The promise and peril of chemical probes

Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action

Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652

Specificity and mechanism of action of some commonly used protein kinase inhibitors

DAVIES, S. P., Reddy, H., Caivano, M., & Cohen, P. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510095 · Cited by 4,366

A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002).

Vlahos, C. J., Matter, W. F., Hui, K. Y., & Brown, R. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37680-9 · Cited by 3,248

Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide-dependent protein kinase and protein kinase C

Hidaka, H., Inagaki, M., Kawamoto, S., & Sasaki, Y. (1984) · Biochemistry · doi:10.1021/bi00316a032 · Cited by 2,688

Staurosporine, a potent inhibitor of phospholipidCa++dependent protein kinase

Tamaoki, T., Nomoto, H., TAKAHASHI, I., Kato, Y., Morimoto, M., & Tomita, F. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(86)90008-2 · Cited by 2,452

Monitoring Drug Target Engagement in Cells and Tissues Using the Cellular Thermal Shift Assay

Molina, D. M., Jafari, R., Ignatushchenko, M., Seki, T., Larsson, E. A., Dan, C., Sreekumar, L., Cao, Y., & Nordlund, P. (2013) · Science · doi:10.1126/science.1233606 · Cited by 2,261

Click Chemistry for Drug Development and Diverse Chemical–Biology Applications

Prakasam, T., Matosiuk, D., & Jóźwiak, K. (2013) · Chemical Reviews · doi:10.1021/cr200409f · Cited by 1,933

Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells

Göttlicher, M., Minucci, S., Zhu, P., Krämer, O. H., Schimpf, A., Giavara, S., Sleeman, J. P., Coco, F. L., Nervi, C., Pelicci, P. G., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.6969 · Cited by 1,930

Targeting bromodomains: epigenetic readers of lysine acetylation

Filippakopoulos, P., & Knapp, S. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4286 · Cited by 1,298

Dorsomorphin inhibits BMP signals required for embryogenesis and iron metabolism

Yu, P. B., Hong, C. C., Sachidanandan, C., Babitt, J. L., Deng, D. Y., Hoyng, S. A., Lin, H. Y.-F., Bloch, K. D., & Peterson, R. T. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.54 · Cited by 1,059

The European Federation for Medicinal Chemistry (EFMC) Best Practice Initiative: Validating Chemical Probes

Quancard, J., Cox, B., Finsinger, D., Guéret, S. M., Hartung, I. V., Koolman, H. F., Messinger, J., Sbardella, G., & Laufer, S. (2020) · ChemMedChem · doi:10.1002/cmdc.202000597 · Cited by 17

Transcriptome screening followed by integrated physicochemical and structural analyses for investigating RNA-mediated berberine activity

Satpathi, S., Endoh, T., Podbevšek, P., Plavec, J., & Sugimoto, N. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab189 · Cited by 17

Small molecules targeting Mcl-1: the search for a silver bullet in cancer therapy

Nhu, D., Lessène, G., Huang, D. C. S., & Burns, C. J. (2016) · MedChemComm · doi:10.1039/c5md00582e · Cited by 16

A grafted ovarian fragment rescues host fertility after chemotherapy

Batchvarov, I. S., Taylor, R. W., Bustamante-Marin, X. M., Czerwinski, M. J., Johnson, E. S., Kornbluth, S. A., & Capel, B. (2016) · Molecular Human Reproduction · doi:10.1093/molehr/gaw064 · Cited by 16

Discovery and pharmacology of the covalent GLP-1 receptor (GLP-1R) allosteric modulator BETP: A novel tool to probe GLP-1R pharmacology

Willard, F. S., Ho, J. D., & Sloop, K. W. (2020) · Advances in pharmacology · doi:10.1016/bs.apha.2020.02.001 · Cited by 17

Affinity Enhancement of Protein Ligands by Reversible Covalent Modification of Neighboring Lysine Residues

Corso, A. D., Catalano, M., Schmid, A. S., Scheuermann, J., & Neri, D. (2018) · Angewandte Chemie · doi:10.1002/ange.201811650 · Cited by 19

The Ecstasy and Agony of Assay Interference Compounds

Aldrich, C. C., Bertozzi, C. R., Georg, G. I., Kiessling, L. L., Lindsley, C. W., Liotta, D. C., Merz, K. M., Schepartz, A., & Wang, S. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00064 · Cited by 17

ortho ‐Boronic Acid Carbonyl Compounds and Their Applications in Chemical Biology**

Haggett, J. G., & Domaille, D. W. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202302485 · Cited by 16

ChemFH: an integrated tool for screening frequent false positives in chemical biology and drug discovery

Shi, S., Fu, L., Yi, J., Yang, Z., Zhang, X., Deng, Y., Wang, W., Wu, C., Zhao, W., Hou, T., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae424 · Cited by 16

Mapping biologically active chemical space to accelerate drug discovery

Sittampalam, G. S., Rudnicki, D. D., Tagle, D. A., Simeonov, A. M., & Austin, C. P. (2018) · Nature Reviews Drug Discovery · doi:10.1038/d41573-018-00007-2 · Cited by 16

Recent developments in ligands and chemical probes targeting solute carrier transporters

Casiraghi, A., Bensimon, A., & Superti‐Furga, G. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.01.012 · Cited by 16

Will the chemical probes please stand up?

Škuta, C., Southan, C., & Bartůněk, P. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00138h · Cited by 17

Precision Oncology Comes of Age: Designing Best-in-Class Small Molecules by Integrating Two Decades of Advances in Chemistry, Target Biology, and Data Science

Stuart, D. D., Guzman-Perez, A., Brooijmans, N., Jackson, E. L., Kryukov, G. V., Friedman, A. A., & Hoos, A. (2023) · Cancer Discovery · doi:10.1158/2159-8290.cd-23-0280 · Cited by 19

Structure-guided design of a selective inhibitor of the methyltransferase KMT9 with cellular activity

Wang, S., Klein, S. O., Urban, S., Staudt, M., Barthes, N. P. F., Willmann, D., Bacher, J., Sum, M., Bauer, H., Peng, L., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44243-6 · Cited by 16

Bacterial Expression and HTS Assessment of Soluble Epoxide Hydrolase Phosphatase

Klingler, F., Wolf, M., Wittmann, S. K., Gribbon, P. M., & Proschak, E. (2016) · SLAS DISCOVERY · doi:10.1177/1087057116637609 · Cited by 16

Recent developments of small molecule chemical probes for fluorescence-based detection of human carbonic anhydrase II and IX

Teruya, K., Tonissen, K. F., & Poulsen, S. (2016) · MedChemComm · doi:10.1039/c6md00296j · Cited by 16

Development of chemical probes for the bromodomains of BRD7 and BRD9

Clark, P. G. K., Dixon, D. J., & Brennan, P. E. (2016) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2016.05.002 · Cited by 16

Selectivity aspects of activity-based (chemical) probes

Heinzlmeir, S., & Müller, S. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.10.021 · Cited by 17

The Ecstasy and Agony of Assay Interference Compounds

Aldrich, C. C., Bertozzi, C. R., Georg, G. I., Kiessling, L. L., Lindsley, C. W., Liotta, D. C., Merz, K. M., Schepartz, A., & Wang, S. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00119 · Cited by 16

The SGC beyond structural genomics: redefining the role of 3D structures by coupling genomic stratification with fragment-based discovery

Bradley, A. R., Echalier, A., Fairhead, M., Strain-Damerell, C. M., Brennan, P. E., Bullock, A. N., Burgess-Brown, N., Carpenter, E. P., Gileadi, O., Marsden, B. D., et al. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170051 · Cited by 15

Chemical Instability and Promiscuity of Arylmethylidenepyrazolinone-Based MDMX Inhibitors

Stefaniak, J., Lewis, A. M., Conole, D., Galan, S. R. G., Bataille, C. J. R., Wynne, G. M., Castaldi, M. P., Lundbäck, T., Russell, A. J., & Huber, K. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00665 · Cited by 16

Fixing Misallocation with Guidelines: Awareness vs. Adherence

Abaluck, J., Agha, L., Chan, D. C., Singer, D. E., & Zhu, D. (2020) · National Bureau of Economic Research · doi:10.3386/w27467 · Cited by 16

Decoupling Activation of Heme Biosynthesis from Anaerobic Toxicity in a Molecule Active in Staphylococcus aureus

Dutter, B. F., Mike, L. A., Reid, P. R., Chong, K. M., Ramos-Hunter, S. J., Skaar, E. P., & Sulikowski, G. A. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.5b00934 · Cited by 14

Virtual library docking for cannabinoid-1 receptor agonists with reduced side effects

Tummino, T. A., Iliopoulos‐Tsoutsouvas, C., Braz, J. M., O’Brien, E. S., Stein, R. M., Craik, V., Tran, N. K., Ganapathy, S., Liu, F., Shiimura, Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-57136-7 · Cited by 25

Latest Advances Towards Ras Inhibition: A Medicinal Chemistry Perspective

Sautier, B., Nising, C. F., & Wortmann, L. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201608270 · Cited by 15

Data Mining and Computational Modeling of High-Throughput Screening Datasets

Ekins, S., Clark, A. M., Dole, K., Gregory, K., McNutt, A. M., Spektor, A. C., Weatherall, C., Litterman, N. K., & Bunin, B. A. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7724-6_14 · Cited by 16

Labelled Chemical Probes for Demonstrating Direct Target Engagement in Living Systems

Prevet, H., & Collins, I. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0370 · Cited by 15

EFMC: Trends in Medicinal Chemistry and Chemical Biology

Auberson, Y. P., Arimondo, P. B., Duca, M., Essig, S., Grether, U., Rufer, A. C., Sbardella, G., Schopfer, U., Torrens, A., van der Stelt, M., et al. (2023) · ChemBioChem · doi:10.1002/cbic.202200690 · Cited by 16

CZ415, a Highly Selective mTOR Inhibitor Showing in Vivo Efficacy in a Collagen Induced Arthritis Model

Cansfield, A. D., Ladduwahetty, T., Sunose, M., Ellard, K., Lynch, R., Newton, A., Lewis, A., Bennett, G. S., Zinn, N., Thomson, D. W., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00149 · Cited by 15

Glycogen Synthase Kinase 3β Promotes the Endocytosis of Transferrin in the African Trypanosome

Guyett, P. J., Xia, S., Swinney, D. C., Pollastri, M. P., & Mensa‐Wilmot, K. (2016) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00077 · Cited by 15

Phosphate Chemical Probes Designed for Location Specific Inhibition of Intracellular Carbonic Anhydrases

Rankin, G. M., Vullo, D., Supuran, C. T., & Poulsen, S. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01228 · Cited by 15

The Elements of Translational Chemical Biology

Copeland, R. A., & Boriack‐Sjodin, P. A. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.11.003 · Cited by 15

‘Design, synthesis, and strategic use of small chemical probes toward identification of novel targets for drug development’

Castaldi, M. P., Hendricks, J. A., & Zhang, A. X. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.03.003 · Cited by 15

Targeting the Water Network in Cyclin G‐Associated Kinase (GAK) with 4‐Anilino‐quin(az)oline Inhibitors

Asquith, C. R. M., Tizzard, G. J., Bennett, J. M., Wells, C. I., Elkins, J. M., Willson, T. M., Poso, A., & Laitinen, T. (2020) · ChemMedChem · doi:10.1002/cmdc.202000150 · Cited by 15

MSC-1186, a Highly Selective Pan-SRPK Inhibitor Based on an Exceptionally Decorated Benzimidazole-Pyrimidine Core

Schröder, M., Leiendecker, M., Grädler, U., Braun, J., Blum, A., Wanior, M., Berger, B., Krämer, A., Müller, S., Esdar, C., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01705 · Cited by 14

Comparison of CX-4945 and SGC-CK2-1 as inhibitors of CSNK2 using quantitative phosphoproteomics: Triple SILAC in combination with inhibitor-resistant CSNK2

Menyhart, D., Gyenis, L., Jurčić, K., Roffey, S. E., Puri, A., Jovanović, P., Szkop, K. J., Pittock, P., Lajoie, G., Axtman, A. D., et al. (2023) · Current Research in Chemical Biology · doi:10.1016/j.crchbi.2023.100041 · Cited by 15

Structure-Guided Design of a Domain-Selective Bromodomain and Extra Terminal N-Terminal Bromodomain Chemical Probe

Bradley, E. K., Fusani, L., Chung, C., Craggs, P. D., Demont, E. H., Humphreys, P. G., Mitchell, D. J., Phillipou, A., Rioja, I., Shah, R. R., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00906 · Cited by 14

Chemogenomics for NR1 nuclear hormone receptors

Isigkeit, L., Schallmayer, E., Busch, R., Brunello, L., Menge, A., Elson, L., Müller, S., Knapp, S., Stolz, A., Marschner, J. A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49493-6 · Cited by 14

Reconciling Selectivity Trends from a Comprehensive Kinase Inhibitor Profiling Campaign with Known Activity Data

Miljković, F. N., & Bajorath, J. (2018) · ACS Omega · doi:10.1021/acsomega.8b00243 · Cited by 14

Selective Inhibitors of a Human Prolyl Hydroxylase (OGFOD1) Involved in Ribosomal Decoding

Thinnes, C. C., Lohans, C. T., Abboud, M. I., Yeh, T., Tumber, A., Nowak, R. P., Attwood, M., Cockman, M. E., Oppermann, U. C. T., Loenarz, C., et al. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201804790 · Cited by 13

A High-Throughput BRET Cellular Target Engagement Assay Links Biochemical to Cellular Activity for Bruton’s Tyrosine Kinase

Ong, L. L., Vasta, J. D., Monereau, L., Locke, G. A., Ribeiro, H., Pattoli, M. A., Skala, S., Burke, J. R., Watterson, S. H., Tino, J. A., et al. (2019) · SLAS DISCOVERY · doi:10.1177/2472555219884881 · Cited by 14

Pharmacological Tool Compounds for the Free Fatty Acid Receptor 4 (FFA4/GPR120)

Hansen, S. V. F., & Ulven, T. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_60 · Cited by 14

The right tools for the job: the central role for next generation chemical probes and chemistry-based target deconvolution methods in phenotypic drug discovery

Jörg, M., & Madden, K. S. (2021) · RSC Medicinal Chemistry · doi:10.1039/d1md00022e · Cited by 14

Discovery of a PCAF Bromodomain Chemical Probe

Moustakim, M., Clark, P. G. K., Trulli, L., de Arriba, A. L. F., Ehebauer, M. T., Chaikuad, A., Murphy, E. J., Méndez, J., Daniels, D. L., Hou, C.-F. D., et al. (2016) · Angewandte Chemie · doi:10.1002/ange.201610816 · Cited by 14

Multivalent interactions with CCR4–NOT and PABPC1 determine mRNA repression efficiency by tristetraprolin

Pekovic, F., Lai, W. S., Corbo, J. H., Hicks, S. N., Luke, K., Blackshear, P. J., & Valkov, E. (2025) · Nature Communications · doi:10.1038/s41467-025-62741-7 · Cited by 15

Combining nano-differential scanning fluorimetry and microscale thermophoresis to investigate VDAC1 interaction with small molecules

Gorny, H., Mularoni, A., Delcros, J., Freton, C., Preto, J., & Krimm, I. (2023) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2022.2121821 · Cited by 15

Chirality: a key parameter in chemical probes

McGown, A., Nafie, J., Otayfah, M., Hassell‐Hart, S., Tizzard, G. J., Coles, S. J., Banks, R., Marsh, G. P., Maple, H. J., Κostakis, G. E., et al. (2023) · RSC Chemical Biology · doi:10.1039/d3cb00082f · Cited by 13

A split-luciferase lysate-based approach to identify small-molecule modulators of phosphatase subunit interactions

Claes, Z., & Bollen, M. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.07.018 · Cited by 11

CK2 Chemical Probes: Past, Present, and Future

Ong, H. W., Drewry, D. H., & Axtman, A. D. (2023) · Kinases and Phosphatases · doi:10.3390/kinasesphosphatases1040017 · Cited by 14

Deorphanization strategies for dark chemical matter

Wassermann, A. M., Tudor, M., & Glick, M. (2017) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2016.11.004 · Cited by 13

Efficient Entropy‐Driven Inhibition of Dipeptidyl Peptidase III by Hydroxyethylene Transition‐State Peptidomimetics

Ivković, J., Jha, S., Lembacher‐Fadum, C., Puschnig, J., Kumar, P., Reithofer, V., Gruber, K. F., Macheroux, P., & Breinbauer, R. (2021) · Chemistry - A European Journal · doi:10.1002/chem.202102204 · Cited by 12

Structure-guided drug discovery: back to the future

Arrowsmith, C. H. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01244-3 · Cited by 13

Tubulin is a molecular target of the Wnt-activating chemical probe

Fukuda, Y., Sano, O., Kazetani, K., Yamamoto, K., Iwata, H., & Matsui, J. (2016) · BMC Biochemistry · doi:10.1186/s12858-016-0066-9 · Cited by 12

Development of small molecule inhibitors of BRPF1 and TRIM24 bromodomains

Palmer, W. S. (2016) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2016.06.005 · Cited by 13

Evaluating and evolving a screening library in academia: the St Jude approach

Nishiguchi, G., Das, S., Ochoada, J., Long, H., Lee, R. E., Jr., Ranković, Z., & Shelat, A. A. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.01.005 · Cited by 14

Public–Private Partnerships in Lead Discovery: Overview and Case Studies

Gottwald, M., Becker, A., Bahr, I., & Mueller‐Fahrnow, A. (2016) · Archiv der Pharmazie · doi:10.1002/ardp.201600078 · Cited by 13

Discovery of a Chemical Probe to Study Implications of BPTF Bromodomain Inhibition in Cellular and in vivo Experiments

Martinelli, P., Schaaf, O., Mantoulidis, A., Martin, L. J., Fuchs, J. E., Bader, G., Gollner, A., Wolkerstorfer, B., Rogers, C. M., Balıkçı, E., et al. (2023) · ChemMedChem · doi:10.1002/cmdc.202200686 · Cited by 12

Paralog-dependent isogenic cell assay cascade generates highly selective SLC16A3 inhibitors

Dvorak, V., Casiraghi, A., Colas, C., Koren, A., Tomek, T., Offensperger, F., Rukavina, A., Tin, G., Hahn, E., Dobner, S., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.06.029 · Cited by 12

Highly Specific Miniaturized Fluorescent Monoacylglycerol Lipase Probes Enable Translational Research

Hentsch, A., Guberman, M., Radetzki, S., Kaushik, S., Huizenga, M. C. W., He, Y., Contzen, J., Kuhn, B., Benz, J., Schippers, M., et al. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c15223 · Cited by 13

Meeting the Challenge: Using Cytological Profiling to Discover Chemical Probes from Traditional Chinese Medicines against Parkinson’s Disease

Wang, C., Yang, X., Mellick, G. D., & Feng, Y. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00245 · Cited by 12

Ein Instrumentarium von αv‐RGD‐Integrin‐Inhibitoren: Wirkstoffsuche, Herausforderungen und Möglichkeiten

Hatley, R. J. D., Macdonald, S. J. F., Slack, R. J., Le, J., Ludbrook, S. B., & Lukey, P. T. (2017) · Angewandte Chemie · doi:10.1002/ange.201707948 · Cited by 13

Probing Embryonic Development Enables the Discovery of Unique Small-Molecule Bone Morphogenetic Protein Potentiators

Wesseler, F., Riege, D., Puthanveedu, M., Halver, J., Müller, E., Bertrand, J., Antonchick, A. P., Sievers, S., Waldmann, H., & Schade, D. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01800 · Cited by 12

Combinatorial Anticancer Drug Screen Identifies Off-Target Effects of Epigenetic Chemical Probes

Barghout, S. H., Mann, M. K., Aman, A. M., Yu, Y., Alteen, M. G., Schimmer, A. D., Schapira, M., Arrowsmith, C. H., & Baršytė-Lovejoy, D. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00451 · Cited by 12

Rational Design of a New RXR Agonist Scaffold Enabling Single-Subtype Preference for RXRα, RXRβ, and RXRγ

Adouvi, G., Isigkeit, L., López-García, Ú., Chaikuad, A., Marschner, J. A., Schubert‐Zsilavecz, M., & Merk, D. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01266 · Cited by 12

New 1,2-Dihydropyridine-Based Fluorophores and Their Applications as Fluorescent Probes

Jamsheena, V., Mishra, R. K., Veena, K. S., Sini, S., Jayamurthy, P., & Lankalapalli, R. S. (2018) · ACS Omega · doi:10.1021/acsomega.7b01835 · Cited by 12

Target Identification Using Chemical Probes.

Moustakim, M., Felce, S., Zaarour, N., Farnie, G., McCann, F., & Brennan, P. (2018) · Methods in Enzymology · doi:10.1016/bs.mie.2018.09.013 · Cited by 9

Pharmacological Modulation of Transcriptional Coregulators in Cancer

Bishop, T. R., Zhang, Y., & Erb, M. A. (2019) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2019.04.004 · Cited by 11

Erratum: Corrigendum: The promise and peril of chemical probes

Arrowsmith, C. H., Audia, J. E., Austin, C. P., Baell, J. B., Bennett, J., Blagg, J., Bountra, C., Brennan, P. E., Brown, P. J., Bunnage, M. E., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio1115-887c · Cited by 12

Chemical genetics and strigolactone perception

Lumba, S., Bunsick, M., & McCourt, P. (2017) · F1000Research · doi:10.12688/f1000research.11379.1 · Cited by 11

Characterizing the role of the dark kinome in neurodegenerative disease – A mini review

Axtman, A. D. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.130014 · Cited by 11

Dbf4-Cdc7 (DDK) Inhibitor PHA-767491 Displays Potent Anti-Proliferative Effects via Crosstalk with the CDK2-RB-E2F Pathway

Pauzaite, T., Tollitt, J., Sopaci, B., Caprani, L., Iwanowytsch, O., Thacker, U., Hardy, J. G., Allinson, S. L., & Copeland, N. A. (2022) · Biomedicines · doi:10.3390/biomedicines10082012 · Cited by 11

Discovery of a 53BP1 Small Molecule Antagonist Using a Focused DNA-Encoded Library Screen

Shell, D. J., Foley, C. A., Wang, Q., Smith, C. M., Guduru, S. K. R., Zeng, H., Dong, A., Norris-Drouin, J. L., Axtman, M., Hardy, P. B., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01192 · Cited by 12

A drug‐resistant mutation in plant target of rapamycin validates the specificity of ATP ‐competitive TOR inhibitors in vivo

Perdoux, R., Barrada, A., Boulaiz, M., Garau, C., Belbachir, C., Lecampion, C., Montané, M., & Menand, B. (2023) · The Plant Journal · doi:10.1111/tpj.16564 · Cited by 11

Illumination of understudied ciliary kinases

Flax, R. G., Rosston, P., Rocha, C., Anderson, B. M., Capener, J. L., Durcan, T. M., Drewry, D. H., Prinos, P., & Axtman, A. D. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1352781 · Cited by 10

Unveiling the potential of phytochemicals to inhibit nuclear receptor binding SET domain protein 2 for cancer: Pharmacophore screening, molecular docking, ADME properties, and molecular dynamics simulation investigations

Mohamed, G. A., Abdallah, H. M., Sindi, I. A., Ibrahim, S. R. M., & Alzain, A. A. (2024) · PLoS ONE · doi:10.1371/journal.pone.0308913 · Cited by 11

Extrapolating Lessons from Targeted Protein Degradation to Other Proximity-Inducing Drugs

Winter, G. E. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00191 · Cited by 13

Enhanced motivated behavior mediated by pharmacological targeting of the FGF14/Nav1.6 complex in nucleus accumbens neurons

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Discovery of Potent Peptidomimetic Antagonists for Heterochromatin Protein 1 Family Proteins

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Development of Chaetocin and S ‐Adenosylmethionine Analogues as Tools for Studying Protein Methylation

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The Ecstasy and Agony of Assay Interference Compounds

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Covalent Ligand Electrophiles Are Differentially Activated by Proximity Effects Which Govern Latent Protein Reactivity

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Fragment‐Based Drug Discovery of Novel High‐affinity, Selective, and Anti‐inflammatory Inhibitors of the Keap1‐Nrf2 Protein‐Protein Interaction

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A machine learning and live-cell imaging tool kit uncovers small molecules induced phospholipidosis

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DMSO‐Related Effects on Ligand‐Binding Properties of Lysine Methyltransferases G9a and SETD8

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Establishing a reliable framework for harnessing the creative power of the scientific crowd

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More Haste, Less Speed: Could Public–Private Partnerships Advance Cellular Immunotherapies?

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Reagent Validation to Facilitate Experimental Reproducibility

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