication by the biologically active lipid oleamide. Proc Natl Acad Sci U S A, 95(9), 4810-4815. https://doi.org/10.1073/pnas.95.9.4810

Boger, D. L., Henriksen, S. J., & Cravatt, B. F. (1998). Oleamide: an endogenous sleep-inducing lipid and prototypical member of a new class of biological signaling molecules. Curr Pharm Des, 4(4), 303-314. https://www.ncbi.nlm.nih.gov/pubmed/10197045

1997:

Thomas, E. A., Cravatt, B. F., Danielson, P. E., Gilula, N. B., & Sutcliffe, J. G. (1997). Fatty acid amide hydrolase, the degradative enzyme for anandamide and oleamide, has selective distribution in neurons within the rat central nervous system. J Neurosci Res, 50(6), 1047-1052. https://doi.org/10.1002/(SICI)1097-4547(19971215)50:6<1047::AID-JNR16>3.0.CO;2-1

Guan, X., Cravatt, B. F., Ehring, G. R., Hall, J. E., Boger, D. L., Lerner, R. A., & Gilula, N. B. (1997). The sleep-inducing lipid oleamide deconvolutes gap junction communication and calcium wave transmission in glial cells. J Cell Biol, 139(7), 1785-1792. https://doi.org/10.1083/jcb.139.7.1785

Giang, D. K., & Cravatt, B. F. (1997). Molecular characterization of human and mouse fatty acid amide hydrolases. Proc Natl Acad Sci U S A, 94(6), 2238-2242. https://doi.org/10.1073/pnas.94.6.2238

Arreaza, G., Devane, W. A., Omeir, R. L., Sajnani, G., Kunz, J., Cravatt, B. F., & Deutsch, D. G. (1997). The cloned rat hydrolytic enzyme responsible for the breakdown of anandamide also catalyzes its formation via the condensation of arachidonic acid and ethanolamine. Neurosci Lett, 234(1), 59-62. https://doi.org/10.1016/s0304-3940(97)00673-3

1996:

Cravatt, B. F., Giang, D. K., Mayfield, S. P., Boger, D. L., Lerner, R. A., & Gilula, N. B. (1996). Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides. Nature, 384(6604), 83-87. https://doi.org/10.1038/384083a0

Cravatt, B. F., Lerner, R. A., & Boger, D. L. (1996). Structure Determination of an Endogenous Sleep-Inducing Lipid, cis-9-Octadecenamide (Oleamide):  A Synthetic Approach to the Chemical Analysis of Trace Quantities of a Natural Product. Journal of the American Chemical Society, 118(3), 580-590. https://doi.org/10.1021/ja9532345 

1995:

Cravatt, B. F., Prospero-Garcia, O., Siuzdak, G., Gilula, N. B., Henriksen, S. J., Boger, D. L., & Lerner, R. A. (1995). Chemical characterization of a family of brain lipids that induce sleep. Science, 268(5216), 1506-1509. https://doi.org/10.1126/science.7770779

1994:

Lerner, R. A., Siuzdak, G., Prospero-Garcia, O., Henriksen, S. J., Boger, D. L., & Cravatt, B. F. (1994). Cerebrodiene: a brain lipid isolated from sleep-deprived cats. Proc Natl Acad Sci U S A, 91(20), 9505-9508. https://doi.org/10.1073/pnas.91.20.9505

Boger, D. L., Lerner, R. A., & Cravatt, B. F. (1994). Synthesis of a Functionalized Rigid Bicyclo[2.2.1]heptane: A Useful Hapten for Eliciting Catalytic Antibodies. The Journal of Organic Chemistry, 59(17), 5078-5079. https://doi.org/10.1021/jo00096a064 

Cravatt, B. F., Ashley, J. A., Janda, K. D., Boger, D. L., & Lerner, R. A. (1994). Crossing Extreme Mechanistic Barriers by Antibody Catalysis: Syn Elimination to a Cis Olefin. Journal of the American Chemical Society, 116(13), 6013-6014. https://doi.org/10.1021/ja00092a080 

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