The Protein Kinase Complement of the Human Genome

Initial sequencing and analysis of the human genome

International Human Genome Sequencing Consortium, Whitehead Institute for Biomedical Research, C. F. G. R., Lander, E. S., Linton, L. M., Birren, B., Nusbaum, C., Zody, M. C., Baldwin, J., Devon, K., Dewar, K., et al. (2001) · Nature · doi:10.1038/35057062 · Cited by 24,216

The sequence of the human genome

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Oncogenic kinase signalling.

Blume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738

The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1

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Signaling—2000 and Beyond

Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586

Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.

Hanks, S. K., & Hunter, T. R. (1995) · PubMed · Cited by 2,518

Protein kinases — the major drug targets of the twenty-first century?

Cohen, P. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd773 · Cited by 2,232

Comparative Genomics of the Eukaryotes

Rubin, G. M., Yandell, M. D., Wortman, J. R., Gabor, G. L., Miklos, Nelson, C. R., Hariharan, I. K., Fortini, M. E., Li, P. W., Apweiler, R., et al. (2000) · Science · doi:10.1126/science.287.5461.2204 · Cited by 1,698

A thousand and one protein kinases

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Evolution of protein kinase signaling from yeast to man

Manning, G., Plowman, G. D., Hunter, T. R., & Sudarsanam, S. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02179-5 · Cited by 1,004

Mutational landscape of metastatic cancer revealed from prospective clinical sequencing of 10,000 patients

Zehir, A., Benayed, R., Shah, R. H., Syed, A., Middha, S., Kim, H. R., Srinivasan, P., Gao, J., Chakravarty, D., Devlin, S. M., et al. (2017) · Nature Medicine · doi:10.1038/nm.4333 · Cited by 3,380

Comprehensive analysis of kinase inhibitor selectivity

Davis, M. I., Hunt, J. P., Herrgard, S., Ciceri, P., Wodicka, L. M., Pallares, G., Hocker, M., Treiber, D. K., & Zarrinkar, P. P. (2011) · Nature Biotechnology · doi:10.1038/nbt.1990 · Cited by 2,409

A quantitative analysis of kinase inhibitor selectivity

Karaman, M. W., Herrgard, S., Treiber, D. K., Gallant, P., Atteridge, C. E., Campbell, B. T., Chan, K. W., Ciceri, P., Davis, M. I., Edeen, P. T., et al. (2008) · Nature Biotechnology · doi:10.1038/nbt1358 · Cited by 2,466

Unresponsiveness of colon cancer to BRAF(V600E) inhibition through feedback activation of EGFR

Prahallad, A., Sun, C., Huang, S., Di Nicolantonio, F., Salazar, R., Zecchin, D., Beijersbergen, R. L., Bardelli, A., & Bernards, R. (2012) · Nature · doi:10.1038/nature10868 · Cited by 2,051

Protein Tyrosine Phosphatases in the Human Genome

Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886

ERK/MAPK signalling pathway and tumorigenesis (Review)

Guo, Y., Pan, W., Liu, S., Shen, Z., Xu, Y., & Hu, L. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8454 · Cited by 1,475

Mechanisms of specificity in protein phosphorylation

Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451

The importance of intrinsic disorder for protein phosphorylation

Iakoucheva, L. M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh253 · Cited by 1,429

FAK in cancer: mechanistic findings and clinical applications

Sulzmaier, F. J., Jean, C., & Schlaepfer, D. D. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3792 · Cited by 1,381

LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR‐1

Lizcano, J. M., Göransson, O., Toth, R., Deak, M., Morrice, N. A., Boudeau, J., Hawley, S. A., Udd, L., Mäkelä, T. P., Hardie, D. G., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600110 · Cited by 1,381

Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease

Hart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060608-102511 · Cited by 1,317

The nuts and bolts of AGC protein kinases

Pearce, L. R., Komander, D., & Alessi, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2822 · Cited by 1,294

Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry

Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.124125 · Cited by 1,270

The Genome of the Sea Urchin Strongylocentrotus purpuratus

Sodergren, E., Weinstock, G. M., Davidson, E. H., Cameron, R. A., Gibbs, R. A., Angerer, R. C., Angerer, L. M., Arnone, M. I., Burgess, D. R., Burke, R. D., et al. (2006) · Science · doi:10.1126/science.1133609 · Cited by 1,132

Mechanisms of receptor tyrosine kinase activation in cancer

Du, Z., & Lovly, C. M. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0782-4 · Cited by 1,066

Kinase inhibitors: the road ahead

Ferguson, F. M., & Gray, N. S. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.21 · Cited by 1,009

Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity

Anastassiadis, T., Deacon, S. W., Devarajan, K., Ma, H., & Peterson, J. R. (2011) · Nature Biotechnology · doi:10.1038/nbt.2017 · Cited by 919

Classification of small molecule protein kinase inhibitors based upon the structures of their drug-enzyme complexes

Roskoski, R. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2015.10.021 · Cited by 886

Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition

Taipale, M., Krykbaeva, I., Koeva, M., Kayatekin, C., Westover, K. D., Karras, G. I., & Lindquist, S. (2012) · Cell · doi:10.1016/j.cell.2012.06.047 · Cited by 879

Specificity, versatility, and control of TGF-β family signaling

Derynck, R., & Budi, E. H. (2019) · Science Signaling · doi:10.1126/scisignal.aav5183 · Cited by 785

Redox regulation of FoxO transcription factors

Klotz, L.-O., Sánchez-Ramos, C., Prieto-Arroyo, I., Urbánek, P., Steinbrenner, H., & Monsalve, M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.019 · Cited by 747

Large-scale phosphorylation analysis of mouse liver

Villén, J., Beausoleil, S. A., Gerber, S. A., & Gygi, S. P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609836104 · Cited by 730

An atlas of substrate specificities for the human serine/threonine kinome

Johnson, J. L., Yaron, T. M., Huntsman, E. M., Kerelsky, A., Song, J., Regev, A., Lin, T.-Y., Liberatore, K., Cizin, D. M., Cohen, B. M., et al. (2023) · Nature · doi:10.1038/s41586-022-05575-3 · Cited by 728

Signaling Receptors for TGF-β Family Members

Heldin, C.-H., & Moustakas, A. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022053 · Cited by 711

Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1

Um, S. H., D'Alessio, D., & Thomas, G. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.003 · Cited by 690

Targeting the cancer kinome through polypharmacology

Knight, Z. A., Lin, H., & Shokat, K. M. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2787 · Cited by 674

Tau protein kinases: Involvement in Alzheimer's disease

Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631

Biology of the TAM Receptors

Lemke, G. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a009076 · Cited by 598

The casein kinase 1 family: participation in multiple cellular processes in eukaryotes

Knippschild, U., Gocht, A., Wolff, S., Huber, N., Löhler, J., & Stöter, M. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2004.12.011 · Cited by 601

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle

Daub, H., Olsen, J. V., Bairlein, M., Gnad, F., Oppermann, F. S., Körner, R., Greff, Z., Kéri, G., Stemmann, O., & Mann, M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.007 · Cited by 594

Properties of FDA-approved small molecule protein kinase inhibitors

Roskoski, R. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.03.006 · Cited by 554

Initiating Cellular Stress Responses

Bakkenist, C. J., & Kastan, M. B. (2004) · Cell · doi:10.1016/j.cell.2004.06.023 · Cited by 544

Small-molecule kinase inhibitors: an analysis of FDA-approved drugs

Wu, P., Nielsen, T. E., & Clausen, M. H. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2015.07.008 · Cited by 457

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation

Rigbolt, K. T. G., Prokhorova, T. A., Akimov, V., Henningsen, J., Johansen, P. T., Kratchmarova, I., Kassem, M., Mann, M., Olsen, J. V., & Blagoev, B. (2011) · Science Signaling · doi:10.1126/scisignal.2001570 · Cited by 451

Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases

Mazanetz, M. P., & Fischer, P. M. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2111 · Cited by 459

MED12 Controls the Response to Multiple Cancer Drugs through Regulation of TGF-β Receptor Signaling

Huang, S., Hölzel, M., Knijnenburg, T., Schlicker, A., Roepman, P., McDermott, U., Garnett, M., Grernrum, W., Sun, C., Prahallad, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.035 · Cited by 430

Kinase mutations in human disease: interpreting genotype–phenotype relationships

Lahiry, P., Torkamani, A., Schork, N. J., & Hegele, R. A. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2707 · Cited by 420

MAPKAP kinases — MKs — two's company, three's a crowd

Gaestel, M. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1834 · Cited by 413

A combinatorial strategy for treating KRAS-mutant lung cancer

Manchado, E., Weissmueller, S., Morris, J. P., Chen, C.-C., Wullenkord, R., Lujambio, A., de Stanchina, E., Poirier, J. T., Gainor, J. F., Corcoran, R. B., et al. (2016) · Nature · doi:10.1038/nature18600 · Cited by 403

Defining a new nomenclature for the structures of active and inactive kinases

Modi, V., & Dunbrack, R. L. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814279116 · Cited by 367

Mapping the Degradable Kinome Provides a Resource for Expedited Degrader Development

Donovan, K. A., Ferguson, F. M., Bushman, J. W., Eleuteri, N. A., Bhunia, D., Ryu, S., Tan, L., Shi, K., Yue, H., Liu, X., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.038 · Cited by 359

Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions

BIONDI, R. M., & NEBREDA, A. R. (2003) · Biochemical Journal · doi:10.1042/bj20021641 · Cited by 334

Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3

Jura, N., Shan, Y., Cao, X., Shaw, D. E., & Kuriyan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912101106 · Cited by 338

Irreversible Protein Kinase Inhibitors: Balancing the Benefits and Risks

Barf, T., & Kaptein, A. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3003203 · Cited by 331

Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms

Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310

The molecular landscape of colorectal cancer cell lines unveils clinically actionable kinase targets

Medico, E., Russo, M., Picco, G., Cancelliere, C., Valtorta, E., Corti, G., Buscarino, M., Isella, C., Lamba, S., Martinoglio, B., et al. (2015) · Nature Communications · doi:10.1038/ncomms8002 · Cited by 302

Atypical mitogen-activated protein kinases: Structure, regulation and functions

Coulombe, P., & Meloche, S. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.11.001 · Cited by 298

FOXP3+ regulatory T cells and their functional regulation

Li, Z., Li, D., Tsun, A., & Li, B. (2015) · Cellular & Molecular Immunology · doi:10.1038/cmi.2015.10 · Cited by 290

Structure of the CaMKIIδ/Calmodulin Complex Reveals the Molecular Mechanism of CaMKII Kinase Activation

Rellos, P., Pike, A. C. W., Niesen, F. H., Salah, E., Lee, W. H., von Delft, F., & Knapp, S. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000426 · Cited by 279

Trans-Omics: How To Reconstruct Biochemical Networks Across Multiple ‘Omic’ Layers

Yugi, K., Kubota, H., Hatano, A., & Kuroda, S. (2016) · Trends in Biotechnology · doi:10.1016/j.tibtech.2015.12.013 · Cited by 258

Abiotic production of sugar phosphates and uridine ribonucleoside in aqueous microdroplets

Nam, I., Lee, J. K., Nam, H. G., & Zare, R. N. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714896114 · Cited by 262

PROTACs: great opportunities for academia and industry (an update from 2020 to 2021)

He, M., Cao, C., Ni, Z., Liu, Y., Song, P., Hao, S., He, Y., Sun, X., & Rao, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00999-9 · Cited by 283

Pim kinases phosphorylate multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL

Macdonald, A., Campbell, D. G., Toth, R., McLauchlan, H., Hastie, C. J., & Arthur, J. S. C. (2006) · BMC Cell Biology · doi:10.1186/1471-2121-7-1 · Cited by 246

Regulation of autophagy by coordinated action of mTORC1 and protein phosphatase 2A

Wong, P.-M., Feng, Y., Wang, J., Shi, R., & Jiang, X. (2015) · Nature Communications · doi:10.1038/ncomms9048 · Cited by 239

On the Integration of In Silico Drug Design Methods for Drug Repurposing

March-Vila, E., Pinzi, L., Sturm, N., Tinivella, A., Engkvist, O., Chen, H., & Rastelli, G. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00298 · Cited by 235

Protein kinase inhibitors in the treatment of inflammatory and autoimmune diseases

Patterson, H., Nibbs, R., McInnes, I., & Siebert, S. (2014) · Clinical and Experimental Immunology · doi:10.1111/cei.12248 · Cited by 199

Docking interactions in protein kinase and phosphatase networks

Reményi, A., Good, M. C., & Lim, W. A. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.10.008 · Cited by 188

CR8, a potent and selective, roscovitine-derived inhibitor of cyclin-dependent kinases

Bettayeb, K., Oumata, N., Echalier, A., Ferandin, Y., Endicott, J. A., Galons, H., & Meijer, L. (2008) · Oncogene · doi:10.1038/onc.2008.191 · Cited by 184

Recent Advances in Selective and Irreversible Covalent Ligand Development and Validation

Zhang, T., Hatcher, J. M., Teng, M., Gray, N. S., & Kostic, M. (2019) · Cell Chemical Biology · doi:10.1016/j.chembiol.2019.09.012 · Cited by 178

Mitochondrial dysfunction in Parkinson's disease

Schapira, A. H. V. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402160 · Cited by 175

Site-specific proteasome phosphorylation controls cell proliferation and tumorigenesis.

Guo, X., Wang, X., Wang, Z., Banerjee, S., Yang, J., Huang, L., & Dixon, J. E. (2016) · Nature Cell Biology · doi:10.1038/ncb3289 · Cited by 169

Role for KAP1 Serine 824 Phosphorylation and Sumoylation/Desumoylation Switch in Regulating KAP1-mediated Transcriptional Repression

Li, X., Lee, Y.-K., Jeng, J.-C., Yen, Y., Schultz, D. C., Shih, H.-M., & Ann, D. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706912200 · Cited by 168

Substrate and Docking Interactions in Serine/Threonine Protein Kinases

Goldsmith, E. J., Akella, R., Min, X., Zhou, T., & Humphreys, J. M. (2007) · Chemical Reviews · doi:10.1021/cr068221w · Cited by 143

Current status of SRC inhibitors in solid tumor malignancies

Puls, L. N., Eadens, M., & Messersmith, W. (2011) · The Oncologist · doi:10.1634/theoncologist.2010-0408 · Cited by 158

Minireview: Alternative Activation Pathways for the Androgen Receptor in Prostate Cancer

Lamont, K. R., & Tindall, D. J. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0469 · Cited by 150

Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism

Hardie, D. G. (2011) · Proceedings of the Nutrition Society · doi:10.1017/s0029665110003915 · Cited by 146

NMR Characterization of Kinase p38 Dynamics in Free and Ligand‐Bound Forms

Vogtherr, M., Saxena, K., Hoelder, S., Grimme, S., Betz, M., Schieborr, U., Pescatore, B., Robin, M., Delarbre, L., Langer, T., et al. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200502770 · Cited by 145

An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease

Cavallini, A., Brewerton, S., Bell, A., Sargent, S., Glover, S., Hardy, C., Moore, R., Calley, J., Ramachandran, D., Poidinger, M., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463984 · Cited by 133

ChimerDB 4.0: an updated and expanded database of fusion genes

Jang, Y. E., Jang, I., Kim, S., Cho, S., Kim, D., Kim, K., Kim, J., Hwang, J., Kim, S., Kim, J., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1013 · Cited by 108

Quantitative Phosphoproteomics Reveals a Cluster of Tyrosine Kinases That Mediates Src Invasive Activity in Advanced Colon Carcinoma Cells

Leroy, C., Fialin, C., Sirvent, A., Simon, V., Urbach, S., Poncet, J., Robert, B., Jouin, P., & Roche, S. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2354 · Cited by 114

A genomic toolkit to investigate kinesin and myosin motor function in cells

Maliga, Z., Junqueira, M., Toyoda, Y., Ettinger, A., Mora-Bermúdez, F., Klemm, R. W., Vasilj, A., Guhr, E., Ibarlucea-Benitez, I., Poser, I., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2689 · Cited by 103

A Docking Site in MKK4 Mediates High Affinity Binding to JNK MAPKs and Competes with Similar Docking Sites in JNK Substrates

Ho, D. T., Bardwell, A. J., Abdollahi, M., & Bardwell, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304229200 · Cited by 108

The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.

Gould, C. M., Kannan, N., Taylor, S. S., & Newton, A. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808436200 · Cited by 113

Identification of new kinase clusters required for neurite outgrowth and retraction by a loss-of-function RNA interference screen

Loh, S. H. Y., Francescut, L., Lingor, P., Bähr, M., & Nicotera, P. (2008) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402258 · Cited by 108

Targeting tumour microenvironment by tyrosine kinase inhibitor

Tan, H.-Y., Wang, N., Lam, W., Guo, W., Feng, Y., & Cheng, Y.-C. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0800-6 · Cited by 107

Glycogen Synthase Kinase (GSK) 3β Directly Phosphorylates Serine 212 in the Regulatory Loop and Inhibits Microtubule Affinity-regulating Kinase (MARK) 2

Timm, T., Balusamy, K., Li, X., Biernat, J., Mandelkow, E., & Mandelkow, E.-M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706596200 · Cited by 95

Shepherding AKT and androgen receptor by Ack1 tyrosine kinase.

Mahajan, K., & Mahajan, N. P. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22162 · Cited by 92

Multiple Post-translational Modifications Affect Heterologous Protein Synthesis

Tokmakov, A. A., Kurotani, A., Takagi, T., Toyama, M., Shirouzu, M., Fukami, Y., & Yokoyama, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.366351 · Cited by 88

High-content siRNA screening of the kinome identifies kinases involved in Alzheimer's disease-related tau hyperphosphorylation

Azorsa, D. O., Robeson, R. H., Frost, D., hoovet, B. M., Brautigam, G. R., Dickey, C., Beaudry, C., Basu, G. D., Holz, D. R., Hernandez, J. A., et al. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-25 · Cited by 88

Phosphorylation of synaptic vesicle protein 2A at Thr84 by casein kinase 1 family kinases controls the specific retrieval of synaptotagmin-1

Zhang, N., Gordon, S. L., Fritsch, M. J., Esoof, N., Campbell, D. G., Gourlay, R., Velupillai, S., Macartney, T., Peggie, M., van Aalten, D. M. F., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.4248-14.2015 · Cited by 72

Induction of Macrophage Function in Human THP-1 Cells Is Associated with Rewiring of MAPK Signaling and Activation of MAP3K7 (TAK1) Protein Kinase

Richter, E., Ventz, K., Harms, M., Mostertz, J., & Hochgräfe, F. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00021 · Cited by 75

The basic biology of PP2A in hematologic cells and malignancies

Haesen, D., Sents, W., Lemaire, K., Hoorne, Y., & Janssens, V. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00347 · Cited by 73

The Omnipresence of DYRK1A in Human Diseases

Deboever, E., Fistrovich, A., Hulme, C., & Dunckley, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169355 · Cited by 77

A community challenge for a pancancer drug mechanism of action inference from perturbational profile data

Douglass, E. F., Allaway, R. J., Szalai, B., Wang, W., Tian, T., Fernández-Torras, A., Realubit, R., Karan, C., Zheng, S., Pessia, A., et al. (2022) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100492 · Cited by 68

Towards simple kinetic models of functional dynamics for a kinase subfamily

Sultan, M. M., Kiss, G., & Pande, V. S. (2018) · Nature Chemistry · doi:10.1038/s41557-018-0077-9 · Cited by 68

PIM kinases: From survival factors to regulators of cell motility

Santio, N. M., & Koskinen, P. J. (2017) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.016 · Cited by 69

Equivocal, explicit and emergent actions of PKC isoforms in cancer

Parker, P. J., Brown, S. J., Calleja, V., Chakravarty, P., Cobbaut, M., Linch, M., Marshall, J. J. T., Martini, S., McDonald, N. Q., Soliman, T., et al. (2021) · Nature Reviews Cancer · doi:10.1038/s41568-020-00310-4 · Cited by 65

Approaches to efficiently estimate solvation and explicit water energetics in ligand binding: the use of WaterMap.

Yang, Y., Lightstone, F. C., & Wong, S. E. (2013) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2013.749853 · Cited by 65

Mass spectrometric analysis of protein tyrosine nitration in aging and neurodegenerative diseases

Yeo, W., Kim, Y. J., Kabir, M. H., Kang, J. W., & Kim, K. P. (2015) · Mass Spectrometry Reviews · doi:10.1002/mas.21429 · Cited by 61

Metabolomic high-content nuclear magnetic resonance-based drug screening of a kinase inhibitor library

Tiziani, S., Kang, Y., Choi, J. S., Roberts, W., & Paternostro, G. (2011) · Nature Communications · doi:10.1038/ncomms1562 · Cited by 60

United States Food and Drug Administration approved oral kinase inhibitors for the treatment of malignancies

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