Ten things you should know about protein kinases: IUPHAR R eview 14

Axitinib in Metastatic Renal Cell Carcinoma: Results of a Pharmacokinetic and Pharmacodynamic Analysis

Rini, B. I., Garrett, M., Poland, B., Dutcher, J. P., Rixe, O., Wilding, G., Stadler, W. M., Pithavala, Y. K., Kim, S., Tarazi, J., et al. (2013) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.73 · Cited by 137

RAF Inhibitors Activate the MAPK Pathway by Relieving Inhibitory Autophosphorylation

Holderfield, M. T., Merritt, H., Chan, J., Wallroth, M., Tandeske, L., Zhai, H., Tellew, J. E., Hardy, S. F., Hekmat-Nejad, M., Stuart, D. D., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.03.033 · Cited by 134

Molecular Mechanism of SSR128129E, an Extracellularly Acting, Small-Molecule, Allosteric Inhibitor of FGF Receptor Signaling

Herbert, C., Schieborr, U., Saxena, K., Juraszek, J., Smet, F. D., Alcouffe, C., Bianciotto, M., Saladino, G., Sibrac, D., Kudlinzki, D., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.018 · Cited by 134

Potential Therapeutic Strategies to Overcome Acquired Resistance to BRAF or MEK Inhibitors in BRAF Mutant Cancers

Corcoran, R. B., Settleman, J. E., & Engelman, J. A. (2011) · Oncotarget · doi:10.18632/oncotarget.262 · Cited by 133

Targeting Cancer with Small-Molecular-Weight Kinase Inhibitors

Fabbro, D., Cowan‐Jacob, S. W., Möbitz, H., & Martiny‐Baron, G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-337-0_1 · Cited by 130

Classical PKC isoforms in cancer

Martiny‐Baron, G., & Fabbro, D. (2007) · Pharmacological Research · doi:10.1016/j.phrs.2007.04.001 · Cited by 129

A broad activity screen in support of a chemogenomic map for kinase signalling research and drug discovery

Gao, Y., Davies, S. P., Augustin, M. A., Woodward, A. M., Patel, U. A., Kovelman, R., & Harvey, K. J. (2013) · Biochemical Journal · doi:10.1042/bj20121418 · Cited by 128

Biomarker Development for the Clinical Activity of the mTOR Inhibitor Everolimus (RAD001): Processes, Limitations, and Further Proposals

O’Reilly, T., & McSheehy, P. M. J. (2010) · Translational Oncology · doi:10.1593/tlo.09277 · Cited by 128

Targeting B-Cell Receptor Signaling for Anticancer Therapy: The Bruton's Tyrosine Kinase Inhibitor Ibrutinib Induces Impressive Responses in B-Cell Malignancies

Wiestner, A. U. (2012) · Journal of Clinical Oncology · doi:10.1200/jco.2012.44.4281 · Cited by 125

BIBW-2992, a dual receptor tyrosine kinase inhibitor for the treatment of solid tumors.

Minkovsky, N., & Berezov, A. (2008) · PubMed · Cited by 124

Afatinib: emerging next-generation tyrosine kinase inhibitor for NSCLC

Agulnik, M., Nelson, Ziehr, & Johnson, J. R. (2013) · OncoTargets and Therapy · doi:10.2147/ott.s23165 · Cited by 124

Binding or Bending: Distinction of Allosteric Abl Kinase Agonists from Antagonists by an NMR-Based Conformational Assay

Jahnke, W., Grotzfeld, R. M., Pellé, X., Strauss, A., Fendrich, G., Cowan‐Jacob, S. W., Cotesta, S., Fabbro, D., Furet, P., Mestan, J., et al. (2010) · Journal of the American Chemical Society · doi:10.1021/ja101837n · Cited by 123

KIT Mutations in GIST

Fletcher, J. A., & Rubin, B. P. (2007) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2006.12.010 · Cited by 121

Sirolimus, a New, Potent Immunosuppressive Agent

Kelly, P. A., Gruber, S. A., Behbod, F., & Kahan, B. D. (1997) · Pharmacotherapy The Journal of Human Pharmacology and Drug Therapy · doi:10.1002/j.1875-9114.1997.tb03080.x · Cited by 119

Sunitinib malate for the treatment of solid tumours: a review of current clinical data

Motzer, R. J., Hoosen, S., Bello, C. L., & Christensen, J. G. (2006) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.15.5.553 · Cited by 119

Discovery and Characterization of a Cell-Permeable, Small-Molecule c-Abl Kinase Activator that Binds to the Myristoyl Binding Site

Yang, J., Campobasso, N., Biju, M. P., Fisher, K. E., Pan, X.-Q., Cottom, J., Galbraith, S., Ho, T. F., Zhang, H., Hong, X., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.12.013 · Cited by 113

The Role of Erlotinib (Tarceva, OSI 774) in the Treatment of Non-Small Cell Lung Cancer

Perez-Soler, R. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-040017 · Cited by 110

Targeting Energy Metabolic and Oncogenic Signaling Pathways in Triple-negative Breast Cancer by a Novel Adenosine Monophosphate-activated Protein Kinase (AMPK) Activator

Lee, K., Hsu, E., Guh, J., Yang, M., Wang, D.-S., Kulp, S. K., Shapiro, C. L., & Chen, C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.264598 · Cited by 107

Archaeal protein kinases and protein phosphatases: insights from genomics and biochemistry

Kennelly, P. J. (2003) · Biochemical Journal · doi:10.1042/bj20021547 · Cited by 106

Bcr-Abl inhibition as a modality of CML therapeutics

Buchdunger, E., Matter, A., & Druker, B. J. (2001) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(01)00022-1 · Cited by 102

Cyclotraxin-B, the First Highly Potent and Selective TrkB Inhibitor, Has Anxiolytic Properties in Mice

Cazorla, M., Jouvenceau, A., Rose, C., Guilloux, J.-P., Pilon, C., Dranovsky, A., & Prémont, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009777 · Cited by 99

Protein kinases and phosphatases as therapeutic targets in cancer

Ventura, J., & Nebreda, Á. R. (2006) · Clinical & Translational Oncology · doi:10.1007/s12094-006-0005-0 · Cited by 98

Sirolimus: A new agent for prevention of renal allograft rejection

Vasquez, E. M. (2000) · American Journal of Health-System Pharmacy · doi:10.1093/ajhp/57.5.437 · Cited by 96

CP-690550, a JAK3 inhibitor as an immunosuppressant for the treatment of rheumatoid arthritis, transplant rejection, psoriasis and other immune-mediated disorders.

West, K. (2009) · PubMed · Cited by 95

Mechanisms of resistance to small molecule kinase inhibition in the treatment of solid tumors

Rubin, B. P., & Duensing, A. U. (2006) · Laboratory Investigation · doi:10.1038/labinvest.3700466 · Cited by 93

Structural biology of protein tyrosine kinases

Cowan‐Jacob, S. W. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6202-8 · Cited by 92

Role of c-kit/SCF in cause and treatment of gastrointestinal stromal tumors (GIST)

Ali, S., & Ali, S. (2007) · Gene · doi:10.1016/j.gene.2007.06.017 · Cited by 92

Novel Approaches for Targeting Kinases: Allosteric Inhibition, Allosteric Activation and Pseudokinases

Cowan‐Jacob, S. W., Jahnke, W., & Knapp, S. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.13.216 · Cited by 91

Why do Kinase Inhibitors Cause Cardiotoxicity and What can be Done About It?

Cheng, H., & Force, T. L. (2010) · Progress in Cardiovascular Diseases · doi:10.1016/j.pcad.2010.06.006 · Cited by 90

Everolimus plus exemestane as first-line therapy in HR+, HER2− advanced breast cancer in BOLERO-2

Beck, J. T., Hortobágyi, G. N., Campone, M., Lebrun, F., Deleu, I., Rugo, H. S., Pistilli, B., Masuda, N., Hart, L. L., Melichar, B., et al. (2013) · Breast Cancer Research and Treatment · doi:10.1007/s10549-013-2814-5 · Cited by 89

Patterns of Pulmonary Complications Associated with Sirolimus

Chhajed, P. N., Dickenmann, M., Bubendorf, L., et al. (2005) · Respiration · doi:10.1159/000087945 · Cited by 89

Epidermal Growth Factor Receptor Inhibitors in Development for the Treatment of Non–Small Cell Lung Cancer

Heymach, J. V., Nilsson, M. B., Blumenschein, G., Papadimitrakopoulou, V. A., & Herbst, R. S. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-0286 · Cited by 88

Ponatinib: A Review of Its Use in Adults with Chronic Myeloid Leukaemia or Philadelphia Chromosome-Positive Acute Lymphoblastic Leukaemia

Hoy, S. M. (2014) · Drugs · doi:10.1007/s40265-014-0216-6 · Cited by 88

A cell-based immunocytochemical assay for monitoring kinase signaling pathways and drug efficacy

Chen, H., Kovar, J. L., Sissons, S. E., Cox, K. L., Matter, W. F., Chadwell, F., Luan, P., Vlahos, C. J., Schutz-Geschwender, A. R., & Olive, D. M. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.11.015 · Cited by 87

Tyrosine kinase inhibitors as potential drugs for B-cell lymphoid malignancies and autoimmune disorders

Robak, T., & Robak, E. (2012) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2012.685650 · Cited by 86

Compensatory Pathways in Oncogenic Kinase Signaling and Resistance to Targeted Therapies: Six Degrees of Separation

Trusolino, L., & Bertotti, A. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0400 · Cited by 86

Vandetanib for the Treatment of Medullary Thyroid Cancer

Chau, N. G., & Haddad, R. I. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-2353 · Cited by 86

Structure-Based Design, Synthesis, and Biological Evaluation of Potent and Selective Macrocyclic Checkpoint Kinase 1 Inhibitors

Tao, Z., Wang, L., Stewart, K. D., Chen, Z., Gu, W., Bui, M.-H., Merta, P. J., Zhang, H., Kovar, P. J., Johnson, E. F., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061247v · Cited by 84

Substrate-Selective Inhibition of Protein Kinase PDK1 by Small Compounds that Bind to the PIF-Pocket Allosteric Docking Site

Busschots, K., Lopez-Garcia, L. A., Lammi, C., Stroba, A., Zeuzem, S., Piiper, A., Alzari, P. M., Neimanis, S., Arencibia, J. M., Engel, M., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.07.017 · Cited by 84

Cabozantinib (XL184) for the Treatment of Locally Advanced or Metastatic Progressive Medullary Thyroid Cancer

Viola, D., Cappagli, V., & Elisei, R. (2013) · Future Oncology · doi:10.2217/fon.13.128 · Cited by 84

The BCR-ABLT315I mutation compromises survival in chronic phase chronic myelogenous leukemia patients resistant to tyrosine kinase inhibitors, in a matched pair analysis

Nicolini, F. E., Ibrahim, A. R., Soverini, S., Martinelli, G., Müller, M. C., Hochhaus, A., Dufva, I. H., Kim, D.-W., Cortes, J. E., Mauro, M. J., et al. (2013) · Haematologica · doi:10.3324/haematol.2012.080234 · Cited by 81

Discovery and Characterization of Non-ATP Site Inhibitors of the Mitogen Activated Protein (MAP) Kinases

Comess, K. M., Sun, C. C., Abad‐Zapatero, C., Goedken, E. R., Gum, R. J., Borhani, D. W., Argiriadi, M. A., Groebe, D. R., Jia, Y., Clampit, J. E., et al. (2010) · ACS Chemical Biology · doi:10.1021/cb1002619 · Cited by 80

Naphthalenesulfonamides as calmodulin antagonists and protein kinase inhibitors.

Inagaki, M., Kawamoto, S., Itoh, H., Saitoh, M., Hagiwara, M., Takahashi, J., & Hidaka, H. (1986) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10284-8 · Cited by 77

Dual irreversible kinase inhibitors: Quinazoline-based inhibitors incorporating two independent reactive centers with each targeting different cysteine residues in the kinase domains of EGFR and VEGFR-2

Wissner, A., Fraser, H. L., Ingalls, C. L., Dushin, R. G., Floyd, M. B., Cheung, K., Nittoli, T., Ravi, M., Tan, X., & Loganzo, F. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.03.055 · Cited by 76

Development of thioquinazolinones, allosteric Chk1 kinase inhibitors

Converso, A., Hartingh, T. J., Garbaccio, R. M., Tasber, E. S., Rickert, K. W., Fraley, M. E., Yan, Y., Kreatsoulas, C., Stirdivant, S. M., Drakas, B. A., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.12.076 · Cited by 75

Small Molecule Glucokinase Activators as Glucose Lowering Agents: A New Paradigm for Diabetes Therapy

Guertin, K. R., & Grimsby, J. S. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706777452551 · Cited by 72

Quercetin inhibits tyrosine phosphorylation by the cyclic nucleotide-independent, transforming protein kinase, pp60src

Glossmann, H. H., Presek, P., & EIGENBRODT, E. (1981) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf00506266 · Cited by 70

Discovery of selective irreversible inhibitors for EGFR-T790M

Zhou, W., Ercan, D., Janne, P. A., & Gray, N. S. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.12.036 · Cited by 67

A Blueprint for Advancing Genetics-Based Cancer Therapy

Sellers, W. R. (2011) · Cell · doi:10.1016/j.cell.2011.09.016 · Cited by 66

Allosteric Regulation of Protein Kinase PKCζ by the N-Terminal C1 Domain and Small Compounds to the PIF-Pocket

Lopez-Garcia, L. A., Schulze, J. O., Fröhner, W., Zhang, H., Süß, E., Weber, N., Navratil, J., Amon, S., Hindie, V., Zeuzem, S., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.08.010 · Cited by 65

Afatinib Prolongs Survival Compared with Gefitinib in an Epidermal Growth Factor Receptor-Driven Lung Cancer Model

Ninomiya, T., Takigawa, N., Ichihara, E., Ochi, N., Murakami, T., Honda, Y., Kubo, T., Minami, D., Kudo, K., Tanimoto, M., et al. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0885 · Cited by 65

Inhibitors of the Abl kinase directed at either the ATP- or myristate-binding site

Fabbro, D., Manley, P. W., Jahnke, W., Liebetanz, J., Szyttenholm, A., Fendrich, G., Strauss, A., Zhang, J., Gray, N. S., Adrián, F., et al. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.009 · Cited by 64

Enhancing mTOR-targeted cancer therapy

Wang, X., & Sun, S. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903225008 · Cited by 60

Genome-based cancer therapeutics: targets, kinase drug resistance and future strategies for precision oncology

Workman, P., Al‐Lazikani, B., & Clarke, P. A. (2013) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2013.06.004 · Cited by 60

Structure-based discovery of cellular-active allosteric inhibitors of FAK

Tomita, N., Hayashi, Y., Suzuki, S., Oomori, Y., Aramaki, Y., Matsushita, Y., Iwatani, M., Iwata, H., Okabe, A., Awazu, Y., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.01.047 · Cited by 59

Discovery and Biological Evaluation of Potent Dual ErbB-2/EGFR Tyrosine Kinase Inhibitors: 6-Thiazolylquinazolines

Gaul, M. D., Guo, Y. C., Affleck, K., Cockerill, G. S., Gilmer, T. M., Griffin, R., Guntrip, S. B., Keith, B. R., Knight, W. B., Mullin, R. J., et al. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)01047-8 · Cited by 58

Allosteric Protein Kinase Regulation by Pseudokinases: Insights from STRAD

Rajakulendran, T., & Sicheri, F. (2010) · Science Signaling · doi:10.1126/scisignal.3111pe8 · Cited by 56

Trametinib (GSK1120212) in the treatment of melanoma

Salama, A. K. S., & Kim, K. B. (2013) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.2013.770475 · Cited by 56

Drugging cancer genomes

Workman, P., & Al‐Lazikani, B. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4184 · Cited by 55

Structural biology contributions to tyrosine kinase drug discovery

Cowan‐Jacob, S. W., Möbitz, H., & Fabbro, D. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.01.012 · Cited by 54

Differential action of small molecule HER kinase inhibitors on receptor heterodimerization: Therapeutic implications

Sánchez‐Martín, M., & Pandiella, A. (2011) · International Journal of Cancer · doi:10.1002/ijc.26358 · Cited by 52

Characterization of the CHK1 Allosteric Inhibitor Binding Site

Vanderpool, D. L., Johnson, T. O., Chen, P., Bergqvist, S., Alton, G., Phonephaly, S., Rui, E. Y., Luo, C., Deng, Y., Grant, S. K., et al. (2009) · Biochemistry · doi:10.1021/bi900258v · Cited by 49

Allosteric IGF-1R Inhibitors

Heinrich, T., Grädler, U., Böttcher, H., Blaukat, A., & Shutes, A. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100044h · Cited by 49

Beyond the MEK-pocket: Can current MEK kinase inhibitors be utilized to synthesize novel type III NCKIs? Does the MEK-pocket exist in kinases other than MEK?

Tecle, H., Shao, J., Li, Y., Kothe, M., Kazmirski, S. L., Penzotti, J. E., Ding, Y., Ohren, J. F., Moshinsky, D., Coli, R., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.10.108 · Cited by 45

Small Molecule Insulin Receptor Activators Potentiate Insulin Action in Insulin-Resistant Cells

Li, M., YOUNGREN, J. F., Manchem, V. P., Kozlowski, M. R., Zhang, B. B., Maddux, B. A., & Goldfine, I. D. (2001) · Diabetes · doi:10.2337/diabetes.50.10.2323 · Cited by 45

Rethinking Pseudokinases

Kannan, N., & Taylor, S. S. (2008) · Cell · doi:10.1016/j.cell.2008.04.005 · Cited by 45

Omics and therapy – A basis for precision medicine

Garay, J. P., & Gray, J. W. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.02.009 · Cited by 43

Profile of bosutinib and its clinical potential in the treatment of chronic myeloid leukemia

Koschmieder, S., & Keller-v.Amsberg (2013) · OncoTargets and Therapy · doi:10.2147/ott.s19901 · Cited by 40

Targeting kinases: a new approach to treating inflammatory rheumatic diseases

Simmons, D. L. (2013) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2013.02.008 · Cited by 39

Regulation of Insulin Receptor Function by a Small Molecule Insulin Receptor Activator

Pender, C., Goldfine, I. D., Manchem, V. P., Evans, J. L., Spevak, W. R., Shi, S., Rao, S., Bajjalieh, S., Maddux, B. A., & YOUNGREN, J. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202426200 · Cited by 37

Kinase inhibition-related adverse events predicted from in vitro kinome and clinical trial data

Yang, X. H., Huang, Y., Crowson, M. G., Li, J., Maitland, M. L., & Lussier, Y. A. (2010) · Journal of Biomedical Informatics · doi:10.1016/j.jbi.2010.04.006 · Cited by 36

Profiling the kinome: Current capabilities and future challenges

Knight, J. D. R., Pawson, T. J., & Gingras, A. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.10.015 · Cited by 30

Targeting Diverse Signaling Interaction Sites Allows the Rapid Generation of Bivalent Kinase Inhibitors

Hill, Z. B., Perera, B. G. K., Andrews, S., & Maly, D. J. (2011) · ACS Chemical Biology · doi:10.1021/cb200387g · Cited by 28

Taking PI3Kδ and PI3Kγ One Step Ahead: Dual Active PI3Kδ/γ Inhibitors for the Treatment of Immune-Mediated Inflammatory Diseases

Rommel, C. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_79 · Cited by 24

Dabrafenib in the treatment of advanced melanoma

Medina, T. M., Amaria, M. N., & Jimeno, A. (2013) · Drugs of today · doi:10.1358/dot.2013.49.6.1968669 · Cited by 22

Ibrutinib for the treatment of chronic lymphocytic leukemia and mantle cell lymphoma

McDermott, J. D., & Jimeno, A. (2014) · Drugs of today · doi:10.1358/dot.2014.50.4.2133570 · Cited by 22

A screen to identify drug resistant variants to target-directed anti-cancer agents

Azam, M., Raz, T., Nardi, V., Opitz, S. L., & Daley, G. Q. (2003) · Biological Procedures Online · doi:10.1251/bpo63 · Cited by 22

Targeting kinases for the treatment of inflammatory diseases

Müller, S., & Knapp, S. (2010) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2010.504203 · Cited by 22

DEF Pocket in p38α Facilitates Substrate Selectivity and Mediates Autophosphorylation

Tzarum, N., Komornik, N., Chetrit, D. B., Engelberg, D., & Livnah, O. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.464511 · Cited by 22

Kinase dysfunction and kinase inhibitors

London, C. A. (2013) · Veterinary Dermatology · doi:10.1111/j.1365-3164.2012.01081.x · Cited by 19

Ibrutinib and Indolent B-Cell Lymphomas

Akinleye, A., Furqan, M., & Adekunle, O. (2013) · Clinical Lymphoma Myeloma & Leukemia · doi:10.1016/j.clml.2013.11.005 · Cited by 19

Targeted Therapy with Imatinib: An Exception or a Rule?

Fabbro, D., Fendrich, G., Guez, V., Meyer, T., Furet, P., Mestan, J., Griffin, J. D., Manley, P. W., & Cowan‐Jacob, S. W. (2005) · Springer eBooks · doi:10.1007/3-540-26670-4_13 · Cited by 8

Regorafenib: from bench to bedside in colorectal cancer

Shahda, S., & Saif, M. W. (2013) · Expert Review of Clinical Pharmacology · doi:10.1586/ecp.13.11 · Cited by 5

Natural products as sources of new drugs from 1981 to 2014

Newman, D. J., & Cragg, G. M. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.5b01055 · Cited by 5,858

The harmonizome: a collection of processed datasets gathered to serve and mine knowledge about genes and proteins

Rouillard, A. D., Gundersen, G. W., Fernandez, N. F., Wang, Z., Monteiro, C. D., McDermott, M. G., & Ma’ayan, A. (2016) · Database · doi:10.1093/database/baw100 · Cited by 1,515

Kinase-targeted cancer therapies: progress, challenges and future directions

Bhullar, K. S., Lagarón, N. O., McGowan, E. M., Parmar, I., Jha, A., Hubbard, B. P., & Rupasinghe, H. P. V. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0804-2 · Cited by 1,245

Classification of small molecule protein kinase inhibitors based upon the structures of their drug-enzyme complexes

Roskoski, R. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2015.10.021 · Cited by 886

The target landscape of clinical kinase drugs

Klaeger, S., Heinzlmeir, S., Wilhelm, M., Polzer, H., Vick, B., Koenig, P.-A., Reinecke, M., Ruprecht, B., Petzoldt, S., Meng, C., et al. (2017) · Science · doi:10.1126/science.aan4368 · Cited by 854