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How Chemoproteomics Can Enable Drug Discovery and Development
Open accessAbstract
Creating first-in-class medications to treat human disease is an extremely challenging endeavor. While genome sequencing and genetics are making direct connections between mutations and human disorders at an unprecedented rate, matching molecular targets with a suitable therapeutic indication must ultimately be achieved by pharmacology. Here, we discuss how the integration of chemical proteomic platforms (such as activity-based protein profiling) into the earliest stages of the drug discovery process has the potential to greatly expand the scope of proteins that can be pharmacologically evaluated in living systems, and, through doing so, promote the identification and prioritization of new therapeutic targets.
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“In addition, some analytical techniques such as click chemistry, activity probes, and mass spectrometry-based proteomics to evaluate binding activity and selectivity in vitro and in vivo are only available for covalent compounds [120–124].”
From The design and development of covalent protein-protein interaction inhibitors for cancer treatment (2020) · cites this paper as [120]
In the citing paper
“This ‘electrophile-first’ approach is partly facilitated by the development of chemoproteomic platforms that enable rapid target identification and selectivity profiling of covalent ligands14–18.”
From Advances in covalent drug discovery (2022) · cites this paper as [17]
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1 retracted
Selective killing of cancer cells by a small molecule targeting the stress response to ROS
Raj, L., Ide, T., Gurkar, A. U., Foley, M. A., Schenone, M., Li, X., Tolliday, N. J., Golub, T. R., Carr, S. A., Shamji, A. F., et al. (2011) · Nature · doi:10.1038/nature10167 · Cited by 1,040
RetractedAn Integrated Genomic Analysis of Human Glioblastoma Multiforme
Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857
Identification of the transforming EML4–ALK fusion gene in non-small-cell lung cancer
Soda, M., Choi, Y. L., Enomoto, M., Takada, S., Yamashita, Y., Ishikawa, S., Fujiwara, S.-I., Watanabe, H., Kurashina, K., Hatanaka, H., et al. (2007) · Nature · doi:10.1038/nature05945 · Cited by 5,439
Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154
How many drug targets are there?
Overington, J. P., Al-Lazikani, B., & Hopkins, A. L. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2199 · Cited by 3,505
BET Bromodomain Inhibition as a Therapeutic Strategy to Target c-Myc
Delmore, J. E., Issa, G. C., Lemieux, M. E., Rahl, P. B., Shi, J., Jacobs, H. M., Kastritis, E., Gilpatrick, T., Paranal, R. M., Qi, J., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.017 · Cited by 2,888
The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., & Cantley, L. C. (2008) · Nature · doi:10.1038/nature06734 · Cited by 2,820
Targeting cancer with small molecule kinase inhibitors
Zhang, J., Yang, P. L., & Gray, N. S. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2559 · Cited by 2,648
A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
Thornberry, N. A., Bull, H. G., Calaycay, J. R., Chapman, K. T., Howard, A. D., Kostura, M. J., Miller, D. K., Molineaux, S. M., Weidner, J. R., Aunins, J. G., et al. (1992) · Nature · doi:10.1038/356768a0 · Cited by 2,613
Comprehensive analysis of kinase inhibitor selectivity
Davis, M. I., Hunt, J. P., Herrgard, S., Ciceri, P., Wodicka, L. M., Pallares, G., Hocker, M., Treiber, D. K., & Zarrinkar, P. P. (2011) · Nature Biotechnology · doi:10.1038/nbt.1990 · Cited by 2,409
Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
Cravatt, B. F., Giang, D. K., Mayfield, S. P., Boger, D. L., Lerner, R. A., & Gilula, N. B. (1996) · Nature · doi:10.1038/384083a0 · Cited by 2,125
Self-citationTankyrase inhibition stabilizes axin and antagonizes Wnt signalling
Huang, S.-M. A., Mishina, Y., Liu, S.-M., Cheung, A. K., Stegmeier, F., Michaud, G., Charlat, O., Wiellette, E., Zhang, Y., Wiessner, S., et al. (2009) · Nature · doi:10.1038/nature08356 · Cited by 2,077
Identification of RIP1 kinase as a specific cellular target of necrostatins
Degterev, A., Hitomi, J., Germscheid, M., Ch'en, I. L., Korkina, O., Teng, X., Abbott, D., Cuny, G. D., Yuan, C., Wagner, G., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.83 · Cited by 2,059
A small molecule–kinase interaction map for clinical kinase inhibitors
Fabian, M. A., Biggs, W., Treiber, D. K., Atteridge, C. E., Azimioara, M. D., Benedetti, M. G., Carter, T. A., Ciceri, P., Edeen, P. T., Floyd, M. B., et al. (2005) · Nature Biotechnology · doi:10.1038/nbt1068 · Cited by 1,923
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
How were new medicines discovered?
Swinney, D. C., & Anthony, J. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3480 · Cited by 1,812
Quantitative reactivity profiling predicts functional cysteines in proteomes
Weerapana, E., Wang, C., Simon, G. M., Richter, F., Khare, S., Dillon, M. B. D., Bachovchin, D. A., Mowen, K., Baker, D., & Cravatt, B. F. (2010) · Nature · doi:10.1038/nature09472 · Cited by 1,684
Self-citationRAS–RAF–MEK-dependent oxidative cell death involving voltage-dependent anion channels
Yagoda, N., von Rechenberg, M., Zaganjor, E., Bauer, A. J., Yang, W. S., Fridman, D. J., Wolpaw, A. J., Smukste, I., Peltier, J. M., Boniface, J. J., et al. (2007) · Nature · doi:10.1038/nature05859 · Cited by 1,631
Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia
Dawson, M. A., Prinjha, R. K., Dittmann, A., Giotopoulos, G., Bantscheff, M., Chan, W.-I., Robson, S. C., Chung, C., Hopf, C., Savitski, M. M., et al. (2011) · Nature · doi:10.1038/nature10509 · Cited by 1,530
Targeting the dynamic HSP90 complex in cancer
Trepel, J. B., Mollapour, M., Giaccone, G., & Neckers, L. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2887 · Cited by 1,523
A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase
Harding, M. W., Gałat, A., Uehling, D., & Schreiber, S. L. (1989) · Nature · doi:10.1038/341758a0 · Cited by 1,396
Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix
Walensky, L. D., Kung, A. L., Escher, I., Malia, T. J., Barbuto, S., Wright, R. D., Wagner, G., Verdine, G. L., & Korsmeyer, S. J. (2004) · Science · doi:10.1126/science.1099191 · Cited by 1,349
Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry
Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.124125 · Cited by 1,270
Self-citationA Pharmacological Map of the PI3-K Family Defines a Role for p110α in Insulin Signaling
Knight, Z. A., Gonzalez, B., Feldman, M. E., Zunder, E. R., Goldenberg, D. D., Williams, O., Loewith, R., Stokoe, D., Balla, A., Toth, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.035 · Cited by 1,174
Activity-based protein profiling: The serine hydrolases
Liu, Y., Patricelli, M. P., & Cravatt, B. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14694 · Cited by 1,143
Self-citationActive-Site Inhibitors of mTOR Target Rapamycin-Resistant Outputs of mTORC1 and mTORC2
Feldman, M. E., Apsel, B., Uotila, A., Loewith, R., Knight, Z. A., Ruggero, D., & Shokat, K. M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000038 · Cited by 1,111
Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors
Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S., Böesche, M., Hobson, S., Mathieson, T., Perrin, J., Raida, M., Rau, C., et al. (2007) · Nature Biotechnology · doi:10.1038/nbt1328 · Cited by 1,036
Selective blockade of 2-arachidonoylglycerol hydrolysis produces cannabinoid behavioral effects
Long, J. Z., Li, W., Booker, L., Burston, J. J., Kinsey, S. G., Schlosburg, J. E., Pavón, F. J., Serrano, A., Selley, D. E., Parsons, L. H., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.129 · Cited by 954
Self-citationA small molecule inhibitor of β-catenin/cyclic AMP response element-binding protein transcription
Emami, K. H., Nguyen, C., Ma, H., Kim, D. H., Jeong, K. W., Eguchi, M., Moon, R. T., Teo, J.-L., Oh, S. W., Kim, H. Y., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404875101 · Cited by 879
A Small-Molecule Inhibitor of Tgf-β Signaling Replaces Sox2 in Reprogramming by Inducing Nanog
Ichida, J. K., Blanchard, J., Lam, K., Son, E. Y., Chung, J. E., Egli, D., Loh, K. M., Carter, A. C., Di Giorgio, F. P., Koszka, K., et al. (2009) · Cell Stem Cell · doi:10.1016/j.stem.2009.09.012 · Cited by 808
Direct inhibition of the NOTCH transcription factor complex
Moellering, R. E., Cornejo, M., Davis, T. N., Bianco, C. D., Aster, J. C., Blacklow, S. C., Kung, A. L., Gilliland, D. G., Verdine, G. L., & Bradner, J. E. (2009) · Nature · doi:10.1038/nature08543 · Cited by 752
Self-citationZou, H. Y., Li, Q., Lee, J. H., Arango, M. E., McDonnell, S. R. P., Yamazaki, S., Koudriakova, T. B., Alton, G., Cui, J. J., Kung, P., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4443 · Cited by 749
Chemical phylogenetics of histone deacetylases
Bradner, J. E., West, N., Grachan, M. L., Greenberg, E. F., Haggarty, S. J., Warnow, T., & Mazitschek, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.313 · Cited by 720
Targeting the cancer kinome through polypharmacology
Knight, Z. A., Lin, H., & Shokat, K. M. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2787 · Cited by 674 · cited 2×
“The realization that drugs often produce their biological activity through affecting multiple protein targets has inspired consideration of purposeful polypharmacology as a way to develop new medicines [76, 79, 80].”
BackgroundChemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes
Bantscheff, M., Hopf, C., Savitski, M. M., Dittmann, A., Grandi, P., Michon, A.-M., Schlegl, J., Abraham, Y., Becher, I., Bergamini, G., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1759 · Cited by 659
Evidence for an Alternative Glycolytic Pathway in Rapidly Proliferating Cells
Heiden, M. G. V., Locasale, J. W., Swanson, K. D., Sharfi, H., Heffron, G. J., Amador‐Noguez, D., Christofk, H. R., Wagner, G., Rabinowitz, J. D., Asara, J. M., et al. (2010) · Science · doi:10.1126/science.1188015 · Cited by 648
Reactivation of the p53 Tumor Suppressor Pathway by a Stapled p53 Peptide
Bernal, F., Tyler, A. F., Korsmeyer, S. J., Walensky, L. D., & Verdine, G. L. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0693587 · Cited by 563
Structural Bioinformatics-Based Design of Selective, Irreversible Kinase Inhibitors
Cohen, M. S., Zhang, C., Shokat, K. M., & Taunton, J. (2005) · Science · doi:10.1126/science1108367 · Cited by 509
Identification and isolation of a membrane protein necessary for leukotriene production
Miller, D. K., Gillard, J. W., Vickers, P. J., Sadowski, S. J., Leveillé, C., Mancini, J. A., Charleson, P., Dixon, R. A. F., Ford‐Hutchinson, A. W., Fortin, R., et al. (1990) · Nature · doi:10.1038/343278a0 · Cited by 458
The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease
Long, J. Z., & Cravatt, B. F. (2011) · Chemical Reviews · doi:10.1021/cr200075y · Cited by 434
Self-citationCharacterization of a selective inhibitor of the Parkinson's disease kinase LRRK2
Deng, X., Dzamko, N. L., Prescott, A. R., Davies, P., Liu, Q., Yang, Q., Lee, J., Patricelli, M. P., Nomanbhoy, T. K., Alessi, D. R., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.538 · Cited by 434
Functional Interrogation of the Kinome Using Nucleotide Acyl Phosphates
Patricelli, M. P., Szardenings, A. K., Liyanage, M., Nomanbhoy, T. K., Wu, M., Weissig, H., Aban, A., Chun, D., Tanner, S. W., & Kozarich, J. W. (2006) · Biochemistry · doi:10.1021/bi062142x · Cited by 426
The druggable genome: an update
Russ, A., & Lampel, S. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03666-4 · Cited by 421
Arastu‐Kapur, S., Anderl, J. L., Kraus, M., Parlati, F., Shenk, K. D., Lee, S. H., Muchamuel, T., Bennett, M. K., Driessen, C., Ball, A. J., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-1950 · Cited by 417
Edwards, A. M., Isserlin, R., Bader, G. D., Frye, S. V., Willson, T. M., & Yu, F. H. (2011) · Nature · doi:10.1038/470163a · Cited by 411
Discovering potent and selective reversible inhibitors of enzymes in complex proteomes
Leung, D., Hardouin, C., Boger, D. L., & Cravatt, B. F. (2003) · Nature Biotechnology · doi:10.1038/nbt826 · Cited by 391
Self-citationIn Situ Kinase Profiling Reveals Functionally Relevant Properties of Native Kinases
Patricelli, M. P., Nomanbhoy, T. K., Wu, J., Brown, H., Zhou, D., Zhang, J., Jagannathan, S., Aban, A., Okerberg, E. S., Herring, C., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.04.011 · Cited by 358
Activity-based Proteomics of Enzyme Superfamilies: Serine Hydrolases as a Case Study
Simon, G. M., & Cravatt, B. F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.097600 · Cited by 327
Self-citationBerg, T., Cohen, S. B., Desharnais, J., Sonderegger, C. K., Maslyar, D. J., Goldberg, J., Boger, D. L., & Vogt, P. K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.062036999 · Cited by 326
Self-renewal of embryonic stem cells by a small molecule
Chen, S., Tae, J., Zhang, Q., Yao, S., Yan, F., Peters, E. C., Schöler, H. R., Schultz, P. G., & Ding, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608156103 · Cited by 310
Identifying the proteins to which small-molecule probes and drugs bind in cells
Ong, S., Schenone, M., Margolin, A. A., Li, X., Do, K., Doud, M. K., Mani, D. R., Kuai, L., Wang, X., Wood, J. L., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900191106 · Cited by 303
An orthosteric inhibitor of the Ras-Sos interaction
Patgiri, A., Yadav, K. K., Arora, P. S., & Bar‐Sagi, D. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.612 · Cited by 298
Contemporary strategies for the stabilization of peptides in the α-helical conformation
Henchey, L. K., Jochim, A. L., & Arora, P. S. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.08.019 · Cited by 294
Acetylcholinesterase inhibitors: novel activities of old molecules
Racchi, M. (2004) · Pharmacological Research · doi:10.1016/j.phrs.2003.12.027 · Cited by 291
A Role for the Protease Falcipain 1 in Host Cell Invasion by the Human Malaria Parasite
Greenbaum, D. C., Baruch, A., Grainger, M., Bozdech, Z., Medzihradszky, K. F., Engel, J. C., DeRisi, J. L., Holder, A. A., & Bogyo, M. S. (2002) · Science · doi:10.1126/science.1077426 · Cited by 290
Bachovchin, D. A., Ji, T., Li, W., Simon, G. M., Blankman, J. L., Adibekian, A., Hoover, H. S., Niessen, S., & Cravatt, B. F. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011663107 · Cited by 274
Self-citationGetting pharmaceutical R&D back on target
Bunnage, M. E. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.581 · Cited by 269
Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90
Moulick, K., Ahn, J. H., Zong, H., Rodina, A., Cerchietti, L. C. A., Gomes-DaGama, E. M., Caldas-Lopes, E., Beebe, K. E., Perna, F., Hatzi, K., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.670 · Cited by 261
Arastu‐Kapur, S., Ponder, E. L., Fonović, U. P., Yeoh, S., Yuan, F., Fonovič, M., Grainger, M., Phillips, C. I., Powers, J. C., & Bogyo, M. S. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.70 · Cited by 260
Systems approaches to polypharmacology and drug discovery.
Boran, A. D. W., & Iyengar, R. (2010) · PubMed · Cited by 253
Click-generated triazole ureas as ultrapotent in vivo–active serine hydrolase inhibitors
Adibekian, A., Martin, B. R., Wang, C., Hsu, K., Bachovchin, D. A., Niessen, S., Hoover, H. S., & Cravatt, B. F. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.579 · Cited by 245
Self-citationBachovchin, D. A., Brown, S. J., Rosen, H., & Cravatt, B. F. (2009) · Nature Biotechnology · doi:10.1038/nbt.1531 · Cited by 245
Self-citationActivity-based probes for proteomic profiling of histone deacetylase complexes
Salisbury, C. M., & Cravatt, B. F. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608659104 · Cited by 243
Self-citationSmall-molecule kinase inhibitors provide insight into Mps1 cell cycle function
Kwiatkowski, N. P., Jelluma, N., Filippakopoulos, P., Soundararajan, M., Manak, M. S., Kwon, M., Choi, H. G., Sim, T., Deveraux, Q. L., Rottmann, S., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.345 · Cited by 240
The human genome and drug discovery after a decade. Roads (still) not takenPreprint
Isserlin, R., Bader, G. D., Edwards, A. M., Frye, S. V., Willson, T. M., & Yu, F. H. (2011) · arXiv (Cornell University) · doi:10.48550/arxiv.1102.0448 · Cited by 236
Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling
Evans, M. J., Saghatelian, A., Sorensen, E. J., & Cravatt, B. F. (2005) · Nature Biotechnology · doi:10.1038/nbt1149 · Cited by 230
Self-citationHigh-throughput kinase profiling as a platform for drug discovery
GOLDSTEIN, D. M., Gray, N. S., & Zarrinkar, P. P. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2541 · Cited by 220
Thornberry, N. A., & Weber, A. E. (2007) · Current Topics in Medicinal Chemistry · doi:10.2174/156802607780091028 · Cited by 205
Discovery of PF-04457845: A Highly Potent, Orally Bioavailable, and Selective Urea FAAH Inhibitor
Johnson, D. S., Stiff, C. M., Lazerwith, S. E., Kesten, S. R., Fay, L. K., Morris, M. J., Beidler, D. R., Liimatta, M. B., Smith, S. E., Dudley, D. T., et al. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100190t · Cited by 200
Self-citationChiang, K. P., Niessen, S., Saghatelian, A., & Cravatt, B. F. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.08.008 · Cited by 200
Self-citationPharmacological Inhibition of BMK1 Suppresses Tumor Growth through Promyelocytic Leukemia Protein
Yang, Q., Deng, X., Lu, B., Cameron, M. D., Fearns, C., Patricelli, M. P., Yates, J. R., Gray, N. S., & Lee, J. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.08.008 · Cited by 194
A Functional Proteomic Strategy to Discover Inhibitors for Uncharacterized Hydrolases
Li, W., Blankman, J. L., & Cravatt, B. F. (2007) · Journal of the American Chemical Society · doi:10.1021/ja073650c · Cited by 180
Self-citationA clickable inhibitor reveals context-dependent autoactivation of p90 RSK
Cohen, M. S., Hadjivassiliou, H., & Taunton, J. (2007) · Nature Chemical Biology · doi:10.1038/nchembio859 · Cited by 157
Optimization of Activity-Based Probes for Proteomic Profiling of Histone Deacetylase Complexes
Salisbury, C. M., & Cravatt, B. F. (2008) · Journal of the American Chemical Society · doi:10.1021/ja074138u · Cited by 127
Self-citationMiduturu, C. V., Deng, X., Kwiatkowski, N. P., Yang, W., Brault, L., Filippakopoulos, P., Chung, E., Yang, Q., Schwaller, J., Knapp, S., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.05.010 · Cited by 124
A Suite of Activity-Based Probes for Human Cytochrome P450 Enzymes
Wright, A., Song, J. D., & Cravatt, B. F. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9037609 · Cited by 113
Self-citationBachovchin, D. A., Mohr, J. T., Speers, A. E., Wang, C., Berlin, J. M., Spicer, T., Fernández-Vega, V., Chase, P. S., Hodder, P., Schürer, S. C., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015248108 · Cited by 108
Self-citationChemical Proteomic Probes for Profiling Cytochrome P450 Activities and Drug Interactions In Vivo
Wright, A., & Cravatt, B. F. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.08.008 · Cited by 103
Self-citationA Potent and Selective Inhibitor of KIAA1363/AADACL1 that Impairs Prostate Cancer Pathogenesis
Chang, J. W., Nomura, D. K., & Cravatt, B. F. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.02.008 · Cited by 98
Self-citationIrreversible Nek2 Kinase Inhibitors with Cellular Activity
Henise, J., & Taunton, J. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200222m · Cited by 95
How to Revive Breakthrough Innovation in the Pharmaceutical Industry
Munos, B. H., & Chin, W. W. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002273 · Cited by 95
Nekrutenko, A., Hillis, D. M., Patton, J. C., Bradley, R. D., & Baker, R. J. (1998) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a025894 · Cited by 84
Inhibition of a viral enzyme by a small-molecule dimer disruptor
Shahian, T., Lee, G., Lazic, A., Arnold, L. A., Velusamy, P., Roels, C. M., Guy, R. K., & Craik, C. S. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.192 · Cited by 80
Acylating drugs: redesigning natural covalent inhibitors
Kluge, A. F., & Petter, R. C. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.03.035 · Cited by 71
Deu, E., Leyva, M. J., Albrow, V. E., Rice, M. J., Ellman, J. A., & Bogyo, M. S. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.06.007 · Cited by 69
Deng, X., Yang, Q., Kwiatkowski, N. P., Sim, T., McDermott, U., Settleman, J. E., Lee, J.-D., & Gray, N. S. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100304b · Cited by 69
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Self-citation
Metadata
- Authors
- Moellering, R. E., & Cravatt, B. F.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- Cravatt, Benjamin F.
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2012-01
- Volume
- 19
- Issue
- 1
- Pages
- 11-22
- ISSN
- 1074-5521 (ISSN-L)
- PMC
- PMC3312051
- OpenAlex
- W2030953184
- Cited by
- 182
- References
- 96
- Citations by year
- 2026: 9 · 2025: 12 · 2024: 22 · 2023: 7 · 2022: 5 · 2021: 11 · 2020: 16 · 2019: 21 · 2018: 9 · 2017: 10 · 2016: 16 · 2015: 15 · 2014: 7 · 2013: 14 · 2012: 7
- FWCI
- 6.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Chemistry & Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- Cancer Research Institute
- Damon Runyon Cancer Research Foundation
- National Institutes of Health
- National Institute on Drug Abuse (DA025285, R01DA025285)
- National Cancer Institute (R01CA132630, CA-087660, R37CA087660, R01CA087660, CA132630)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- chemoproteomics, drug discovery, drug development, activity-based protein profiling, drug target identification, target prioritization, first-in-class drugs
- MeSH terms
- Enzymes, Humans, Serine Proteinase Inhibitors, Genome, Human, Proteomics, Metabolic Networks and Pathways, Small Molecule Libraries, Drug Discovery
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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