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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
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–184 of 184
Chemoproteomics: Towards Global Drug Target Profiling
Lu, K. (2020) · ChemBioChem · doi:10.1002/cbic.202000439 · Cited by 8
Chemical Genetics Screening Reveals KIAA1363 as a Cytokine-Lowering Target
Hunerdosse, D. M., Morris, P. J., Miyamoto, D. K., Fisher, K. J., Bateman, L. A., Ghazaleh, J. R., Zhong, S., & Nomura, D. K. (2014) · ACS Chemical Biology · doi:10.1021/cb500717g · Cited by 8
DNA Minor Groove Binders as Therapeutic Agents
Withers, J. M., Padroni, G., Pauff, S. M., Clark, A. W., Mackay, S. P., & Burley, G. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12561-2 · Cited by 8
Chemical probes for spatially resolved measurement of active enzymes in single cells
Li, G., & Moellering, R. E. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.06.017 · Cited by 6
Self-citationHellyer, S. D., Aggarwal, S., Chen, A. N. Y., Leach, K., Lapinsky, D. J., & Gregory, K. J. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00009 · Cited by 8
Activity-Based Protein Profiling at the Host–Pathogen Interface
Kovalyova, Y., & Hatzios, S. K. (2018) · Current topics in microbiology and immunology · doi:10.1007/82_2018_129 · Cited by 7
Getting a Handle on Chemical Probes of Chomatin Readers
Waybright, J. M., & James, L. I. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0274 · Cited by 7
Click Chemistry Patents and Their Impact on Drug Discovery and Chemical Biology
Xu, H., & Jones, L. H. (2015) · Pharmaceutical Patent Analyst · doi:10.4155/ppa.14.59 · Cited by 7
Baggelaar, M. P., Janssen, F. J., van Esbroeck, A. C. M., den Dulk, H., Allarà, M., Hoogendoorn, S., McGuire, R., Florea, B. I., Meeuwenoord, N. J., van den Elst, H., et al. (2013) · Angewandte Chemie · doi:10.1002/ange.201306295 · Cited by 7
Chemoproteomics identifies protein ligands for monoacylglycerol lipids
Shanbhag, K., Mhetre, A. B., Saharan, O., Devarajan, A., Rai, A., Madhusudhan, M. S., Chakrapani, H., & Kamat, S. S. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01589-w · Cited by 6
Boatner, L. M., Eberhardt, J., Shikwana, F., Holcomb, M., Lee, P., Houk, K. N., Forli, S., & Backus, K. M. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00225 · Cited by 6
Measurement and utilization of the proteomic reactivity by mass spectrometry
Punzalan, C., Wang, L., Bajrami, B., & Yao, X. (2023) · Mass Spectrometry Reviews · doi:10.1002/mas.21837 · Cited by 7
Pharmacological approaches to understanding protein kinase signaling networks
Stephenson, E. H., & Higgins, J. M. G. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1310135 · Cited by 6
Moriyama, A., Katagiri, N., Nishimura, S., Takahashi, N., & Kakeya, H. (2015) · Scientific Reports · doi:10.1038/srep17427 · Cited by 6
Kirmeier, T., Gopalakrishnan, R., Gormanns, V., Werner, A. M., Cuboni, S., Rudolf, G. C., Höfner, G. C., Wanner, K. T., Sieber, S. A., Schmidt, U., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148608 · Cited by 6
Quantification of In Vivo Target Engagement Using Microfluidic Activity-Based Protein Profiling
Reardon, H. T., Herbst-Graham, R. A., Henry, C. L., Herbst, D. M., Ngo, N., Cisar, J. S., Weber, O. D., Niphakis, M. J., & O’Neill, G. P. (2019) · SLAS TECHNOLOGY · doi:10.1177/2472630319852303 · Cited by 8
Evaluation of a Pooling Chemoproteomics Strategy with an FDA-Approved Drug Library
Sun, H., Yang, K., Zhang, X., Fu, Y., Yarbro, J. M., Wu, Z., Chen, P., Chen, T., & Peng, J. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00256 · Cited by 5
Affinity‐Based Chemoproteomics for Target Identification
Jensen, A. J., & Cornella‐Taracido, I. (2019) · Methods and principles in medicinal chemistry · doi:10.1002/9783527818242.ch2 · Cited by 7
Discovery of Potent, Allosteric GSTO1 Covalent Inhibitors with a New Binding Mode
Sun, Y., Zhang, F., Zhou, L., Feng, Y., Yang, S., Lu, Q., Yuan, X. Y., Hou, W., Liu, B., Guo, Z., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01724 · Cited by 5
Wang, L., Riel, L. P., Bajrami, B., Deng, B., Howell, A. R., & Yao, X. (2020) · ChemBioChem · doi:10.1002/cbic.202000605 · Cited by 7
Identification of Fungicide Targets in Pathogenic Fungi
Foster, A. J. (2018) · Springer eBooks · doi:10.1007/978-3-319-71740-1_9 · Cited by 6
Large-scale characterization of drug mechanism of action using proteome-wide thermal shift assaysPreprint
Vranken, J. G. V., Li, J., Mintseris, J., Wei, T.-Y., Sniezek, C. M., Gadzuk-Shea, M. M., Gygi, S. P., & Schweppe, D. K. (2024) · eLife · doi:10.7554/elife.95595.2 · Cited by 6
Technological Advances in Preclinical Drug Evaluation: The Role of -Omics Methods
Pavelić, S. K., Markova-Car, E., Klobučar, M., Sappe, L., & Spaventi, R. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867326666190711122819 · Cited by 4
Spatial Chemoproteomics for Mapping the Active Proteome
Swenson, C., Pillai, K. S., Carlos, A. J., & Moellering, R. E. (2023) · Israel Journal of Chemistry · doi:10.1002/ijch.202200104 · Cited by 3
Self-citationReactivity of N -acyl hydrazone probes with the mammalian proteome
Shaw, T. A., Powdrill, M. H., Sherratt, A. R., Garland, K., Li, B.-J., Beauchemin, A. M., & Pezacki, J. P. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00027f · Cited by 4
ICBS and ECBS Chemical Biology Meeting 2015 - Let Them Come to Berlin!
Komatsu, T., & Virdee, S. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00268 · Cited by 4
An expanded role for single-cell chemical genomics profiling in drug discovery
Wyatt, A., Hoffer-Hawlik, K., Giglio, R. M., Azizi, E., & McFaline‐Figueroa, J. L. (2026) · Biochemical Journal · doi:10.1042/bcj20253273 · Cited by 3
Small-molecule binding-site discovery using silyl ether-enabled chemoproteomics
Ngo, C., Takechi, S., Sivakumar, A., Villanueva, M., Yu, F., Ball, A. B., Rubio, J. A., Biletch, E., Burton, N. R., Boatner, L. M., et al. (2026) · Nature Chemistry · doi:10.1038/s41557-026-02127-4 · Cited by 3
Target Identification Using Cell Permeable and Cleavable Chloroalkane Derivatized Small Molecules
Méndez, J., Daniels, D. L., Urh, M., & Ohana, R. F. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7201-2_6 · Cited by 3
Suleiman, T. A., Francis, A. C., Ibrahim, A., Owolade, A. J.-J., Adebiyi, E. O., & Anyimadu, D. T. (2023) · OALib · doi:10.4236/oalib.1110520 · Cited by 2
Large-scale characterization of drug mechanism of action using proteome-wide thermal shift assaysPreprint
Vranken, J. G. V., Li, J., Mintseris, J., Gadzuk-Shea, M. M., Gygi, S. P., & Schweppe, D. K. (2024) · eLife · doi:10.7554/elife.95595.1 · Cited by 3
Chaheine, C. M., Tang, J., Conway, L. P., & Parker, C. G. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202502648 · Cited by 2
Systematic Review of Preclinical Evidence on Antifibrotic Potential of Natural Polysaccharides
Wang, J., Ye, Y., Jiang, W., Yang, H., Xu, J., Han, Q., Lü, A., & Kwan, H. Y. (2026) · Polysaccharides · doi:10.3390/polysaccharides7010019 · Cited by 2
Jepras, R., Shah, P., Patel, M., Ludbrook, S. B., Wands, G. D., Bonhert, G., Lake, A. C., Davis, S. P., & Hill, J. A. (2017) · Series in bioengineering · doi:10.1007/978-981-10-4499-1_11 · Cited by 2
Chemical proteomics of reactive molecules
Wang, L., & Yao, X. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821433-6.00008-8 · Cited by 2
A Toolbox for the Identification of Modes of Action of Natural Products
Rodrigues, T. (2019) · Fortschritte der Chemie Organischer Naturstoffe/Fortschritte der Chemie organischer Naturstoffe/Progress in the chemistry of organic natural products · doi:10.1007/978-3-030-14632-0_3 · Cited by 2
Zhao, C., Wang, Y., Steele, A. D., Mori, S., Shen, B., & Wasa, M. (2024) · ChemRxiv · doi:10.26434/chemrxiv-2024-8fdhv · Cited by 2
Aetiopathogenetic Architecture for Pharmaceutical Development (Using Gout as a Case Study)
Avdeeva, E. V., Варина, Н. Р., Ryazanova, T. K., Куркин, В. А., Исакова, Н. В., Volova, L. T., & А., П. Д. (2025) · Ведомости Научного центра экспертизы средств медицинского применения · doi:10.30895/1991-2919-2025-724 · Cited by 1
Saito, Y., Yatabe, H., Krishna, M. C., Yamamoto, K., & Sando, S. (2025) · Chemistry Letters · doi:10.1093/chemle/upaf150 · Cited by 1
Chaheine, C. M., Tang, J., Conway, L. P., & Parker, C. G. (2025) · Angewandte Chemie · doi:10.1002/ange.202502648 · Cited by 1
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Chakraborty, P., Carlos, A. J., Thomas, T., Ghaby, K., Fathi, S., Sharma, M., Nguyen, N. K., Farmwald, M., Blachowicz, L., Alcyone, E., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c18691 · Cited by 2
Self-citationScaling covalent ligand discovery through dynamic combinatorial library-versus-proteome screening
Huang, Y., Hou, L., He, R., Zhu, L., Xu, C., Duan, S., Hu, J., Yang, X. Y., Tsai, Y., Wang, C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74672-y · Cited by 1
[Diversity-oriented synthesis and its application in drug discovery].
Zhang, L. J., Zheng, M.-Y., & Liu, H. (2015) · PubMed · Cited by 1
Assays to Characterize the Cellular Pharmacology of a Chemical Probe
Stefaniak, J., Galan, S. R. G., & Huber, K. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160745-00247 · Cited by 1
Zanders, E. D. (2020) · Springer eBooks · doi:10.1007/978-3-030-57814-5_9 · Cited by 1
In Vivo Imaging of the Tumor‐Associated Enzyme NCEH1 with a Covalent PET Probe
Chang, J. W., Bhuiyan, M. P. I., Tsai, H., Zhang, H. J., Li, G., Fathi, S., McCutcheon, D. C., Leoni, L., Freifelder, R. H., Chen, C., et al. (2020) · Angewandte Chemie · doi:10.1002/ange.202004762 · Cited by 1
Self-citationBiomarkers for Drug Discovery and Development
Oda, Y. (2016) · Journal of the Mass Spectrometry Society of Japan · doi:10.5702/massspec.s16-12 · Cited by 1
Rothweiler, E. M., Stefaniak, J., Ward, J., Rogers, C. M., Balıkçı, E., & Huber, K. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.20.477145 · Cited by 1
Ye, F. (2017) · Methods and principles in medicinal chemistry · doi:10.1002/9783527674381.ch11 · Cited by 1
Closing in on a new treatment for sleeping sickness
Derbyshire, E. R., & Clardy, J. (2013) · eLife · doi:10.7554/elife.01042
Hunerdosse, D. M. (2015) · eScholarship (California Digital Library)
Approaching the Chemometric Modeling of Realistically Diverse Biochemical Data
Cramer, J. A. (2015) · ACS symposium series · doi:10.1021/bk-2015-1199.ch012
Drug Targets from Molecular Wilderness
(2015) · Pan Stanford eBooks · doi:10.1201/b18860-4
Medina-Cleghorn, D. A. (2015) · eScholarship (California Digital Library)
Mass Spectrometry and Chemical Biology in Epigenetics Drug Discovery
Feller, C., Weigt, D., & Hopf, C. (2019) · Methods and principles in medicinal chemistry · doi:10.1002/9783527809257.ch4
A systems chemoproteomic analysis of acyl-CoA/protein interaction networksPreprint
Levy, M. J., Montgomery, D. C., Sardiu, M. E., Bergholtz, S. E., Nance, K. D., Montano, J., Thorpe, A. L., Fox, S. D., Lin, Q., Andresson, T., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/665281
Chemical Probes for Proteins and Networks
Lovell, S., Sutherell, C. L., & Tate, E. W. (2019) · Wiley eBooks · doi:10.1002/9781118970195.ch5
Baccalaureate and Higher Degree Program's Accreditation Committee reports on evaluation data.
Schultz, C. M., & Niedringhaus, L. (1995) · PubMed
Holistic Assessment of Compound Properties—In Vitro to In Vivo Pharmacology
Baxter, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00016-5
α-Methylene-β-Lactone Probe for Measuring Live-Cell Reactions of Small MoleculesPreprint
Wang, L., Riel, L. P., Bajrami, B., Deng, B., Howell, A. R., & Yao, X. (2020) · ChemRxiv · doi:10.26434/chemrxiv.12078582.v1
Introduction to proteomics for chemical biology
Wang, L. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821433-6.00005-2
Recent Advances in Small Molecule Target Identification Methods
Beckwith, R. E. J., & Jain, R. K. (2013) · Annual reports in medicinal chemistry · doi:10.1016/b978-0-12-417150-3.00019-3
Drug Targets from Molecular Wilderness
Yuthavong, Y. (2015) · doi:10.1201/b18860-8
α-Methylene-β-Lactone Probe for Measuring Live-Cell Reactions of Small MoleculesPreprint
Wang, L., Riel, L. P., Bajrami, B., Deng, B., Howell, A. R., & Yao, X. (2020) · ChemRxiv · doi:10.26434/chemrxiv.12078582
Yedji, R. S., Sohm, B., Salnot, V., Guillonneau, F., Cossu‐Leguille, C., & Battaglia, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232416060
Identification of Covalent Ligands – from Single Targets to Whole Proteome
Ngo, C., Ekanayake, A. I., & Zhang, C. (2023) · Israel Journal of Chemistry · doi:10.1002/ijch.202200105
Genetic Basis of Sickle Cell Disease and Relevance to Pharmacoproteomics
Muolokwu, C. E., & Quainoo, L. (2024) · Springer eBooks · doi:10.1007/978-3-031-64021-6_7
Emerging Technologies for Epigenetic Drug Discovery
(2024) · Royal Society of Chemistry eBooks · doi:10.1039/9781837674916-part2
Mass Spectrometry and Chemical Biology Approaches for Deconvoluting Epigenetic Targets
Burton, A. J., Hamza, G. M., Iannetta, A. A., Miele, E., & Zhang, A. X. (2024) · Royal Society of Chemistry eBooks · doi:10.1039/9781837674916-00050
Charting the ligandable proteome for stereoselective interactions
Pezacki, J. P., Lundrigan, E., Evers, P., & Uguccioni, S. M. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01639-1
Jackson, P. A., Kisty, E. A., Pradhan, V., Swank, C., Bohrer, L., Nolan, T. L., Weerapana, E., & Lapinsky, D. J. (2024) · ACS Omega · doi:10.1021/acsomega.4c06879
Vráblová, L., Majerová, P., Pindjaková, D., Goněc, T., Kováč, A., Čížek, A., & Jampílek, J. (2024) · doi:10.3390/ecsoc-28-20152
Chemical Proteomics Identifies Protein Ligands for Monoacylglycerol LipidsPreprint
Shanbhag, K., Mhetre, A. B., Saharan, O., Devarajan, A., Rai, A., Madhusudhan, M. S., Chakrapani, H., & Kamat, S. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.22.629584
Mass Spectrometry-Based Methods in CNS Drug Discovery
Blasco, G., Schreiber, R., & van Kruining, D. (2024) · Springer eBooks · doi:10.1007/978-3-031-61992-2_6
Chemoproteomics Approaches for Diverse Modalities
Eberl, H. C., Knecht, S., Queisser, M. A., & Bantscheff, M. (2025) · Wiley eBooks · doi:10.1002/9781394236145.ch19
Scaling Covalent Ligand Discovery via Library-Versus-Proteome ScreeningPreprint
Huang, Y., Hou, L., He, R., Zhu, L. F., Xu, C., Duan, S., Hu, J. Z., Yang, X., Tsai, Y., Wang, C., et al. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5397846
Molecular Dynamics-Guided Design and Chemoproteomic Profiling of Covalent Kinase Activity ProbesPreprint
Chakraborty, P., Carlos, A. J., Thomas, T., Ghaby, K., Fathi, S., Sharma, M., Nguyen, N. K., Farmwald, M., Blachowicz, L., Yu, S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.17.683178
Self-citationChemoproteomic profiling of itaconate-derived protein modifications
Wang, Y. S., & Wang, C. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2026.08.016
Chemoproteomics in covalent cancer drug discovery
Ong, J.-P., Dalziel, M., Johns, D., Zhu, J., & Bertoldo, J. B. (2026) · Drug Discovery Today · doi:10.1016/j.drudis.2026.104817
Progress and challenges in traceless ligand-directed labelling chemistry
Hopkinson, T., Cox, L. R., & Wilson, A. J. (2026) · Communications Chemistry · doi:10.1038/s42004-026-02222-0
Qiu, J., Bosch, M. A., Wolfe, M. S., Korać, K., Rizzo, S., Stincic, T. L., Farley, S. E., Fitzgerald, W., Rajendran, M., Laguerre, A., et al. (2026) · eLife · doi:10.7554/elife.111731.2
BindingDB (2025) · UC San Diego · doi:10.7270/q2vm4hvh
BindingDB Entry 50045445: Target engagement in lead generation.
BindingDB (2016) · UC San Diego · doi:10.7270/q28s4rmq
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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