The Btk tyrosine kinase is a major target of the Bcr-Abl inhibitor dasatinib

Five-Year Follow-up of Patients Receiving Imatinib for Chronic Myeloid Leukemia

Druker, B. J., Guilhot, F., O’Brien, S. G., Gathmann, I., Kantarjian, H. M., Gattermann, N., Deininger, M. W., Silver, R. T., Goldman, J. M., Stone, R. M., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa062867 · Cited by 3,474 · see citing works

A small molecule–kinase interaction map for clinical kinase inhibitors

Fabian, M. A., Biggs, W., Treiber, D. K., Atteridge, C. E., Azimioara, M. D., Benedetti, M. G., Carter, T. A., Ciceri, P., Edeen, P. T., Floyd, M. B., et al. (2005) · Nature Biotechnology · doi:10.1038/nbt1068 · Cited by 1,901 · see citing works

Overriding Imatinib Resistance with a Novel ABL Kinase Inhibitor

Shah, N. P., Tran, C., Lee, F. Y., Chen, P., Norris, D. J., & Sawyers, C. L. (2004) · Science · doi:10.1126/science.1099480 · Cited by 1,785 · see citing works

Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase

Schindler, T. H., Bornmann, W. G., Pellicena, P., Miller, W. T., Clarkson, B., & Kuriyan, J. (2000) · Science · doi:10.1126/science.289.5486.1938 · Cited by 1,785 · see citing works

Dasatinib in imatinib-resistant Philadelphia chromosome-positive leukemias

Talpaz, M., Shah, N. P., Kantarjian, H., Donato, N., Nicoll, J., Paquette, R., Cortes, J., O'Brien, S., Nicaise, C., Bleickardt, E., et al. (2006) · New England Journal of Medicine · doi:10.1056/nejmoa055229 · Cited by 1,760 · see citing works

Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia

Shah, N. P., Nicoll, J. M., Nagar, B., Gorre, M. E., PAQUETTE, R. L., Kuriyan, J., & Sawyers, C. L. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00096-x · Cited by 1,608 · see citing works

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. J. P., Fabbro, D., Fendrich, G., Hall–Meyers, E., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.01.007 · Cited by 1,494 · see citing works

Discovery of N -(2-Chloro-6-methyl- phenyl)-2-(6-(4-(2-hydroxyethyl)- piperazin-1-yl)-2-methylpyrimidin-4- ylamino)thiazole-5-carboxamide (BMS-354825), a Dual Src/Abl Kinase Inhibitor with Potent Antitumor Activity in Preclinical Assays

Lombardo, L. J., Lee, F. Y., Chen, P., Norris, D. J., 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 1,303 · see citing works

The development of imatinib as a therapeutic agent for chronic myeloid leukemia

Deininger, M. W., Buchdunger, E., & Druker, B. J. (2004) · Blood · doi:10.1182/blood-2004-08-3097 · Cited by 1,252 · see citing works

Inhibition of the Abl protein-tyrosine kinase in vitro and in vivo by a 2-phenylaminopyrimidine derivative.

Buchdunger, E., Zimmermann, J., Mett, H., Meyer, T., Müller, M., Druker, B. J., & Lydon, N. (1996) · PubMed · Cited by 1,060 · see citing works

<i>In vitro</i> Activity of Bcr-Abl Inhibitors AMN107 and BMS-354825 against Clinically Relevant Imatinib-Resistant Abl Kinase Domain Mutants

O'Hare, T., Walters, D. K., Stoffregen, E. P., Jia, T., Manley, P. W., Mestan, J., Cowan-Jacob, S. W., Lee, F. Y., Heinrich, M. C., Deininger, M. W. N., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0259 · Cited by 1,036 · see citing works

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 928 · see citing works

Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

Songyang, Z., Carraway, K. L., Eck, M. J., Harrison, S. C., Feldman, R. A., Mohammadi, M., Schlessinger, J., Hubbard, S. R., Smith, D. P., Eng, C., et al. (1995) · Nature · doi:10.1038/373536a0 · Cited by 919 · see citing works

Structural Basis for the Autoinhibition of c-Abl Tyrosine Kinase

Nagar, B., Hantschel, O. D., Young, M. A., Scheffzek, K., Veach, D. R., Bornmann, W. G., Clarkson, B., Superti‐Furga, G., & Kuriyan, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00194-6 · Cited by 880 · see citing works

The Structure of Dasatinib (BMS-354825) Bound to Activated ABL Kinase Domain Elucidates Its Inhibitory Activity against Imatinib-Resistant ABL Mutants

Tokarski, J. S., Newitt, J. A., Chang, C. Y. J., Cheng, J. D., Wittekind, M. G., Kiefer, S. E., Kish, K., Lee, F. Y., Borzilleri, R. M., Lombardo, L. J., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4187 · Cited by 698 · see citing works

Structural Basis for the Autoinhibition and STI-571 Inhibition of c-Kit Tyrosine Kinase

Mol, C. D., Dougan, D. R., Schneider, T. R., Skene, R. J., Kraus, M. L., Scheibe, D. N., Snell, G., Zou, H., Sang, B., & Wilson, K. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403319200 · Cited by 634 · see citing works

Inhibition of drug-resistant mutants of ABL, KIT, and EGF receptor kinases

Carter, T. A., Wodicka, L. M., Shah, N. P., Velasco, A. M., Fabian, M. A., Treiber, D. K., Milanov, Z. V., Atteridge, C. E., Biggs, W., Edeen, P. T., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504952102 · Cited by 550 · see citing works

Regulation of the c-Abl and Bcr–Abl tyrosine kinases

Hantschel, O. D., & Superti‐Furga, G. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1280 · Cited by 491 · see citing works

The BCR-ABL Story: Bench to Bedside and Back

Wong, S., & Witte, O. N. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104753 · Cited by 402 · see citing works

Dasatinib or high-dose imatinib for chronic-phase chronic myeloid leukemia after failure of first-line imatinib: a randomized phase 2 trial

Kantarjian, H. M., Pasqüini, R., Hamerschlak, N., Rousselot, P. H., Hołowiecki, J., Jootar, S., Robak, T., Хорошко, Н. Д., Masszi, T., Skotnicki, A. B., et al. (2007) · Blood · doi:10.1182/blood-2006-11-056028 · Cited by 370 · see citing works

Regulation of Btk Function by a Major Autophosphorylation Site Within the SH3 Domain

Park, H., Wahl, M. I., Afar, D., Turck, C. W., Rawlings, D. J., Tam, C. C., Scharenberg, A. M., Kinet, J., & Witte, O. N. (1996) · Immunity · doi:10.1016/s1074-7613(00)80417-3 · Cited by 323 · see citing works

The Tec family of cytoplasmic tyrosine kinases: mammalian Btk, Bmx, Itk, Tec, Txk and homologs in other species

Smith, C. I. E., Islam, T. C., Mattsson, P. T., Mohamed, A. J., Nore, B. F., & Vihinen, M. (2001) · BioEssays · doi:10.1002/bies.1062 · Cited by 316 · see citing works

Involvement of Bruton's Tyrosine Kinase in FcεRI-dependent Mast Cell Degranulation and Cytokine Production

Hata, D., Kawakami, Y., Inagaki, N., Lantz, C. S., Kitamura, T., Khan, W. N., Maeda‐Yamamoto, M., Miura, T., Han, W., Hartman, S. E., et al. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.8.1235 · Cited by 262 · see citing works

Target Identification in Chemical Genetics

Burdine, L. J., & Kodadek, T. J. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.05.001 · Cited by 191 · see citing works

Targeted CML therapy: controlling drug resistance, seeking cure

O’Hare, T., Corbin, A. S., & Druker, B. J. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2005.11.002 · Cited by 176 · see citing works

Redundant and Opposing Functions of Two Tyrosine Kinases, Btk and Lyn, in Mast Cell Activation

Kawakami, Y., Kitaura, J., Satterthwaite, A. B., Kato, R. M., Asai, K., Hartman, S. E., Maeda‐Yamamoto, M., Lowell, C. A., Rawlings, D. J., Witte, O. N., et al. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.3.1210 · Cited by 159 · see citing works

Dasatinib

Kantarjian, H., Jabbour, E., Grimley, J., & Kirkpatrick, P. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2135 · Cited by 149 · see citing works

Bruton's Tyrosine Kinase Is Required For Lipopolysaccharide-induced Tumor Necrosis Factor α Production

Horwood, N. J., Mahon, T., McDaid, J., Campbell, J., Mano, H., Brennan, F. M., Webster, D., & Foxwell, B. M. J. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021845 · Cited by 145 · see citing works

Crystal Structure of Bruton's Tyrosine Kinase Domain Suggests a Novel Pathway for Activation and Provides Insights into the Molecular Basis of X-linked Agammaglobulinemia

Chen, M., Zhou, M., & Uckun, F. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104828200 · Cited by 105 · see citing works

Tec kinases: modulators of lymphocyte signaling and development

Lewis, C. M., Broussard, C., Czar, M. J., & Schwartzberg, P. L. (2001) · Current Opinion in Immunology · doi:10.1016/s0952-7915(00)00221-1 · Cited by 101 · see citing works

Mimicry of a constitutively active pre–B cell receptor in acute lymphoblastic leukemia cells

Feldhahn, N., Klein, F., Mooster, J. L., Hadweh, P., Sprangers, M., Wartenberg, M., Bekhite, M. M., Hofmann, W., Herzog, S., Jumaa, H., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042101 · Cited by 88 · see citing works

Chemical Proteomic Analysis Reveals Alternative Modes of Action for Pyrido[2,3-d]pyrimidine Kinase Inhibitors

Wissing, J. B., Godl, K., Brehmer, D., Blencke, S., Weber, M., Habenberger, P., Stein-Gerlach, M., Missio, A., Cotten, M. L., Müller, S., et al. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400124-mcp200 · Cited by 78 · see citing works

Dual tyrosine kinase inhibitors in chronic myeloid leukemia

Martinelli, G., Soverini, S., Rosti, G., & Baccarani, M. (2005) · Leukemia · doi:10.1038/sj.leu.2403950 · Cited by 67 · see citing works

Crystal Structures of Interleukin-2 Tyrosine Kinase and Their Implications for the Design of Selective Inhibitors

Brown, K., Long, J. M., Vial, S., Dedi, N., Dunster, N. J., RENWICK, S. B., Tanner, A. J., Frantz, J. D., Fleming, M. A., & Cheetham, G. M. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400031200 · Cited by 62 · see citing works

Bruton tyrosine kinase (BTK) in X-linked agammaglobulinemia (XLA)

Vihinen, M. (2000) · Frontiers in bioscience · doi:10.2741/vihinen · Cited by 61 · see citing works

Identification of intracellular targets of small molecular weight chemical compounds using affinity chromatography

Guiffant, D., Tribouillard‐Tanvier, D., Gug, F., Galons, H., Meijer, L., Blondel, M., & Bach, S. (2007) · Biotechnology Journal · doi:10.1002/biot.200600223 · Cited by 60 · see citing works

Characterisation of kinase-selective inhibitors by chemical proteomics

Daub, H. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.07.028 · Cited by 44 · see citing works

BTK the tyrosine kinase affected in X-linked agammaglobulinemia

Vihinen, M. (1997) · Frontiers in bioscience · doi:10.2741/a172 · Cited by 31 · see citing works

Chronic active B-cell-receptor signalling in diffuse large B-cell lymphoma

Davis, R. E., Ngo, V. N., Lenz, G., Tolar, P., Young, R. M., Romesser, P. B., Kohlhammer, H., Lamy, L., Zhao, H., Yang, Y., et al. (2010) · Nature · doi:10.1038/nature08638 · Cited by 1,651 · see citing works

Resistance Mechanisms for the Bruton's Tyrosine Kinase Inhibitor Ibrutinib

Woyach, J. A., Furman, R. R., Liu, T.-M., Ozer, H. G., Zapatka, M., Ruppert, A. S., Xue, L., Li, D. H.-H., Steggerda, S. M., Versele, M., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1400029 · Cited by 1,275 · see citing works

Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets

Rix, U., Hantschel, O. D., Dürnberger, G., Rix, L. L. R., Planyavsky, M., Fernbach, N. V., Kaupe, I., Bennett, K. L., Valent, P., Colinge, J., et al. (2007) · Blood · doi:10.1182/blood-2007-07-102061 · Cited by 671 · see citing works

Target profiling of small molecules by chemical proteomics

Rix, U., & Superti‐Furga, G. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.216 · Cited by 573 · see citing works

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 564 · see citing works

Oncogenic Activation of NF- B

Staudt, L. M. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000109 · Cited by 485 · see citing works

Prolonged and tunable residence time using reversible covalent kinase inhibitors

Bradshaw, J. M., McFarland, J. M., Paavilainen, V. O., Bisconte, A. R., Tam, D., Phan, V. T., Romanov, S., Finkle, D., Shu, J., Patel, V. P., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1817 · Cited by 428 · see citing works

The tyrosine kinase network regulating mast cell activation

Gilfillan, A. M., & Rivera, J. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00742.x · Cited by 432 · see citing works

The B-cell receptor signaling pathway as a therapeutic target in CLL

Woyach, J. A., Johnson, A. J., & Byrd, J. C. (2012) · Blood · doi:10.1182/blood-2012-02-362624 · Cited by 412 · see citing works

Targeting pathological B cell receptor signalling in lymphoid malignancies

Young, R. M., & Staudt, L. M. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd3937 · Cited by 400 · see citing works

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. S., Herring, C., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.04.011 · Cited by 357 · see citing works

Clonal expansion of T/NK-cells during tyrosine kinase inhibitor dasatinib therapy

Mustjoki, S. M., Ekblom, M., Arstila, T. P., Dybedal, I., Epling‐Burnette, P. K., Guilhot, F., Hjorth‐Hansen, H., Höglund, M., Kovanen, P. E., Laurinolli, T., et al. (2009) · Leukemia · doi:10.1038/leu.2009.46 · Cited by 329 · see citing works

Global target profile of the kinase inhibitor bosutinib in primary chronic myeloid leukemia cells

Rix, L. L. R., Rix, U., Colinge, J., Hantschel, O. D., Bennett, K. L., Stranzl, T., Müller, A. C., Baumgärtner, C., Valent, P., Augustin, M. A., et al. (2008) · Leukemia · doi:10.1038/leu.2008.334 · Cited by 280 · see citing works

A chemical and phosphoproteomic characterization of dasatinib action in lung cancer

Li, J., Rix, U., Fang, B., Bai, Y., Edwards, A., Colinge, J., Bennett, K. L., Gao, J., Song, L., Eschrich, S. A., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.332 · Cited by 279 · see citing works

Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib

Hantschel, O., Rix, U., & Superti-Furga, G. (2008) · Leukemia &amp; Lymphoma · doi:10.1080/10428190801896103 · Cited by 256 · see citing works

Targeting Src Family Kinases Inhibits Growth and Lymph Node Metastases of Prostate Cancer in an Orthotopic Nude Mouse Model

Park, S. I., Zhang, J., Phillips, K. A., Araujo, J. C., Najjar, A. M., Volgin, A. Y., Gelovani, J. G., Kim, S., Wang, Z., & Gallick, G. E. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-2997 · Cited by 233 · see citing works

Cell-Based Proteome Profiling of Potential Dasatinib Targets by Use of Affinity-Based Probes

Shi, H., Zhang, C., Chen, G. Y. J., & Yao, S. Q. (2012) · Journal of the American Chemical Society · doi:10.1021/ja208518u · Cited by 228 · see citing works

Inhibition of Btk with CC-292 Provides Early Pharmacodynamic Assessment of Activity in Mice and Humans

Evans, E. K., Tester, R. W., Aslanian, S., Karp, R., Sheets, M. P., Labenski, M., Witowski, S. R., Lounsbury, H. A., Chaturvedi, P., Mazdiyasni, H., et al. (2013) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.203489 · Cited by 223 · see citing works

Global Effects of Kinase Inhibitors on Signaling Networks Revealed by Quantitative Phosphoproteomics

Pan, C., Olsen, J. V., Daub, H., & Mann, M. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900285-mcp200 · Cited by 222 · see citing works

Bruton Tyrosine Kinase (BTK) and Its Role in B-cell Malignancy

Buggy, J. J., & Elias, L. (2012) · International Reviews of Immunology · doi:10.3109/08830185.2012.664797 · Cited by 213 · see citing works

Evidence that Resistance to Nilotinib May Be Due to BCR-ABL, Pgp, or Src Kinase Overexpression

Mahon, F., Hayette, S., Lagarde, V., Belloc, F., Turcq, B., Nicolini, F. E., Bélanger, C., Manley, P. W., Leroy, C., Étienne, G., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1008 · Cited by 212 · see citing works

B-cell receptor signaling as a driver of lymphoma development and evolution

Niemann, C. U., & Wiestner, A. U. (2013) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.09.001 · Cited by 206 · see citing works

A cellular screen identifies ponatinib and pazopanib as inhibitors of necroptosis

Fauster, A., Rebsamen, M., Huber, K., Bigenzahn, J. W., Stukalov, A., Lardeau, C.-H., Scorzoni, S., Brückner, M., Gridling, M., Parapatics, K., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.130 · Cited by 192 · see citing works

Mono/oligoclonal T and NK cells are common in chronic myeloid leukemia patients at diagnosis and expand during dasatinib therapy

Kreutzman, A. S., Juvonen, V., Kairisto, V., Ekblom, M., Stenke, L., Seggewiss, R., Porkka, K., & Mustjoki, S. M. (2010) · Blood · doi:10.1182/blood-2009-12-256800 · Cited by 173 · see citing works

Charting the molecular network of the drug target Bcr-Abl

Brehme, M., Hantschel, O. D., Colinge, J., Kaupe, I., Planyavsky, M., Köcher, T., Mechtler, K., Bennett, K. L., & Superti‐Furga, G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900653106 · Cited by 171 · see citing works

Crosstalk between ROR1 and the Pre-B Cell Receptor Promotes Survival of t(1;19) Acute Lymphoblastic Leukemia

Bicocca, V. T., Chang, B. H., Masouleh, B. K., Müschen, M., Loriaux, M., Druker, B. J., & Tyner, J. W. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.08.027 · Cited by 170 · see citing works

Dasatinib regulates LPS-induced microglial and astrocytic neuroinflammatory responses by inhibiting AKT/STAT3 signaling

Ryu, K., Lee, H., Woo, H., Kang, R.-J., Han, K., Park, H., Lee, S. M., Lee, J., Jeong, Y. J., Nam, H.-W., et al. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1561-x · Cited by 160 · see citing works

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 · see citing works

Functional characterization of BTKC481S mutation that confers ibrutinib resistance: exploration of alternative kinase inhibitors

Cheng, S.-H., Guo, A., Lu, P., Ma, J., Coleman, M., & Wang, Y.-L. (2014) · Leukemia · doi:10.1038/leu.2014.263 · Cited by 155 · see citing works

Structure, Regulation, Signaling, and Targeting of Abl Kinases in Cancer

Hantschel, O. D. (2012) · Genes & Cancer · doi:10.1177/1947601912458584 · Cited by 156 · see citing works

Emerging role of kinase-targeted strategies in chronic lymphocytic leukemia

Wiestner, A. U. (2012) · Blood · doi:10.1182/blood-2012-05-423194 · Cited by 151 · see citing works

Kinase Pathway Dependence in Primary Human Leukemias Determined by Rapid Inhibitor Screening

Tyner, J. W., Yang, W. F., Bankhead, A., Fan, G., Fletcher, L. B., Bryant, J. A., Glover, J., Chang, B. H., Spurgeon, S. E. F., Fleming, W., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-1906 · Cited by 150 · see citing works

Resistance to ABT-199 induced by microenvironmental signals in chronic lymphocytic leukemia can be counteracted by CD20 antibodies or kinase inhibitors

Thijssen, R., Slinger, E., Weller, K., Geest, C. R., Beaumont, T., van Oers, M. H. J., Kater, A. P., & Eldering, E. (2015) · Haematologica · doi:10.3324/haematol.2015.124560 · Cited by 133 · see citing works

Targeting DDR2 enhances tumor response to anti–PD-1 immunotherapy

Tu, M. M., Lee, F. Y., Jones, R. T., Kimball, A. K., Saravia, E., Graziano, R. F., Coleman, B. M., Menard, K., Yan, J., Michaud, E., et al. (2019) · Science Advances · doi:10.1126/sciadv.aav2437 · Cited by 130 · see citing works

Specificity and mechanism-of-action of the JAK2 tyrosine kinase inhibitors ruxolitinib and SAR302503 (TG101348)

Zhou, T., Georgeon, S., Moser, R., Moore, D. J., Caflisch, A., & Hantschel, O. D. (2013) · Leukemia · doi:10.1038/leu.2013.205 · Cited by 125 · see citing works

Small molecule photocatalysis enables drug target identification via energy transfer

Trowbridge, A., Seath, C. P., Rodriguez‐Rivera, F. P., Li, B. X., Dul, B. E., Schwaid, A. G., Buksh, B. F., Geri, J. B., Oakley, J. V., Fadeyi, O., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208077119 · Cited by 119 · see citing works

c-Abl kinase inhibitors overcome CD40-mediated drug resistance in CLL: implications for therapeutic targeting of chemoresistant niches

Hallaert, D. Y. H., Jaspers, A., van Noesel, C. J. M., van Oers, M. H. J., Kater, A. P., & Eldering, E. (2008) · Blood · doi:10.1182/blood-2008-03-146704 · Cited by 119 · see citing works

Off-target effects of BCR–ABL1 inhibitors and their potential long-term implications in patients with chronic myeloid leukemia

Steegmann, J. L., Cervantes, F., le Coutre, P., Porkka, K., & Saglio, G. N. (2012) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2012.695779 · Cited by 113 · see citing works

Predictors of Primary Imatinib Resistance in Chronic Myelogenous Leukemia Are Distinct From Those in Secondary Imatinib Resistance

Zhang, W. W., Cortes, J. E., Yao, H., Zhang, L., Reddy, N. G., Jabbour, E. J., Kantarjian, H. M., & Jones, D. M. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2008.19.4076 · Cited by 112 · see citing works

Tyrosine kinase inhibitors impair B-cell immune responses in CML through off-target inhibition of kinases important for cell signaling

de Lavallade, H., Khoder, A., Hart, M., Sarvaria, A., Sekine, T., Alsuliman, A., Mielke, S., Bazeos, A., Stringaris, K., Ali, S., et al. (2013) · Blood · doi:10.1182/blood-2012-11-465039 · Cited by 110 · see citing works

A phase I trial of PRN1008, a novel reversible covalent inhibitor of Bruton's tyrosine kinase, in healthy volunteers

Smith, P. F., Krishnarajah, J., Nunn, P. A., Hill, R. J., Karr, D. E., Tam, D., Masjedizadeh, M. R., Funk, J. O., & Gourlay, S. G. (2017) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.13351 · Cited by 108 · see citing works

Immunosuppression and atypical infections in CML patients treated with dasatinib at 140 mg daily

Sillaber, C., Herrmann, H., Bennett, K. L., Rix, U., Baumgärtner, C., Böhm, A., Herndlhofer, S., Tschachler, E., Superti‐Furga, G., Jaeger, U., et al. (2009) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2009.02206.x · Cited by 104 · see citing works

Proteomic Contributions to Personalized Cancer Care

Koomen, J. M., Haura, E. B., Bepler, G., Sutphen, R., Remily-Wood, E. R., Benson, K., Hussein, M. A., Hazlehurst, L., Yeatman, T. J., Hildreth, L. T., et al. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r800002-mcp200 · Cited by 103 · see citing works

Biology of Chronic Lymphocytic Leukemia in Different Microenvironments

Herishanu, Y., Katz, B., Lipsky, A. H., & Wiestner, A. U. (2013) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2013.01.002 · Cited by 103 · see citing works

DCAF1-based PROTACs with activity against clinically validated targets overcoming intrinsic- and acquired-degrader resistance

Schröder, M., Renatus, M., Liang, X., Meili, F., Zoller, T., Ferrand, S., Gauter, F., Li, X., Sigoillot, F. D., Gleim, S., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44237-4 · Cited by 110 · see citing works

Rapid mobilization of cytotoxic lymphocytes induced by dasatinib therapy

Mustjoki, S. M., Auvinen, K., Kreutzman, A. S., Rousselot, P. H., Hernesniemi, S., Melo, T., Lahesmaa-Korpinen, A.-M., Hautaniemi, S., Bouchet, S., Molimard, M., et al. (2012) · Leukemia · doi:10.1038/leu.2012.348 · Cited by 93 · see citing works

Turning liabilities into opportunities: Off-target based drug repurposing in cancer

Palve, V. C., Liao, Y., Rix, L. L. R., & Rix, U. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.02.003 · Cited by 92 · see citing works

Ibrutinib inhibition of Bruton protein-tyrosine kinase (BTK) in the treatment of B cell neoplasms

Roskoski, R. J. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.09.011 · Cited by 92 · see citing works

Ibrutinib inhibits pre-BCR+ B-cell acute lymphoblastic leukemia progression by targeting BTK and BLK

Kim, E., Hurtz, C., Koehrer, S., Wang, Z., Balasubramanian, S., Chang, B. Y., Müschen, M., Davis, R. E., & Burger, J. A. (2016) · Blood · doi:10.1182/blood-2016-06-722900 · Cited by 88 · see citing works

Bruton’s Tyrosine Kinase Inhibitors: Approaches to Potent and Selective Inhibition, Preclinical and Clinical Evaluation for Inflammatory Diseases and B Cell Malignancies

Lou, Y. C., Owens, T. D., Kuglstatter, A., Kondru, R. K., & GOLDSTEIN, D. M. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300035p · Cited by 88 · see citing works

Unexpected Off-Targets and Paradoxical Pathway Activation by Kinase Inhibitors

Hantschel, O. D. (2014) · ACS Chemical Biology · doi:10.1021/cb500886n · Cited by 87 · see citing works

BTK signaling—a crucial link in the pathophysiology of chronic spontaneous urticaria

Bernstein, J. A., Maurer, M., & Saini, S. S. (2023) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2023.12.008 · Cited by 92 · see citing works

The clinically approved drugs dasatinib and bosutinib induce anti-inflammatory macrophages by inhibiting the salt-inducible kinases

Ozanne, J., Prescott, A. R., & Clark, K. (2014) · Biochemical Journal · doi:10.1042/bj20141165 · Cited by 88 · see citing works

The effects of dasatinib on IgE receptor–dependent activation and histamine release in human basophils

Kneidinger, M., Schmidt, U., Rix, U., Gleixner, K. V., Vales, A., Baumgärtner, C., Lupinek, C., Weghofer, M., Bennett, K. L., Herrmann, H., et al. (2008) · Blood · doi:10.1182/blood-2007-08-104372 · Cited by 84 · see citing works

Strategies for senolytic drug discovery

Power, H., Valtchev, P., Dehghani, F., & Schindeler, A. (2023) · Aging Cell · doi:10.1111/acel.13948 · Cited by 81 · see citing works

Pharmacological treatment options for mast cell activation disease

Molderings, G. J., Haenisch, B., Brettner, S., Homann, J., Menzen, M., Dumoulin, F. L., Panse, J., Butterfield, J. H., & Afrin, L. B. (2016) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-016-1247-1 · Cited by 77 · see citing works

Dasatinib

Lindauer, M., & Hochhaus, A. (2018) · Recent results in cancer research/Recent Results in Cancer Research · doi:10.1007/978-3-319-91439-8_2 · Cited by 79 · see citing works

Inhibitors of BTK and ITK : State of the New Drugs for Cancer, Autoimmunity and Inflammatory Diseases

Vargas, L., Hamasy, A., Nore, B. F., & Smith, C. I. E. (2013) · Scandinavian Journal of Immunology · doi:10.1111/sji.12069 · Cited by 77 · see citing works

A comprehensive target selectivity survey of the BCR-ABL kinase inhibitor INNO-406 by kinase profiling and chemical proteomics in chronic myeloid leukemia cells

Rix, U., Rix, L. L. R., Terker, A. S., Fernbach, N. V., Hantschel, O. D., Planyavsky, M., Breitwieser, F. P., Herrmann, H., Colinge, J., Bennett, K. L., et al. (2009) · Leukemia · doi:10.1038/leu.2009.228 · Cited by 77 · see citing works

Dasatinib

Lindauer, M., & Hochhaus, A. (2014) · Recent results in cancer research/Recent Results in Cancer Research · doi:10.1007/978-3-642-54490-3_2 · Cited by 76 · see citing works

Dasatinib inhibits B cell receptor signalling in chronic lymphocytic leukaemia but novel combination approaches are required to overcome additional pro‐survival microenvironmental signals

McCaig, A. M., Cosimo, E., Leach, M. T. J., & Michie, A. (2011) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08507.x · Cited by 80 · see citing works

Chemoproteomics-based kinome profiling and target deconvolution of clinical multi-kinase inhibitors in primary chronic lymphocytic leukemia cells

Kruse, U., Pallasch, C. P., Bantscheff, M., Eberhard, D., Frenzel, L., Ghidelli, S., Maier, S., Werner, T., Wendtner, C., & Drewes, G. (2010) · Leukemia · doi:10.1038/leu.2010.233 · Cited by 76 · see citing works

Bruton Tyrosine Kinase Is a Therapeutic Target in Stem-like Cells from Multiple Myeloma

Yang, Y., Shi, J., Gu, Z., Salama, M. E., Das, S., Wendlandt, E. B., Xu, H., Huang, J., Yi, T., Hao, M., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2362 · Cited by 75 · see citing works

KIT-D816V–independent oncogenic signaling in neoplastic cells in systemic mastocytosis: role of Lyn and Btk activation and disruption by dasatinib and bosutinib

Gleixner, K. V., Mayerhofer, M., Cerny‐Reiterer, S., Hoermann, G., Rix, U., Bennett, K. L., Hadzijusufovic, E., Meyer, R. A., Pickl, W. F., Gotlib, J. R., et al. (2011) · Blood · doi:10.1182/blood-2010-06-289959 · Cited by 74 · see citing works

Inhibition of IgE-mediated secretion from human basophils with a highly selective Bruton's tyrosine kinase, Btk, inhibitor

MacGlashan, D. W., Honigberg, L. A., Smith, A., Buggy, J. J., & Schroeder, J. T. (2011) · International Immunopharmacology · doi:10.1016/j.intimp.2010.12.018 · Cited by 74 · see citing works

Fyn Kinase in Brain Diseases and Cancer: The Search for Inhibitors

Schenone, S., Brullo, C., Musumeci, F., Biava, M., Falchi, F., & Botta, M. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711796150531 · Cited by 74 · see citing works

Tyrosine kinases as targets for the treatment of rheumatoid arthritis

Swanson, C., Paniagua, R. T., Lindström, T. M., & Robinson, W. H. (2009) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2009.82 · Cited by 73 · see citing works

Tec Family Kinases in Inflammation and Disease

Horwood, N. J., Urbaniak, A. M., & Danks, L. (2012) · International Reviews of Immunology · doi:10.3109/08830185.2012.670334 · Cited by 73 · see citing works

Metastasis gene NEDD9 acts through integrin β3 and Src to promote mesenchymal motility and inhibit amoeboid motility.

Ahn, J., Sanz‐Moreno, V., & Marshall, C. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.101444 · Cited by 71 · see citing works

The development of dasatinib as a treatment for chronic myeloid leukemia (CML): from initial studies to application in newly diagnosed patients

Hochhaus, A., & Kantarjian, H. M. (2013) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-013-1488-z · Cited by 72 · see citing works

Cell signalling in macrophages, the principal innate immune effector cells of rheumatoid arthritis

Drexler, S. K., Kong, P. L., Wales, J., & Foxwell, B. M. J. (2008) · Arthritis Research & Therapy · doi:10.1186/ar2481 · Cited by 70 · see citing works

Bruton tyrosine kinase inhibitors: a promising novel targeted treatment for B cell lymphomas

Aalipour, A., & Advani, R. H. (2013) · British Journal of Haematology · doi:10.1111/bjh.12573 · Cited by 69 · see citing works

Application of Multiplexed Kinase Inhibitor Beads to Study Kinome Adaptations in Drug-Resistant Leukemia

Cooper, M. J., Cox, N. J., Zimmerman, E. I., Dewar, B. J., Duncan, J. S., Whittle, M. C., Nguyen, T., Jones, L., Roy, S. G., Smalley, D. M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066755 · Cited by 69 · see citing works

Pharmacological targeting of the KIT growth factor receptor: a therapeutic consideration for mast cell disorders

Jensen, B. M., Akin, C., & Gilfillan, A. M. (2008) · British Journal of Pharmacology · doi:10.1038/bjp.2008.204 · Cited by 67 · see citing works

Dasatinib

McCormack, P. L., & Keam, S. J. (2011) · Drugs · doi:10.2165/11207580-000000000-00000 · Cited by 67 · see citing works

Target interaction profiling of midostaurin and its metabolites in neoplastic mast cells predicts distinct effects on activation and growth

Peter, B., Winter, G. E., Blatt, K., Bennett, K. L., Stefanzl, G., Rix, U., Eisenwort, G., Hadzijusufovic, E., Gridling, M., Dutreix, C., et al. (2016) · Leukemia · doi:10.1038/leu.2015.242 · Cited by 63 · see citing works

Discovery of a Series of 2,5-Diaminopyrimidine Covalent Irreversible Inhibitors of Bruton’s Tyrosine Kinase with in Vivo Antitumor Activity

Li, X., Zuo, Y., Tang, G., Wang, Y., Zhou, Y., Wang, X., Guo, T., Xia, M., Ding, N., & Pan, Z. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4017762 · Cited by 64 · see citing works

Lymphocytosis after treatment with dasatinib in chronic myeloid leukemia: Effects on response and toxicity

Schiffer, C. A., Cortes, J. E., Hochhaus, A., Saglio, G. N., le Coutre, P., Porkka, K., Mustjoki, S. M., Mohamed, H., & Shah, N. P. (2016) · Cancer · doi:10.1002/cncr.29933 · Cited by 63 · see citing works

NF-κB Activation in Lymphoid Malignancies: Genetics, Signaling, and Targeted Therapy

Grondona, P., Bucher, P., Schulze‐Osthoff, K., Hailfinger, S., & Schmitt, A. (2018) · Biomedicines · doi:10.3390/biomedicines6020038 · Cited by 62 · see citing works

Energetics-Based Discovery of Protein–Ligand Interactions on a Proteomic Scale

Liu, P.-F., Kihara, D., & Park, C. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.02.026 · Cited by 61 · see citing works

Emerging stem cell concepts for imatinib‐resistant chronic myeloid leukaemia: implications for the biology, management, and therapy of the disease

Valent, P. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07197.x · Cited by 61 · see citing works

Paradigm shift in oncology: targeting the immune system rather than cancer cells

Shekarian, T., Valsesia‐Wittmann, S., Caux, C., & Marabelle, A. (2015) · Mutagenesis · doi:10.1093/mutage/geu073 · Cited by 60 · see citing works

BTK inhibition is a potent approach to block IgE‐mediated histamine release in human basophils

Smiljkovic, D., Blatt, K., Stefanzl, G., Dorofeeva, Y., Skrabs, C., Focke‐Tejkl, M., Sperr, W. R., Jaeger, U., Valenta, R., & Valent, P. (2017) · Allergy · doi:10.1111/all.13166 · Cited by 58 · see citing works

Emerging role of kinase-targeted strategies in chronic lymphocytic leukemia

Wiestner, A. U. (2012) · Hematology · doi:10.1182/asheducation.v2012.1.88.3801172 · Cited by 57 · see citing works

A phase II trial of dasatinib in patients with metastatic castration-resistant prostate cancer treated previously with chemotherapy

Twardowski, P. W., Beumer, J. H., Chen, C. S., Kraft, A. S., Chatta, G. S., Mitsuhashi, M., Ye, W., Christner, S. M., & Lilly, M. B. (2013) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e328361feb0 · Cited by 56 · see citing works

An Update On Dual Src/Abl Inhibitors

Musumeci, F., Schenone, S., Brullo, C., & Botta, M. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.29 · Cited by 53 · see citing works

Tec family kinases: regulation of FcεRI‐mediated mast‐cell activation

Ellmeier, W., Abramova, A., & Schebesta, A. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08073.x · Cited by 52 · see citing works

Dasatinib-Loaded Topical Nano-Emulgel for Rheumatoid Arthritis: Formulation Design and Optimization by QbD, In Vitro, Ex Vivo, and In Vivo Evaluation

Donthi, M. R., Saha, R. N., Singhvi, G., & Dubey, S. K. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030736 · Cited by 51 · see citing works

Inhibition of PVR with a Tyrosine Kinase Inhibitor, Dasatinib, in the Swine

Umazume, K., Liu, L., Scott, P. A., de Castro, J. P. F., McDonald, K., Kaplan, H. J., & Tamiya, S. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-10418 · Cited by 51 · see citing works

Intrinsic differences between the catalytic properties of the oncogenic NUP214-ABL1 and BCR-ABL1 fusion protein kinases

Keersmaecker, K. D., Versele, M., Cools, J., Superti‐Furga, G., & Hantschel, O. D. (2008) · Leukemia · doi:10.1038/leu.2008.242 · Cited by 50 · see citing works

Kinase inhibitors as drugs for chronic inflammatory and immunological diseases: progress and challenges

Rokosz, L. L., Beasley, J. R., Carroll, C. D., Lin, T. H., Zhao, J., Appell, K. C., & Webb, M. L. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.7.883 · Cited by 49 · see citing works

Affinity-Based Probes Based on Type II Kinase Inhibitors

Ranjitkar, P., Perera, B. G. K., Swaney, D. L., Hari, S. B., Larson, E. T., Krishnamurty, R., Merritt, E. A., Villén, J., & Maly, D. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306035v · Cited by 48 · see citing works

Targeting inflammatory pathways in chronic lymphocytic leukemia

Rozovski, U., Keating, M. J., & Estrov, Z. E. (2013) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2013.07.011 · Cited by 48 · see citing works

B-Cell Receptor Signaling in Lymphoid Malignancies and Autoimmunity

Avalos, A. M., Meyer‐Wentrup, F. A. G., & Ploegh, H. L. (2014) · Advances in immunology · doi:10.1016/b978-0-12-800266-7.00004-2 · Cited by 47 · see citing works

Inhibition of STAT5: A therapeutic option in BCR-ABL1-driven leukemia

Berger, A., Sexl, V., Valent, P., & Moriggl, R. (2014) · Oncotarget · doi:10.18632/oncotarget.2465 · Cited by 47 · see citing works

Large granular lymphocytosis during dasatinib therapy

Qiu, Z.-Y., Xu, W., & Li, J. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.27310 · Cited by 46 · see citing works

New insights into small‐molecule inhibitors of Bcr‐Abl

Schenone, S., Bruno, O., Radi, M., & Botta, M. (2009) · Medicinal Research Reviews · doi:10.1002/med.20175 · Cited by 45 · see citing works

Emerging role of kinase-targeted strategies in chronic lymphocytic leukemia.

Wiestner, A. U. (2012) · PubMed · doi:10.1182/asheducation-2012.1.88 · Cited by 45 · see citing works

Synergistic growth-inhibitory effects of ponatinib and midostaurin (PKC412) on neoplastic mast cells carrying KIT D816V

Gleixner, K. V., Peter, B., Blatt, K., Suppan, V., Reiter, A., Radia, D. H., Hadzijusufovic, E., & Valent, P. (2013) · Haematologica · doi:10.3324/haematol.2012.079202 · Cited by 45 · see citing works

Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms

Duarte, D., Lamontanara, A. J., Sala, G. L., Jeong, S., Sohn, Y., Panjkovich, A., Georgeon, S., Kükenshöner, T., Marcaida, M. J., Pojer, F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16128-5 · Cited by 46 · see citing works

Systematic Profiling and Novel Targets of the Bcr-Abl Kinase Inhibitors Imatinib, Nilotinib and Dasatinib.

Hantschel, O. D., Rix, U., Bürckstümmer, T., Schmidt, U., Kneidinger, M., Bennett, K. L., Kaupe, I., Ellmeier, W., Valent, P., & Superti‐Furga, G. (2007) · Blood · doi:10.1182/blood.v110.11.4542.4542 · Cited by 1 · see citing works

Abstract 3099: Hnd-01: a potent inhibitor of wild type mutant BTK

Zhang, J., Samatar, A. A., Tan, Y., Pi, S., Zhou, Z., Xu, Y., & Yang, D. (2023) · Cancer Research · doi:10.1158/1538-7445.am2023-3099

Characteristics of Dasatinib- and Imatinib-Resistant Chronic Myelogenous Leukemia Cells

Okabe, S., Tauchi, T., & Ohyashiki, K. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-0461 · Cited by 30 · see citing works

Mechanism of Drug Resistance to Dasatinib (BMS-354825) and Imatinib in Chronic Myelogenous Leukemia Cells.

Okabe, S., Tauchi, T., Broxmeyer, H. E., & Ohyashiki, K. (2006) · Blood · doi:10.1182/blood.v108.11.1386.1386 · Cited by 1 · see citing works

Dasatinib: a new step in molecular target therapy

Olivieri, A., & Manzione, L. (2007) · Annals of Oncology · doi:10.1093/annonc/mdm223 · Cited by 98 · see citing works