Role of Bruton’s tyrosine kinase in B cells and malignancies
Open accessAbstract
Bruton’s tyrosine kinase (BTK) is a non-receptor kinase that plays a crucial role in oncogenic signaling that is critical for proliferation and survival of leukemic cells in many B cell malignancies. BTK was initially shown to be defective in the primary immunodeficiency X-linked agammaglobulinemia (XLA) and is essential both for B cell development and function of mature B cells. Shortly after its discovery, BTK was placed in the signal transduction pathway downstream of the B cell antigen receptor (BCR). More recently, small-molecule inhibitors of this kinase have shown excellent anti-tumor activity, first in animal models and subsequently in clinical studies. In particular, the orally administered irreversible BTK inhibitor ibrutinib is associated with high response rates in patients with relapsed/refractory chronic lymphocytic leukemia (CLL) and mantle-cell lymphoma (MCL), including patients with high-risk genetic lesions. Because ibrutinib is generally well tolerated and shows durable single-agent efficacy, it was rapidly approved for first-line treatment of patients with CLL in 2016. To date, evidence is accumulating for efficacy of ibrutinib in various other B cell malignancies. BTK inhibition has molecular effects beyond its classic role in BCR signaling. These involve B cell-intrinsic signaling pathways central to cellular survival, proliferation or retention in supportive lymphoid niches. Moreover, BTK functions in several myeloid cell populations representing important components of the tumor microenvironment. As a result, there is currently a considerable interest in BTK inhibition as an anti-cancer therapy, not only in B cell malignancies but also in solid tumors. Efficacy of BTK inhibition as a single agent therapy is strong, but resistance may develop, fueling the development of combination therapies that improve clinical responses. In this review, we discuss the role of BTK in B cell differentiation and B cell malignancies and highlight the importance of BTK inhibition in cancer therapy.
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BTK is a non-receptor tyrosine kinase that amplifies upstream BCR signaling and is essential for B-cell development and maturation.
“Bruton tyrosine kinase (BTK) is a non-receptor tyrosine kinase that amplifiesupstream B-cell receptor (BCR) signaling and is essential for B-cell development and maturation(1, 2).”
From Resistance Mechanisms and Approach to Chronic Lymphocytic Leukemia after BTK Inhibitor Therapy (2025) · cites this paper as [1]
The Background and BTK structure sections identify BTK as a non-receptor tyrosine kinase downstream of the BCR. The Abstract states that it is essential for B-cell development and mature B-cell function, and the peripheral-development section describes impaired maturation without BTK. The paper describes BTK transmitting signals to downstream targets, but does not say it amplifies upstream BCR signaling. (LLM, conf=0.86)
Experimental — accuracy not yet measuredBTK became a target in CLL due to its role downstream of the B cell receptor.
“BTK became a target of interest in chronic lymphocytic leukaemia owing to its crucial role downstream of the B cell receptor53.”
From Advances in covalent drug discovery (2022) · cites this paper as [53]
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- [211]Tillman BF, Pauff JM, Satyanarayana G, Talbott M, Warner JL. Systematic review of infectious events with the BTK inhibitor ibrutinib in the treatment of haematologic malignancies. Eur J Haematol. 2017; 29285806
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Advances in covalent drug discovery
Boike, L., Henning, N. J., & Nomura, D. K. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00542-z · Cited by 823 · see citing works
Molecular targeted therapy for anticancer treatment
Min, H.-Y., & Lee, H.-Y. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00864-3 · Cited by 569 · see citing works
Properties of FDA-approved small molecule protein kinase inhibitors
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Memory B Cells Activate Brain-Homing, Autoreactive CD4+ T Cells in Multiple Sclerosis
Jelčić, I., Nimer, F. A., Wang, J., Lentsch, V., Planas, R., Jelčić, I., Madjovski, A., Ruhrmann, S., Faigle, W., Frauenknecht, K. B. M., et al. (2018) · Cell · doi:10.1016/j.cell.2018.08.011 · Cited by 510 · see citing works
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Advances in covalent kinase inhibitors
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Targeted protein degradation: advances in drug discovery and clinical practice
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B Cells in Rheumatoid Arthritis：Pathogenic Mechanisms and Treatment Prospects
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“Targeted B Cell Checkpoints Bruton’s tyrosine kinase (BTK) is a cytoplasmic tyrosine kinase expressed in B cells, which plays a key role in BCR signal transduction and in the development and maturation of B cells (123).”
BackgroundComparative Analysis of BTK Inhibitors and Mechanisms Underlying Adverse Effects
Estupiñan, H. Y., Berglöf, A., Zain, R., & Smith, C. I. E. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.630942 · Cited by 272 · see citing works
“…receptor (BCR) signaling pathway led to the deciphering of the central role of Bruton’s tyrosine kinase (BTK) and the importance of its inhibition as an effective strategy for the treatment of B-cell malignancies (Herman et al., 2011; Smith, 2017; Pal Singh et al., 2018; Lucas and Woyach, 2019).”
BackgroundFMS-like Tyrosine Kinase 3/FLT3: From Basic Science to Clinical Implications
Kazi, J. U., & Rönnstrand, L. (2019) · Physiological Reviews · doi:10.1152/physrev.00029.2018 · Cited by 216 · see citing works
“The Bruton tyrosine kinase (BTK) plays important roles in B cell development as well as in mast cell activation and has been implicated in B cell malignancies (65, 247).”
BackgroundEfficient targeted degradation via reversible and irreversible covalent PROTACs
Gabizon, R., Shraga, A., Gehrtz, P., Livnah, E., Gurwicz, N., Avram, L., Unger, T., Albeck, S., Shulman, Z., & London, N. (2020) · doi:10.26434/chemrxiv.11494398.v1 · Cited by 213 · see citing works
Bruton tyrosine kinase inhibitors for multiple sclerosis
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Phosphorylation-Inducing Chimeric Small Molecules
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The B-Side of Cancer Immunity: The Underrated Tune
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“It is worth noting that Bruton’s tyrosine kinase (BTK) inhibitor ibrutinib used for the treatment of some B cell-associated lymphomas/leukemias has been tested in solid tumors [117].”
BackgroundPyrazole-containing pharmaceuticals: target, pharmacological activity, and their SAR studies
Li, G., Cheng, Y., Han, C., Song, C., Huang, N., & Du, Y. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00206j · Cited by 170 · see citing works
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Strategies for Targeting the NLRP3 Inflammasome in the Clinical and Preclinical Space
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NLRP3 inflammasome: a key player in the pathogenesis of life-style disorders
Ramachandran, R., Manan, A., Kim, J., & Choi, S. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01261-8 · Cited by 142 · see citing works
“Bruton ’ s tyrosine kinase directly interacts with NLRP3 and ASC, initiating ASC oligomerization and caspase-1 activation 81,82 .”
BackgroundDhillon, S. (2021) · Drugs · doi:10.1007/s40265-021-01482-5 · Cited by 141 · see citing works
“This has led to the development of highly selective, second-generation BTK inhibitors with fewer off-target effects [3, 5].”
BackgroundAdvances in targeted therapy for malignant lymphoma
Wang, L., Qin, W. D., Huo, Y., Li, X., Shi, Q., Rasko, J. E. J., Janin, A., & Zhao, W. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0113-2 · Cited by 140 · see citing works
“The offtarget inhibition of kinases containing an analogous cysteine residue with BTK may also be crucial to the side effects of ibrutinib.(287) Moreover, drug resistance reduces the clinical efficacy, warranting further investigation on combined treatment and dual inhibitors.”
BackgroundThe Importance of Being PI3K in the RAS Signaling Network
Cuesta, C., Arévalo-Alameda, C., & Castellano, E. (2021) · Genes · doi:10.3390/genes12071094 · Cited by 123 · see citing works
“BTK has a critical role in B-cell function and malignancy [66].”
BackgroundProtein kinases: drug targets for immunological disorders
Castelo‐Soccio, L. A., Kim, H., Gadina, M., Schwartzberg, P. L., Laurence, A. D. J., & O’Shea, J. J. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00877-7 · Cited by 125 · see citing works
ROBBINS, D. W., Noviski, M., Tan, Y. S., Könst, Z. A., Kelly, A., Auger, P., Brathaban, N., Cass, R. T., Chan, M. L., Cherala, G., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01007 · Cited by 120 · see citing works
Pathogenetic Aspects of Systemic Sclerosis: A View Through the Prism of B Cells
Μελισσαρόπουλος, Κ., Iliopoulos, G., Sakkas, L. I., & Daoussis, D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.925741 · Cited by 119 · see citing works
“Therapeutic targeting of key signaling molecules of B cells, such as the Bruton’s tyrosine kinase (BTK), is already employed in hematology (31) and research efforts show promising results in samples from patients with SSc.”
BackgroundTherapeutic targets and interventional strategies in COVID-19: mechanisms and clinical studies
Zhou, Y., Xie, Y., Tang, L., Pu, D., Zhu, Y., Liu, J., & Ma, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00733-x · Cited by 115 · see citing works
“Acalabrutinib, ibrutinib, and zanubrutinib are representatives of BTK inhibitors that are approved in the treatment of certain lymphomas.(278) The attempt for use of BTK inhibitors in COVID-19 treatment is limited in small-scale retrospective clinical studies.”
BackgroundPROTAC’ing oncoproteins: targeted protein degradation for cancer therapy
Kelm, J. M., Pandey, D. S., Malin, E., Kansou, H. W., Arora, S., Kumar, R., & Gavande, N. S. (2023) · Molecular Cancer · doi:10.1186/s12943-022-01707-5 · Cited by 115 · see citing works
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“6 Introduction Targeted Bruton tyrosine kinase (BTK) inhibitors are highly effective for the treatment of chronic lymphocytic leukemia (CLL).(1) These agents block signalling by inhibiting BTK, a key kinase in the B-cell receptor signalling pathway.”
Rozkiewicz, D., Hermanowicz, J. M., Kwiatkowska, I., Krupa, A., & Pawlak, D. (2023) · Molecules · doi:10.3390/molecules28052400 · Cited by 110 · see citing works
B cell checkpoints in autoimmune rheumatic diseases
Rubin, S. J. S., Bloom, M. S., & Robinson, W. H. (2019) · Nature Reviews Rheumatology · doi:10.1038/s41584-019-0211-0 · Cited by 107 · see citing works
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Bleeding by Bruton Tyrosine Kinase-Inhibitors: Dependency on Drug Type and Disease
von Hundelshausen, P., & Siess, W. (2021) · Cancers · doi:10.3390/cancers13051103 · Cited by 100 · see citing works
“Bruton’s tyrosine kinase (Btk), a non-receptor cytoplasmic tyrosine kinase expressed in pre-B cells and B-lymphocytes, plays a central role in B-cell receptor (BCR) signaling, and is crucial for B cell development and proliferation [1].”
BackgroundIbrutinib Resistance Mechanisms and Treatment Strategies for B-Cell Lymphomas
George, B., Chowdhury, S. M., Hart, A., Sircar, A., Singh, S. K., Nath, U. K., Mamgain, M., Singhal, N. K., Sehgal, L., & Jain, N. K. (2020) · Cancers · doi:10.3390/cancers12051328 · Cited by 96 · see citing works
CXCR4 in Waldenström’s Macroglobulinema: chances and challenges
Kaiser, L., Hunter, Z. R., Treon, S. P., & Buske, C. (2020) · Leukemia · doi:10.1038/s41375-020-01102-3 · Cited by 96 · see citing works
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Current Understanding of Immune Thrombocytopenia: A Review of Pathogenesis and Treatment Options
Mititelu, A., Onisâi, M., Roşca, A. E., & Vlădăreanu, A. M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042163 · Cited by 92 · see citing works
“Both Syk and BTK contribute to B-cell receptor signaling and could affect antibody production [92].”
BackgroundThe Trinity of cGAS, TLR9, and ALRs Guardians of the Cellular Galaxy Against Host-Derived Self-DNA
Kumar, V. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.624597 · Cited by 93 · see citing works
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“To a solution of 3-(4-phenoxyphenyl)-1-(4-piperidyl)pyrazolo[3,4-d] -pyrimidin-4-amine (1) (7.”
BackgroundMethodInfluentialvon Hundelshausen, P., Lorenz, R. L., Siess, W., & Weber, C. (2021) · Thrombosis and Haemostasis · doi:10.1055/a-1481-3039 · Cited by 88 · 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
Mechanisms of resistance to tyrosine kinase inhibitor‐targeted therapy and overcoming strategies
Ou, X., Gao, G., Habaz, I. A., & Wang, Y. (2024) · MedComm · doi:10.1002/mco2.694 · Cited by 93 · see citing works
Bruton’s Tyrosine Kinase Inhibition Promotes Myelin Repair
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“Our data complement preclinical and clinical findings with BTKi, which have been shown to affect B cell proliferation and survival (for review see [24, 25]).”
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Targeting Bruton’s Tyrosine Kinase in Inflammatory and Autoimmune Pathologies
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“In treatment of B cell malignancies, such combinational or sequential therapeutic strategies are often focused on combinations with other inhibitors acting on B cells [e.g., idelalisib targeting phosphoinositide 3-kinase (PI3K; de Rooij et al., 2015; Pal Singh et al., 2018)].”
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Systematic Review of Available CAR-T Cell Trials around the World
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Review of the development of BTK inhibitors in overcoming the clinical limitations of ibrutinib
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Structure-Function Relationships of Covalent and Non-Covalent BTK Inhibitors
Zain, R., & Vihinen, M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.694853 · Cited by 74 · see citing works
Recent Advances of Pyridinone in Medicinal Chemistry
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Nastoupil, L. J., Lunning, M. A., Vose, J. M., Schreeder, M. T., Siddiqi, T., Flowers, C. R., Cohen, J. B., Burger, J. A., Wierda, W. G., O'Brien, S. M., et al. (2019) · The Lancet Haematology · doi:10.1016/s2352-3026(18)30216-3 · Cited by 70 · see citing works
Systemic lupus erythematosus-complicating immune thrombocytopenia: From pathogenesis to treatment
Jiang, Y., Cheng, Y., Ma, S., Li, T., Chen, Z., Zuo, X., & Zhang, X. (2022) · Journal of Autoimmunity · doi:10.1016/j.jaut.2022.102887 · Cited by 73 · see citing works
Protein kinase inhibitors’ classification using K-Nearest neighbor algorithm
Arian, R., Hariri, A., Mehridehnavi, A., Fassihi, A., & Ghasemi, F. (2020) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2020.107269 · Cited by 68 · see citing works
NLRP3 Inflammasome/Pyroptosis: A Key Driving Force in Diabetic Cardiomyopathy
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“Bruton’s tyrosine kinase (BTK), a key receptor in B cell signal transduction, usually play a crucial part in the genesis of hematological tumors [93].”
BackgroundHeukels, P., van Hulst, J. A. C., van Nimwegen, M., Boorsma, C. E., Melgert, B. N., von der Thüsen, J. H., van den Blink, B., Hoek, R. A. S., Miedema, J., Neys, S. F. H., et al. (2019) · Respiratory Research · doi:10.1186/s12931-019-1195-7 · Cited by 67 · see citing works
“However, the interpretation of this finding is complicated, because ibrutinib is shown to have off-target effects and BTK is also expressed in myeloid lineages [37, 38].”
BackgroundSelf-citationTargeting Gatekeeper Mutations for Kinase Drug Discovery
Zhou, Y., Xiang, S., Yang, F., & Lu, X. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01361 · Cited by 68 · see citing works
Bat genomes illuminate adaptations to viral tolerance and disease resistance
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Medicinal Chemistry Strategies for the Development of Kinase Inhibitors Targeting Point Mutations
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Monitoring and Managing BTK Inhibitor Treatment-Related Adverse Events in Clinical Practice
O'Brien, S. M., Brown, J. R., Byrd, J. C., Furman, R. R., Ghia, P., Sharman, J. P., & Wierda, W. G. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.720704 · Cited by 66 · see citing works
Switch-like activation of Bruton’s tyrosine kinase by membrane-mediated dimerization
Chung, J. K., Nocka, L. M., Decker, A., Wang, Q., Kadlecek, T. A., Weiss, A., Kuriyan, J., & Groves, J. T. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819309116 · Cited by 64 · see citing works
“These findings could further our understanding of how to specifically target Btk in the context of diseases such as chronic lymphocytic leukemia (21, 23).”
BackgroundBtk Inhibitors: A Medicinal Chemistry and Drug Delivery Perspective
Brullo, C., Villa, C., Tasso, B., Russo, E., & Spallarossa, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147641 · Cited by 64 · see citing works
“Simultaneously, Btk could activate Akt/NfkB signaling pathways [15,16].”
BackgroundFurman, R. R., Byrd, J. C., Owen, R. G., O'Brien, S. M., Brown, J. R., Hillmen, P., Stephens, D. M., Chernyukhin, N., Lezhava, T., Hamdy, A., et al. (2021) · Leukemia · doi:10.1038/s41375-021-01252-y · Cited by 62 · see citing works
“Children with XLA demonstrate a phenotype of B-cell depletion and frequent infection without the other toxicities observed with ibrutinib [5], suggesting that the latter may be due to off-target effects [2, 12].”
BackgroundPost-translational Modifications of IκBα: The State of the Art
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Harnessing the cyclization strategy for new drug discovery
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Stepping forward: T-cell redirecting bispecific antibodies in cancer therapy
Qin, X., Ning, W., Liu, H., Liu, X., Luo, W., & Xia, N. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.03.027 · Cited by 59 · see citing works
“Bruton tyrosine kinase inhibitors are the preferred therapeutic agents for patients with chronic lymphocytic leukemia (CLL) 168,169 .”
BackgroundDevelopment of BTK inhibitors for the treatment of B-cell malignancies
Kim, H.-O. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01124-1 · Cited by 58 · see citing works
Flinsenberg, T. W. H., Tromedjo, C. C., Hu, N., Liu, Y., Guo, Y., Thia, K. Y. T., Noori, T., Song, X., Aw Yeang, H. X., Tantalo, D. G., et al. (2020) · Haematologica · doi:10.3324/haematol.2019.220590 · Cited by 56 · see citing works
“Ibrutinib, the first clinically approved Bruton’s tyrosine kinase (BTK) inhibitor, is an effective and widely used therapy for chronic lymphocytic leukemia (CLL).(1) The significant homology between BTK and IL-2-inducible kinase (ITK) makes ITK an off-target kinase inhibited by ibrutinib.”
BackgroundNeutrophils and NETs in kidney disease
Nakazawa, D., Masuda, S., Nishibata, Y., Watanabe‐Kusunoki, K., Tomaru, U., & Ishizu, A. (2025) · Nature Reviews Nephrology · doi:10.1038/s41581-025-00944-3 · Cited by 66 · see citing works
“BTK is an enzyme expressed in leukocytes other than T and plasma cells and is involved in signal transduction mediated by the B cell receptor and FcγRs 190,191 .”
A Fast and Clean BTK Inhibitor
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Targeting Protein Kinases Degradation by PROTACs
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Clinical immunotherapy in pancreatic cancer
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An update of new small-molecule anticancer drugs approved from 2015 to 2020
Liang, X., Wu, P., Yang, Q., Xie, Y., He, C., Yin, L., Yin, Z., Yue, G., Zou, Y., Li, L., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113473 · Cited by 53 · see citing works
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Degraders upgraded: the rise of PROTACs in hematological malignancies
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Efficacy and safety of ibrutinib in diffuse large B-cell lymphoma: A single-arm meta-analysis
Hou, K., Yu, Z., Jia, Y., Fang, H., Shao, S., Huang, L., & Feng, Y. (2020) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2020.103010 · Cited by 51 · see citing works
Emerging therapies in mantle cell lymphoma
Hanel, W. G., & Epperla, N. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00914-1 · Cited by 50 · see citing works
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“Additional studies have shown that PMIBCR/Abl-R6 is not toxic in LK-Ph(-) cell lines, does not affect target expression, and is able to promote the degradation of different isoforms of the Bcr/Abl protein and even some mutant forms that confer imatinib resistance, which is accompanied by increases in p53 levels [74,75…”
BackgroundInfluentialPathogenesis and Treatment of Myeloma-Related Bone Disease
Gau, Y.-C., Yeh, T.-J., Hsu, C.-M., Hsiao, S. Y., & Hsiao, H.-H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063112 · Cited by 48 · see citing works
“Bruton’s tyrosine kinase (BTK) is a nonreceptor tyrosine kinase of the TEC family and plays a crucial role in oncogenic signaling that is critical for the proliferation and survival of leukemic cells in many B cell malignancies and osteoclast differentiation [35,36].”
BackgroundGarg, N., Padron, E., Rammohan, K. W., & Goodman, C. F. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11206139 · Cited by 52 · see citing works
The synthesis review of the approved tyrosine kinase inhibitors for anticancer therapy in 2015–2020
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Ibrutinib in the Treatment of Solid Tumors: Current State of Knowledge and Future Directions
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SLC7A11, a Potential Therapeutic Target Through Induced Ferroptosis in Colon Adenocarcinoma
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The impact of E3 ligase choice on PROTAC effectiveness in protein kinase degradation
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“Similar to IP3, DAG can act as a second messenger and activate protein kinase C (PKC) and, together with Syk, engage the mitogen-activated protein kinase (MAPK) pathway and increase survival and accelerate proliferation [47, 49, 50].”
BackgroundOpat, S., Tedeschi, A., Hu, B., Linton, K., McKay, P., Leitch, S., Coleman, M., Zinzani, P. L., Jin, J., Sun, M. Y., et al. (2023) · Blood Advances · doi:10.1182/bloodadvances.2023010668 · Cited by 45 · see citing works
“4 This led to the development and approval of the fi rst BTK inhibitor, ibru-tinib, which changed the treatment landscape for indolent B-cell malignancies.”
BackgroundDuarte, 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
“Here, allosteric inhibition of Btk in Fc receptor (FcRs) signaling in basophils and mast cells could provide potential therapeutic benefits (Pal Singh et al., 2018).”
BackgroundNadeem, A., Ahmad, S. F., Al-Harbi, N. O., Ibrahim, K. E., Alqahtani, F., Alanazi, W. A., Mahmood, H. M., Alsanea, S., & Attia, S. M. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.107123 · Cited by 45 · see citing works
Differential impact of BTK active site inhibitors on the conformational state of full-length BTK
Joseph, R. E., Amatya, N., Fulton, D. B., Engen, J. R., Wales, T. E., & Andreotti, A. H. (2020) · eLife · doi:10.7554/elife.60470 · Cited by 46 · see citing works
- Authors
- Pal Singh, S., Dammeijer, F., & Hendriks, R. W.
- Affiliations
- Erasmus MC (NL)
- Corresponding author
- Hendriks, Rudi W.
- Venue
- Molecular Cancer
- Published
- 2018-02-19
- Volume
- 17
- Issue
- 1
- Pages
- 57-57
- ISSN
- 1476-4598 (ISSN-L)
- PMC
- PMC5817726
- OpenAlex
- W2791299132
- Cited by
- 726
- References
- 272
- Citations by year
- 2026: 62 · 2025: 89 · 2024: 123 · 2023: 104 · 2022: 127 · 2021: 100 · 2020: 67 · 2019: 45 · 2018: 9
- FWCI
- 8.03
- Type
- journal article
- Language
- en
- Update notices
- correction (2019-04-03)
- Open access
- gold
- doi.org
- Locations
- Molecular Cancer (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (publishedVersion, other-oa)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion, other-oa)
- RePub (Erasmus University Rotterdam) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- ZonMw
- Topics
- Health Sciences › Medicine › Genetics › Chronic Lymphocytic Leukemia Research
- Health Sciences › Medicine › Pathology and Forensic Medicine › Lymphoma Diagnosis and Treatment
- Life Sciences › Immunology and Microbiology › Immunology › Immunodeficiency and Autoimmune Disorders
- Keywords
- Bruton's tyrosine kinase, B-cell malignancies, ibrutinib, chronic lymphocytic leukemia, mantle cell lymphoma, B cell receptor signaling, X-linked agammaglobulinemia, B cell differentiation, BTK inhibitors, tumor microenvironment, myeloid cells, drug resistance, combination therapy, solid tumors
- MeSH terms
- Agammaglobulinaemia Tyrosine Kinase, Animals, Antineoplastic Combined Chemotherapy Protocols, B-Lymphocytes, Bone Marrow, Cell Differentiation, Cell Transformation, Neoplastic, Humans, Receptors, Antigen, B-Cell, Biomarkers, Tumor, Signal Transduction, Leukemia, B-Cell, Gene Expression Regulation, Neoplastic, Lymphoma, B-Cell, Treatment Outcome, Lymphopoiesis, Protein Kinase Inhibitors, Molecular Targeted Therapy, Tumor Microenvironment
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