Chemoproteomics and Chemical Probes for Target Discovery

Selective inhibition of BET bromodomains

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Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

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How to improve R&D productivity: the pharmaceutical industry's grand challenge

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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 · see citing works

The druggable genome

Hopkins, A. L., & Groom, C. R. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd892 · Cited by 3,305 · see citing works

A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

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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 · see citing works

Tankyrase inhibition stabilizes axin and antagonizes Wnt signalling

Huang, S.-M. A., Mishina, Y., Liu, S.-M., Cheung, A. K., Stegmeier, F., Michaud, G., Charlat, O., Wiellette, E., Zhang, Y., Wiessner, S., et al. (2009) · Nature · doi:10.1038/nature08356 · Cited by 2,077 · see citing works

The Essential Medicinal Chemistry of Curcumin

Nelson, K. M., Dahlin, J. L., Bisson, J., Graham, J., Pauli, G. F., & Walters, M. A. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00975 · Cited by 1,956 · see citing works

A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p

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How were new medicines discovered?

Swinney, D. C., & Anthony, J. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3480 · Cited by 1,812 · see citing works

Suppression of inflammation by a synthetic histone mimic

Nicodeme, E., Jeffrey, K. L., Schaefer, U., Beinke, S., Dewell, S., Chung, C.-W., Chandwani, R., Marazzi, I., Wilson, P., Coste, H., et al. (2010) · Nature · doi:10.1038/nature09589 · Cited by 1,563 · see citing works

Inhibition of Hedgehog signaling by direct binding of cyclopamine to SmoothenedPreprint

Chen, J., Taipale, J., Cooper, M. K., & Beachy, P. A. (2002) · Genes & Development · doi:10.1101/gad.1025302 · Cited by 1,464 · see citing works

A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase

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Targeting bromodomains: epigenetic readers of lysine acetylation

Filippakopoulos, P., & Knapp, S. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4286 · Cited by 1,274 · see citing works

Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry

Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.124125 · Cited by 1,270 · see citing works

Tracking cancer drugs in living cells by thermal profiling of the proteome

Savitski, M. M., Reinhard, F. B. M., Franken, H., Werner, T., Savitski, M. F., Eberhard, D., Molina, D. M., Jafari, R., Dovega, R. B., Klaeger, S., et al. (2014) · Science · doi:10.1126/science.1255784 · Cited by 1,187 · see citing works

Target identification using drug affinity responsive target stability (DARTS)

Lomenick, B., Hao, R., Jonai, N., Chin, R., Aghajan, M., Warburton, S., Wang, J., Wu, R. P., Gómez, F., Loo, J. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910040106 · Cited by 1,113 · see citing works

Chemistry: Chemical con artists foil drug discovery

Baell, J. B., & Walters, M. A. (2014) · Nature · doi:10.1038/513481a · Cited by 1,048 · see citing works

Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors

Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S., Böesche, M., Hobson, S., Mathieson, T., Perrin, J., Raida, M., Rau, C., et al. (2007) · Nature Biotechnology · doi:10.1038/nbt1328 · Cited by 1,036 · see citing works

The druggable genome and support for target identification and validation in drug development

Finan, C., Gaulton, A., Krüger, F. A., Lumbers, R. T., Shah, T., Engmann, J., Galver, L., Kelley, R., Karlsson, A., Santos, R., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aag1166 · Cited by 1,011 · see citing works

Opportunities and challenges in phenotypic drug discovery: an industry perspective

Moffat, J. G., Vincent, F., Lee, J. A., Eder, J., & Prunotto, M. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.111 · Cited by 939 · see citing works

The promise and peril of chemical probes

Arrowsmith, C. H., Audia, J. E., Austin, C., Baell, J., Bennett, J., Blagg, J., Bountra, C., Brennan, P. E., Brown, P. J., Bunnage, M. E., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1867 · Cited by 839 · see citing works

Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present

Bantscheff, M., Lemeer, S., Savitski, M. M., & Kuster, B. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-6203-4 · Cited by 801 · see citing works

Thermal proteome profiling for unbiased identification of direct and indirect drug targets using multiplexed quantitative mass spectrometry

Franken, H., Mathieson, T., Childs, D., Sweetman, G. M. A., Werner, T., Tögel, I., Doce, C., Gade, S., Bantscheff, M., Drewes, G., et al. (2015) · Nature Protocols · doi:10.1038/nprot.2015.101 · Cited by 663 · see citing works

Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes

Bantscheff, M., Hopf, C., Savitski, M. M., Dittmann, A., Grandi, P., Michon, A.-M., Schlegl, J., Abraham, Y., Becher, I., Bergamini, G., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1759 · Cited by 659 · see citing works

The metabolite alpha-ketoglutarate extends lifespan by inhibiting the ATP synthase and TOR

Chin, R., Fu, X., Pai, M. Y., Vergnes, L., Hwang, H., Deng, G., Diep, S., Lomenick, B., Meli, V., Monsalve, G. C., et al. (2014) · Nature · doi:10.1038/nature13264 · Cited by 570 · see citing works

A Map of Protein-Metabolite Interactions Reveals Principles of Chemical Communication

Piazza, I., Kochanowski, K., Cappelletti, V., Fuhrer, T., Noor, Ε., Sauer, U., & Picotti, P. (2018) · Cell · doi:10.1016/j.cell.2017.12.006 · Cited by 547 · see citing works

The anti-inflammatory natural product parthenolide from the medicinal herb Feverfew directly binds to and inhibits IκB kinase

Kwok, B. H. B., Koh, B. D., Ndubuisi, M. I., Elofsson, M., & Crews, C. M. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00049-7 · Cited by 516 · see citing works

In situ click chemistry: probing the binding landscapes of biological molecules

Mamidyala, S. K., & Finn, M. G. (2010) · Chemical Society Reviews · doi:10.1039/b901969n · Cited by 490 · see citing works

Global profiling of lysine reactivity and ligandability in the human proteome

Hacker, S. M., Backus, K. M., Lazear, M. R., Forli, S., Correia, B. E., & Cravatt, B. F. (2017) · Nature Chemistry · doi:10.1038/nchem.2826 · Cited by 485 · see citing works

Target Identification for Small Bioactive Molecules: Finding the Needle in the Haystack

Ziegler, S., Pries, V., Hedberg, C., & Waldmann, H. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208749 · Cited by 466 · see citing works

A Mass Spectrometric-Derived Cell Surface Protein Atlas

Bausch‐Fluck, D., Hofmann, A., Bock, T., Frei, A. P., Cerciello, F., Jacobs, A., Moest, H., Omasits, U., Gundry, R. L., Yoon, C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0121314 · Cited by 445 · see citing works

Ligand and Target Discovery by Fragment-Based Screening in Human Cells

Parker, C. G., Galmozzi, A., Wang, Y., Correia, B. E., Sasaki, K., Joslyn, C. M., Kim, A. S., Cavallaro, C. L., Lawrence, R. M., Johnson, S. R., et al. (2017) · Cell · doi:10.1016/j.cell.2016.12.029 · Cited by 439 · see citing works

Target validation using chemical probes

Bunnage, M. E., Chekler, E. L. P., & Jones, L. H. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1197 · Cited by 420 · see citing works

Stereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategy

Huber, K., Salah, E., Radic-Sarikas, B., Gridling, M., Elkins, J. M., Stukalov, A., Jemth, A., Göktürk, C., Sanjiv, K., Strömberg, K., et al. (2014) · Nature · doi:10.1038/nature13194 · Cited by 398 · see citing works

Biochemical mechanisms of drug action: what does it take for success?

Swinney, D. C. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1500 · Cited by 396 · see citing works

Drug Affinity Responsive Target Stability (DARTS) for Small-Molecule Target Identification

Pai, M. Y., Lomenick, B., Hwang, H., Schiestl, R. H., McBride, W. H., Loo, J. A., & Huang, J. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2269-7_22 · Cited by 362 · see citing works

Systems Pharmacology: Network Analysis to Identify Multiscale Mechanisms of Drug Action

Zhao, S., & Iyengar, R. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134520 · Cited by 358 · see citing works

Dual kinase-bromodomain inhibitors for rationally designed polypharmacology

Ciceri, P., Müller, S., O’Mahony, A., Fedorov, O., Filippakopoulos, P., Hunt, J. P., Lasater, E. A., Pallares, G., Picaud, S., Wells, C. D., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1471 · Cited by 345 · see citing works

Discovery and Characterization of Small Molecule Inhibitors of the BET Family Bromodomains

Chung, C., Coste, H., White, J. H. M., Mirguet, O., Wilde, J. I., Gosmini, R. L., Delves, C. J., Magny, S. D., Woodward, R., Hughes, S. A., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200108t · Cited by 334 · see citing works

Comprehensive characterization of the Published Kinase Inhibitor Set

Elkins, J. M., Fedele, V., Szklarz, M., Abdul Azeez, K. R., Salah, E., Mikolajczyk, J., Romanov, S., Sepetov, N., Huang, X.-P., Roth, B. L., et al. (2016) · Nature Biotechnology · doi:10.1038/nbt.3374 · Cited by 323 · see citing works

Thermal proteome profiling monitors ligand interactions with cellular membrane proteins

Reinhard, F. B. M., Eberhard, D., Werner, T., Franken, H., Childs, D., Doce, C., Savitski, M. F., Huber, W. K., Bantscheff, M., Savitski, M. M., et al. (2015) · Nature Methods · doi:10.1038/nmeth.3652 · Cited by 310 · see citing works

The (un)targeted cancer kinome

Fedorov, O., Müller, S., & Knapp, S. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.297 · Cited by 293 · see citing works

Solid-phase extraction of N-linked glycopeptides

Tian, Y., Zhou, Y. F., Elliott, S., Aebersold, R. H., & Zhang, H. (2007) · Nature Protocols · doi:10.1038/nprot.2007.42 · Cited by 286 · see citing works

The ins and outs of selective kinase inhibitor development

Müller, S., Chaikuad, A., Gray, N. S., & Knapp, S. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1938 · Cited by 276 · see citing works

Antimalarial efficacy of MMV390048, an inhibitor of Plasmodium phosphatidylinositol 4-kinase

Paquet, T., Manach, C. L., Cabrera, D. G., Younis, Y., Henrich, P. P., Abraham, T. S., Lee, M., Basak, R., Ghidelli, S., Lafuente-Monasterio, M. J., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aad9735 · Cited by 276 · see citing works

Superfamily-wide portrait of serine hydrolase inhibition achieved by library-versus-library screening

Bachovchin, D. A., Ji, T., Li, W., Simon, G. M., Blankman, J. L., Adibekian, A., Hoover, H. S., Niessen, S., & Cravatt, B. F. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011663107 · Cited by 275 · see citing works

Chemical Proteomics Identifies Druggable Vulnerabilities in a Genetically Defined Cancer

Bar-Peled, L., Kemper, E. K., Suciu, R. M., Vinogradova, E. V., Backus, K. M., Horning, B. D., Paul, T. A., Ichu, T.-A., Svensson, R. U., Olucha, J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.08.051 · Cited by 262 · see citing works

Thermal profiling reveals phenylalanine hydroxylase as an off-target of panobinostat

Becher, I., Werner, T., Doce, C., Zaal, E. A., Tögel, I., Khan, C. A., Rueger, A., Muelbaier, M., Salzer, E., Berkers, C. R., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2185 · Cited by 251 · see citing works

Ion Coalescence of Neutron Encoded TMT 10-Plex Reporter Ions

Werner, T., Sweetman, G. M. A., Savitski, M. F., Mathieson, T., Bantscheff, M., & Savitski, M. M. (2014) · Analytical Chemistry · doi:10.1021/ac500140s · Cited by 250 · see citing works

Can Invalid Bioactives Undermine Natural Product-Based Drug Discovery?

Bisson, J., McAlpine, J. B., Friesen, J. B., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01009 · Cited by 249 · see citing works

A unique inhibitor binding site in ERK1/2 is associated with slow binding kinetics

Chaikuad, A., Tacconi, E. M., Zimmer, J., Liang, Y., Gray, N. S., Tarsounas, M., & Knapp, S. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1629 · Cited by 247 · see citing works

The Cysteinome of Protein Kinases as a Target in Drug Development

Chaikuad, A., Koch, P., Laufer, S., & Knapp, S. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201707875 · Cited by 237 · see citing works

Acetyl-lysine Binding Site of Bromodomain-Containing Protein 4 (BRD4) Interacts with Diverse Kinase Inhibitors

Ember, S. W., Zhu, J.-Y., Olesen, S. H., Martin, M. P., Becker, A., Berndt, N., Georg, G. I., & Schönbrunn, E. (2014) · ACS Chemical Biology · doi:10.1021/cb500072z · Cited by 227 · see citing works

PIKfyve, a Class III PI Kinase, Is the Target of the Small Molecular IL-12/IL-23 Inhibitor Apilimod and a Player in Toll-like Receptor Signaling

Cai, X., Xu, Y., Cheung, A. K., Tomlinson, R., Alcázar-Román, A. R., Murphy, L. O., Billich, A., Zhang, B., Feng, Y., Klumpp, M., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.05.010 · Cited by 225 · see citing works

Thermal proximity coaggregation for system-wide profiling of protein complex dynamics in cells

Tan, C. S. H., Go, K. D., Bisteau, X., Dai, L., Yong, C. H., Prabhu, N., Ozturk, M. B., Lim, Y. T., Sreekumar, L., Lengqvist, J., et al. (2018) · Science · doi:10.1126/science.aan0346 · Cited by 224 · see citing works

Multiplexed Proteome Dynamics Profiling Reveals Mechanisms Controlling Protein Homeostasis

Savitski, M. M., Zinn, N., Faelth-Savitski, M., Poeckel, D., Gade, S., Becher, I., Muelbaier, M., Wagner, A. J., Strohmer, K., Werner, T., et al. (2018) · Cell · doi:10.1016/j.cell.2018.02.030 · Cited by 217 · see citing works

Choose and Use Your Chemical Probe Wisely to Explore Cancer Biology

Blagg, J., & Workman, P. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.06.005 · Cited by 203 · see citing works

Class III Phosphatidylinositol 4-Kinase Alpha and Beta Are Novel Host Factor Regulators of Hepatitis C Virus Replication

Borawski, J. A., Troke, P. J. F., Puyang, X., Gibaja, V., Zhao, S., Mickanin, C., Leighton-Davies, J. R., Wilson, C. J., Myer, V. E., Cornella‐Taracido, I., et al. (2009) · Journal of Virology · doi:10.1128/jvi.02418-08 · Cited by 202 · see citing works

High-Resolution Enabled TMT 8-plexing

Werner, T., Becher, I., Sweetman, G. M. A., Doce, C., Savitski, M. M., & Bantscheff, M. (2012) · Analytical Chemistry · doi:10.1021/ac301553x · Cited by 189 · see citing works

Kinase Inhibitor Selectivity Profiling Using Differential Scanning Fluorimetry

Fedorov, O., Niesen, F., & Knapp, S. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-337-0_7 · Cited by 183 · see citing works

How Chemoproteomics Can Enable Drug Discovery and Development

Moellering, R. E., & Cravatt, B. F. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.01.001 · Cited by 182 · see citing works

A Cell-permeable, Activity-based Probe for Protein and Lipid Kinases

Yee, M., Fas, S. C., Stohlmeyer, M. M., Wandless, T. J., & Cimprich, K. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504730200 · Cited by 165 · see citing works

Eponemycin exerts its antitumor effect through the inhibition of proteasome function.

Meng, L., Kwok, B. H. B., Sin, N., & Crews, C. M. (1999) · PubMed · Cited by 155 · see citing works

Progress towards a public chemogenomic set for protein kinases and a call for contributions

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) · PLoS ONE · doi:10.1371/journal.pone.0181585 · Cited by 154 · see citing works

Covalent Ligand Discovery against Druggable Hotspots Targeted by Anti-cancer Natural Products

Grossman, E. A., Ward, C. C., Spradlin, J. N., Bateman, L. A., Huffman, T. R., Miyamoto, D. K., Kleinman, J. I., & Nomura, D. K. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.013 · Cited by 124 · see citing works

The Commonly Used PI3-Kinase Probe LY294002 Is an Inhibitor of BET Bromodomains

Dittmann, A., Werner, T., Chung, C., Savitski, M. M., Savitski, M. F., Grandi, P., Hopf, C., Lindon, M. J., Neubauer, G., Prinjha, R. K., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb400789e · Cited by 118 · see citing works

CRISPR/Cas9 library screening for drug target discovery

Kurata, M., Yamamoto, K., Moriarity, B. S., Kitagawa, M., & Largaespada, D. A. (2017) · Journal of Human Genetics · doi:10.1038/s10038-017-0376-9 · Cited by 108 · see citing works

Donated chemical probes for open science

Müller, S., Ackloo, S. Z., Arrowsmith, C. H., Bauser, M., Baryza, J. L., Blagg, J., Böttcher, J., Bountra, C., Brown, P. J., Bunnage, M. E., et al. (2018) · eLife · doi:10.7554/elife.34311 · Cited by 107 · see citing works

Chemoproteomic approaches to drug target identification and drug profiling

Bantscheff, M., & Drewes, G. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.11.003 · Cited by 103 · see citing works

Identification of KasA as the cellular target of an anti-tubercular scaffold

Abrahams, K. A., Chung, C., Ghidelli, S., Rullás, J., Rebollo-López, M. J., Gurcha, S. S., Cox, J. A. G., Mendoza-Losana, A., Jiménez‐Navarro, E., Martínez, M. S., et al. (2016) · Nature Communications · doi:10.1038/ncomms12581 · Cited by 97 · see citing works

Essential but Not Vulnerable: Indazole Sulfonamides Targeting Inosine Monophosphate Dehydrogenase as Potential Leads againstMycobacterium tuberculosis

Park, Y., Pacitto, A., Bayliss, T., Cleghorn, L. A. T., Wang, Z., Hartman, T. E., Arora, K., Ioerger, T. R., Sacchettini, J. C., Rizzi, M., et al. (2016) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.6b00103 · Cited by 95 · see citing works

Identification of broad-spectrum antiviral compounds and assessment of the druggability of their target for efficacy against respiratory syncytial virus (RSV)

Bonavia, A., Franti, M., Keaney, E. P., Kuhen, K., Seepersaud, M., Radetich, B., Shao, J., Honda, A., Dewhurst, J. M., Balabanis, K. A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017142108 · Cited by 92 · see citing works

A kinase-independent function of AKT promotes cancer cell survival

Vivanco, I., Chen, Z. C., Tanos, B. E., Oldrini, B., Hsieh, W.-Y., Yannuzzi, N. A., Campos, C., & Mellinghoff, I. K. (2014) · eLife · doi:10.7554/elife.03751 · Cited by 88 · see citing works

Multiple cyclophilins involved in different cellular pathways mediate HCV replication

Gaither, L. A., Borawski, J. A., Anderson, L. J., et al. (2009) · Virology · doi:10.1016/j.virol.2009.10.043 · Cited by 86 · see citing works

A Modular Probe Strategy for Drug Localization, Target Identification and Target Occupancy Measurement on Single Cell Level

Rutkowska, A., Thomson, D. W., Vappiani, J., Werner, T., Mueller, K. M., Dittus, L., Krause, J., Muelbaier, M., Bergamini, G., & Bantscheff, M. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00346 · Cited by 86 · see citing works

Early Accelerated Approval for Highly Targeted Cancer Drugs

Chabner, B. A. (2011) · New England Journal of Medicine · doi:10.1056/nejmp1100548 · Cited by 79 · see citing works

Characterizing the Covalent Targets of a Small Molecule Inhibitor of the Lysine Acetyltransferase P300

Shrimp, J. H., Sorum, A. W., Garlick, J. M., Guasch, L., Nicklaus, M. C., & Meier, J. L. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00385 · Cited by 71 · see citing works

THPP target assignment reveals EchA6 as an essential fatty acid shuttle in mycobacteria

Cox, J. A. G., Abrahams, K. A., Alemparte, C., Ghidelli, S., Rullás, J., Angulo‐Barturen, Í., Singh, A., Gurcha, S. S., Nataraj, V., Bethell, S., et al. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2015.6 · Cited by 68 · see citing works

Response to crizotinib in advanced ALK -rearranged non-small cell lung cancers with different ALK -fusion variants

Li, Y., Zhang, T., Zhang, J., Li, W., Yuan, P., Xing, P., Zhang, Z., Chuai, S., Li, J., & Ying, J. (2018) · Lung Cancer · doi:10.1016/j.lungcan.2018.01.026 · Cited by 66 · see citing works

Multiplexed Thiol Reactivity Profiling for Target Discovery of Electrophilic Natural Products

Tian, C., Sun, R., Liu, K., Fu, L., Liu, X., Zhou, W., Yang, Y., & Yang, J. H. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.022 · Cited by 62 · see citing works

Chemical Proteomics Identifies Nampt as the Target of CB30865, An Orphan Cytotoxic Compound

Fleischer, T. C., Murphy, B. R., Flick, J. S., Terry-Lorenzo, R. T., Gao, Z.-H., Davis, T., McKinnon, R. S., Ostanin, K., Willardsen, J. A., & Boniface, J. J. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.05.008 · Cited by 54 · see citing works

Comparing Immobilized Kinase Inhibitors and Covalent ATP Probes for Proteomic Profiling of Kinase Expression and Drug Selectivity

Lemeer, S., Zörgiebel, C., Ruprecht, B., Kohl, K., & Küster, B. (2013) · Journal of Proteome Research · doi:10.1021/pr301073j · Cited by 54 · see citing works

Use of CRISPR/Cas9 gene-editing tools for developing models in drug discovery

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The Role of γ-Secretase Activating Protein (GSAP) and Imatinib in the Regulation of γ-Secretase Activity and Amyloid-β Generation

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