References
- Cohen P, Cross D, Jänne PA. Kinase drug discovery 20 years after imatinib: progress and future directions. Nat Rev Drug Discov. 2021;20(7):551–569. doi: 10.1038/s41573-021-00195-4
- Cohen P. Protein kinases-the major drug targets of the twenty-first century? Nat Rev Drug Discov. 2002;1(4):309–315. doi: 10.1038/nrd773
- Levitzki A. Protein kinase inhibitors as a therapeutic modality. Acc Chem Res. 2003;36(6):462–469. doi: 10.1021/ar0201207
- Cohen P. The origins of protein phosphorylation. Nat Cell Biol. 2002;4(5):E127–E130. doi: 10.1038/ncb0502-e127
- Manning G, Whyte DB, Martinez R, et al. The protein kinase complement of the human genome. Science. 2002;298(5600):1912–1934. doi: 10.1126/science.1075762
- Kanev GK, de Graaf C, de Esch IJP, et al. The landscape of atypical and eukaryotic protein kinases. Trend Pharm Sci. 2019;40(11):818–832. doi: 10.1016/j.tips.2019.09.002
- Attwood MM, Fabbro D, Sokolov AV, et al. Trends in kinase drug discovery: targets, indications and inhibitor design. Nat Rev Drug Discov. 2021;20(11):839–861. doi: 10.1038/s41573-021-00252-y
- Roskoski R. Classification of small molecule protein kinase inhibitors based upon the structures of their drug-enzyme complexes. Pharmacol Res. 2016;103:26–48. doi: 10.1016/j.phrs.2015.10.021
- Castelo-Soccio L, Kim H, Gadina M, et al. Protein kinases: drug targets for immunological disorders. Nat Rev Immunol. 2023;23(12):787–806. doi: 10.1038/s41577-023-00877-7
- Roskoski R. Jr. Properties of FDA-approved small molecule protein kinase inhibitors: a 2023 update. Pharmacol Res. 2023;187:106552. doi: 10.1016/j.phrs.2022.106552
- Fabbro D, Cowan-Jacob SW, Moebitz H. Ten things you should know about protein kinases: IUPHAR R eview 14. British J Pharmacol. 2015;172(11):2675–2700. doi: 10.1111/bph.13096
- Fedorov O, Müller S, Knapp S. The (un)targeted cancer kinome. Nat Chem Biol. 2010;6(3):166–169. doi: 10.1038/nchembio.297
- Roskoski R. A historical overview of protein kinases and their targeted small molecule inhibitors. Pharmacol Res. 2015;100:1–23. doi: 10.1016/j.phrs.2015.07.010
- FDA approves everolimus for tuberous sclerosis complex-associated partial-onset seizures. FDA gov. [cited 2023 Oct 11]. Available from: https://www.fda.gov/drugs/resources-informationapproved-drugs/fda-approves-everolimus-tuberoussclerosis-complex-associated-partial-onset-seizures
- McCormack PL. Nintedanib: first global approval. Drugs. 2015;75(1):129–139. doi: 10.1007/s40265-014-0335-0
- Kasamon YL, Ko C-Y, Subramaniam S, et al. FDA approval summary: midostaurin for the treatment of advanced systemic mastocytosis. The Oncologist. 2018;23(12):1511–1519. doi: 10.1634/theoncologist.2018-0222
- Hoy SM. Netarsudil ophthalmic solution 0.02%: first global approval. Drugs. 2018;78(3):389–396. doi: 10.1007/s40265-018-0877-7
- Dimiter D, Chuan C, Zehus S, Yael M. Anaplastic lymphoma kinase antibodies and methods of use thereof. WO2023147292A2.
- Morris SW, Kirstein MN, Valentine MB, et al. Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin’s lymphoma. Science. 1994;263(5151):1281–1284. doi: 10.1126/science.8122112
- Shiota M, Fujimoto J, Semba T, et al. Hyperphosphorylation of a novel 80 kDa protein-tyrosine kinase similar to Ltk in a human Ki-1 lymphoma cell line, AMS3. Oncogene. 1994;9(6):1567–1574.
- Iwahara T, Fujimoto J, Wen D, et al. Molecular characterization of ALK, a receptor tyrosine kinase expressed specifically in the nervous system. Oncogene. 1997;14(4):439–449. doi: 10.1038/sj.onc.1200849
- Morris SW, Naeve C, Mathew P, et al. ALK, the chromosome 2 gene locus altered by the t(2;5) in non-Hodgkin’s lymphoma, encodes a novel neural receptor tyrosine kinase that is highly related to leukocyte tyrosine kinase (LTK). Oncogene. 1997;14(18):2175–2188. doi: 10.1038/sj.onc.1201062
- Lorén CE, Scully A, Grabbe C, et al. Identification and characterization of DAlk: a novel drosophila melanogaster RTK which drives ERK activation in vivo. Genes Cells. 2001;6(6):531–544. doi: 10.1046/j.1365-2443.2001.00440.x
- U.S. Food and Drug Administration Approves Pfizer’s XALKORI® (crizotinib) as First and Only Therapy Specifically for Patients with Locally Advanced or Metastatic ALK-Positive Non-Small Cell Lung Cancer | Pfizer. 2024 Feb 21. https://www.pfizer.com/und/news/press-release/press-release-detail/u_s_food_and_drug_administration_approves_pfizer_s_xalkori_crizotinib_as_first_and_only_therapy_specifically_for_patients_with_locally_advanced_or_metastatic_alk_positive_non_small_cell_lung_cancer
- FDA D.I.S.C.O.: Two approvals for ALK-positive non-small cell lung cancer. [cited 2024 Feb 21]. Available from: https://www.fda.gov/drugs/resources-information-approved-drugs/fda-disco-two-approvals-alk-positive-non-small-cell-lung-cancer
- Alectinib approved for (ALK) positive metastatic non-small cell lung cancer (NSCLC) | FDA. 2024 Feb 21.
- Brigatinib. [cited 2024 Feb 21]. Available from: https://www.fda.gov/drugs/resources-information-approved-drugs/brigatinib
- FDA approves lorlatinib for second- or third-line treatment of ALK-positive metastatic NSCLC | FDA. 2024 Feb 21.
- Hartmut D, Alfred E, Frank K, et al. Novel anti-thymidine kinase antibodies. WO2019201901A1. 2019.
- Kipps TJ, Widhopf II. Anti-related-to-receptor-tyrosine-kinase (RYK) antibodies and uses thereof. WO2023023600A1.
- Hovens CM, Stacker SA, Andres AC, et al. RYK, a receptor tyrosine kinase-related molecule with unusual kinase domain motifs. Proc Natl Acad Sci, USA. 1992;89(24):11818–11822. doi: 10.1073/pnas.89.24.11818
- Halford MM, Stacker SA. Revelations of the RYK receptor. BioEssays. 2001;23(1):34–45. doi: 10.1002/1521-1878(200101)23:1<34:AID-BIES1005>3.0.CO;2-D
- Hollis ER, Ishiko N, Yu T, et al. Ryk controls remapping of motor cortex during functional recovery after spinal cord injury. Nat Neurosci. 2016;19(5):697–705. doi: 10.1038/nn.4282
- Fu Y, Chen Y, Huang J, et al. RYK, a receptor of noncanonical Wnt ligand Wnt5a, is positively correlated with gastric cancer tumorigenesis and potential of liver metastasis. Am J Physiol Gastrointest Liver Physiol. 2020;318(2):G352–G360. doi: 10.1152/ajpgi.00228.2019
- Costa A, Amin R, Bailey J, et al. Antibodies and chimeric antigen receptors specific for receptor tyrosine kinase like orphan receptor 1 (ROR1). WO2020160050A1. 2020.
- Shabani M, Naseri J, Shokri F. Receptor tyrosine kinase-like orphan receptor 1: a novel target for cancer immunotherapy. Expert Opin Ther Targets. 2015;19(7):941–955. doi: 10.1517/14728222.2015.1025753
- Laquerre S, Lorenzi M, Moores S. Combination therapies with bispecific anti-egfr/c-met antibodies and third generation egfr tyrosine kinase inhibitors. WO2020230091A1.
- Leonhardt H, Stengl A, Roas M, et al. Novel flt3 antibodies and antibody-drug-conjugates based thereon, therapeutic methods and uses thereof in combination with tyrosine kinase inhibitors. WO2023105087A1.
- Chew S, Mackey MC, Jabbour E. Gilteritinib in the treatment of relapsed and refractory acute myeloid leukemia with a FLT3 mutation. Ther Adv Hematol. 2020;11:2040620720930614. doi: 10.1177/2040620720930614
- Perl AE, Martinelli G, Cortes JE, et al. Gilteritinib or chemotherapy for relapsed or refractory FLT3-mutated AML. N Engl J Med. 2019;381(18):1728–1740. doi: 10.1056/NEJMoa1902688
- FDA approves gilteritinib for relapsed or refractory acute myeloid leukemia (AML) with a FLT3 mutation. 2023 Oct 11. Available from: https://www.fda.gov/drugs/fda-approves-gilteritinib-relapsed-or-refractory-acute-myeloid-leukemia-aml-flt3-mutation
- FDA approves quizartinib for newly diagnosed acute myeloid leukemia. 2023 Oct 11. Available from: https://www.fda.gov/drugs/drug-approvals-and-databases/fda-approves-quizartinib-newly-diagnosed-acute-myeloid-leukemia
- Metzelder S, Wang Y, Wollmer E, et al. Compassionate use of sorafenib in FLT3-ITD-positive acute myeloid leukemia: sustained regression before and after allogeneic stem cell transplantation. Blood. 2009;113(26):6567–6571. doi: 10.1182/blood-2009-03-208298
- Zhang W, Konopleva M, Shi Y-X, et al. Mutant FLT3: a direct target of sorafenib in acute myelogenous leukemia. J Natl Cancer Inst. 2008;100(3):184–198. doi: 10.1093/jnci/djm328
- Smith CC, Wang Q, Chin C-S, et al. Validation of ITD mutations in FLT3 as a therapeutic target in human acute myeloid leukaemia. Nature. 2012;485(7397):260–263. doi: 10.1038/nature11016
- Zhiwen F, Shijun L, Sifei H, et al. Antibody drug conjugate: the “biological missile” for targeted cancer therapy. Signal Transduct Target Ther. 2022;7(1):93. doi: 10.1038/s41392-022-00947-7
- Ermine K, Yu J, Zhang L. Role of receptor interacting protein (RIP) kinases in cancer. Genes Dis. 2021;9(6):1579–1593. doi: 10.1016/j.gendis.2021.10.007
- Zhang D, Lin J, Han J. Receptor-interacting protein (RIP) kinase family. Cell Mol Immunol. 2010;7(4):243–249. doi: 10.1038/cmi.2010.10
- Estrada AA, Feng JA, Fox B, et al. Compounds, compositions and methods. WO2017136727A2.
- Schnyder S, Caminis J, Florian P, et al. Eclitasertib for use in treating conditions involving systemic hyperinflammatory response. WO2021211919A1.
- Guo J, Cheng B, Chen H, et al. Novel protein kinase inhibitors. WO2021216440A1.
- Burger JA. Bruton tyrosine kinase inhibitors: present and future. Cancer J. 2019;25(6):386–393. doi: 10.1097/PPO.0000000000000412
- Wen T, Wang J, Shi Y, et al. Inhibitors targeting Bruton’s tyrosine kinase in cancers: drug development advances. Leukemia. 2021;35(2):312–332. doi: 10.1038/s41375-020-01072-6
- McDonald C, Xanthopoulos C, Kostareli E. The role of Bruton’s tyrosine kinase in the immune system and disease. Immunology. 2021;164(4):722–736. doi: 10.1111/imm.13416
- Brullo C, Villa C, Tasso B, et al. Btk inhibitors: a medicinal chemistry and drug delivery perspective. Int J Mol Sci. 2021;22(14):7641. doi: 10.3390/ijms22147641
- Jain M, Chatterjee A, Mohapatra J, et al. A novel Bruton’s tyrosine kinase (BTK) inhibitor with anticancer and antiinflammatory activities. Eur J Canc. 2015;51:S63. doi: 10.1016/S0959-8049(16)30191-5
- Molina-Cerrillo J, Alonso-Gordoa T, Gajate P, et al. Bruton’s tyrosine kinase (BTK) as a promising target in solid tumors. Canc Treat Rev. 2017;58:41. doi: 10.1016/j.ctrv.2017.06.001
- De CS, Kurian J, Dufresne C, et al. Covalent inhibitors design and discovery. Eur J Med Chem. 2017;138:96–114. doi: 10.1016/j.ejmech.2017.06.019
- Barf T, Kaptein A. Irreversible protein kinase inhibitors: balancing the benefits and risks. J Med Chem. 2012;55(14):6243–6262. doi: 10.1021/jm3003203
- Update on IMBRUVICA® (ibrutinib) U.S. Accelerated Approvals for Mantle Cell Lymphoma and Marginal Zone Lymphoma Indications. 2024 Feb 21. Available from: https://www.jnj.com/media-center/press-releases/update-on-imbruvica-ibrutinib-u-s-accelerated-approvals-for-mantle-cell-lymphoma-and-marginal-zone-lymphoma-indications
- Edward R, Scheffer C, Talal H, et al. Complicated regulatory decision-making following inconsistent trial results: the issue with ibrutinib for mantle cell lymphoma. Nat Rev Clin Oncol. 2024;1(1):1–2. doi: 10.1038/s41571-023-00821-7
- Project Orbis: FDA approves acalabrutinib for CLL and SLL. 2024 Feb 21. Available from: https://www.fda.gov/drugs/resources-information-approved-drugs/project-orbis-fda-approves-acalabrutinib-cll-and-sll
- FDA D.I.S.C.O. Burst Edition: FDA approvals of Brukinsa (zanubrutinib), for adult patients with relapsed or refractory marginal zone lymphoma, and Exkivity (mobocertinib) for adult patients with locally advanced or metastatic non-small cell lung cancer with epidermal growth factor receptor exon 20 insertion mutations. 2024 Feb 21. Available from: https://www.fda.gov/drugs/resources-information-approved-drugs/fda-disco-burst-edition-fda-approvals-brukinsa-zanubrutinib-adult-patients-relapsed-or-refractory
- Coburn CA, Kumar DV, Buzard DJ, et al. Kinase inhibitors. WO2021247748 A1.
- Liang C, Tian D, Ren X, et al. The development of Bruton’s tyrosine kinase (BTK) inhibitors from 2012 to 2017: A mini-review. Eur J Med Chem. 2018;151:315–326. doi: 10.1016/j.ejmech.2018.03.062
- Mainolfi N, Ji N, Weiss MM, et al. Irak degraders and uses thereof. WO2020264490. A1.
- Flannery S, Bowie AG. The interleukin-1 receptor-associated kinases: critical regulators of innate immune signalling. Biochem Pharmacol. 2010;80(12):1981–1991. doi: 10.1016/j.bcp.2010.06.020
- Jain A, Kaczanowska S, Davila E. IL-1 receptor-associated kinase signaling and its role in inflammation, cancer progression, and therapy resistance. Front Immunol. 2014;5:553. doi: 10.3389/fimmu.2014.00553
- Janssens S, Beyaert R. Functional diversity and regulation of different interleukin-1 receptor-associated kinase (IRAK) family members. Mol Cell. 2003;11(2):293–302. doi: 10.1016/S1097-2765(03)00053-4
- Zhang J, Wang J, Li Y, et al. A patent perspective of antiangiogenic agents. Expert Opin Ther Pat. 2023;12(12):821–840. doi: 10.1080/13543776.2023.2294808
- Linjie L, Yu G, Yang L, et al. An updated patent review of AKT inhibitors (2020 – present). Expert Opin Ther Pat. 2023;9(9):549–564. doi: 10.1080/13543776.2023.2273895
- Jaworski C, Iliev P, Wängler C, et al. Type I inhibitors of tropomyosin receptor kinase (Trk): a 2020–2022 patent update. Expert Opin Ther Pat. 2023;33(7–8):503–521. doi: 10.1080/13543776.2023.2262136
- Takayuki I, Masaaki S. CDC7 kinase inhibitors: a survey of recent patent literature (2017–2022). Expert Opin Ther Pat. 2023;33(7–8):493–501. doi: 10.1080/13543776.2023.2262138
- Pengyun L, Bingkun L, Ning Y, et al. The next generation of EGFR inhibitors: a patenting perspective of PROTACs based EGFR degraders. Expert Opin Ther Pat. 2023;33(7–8):477–492. doi: 10.1080/13543776.2023.2262176
- Yadav V, Sharma AK, Parashar G, et al. Patent landscape highlighting therapeutic implications of peptides targeting myristoylated alanine-rich protein kinase-C substrate (MARCKS). Expert Opin Ther Pat. 2023;33(6):445–454. doi: 10.1080/13543776.2023.2240020
- Ashwell JD. The many paths to p38 mitogen-activated protein kinase activation in the immune system. Nature Rev Immunol. 2006;6(7):532–540. doi: 10.1038/nri1865
- Boni LT, Rando RR. The nature of protein kinase C activation by physically defined phospholipid vesicles and diacylglycerols. J Biol Chem. 1985;260(19):10819–10825. doi: 10.1016/S0021-9258(19)85156-6
- Hardie DG. Regulation of AMP-activated protein kinase by natural and synthetic activators. Acta Pharm Sin B. 2016;6(1):1–19. doi: 10.1016/j.apsb.2015.06.002
- Steinberg GR, Carling D. AMP-activated protein kinase: the current landscape for drug development. Nature Rev Drug Discov. 2019;18(7):527–551. doi: 10.1038/s41573-019-0019-2
- Sadowsky JD, Burlingame MA, Wolan DW, et al. Turning a protein kinase on or off from a single allosteric site via disulfide trapping. Proc Natl Acad Sci USA. 2011;108(15):6056–6061. doi: 10.1073/pnas.1102376108
- Feng D, Biftu T, Romero FA, et al. Discovery of MK-8722: a systemic, direct pan-activator of AMP-Activated protein kinase. ACS Med Chem Lett. 2018;9(1):39–44. doi: 10.1021/acsmedchemlett.7b00417
- Peerzada MN, Hamel E, Bai R, et al. Deciphering the key heterocyclic scaffolds in targeting microtubules, kinases and carbonic anhydrases for cancer drug development. Pharmacol Ther. 2021;225:107860. doi: 10.1016/j.pharmthera.2021.107860
- Ismail RSM, El Kerdawy AM, et al. Discovery of a new potent oxindole multi-kinase inhibitor among a series of designed 3-alkenyl-oxindoles with ancillary carbonic anhydrase inhibitory activity as antiproliferative agents. BMC Chem. 2023;17(1):81. doi: 10.1186/s13065-023-00994-3
- Elsawi AE, Elbadawi MM, Nocentini A, et al. 1,5-diaryl-1,2,4-triazole ureas as new SLC-0111 analogues endowed with dual carbonic anhydrase and VEGFR-2 inhibitory activities. J Med Chem. 2023;66(15):10558–10578. doi: 10.1021/acs.jmedchem.3c00721
- Benito G, D’Agostino I, Carradori S, et al. Erlotinib-containing benzenesulfonamides as anti-Helicobacter pylori agents through carbonic anhydrase inhibition. Fut Med Chem. 2023;20(20):1865–1883. doi: 10.4155/fmc-2023-0208