recent publications
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academic article
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Huang, Z.*, Ogasawara, D.*, Seneviratne, U. I., Cognetta III, A. B., Ende, C. W. A., Nason, D. M., Lapham, K., Litchfield, J., Johnson, D. S., Cravatt, B. F.
Global portrait of protein targets of metabolites of the neurotoxic compound BIA 10-2474
ACS Chemical Biology
2019
14:192-197
DOI:10.1021/acschembio.8b01097
PMID:30702848
PMCID:PMC6383364
(* = equal contribution)
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Pentinmikko, N., Iqbal, S., Mana, M., Andersson, S., Cognetta III, A. B., Suciu, R. M., Roper, J., Luopajarvi, K., Markelin, E., Gopalakrishnan, S., Smolander, O. P., Naranjo, S., et al.
Notum produced by Paneth cells attenuates regeneration of aged intestinal epithelium
Nature
2019
571:398-402
DOI:10.1038/s41586-019-1383-0
PMID:31292548
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Chen, A. L., Lum, K. M., Lara-Gonzalez, P., Ogasawara, D., Cognetta III, A. B., To, A., Parsons, W. H., Simon, G. M., Desai, A., Petrascheck, M., Bar-Peled, L., Cravatt, B. F.
Pharmacological convergence reveals a lipid pathway that regulates C. elegans lifespan
Nature Chemical Biology
2019
15:453-462
DOI:10.1038/s41589-019-0243-4
PMID:30911178
PMCID:PMC6548519
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Suciu, R. M., Cognetta, A. B., Potter, Z. E., Cravatt, B. F.
Selective irreversible inhibitors of the Wnt-deacylating enzyme NOTUM developed by activity-based protein profiling
ACS Medicinal Chemistry Letters
2018
9:563-568
DOI:10.1021/acsmedchemlett.8b00191
PMID:29937983
PMCID:PMC6004566
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Touchette, M. H., Van Vlack, E. R., Bai, L., Kim, J., Cognetta III, A. B., Previti, M. L., Backus, K. M., Martin, D. W., Cravatt, B. F., Seeliger, J. C.
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 Infectious Diseases
2017
3:336-348
DOI:10.1021/acsinfecdis.6b00179
PMID:28276676
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van Esbroeck, A. C. M., Janssen, A. P. A., Cognetta III, A. B., Ogasawara, D., Shpak, G., van der Kroeg, M., Kantae, V., Baggelaar, M. P., de Vrij, F. M. S., Deng, H., Allara, M., Fezza, F., et al.
Activity-based protein profiling reveals off-target proteins of the FAAH inhibitor BIA 10-2474
Science
2017
356:1084-1087
DOI:10.1126/science.aaf7497
PMID:28596366
PMCID:PMC5641481
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Kornahrens, A. F., Cognetta III, A. B., Brody, D. M., Matthews, M. L., Cravatt, B. F., Boger, D. L.
Design of benzoxathiazin-3-one 1,1-dioxides as a new class of irreversible serine hydrolase inhibitors: Discovery of a uniquely selective PNPLA4 inhibitor
Journal of the American Chemical Society
2017
139:7052-7061
DOI:10.1021/jacs.7602985
PMID:28498651
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Tan, J., Cognetta III, A. B., Diaz, D. B., Lum, K. M., Adachi, S., Kundu, S., Cravatt, B. F., Yudin, A. K.
Multicomponent mapping of boron chemotypes furnishes selective enzyme inhibitors
Nature Communications
2017
8
DOI:10.1038/s41467-017-01319-4
PMID:29170371
PMCID:PMC5701053
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Parsons, W. H., Kolar, M. J., Kamat, S. S., Cognetta III, A. B., Hulce, J. J., Saez, E., Kahn, B. B., Saghatelian, A., Cravatt, B. F.
AIG1 and ADTRP are atypical integral membrane hydrolases that degrade bioactive FAHFAs
Nature Chemical Biology
2016
12:367-372
DOI:10.1038/nchembio.2051
PMID:27018888
PMCID:PMC4837090
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Niphakis, M. J., Lum, K. M., Cognetta III, A. B., Correia, B. E., Ichu, T. A., Olucha, J., Brown, S. J., Kundu, S., Piscitelli, F., Rosen, H., Cravatt, B. F.
A global map of lipid-binding proteins and their ligandability in cells
Cell
2015
161:1668-1680
DOI:10.1016/j.cell.2015.05.045
PMID:26091042
PMCID:PMC4615699
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Adachi, S., Cognetta III, A. B., Niphakis, M. J., He, Z., Zajdlik, A., St. Denis, J. D., Scully, C. C. G., Cravatt, B. F., Yudin, A. K.
Facile synthesis of borofragments and their evaluation in activity-based protein profiling
Chemical Communications
2015
51:3608-3611
DOI:10.1039/c4cc09107h
PMID:25633248
PMCID:PMC4330092
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Cognetta III, A. B., Niphakis, M. J., Lee, H. C., Martini, M. L., Hulce, J. J., Cravatt, B. F.
Selective N-hydroxyhydantoin carbamate inhibitors of mammalian serine hydrolases
Chemistry & Biology
2015
22:928-937
DOI:10.1016/j.chembiol.2015.05.018
PMID:26120000
PMCID:PMC4527528
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Lajkiewicz, N. J., Cognetta III, A. B., Niphakis, M. J., Cravatt, B. F., Porco Jr., J. A.
Remodeling natural products: chemistry and serine hydrolase activity of a rocaglate-derived beta-lactone
Journal of the American Chemical Society
2014
136:2659-2664
DOI:10.1021/ja412431g
PMID:24447064
PMCID:PMC3978386
- Niphakis, M. J., Cognetta III, A. B., Chang, J. W., Buczynski, M. W., Parsons, L. H., Byrne, F., Burston, J. J., Chapman, V., Cravatt, B. F. Evaluation of NHS carbamates as a potent and selective class of endocannabinoid hydrolase inhibitors ACS Chemical Neuroscience 2013 4:1322-1332 DOI:10.1021/cn400116z PMID:23731016 PMCID:PMC3778430
- Hulce, J. J., Cognetta III, A. B., Niphakis, M. J., Tully, S. E., Cravatt, B. F. Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells Nature Methods 2013 10:259-264 DOI:10.1038/nmeth.2368 PMID:23396283 PMCID:PMC3601559
- Chang, J. W., Cognetta III, A. B., Niphakis, M. J., Cravatt, B. F. Proteome-wide reactivity profiling identifies diverse carbamate chemotypes tuned for serine hydrolase inhibition ACS Chemical Biology 2013 8:1590-1599 DOI:10.1021/cb400261h PMID:23701408 PMCID:PMC3806897
- Chang, J. W., Niphakis, M. J., Lum, K. M., Cognetta III, A. B., Wang, C., Matthews, M. L., Niessen, S., Buczynski, M. W., Parsons, L. H., Cravatt, B. F. Highly selective inhibitors of monoacylglycerol lipase bearing a reactive group that is bioisosteric with endocannabinoid substrates Chemistry & Biology 2012 19:579-588 DOI:10.1016/j.chembiol.2012.03.009 PMID:22542104 PMCID:PMC3361572
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