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

Enhancer of Zeste Homolog 2 (EZH2) Contributes to Rod Photoreceptor Death Process in Several Forms of Retinal Degeneration and Its Activity Can Serve as a Biomarker for Therapy Efficacy

Mbefo, M. K., Berger, A., Schouwey, K., Gérard, X., Kostic, C., Beryozkin, A., Sharon, D., Dolfuss, H., Munier, F. L., Tran, H. V., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179331 · Cited by 10

Covalent‐Allosteric Inhibitors to Achieve Akt Isoform‐Selectivity

Quambusch, L., Landel, I., Depta, L., Weisner, J., Uhlenbrock, N., Müller, M. P., Glanemann, F., Althoff, K., Siveke, J. T., & Rauh, D. (2019) · Angewandte Chemie · doi:10.1002/ange.201909857 · Cited by 10

A conversation on using chemical probes to study protein function in cells and organisms

(2022) · Nature Communications · doi:10.1038/s41467-022-31271-x · Cited by 10

Changes in cell morphology guide identification of tubulin as the off-target for protein kinase inhibitors

Hoque, M., Abbassi, R. H., Froio, D., Man, J., Johns, T. G., Stringer, B. W., Day, B. W., Pajic, M., Kassiou, M., & Munoz, L. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.06.023 · Cited by 11

Crowdsourced mapping extends the target space of kinase inhibitorsPreprint

Cichońska, A., Ravikumar, B., Allaway, R. J., Park, S., Wan, F., Isayev, O., Li, S., Mason, M. J., Lamb, A. E., Tanoli, Z., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2019.12.31.891812 · Cited by 10

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 Infectious Diseases · doi:10.1021/acsinfecdis.7b00023 · Cited by 10

Design and synthesis of efficient fluororethylene-peptidomimetic inhibitors of dipeptidyl peptidase III (DPP3)

Podversnik, H., Jha, S., Macheroux, P., & Breinbauer, R. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116831 · Cited by 9

Open resources for chemical probes and their implications for future drug discovery

Balıkçı, E., Marques, A.-S. M. C., Hansen, J. S., & Huber, K. (2023) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2023.2199979 · Cited by 11

Tudor-Containing Methyl-Lysine and Methyl-Arginine Reader Proteins: Disease Implications and Chemical Tool Development

Uguen, M., Liu, T., James, L. I., & Frye, S. V. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00661 · Cited by 9

Hydrazonophenol, a Food Vacuole-Targeted and Ferriprotoporphyrin IX-Interacting Chemotype Prevents Drug-Resistant Malaria

Saha, S. J., Siddiqui, A. A., Pramanik, S., Saha, D., De, R., Mazumder, S., Debsharma, S., Nag, S., Banerjee, C., & Bandyopadhyay, U. (2018) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.8b00178 · Cited by 8

Unveiling (−)‐Englerin A as a Modulator of L‐Type Calcium Channels

Rodrigues, T., Sieglitz, F., Somovilla, V. J., Cal, P. M. S. D., Galione, A., Corzana, F., & Bernardes, G. J. L. (2016) · Angewandte Chemie · doi:10.1002/ange.201604336 · Cited by 9

Mannich Base PIP-199 Is a Chemically Unstable Pan-Assay Interference Compound

Wu, X., Sudhakar, H. K., Alcock, L. J., & Lau, Y. H. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00674 · Cited by 9

Modular Nanotransporters Delivering Biologically Active Molecules to the Surface of Mitochondria

Khramtsov, Y. V., Ulasov, A. V., Slastnikova, T. A., Rosenkranz, A. A., Lupanova, T. N., Georgiev, G. P., & Sobolev, A. S. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15122687 · Cited by 8

The first international workshop on the epigenetics of osteoarthritis

Meulenbelt, I., Bhutani, N., den Hollander, W., Gay, S., Oppermann, U., Reynard, L., Skelton, A., Young, D., Beier, F., & Loughlin, J. (2017) · Connective Tissue Research · doi:10.3109/03008207.2016.1168409 · Cited by 8

Molecular Modeling and Chemoinformatics to Advance the Development of Modulators of Epigenetic Targets

Prieto-Martínez, F. D., Peña‐Castillo, A., Méndez‐Lucio, O., Gortari, E. F., & Medina‐Franco, J. L. (2016) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2016.05.001 · Cited by 8

Defining Metabolic and Nonmetabolic Regulation of Histone Acetylation by NSAID Chemotypes

Shrimp, J. H., Garlick, J. M., Tezil, T., Sorum, A. W., Worth, A. J., Blair, I. A., Verdin, E. M., Snyder, N. W., & Meier, J. L. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.7b00943 · Cited by 9

Repurposing the Damage Repair Protein Methyl Guanine Methyl Transferase as a Ligand Inducible Fusion Degron

Murawska, G. M., Vogel, C., Jan, M., Lu, X., Schild, M., Slabicki, M. M., Zou, C., Zhanybekova, S., Manojkumar, M., Petzold, G., et al. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.1c00771 · Cited by 9

Chemical synthesis of a reported p47phox/p22phox inhibitor and characterization of its instability and irreproducible activity

Zang, J., Cambet, Y., Jaquet, V., & Bach, A. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1075328 · Cited by 9

Focusing on probe-modified peptides: a quick and effective method for target identification

Sun, H., Ren, Y., Hou, W., Li, L., Zeng, F., Li, S., Ma, Y., Liu, X., Chen, S., & Zhang, Z. (2016) · Chemical Communications · doi:10.1039/c6cc04030f · Cited by 9

Rational Adaptation of L3MBTL1 Inhibitors to Create Small‐Molecule Cbx7 Antagonists

Simhadri, C., Daze, K. D., Douglas, S. F., Milosevich, N., Monjas, L., Dev, A., Brown, T. M., Hirsch, A. K. H., Wulff, J. E., & Hof, F. A. (2019) · ChemMedChem · doi:10.1002/cmdc.201900021 · Cited by 9

The chemical probe – scopes, limitations and challenges

Stark, H. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1781086 · Cited by 9

Phenotypic Screening of Chemical Libraries Enriched by Molecular Docking to Multiple Targets Selected from Glioblastoma Genomic Data

Xu, D. D., Zhou, D., Bum‐Erdene, K., Bailey, B. J., Sishtla, K. L., Liu, S., Wan, J., Aryal, U. K., Lee, J. A., Wells, C. D., et al. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00078 · Cited by 8

Recommended Tool Compounds: Thienotriazolodiazepines-Derivatized Chemical Probes to Target BET Bromodomains

Huang, C., Harris, C. L., Siddiqui, G., & Jörg, M. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00726 · Cited by 8

Enhancing Selectivity and Potency of S N Ar Covalent Inhibitors of NADPH Oxidase Enzymes

Ogboo, B. C., Patel, K. B., Massari, M., Marchese, S., Reis, J., Joyce, E. J., Lin, M.-C. J., Rabb, J. D., Abidakun, O. A., Lin, Q., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01272 · Cited by 8

A general one-step protocol to generate impermeable fluorescent HaloTag substrates for in situ live cell application and super-resolution imaging

Roßmann, K., Pabst, U., Baciu, B. C., Sun, S., Huhn, C., Olesen, C. H., Kowald, M., Tapp, E., Bieck, M., Birke, R., et al. (2026) · Nature Communications · doi:10.1038/s41467-025-68134-0 · Cited by 9

Optimization of the 4-anilinoquin(az)oline scaffold as epidermal growth factor receptor (EGFR) inhibitors for chordoma utilizing a toxicology profiling assay platform

Bieberich, A. A., Laitinen, T., Maffuid, K., Fatig, R. O., Torrice, C., Morris, D. C., Crona, D. J., & Asquith, C. R. M. (2022) · Scientific Reports · doi:10.1038/s41598-022-15552-5 · Cited by 9

Small-Molecule Probes as Pharmacological Tools for the Bone Morphogenetic Protein Signaling Pathway

Riege, D., Herschel, S., Fenkl, T., & Schade, D. (2023) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00170 · Cited by 9

Rapid, potent, and persistent covalent chemical probes to deconvolute PI3Kα signaling

Bissegger, L., Constantin, T. A., Keleş, E., Raguž, L., Barlow-Busch, I., Orbegozo, C., Schaefer, T., Borlandelli, V., Bohnacker, T., Sriramaratnam, R., et al. (2024) · Chemical Science · doi:10.1039/d4sc05459h · Cited by 9

A Small‐Molecule Drug for the Self‐Checking of Mitophagy

Gao, Y., Bai, Q., Ren, Y., Shao, X., Zhang, M., Wu, L., Lewis, S. E., James, T. D., Chen, X. S., & Chen, Q. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202421269 · Cited by 8

Potential of Enzymomics Methodologies to Characterize Disease-Related Protein Functions

Komatsu, T. (2017) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c17-00144 · Cited by 8

Anti-Inflammatory Properties of Chemical Probes in Human Whole Blood: Focus on Prostaglandin E2 Production

Bergqvist, F., Sundström, Y., Shang, M.-M., Gunnarsson, I., Lundberg, I. E., Sundström, M., Jakobsson, P., & Berg, L. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00613 · Cited by 8

Industrial Organic Synthesis in Life Sciences – Today and Tomorrow

Nising, C. F., & von Nussbaum, F. (2022) · European Journal of Organic Chemistry · doi:10.1002/ejoc.202200252 · Cited by 8

ChemBioPort: an online portal to navigate the structure, function and chemical inhibition of the human proteome

Liu, L., Rovers, E., & Schapira, M. (2022) · Database · doi:10.1093/database/baac088 · Cited by 8

Distinct phases of cellular signaling revealed by time-resolved protein synthesis

Lee, G., & Muir, T. W. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01677-3 · Cited by 10

Interpreting the behavior of concentration–response curves of hyaluronidase inhibitors under DMSO-perturbed assay conditions

Tomohara, K., Ito, T., Onikata, S., Furusawa, K., Kato, A., & Adachi, I. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.04.082 · Cited by 8

HIV and HIV-Tat inhibit LPS-induced IL-27 production in human macrophages by distinct intracellular signaling pathways

Gajanayaka, N., O’Hara, S., Konarski, Y., Fernandes, J. R., Muthumani, K., Kozlowski, M., Angel, J. B., & Kumar, A. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.4a0716-332rr · Cited by 8

Chemical Proteomics for Target Discovery of Head-to-Tail Cyclized Mini-Proteins

Hellinger, R., Thell, K., Vasileva, M., Muhammad, T., Gunasekera, S., Kümmel, D., Göransson, U., Becker, C., & Gruber, C. W. (2017) · Frontiers in Chemistry · doi:10.3389/fchem.2017.00073 · Cited by 9

Identifying novel B-cell targets for chronic inflammatory autoimmune disease by screening of chemical probes in a patient-derived cell assay

Sundström, Y., Shang, M.-M., Panda, S. K., Grönwall, C., Wermeling, F., Gunnarsson, I., Lundberg, I. E., Sundström, M., Jakobsson, P., & Berg, L. (2020) · Translational research · doi:10.1016/j.trsl.2020.09.003 · Cited by 8

High-Throughput Screening (HTS) Technology

Roy, A. (2021) · Springer eBooks · doi:10.1007/978-3-030-57401-7_73 · Cited by 9

Discovery of a Potent, Selective, and Cell-Active SPIN1 Inhibitor

Xiong, Y., Greschik, H., Johansson, C., Seifert, L., Gamble, V., Park, K., Fagan, V., Li, F., Chau, I., Vedadi, M., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00121 · Cited by 7

Insights of affinity-based probes for target identification in drug discovery

Wang, H., Liu, L., Zhang, Z., Li, C., Wang, K., Gao, J., Hu, Q., Wang, W., & Li, H. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117711 · Cited by 7

Advances in BRET probes for intracellular target engagement studies

Capener, J. L., Schwalm, M. P., Vasta, J. D., Michaud, A., Teske, K. A., Marsiglia, W. M., Huber, K., Dar, A. C., Knapp, S., Axtman, A. D., et al. (2026) · Nature Chemical Biology · doi:10.1038/s41589-025-02103-y · Cited by 9

SOD1 lactylation impair its enzymatic activity by conformational change to aggravate intervertebral disc degeneration

Zhang, Y., Zhai, Y., Liu, C., Chen, M., Zhang, Y., Bian, Z., Chang, X., Hu, Z., Li, J., Zhang, C., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69127-3 · Cited by 9

Investigating impacts of the mycothiazole chemotype as a chemical probe for the study of mitochondrial function and aging

Dutta, N., Gerke, J. A., Odron, S. F., Morris, J. D., Hruby, A. J., Kim, J., Torres, T. C., Shemtov, S. J., Clarke, J. G., Chang, M. C., et al. (2024) · GeroScience · doi:10.1007/s11357-024-01144-w · Cited by 6

Identification and Benchmarking of Myokinasib-II as a Selective and Potent Chemical Probe for Exploring MLCK1 Inhibition

Kumar, G., Agarwala, P. K., Srivatsav, A. T., Ravula, A., Ashmitha, G., Balakrishnan, S., Kapoor, S., & Narayan, R. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00336 · 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

Use of AD Informer Set compounds to explore validity of novel targets in Alzheimer's disease pathology

Potjewyd, F., Annor‐Gyamfi, J. K., Aubé, J., Chu, S., Conlon, I. L., Frankowski, K. J., Guduru, S. K. R., Hardy, B. P., Hopkins, M. D., Kinoshita, C., et al. (2022) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12253 · Cited by 8

Applying HT-SAXS to chemical ligand screening

Brosey, C. A., Shen, R., Moiani, D., Jones, D. E., Burnett, K. H., Hura, G. L., & Tainer, J. A. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.09.022 · Cited by 7

Gasdermins assemble; recent developments in bacteriology and pharmacology

Greenwood, C. S., Wynosky-Dolfi, M. A., Beal, A. M., & Booty, L. M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1173519 · Cited by 6

Chemical Biology Approaches for Characterization of Epigenetic Regulators

Baršytė-Lovejoy, D., Szewczyk, M., Prinos, P., Lima‐Fernandes, E., Ackloo, S. Z., & Arrowsmith, C. H. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.01.011 · Cited by 7

Metal-binding effects of sirtuin inhibitor sirtinol

Akam, E. A., Gautam, R., & Tomat, E. (2015) · Supramolecular chemistry · doi:10.1080/10610278.2015.1092537 · Cited by 7

Design and Applications of Bifunctional Small Molecules in Biology

Boyd, S. R., Chang, L., de Rezende, W. C., Raji, I. O., Kandel, P., Holmes, S. L., & Young, D. W. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140534 · Cited by 7

Selective Inhibition of Cysteine-Dependent Enzymes by Bioorthogonal Tethering

Spear, L. A., Huang, Y., Chen, J., Nödling, A. R., Virdee, S., & Tsai, Y. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167524 · Cited by 7

EFMC, Medicinal Chemistry and Chemical Biology in Europe

Auberson, Y. P. (2020) · ChemMedChem · doi:10.1002/cmdc.202000178 · Cited by 7

Integrative GWAS and co-localisation analysis suggests novel genes associated with age-related multimorbidity

West, C. E., Karim, M. A., Falaguera, M. J., Speidel, L., Green, C., Logie, L., Schwartzentruber, J., Ochoa, D., Lord, J. M., Ferguson, M. A. J., et al. (2023) · Scientific Data · doi:10.1038/s41597-023-02513-4 · Cited by 8

Targeting LC3/GABARAP for degrader development and autophagy modulationPreprint

Schwalm, M. P., Dopfer, J., Kumar, A. M., Greco, F., Bauer, N., Löhr, F., Heering, J., Cano, S., Lechner, S., Hanke, T., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.05.560930 · Cited by 7

Discovery of a cell-active chikungunya virus nsP2 protease inhibitor using a covalent fragment-based screening approachPreprint

Merten, E. M., Sears, J. D., Leisner, T. M., Hardy, P. B., Ghoshal, A., Hossain, M. A., Asressu, K. H., Brown, P. J., Stashko, M. A., Herring, L. E., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.22.586341 · Cited by 7

Chaetocin disrupts the SUV39H1–HP1 interaction independent of SUV39H1 methyltransferase activity

Han, L., Lee, J. B., Indermaur, E. W., & Keung, A. J. (2023) · Biochemical Journal · doi:10.1042/bcj20220528 · Cited by 6

Chemical coverage of human biological pathways

Kwak, H. A., Liu, L., Tredup, C., Röhm, S., Prinos, P., Böttcher, J., & Schapira, M. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104144 · Cited by 6

Toward target 2035: EUbOPEN - a public–private partnership to enable & unlock biology in the open

Tredup, C., Ackloo, S. Z., Beck, H., Brown, P. J., Bullock, A. N., Ciulli, A., Đikić, I., Edfeldt, K., Edwards, A. M., Elkins, J. M., et al. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00735b · Cited by 6

On drug discovery against infectious diseases and academic medicinal chemistry contributions

Janin, Y. L. (2022) · Beilstein Journal of Organic Chemistry · doi:10.3762/bjoc.18.141 · Cited by 6

Improving data quality in chemical biology

Knapp, S., & Müller, S. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01449-5 · Cited by 6

Characterisation of Photoaffinity‐Based Chemical Probes by Fluorescence Imaging and Native‐State Mass Spectrometry

Teruya, K., Rankin, G. M., Chrysanthopoulos, P. K., Tonissen, K. F., & Poulsen, S. (2017) · ChemBioChem · doi:10.1002/cbic.201600598 · Cited by 6

The histone methyltransferase inhibitor A-366 enhances hemoglobin expression in erythroleukemia cells upon co‐exposure with chemical inducers in culture

Papagiannopoulos, C. I., Theodoroula, N. F., Kyritsis, K., Akrivou, M. G., Kosmidou, M. S., Tsouderou, K., Grigoriadis, N., & Vizirianakis, I. S. (2021) · Journal of Biological Research - Thessaloniki · doi:10.1186/s40709-020-00132-3 · Cited by 6

Insights on Targeting Small Molecules to the Mitochondrial Matrix and the Preparation of MitoB and MitoP as Exomarkers of Mitochondrial Hydrogen Peroxide

Cairns, A. G., McQuaker, S. J., Murphy, M. P., & Hartley, R. C. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1262-0_6 · Cited by 6

Epigenetic Modulators as Treatment Alternative to Diverse Types of Cancer

Gutiérrez, J. R., Salgado, A. R. M., De-Ávila-Arias, M., San-Juan-Vergara, H. G., Rosales, W., & Gomez, C. M. M. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867329666211228111036 · Cited by 6

Bioluminescent Zebrafish Transplantation Model for Drug Discovery

Hason, M., Jovicic, J., Vonkova, I., Bojic, M., Simon-Vermot, T., White, R. M., & Bartůněk, P. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.893655 · Cited by 6

Development of new 1, 3-dihydroxyacridone derivatives as Akt pathway inhibitors in skeletal muscle cells

Irazoqui, A. P., Menéndez, C. A., Steingruber, H. S., Gonzalez, A., Appignanesi, G. A., Buitrago, C., & Gerbino, D. C. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106222 · Cited by 6

Novel quinazolin-4(3H)-one based Cyclin K degraders regulate alternative polyadenylation activity

Sano, O., Ito, M., Saito, M., Toita, A., Tanaka, T., Maezaki, H., Araki, S., & Iwata, H. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.07.028 · Cited by 6

An Introduction to Chemogenomics

Chaikuad, A., & Merk, D. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3397-7_1 · Cited by 6

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

Development of Novel Phosphonodifluoromethyl-Containing Phosphotyrosine Mimetics and a First-In-Class, Potent, Selective, and Bioavailable Inhibitor of Human CDC14 Phosphatases

Dong, J., Jassim, B. A., Milholland, K. L., Qu, Z., Bai, Y., Miao, Y., Miao, J., Ma, Y., Lin, J., Hall, M. C., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00149 · Cited by 6

Non-substrate based, small molecule inhibitors of the human isoprenylcysteine carboxyl methyltransferase

Butler, K. V., Bohn, K. C., Hrycyna, C. A., & Jin, J. J. (2016) · MedChemComm · doi:10.1039/c6md00130k · Cited by 6

Probing biological mechanisms with chemical tools

Kang, C., & Keller, T. H. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104656 · Cited by 6

AD Informer Set: Chemical tools to facilitate Alzheimer's disease drug discovery

Potjewyd, F., Annor‐Gyamfi, J. K., Aubé, J., Chu, S., Conlon, I. L., Frankowski, K. J., Guduru, S. K. R., Hardy, B. P., Hopkins, M. D., Kinoshita, C., et al. (2022) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1002/trc2.12246 · Cited by 6

Effectively utilizing publicly available databases for cancer target evaluation

Croft, D. R., Lodhia, P., Lourenco, S. D. S., & MacKay, C. (2023) · NAR Cancer · doi:10.1093/narcan/zcad035 · Cited by 7

Reproducibility in Biomedical Research

Mullane, K., Curtis, M. J., & Williams, M. J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804725-5.00001-x · Cited by 8

A Medicinal Chemist’s Perspective on Transitioning from Industry to Academic Drug Discovery

Barrow, J. C. (2019) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00107 · Cited by 6

Docking, Scoring, and Virtual Screening in Drug Discovery

Spyrakis, F., Sarkar, A., & Kellogg, G. E. (2021) · Wiley eBooks · doi:10.1002/0471266949.bmc301 · Cited by 6

Design of an equilibrative nucleoside transporter subtype 1 inhibitor for pain relief

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NUAK kinases: Signaling mechanisms and therapeutic applications

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Emerging opportunities and challenges in small molecule development for non-HSP90 chaperones

Tang, M., Wu, Q., Liu, Y., Liu, X., You, Q., & Wang, L. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.118100 · Cited by 5

Pharmacologic interrogation of USP28 cellular function in p53 signaling

Bratt, A. S., Kilgas, S., Guzman, M. I. T., Magin, R. S., Maisonet, I. J., Starnbach, C. A., Teh, W. P., Varca, A. C., Hu, B., Guzman, E. T., et al. (2025) · Cell chemical biology · doi:10.1016/j.chembiol.2025.08.002 · Cited by 5

It's ok to be outnumbered – sub-stoichiometric modulation of homomeric protein complexes

Dimitrova, Y. N., Gutierrez, J. A., & Huard, K. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00212d · Cited by 6

Integrating fragment-based screening with targeted protein degradation and genetic rescue to explore eIF4E function

Sharp, S. Y., Martella, M., D’Agostino, S., Milton, C. I., Ward, G., Woodhead, A., Richardson, C. J., Carr, M. G., Chiarparin, E., Cons, B. D., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54356-1 · Cited by 6

Identifying and evaluating understudied protein kinases using biological and chemical criteria

Koch, S., & Bajorath, J. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00306g · Cited by 5

Beyond PAINs: Chemotype Sensitivity of Protein Methyltransferases in Screens

Gao, C., Margolis, B. J., Strelow, J. M., Vidler, L. R., & Mader, M. M. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00375 · Cited by 5

Identification of 4‐Anilinoquin(az)oline as a Cell‐Active Protein Kinase Novel 3 (PKN3) Inhibitor Chemotype**

Asquith, C. R. M., Temme, L., East, M. P., Laitinen, T., Pickett, J. E., Kwarcinski, F. E., Sinha, P., Wells, C. I., Johnson, G. L., Zutshi, R., et al. (2022) · ChemMedChem · doi:10.1002/cmdc.202200161 · Cited by 6

Detection of the oxidation products of thiols: Disulfides, and sulfenic, sulfinic, and sulfonic acids

Shi, Y., & Carroll, K. S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90219-9.00010-8 · Cited by 6

Scale-Up Synthesis of 1-Methyladamantane and Its Functionalization as a Key Point for Promising Antiviral Agents

Pashenko, A. E., Gaidai, A. V., Hryhoriev, N., Volovenko, O. B., Levandovskiy, I. A., Maksymenko, O., Volochnyuk, D. M., & Ryabukhin, S. V. (2023) · Organic Process Research & Development · doi:10.1021/acs.oprd.2c00305 · Cited by 5

Deep Annotation of Donated Chemical Probes (DCP) in Organotypic Human Liver Cultures and Patient-Derived Organoids from Tumor and Normal Colorectum

Tredup, C., Ndreshkjana, B., Schneider, N. S., Tjaden, A., Kemas, A. M., Youhanna, S. C., Lauschke, V. M., Berger, B., Krämer, A., Berger, L. M., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00877 · Cited by 5

Activity-based probes in pathogenic bacteria: Investigating drug targets and molecule specificity

Lembke, H. K., & Carlson, E. E. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102359 · Cited by 5

Quantitative Prioritization of Tool Compounds for Phenotypic Screening

Wang, Y., & Jenkins, J. L. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7847-2_15 · Cited by 5

Opportunities for Lipid-Based Probes in the Field of Immunology

Koenders, S. T. A., Gagestein, B., & van der Stelt, M. (2018) · Current topics in microbiology and immunology · doi:10.1007/82_2018_127 · Cited by 5

Synthesis of Aza-acyclic Nucleoside Libraries of Purine, Pyrimidine, and 1,2,4-Triazole

Pathak, V., Pathak, A. K., & Reynolds, R. C. (2019) · ACS Combinatorial Science · doi:10.1021/acscombsci.8b00136 · Cited by 5

Neuromodulation by selective angiotensin-converting enzyme 2 inhibitors

Pozdnyakova, N., Krisanova, N. V., Pastukhov, A. O., Tarasenko, A. S., Dudarenko, M., Chernykh, A. V., Pashenko, A. E., Ryabukhin, S. V., Tolstanova, G. M., Volochnyuk, D. M., et al. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.07.003 · Cited by 5

Fluorescent Probe Combined with Photoelectric Analysis Technology for Detection of Escherichia coli

Cui, Q., Zhong, Y., Shang, W., Deng, F., Wang, B., Wu, J., Wang, P., Wan, L., Wang, K., Fang, L., et al. (2023) · Biosensors · doi:10.3390/bios13020150 · Cited by 5

Cellular analysis of the action of epigenetic drugs and probes

Hau, M., Zenk, F. L., Ganesan, A., Iovino, N., & Jung, M. (2017) · Epigenetics · doi:10.1080/15592294.2016.1274472 · Cited by 6

Chlorocarbonylsulfenyl Chloride Cyclizations Towards Piperidin-3-yl-oxathiazol-2-ones as Potential Covalent Inhibitors of Threonine Proteases

Jukič, M., Grabrijan, K., Kadić, S., de Lera-Garrido, F., Sosič, I., Gobec, S., & Obreza, A. (2017) · Acta chimica slovenica · doi:10.17344/acsi.2017.3883 · Cited by 5

Peptide Technologies in the Development of Chemical Tools for Chromatin‐Associated Machinery

Barnash, K. D., Lamb, K. N., James, L. I., & Frye, S. V. (2017) · Drug Development Research · doi:10.1002/ddr.21398 · Cited by 5

The Chemical Probes Portal: an expert review-based public resource to empower chemical probe assessment, selection and use

Antolín, A. A., Sanfelice, D., Crisp, A., Villasclaras-Fernández, E. D., Mica, I. L., Chen, Y., Collins, I., Edwards, A. M., Müller, S., Al‐Lazikani, B., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac909 · Cited by 56

Probing questions

(2015) · Nature Chemical Biology · doi:10.1038/nchembio.1882 · Cited by 3

Perfecting probes

(2009) · Nature Chemical Biology · doi:10.1038/nchembio0709-435 · Cited by 3

Retooling chemical probes

(2010) · Nature Chemical Biology · doi:10.1038/nchembio.330 · Cited by 6

Introduction to Chemical Probes

Wagner, B. K. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160745-00001 · Cited by 4