The DOI matches its Crossref record; 283 of the 283 references it cites were found in a registry or an index.
Ten things you should know about protein kinases: IUPHAR R eview 14
Open accessAbstract
Many human malignancies are associated with aberrant regulation of protein or lipid kinases due to mutations, chromosomal rearrangements and/or gene amplification. Protein and lipid kinases represent an important target class for treating human disorders. This review focus on ‘the 10 things you should know about protein kinases and their inhibitors', including a short introduction on the history of protein kinases and their inhibitors and ending with a perspective on kinase drug discovery. Although the ‘10 things’ have been, to a certain extent, chosen arbitrarily, they cover in a comprehensive way the past and present efforts in kinase drug discovery and summarize the status quo of the current kinase inhibitors as well as knowledge about kinase structure and binding modes. Besides describing the potentials of protein kinase inhibitors as drugs, this review also focus on their limitations, particularly on how to circumvent emerging resistance against kinase inhibitors in oncological indications.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors
Kawai, T., & Akira, S. (2010) · Nature Immunology · doi:10.1038/ni.1863 · Cited by 9,304
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
The Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity
Barretina, J., Caponigro, G., Stransky, N., Venkatesan, K., Margolin, A. A., Kim, S., Wilson, C. J., Lehár, J., Kryukov, G. V., Sonkin, D., et al. (2012) · Nature · doi:10.1038/nature11003 · Cited by 7,950
Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929
Improved survival with vemurafenib in melanoma with BRAF V600E mutation
Chapman, P. B., Hauschild, A., Robert, C., Haanen, J. B., Ascierto, P., Larkin, J., Dummer, R., Garbe, C., Testori, A., Maio, M., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1103782 · Cited by 7,720
The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains
Hanks, S. K., Quinn, A. M., & Hunter, T. (1988) · Science · doi:10.1126/science.3291115 · Cited by 5,039
Efficacy and Safety of Nintedanib in Idiopathic Pulmonary Fibrosis
Richeldi, L., du Bois, R. M., Raghu, G., Azuma, A., Brown, K. K., Costabel, U., Cottin, V., Flaherty, K. R., Hansell, D. M., Inoue, Y., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1402584 · Cited by 4,654
MET Amplification Leads to Gefitinib Resistance in Lung Cancer by Activating ERBB3 Signaling
Engelman, J. A., Zejnullahu, K., Mitsudomi, T., Song, Y., Hyland, C., Park, J. O., Lindeman, N., Gale, C.-M., Zhao, X., Christensen, J., et al. (2007) · Science · doi:10.1126/science.1141478 · Cited by 4,496
EGFR Mutation and Resistance of Non–Small-Cell Lung Cancer to Gefitinib
Kobayashi, S., Boggon, T. J., Dayaram, T., Jänne, P. A., Kocher, O., Meyerson, M., Johnson, B. E., Eck, M. J., Tenen, D. G., & Halmos, B. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa044238 · Cited by 3,964
Cell cycle, CDKs and cancer: a changing paradigm
Malumbres, M., & Barbacid, M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2602 · Cited by 3,957 · cited 2×
“The physiological activation of kinase occurs in many different ways and their mechanisms of activation have been summarized in excellent reviews (Taylor et al., 2005; Murray, 2007; Rommel et al., 2007; Schmierer and Hill, 2007; Engelman, 2009; Malumbres and Barbacid, 2009; Kawai and Akira, 2010; Lemmon and Schlessing…”
BackgroundBlume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
Targeting multidrug resistance in cancer
Szakács, G., Paterson, J. K., Ludwig, J. A., Booth-Genthe, C., & Gottesman, M. M. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1984 · Cited by 3,609
Pao, W., Miller, V. A., Politi, K. A., Riely, G. J., Somwar, R., Zakowski, M. F., Kris, M. G., & Varmus, H. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020073 · Cited by 3,527 · cited 10×
“Other covalent inhibitors like ibrutinib, targeting BTK, and afatinib, targeting the gefitinib-resistant EGFR, have been recently approved by the Food and Drug Administration (Figure 4D and Table 1) (Minkovsky and Berezov, 2008; Ninomiya et al., 2013; Akinleye et al., 2014).”
BackgroundInfluentialFive-Year Follow-up of Patients Receiving Imatinib for Chronic Myeloid Leukemia
Druker, B. J., Guilhot, F., O'Brien, S. G., Gathmann, I., Kantarjian, H., Gattermann, N., Deininger, M. W. N., Silver, R. T., Goldman, J. M., Stone, R. M., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa062867 · Cited by 3,488
A Gain-of-Function Mutation of JAK2 in Myeloproliferative Disorders
Kralovics, R., Passamonti, F., Buser, A. S., Teo, S.-S., Tiedt, R., Passweg, J. R., Tichelli, A., Cazzola, M., & Skoda, R. C. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa051113 · Cited by 3,470
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
The complexity of NF-κB signaling in inflammation and cancer
Hoesel, B., & Schmid, J. A. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-86 · Cited by 3,165
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/bj3510095 · Cited by 3,132
Clinical Resistance to STI-571 Cancer Therapy Caused by BCR-ABL Gene Mutation or Amplification
Gorre, M. E., Mohammed, M., Ellwood, K., Hsu, N., Paquette, R., Rao, P. N., & Sawyers, C. L. (2001) · Science · doi:10.1126/science.1062538 · Cited by 3,104
Inhibition of Mutated, Activated BRAF in Metastatic Melanoma
Flaherty, K. T., Puzanov, I., Kim, K. B., Ribas, A., McArthur, G. A., Sosman, J. A., O'Dwyer, P. J., Lee, R. J., Grippo, J. F., Nolop, K., et al. (2010) · New England Journal of Medicine · doi:10.1056/nejmoa1002011 · Cited by 3,103
Patterns of somatic mutation in human cancer genomes
Greenman, C., Stephens, P., Smith, R., Dalgliesh, G. L., Hunter, C., Bignell, G., Davies, H., Teague, J., Butler, A., Stevens, C., et al. (2007) · Nature · doi:10.1038/nature05610 · Cited by 3,080
Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells
Druker, B. J., Tamura, S., Buchdunger, E., Ohno, S., Segal, G. M., Fanning, S., Zimmermann, J., & Lydon, N. B. (1996) · Nature Medicine · doi:10.1038/nm0596-561 · Cited by 2,967
Everolimus in Postmenopausal Hormone-Receptor–Positive Advanced Breast Cancer
Baselga, J., Campone, M., Piccart, M., Burris, H. A., Rugo, H. S., Sahmoud, T., Noguchi, S., Gnant, M., Pritchard, K. I., Lebrun, F., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1109653 · Cited by 2,863
Hidaka, H., Inagaki, M., Kawamoto, S., & Sasaki, Y. (1984) · Biochemistry · doi:10.1021/bi00316a032 · Cited by 2,687
Mechanisms of Cancer Drug Resistance
Gottesman, M. M. (2002) · Annual Review of Medicine · doi:10.1146/annurev.med.53.082901.103929 · Cited by 2,643
Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586
Targeting cancer with small molecule kinase inhibitors
Zhang, J., Yang, P. L., & Gray, N. S. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2559 · Cited by 2,576
Hanks, S. K., & Hunter, T. R. (1995) · PubMed · Cited by 2,518
A quantitative analysis of kinase inhibitor selectivity
Karaman, M. W., Herrgard, S., Treiber, D. K., Gallant, P., Atteridge, C. E., Campbell, B. T., Chan, K. W., Ciceri, P., Davis, M. I., Edeen, P. T., et al. (2008) · Nature Biotechnology · doi:10.1038/nbt1358 · Cited by 2,466
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
Targeting PI3K signalling in cancer: opportunities, challenges and limitations
Engelman, J. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2664 · Cited by 2,445
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
The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1
Hanks, S. K., & Hunter, T. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.8.7768349 · Cited by 2,318
Kinase Mutations and Imatinib Response in Patients With Metastatic Gastrointestinal Stromal Tumor
Heinrich, M. C., Corless, C. L., Demetri, G. D., Blanke, C. D., von Mehren, M., Joensuu, H., McGreevey, L. S., Chen, C.-J., Van den Abbeele, A. D., Druker, B. J., et al. (2003) · Journal of Clinical Oncology · doi:10.1200/jco.2003.04.190 · Cited by 2,299
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
Protein kinases — the major drug targets of the twenty-first century?
Cohen, P. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd773 · Cited by 2,186
Unresponsiveness of colon cancer to BRAF(V600E) inhibition through feedback activation of EGFR
Prahallad, A., Sun, C., Huang, S., Di Nicolantonio, F., Salazar, R., Zecchin, D., Beijersbergen, R. L., Bardelli, A., & Bernards, R. (2012) · Nature · doi:10.1038/nature10868 · Cited by 2,051
The resurgence of covalent drugs
Singh, J., Petter, R. C., Baillie, T. A., & Whitty, A. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3410 · Cited by 1,873
Borst, O., Walker, B., Münzer, P., Russo, A., Schmid, E., Faggio, C., Bigalke, B., Laufer, S., Gawaz, M., & Lang, F. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350110 · Cited by 1,860
PI3K pathway alterations in cancer: variations on a theme
Yuan, T. L., & Cantley, L. C. (2008) · Oncogene · doi:10.1038/onc.2008.245 · Cited by 1,845
JAK inhibition with ruxolitinib versus best available therapy for myelofibrosis
Harrison, C., Kiladjian, J.-J., Al-Ali, H. K., Gisslinger, H., Waltzman, R., Stalbovskaya, V., McQuitty, M., Hunter, D. S., Levy, R., Knoops, L., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1110556 · Cited by 1,825
The Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation
Mendoza, M. C., Er, E. E., & Blenis, J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.03.006 · Cited by 1,817
RAF inhibitors transactivate RAF dimers and ERK signalling in cells with wild-type BRAF
Poulikakos, P. I., Zhang, C., Bollag, G., Shokat, K. M., & Rosen, N. (2010) · Nature · doi:10.1038/nature08902 · Cited by 1,811
Principles of cancer therapy: oncogene and non-oncogene addiction
Luo, J., Solimini, N. L., & Elledge, S. J. (2009) · Cell · doi:10.1016/j.cell.2009.02.024 · Cited by 1,765
Addiction to Oncogenes--the Achilles Heal of Cancer
Weinstein, I. B. (2002) · Science · doi:10.1126/science.1073096 · Cited by 1,728
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
RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth
Hatzivassiliou, G., Song, K., Yen, I., Brandhuber, B. J., Anderson, D. J., Alvarado, R., Ludlam, M. J. C., Stokoe, D., Gloor, S. L., Vigers, G., et al. (2010) · Nature · doi:10.1038/nature08833 · Cited by 1,622
Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
Cho, H.-S., Mason, K., Ramyar, K. X., Stanley, A. M., Gabelli, S. B., Denney, D. W., & Leahy, D. J. (2003) · Nature · doi:10.1038/nature01392 · Cited by 1,612
Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications
Walsh, C. T., Garneau‐Tsodikova, S., & Gatto, G. J. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200501023 · Cited by 1,604
Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl
Weisberg, E., Manley, P. W., Breitenstein, W., Brüggen, J., Cowan-Jacob, S. W., Ray, A., Huntly, B., Fabbro, D., Fendrich, G., Hall-Meyers, E., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.01.007 · Cited by 1,492
Self-citationCOT drives resistance to RAF inhibition through MAP kinase pathway reactivation
Johannessen, C. M., Boehm, J. S., Kim, S. Y., Thomas, S. R., Wardwell, L., Johnson, L. A., Emery, C. M., Stransky, N., Cogdill, A. P., Barretina, J., et al. (2010) · Nature · doi:10.1038/nature09627 · Cited by 1,460
RAF inhibitor resistance is mediated by dimerization of aberrantly spliced BRAF(V600E)
Poulikakos, P. I., Persaud, Y., Janakiraman, M., Kong, X., Ng, C., Moriceau, G., Shi, H., Atefi, M., Titz, B., Gabay, M. T., et al. (2011) · Nature · doi:10.1038/nature10662 · Cited by 1,454
Mechanisms of specificity in protein phosphorylation
Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451
Melanoma biology and new targeted therapy
Gray-Schopfer, V., Wellbrock, C., & Marais, R. (2007) · Nature · doi:10.1038/nature05661 · Cited by 1,371
Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity
Tsai, J., Lee, J. T., Wang, W., Zhang, J., Cho, H., Mamo, S., Bremer, R., Gillette, S., Kong, J., Haass, N. K., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711741105 · Cited by 1,346
Engelman, J. A., Chen, L., Tan, X., Crosby, K., Guimaraes, A. R., Upadhyay, R., Maira, M., McNamara, K., Perera, S. A., Song, Y., et al. (2008) · Nature Medicine · doi:10.1038/nm.1890 · Cited by 1,330
Mechanisms of Acquired Crizotinib Resistance in ALK-Rearranged Lung Cancers
Katayama, R., Shaw, A. T., Khan, T. M., Mino-Kenudson, M., Solomon, B. J., Halmos, B., Jessop, N. A., Wain, J. C., Yeo, A. T., Benes, C., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003316 · Cited by 1,309
Lombardo, L. J., Lee, F. Y., Chen, P., Norris, D., Barrish, J. C., Behnia, K., Castaneda, S., Cornelius, L. A. M., Das, J., Doweyko, A. M., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049486a · Cited by 1,297
TGFβ–SMAD signal transduction: molecular specificity and functional flexibility
Schmierer, B., & Hill, C. S. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2297 · Cited by 1,271
O'Hare, T., Shakespeare, W. C., Zhu, X., Eide, C. A., Rivera, V. M., Wang, F., Adrian, L. T., Zhou, T., Huang, W.-S., Xu, Q., et al. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.09.028 · Cited by 1,259
The PI3K Pathway As Drug Target in Human Cancer
Courtney, K. D., Corcoran, R. B., & Engelman, J. A. (2010) · Journal of Clinical Oncology · doi:10.1200/jco.2009.25.3641 · Cited by 1,237
Graham, S. M., Jørgensen, H. G., Allan, E., Pearson, C., Alcorn, M. J., Richmond, L., & Holyoake, T. L. (2002) · Blood · doi:10.1182/blood.v99.1.319 · Cited by 1,181
The JAK-STAT Signaling Pathway: Input and Output Integration
Murray, P. J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.5.2623 · Cited by 1,179
Nolen, B., Taylor, S., & Ghosh, G. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.024 · Cited by 1,167
Sawyers, C. (2004) · Nature · doi:10.1038/nature03095 · Cited by 1,165
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
Rational design of inhibitors that bind to inactive kinase conformations
Liu, Y., & Gray, N. S. (2006) · Nature Chemical Biology · doi:10.1038/nchembio799 · Cited by 1,094
mTOR kinase structure, mechanism and regulation
Yang, H., Rudge, D. G., Koos, J. D., Vaidialingam, B., Yang, H. J., & Pavletich, N. P. (2013) · Nature · doi:10.1038/nature12122 · Cited by 1,075
PI3Kδ Inhibition by Idelalisib in Patients with Relapsed Indolent Lymphoma
Gopal, A. K., Kahl, B. S., de Vos, S., Wagner-Johnston, N. D., Schuster, S. J., Jurczak, W. J., Flinn, I. W., Flowers, C. R., Martin, P., Viardot, A., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1314583 · Cited by 1,069
Preexistence and clonal selection of MET amplification in EGFR mutant NSCLC
Turke, A. B., Zejnullahu, K., Wu, Y.-L., Song, Y., Dias-Santagata, D., Lifshits, E., Toschi, L., Rogers, A., Mok, T., Sequist, L., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.11.022 · Cited by 1,059
The quest to overcome resistance to EGFR-targeted therapies in cancer
Chong, C. R., & Jänne, P. A. (2013) · Nature Medicine · doi:10.1038/nm.3388 · Cited by 1,052
Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors
Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S., Boesche, M., Hobson, S., Mathieson, T., Perrin, J., Raida, M., Rau, C., et al. (2007) · Nature Biotechnology · doi:10.1038/nbt1328 · Cited by 1,034
Novel mutant-selective EGFR kinase inhibitors against EGFR T790M
Zhou, W., Ercan, D., Chen, L., Yun, C.-H., Li, D., Capelletti, M., Cortot, A. B., Chirieac, L., Iacob, R. E., Padera, R., et al. (2009) · Nature · doi:10.1038/nature08622 · Cited by 1,013
Everolimus for Subependymal Giant-Cell Astrocytomas in Tuberous Sclerosis
Krueger, D. A., Care, M. M., Holland, K., Agricola, K., Tudor, C., Mangeshkar, P., Wilson, K. A., Byars, A., Sahmoud, T., & Franz, D. N. (2010) · New England Journal of Medicine · doi:10.1056/nejmoa1001671 · Cited by 1,006
Dissecting Therapeutic Resistance to RAF Inhibition in Melanoma by Tumor Genomic Profiling
Wagle, N., Emery, C., Berger, M. F., Davis, M. J., Sawyer, A., Pochanard, P., Kehoe, S. M., Johannessen, C. M., MacConaill, L. E., Hahn, W. C., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2010.33.2312 · Cited by 1,005
High-throughput oncogene mutation profiling in human cancer
Thomas, R. K., Baker, A. C., DeBiasi, R. M., Winckler, W., LaFramboise, T., Lin, W. M., Wang, M., Feng, W., Zander, T., MacConaill, L. E., et al. (2007) · Nature Genetics · doi:10.1038/ng1975 · Cited by 988
The landscape of kinase fusions in cancer
Stransky, N., Cerami, E., Schalm, S., Kim, J. L., & Lengauer, C. (2014) · Nature Communications · doi:10.1038/ncomms5846 · Cited by 968
AKT inhibition relieves feedback suppression of receptor tyrosine kinase expression and activity
Chandarlapaty, S., Sawai, A., Scaltriti, M., Rodrik-Outmezguine, V., Grbovic-Huezo, O., Serra, V., Majumder, P. K., Baselga, J., & Rosen, N. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.10.031 · Cited by 967
Irreversible inhibitors of the EGF receptor may circumvent acquired resistance to gefitinib
Kwak, E. L., Sordella, R., Bell, D. W., Godin-Heymann, N., Okimoto, R. A., Brannigan, B. W., Harris, P. L., Driscoll, D. R., Fidias, P., Lynch, T. J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502860102 · Cited by 952
Reck, M., Kaiser, R., Mellemgaard, A., Douillard, J.-Y., Orlov, S., Krzakowski, M., von Pawel, J., Gottfried, M., Bondarenko, I., Liao, M., et al. (2014) · The Lancet Oncology · doi:10.1016/s1470-2045(13)70586-2 · Cited by 951
Protein kinases: evolution of dynamic regulatory proteins
Taylor, S. S., & Kornev, A. P. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.006 · Cited by 945
Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity
Anastassiadis, T., Deacon, S. W., Devarajan, K., Ma, H., & Peterson, J. R. (2011) · Nature Biotechnology · doi:10.1038/nbt.2017 · Cited by 919
The Genetic Landscape of Clinical Resistance to RAF Inhibition in Metastatic Melanoma
Van Allen, E. M., Wagle, N., Sucker, A., Treacy, D. J., Johannessen, C. M., Goetz, E. M., Place, C. S., Taylor-Weiner, A., Whittaker, S., Kryukov, G. V., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0617 · Cited by 912
Pawson, A. J., Sharman, J. L., Benson, H. E., Faccenda, E., Alexander, S. P. H., Buneman, O. P., Davenport, A. P., McGrath, J. C., Peters, J. A., Southan, C., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gkt1143 · Cited by 849
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
Kunz, J., Henriquez, R., Schneider, U., Deuter-Reinhard, M., Movva, N. R., & Hall, M. N. (1993) · Cell · doi:10.1016/0092-8674(93)90144-f · Cited by 834
Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site
Pargellis, C., Tong, L., Churchill, L., Cirillo, P. F., Gilmore, T., Graham, A. G., Grob, P. M., Hickey, E. R., Moss, N., Pav, S., et al. (2002) · Nature Structural Biology · doi:10.1038/nsb770 · Cited by 833
Molecular mechanisms of cardiotoxicity of tyrosine kinase inhibition
Force, T., Krause, D. S., & Van Etten, R. A. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2106 · Cited by 801
Development of PI3K inhibitors: lessons learned from early clinical trials
Rodon, J., Dienstmann, R., Serra, V., & Tabernero, J. (2013) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2013.10 · Cited by 766
Kornev, A. P., Haste, N. M., Taylor, S. S., & Ten Eyck, L. F. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607656103 · Cited by 762
Molecular basis for sunitinib efficacy and future clinical development
Faivre, S., Demetri, G., Sargent, W., & Raymond, E. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2380 · Cited by 721
Validating therapeutic targets through human genetics
Plenge, R. M., Scolnick, E. M., & Altshuler, D. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4051 · Cited by 712
Takano, T., Ohe, Y., Sakamoto, H., Tsuta, K., Matsuno, Y., Tateishi, U., Yamamoto, S., Nokihara, H., Yamamoto, N., Sekine, I., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.01.0793 · Cited by 695
Galanis, E., Buckner, J. C., Maurer, M. J., Kreisberg, J. I., Ballman, K., Boni, J., Peralba, J. M., Jenkins, R. B., Dakhil, S. R., Morton, R. F., et al. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.23.622 · Cited by 694
Wymann, M. P., Bulgarelli-Leva, G., Zvelebil, M. J., Pirola, L., Vanhaesebroeck, B., Waterfield, M. D., & Panayotou, G. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.4.1722 · Cited by 682
Discovery of Selective Irreversible Inhibitors for Bruton’s Tyrosine Kinase
Pan, Z., Scheerens, H., Li, S., Schultz, B. E., Sprengeler, P. A., Burrill, L. C., Mendonca, R. V., Sweeney, M. D., Scott, K. C. K., Grothaus, P. G., et al. (2007) · ChemMedChem · doi:10.1002/cmdc.200600221 · Cited by 674
Features of Selective Kinase Inhibitors
Knight, Z. A., & Shokat, K. M. (2005) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.04.011 · Cited by 657
Developing Irreversible Inhibitors of the Protein Kinase Cysteinome
Liu, Q., Sabnis, Y., Zhao, Z., Zhang, T., Buhrlage, S. J., Jones, L. H., & Gray, N. S. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.12.006 · Cited by 652
Cell Signaling in Space and Time: Where Proteins Come Together and When They’re Apart
Scott, J. D., & Pawson, T. (2009) · Science · doi:10.1126/science.1175668 · Cited by 645
Part I: Mechanisms of resistance to imatinib in chronic myeloid leukaemia
Apperley, J. F. (2007) · The Lancet Oncology · doi:10.1016/s1470-2045(07)70342-x · Cited by 643
Antitumor Activity of HKI-272, an Orally Active, Irreversible Inhibitor of the HER-2 Tyrosine Kinase
Rabindran, S. K., Discafani, C. M., Rosfjord, E. C., Baxter, M., Floyd, M. B., Golas, J., Hallett, W. A., Johnson, B. D., Nilakantan, R., Overbeek, E., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2868 · Cited by 639
Phosphoinositide 3-Kinase δ Gene Mutation Predisposes to Respiratory Infection and Airway Damage
Angulo, I., Vadas, O., Garçon, F., Banham-Hall, E., Plagnol, V., Leahy, T. R., Baxendale, H., Coulter, T., Curtis, J., Wu, C., et al. (2013) · Science · doi:10.1126/science.1243292 · Cited by 636
Cohen, P. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02473.x · Cited by 634
Ohren, J. F., Chen, H., Pavlovsky, A., Whitehead, C., Zhang, E., Kuffa, P., Yan, C., McConnell, P., Spessard, C., Banotai, C., et al. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb859 · Cited by 626
Targeting Bcr–Abl by combining allosteric with ATP-binding-site inhibitors
Zhang, J., Adrián, F. J., Jahnke, W., Cowan-Jacob, S. W., Li, A. G., Iacob, R. E., Sim, T., Powers, J., Dierks, C., Sun, F., et al. (2010) · Nature · doi:10.1038/nature08675 · Cited by 597
Self-citationBarker, A. J., Gibson, K. H., Grundy, W., Godfrey, A. A., Barlow, J. J., Healy, M. P., Woodburn, J. R., Ashton, S. E., Curry, B. J., Scarlett, L., et al. (2001) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(01)00344-4 · Cited by 569
Cutaneous side-effects of kinase inhibitors and blocking antibodies
Robert, C., Soria, J.-C., Spatz, A., Le Cesne, A., Malka, D., Pautier, P., Wechsler, J., Lhomme, C., Escudier, B., Boige, V., et al. (2005) · The Lancet Oncology · doi:10.1016/s1470-2045(05)70243-6 · Cited by 554
Emerging roles of pseudokinases
Boudeau, J., Miranda-Saavedra, D., Barton, G. J., & Alessi, D. R. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.07.003 · Cited by 547
Residence Time of Receptor−Ligand Complexes and Its Effect on Biological Function
Tummino, P. J., & Copeland, R. A. (2008) · Biochemistry · doi:10.1021/bi8002023 · Cited by 544
MDR1 gene overexpression confers resistance to imatinib mesylate in leukemia cell line models
Mahon, F.-X., Belloc, F., Lagarde, V., Chollet, C., Moreau-Gaudry, F., Reiffers, J., Goldman, J. M., & Melo, J. V. (2003) · Blood · doi:10.1182/blood.v101.6.2368 · Cited by 538
Serra, V, Scaltriti, M., Prudkin, L., Eichhorn, P. J. A., Ibrahim, Y. H., Chandarlapaty, S., Markman, B., Rodriguez, O., Guzman, M., Rodriguez, S., et al. (2011) · Oncogene · doi:10.1038/onc.2010.626 · Cited by 528
Sun, L., Liang, C., Shirazian, S., Zhou, Y., Miller, T., Cui, J., Fukuda, J. Y., Chu, J.-Y., Nematalla, A., Wang, X., et al. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm0204183 · Cited by 521
Through the “Gatekeeper Door”: Exploiting the Active Kinase Conformation
Zuccotto, F., Ardini, E., Casale, E., & Angiolini, M. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901443h · Cited by 518
Allosteric Akt (PKB) inhibitors: discovery and SAR of isozyme selective inhibitors
Lindsley, C. W., Zhao, Z., Leister, W. H., Robinson, R. G., Barnett, S. F., Defeo-Jones, D., Jones, R. E., Hartman, G. D., Huff, J. R., Huber, H. E., et al. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.11.011 · Cited by 503
AMPK: positive and negative regulation, and its role in whole-body energy homeostasis
Hardie, D. G. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.09.004 · Cited by 485
le Coutre, P., Tassi, E., Varella-Garcia, M., Barni, R., Mologni, L., Cabrita, G., Marchesi, E., Supino, R., & Gambacorti-Passerini, C. (2000) · Blood · doi:10.1182/blood.v95.5.1758.005a41_1758_1766 · Cited by 484
Mutational Analysis of the Tyrosine Kinome in Colorectal Cancers
Bardelli, A., Parsons, D. W., Silliman, N., Ptak, J., Szabo, S., Saha, S., Markowitz, S., Willson, J. K. V., Parmigiani, G., Kinzler, K. W., et al. (2003) · Science · doi:10.1126/science.1082596 · Cited by 484
mTOR Kinase Inhibition Causes Feedback-Dependent Biphasic Regulation of AKT Signaling
Rodrik-Outmezguine, V. S., Chandarlapaty, S., Pagano, N. C., Poulikakos, P. I., Scaltriti, M., Moskatel, E., Baselga, J., Guichard, S., & Rosen, N. (2011) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0085 · Cited by 442
Scaltriti, M., Verma, C., Guzman, M., Jimenez, J., Parra, J. L., Pedersen, K., Smith, D. J., Landolfi, S., Ramon y Cajal, S., Arribas, J., et al. (2009) · Oncogene · doi:10.1038/onc.2008.432 · Cited by 439
Targeting the sphingosine-1-phosphate axis in cancer, inflammation and beyond
Kunkel, G. T., Maceyka, M., Milstien, S., & Spiegel, S. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4099 · Cited by 434
The Concise Guide to PHARMACOLOGY 2013/14: Enzymes
Alexander, S. P. H., Benson, H. E., Faccenda, E., Pawson, A. J., Sharman, J. L., Spedding, M., Peters, J. A., Harmar, A. J., & Collaborators, C. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12451 · Cited by 425
Kinase mutations in human disease: interpreting genotype–phenotype relationships
Lahiry, P., Torkamani, A., Schork, N. J., & Hegele, R. A. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2707 · Cited by 420
Functional Interrogation of the Kinome Using Nucleotide Acyl Phosphates
Patricelli, M. P., Szardenings, A. K., Liyanage, M., Nomanbhoy, T. K., Wu, M., Weissig, H., Aban, A., Chun, D., Tanner, S., & Kozarich, J. W. (2007) · Biochemistry · doi:10.1021/bi062142x · Cited by 418
Mechanism of Activation of Protein Kinase JAK2 by the Growth Hormone Receptor
Brooks, A. J., Dai, W., O’Mara, M. L., Abankwa, D., Chhabra, Y., Pelekanos, R. A., Gardon, O., Tunny, K. A., Blucher, K. M., Morton, C. J., et al. (2014) · Science · doi:10.1126/science.1249783 · Cited by 418
Activation of tyrosine kinases by mutation of the gatekeeper threonine
Azam, M., Seeliger, M. A., Gray, N. S., Kuriyan, J., & Daley, G. Q. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1486 · Cited by 411
Small molecule BDNF mimetics activate TrkB signaling and prevent neuronal degeneration in rodents
Massa, S. M., Yang, T., Xie, Y., Shi, J., Bilgen, M., Joyce, J. N., Nehama, D., Rajadas, J., & Longo, F. M. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41356 · Cited by 406
PI3Kδ and PI3Kγ: partners in crime in inflammation in rheumatoid arthritis and beyond?
Rommel, C., Camps, M., & Ji, H. (2007) · Nature Reviews Immunology · doi:10.1038/nri2036 · Cited by 398
BARNETT, S. F., DEFEO-JONES, D., FU, S., HANCOCK, P. J., HASKELL, K. M., JONES, R. E., KAHANA, J. A., KRAL, A. M., LEANDER, K., LEE, L. L., et al. (2005) · Biochemical Journal · doi:10.1042/bj20041140 · Cited by 396
Allosteric inhibitors of Bcr-abl–dependent cell proliferation
Adrián, F. J., Ding, Q., Sim, T., Velentza, A., Sloan, C., Liu, Y., Zhang, G., Hur, W., Ding, S., Manley, P., et al. (2006) · Nature Chemical Biology · doi:10.1038/nchembio760 · Cited by 381
Self-citationStructure of the LKB1-STRAD-MO25 Complex Reveals an Allosteric Mechanism of Kinase Activation
Zeqiraj, E., Filippi, B. M., Deak, M., Alessi, D. R., & van Aalten, D. M. F. (2009) · Science · doi:10.1126/science.1178377 · Cited by 365
In Situ Kinase Profiling Reveals Functionally Relevant Properties of Native Kinases
Patricelli, M. P., Nomanbhoy, T. K., Wu, J., Brown, H., Zhou, D., Zhang, J., Jagannathan, S., Aban, A., Okerberg, E., Herring, C., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.04.011 · Cited by 348
Sanders, M. J., Ali, Z. S., Hegarty, B. D., Heath, R., Snowden, M. A., & Carling, D. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706543200 · Cited by 347 · cited 6×
“…a few protein kinases that require activation rather than inhibition to fulfil their therapeutic need, like the AMPK or the insulin receptor for which activators have been identified (Li et al., 2001; Pender et al., 2002; Sanders et al., 2007; Lee et al., 2011; Salt and Palmer, 2012; Hardie, 2014).”
BackgroundInfluentialProtein kinases as targets for anticancer agents: from inhibitors to useful drugs
Fabbro, D., Ruetz, S., Buchdunger, E., Cowan-Jacob, S. W., Fendrich, G., Liebetanz, J., Mestan, J., O'Reilly, T., Traxler, P., Chaudhuri, B., et al. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00179-1 · Cited by 335
Self-citationStrategies to overcome resistance to targeted protein kinase inhibitors
Daub, H., Specht, K., & Ullrich, A. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1579 · Cited by 334
Tyrosine kinase inhibitors: From rational design to clinical trials
Traxler, P., Bold, G., Buchdunger, E., Caravatti, G., Furet, P., Manley, P., O'Reilly, T., Wood, J., & Zimmermann, J. (2001) · Medicinal Research Reviews · doi:10.1002/med.1022 · Cited by 324
Mechanism of MEK inhibition determines efficacy in mutant KRAS- versus BRAF-driven cancers
Hatzivassiliou, G., Haling, J. R., Chen, H., Song, K., Price, S., Heald, R., Hewitt, J. F. M., Zak, M., Peck, A., Orr, C., et al. (2013) · Nature · doi:10.1038/nature12441 · Cited by 319
Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms
Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310
Flying under the radar: the new wave of BCR–ABL inhibitors
Quintás-Cardama, A., Kantarjian, H., & Cortes, J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2324 · Cited by 305
Factors underlying sensitivity of cancers to small-molecule kinase inhibitors
Jänne, P. A., Gray, N., & Settleman, J. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2871 · Cited by 303
Natural-product-derived fragments for fragment-based ligand discovery
Over, B., Wetzel, S., Grütter, C., Nakai, Y., Renner, S., Rauh, D., & Waldmann, H. (2013) · Nature Chemistry · doi:10.1038/nchem.1506 · Cited by 300
Ibrutinib Resistance in Chronic Lymphocytic Leukemia
Furman, R. R., Cheng, S., Lu, P., Setty, M., Perez, A. R., Guo, A., Racchumi, J., Xu, G., Wu, H., Ma, J., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmc1402716 · Cited by 299
Targeting protein kinases in central nervous system disorders
Chico, L. K., Van Eldik, L. J., & Watterson, D. M. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2999 · Cited by 298
Inhibitor hijacking of Akt activation
Okuzumi, T., Fiedler, D., Zhang, C., Gray, D. C., Aizenstein, B., Hoffman, R., & Shokat, K. M. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.183 · Cited by 294
The (un)targeted cancer kinome
Fedorov, O., Müller, S., & Knapp, S. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.297 · Cited by 292
MEK and the inhibitors: from bench to bedside
Akinleye, A., Furqan, M., Mukhi, N., Ravella, P., & Liu, D. (2013) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-6-27 · Cited by 291
She, Q., Solit, D. B., Basso, A., & Moasser, M. M. (2003) · PubMed · Cited by 287
Acquired resistance to tyrosine kinase inhibitors during cancer therapy
Engelman, J. A., & Settleman, J. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.01.004 · Cited by 284
Cancer Drugs in the United States: Justum Pretium—The Just Price
Kantarjian, H. M., Fojo, T., Mathisen, M., & Zwelling, L. A. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2013.49.1845 · Cited by 284
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
Targeting HER proteins in cancer therapy and the role of the non-target HER3
Hsieh, A. C., & Moasser, M. M. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6603910 · Cited by 269
Structural and Functional Diversity of the Microbial Kinome
Kannan, N., Taylor, S. S., Zhai, Y., Venter, J. C., & Manning, G. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050017 · Cited by 264
A putative molecular-activation switch in the transmembrane domain of erbB2
Fleishman, S. J., Schlessinger, J., & Ben-Tal, N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252640799 · Cited by 262
The Use of AlphaScreen Technology in HTS: Current Status
Eglen, R. M., Reisine, T., Roby, P., Rouleau, N., Illy, C., Bossé, R., & Bielefeld, M. (2008) · Current Chemical Genomics · doi:10.2174/1875397300801010002 · Cited by 260
Is resistance useless? Multidrug resistance and collateral sensitivity
Hall, M. D., Handley, M. D., & Gottesman, M. M. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.07.003 · Cited by 259
Complexity in the signaling network: insights from the use of targeted inhibitors in cancer therapy
Logue, J. S., & Morrison, D. K. (2012) · Genes & Development · doi:10.1101/gad.186965.112 · Cited by 250
Taylor, S. S., Kim, C., Vigil, D., Haste, N. M., Yang, J., Wu, J., & Anand, G. S. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.08.024 · Cited by 249
Effects of HER2 overexpression on cell signaling networks governing proliferation and migration
Wolf‐Yadlin, A., Kumar, N., Zhang, Y., Hautaniemi, S., Zaman, M., Kim, H., Grantcharova, V., Lauffenburger, D. A., & White, F. M. (2006) · Molecular Systems Biology · doi:10.1038/msb4100094 · Cited by 247
Ba/F3 cells and their use in kinase drug discovery
Warmuth, M., Kim, S., Gu, X.-J., Xia, G., & Adrián, F. (2007) · Current Opinion in Oncology · doi:10.1097/cco.0b013e328011a25f · Cited by 240
Britschgi, A., Andraos, R., Brinkhaus, H., Klebba, I., Romanet, V., Müller, U., Murakami, M., Radimerski, T., & Bentires-Alj, M. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.10.023 · Cited by 240
Christopoulos, A., Changeux, J.-P., Catterall, W. A., Fabbro, D., Burris, T. P., Cidlowski, J. A., Olsen, R. W., Peters, J. A., Neubig, R. R., Pin, J.-P., et al. (2014) · Pharmacological Reviews · doi:10.1124/pr.114.008862 · Cited by 238
Self-citationNegative Feedback and Adaptive Resistance to the Targeted Therapy of Cancer
Chandarlapaty, S. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0018 · Cited by 234
Chronic myeloid leukemia: current treatment options
Goldman, J. M., & Druker, B. J. (2001) · Blood · doi:10.1182/blood.v98.7.2039 · Cited by 224
A Peptoid “Antibody Surrogate” That Antagonizes VEGF Receptor 2 Activity
Udugamasooriya, D. G., Dineen, S. P., Brekken, R. A., & Kodadek, T. (2008) · Journal of the American Chemical Society · doi:10.1021/ja711193x · Cited by 222
The Concise Guide to PHARMACOLOGY 2013/14: Catalytic Receptors
Alexander, S. P. H., Benson, H. E., Faccenda, E., Pawson, A. J., Sharman, J. L., Spedding, M., Peters, J. A., Harmar, A. J., & Collaborators, C. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12449 · Cited by 221
King, A. J., Arnone, M. R., Bleam, M. R., Moss, K. G., Yang, J., Fedorowicz, K. E., Smitheman, K. N., Erhardt, J. A., Hughes-Earle, A., Kane-Carson, L. S., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067583 · Cited by 221
McIntyre, K. W., Shuster, D. J., Gillooly, K. M., Dambach, D. M., Pattoli, M. A., Lu, P., Zhou, X., Qiu, Y., Zusi, F. C., & Burke, J. R. (2003) · Arthritis & Rheumatism · doi:10.1002/art.11131 · Cited by 217
Cools, J., Stover, E. H., Boulton, C. L., Gotlib, J., Legare, R. D., Amaral, S. M., Curley, D. P., Duclos, N., Rowan, R., Kutok, J. L., et al. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00108-9 · Cited by 216
Self-citationTargeting the PI3K signaling pathway in cancer therapy
Bartholomeusz, C., & Gonzalez-Angulo, A. M. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.644788 · Cited by 216
High-throughput kinase profiling as a platform for drug discovery
Goldstein, D. M., Gray, N. S., & Zarrinkar, P. P. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2541 · Cited by 215
Trametinib: First Global Approval
Wright, C. J. M., & McCormack, P. L. (2013) · Drugs · doi:10.1007/s40265-013-0096-1 · Cited by 206
Fragments, network biology and designing multiple ligands
Morphy, R., & Rankovic, Z. (2007) · Drug Discovery Today · doi:10.1016/j.drudis.2006.12.006 · Cited by 204
Filippakopoulos, P., Kofler, M., Hantschel, O., Gish, G. D., Grebien, F., Salah, E., Neudecker, P., Kay, L. E., Turk, B. E., Superti-Furga, G., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.047 · Cited by 201
Protein kinases and protein phosphatases in prokaryotes: a genomic perspective
Kennelly, P. (2002) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(01)00479-7 · Cited by 197
The challenge of selecting protein kinase assays for lead discovery optimization
Ma, H., Deacon, S., & Horiuchi, K. (2008) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.3.6.607 · Cited by 197
The secret life of kinases: functions beyond catalysis
Rauch, J., Volinsky, N., Romano, D., & Kolch, W. (2011) · Cell Communication and Signaling · doi:10.1186/1478-811x-9-23 · Cited by 196
Chipping away at the lung cancer genome
Pao, W., & Hutchinson, K. E. (2012) · Nature Medicine · doi:10.1038/nm.2697 · Cited by 192
An efficient rapid system for profiling the cellular activities of molecular libraries
Melnick, J. S., Janes, J., Kim, S., Chang, J. Y., Sipes, D. G., Gunderson, D., Jarnes, L., Matzen, J. T., Garcia, M. E., Hood, T. L., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511292103 · Cited by 186
Switching on kinases: oncogenic activation of BRAF and the PDGFR family
Dibb, N. J., Dilworth, S. M., & Mol, C. D. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1434 · Cited by 179
Prediction of Resistance to Small Molecule FLT3 Inhibitors
Cools, J., Mentens, N., Furet, P., Fabbro, D., Clark, J. J., Griffin, J. D., Marynen, P., & Gilliland, D. G. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2148 · Cited by 178
Self-citationKinomics—structural biology and chemogenomics of kinase inhibitors and targets
Vieth, M., Higgs, R. E., Robertson, D. H., Shapiro, M., Gragg, E. A., & Hemmerle, H. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.028 · Cited by 175
An ATP-Site On-Off Switch That Restricts Phosphatase Accessibility of Akt
Lin, K., Lin, J., Wu, W.-I., Ballard, J., Lee, B. B., Gloor, S. L., Vigers, G. P. A., Morales, T. H., Friedman, L. S., Skelton, N., et al. (2012) · Science Signaling · doi:10.1126/scisignal.2002618 · Cited by 173
Tyrphostins—Potential antiproliferative agents and novel molecular tools
Levitzki, A. (1990) · Biochemical Pharmacology · doi:10.1016/0006-2952(90)90474-y · Cited by 170
Modular evolution of phosphorylation-based signalling systems
Jin, J., & Pawson, T. (2012) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2012.0106 · Cited by 163
Kinomics: characterizing the therapeutically validated kinase space
Vieth, M., Sutherland, J. J., Robertson, D. H., & Campbell, R. M. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03477-x · Cited by 157
Turning a protein kinase on or off from a single allosteric site via disulfide trapping
Sadowsky, J., Burlingame, M. A., Wolan, D. W., McClendon, C. L., Jacobson, M. P., & Wells, J. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102376108 · Cited by 157
A clickable inhibitor reveals context-dependent autoactivation of p90 RSK
Cohen, M. S., Hadjivassiliou, H., & Taunton, J. (2007) · Nature Chemical Biology · doi:10.1038/nchembio859 · Cited by 156
Effect of SB 203580 on the activity of c-Raf in vitro and in vivo
Hall-Jackson, C. A., Goedert, M., Hedge, P., & Cohen, P. (1999) · Oncogene · doi:10.1038/sj.onc.1202603 · Cited by 151
Design and Discovery of Small Molecules Targeting Raf-1 Kinase
Lowinger, T. B., Riedl, B., Dumas, J., & Smith, R. A. (2002) · Current Pharmaceutical Design · doi:10.2174/1381612023393125 · Cited by 150
Bono, F., Smet, F. D., Herbert, C., Bock, K. D., Γεωργιάδου, Μ., Fons, P., Tjwa, M., Alcouffe, C., Ny, A., Bianciotto, M., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.02.019 · Cited by 146
Dabrafenib: First Global Approval
Ballantyne, A. D., & Garnock-Jones, K. P. (2013) · Drugs · doi:10.1007/s40265-013-0095-2 · Cited by 146
Blencke, S., Zech, B., Engkvist, O., Greff, Z., Őrfi, L., Horváth, Z., Kéri, G., Ullrich, A., & Daub, H. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.02.029 · Cited by 145
ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system
Polier, S., Samant, R. S., Clarke, P. A., Workman, P., Prodromou, C., & Pearl, L. H. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1212 · Cited by 145
Modulation of Activation-Loop Phosphorylation by JAK Inhibitors Is Binding Mode Dependent
Andraos, R., Qian, Z., Bonenfant, D., Rubert, J., Vangrevelinghe, E., Scheufler, C., Marque, F., Régnier, C. H., Pover, A. D., Ryckelynck, H., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0324 · Cited by 144
Albrecht, B. K., Harmange, J.-C., Bauer, D., Berry, L., Bode, C., Boezio, A. A., Chen, A., Choquette, D. M., Dussault, I., Fridrich, C., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800043g · Cited by 143
Exploiting the anti-inflammatory effects of AMP-activated protein kinase activation
Salt, I. P., & Palmer, T. M. (2012) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2012.696609 · Cited by 142
Structure and allosteric effects of low-molecular-weight activators on the protein kinase PDK1
Hindie, V., Stroba, A., Zhang, H., Lopez-Garcia, L. A., Idrissova, L., Zeuzem, S., Hirschberg, D., Schaeffer, F., Jørgensen, T. J. D., Engel, M., et al. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.208 · Cited by 141
Shaw, A. T., Yasothan, U., & Kirkpatrick, P. N. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3600 · Cited by 140
A public-private partnership to unlock the untargeted kinome
Knapp, S., Arruda, P., Blagg, J., Burley, S. K., Drewry, D. H., Edwards, A. M., Fabbro, D., Gillespie, P., Gray, N. S., Küster, B., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1113 · Cited by 139
Self-citationSkóra, L., Mestan, J., Fabbro, D., Jahnke, W., & Grzesiek, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314712110 · Cited by 138
Self-citation
Cited by
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
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
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
Metadata
- Authors
- Fabbro, D., Cowan‐Jacob, S. W., & Moebitz, H.
- Venue
- British Journal of Pharmacology
- Publisher
- Wiley
- Published
- 2015-03-24
- Volume
- 172
- Issue
- 11
- Pages
- 2675-2700
- ISSN
- 0007-1188 (ISSN-L)
- 1476-5381
- OpenAlex
- W1691796058
- Cited by
- 347
- References
- 283
- FWCI
- 8.49
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
