FDA-approved small-molecule kinase inhibitors

The biology of VEGF and its receptors

Ferrara, N., Gerber, H.-P., & LeCouter, J. (2003) · Nature Medicine · doi:10.1038/nm0603-669 · Cited by 9,591

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145

Efficacy and Safety of a Specific Inhibitor of the BCR-ABL Tyrosine Kinase in Chronic Myeloid Leukemia

Druker, B. J., Talpaz, M., Resta, D. J., Peng, B., Buchdunger, E., Ford, J. M., Lydon, N. B., Kantarjian, H., Capdeville, R., Ohno-Jones, S., et al. (2001) · New England Journal of Medicine · doi:10.1056/nejm200104053441401 · Cited by 5,243

ERBB receptors and cancer: the complexity of targeted inhibitors

Hynes, N. E., & Lane, H. A. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1609 · Cited by 3,313

Combined BRAF and MEK inhibition in melanoma with BRAF V600 mutations

Flaherty, K. T., Infante, J. R., Daud, A., Gonzalez, R., Kefford, R. F., Sosman, J., Hamid, O., Schuchter, L., Cebon, J., Ibrahim, N., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1210093 · Cited by 2,810

Mechanism of Activation of the RAF-ERK Signaling Pathway by Oncogenic Mutations of B-RAF

Wan, P. T. C., Garnett, M. J., Roe, S. M., Lee, S., Niculescu-Duvaz, D., Good, V. M., Project, C. G., Jones, C. M., Marshall, C. J., Springer, C. J., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00215-6 · Cited by 2,808

Comprehensive analysis of kinase inhibitor selectivity

Davis, M. I., Hunt, J. P., Herrgard, S., Ciceri, P., Wodicka, L. M., Pallares, G., Hocker, M., Treiber, D. K., & Zarrinkar, P. P. (2011) · Nature Biotechnology · doi:10.1038/nbt.1990 · Cited by 2,409

Targeting BTK with Ibrutinib in Relapsed Chronic Lymphocytic Leukemia

Byrd, J. C., Furman, R. R., Coutre, S. E., Flinn, I. W., Burger, J. A., Blum, K. A., Grant, B., Sharman, J. P., Coleman, M., Wierda, W. G., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1215637 · Cited by 2,270

EGF–ERBB signalling: towards the systems level

Citri, A., & Yarden, Y. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1962 · Cited by 2,004

Combined BRAF and MEK Inhibition versus BRAF Inhibition Alone in Melanoma

Long, G. V., Stroyakovskiy, D., Gogas, H., Levchenko, E., de Braud, F., Larkin, J., Garbe, C., Jouary, T., Hauschild, A., Grob, J. J., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1406037 · Cited by 1,899

Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma

Bollag, G., Hirth, P., Tsai, J., Zhang, J., Ibrahim, P. N., Cho, H., Spevak, W., Zhang, C., Zhang, Y., Habets, G., et al. (2010) · Nature · doi:10.1038/nature09454 · Cited by 1,831

Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

Knighton, D. R., Zheng, J., Ten Eyck, L. F., Ashford, V. A., Xuong, N.-H., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,759

Activities at the Universal Protein Resource (UniProt)

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Idelalisib and Rituximab in Relapsed Chronic Lymphocytic Leukemia

Furman, R. R., Sharman, J. P., Coutre, S. E., Cheson, B. D., Pagel, J. M., Hillmen, P., Barrientos, J. C., Zelenetz, A. D., Kipps, T. J., Flinn, I., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1315226 · Cited by 1,710

PI3K and cancer: lessons, challenges and opportunities

Fruman, D. A., & Rommel, C. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4204 · Cited by 1,709

Structure of the Epidermal Growth Factor Receptor Kinase Domain Alone and in Complex with a 4-Anilinoquinazoline Inhibitor

Stamos, J., Sliwkowski, M. X., & Eigenbrot, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207135200 · Cited by 1,574

Ceritinib in ALK -Rearranged Non–Small-Cell Lung Cancer

Shaw, A. T., Kim, D.-W., Mehra, R., Tan, D. S. W., Felip, E., Chow, L. Q. M., Camidge, D. R., Vansteenkiste, J., Sharma, S., De Pas, T., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1311107 · Cited by 1,495

An Adenosine 3′,5′-Monophosphate-dependant Protein Kinase from Rabbit Skeletal Muscle

Walsh, D. A., Perkins, J. P., & Krebs, E. G. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34204-8 · Cited by 1,445

MET signalling: principles and functions in development, organ regeneration and cancer

Trusolino, L., Bertotti, A., & Comoglio, P. M. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3012 · Cited by 1,240

Protein Kinase Inhibitors: Insights into Drug Design from Structure

Noble, M. E. M., Endicott, J. A., & Johnson, L. N. (2004) · Science · doi:10.1126/science.1095920 · Cited by 1,198

Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

Yun, C.-H., Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., & Eck, M. J. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.12.017 · Cited by 1,192

The origins of protein phosphorylation

Cohen, P. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e127 · Cited by 1,139

A Unique Structure for Epidermal Growth Factor Receptor Bound to GW572016 (Lapatinib)

Wood, E. R., Truesdale, A. T., McDonald, O. B., Yuan, D., Hassell, A., Dickerson, S. H., Ellis, B., Pennisi, C., Horne, E., Lackey, K., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1168 · Cited by 1,122

Structure Based Drug Design of Crizotinib (PF-02341066), a Potent and Selective Dual Inhibitor of Mesenchymal–Epithelial Transition Factor (c-MET) Kinase and Anaplastic Lymphoma Kinase (ALK)

Cui, J. J., Tran-Dubé, M., Shen, H., Nambu, M., Kung, P.-P., Pairish, M., Jia, L., Meng, J., Funk, L., Botrous, I., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2007613 · Cited by 932

Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571).

Nagar, B., Bornmann, W. G., Pellicena, P., Schindler, T. H., Veach, D. R., Miller, W. T., Clarkson, B. D., & Kuriyan, J. (2002) · PubMed · Cited by 923

The anaplastic lymphoma kinase in the pathogenesis of cancer

Chiarle, R., Voena, C., Ambrogio, C., Piva, R., & Inghirami, G. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2291 · Cited by 882

Target Binding Properties and Cellular Activity of Afatinib (BIBW 2992), an Irreversible ErbB Family Blocker

Solca, F., Dahl, G., Zoephel, A., Bader, G., Sanderson, M., Klein, C., Kraemer, O., Himmelsbach, F., Haaksma, E., & Adolf, G. R. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.197756 · Cited by 865

The ALK Inhibitor Ceritinib Overcomes Crizotinib Resistance in Non–Small Cell Lung Cancer

Friboulet, L., Li, N., Katayama, R., Lee, C. C., Gainor, J. F., Crystal, A. S., Michellys, P.-Y., Awad, M. M., Yanagitani, N., Kim, S., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0846 · Cited by 840

Vemurafenib: the first drug approved for BRAF-mutant cancer

Bollag, G., Tsai, J., Zhang, J., Zhang, C., Ibrahim, P., Nolop, K., & Hirth, P. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3847 · Cited by 822

Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation

Whitman, M., Kaplan, D. R., Schaffhausen, B., Cantley, L., & Roberts, T. M. (1985) · Nature · doi:10.1038/315239a0 · Cited by 810

Vascular endothelial growth factor B, a novel growth factor for endothelial cells.

Olofsson, B., Pajusola, K., Kaipainen, A., von Euler, G., Joukov, V, Saksela, O., Orpana, A., Pettersson, R. F., Alitalo, K., & Eriksson, U. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.6.2576 · Cited by 803

JAK/STAT, Raf/MEK/ERK, PI3K/Akt and BCR-ABL in cell cycle progression and leukemogenesis

Steelman, L. S., Pohnert, S. C., Shelton, J. G., Franklin, R. A., Bertrand, F. E., & McCubrey, J. A. (2004) · Leukemia · doi:10.1038/sj.leu.2403241 · Cited by 684

Update on activities at the Universal Protein Resource (UniProt) in 2013

The UniProt Consortium (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1068 · Cited by 672

Structural Basis for Control by Phosphorylation

Johnson, L. N., & Lewis, R. J. (2001) · Chemical Reviews · doi:10.1021/cr000225s · Cited by 636

Kinetic and Catalytic Mechanisms of Protein Kinases

Adams, J. A. (2001) · Chemical Reviews · doi:10.1021/cr000230w · Cited by 627

Discovery and Development of Janus Kinase (JAK) Inhibitors for Inflammatory Diseases: Miniperspective

Clark, J. D., Flanagan, M. E., & Telliez, J.-B. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401490p · Cited by 601

Tyrphostins I: synthesis and biological activity of protein tyrosine kinase inhibitors

Gazit, A., Yaish, P., Gilon, C., & Levitzki, A. (1989) · Journal of Medicinal Chemistry · doi:10.1021/jm00130a020 · Cited by 600

Molecular conformations, interactions, and properties associated with drug efficiency and clinical performance among VEGFR TK inhibitors

McTigue, M., Murray, B. W., Chen, J. H., Deng, Y.-L., Solowiej, J., & Kania, R. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207759109 · Cited by 592

Idelalisib, an inhibitor of phosphatidylinositol 3-kinase p110δ, for relapsed/refractory chronic lymphocytic leukemia

Brown, J. R., Byrd, J. C., Coutre, S. E., Benson, D. M., Flinn, I. W., Wagner-Johnston, N. D., Spurgeon, S. E., Kahl, B. S., Bello, C., Webb, H. K., et al. (2014) · Blood · doi:10.1182/blood-2013-11-535047 · Cited by 590

Blocking of EGF-Dependent Cell Proliferation by EGF Receptor Kinase Inhibitors

Yaish, P., Gazit, A., Gilon, C., & Levitzki, A. (1988) · Science · doi:10.1126/science.3263702 · Cited by 587

THE ENZYMATIC PHOSPHORYLATION OF PROTEINS

Burnett, G., & Kennedy, E. P. (1954) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71184-8 · Cited by 582

Targeting Bruton's tyrosine kinase in B cell malignancies

Hendriks, R. W., Yuvaraj, S., & Kil, L. P. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3702 · Cited by 552

ENCODE Project Writes Eulogy for Junk DNA

Pennisi, E. (2012) · Science · doi:10.1126/science.337.6099.1159 · Cited by 545

CONVERSION OF PHOSPHORYLASE b TO PHOSPHORYLASE a IN MUSCLE EXTRACTS

Fischer, E. H., & Krebs, E. G. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52289-x · Cited by 543

Inactivation of PI(3)K p110δ breaks regulatory T-cell-mediated immune tolerance to cancer

Ali, K., Soond, D. R., Piñeiro, R., Hagemann, T., Pearce, W., Lim, E. L., Bouabe, H., Scudamore, C. L., Hancox, T., Maecker, H., et al. (2014) · Nature · doi:10.1038/nature13444 · Cited by 529

The phosphorylase b to a converting enzyme of rabbit skeletal muscle

Krebs, E. G., & Fischer, E. H. (1956) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(56)90273-6 · Cited by 484

Exploration of Type II Binding Mode: A Privileged Approach for Kinase Inhibitor Focused Drug Discovery?

Zhao, Z., Wu, H., Wang, L., Liu, Y., Knapp, S., Liu, Q., & Gray, N. S. (2014) · ACS Chemical Biology · doi:10.1021/cb500129t · Cited by 433

Acquired Resistance to Crizotinib from a Mutation in CD74–ROS1

Awad, M. M., Katayama, R., McTigue, M., Liu, W., Deng, Y.-L., Brooun, A., Friboulet, L., Huang, D., Falk, M. D., Timofeevski, S., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1215530 · Cited by 416

New anti-inflammatory targets for chronic obstructive pulmonary disease

Barnes, P. J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4025 · Cited by 392

Discovery of 5-[[4-[(2,3-Dimethyl-2 H-indazol-6-yl)methylamino]-2-pyrimidinyl]amino]-2-methyl-benzenesulfonamide (Pazopanib), a Novel and Potent Vascular Endothelial Growth Factor Receptor Inhibitor

Harris, P. A., Boloor, A., Cheung, M., Kumar, R., Crosby, R. M., Davis-Ward, R. G., Epperly, A. H., Hinkle, K. W., Hunter, R. N., Johnson, J. H., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800566m · Cited by 352

Novel Agents on the Horizon for Cancer Therapy

Ma, W. W., & Adjei, A. A. (2009) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.20003 · Cited by 304

Structure and Chemical Inhibition of the RET Tyrosine Kinase Domain

Knowles, P. P., Murray-Rust, J., Kjær, S., Scott, R. P., Hanrahan, S., Santoro, M., Ibáñez, C. F., & McDonald, N. Q. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605604200 · Cited by 302

An ERK/Cdk5 axis controls the diabetogenic actions of PPARγ

Banks, A. S., McAllister, F. E., Camporez, J. P. G., Zushin, P.-J. H., Jurczak, M. J., Laznik-Bogoslavski, D., Shulman, G. I., Gygi, S. P., & Spiegelman, B. M. (2015) · Nature · doi:10.1038/nature13887 · Cited by 297

The p110δ structure: mechanisms for selectivity and potency of new PI(3)K inhibitors

Berndt, A., Miller, S., Williams, O., Le, D. D., Houseman, B. T., Pacold, J. I., Gorrec, F., Hon, W.-C., Ren, P., Liu, Y., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.293 · Cited by 292

Molecularly targeted cancer therapy: some lessons from the past decade

Huang, M., Shen, A., Ding, J., & Geng, M. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.11.004 · Cited by 291

Distinct binding mode of multikinase inhibitor lenvatinib revealed by biochemical characterization.

Okamoto, K., Ikemori-Kawada, M., Jestel, A., von König, K., Funahashi, Y., Matsushima, T., Tsuruoka, A., Inoue, A., & Matsui, J. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/ml500394m · Cited by 285

An essential role of the JAK-STAT pathway in ischemic preconditioning

Xuan, Y.-T., Guo, Y., Han, H., Zhu, Y., & Bolli, R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161283798 · Cited by 285

The Druggable Genome: Evaluation of Drug Targets in Clinical Trials Suggests Major Shifts in Molecular Class and Indication

Rask-Andersen, M., Masuram, S., & Schiöth, H. B. (2014) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-135943 · Cited by 282

Signaling through cyclin D-dependent kinases

Choi, Y. J., & Anders, L. (2014) · Oncogene · doi:10.1038/onc.2013.137 · Cited by 278

Current treatment strategies for inhibiting mTOR in cancer

Chiarini, F., Evangelisti, C., McCubrey, J. A., & Martelli, A. M. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.11.004 · Cited by 275

Dissecting Specificity in the Janus Kinases: The Structures of JAK-Specific Inhibitors Complexed to the JAK1 and JAK2 Protein Tyrosine Kinase Domains

Williams, N. K., Bamert, R. S., Patel, O., Wang, C., Walden, P. M., Wilks, A. F., Fantino, E., Rossjohn, J., & Lucet, I. S. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.01.041 · Cited by 270

Feedback Suppression of PI3Kα Signaling in PTEN-Mutated Tumors Is Relieved by Selective Inhibition of PI3Kβ

Schwartz, S., Wongvipat, J., Trigwell, C. B., Hancox, U., Carver, B. S., Rodrik-Outmezguine, V., Will, M., Yellen, P., de Stanchina, E., Baselga, J., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2014.11.008 · Cited by 246

ALK inhibitors in non-small cell lung cancer: crizotinib and beyond.

Awad, M. M., & Shaw, A. T. (2014) · PubMed · Cited by 245

Crystal structure of the HGF β‐chain in complex with the Sema domain of the Met receptor

Stamos, J., Lazarus, R. A., Yao, X., Kirchhofer, D., & Wiesmann, C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600243 · Cited by 240

Structural and Thermodynamic Characterization of the TYK2 and JAK3 Kinase Domains in Complex with CP-690550 and CMP-6

Chrencik, J. E., Patny, A., Leung, I. K., Korniski, B., Emmons, T. L., Hall, T., Weinberg, R. A., Gormley, J. A., Williams, J. M., Day, J. E., et al. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.020 · Cited by 227

Idelalisib, a selective inhibitor of phosphatidylinositol 3-kinase-δ, as therapy for previously treated indolent non-Hodgkin lymphoma

Flinn, I. W., Kahl, B. S., Leonard, J. P., Furman, R. R., Brown, J. R., Byrd, J. C., Wagner-Johnston, N. D., Coutre, S. E., Benson, D. M., Peterman, S., et al. (2014) · Blood · doi:10.1182/blood-2013-11-538546 · Cited by 210

Insights into the Aberrant Activity of Mutant EGFR Kinase Domain and Drug Recognition

Gajiwala, K. S., Feng, J., Ferre, R., Ryan, K., Brodsky, O., Weinrich, S., Kath, J. C., & Stewart, A. (2013) · Structure · doi:10.1016/j.str.2012.11.014 · Cited by 204

Measurement of PIP3 Levels Reveals an Unexpected Role for p110β in Early Adaptive Responses to p110α-Specific Inhibitors in Luminal Breast Cancer

Costa, C., Ebi, H., Martini, M., Beausoleil, S. A., Faber, A. C., Jakubik, C. T., Huang, A., Wang, Y., Nishtala, M., Hall, B., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2014.11.007 · Cited by 203

Cabozantinib Overcomes Crizotinib Resistance in ROS1 Fusion–Positive Cancer

Katayama, R., Kobayashi, Y., Friboulet, L., Lockerman, E. L., Koike, S., Shaw, A. T., Engelman, J. A., & Fujita, N. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1385 · Cited by 201

Strategies for the Selective Regulation of Kinases with Allosteric Modulators: Exploiting Exclusive Structural Features

Fang, Z., Grütter, C., & Rauh, D. (2013) · ACS Chemical Biology · doi:10.1021/cb300663j · Cited by 197

Discovery of a Highly Potent and Selective MEK Inhibitor: GSK1120212 (JTP-74057 DMSO Solvate)

Abe, H., Kikuchi, S., Hayakawa, K., Iida, T., Nagahashi, N., Maeda, K., Sakamoto, J., Matsumoto, N., Miura, T., Matsumura, K., et al. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200004g · Cited by 196

An antiangiogenic isoform of VEGF-A contributes to impaired vascularization in peripheral artery disease

Kikuchi, R., Nakamura, K., MacLauchlan, S., Ngo, D. T.-M., Shimizu, I., Fuster, J. J., Katanasaka, Y., Yoshida, S., Qiu, Y., Yamaguchi, T. P., et al. (2014) · Nature Medicine · doi:10.1038/nm.3703 · Cited by 195

Mechanism of Activation and Inhibition of the HER4/ErbB4 Kinase

Qiu, C., Tarrant, M. K., Choi, S. H., Sathyamurthy, A., Bose, R., Banjade, S., Pal, A., Bornmann, W. G., Lemmon, M. A., Cole, P. A., et al. (2008) · Structure · doi:10.1016/j.str.2007.12.016 · Cited by 191

Tyrosine Kinase Inhibitors: Views of Selectivity, Sensitivity, and Clinical Performance

Levitzki, A. (2013) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011112-140341 · Cited by 186

Overview of cyclins D1 function in cancer and the CDK inhibitor landscape: past and present

Casimiro, M. C., Velasco-Velázquez, M., Aguirre-Alvarado, C., & Pestell, R. G. (2014) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2014.867017 · Cited by 184

Approaches to discover non-ATP site kinase inhibitors

Gavrin, L. K., & Saiah, E. (2013) · MedChemComm · doi:10.1039/c2md20180a · Cited by 184

New Directions in Targeting Protein Kinases: Focusing Upon True Allosteric and Bivalent Inhibitors

Lamba, V., & Ghosh, I. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212800672813 · Cited by 182

Advances in kinase targeting: current clinical use and clinical trials

Rask-Andersen, M., Zhang, J., Fabbro, D., & Schiöth, H. B. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.09.007 · Cited by 181

A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivity

Levinson, N. M., & Boxer, S. G. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1404 · Cited by 171

Molecular Pathways: Molecular Basis for Sensitivity and Resistance to JAK Kinase Inhibitors

Meyer, S. C., & Levine, R. L. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0279 · Cited by 159

Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases

Marcotte, D. J., Liu, Y., Arduini, R. M., Hession, C. A., Miatkowski, K., Wildes, C. P., Cullen, P. F., Hong, V. S., Hopkins, B. T., Mertsching, E., et al. (2010) · Protein Science · doi:10.1002/pro.321 · Cited by 158

Structural, Biochemical, and Biophysical Characterization of Idelalisib Binding to Phosphoinositide 3-Kinase δ

Somoza, J. R., Koditek, D., Villaseñor, A. G., Novikov, N. Y., Wong, M. H. L., Liclican, A. C., Xing, W., Lagpacan, L., Wang, R., Schultz, B. E., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.634683 · Cited by 157

Feedback and redundancy in receptor tyrosine kinase signaling: relevance to cancer therapies

Sun, C., & Bernards, R. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.08.010 · Cited by 155

Development of a Fluorescent-Tagged Kinase Assay System for the Detection and Characterization of Allosteric Kinase Inhibitors

Simard, J. R., Getlik, M., Grütter, C., Pawar, V. T., Wulfert, S., Rabiller, M., & Rauh, D. (2009) · Journal of the American Chemical Society · doi:10.1021/ja902010p · Cited by 153

A High Affinity Hepatocyte Growth Factor-binding Site in the Immunoglobulin-like Region of Met

Basilico, C., Arnesano, A., Galluzzo, M., Comoglio, P. M., & Michieli, P. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800727200 · Cited by 148

A therapeutically targetable mechanism of BCR-ABL–independent imatinib resistance in chronic myeloid leukemia

Ma, L., Shan, Y., Bai, R., Xue, L., Eide, C. A., Ou, J., Zhu, L. J., Hutchinson, L., Černý, J., Khoury, H. J., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009073 · Cited by 136

Structure and Dynamic Regulation of Abl Kinases*

Panjarian, S. B., Iacob, R. E., Chen, S., Engen, J. R., & Smithgall, T. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.438382 · Cited by 130

Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations

Littlefield, P., Liu, L., Mysore, V., Shan, Y., Shaw, D. E., & Jura, N. (2014) · Science Signaling · doi:10.1126/scisignal.2005786 · Cited by 126

Discovery of TAK-733, a potent and selective MEK allosteric site inhibitor for the treatment of cancer

Dong, Q., Dougan, D. R., Gong, X., Halkowycz, P., Jin, B., Kanouni, T., O’Connell, S. M., Scorah, N., Shi, L., Wallace, M. B., et al. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.01.071 · Cited by 124

Targeting Conformational Plasticity of Protein Kinases

Tong, M., & Seeliger, M. A. (2014) · ACS Chemical Biology · doi:10.1021/cb500870a · Cited by 120

Toward Understanding the Structural Basis of Cyclin-Dependent Kinase 6 Specific Inhibition

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PI3K/Akt/mTOR Pathway Inhibitors in Cancer: A Perspective on Clinical Progress

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