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

Natural allosteric modulators and their biological targets: molecular signatures and mechanisms

Bruder, M., Polo, G., & Trivella, D. B. B. (2020) · Natural Product Reports · doi:10.1039/c9np00064j · Cited by 32

Discovery of the SMYD3 Inhibitor BAY-6035 Using Thermal Shift Assay (TSA)-Based High-Throughput Screening

Gradl, S., Steuber, H., Weiske, J., Szewczyk, M., Schmees, N., Siegel, S., Stoeckigt, D., Christ, C. D., Li, F., Organ, S. L., et al. (2021) · SLAS DISCOVERY · doi:10.1177/24725552211019409 · Cited by 31

Robust proteome profiling of cysteine-reactive fragments using label-free chemoproteomics

Biggs, G. S., Cawood, E. E., Vuorinen, A., McCarthy, W. J., Wilders, H., Riziotis, I. G., van der Zouwen, A. J., Pettinger, J., Nightingale, L., Chen, P., et al. (2025) · Nature Communications · doi:10.1038/s41467-024-55057-5 · Cited by 36

Targeting Pim Kinases and DAPK3 to Control Hypertension

Carlson, D. A., Singer, M. R., Sutherland, C., Redondo, C., Alexander, L. T., Hughes, P. F., Knapp, S., Gurley, S. B., Sparks, M. A., MacDonald, J. A., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.06.006 · Cited by 29

EU-OPENSCREEN: A Novel Collaborative Approach to Facilitate Chemical Biology

Brennecke, P., Rasiņa, D., Aubi, O., Herzog, K., Landskron, J., Cautain, B., Vicente, F., Quintana, J. R., Mestres, J., Stechmann, B., et al. (2019) · SLAS DISCOVERY · doi:10.1177/2472555218816276 · Cited by 30

Propargylic Se-adenosyl- l -selenomethionine: A Chemical Tool for Methylome Analysis

Sohtome, Y., Shimazu, T., Shinkai, Y., & Sodeoka, M. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.1c00395 · Cited by 30

Image-Based Annotation of Chemogenomic Libraries for Phenotypic Screening

Tjaden, A., Chaikuad, A., Kowarz, E., Marschalek, R., Knapp, S., Schröder, M., & Müller, S. (2022) · Molecules · doi:10.3390/molecules27041439 · Cited by 30

Structural features and inhibitors of bromodomains

Meslamani, J. E., Smith, S. G., Sánchez, R., & Zhou, M. (2016) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2016.09.001 · Cited by 32

SKI-178: A multitargeted inhibitor of sphingosine kinase and microtubule dynamics demonstrating therapeutic efficacy in acute myeloid leukemia models

Yun, J., Hengst, J., Dick, T., Sharma, A. K., Doi, K., Hegde, S., Tan, S., Geffert, L., Fox, T., Sharma, A., et al. (2017) · Cancer translational medicine · doi:10.4103/ctm.ctm_7_17 · Cited by 30

Challenges in validating candidate therapeutic targets in cancer

Settleman, J. E., Sawyers, C. L., & Hunter, T. R. (2018) · eLife · doi:10.7554/elife.32402 · Cited by 32

The transcriptional repressor REV-ERB as a novel target for disease

Úriz, A., Date, A., Ang, H. Y.-K., Ali, S., Brady, H. J. M., & Fuchter, M. J. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127395 · Cited by 29

Discovery of a Novel Class of Covalent Dual Inhibitors Targeting the Protein Kinases BMX and BTK

Förster, M., Liang, X. J., Schröder, M., Gerstenecker, S., Chaikuad, A., Knapp, S., Laufer, S., & Gehringer, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239269 · Cited by 29

Discovery and Characterization of the Potent and Highly Selective 1,7-Naphthyridine-Based Inhibitors BAY-091 and BAY-297 of the Kinase PIP4K2A

Wortmann, L., Bräuer, N., Holton, S. J., Irlbacher, H., Weiske, J., Lechner, C., Meier, R., Karén, J., Sioberg, C., Pütter, V., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01245 · Cited by 28

The role of ZA channel water-mediated interactions in the design of bromodomain-selective BET inhibitors

Bharatham, N., Slavish, P. J., Shadrick, W. R., Young, B. M., & Shelat, A. A. (2018) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2018.03.005 · Cited by 28

Genetically encoded sensors for Chloride concentration

Lodovichi, C., Ratto, G. M., Trevelyan, A. J., & Arosio, D. (2021) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2021.109455 · Cited by 27

Structure-Based Design of a Chemical Probe Set for the 5-HT 5A Serotonin Receptor

Kaplan, A. L., Strachan, R. T., Bráz, J. M., Craik, V., Slocum, S. T., Mangano, T. J., Amabo, V., O’Donnell, H. R., Lak, P., Basbaum, A. I., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02031 · Cited by 29

Highly Selective, Amine‐Derived Cannabinoid Receptor 2 Probes

Westphal, M. V., Sarott, R. C., Zirwes, E. A., Osterwald, A., Guba, W., Ullmer, C., Grether, U., & Carreira, E. M. (2020) · Chemistry - A European Journal · doi:10.1002/chem.201904584 · Cited by 27

Redox active or thiol reactive? Optimization of rapid screens to identify less evident nuisance compounds

Proj, M., Knez, D., Sosič, I., & Gobec, S. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.03.008 · Cited by 27

Host Kinase CSNK2 is a Target for Inhibition of Pathogenic SARS-like β-Coronaviruses

Yang, X., Dickmander, R. J., Bayati, A., Taft-Benz, S., Smith, J. L., Wells, C. I., Madden, E. A., Brown, J. W., Lenarcic, E. M., Yount, B. L., et al. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00378 · Cited by 29

Chemical biology and pharmacology of histone lysine methylation inhibitors

Barghout, S. H., Machado, R. A. C., & Baršytė-Lovejoy, D. (2022) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2022.194840 · Cited by 29

Discovery and Characterization of BAY-805, a Potent and Selective Inhibitor of Ubiquitin-Specific Protease USP21

Göricke, F., Vu, V., Smith, L., Scheib, U., Böhm, R., Akkılıç, N., Wohlfahrt, G., Weiske, J., Bömer, U., Brzezinka, K., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01933 · Cited by 30

Identification and Visualization of Kinase-Specific Subpockets

Volkamer, A., Eid, S., Turk, S., Rippmann, F., & Fulle, S. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00627 · Cited by 27

Chemical probes targeting epigenetic proteins: Applications beyond oncology

Ackloo, S. Z., Brown, P. J., & Müller, S. (2017) · Epigenetics · doi:10.1080/15592294.2017.1279371 · Cited by 27

Kinase-Centric Computational Drug Development

Kooistra, A. J., & Volkamer, A. (2017) · Annual reports in medicinal chemistry · doi:10.1016/bs.armc.2017.08.001 · Cited by 27

Comparative Analysis of Small-Molecule LIMK1/2 Inhibitors: Chemical Synthesis, Biochemistry, and Cellular Activity

Collins, R. J., Lee, H.-A., Jones, D. H., Elkins, J. M., Gillespie, J. A., Thomas, C., Baldwin, A. G., Jones, K. M., Waters, L., Paine, M., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00751 · Cited by 26

Chemogenetics for cell-type-specific modulation of signalling and neuronal activity

Kang, H. J., Minamimoto, T., Wess, J., & Roth, B. L. (2023) · Nature Reviews Methods Primers · doi:10.1038/s43586-023-00276-1 · Cited by 27

Early Perspective

Seashore-Ludlow, B. A., & Lundbäck, T. (2016) · SLAS DISCOVERY · doi:10.1177/1087057116659256 · Cited by 26

Hydrogen improves cell viability partly through inhibition of autophagy and activation of PI3K/Akt/GSK3β signal pathway in a microvascular endothelial cell model of traumatic brain injury

Wang, Y., Wang, L., Hu, T., Wang, F., Han, Z., Yin, Z., Ge, X., Xie, K., & Lei, P. (2020) · Neurological Research · doi:10.1080/01616412.2020.1747717 · Cited by 26

Validating Small Molecule Chemical Probes for Biological Discovery

Vu, V., Szewczyk, M. M., Nie, D. Y., Arrowsmith, C. H., & Baršytė-Lovejoy, D. (2022) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-032620-105344 · Cited by 26

canSAR chemistry registration and standardization pipeline

Dolciami, D., Villasclaras-Fernández, E. D., Kannas, C. C., Meniconi, M., Al‐Lazikani, B., & Antolín, A. A. (2022) · Journal of Cheminformatics · doi:10.1186/s13321-022-00606-7 · Cited by 26

Opportunities and challenges in targeting orphan nuclear receptors

Isigkeit, L., & Merk, D. (2023) · Chemical Communications · doi:10.1039/d3cc00954h · Cited by 27

Investigating Apoptozole as a Chemical Probe for HSP70 Inhibition

Evans, L. E., Cheeseman, M. D., Yahya, N., & Jones, K. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140006 · Cited by 26

Chemical genetics approaches for selective intervention in epigenetics

Runcie, A. C., Chan, K.-H., Zengerle, M., & Ciulli, A. (2016) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2016.06.031 · Cited by 25

Which Small Molecule? Selecting Chemical Probes for Use in Cancer Research and Target Validation

Mader, M. M., Rudolph, J., Hartung, I. V., Uehling, D., Workman, P., & Zuercher, W. J. (2023) · Cancer Discovery · doi:10.1158/2159-8290.cd-23-0536 · Cited by 25

Critical assessment of LC3/GABARAP ligands used for degrader development and ligandability of LC3/GABARAP binding pockets

Schwalm, M. P., Dopfer, J., Kumar, A. M., Greco, F., Bauer, N., Löhr, F., Heering, J., Cano-Franco, S., Lechner, S., Hanke, T., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54409-5 · Cited by 33

An organizing role for the TGF-β signaling pathway in axes formation of the annelid Capitella teleta

Lanza, A. R., & Seaver, E. C. (2018) · Developmental Biology · doi:10.1016/j.ydbio.2018.01.004 · Cited by 25

Discovery and Characterization of BAY 1214784, an Orally Available Spiroindoline Derivative Acting as a Potent and Selective Antagonist of the Human Gonadotropin-Releasing Hormone Receptor as Proven in a First-In-Human Study in Postmenopausal Women

Panknin, O., Wagenfeld, A., Bone, W., Bender, E., Nowak‐Reppel, K., Fernández‐Montalván, A. E., Nubbemeyer, R., Bäurle, S., Ring, S., Schmees, N., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01076 · Cited by 26

Inhibitors of cullin-RING E3 ubiquitin ligase 4 with antitumor potential

Wu, K., Huynh, K. Q., Lu, I., Moustakim, M., Miao, H., Yu, C., Haeusgen, M. J., Hopkins, B. D., Huang, L., Zheng, N., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2007328118 · Cited by 26

In-gel activity-based protein profiling of a clickable covalent ERK1/2 inhibitor

Lebraud, H., Wright, D. J., East, C., Holding, F. P., O’Reilly, M., & Heightman, T. D. (2016) · Molecular BioSystems · doi:10.1039/c6mb00367b · Cited by 25

BI 1002494, a Novel Potent and Selective Oral Spleen Tyrosine Kinase Inhibitor, Displays Differential Potency in Human Basophils and B Cells

Lamb, D. J., Wollin, S. L., Schnapp, A., Bischoff, D., Erb, K. J., Bouyssou, T., Guilliard, B., Strasser, C., Wex, E., Blum, S., et al. (2016) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.116.233155 · Cited by 25

Chemical inhibitors targeting histone methylation readers

Huang, X., Chen, Y., Xiao, Q., Shang, X., & Liu, Y. (2024) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2024.108614 · Cited by 24

A chemical screen identifies PRMT5 as a therapeutic vulnerability for paclitaxel-resistant triple-negative breast cancer

Zhang, K., Wei, J., Zhang, S.-Y., Fei, L., Guo, L., Liu, X., Ji, Y., Chen, W., Ciamponi, F. E., Chen, W., et al. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.08.003 · Cited by 24

Glial cells as drug targets: What does it take?

Möller, T., & Boddeke, H. W. G. M. (2016) · Glia · doi:10.1002/glia.22993 · Cited by 24

Selective targeting of epigenetic reader domains

Greschik, H., Schüle, R., & Günther, T. (2017) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2017.1303474 · Cited by 25

Quantitative Interpretation of Intracellular Drug Binding and Kinetics Using the Cellular Thermal Shift Assay

Seashore-Ludlow, B. A., Axelsson, H., Almqvist, H., Dahlgren, B., Jönsson, M., & Lundbäck, T. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b01057 · Cited by 24

Discovery of BAY-298 and BAY-899: Tetrahydro-1,6-naphthyridine-Based, Potent, and Selective Antagonists of the Luteinizing Hormone Receptor Which Reduce Sex Hormone Levels in Vivo

Wortmann, L., Lindenthal, B., Muhn, P., Walter, A., Nubbemeyer, R., Heldmann, D., Sobek, L., Morandi, F., Schrey, A. K., Moosmayer, D., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01382 · Cited by 23

Detectives and helpers: Natural products as resources for chemical probes and compound libraries

Parthasarathy, A., Mantravadi, P. K., & Kalesh, K. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107688 · Cited by 24

Drugging Fuzzy Complexes in Transcription

Su, B. G., & Henley, M. J. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.795743 · Cited by 27

BAY-069, a Novel (Trifluoromethyl)pyrimidinedione-Based BCAT1/2 Inhibitor and Chemical Probe

Günther, J., Hillig, R. C., Zimmermann, K. C., Kaulfuß, S., Lemos, C., Nguyen, D., Rehwinkel, H., Habgood, M., Lechner, C., Neuhaus, R., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00441 · Cited by 25

Discovery of a Novel Potent and Selective HSD17B13 Inhibitor, BI-3231, a Well-Characterized Chemical Probe Available for Open Science

Thamm, S., Willwacher, M. K., Aspnes, G. E., Bretschneider, T., Brown, N. F., Buschbom-Helmke, S., Fox, T., Gargano, E. M., Grabowski, D., Hoenke, C., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01884 · Cited by 24

Engaging a Non-catalytic Cysteine Residue Drives Potent and Selective Inhibition of Caspase-6

Horn, K. S. V., Wang, D., Medina-Cleghorn, D. A., Lee, P. S., Bryant, C., Altobelli, C. R., Jaishankar, P., Leung, K., Ng, R. A., Ambrose, A. J., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c12240 · Cited by 21

Joining Forces: The Chemical Biology–Medicinal Chemistry Continuum

Plowright, A. T., Ottmann, C., Arkin, M. R., Auberson, Y. P., Timmerman, H., & Waldmann, H. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.05.019 · Cited by 25

ALARM NMR for HTS Triage and Chemical Probe Validation

Dahlin, J. L., Cuellar, M. E., Singh, G., Nelson, K. M., Strasser, J. M., Rappe, T. M., Xia, Y., Veglia, G., & Walters, M. A. (2018) · Current Protocols in Chemical Biology · doi:10.1002/cpch.35 · Cited by 24

Chemogenomic Analysis of the Druggable Kinome and Its Application to Repositioning and Lead Identification Studies

Ravikumar, B., Timonen, S., Alam, Z., Parri, E., Wennerberg, K., & Aittokallio, T. A. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.08.007 · Cited by 24

A Highly Selective Chemical Probe for Activin Receptor-like Kinases ALK4 and ALK5

Hanke, T., Wong, J. F., Berger, B., Abdi, I., Berger, L. M., Tesch, R., Tredup, C., Bullock, A. N., Müller, S., & Knapp, S. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00076 · Cited by 24

A New Chemical Probe Challenges the Broad Cancer Essentiality of CK2

Licciardello, M. P., & Workman, P. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.02.002 · Cited by 24

Kinobeads: A Chemical Proteomic Approach for Kinase Inhibitor Selectivity Profiling and Target Discovery

Reinecke, M., Heinzlmeir, S., Wilhelm, M., Médard, G., Klaeger, S., & Küster, B. (2019) · Methods and principles in medicinal chemistry · doi:10.1002/9783527818242.ch4 · Cited by 23

Cytotoxic Profiling of Annotated and Diverse Chemical Libraries Using Quantitative High-Throughput Screening

Lee, O. W., Austin, S., Gamma, M., Cheff, D. M., Lee, T. D., Wilson, K. M., Johnson, J. M., Travers, J., Braisted, J. C., Guha, R., et al. (2019) · SLAS DISCOVERY · doi:10.1177/2472555219873068 · Cited by 23

Synthesis and mode of action of oligomeric sesquiterpene lactones

Li, C., Jones, A. X., & Lei, X. (2015) · Natural Product Reports · doi:10.1039/c5np00089k · Cited by 23

eCF309 : a potent, selective and cell-permeable mTOR inhibitor

Fraser, C., Carragher, N. O., & Unciti‐Broceta, A. (2015) · MedChemComm · doi:10.1039/c5md00493d · Cited by 23

Discovery of a Selective Covalent Inhibitor of Lysophospholipase-like 1 (LYPLAL1) as a Tool to Evaluate the Role of this Serine Hydrolase in Metabolism

Ahn, K., Boehm, M., Brown, M. F., Calloway, J., Che, Y., Chen, J., Fennell, K. F., Geoghegan, K. F., Gilbert, A. M., Gutierrez, J. A., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00266 · Cited by 23

Reflections and Outlook on Targeting HSP90, HSP70 and HSF1 in Cancer: A Personal Perspective

Workman, P. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-40204-4_11 · Cited by 22

Structural and functional characterization of ubiquitin variant inhibitors for the JAMM-family deubiquitinases STAMBP and STAMBPL1

Guo, Y., Liu, Q., Mallette, E., Caba, C., Hou, F., Fux, J. E., LaPlante, G., Dong, A., Zhang, Q., Zheng, H., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101107 · Cited by 22

Combating small-molecule aggregation with machine learning

Lee, K., Yang, A., Lin, Y., Reker, D., Bernardes, G. J. L., & Rodrigues, T. (2021) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2021.100573 · Cited by 22

Dynamic modifications of biomacromolecules: mechanism and chemical interventions

Wang, C., Zou, P., Yang, C., Liu, L., Cheng, L., He, X., Zhang, L., Zhang, Y., Jiang, H., & Chen, P. R. (2019) · Science China Life Sciences · doi:10.1007/s11427-019-9823-1 · Cited by 23

Progress Towards a Public Chemogenomic Set for Protein Kinases and a Call for ContributionsPreprint

Drewry, D. H., Wells, C. I., Andrews, D. M., Angell, R. M., Al‐Ali, H., Axtman, A. D., Capuzzi, S. J., Elkins, J. M., Ettmayer, P., Frederiksen, M. U., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/104711 · Cited by 23

Tryptophan scanning mutagenesis as a way to mimic the compound-bound state and probe the selectivity of allosteric inhibitors in cells

Taylor, I. R., Assimon, V. A., Kuo, S. Y., Rinaldi, S., Li, X., Young, Z. T., Morra, G., Green, K. D., Nguyen, D. N., Shao, H., et al. (2020) · Chemical Science · doi:10.1039/c9sc04284a · Cited by 21

From Phenotypic Hit to Chemical Probe: Chemical Biology Approaches to Elucidate Small Molecule Action in Complex Biological Systems

Pasquer, Q. T. L., Tsakoumagkos, I. A., & Hoogendoorn, S. (2020) · Molecules · doi:10.3390/molecules25235702 · Cited by 21

Identification of β-strand mediated protein–protein interaction inhibitors using ligand-directed fragment ligation

Hegedüs, Z., Hóbor, F., Shoemark, D. K., Celis, S., Lian, L., Trinh, C. H., Sessions, R. B., Edwards, T. A., & Wilson, A. J. (2021) · Chemical Science · doi:10.1039/d0sc05694d · Cited by 21

Targeting the ubiquitin system by fragment-based drug discovery

Kennedy, C. R., McPhie, K. A., & Rittinger, K. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1019636 · Cited by 21

Target 2035 – an update on private sector contributions

Ackloo, S. Z., Antolín, A. A., Bartolomé, J. M., Beck, H., Bullock, A. N., Betz, U. A. K., Böttcher, J., Brown, P. J., Chaturvedi, M., Crisp, A., et al. (2023) · RSC Medicinal Chemistry · doi:10.1039/d2md00441k · Cited by 20

Chemo‐proteomics in antimalarial target identification and engagement

Bailey, B. L., Nguyen, W., Cowman, A. F., & Sleebs, B. E. (2023) · Medicinal Research Reviews · doi:10.1002/med.21975 · Cited by 21

Reviewing Hit Discovery Literature for Difficult Targets: Glutathione Transferase Omega-1 as an Example

Xie, Y., Dahlin, J. L., Oakley, A. J., Casarotto, M. G., Philip G. Board, & Baell, J. B. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00318 · Cited by 21

Cutting Edge Therapeutic Insights Derived from Molecular Biology of Pediatric High-Grade Glioma and Diffuse Intrinsic Pontine Glioma (DIPG)

Bailey, C. P., Figueroa, M., Mohiuddin, S., Zaky, W. T., & Chandra, J. (2018) · Bioengineering · doi:10.3390/bioengineering5040088 · Cited by 21

Bioorthogonal Probes for the Study of MDM2‐p53 Inhibitors in Cells and Development of High‐Content Screening Assays for Drug Discovery

D’Alessandro, P. L., Buschmann, N., Kaufmann, M., Furet, P., Baysang, F., Brunner, R., Marzinzik, A. L., Vorherr, T. E., Stachyra, T., Ottl, J., et al. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201608568 · Cited by 21

An exon skipping screen identifies antitumor drugs that are potent modulators of pre-mRNA splicing, suggesting new therapeutic applications

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