Cited by 1,369Protein Kinase Regulation and GTPase SignalingPI3K/AKT/mTOR signaling in cancerCancer Mechanisms and Therapy

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The specificities of protein kinase inhibitors: an update

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BAIN, Jenny, McLAUCHLAN, Hilary, ELLIOTT, Matthew, COHEN, Philip·2003·Biochemical Journal

DOI 10.1042/bj20021535PMC PMC1223271

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Abstract

We have previously examined the specificities of 28 commercially available compounds, reported to be relatively selective inhibitors of particular serine/threonine-specific protein kinases [Davies, Reddy, Caivano and Cohen (2000) Biochem. J. 351, 95—105]. In the present study, we have extended this analysis to a further 14 compounds. Of these, indirubin-3′-monoxime, SP 600125, KT 5823 and ML-9 were found to inhibit a number of protein kinases and conclusions drawn from their use in cell-based assays are likely to be erroneous. Kenpaullone, Alsterpaullone, Purvalanol, Roscovitine, pyrazolopyrimidine 1 (PP1), PP2 and ML-7 were more specific, but still inhibited two or more protein kinases with similar potency. Our results suggest that the combined use of Roscovitine and Kenpaullone may be useful for identifying substrates and physiological roles of cyclin-dependent protein kinases, whereas the combined use of Kenpaullone and LiCl may be useful for identifying substrates and physiological roles of glycogen synthase kinase 3. The combined use of SU 6656 and either PP1 or PP2 may be useful for identifying substrates of Src family members. Epigallocatechin 3-gallate, one of the main polyphenolic constituents of tea, inhibited two of the 28 protein kinases in the panel, dual-specificity, tyrosine-phosphorylated and regulated kinase 1A (DYRK1A; IC50 = 0.33μM) and p38-regulated/activated kinase (PRAK; IC50 = 1.0μM).

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System-based drug discovery within the human kinome
Bamborough, P. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.724056 · Cited by 33
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Background
Focal adhesion and actin organization by a cross-talk of TM4SF5 with integrin α2 are regulated by serum treatment
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Background
Synthesis and Properties of a Selective Inhibitor of Homeodomain–Interacting Protein Kinase 2 (HIPK2)
Cozza, G., Zanin, S., Determann, R., Ruzzene, M., Kunick, C., & Pinna, L. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089176 · Cited by 33
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Background
Regulation of contractility by Hsp27 and Hic-5 in rat mesenteric small arteries
Srinivasan, R., Forman, S., Quinlan, R. A., Ohanian, J., & Ohanian, V. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00939.2007 · Cited by 33
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Background
Quantitative Imaging of Epithelial Cell Scattering Identifies Specific Inhibitors of Cell Motility and Cell-Cell Dissociation
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c‐jun N‐terminal kinase hyperphosphorylates R406W tau at the PHF‐1 site during mitosis
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“Although SP600125 has been reported to inhibit not only JNK but also several other Ser396 kinases, such as GSK-3β, cdk2, and casein kinase 1 in vitro (44), JNK may be the most probable candidate for the endogenous Ser396 kinase in COS7 cells.”
Background
Contrasting Roles of Mitogen-Activated Protein Kinases in Cellular Entry and Replication of Hepatitis C Virus: MKNK1 Facilitates Cell Entry
Kim, S., Ishida, H., Yamane, D., Yi, M., Swinney, D. C., Foung, S. K. H., & Lemon, S. M. (2013) · Journal of Virology · doi:10.1128/jvi.00954-12 · Cited by 32
“(57) reported that SP600125 inhibited 13 of 28”
Background
The Tumor Suppressor p53 Transcriptionally Regulates cGKI Expression during Neuronal Maturation and Is Required for cGMP-Dependent Growth Cone Collapse
Tedeschi, A., Nguyen, T. N., Steele, S. U., Feil, S. C., Naumann, U., Feil, R., & Giovanni, S. D. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4416-09.2009 · Cited by 32
“However, it is important to note that the efficiency and/or specificity of protein kinase inhibitors, including cGKI inhibitors, may be unpredictable and lower than expected in particular when administered to intact cells (Burkhardt et al., 2000; Bain et al., 2003, 2007; Valtcheva et al., 2009).”
Background
Transcriptional regulation of the growth-regulated oncogene α gene by early growth response protein-1 in response to tumor necrosis factor α stimulation
Shin, S. Y., Lee, J. M., Lim, Y., & Lee, Y. H. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.07.005 · Cited by 32
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“PP2 was developed as a specific inhibitor of the Src family of sTKs (4), but it also inhibits Bcr-Abl (53), which is an sTK, as well as Kit, (53) which is an RTK.”
Background
Genetics of melanoma
Wangari‐Talbot, J., & Chen, S. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2012.00330 · Cited by 34
“These two compounds however have pharmaceutical limitations such as off-target activities that prevent them from transitioning from the bench to the clinic (Bain et al., 2003; Knight and Shokat, 2007).”
Background
Effect of the myosin light chain kinase inhibitor ML-7 on the proteome of hearts subjected to ischemia–reperfusion injury
Lin, H., Cadete, V. J. J., Sawicka, J., Woźniak, M., & Sawicki, G. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.06.016 · Cited by 32
Validation of microarray data in human lymphoblasts shows a role of the ubiquitin-proteasome system and NF-kB in the pathogenesis of Down syndrome
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“Interestingly, the over-expression of DYRK1A can also be modulated by EGCG [111] and transgenic mice overexpressing this gene and presenting cognitive impairment, rescue the cognitive phenotype after a polyphenol-based diet [112].”
Background
Synthesis of aminopyrimidylindoles structurally related to meridianins
Rossignol, E., Youssef, A., Moreau, P., Prudhomme, M., & Anizon, F. (2007) · Tetrahedron · doi:10.1016/j.tet.2007.07.095 · Cited by 32
Protein kinase signaling cascades in CNS trauma
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Nogo-B is a new physiological substrate for MAPKAP-K2
Rousseau, S., Peggie, M. W., Campbell, D. G., Nebreda, Á. R., & Cohen, P. (2005) · Biochemical Journal · doi:10.1042/bj20050935 · Cited by 32
Self-citation
Nonredundant roles of Src-family kinases and Syk in the initiation of B-cell antigen receptor signaling
Stepanek, O., Draber, P., Drobek, A., Horejsi, V., & Brdicka, T. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202401 · Cited by 31
“The combination of genetic and chemical inhibitors did not block the antiBCR–induced response entirely, probably because of the partial inhibition of Csk kinase activity in LAT-Csk chimera by PP2 (52) (Supplemental Fig.”
Background
Characterization of a novel JNK (c-Jun N-terminal kinase) inhibitory peptide
Ngoei, K. R. W., Catimel, B., Church, N., Lio, D. S., Dogovski, C., Perugini, M. A., Watt, P. M., Cheng, H.-C., Ng, D. C. H., & Bogoyevitch, M. A. (2011) · Biochemical Journal · doi:10.1042/bj20101244 · Cited by 31
Role for mitogen-activated protein kinase p38α in lung epithelial branching morphogenesis
Liu, Y., Martinez, L. C., Ebine, K., & Abe, M. K. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2007.12.003 · Cited by 31
(R)-Roscovitine (CYC202, Seliciclib)
Galons, H., Bettayeb, K., & Meijer, L. (2006) · Enzyme inhibitors series/CRC enzyme inhibitors series · doi:10.1201/9781420005400.ch9 · Cited by 31
Multiscale analysis of single and double maternal-zygotic Myh9 and Myh10 mutants during mouse preimplantation development
Schliffka, M. F., Tortorelli, A. F., Özgüç, Ö., de Plater, L., Polzer, O., Pelzer, D., & Maître, J. (2021) · eLife · doi:10.7554/elife.68536 · Cited by 31
Discovery of potent and bioavailable GSK-3β inhibitors
Gong, L., Hirschfeld, D., Tan, Y.-C., Hogg, J. H., Peltz, G., Avnur, Z., & Dunten, P. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.01.038 · Cited by 31
Affinity Classification of Kinase Inhibitors by Mass Spectrometric Methods and Validation Using Standard IC50 Measurements
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Odin (ANKS1A) is a Src family kinase target in colorectal cancer cells
Emaduddin, M., Edelmann, M. J., Kessler, B. M., & Feller, S. M. (2008) · Cell Communication and Signaling · doi:10.1186/1478-811x-6-7 · Cited by 31
“Treatment of SW620 cells with the SFK inhibitor PP2 [24,25], but not compound solvent alone, greatly reduced the detectable tyrosine phosphorylation of Odin, indicating that Odin is a SFK substrate, or a substrate of another tyrosine kinase that is regulated by SFK (Figure 5).”
Influential
Platelets undergo phosphorylation of Syk at Y525/526 and Y352 in response to pathophysiological shear stress
Speich, H. E., Grgurevich, S., Kueter, T. J., Earhart, A. D., Slack, S. M., & Jennings, L. K. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.90644.2007 · Cited by 31
INHIBITION OF C-JUN N-TERMINAL KINASE AFTER HEMORRHAGE BUT BEFORE RESUSCITATION MITIGATES HEPATIC DAMAGE AND INFLAMMATORY RESPONSE IN MALE RATS
Relja, B., Schwestka, B., Lee, V. S.-Y., Henrich, D. M., Czerny, C., Borsello, T., Marzi, İ., & Lehnert, M. (2009) · Shock · doi:10.1097/shk.0b013e3181a2530d · Cited by 31
“D-JNKI-1 has therefore a fundamentally different mechanism to inhibit JNK as compared with the small chemical inhibitors, such as SP600125 and AS601245, which competitively target the ATP binding site not only of JNK but also of other kinases, and therefore concerns about their specificity have been raised (42, 43).”
Background
Development of Extracellular Signal-Regulated Kinase Inhibitors
Burkhard, K. A., Smith, S., Deshmukh, R. R., MacKerell, A. D., & Shapiro, P. (2009) · Current Topics in Medicinal Chemistry · doi:10.2174/156802609789044416 · Cited by 31
“In addition, because the ATP-binding domain is a relatively well-conserved region among many kinases, questions have been raised regarding the specificity achievable by targeting this domain [57–59].”
Background
Myosin light chain kinase‐independent inhibition by ML‐9 of murine TRPC6 channels expressed in HEK293 cells
Shi, J., Takahashi, S., Jin, X., Li, Y., Ito, Y., Mori, Y., & Inoue, R. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707368 · Cited by 31
“Firstly, neither wortmannin, a structurally different MLCK inhibitor (Davies et al., 2000; Bain et al., 2003) nor MLCKspecific inhibitory peptides (MLCK-IP11 19 and MLCKIP480 501) targeted to the catalytic and ATP binding domains of MLCK (Ikebe, 1990; Kemp et al., 1991), affected the extent of…”
Background
Synthesis and SAR of 1,9-dihydro-9-hydroxypyrazolo[3,4-b]quinolin-4-ones as novel, selective c-Jun N-terminal kinase inhibitors
Liu, M., Xin, Z., Clampit, J. E., Wang, S., Gum, R. J., Haasch, D. L., Trevillyan, J. M., Abad‐Zapatero, C., Fry, E. H., Sham, H. L., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.02.046 · Cited by 31
Antagonistic regulation of swelling-activated Cl−current in rabbit ventricle by Src and EGFR protein tyrosine kinases
Ren, Z., & Baumgarten, C. M. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00992.2004 · Cited by 31
“To exclude the possibility that a nonspecific effect of PP2 was responsible for stimulation of ICl,swell, we applied PP3, an inactive analog of PP2 (3, 46), in separate experiments.”
Contribution of BCR–ABL‐independent activation of ERK1/2 to acquired imatinib resistance in K562 chronic myeloid leukemia cells
Nambu, T., Araki, N., Nakagawa, A., Kuniyasu, A., Kawaguchi, T., Hamada, A., & Saito, H. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01365.x · Cited by 30
New Perspectives for the Rescue of Cognitive Disability in Down Syndrome
Bartesaghi, R., Haydar, T. F., Delabar, J. M., Dierssen, M., Martínez‐Cué, C., & Bianchi, D. W. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2775-15.2015 · Cited by 32
DNA damaging agent-induced apoptosis is regulated by MCL-1 phosphorylation and degradation mediated by the Noxa/MCL-1/CDK2 complex
Nakajima, W., Sharma, K., Lee, J. Y., Maxim, N. T., Hicks, M. A., Vu, T.-T., Luu, A., Yeudall, W. A., Tanaka, N., & Harada, H. (2016) · Oncotarget · doi:10.18632/oncotarget.9217 · Cited by 30
“Roscovitine has a broad specificity to inhibit CDKs and SP600125 was originally identified as a JNK inhibitor, but it non-specifically inhibits a variety of kinases including CDK2 [16].”
Background
Targeting Pim Kinases and DAPK3 to Control Hypertension
Carlson, D. A., Singer, M. R., Sutherland, C., Redondo, C., Alexander, L. T., Hughes, P. F., Knapp, S., Gurley, S. B., Sparks, M. A., MacDonald, J. A., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.06.006 · Cited by 29
Use of Inhibitors in the Study of MAP Kinases
Burkhard, K. A., & Shapiro, P. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-795-2_6 · Cited by 30
“However, SP600125 has also been shown to inhibit a number of other kinases (19), which must be considered when using this compound for evaluating JNK pathway regulation.”
Harpagoside attenuates MPTP/MPP+ induced dopaminergic neurodegeneration and movement disorder via elevating glial cell line‐derived neurotrophic factor
Sun, X., Xiong, Z., Zhang, Y., Meng, Y. J., Xu, G., Xia, Z., Li, J., Zhang, R., Ke, Z., Xia, Z., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07635.x · Cited by 30
Diversity of the intracellular mechanisms underlying the anti-tumor properties of indirubins
Meijer, L., Shearer, J., Bettayeb, K., & Ferandin, Y. (2007) · International Congress Series · doi:10.1016/j.ics.2007.07.041 · Cited by 29
Akt Inhibitor Akt-IV Blocks Virus Replication through an Akt-Independent Mechanism
Dunn, E. F., Fearns, R., & Connor, J. H. (2009) · Journal of Virology · doi:10.1128/jvi.01092-09 · Cited by 30
“The difference in the actions of Akt-IV and A-443654 are highlighted by the results of our in vitro kinaseprofiling assays; these show that Akt-IV does not directly inhibit Akt kinase activity in vitro (Table 1), while A-443654 in an identical screen does (5).”
BackgroundMethod
Regulation of Src kinase activity during Xenopus oocyte maturation
Tokmakov, A. A., Iwasaki, T., Itakura, S., Sato, K., Shirouzu, M., Fukami, Y., & Yokoyama, S. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.10.018 · Cited by 30
“Although PP2 was developed as a specific inhibitor of SFKs, it was also reported to inhibit the activity of some other tyrosine kinases (Bain et al., 2003).”
Background
Context-dependent roles of mutant B-Raf signaling in melanoma and colorectal carcinoma cell growth
Hao, H., Muniz-Medina, V. M., Mehta, H., Thomas, N. E., Khazak, V., Der, C. J., & Shields, J. M. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0728 · Cited by 30
“inhibitor of Ras interaction with Raf (29, 34, 35).”
Background
Inhibition of Src family kinases enhances retinoic acid–induced gene expression and myeloid differentiation
Miranda, M. B., Redner, R. L., & Johnson, D. E. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-0514 · Cited by 30
“The PP1 and PP2 inhibitors are selective inhibitors of SFKs and exhibit a broad spectrum activity against multiple members of the SFK family (26, 27).”
Background
Inhibition of FGF Receptor-1 Suppresses Alcohol Consumption: Role of PI3 Kinase Signaling in Dorsomedial Striatum
Even‐Chen, O., & Barak, S. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.0805-19.2019 · Cited by 30
“After recovery from the cannulation surgery, we used the specific PI3K inhibitor wortmannin (Bain et al., 2003), or the specific MEK inhibitor U0126 (Sweatt, 2001), in two separate experiments.”
Method
Pyrimidine and Purine Analogues, Effects on Cell Cycle Regulation and the Role of Cell Cycle Inhibitors to Enhance Their Cytotoxicity
Sigmond, J., & Peters, G. J. (2005) · Nucleosides Nucleotides & Nucleic Acids · doi:10.1080/15257770500269556 · Cited by 30
“Roscovitine has high specifity to cdk2, but also cdk1, cdk5, and cdk7 can be inhibited.[31,32] It has antitumor activity in numerous cancer cell lines and xenografts.”
Background
Varicella-Zoster Virus IE63 Protein Phosphorylation by Roscovitine-sensitive Cyclin-dependent Kinases Modulates Its Cellular Localization and Activity
Habran, L., Bontems, S., Valentin, E. D., Sadzot‐Delvaux, C., & Piette, J. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503312200 · Cited by 30
c-Jun N-terminal Kinase-mediated Stabilization of Microsomal Prostaglandin E2 Synthase-1 mRNA Regulates Delayed Microsomal Prostaglandin E2 Synthase-1 Expression and Prostaglandin E2 Biosynthesis by Cardiomyocytes
Degousée, N., Angoulvant, D., Fazel, S. S., Stefanski, E., Saha, S., Iliescu, K., Lindsay, T. F., Fish, J. E., Marsden, P. A., Li, R., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602815200 · Cited by 30
Profiling the kinome: Current capabilities and future challenges
Knight, J. D. R., Pawson, T. J., & Gingras, A. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.10.015 · Cited by 29
Characteristics and trends in global tea research: a Science Citation Index Expanded‐based analysis
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HER2-driven breast cancer suppression by the JNK signaling pathway
Itah, Z., Chaudhry, S., Ponny, S. R., Aydemir, Ö., Lee, A., Cavanagh, J., Tournier, C., Muller, W. J., & Davis, R. J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218373120 · Cited by 28
Mitotic phosphorylation of tankyrase, a PARP that promotes spindle assembly, by GSK3
Yeh, T.-Y. J., Sbodio, J. I., & Chi, N. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.09.080 · Cited by 30
Anti-obesity effects of 3-hydroxychromone derivative, a novel small-molecule inhibitor of glycogen synthase kinase-3
Lee, S., Yang, W. K., Song, J. H., Ra, Y. M., Jeong, J.-H., Choe, W., Kang, I., Kim, S. S., & Ha, J. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.12.023 · Cited by 29
“However, the selectivity of most pharmacological GSK-3 inhibitors is poorly understood [16–18].”
Background
Role of Src homology 2 domain-mediated PTK signaling in mouse zygotic development
Li, M., Luo, J., Li, C., & Kinsey, W. H. (2006) · Reproduction · doi:10.1530/rep.1.01151 · Cited by 29
“Analysis of mammalian egg activation using chemical inhibitors (PP2 and SU6656), which are reasonably specific for Src-family PTKs (Bain et al. 2003) has demonstrated that MII resumption induced parthenogenetically by calcium ionophore or by Tr-kit required Src-family PTK activity (Sette et al.”
Background
Chemical tools to probe cellularO-GlcNAc signalling
Ostrowski, A., & van Aalten, D. M. F. (2013) · Biochemical Journal · doi:10.1042/bj20131081 · Cited by 30
Myristoylation of the dual‐specificity phosphatase c‐JUN N‐terminal kinase (JNK) stimulatory phosphatase 1 is necessary for its activation of JNK signaling and apoptosis
Schwertassek, U., Buckley, D. A., Xu, C., Lindsay, A. J., McCaffrey, M., Neubert, T. A., & Tonks, N. K. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07661.x · Cited by 28
“However, these efforts were frustrated by the lack of specificity of SP600125, which has also been reported by others [42,43].”
Background
ML-9, a myosin light chain kinase inhibitor, reduces intracellular Ca2+ concentration in guinea pig trachealis
Ito, S., Kume, H., Honjo, H., Kodama, I., Katoh, H., Hayashi, H., & Shimokata, K. (2004) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2004.01.013 · Cited by 29
Lyn-mediated mitochondrial tyrosine phosphorylation is required to preserve mitochondrial integrity in early liver regeneration
Gringeri, E., Carraro, A., Tibaldi, E. V., D’Amico, F., Mancon, M., Toninello, A., Pagano, M. A., Vio, C., Cillo, U., & Brunati, A. M. (2009) · Biochemical Journal · doi:10.1042/bj20090902 · Cited by 29
Src-family tyrosine kinases as therapeutic targets in advanced cancer
Gelman, I. H. (2011) · Frontiers in Bioscience · doi:10.2741/e287 · Cited by 28
The expanding landscape of canonical and non-canonical protein phosphorylation
Houlès, T., Yoon, S.-O., & Roux, P. P. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.08.004 · Cited by 29
Role of LARP6 and Nonmuscle Myosin in Partitioning of Collagen mRNAs to the ER Membrane
Wang, H., & Stefanovic, B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108870 · Cited by 28
“Myosin light chain kinase (MLCK) phosphorylates regulatory light chains of nonmuscle myosin to promote assembly of the filaments [66].”
MethodInfluential
Inhibition of the mitochondrial permeability transition by protein kinase A in rat liver mitochondria and hepatocytes
Pediaditakis, P., Js, K., He, L., Zhang, X., Graves, L. M., & Lemasters, J. J. (2010) · Biochemical Journal · doi:10.1042/bj20091741 · Cited by 28
“Since KT-5823, a staurosporine analogue, inhibits a number of protein kinases, including PKA [18,36,39,40], we examined the effects of highly specific peptide inhibitors of PKA and PKG to address further the possible involvement of PKG and PKA in cytosol-dependent inhibition of the MPT.”
Prostaglandins from Cytosolic Phospholipase A2α/Cyclooxygenase-1 Pathway and Mitogen-activated Protein Kinases Regulate Gene Expression in Candida albicans-infected Macrophages
Yun, B., Lee, H.-J., Jayaraja, S., Suram, S., Murphy, R. C., & Leslie, C. C. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.714873 · Cited by 28
“A thorough characterization has shown that SP600125 exhibits poor specificity (44).”
Background
Cyclic stretch induces reorientation of cells in a Src family kinase- and p130Cas-dependent manner
Niediek, V., Born, S., Hampe, N., Kirchgeßner, N., Merkel, R., & Hoffmann, B. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.10.003 · Cited by 29
Molecular dissection of egg fertilization signaling with the aid of tyrosine kinase-specific inhibitor and activator strategies
Sato, K., Iwasaki, T., Hirahara, S., Nishihira, Y., & Fukami, Y. (2003) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.11.017 · Cited by 28
The Effects of Mitogen-Activated Protein Kinase Inhibitors or Small Interfering RNAs on Gallic Acid-Induced HeLa Cell Death in Relation to Reactive Oxygen Species and Glutathione
You, B. R., & Park, W. H. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf103379d · Cited by 28
Cross‐talk between MAP kinase pathways is involved in IGF‐independent, IGFBP‐6‐induced Rh30 rhabdomyosarcoma cell migration
Fu, P., Liang, G. J., Khot, S. S., Phan, R., & Bach, L. A. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22156 · Cited by 28
“SP600125, although widely used as a JNK inhibitor, is less specific (Bain et al., 2003).”
BackgroundInfluential
5′-OH-5-nitro-Indirubin oxime (AGM130), an Indirubin derivative, induces apoptosis of Imatinib-resistant chronic myeloid leukemia cells
Kim, W., Lee, M.-J., Kim, D.-H., Lee, J.-E., Kim, J., Kim, Y., Song, M., & Park, S. (2013) · Leukemia Research · doi:10.1016/j.leukres.2012.12.017 · Cited by 28
Potentiation of the lethality of the histone deacetylase inhibitor LAQ824 by the cyclin-dependent kinase inhibitor roscovitine in human leukemia cells
Rosato, R. R., Almenara, J. A., Maggio, S. C., Atadja, P. W., Craig, R. W., Vrana, J. A., Dent, P., & Grant, S. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0157 · Cited by 28
“Among these, the purine analogue roscovitine primarily targets CDK1 and CDK2 (16).”
Background
An Indirubin Derivative, Indirubin-3′-Monoxime Suppresses Oral Cancer Tumorigenesis through the Downregulation of Survivin
Lo, W., & Chang, N.-W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070198 · Cited by 28
“Furthermore, compared with indirubin, I3M inhibits many additional protein kinases as well as STAT3 signaling, and it has been shown to have anti-proliferative effects in vascular smooth muscle cells [10–12].”
Background
Evaluation of the Role of JNK1 in the Hippocampus in an Experimental Model of Familial Alzheimer’s Disease
Petrov, D., Luque, M., Pedrós, I., Ettcheto, M., Abad, S., Pallàs, M., Verdaguer, E., Auladell, C., Folch, J., & Camins, A. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9522-6 · Cited by 28
Novel tumor-suppressor function of KLF4 in pediatric T-cell acute lymphoblastic leukemia
Shen, Y., Chen, T. J., & Lacorazza, H. D. (2017) · Experimental Hematology · doi:10.1016/j.exphem.2017.04.009 · Cited by 28
“Although SP600125 has served as an important tool to study the JNK pathway, it inhibits other kinases such as Erk and p38 (Table 1) and showed low specificity for JNK proteins, an important caveat for cancer treatment where JNK1 and JNK2 can display opposite functions (95).”
Method
Development of novel 2,4-bispyridyl thiophene–based compounds as highly potent and selective Dyrk1A inhibitors. Part I: Benzamide and benzylamide derivatives
Darwish, S. S., Abdel‐Halim, M., Salah, M., Abadi, A., Becker, W. B., & Engel, M. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.07.050 · Cited by 28
PDE2 inhibition by the PI3 kinase inhibitor LY294002 and analogues
Abbott, B. M., & Thompson, P. E. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.03.043 · Cited by 28
The Proline-Histidine-Rich CDK2/CDK4 Interaction Region of C/EBPα Is Dispensable for C/EBPα-Mediated Growth Regulation In Vivo
Porse, B. T., Pedersen, T. Å., Hasemann, M. S., Schuster, M. B., Kirstetter, P., Luedde, T., Damgaard, I., Kurz, E., Schjerling, C. K., & Nerlov, C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.3.1028-1037.2006 · Cited by 25
“5 embryos were prepared, and the ability of the immunoprecipitated CDK2 to phosphorylate histone H1 was assayed in the presence or absence of the CDK inhibitor roscovitine (which inhibits CDKs 1, 2, 5, and 7 [1]).”
Method
Inhibitory role of Src family tyrosine kinases on Ca2+-dependent insulin release
Cheng, H. M., Straub, S. G., & Sharp, G. W. G. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00103.2006 · Cited by 28
“To circumvent this problem, two structurally different inhibitors of Src family kinases, PP2 and SU-6656 (3), were tested, and similar effects on insulin secretion were demonstrated.”
Influential
Murine leukemia virus p12 tethers the capsid-containing pre-integration complex to chromatin by binding directly to host nucleosomes in mitosis
Wanaguru, M., Barry, D. J., Benton, D. J., O’Reilly, N. J., & Bishop, K. N. (2018) · PLOS Pathogens · doi:10.1371/journal.ppat.1007117 · Cited by 27
Selectivity of pharmacological tools: implications for use in cell physiology. A Review in the Theme: Cell Signaling: Proteins, Pathways and Mechanisms
Michel, M. C., & Seifert, R. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00389.2014 · Cited by 27
“For instance, one group of investigators has systematically screened 42 protein kinase inhibitors in common use against a broad panel of kinases (11, 47).”
Background
Kinase Targets in Cns Drug Discovery
Gunosewoyo, H., Yu, L.-F., Munoz, L., & Kassiou, M. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0214 · Cited by 27
Integrative Multi-Kinase Approach for the Identification of Potent Antiplasmodial Hits
Lima, M. N. N., Cassiano, G. C., Tomaz, K. C. P., Silva, A. C., Sousa, B. K. D. P., Ferreira, L. T., Tavella, T. A., Calit, J., Bargieri, D. Y., Neves, B. J., et al. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00773 · Cited by 26
Unbiased evaluation of rapamycin's specificity as an mTOR inhibitor
Artoni, F., Grützmacher, N., & Demetriades, C. (2023) · Aging Cell · doi:10.1111/acel.13888 · Cited by 25
“Sometimes, inhibitors even show higher potency towards off- targets compared to on- target effects (Bain et al., 2003, 2007; Davies et al., 2000; Davis et al., 2011; Fedorov et al., 2007).”
Cell cycle inhibition without disruption of neurogenesis is a strategy for treatment of central nervous system diseases
Liu, D., Ander, B. P., & Sharp, F. R. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.11.013 · Cited by 27
“inhibitors, which also makes it difficult to rule out actions on other molecules (Bain et al., 2003; Sausville, 2003; Blagden and de Bono, 2005; Sridhar et al., 2006; Bain et al., 2007).”
Background
Myosin-based contraction is not necessary for cardiac c-looping in the chick embryo
Rémond, M. C., Fee, J. A., Elson, E. L., & Taber, L. A. (2006) · Anatomy and Embryology · doi:10.1007/s00429-006-0094-0 · Cited by 27
“(2001) found that the MLCK inhibitor ML-9, which is similar to but less specific than ML-7 (Bain et al. 2003), does not affect looping in the chick.”
Background
G12 Signaling through c-Jun NH2-Terminal Kinase Promotes Breast Cancer Cell Invasion
Juneja, J., Cushman, I., & Casey, P. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026085 · Cited by 27
“activation [24], we also employed siRNA-mediated silencing of JNK expression.”
Method
Indirubin-3′-monoxime, a derivative of a Chinese anti-leukemia medicine, inhibits Notch1 signaling
Lee, M.-J., Kim, M., Mo, J., Ann, E., Seo, M., Hong, J., Kim, Y., & Park, H.-S. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.02.013 · Cited by 27
“Indirubin and its derivatives have been identified as selective inhibitors of the cyclin-dependent kinases (CDKs), glycogen synthase kinase-3b (GSK-3b), c-Jun N-terminal kinase (JNK), Src kinase, fibroblast growth factor receptor 1 (FGFR1), the aryl hydrocarbon receptor, and muscle glycogen phosphorylase b [31–42].”
Background
Discovery of Potent and Highly Selective Inhibitors of GSK3b
An, W. F., Germain, A. R., Bishop, J. A., Nag, P. P., Metkar, S. R., Ketterman, J., Walk, M., Weïwer, M., Liu, X., Patnaik, D., et al. (2014) · Cited by 27
Differential effects of quercetin and resveratrol on Band 3 tyrosine phosphorylation signalling of red blood cells
Maccaglia, A., Mallozzi, C., & Minetti, M. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00762-9 · Cited by 27
Phosphorylation by JNK switches BRD4 functions
Devaiah, B. N., Singh, A. K., Mu, J., Chen, Q., Meerzaman, D. M., & Singer, D. S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.09.030 · Cited by 25
Stimulation of Insulin Signaling and Inhibition of JNK-AP1 Activation Protect Cells from Amyloid-β-Induced Signaling Dysregulation and Inflammatory Response
Bamji‐Mirza, M., Callaghan, D., Najem, D., Shen, S., Hasim, M. S., Yang, Z., & Zhang, W. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131949 · Cited by 26
“SP600125 was originally reported to inhibit JNK2 activity; however, more recent data has shown that 13 of 30 tested protein kinases were inhibited by 10 M SP600125 at various degrees [50].”
Result
Atypical (RIO) protein kinases from Haemonchus contortus — Promise as new targets for nematocidal drugs
Campbell, B. E., Boag, P. R., Hofmann, A., Cantacessi, C., Wang, C. K. L., Taylor, P., Hu, M., Sindhu, Z. U. D., Loukas, A. C., Sternberg, P. W., et al. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.01.006 · Cited by 26
Molecular interdiction of Src-family kinase signaling in hematopoietic cells
Geahlen, R. L., Handley, M. D., & Harrison, M. L. (2004) · Oncogene · doi:10.1038/sj.onc.1208078 · Cited by 26
Neuronal differentiation by analogs of staurosporine
Thompson, A. F., & Levin, L. A. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2009.12.018 · Cited by 26
“…kinase 1, cyclin-dependent kinase 2, cyclin-dependent kinase 5, Janus kinase 2, epidermal growth factor receptor kinase, plateletderived growth factor receptor kinase, myosin light-chain kinase, calmodulin-dependent protein kinase, Rho kinase, MAP/ERK kinase, and Akt (Bain et al., 2003).”
Background
Rational design of potent GSK3β inhibitors with selectivity for Cdk1 and Cdk2
Lesuisse, D., Dutruc-Rosset, G., Tiraboschi, G., Dreyer, M., Maignan, S., Chevalier, A., Halley, F., Bertrand, P., Burgevin, M., Quarteronet, D., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.01.114 · Cited by 26
Steroid-Insensitive ERK1/2 Activity Drives CXCL8 Synthesis and Neutrophilia by Airway Smooth Muscle
Robins, S., Roussel, L., Schachter, A., Risse, P., Mogas, A. K., Olivenstein, R., Martin, J. G., Hamid, Q. A., & Rousseau, S. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2010-0450oc · Cited by 26
Hematopoiesis and Thymic Apoptosis Are Not Affected by the Loss of Cdk2
Berthet, C., Rodriguez‐Galán, M. C., Hodge, D. L., Gooya, J. M., Pascal, V., Young, H. A., Keller, J. R., Bosselut, R., & Kaldis, P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00029-07 · Cited by 26
“5 M, which is considered more specific for inhibition of Cdk2 (3), instead of the commonly used concentration of 50 M.”
Background
Development of novel amide–derivatized 2,4-bispyridyl thiophenes as highly potent and selective Dyrk1A inhibitors. Part II: Identification of the cyclopropylamide moiety as a key modification
Darwish, S. S., Abdel‐Halim, M., ElHady, A. K., Salah, M., Abadi, A., Becker, W. B., & Engel, M. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.08.097 · Cited by 26
Src-family kinases play an essential role in differentiation signaling downstream of macrophage colony-stimulating factor receptors mediating persistent phosphorylation of phospholipase C-γ2 and MAP kinases ERK1 and ERK2
Bourgin, C., Gobert, S., Thérier, J., Grasset, M.-F., & Mouchiroud, G. (2007) · Leukemia · doi:10.1038/sj.leu.2404986 · Cited by 27
Interleukin-6 in the pathogenesis of posterior capsule opacification and the potential role for interleukin-6 inhibition in the future of cataract surgery
Lewis, A. C. (2013) · Medical Hypotheses · doi:10.1016/j.mehy.2012.12.042 · Cited by 26
Glucose Utilization Is Essential for Hypoxia-Inducible Factor 1α-Dependent Phosphorylation of c-Jun
Laderoute, K. R., Calaoagan, J. M., Knapp, M., & Johnson, R. S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4128-4137.2004 · Cited by 26
“GST–c-Jun(1-141) protein was prepared by elution from the beads with a glu-”
BackgroundMethodInfluential
Tyrosine kinase and phosphatase regulation of slow delayed‐rectifier K+ current in guinea‐pig ventricular myocytes
Missan, S., Linsdell, P., & McDonald, T. F. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.104422 · Cited by 26
“I Ks was unaffected by AG1478 (10 μM), an inhibitor of epidermal growth factor receptor TK, and was strongly suppressed by the Src TK inhibitor PP2 (10 μM) but not by the inactive analogue PP3 (10 μM).”
BackgroundResultInfluential
Epigallocatechin-3-Gallate Plus Omega-3 Restores the Mitochondrial Complex I and F0F1-ATP Synthase Activities in PBMCs of Young Children with Down Syndrome: A Pilot Study of Safety and Efficacy
Scala, I., Valenti, D., Scotto D’Aniello, V., Marino, M., Riccio, M. P., Bravaccio, C., Vacca, R. A., & Strisciuglio, P. (2021) · Antioxidants · doi:10.3390/antiox10030469 · Cited by 25
“Regarding cognitive improvements, parents should be informed that efficacy data are still lacking in young children with DS. Future clinical studies addressing the interaction between EGCG and omega-3 as well as the analysis of EGCG effects on other relevant targets such as DYRK1A, mtDNA and ROS defense proteins will…”
BackgroundInfluential
Scapinin-induced Inhibition of Axon Elongation Is Attenuated by Phosphorylation and Translocation to the Cytoplasm
Farghaian, H., Chen, Y., Fu, A. W. Y., Fu, A. K. Y., Ip, J. P. K., Ip, N. Y., Turnley, A. M., & Cole, A. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.205781 · Cited by 25

Authors: BAIN, J., McLAUCHLAN, H., ELLIOTT, M., & COHEN, P.
Affiliations: University of Dundee (GB)
Corresponding author: BAIN, Jenny
McLAUCHLAN, Hilary
ELLIOTT, Matthew
COHEN, Philip
ORCID: ELLIOTT, Matthew
COHEN, Philip
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2003-04-01
Volume: 371
Issue: 1
Pages: 199-204
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20021535
PMC: PMC1223271
OpenAlex: W2011588737
Cited by: 1,369
References: 42
Citations by year: 2026: 9 · 2025: 21 · 2024: 12 · 2023: 16 · 2022: 26 · 2021: 35 · 2020: 28 · 2019: 38 · 2018: 42 · 2017: 48 · 2016: 42 · 2015: 44 · 2014: 52 · 2013: 66 · 2012: 70
FWCI: 43.75
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Mechanisms and Therapy
Keywords: protein kinase inhibitors, kinase selectivity, serine/threonine kinase, indirubin-3'-monoxime, KT5823, ML-9, kenpaullone, roscovitine, pyrazolopyrimidines, cyclin-dependent kinases, glycogen synthase kinase-3, Src family kinases, epigallocatechin gallate, DYRK1A, kinase substrate identification
MeSH terms: Alkaloids, Anthracenes, Azepines, Benzazepines, Carbazoles, Catechin, Enzyme Inhibitors, Indoles, Kinetin, Naphthalenes, Oximes, Purines, Pyrazoles, Pyrimidines, Substrate Specificity, Signal Transduction, Cyclin-Dependent Kinases, src-Family Kinases, Mitogen-Activated Protein Kinases, Glycogen Synthase Kinase 3, Protein Kinase Inhibitors, JNK Mitogen-Activated Protein Kinases

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The specificities of protein kinase inhibitors: an update

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