Kinase mutations in human disease: interpreting genotype–phenotype relationships

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145

Mitogen-Activated Protein Kinase Pathways Mediated by ERK, JNK, and p38 Protein Kinases

Johnson, G. L., & Lapadat, R. (2002) · Science · doi:10.1126/science.1072682 · Cited by 4,295

The MAPK signaling cascade

Seger, R., & Krebs, E. G. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.9.7601337 · Cited by 3,631

Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders

Baxter, E. J., Scott, L. M., Campbell, P. J., East, C., Fourouclas, N., Swanton, S., Vassiliou, G. S., Bench, A. J., Boyd, E. M., Curtin, N., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)71142-9 · Cited by 3,548

The druggable genome

Hopkins, A. L., & Groom, C. R. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd892 · Cited by 3,305

Principles of interleukin (IL)-6-type cytokine signalling and its regulation

HEINRICH, P. C., BEHRMANN, I., HAAN, S., HERMANNS, H. M., MÜLLER-NEWEN, G., & SCHAPER, F. (2003) · Biochemical Journal · doi:10.1042/bj20030407 · Cited by 3,272

A census of human cancer genes

Futreal, P. A., Coin, L., Marshall, M., Down, T., Hubbard, T., Wooster, R., Rahman, N., & Stratton, M. R. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1299 · Cited by 3,184

Patterns of somatic mutation in human cancer genomes

Greenman, C. D., Stephens, P., Smith, R., Dalgliesh, G. L., Hunter, C., Bignell, G. R., Davies, H. R., Teague, J. W., Butler, A. P., Stevens, C., et al. (2007) · Nature · doi:10.1038/nature05610 · Cited by 3,143

Clinical Resistance to STI-571 Cancer Therapy Caused by BCR-ABL Gene Mutation or Amplification

Gorre, M. E., Mohammed, M., Ellwood, K., Hsu, N., Paquette, R., Rao, P. N., & Sawyers, C. L. (2001) · Science · doi:10.1126/science.1062538 · Cited by 3,104

Mechanism of Activation of the RAF-ERK Signaling Pathway by Oncogenic Mutations of B-RAF

Wan, P., Garnett, M. J., Roe, S. M., Lee, S., Niculescu‐Duvaz, D., Good, V. M., Cancer Genome Project, Jones, C. M., Marshall, C. J., Springer, C. J., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00215-6 · Cited by 2,863

Transcriptional Profiling of Endocrine Cerebro-Osteodysplasia Using Microarray and Next-Generation Sequencing

Lahiry, P., Lee, L. J., Frey, B. J., Rupar, C. A., Siu, V. M., Blencowe, B. J., & Hegele, R. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025400 · Cited by 12

Application of Adenosine Triphosphate Affinity Probe and Scheduled Multiple-Reaction Monitoring Analysis for Profiling Global Kinome in Human Cells in Response to Arsenite Treatment

Guo, L., Xiao, Y., & Wang, Y. (2014) · Analytical Chemistry · doi:10.1021/ac502592d · Cited by 12

Lighting Up T Lymphocyte Signaling with Quantitative Phosphoproteomics

Álvarez-Salamero, C., Castillo‐González, R., & Navarro, M. N. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00938 · Cited by 11

Enhancing kinase-inhibitor activity and selectivity prediction through contrastive learning

Tian, Y., Lu, R., Gong, X., Zhao, W., Li, Y., Wang, X., Jia, X., Li, Q., Yang, Y., Tong, H. H. Y., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65869-8 · Cited by 11

Characterizing the role of the dark kinome in neurodegenerative disease – A mini review

Axtman, A. D. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.130014 · Cited by 11

Kinome inhibition states and multiomics data enable prediction of cell viability in diverse cancer types

Berginski, M. E., Joisa, C. U., Golitz, B. T., & Gomez, S. M. (2023) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010888 · Cited by 11

Identification of Activated Cdc42-Associated Kinase Inhibitors as Potential Anticancer Agents Using Pharmacoinformatic Approaches

Kumar, V., Kumar, R., Parate, S., Danishuddin, M., Lee, G., Kwon, M., Jeong, S.-H., Ro, H., Lee, K. W., & Kim, S.-W. (2023) · Biomolecules · doi:10.3390/biom13020217 · Cited by 11

A patent review of BRAF inhibitors: 2013-2018

Wang, P., Qiu, H., & Zhu, H. (2019) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2019.1640680 · Cited by 11

Advances in kinome research of parasitic worms - implications for fundamental research and applied biotechnological outcomes

Stroehlein, A. J., Young, N. D., & Gasser, R. B. (2018) · Biotechnology Advances · doi:10.1016/j.biotechadv.2018.02.013 · Cited by 11

Exploring the Druggable Conformational Space of Protein Kinases Using AI-Generated StructuresPreprint

Herrington, N. B., Stein, D. F., Li, Y. C., Pandey, G. S., & Schlessinger, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.31.555779 · Cited by 11

Phosphorylierung reguliert den Membrantransport von Peptiden

Peng, S., Barba‐Bon, A., Pan, Y., Nau, W. M., Guo, D., & Hennig, A. (2017) · Angewandte Chemie · doi:10.1002/ange.201707979 · Cited by 10

Beyond expectations: investigating nilotinib’s potential in attenuating neurodegeneration in Alzheimer’s disease

Tocci, D. R., Fogel, M., Gupta, V., Kim, P. S.-H., Latimer, J. J., Adlimoghaddam, A., Robison, L. S., & Albensi, B. C. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01706-w · Cited by 13

Rigid Scaffolds Are Promising for Designing Macrocyclic Kinase Inhibitors

Zhao, Z., & Bourne, P. E. (2023) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00078 · Cited by 8

Therapeutic Potential of Protein Tyrosine Kinase 6 in Colorectal Cancer

Jerin, S., Harvey, A., & Lewis, A. (2023) · Cancers · doi:10.3390/cancers15143703 · Cited by 10

Opportunities and Challenges for Nutritional Proteomics in Cancer Prevention,

Romagnolo, D. F., & Milner, J. A. (2012) · Journal of Nutrition · doi:10.3945/jn.111.151803 · Cited by 10

Effects of multi and selective targeted tyrosine kinase inhibitors on function and signaling of different bladder cancer cells

Hänze, J., Kessel, F., Fazio, P. D., Hofmann, R. W., & Hegele, A. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.06.110 · Cited by 10

Ultrasensitive amplification-free detection of protein kinase based on catalyzed assembly and enumeration of gold nanoparticles

Tian, T., Yao, Y., Yang, B., Zhang, K., & Liu, B. (2019) · Chemical Communications · doi:10.1039/c9cc00131j · Cited by 10

Non-receptor Tyrosine Kinases Role and Significance in Hematological Malignancies

Azevedo, A. P., Silva, S., & Rueff, J. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.84873 · Cited by 9

Orthosteric and allosteric modulation of human kinases A mechanistic view

Mathur, P. (2020) · Frontiers in bioscience · doi:10.2741/4864 · Cited by 10

Large-Scale Label-Free Phosphoproteomics: from Technology to Data Interpretation

Guo, H., Isserlin, R., Lugowski, A., Kuzmanov, U., & Emili, A. (2014) · Bioanalysis · doi:10.4155/bio.14.188 · Cited by 10

Conceptual Thinking for In Silico Prioritization of Candidate Disease Genes

Tiffin, N. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-176-5_11 · Cited by 10

Approaches to identify kinase dependencies in cancer signalling networks

Dermit, M., Dokal, A. D., & Cutillas, P. R. (2017) · FEBS Letters · doi:10.1002/1873-3468.12748 · Cited by 10

KRSA: Network-based Prediction of Differential Kinase Activity from Kinome Array DataPreprint

DePasquale, E. A. K., Alganem, K., Bentea, E., Nawreen, N., McGuire, J. L., Naji, F., Hilhorst, R., Meller, J., & McCullumsmith, R. E. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.26.268581 · Cited by 10

Selective Identification of Allosteric Inhibitors and Co-Drug Combinations Targeting Kinases by Using a Nanopore Tweezer Approach

Li, F., Foster, J. C., Nguyen, L., & Chen, M. (2025) · ACS Nano · doi:10.1021/acsnano.5c07468 · Cited by 11

The role of kinases in peripheral nerve regeneration: mechanisms and implications

Zhang, X., Duan, X., & Liu, X. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1340845 · Cited by 9

Midgut‐enriched receptor protein tyrosine phosphatase PTP52F is required for Drosophila development during larva–pupa transition

Santhanam, A., Liang, S., Chen, D.-Y., Chen, G., & Meng, T. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08696.x · Cited by 9

Thiazolidinone Derivatives as Competitive Inhibitors of Protein Tyrosine Phosphatase 1B (PTP1B)

Aher, N. G., Kafle, B., & Cho, H. (2013) · Bulletin of the Korean Chemical Society · doi:10.5012/bkcs.2013.34.4.1275 · Cited by 9

Identification of a Tumor Specific, Active-Site Mutation in Casein Kinase 1α by Chemical Proteomics

Okerberg, E. S., Hainley, A., Brown, H., Aban, A., Alemayehu, S., Shih, A. Y.-J., Wu, J., Patricelli, M. P., Kozarich, J. W., Nomanbhoy, T. K., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152934 · Cited by 10

Modulation of Phosphopeptide Fragmentation via Dual Spray Ion/Ion Reactions Using a Sulfonate-Incorporating Reagent

Cotham, V. C., McGee, W. M., & Brodbelt, J. S. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b01901 · Cited by 9

The Encyclopedia of Proteome Dynamics: the KinoViewer

Brenes, A. J., & Lamond, A. I. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty823 · Cited by 8

Drugging the Undruggable: How Isoquinolines and PKA Initiated the Era of Designed Protein Kinase Inhibitor Therapeutics

Lorenz, R., Wu, J., Herberg, F. W., Taylor, S. S., & Engh, R. A. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00359 · Cited by 9

Identification of the Host Substratome of Leishmania-Secreted Casein Kinase 1 Using a SILAC-Based Quantitative Mass Spectrometry Assay

Smirlis, D., Dingli, F., Sabatet, V., Roth, A., Knippschild, U., Loew, D., Späth, G. F., & Rachidi, N. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.800098 · Cited by 9

Synthesis and Evaluation of Activity‐Based Probes Carrying a 5′‐Fluorosulfonylbenzoyl Adenosine Moiety for Protein Kinases

Hsu, Y., Yang, C., Lan, C., Lin, J., & Lo, L. (2013) · Journal of the Chinese Chemical Society · doi:10.1002/jccs.201300092 · Cited by 9

Cyclic Nucleotide-Directed Protein Kinases in Cardiovascular Inflammation and Growth

Holland, N. A., Francisco, J. T., Johnson, S., Morgan, J., Dennis, T., Gadireddy, N., & Tulis, D. A. (2018) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd5010006 · Cited by 10

Target-Triggered Polymerization of Branched DNA Enables Enzyme-free and Fast Discrimination of Single-Base Changes

Dong, Y., Yao, C., Wang, Z., Luo, D., & Yang, D. (2019) · iScience · doi:10.1016/j.isci.2019.10.029 · Cited by 9

A Structurally-Validated Multiple Sequence Alignment of 497 Human Protein Kinase DomainsPreprint

Modi, V., & Dunbrack, R. L. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/776740 · Cited by 9

Phosphorylation of the compartmentalized PKA substrate TAF15 regulates RNA–protein interactions

Feichtner, A., Enzler, F., Kugler, V., Hoppe, K., Mair, S., Kremser, L., Lindner, H., Huber, R. G., Stelzl, U., Stefan, E., et al. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05204-4 · Cited by 8

GPT4Kinase: High-accuracy prediction of inhibitor-kinase binding affinity utilizing large language model

Liu, K., Yu, X., Cui, H., Li, W., & Han, W. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137069 · Cited by 8

Modular bioengineered kinase sensors via scaffold protein-mediated split-luciferase complementation

Xu, X., Lemmens, L. J. M., den Hamer, A., Merkx, M., Ottmann, C., & Brunsveld, L. (2020) · Chemical Science · doi:10.1039/d0sc00074d · Cited by 8

Development of Kinase‐Centric Drugs: A Computational Perspective

Gajulapalli, V. P. R. (2023) · ChemMedChem · doi:10.1002/cmdc.202200693 · Cited by 8

Identifying Differences in Molecular Characteristics Relevant for Remodeling of Periodontal Ligament Stem Cells from the Upper and Lower Jaw

Malyaran, H., Craveiro, R. B., Mert, S., Niederau, C., Maas, S. L., van der Vorst, E. P. C., Hölzle, F., Jahnen‐Dechent, W., Wolf, M. F., & Neuß, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063207 · Cited by 8

Exploring Missense Mutations in Tyrosine Kinases Implicated with Neurodegeneration

Sami, N., Kumar, V., Islam, A., Ali, S., Ahmad, F., & Hassan, M. I. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0046-5 · Cited by 9

Accessing isotopically labeled proteins containing genetically encoded phosphoserine for NMR with optimized expression conditions

Vesely, C. H., Reardon, P. N., Yu, Z., Barbar, E. J., Mehl, R. A., & Cooley, R. B. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102613 · Cited by 8

Kinase inhibitors for cancer alter metabolism, blood glucose, and insulin

Duggan, B. M., Marko, D. M., Muzaffar, R., Chan, D. Y., & Schertzer, J. D. (2022) · Journal of Endocrinology · doi:10.1530/joe-22-0212 · Cited by 8

Design, synthesis, and evaluation of cell permeable probes for protein kinases

Hsu, Y.-L., Yang, C.-C., Chou, T., Tai, C., Chen, L.-Y., Fu, S., Lin, J., & Lo, L. (2015) · Tetrahedron · doi:10.1016/j.tet.2015.10.053 · Cited by 8

Effect of Glucuronidation on the Potential of Kaempferol To Inhibit Serine/Threonine Protein Kinases

Beekmann, K., de Haan, L. H. J., Actis‐Goretta, L., van BLADEREN, P. J., & Rietjens, I. M. C. M. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b05456 · Cited by 8

A computational protocol to evaluate the effects of protein mutants in the kinase gatekeeper position on the binding of ATP substrate analogues

Romano, V. C., de Beer, T., & Schwede, T. F. (2017) · BMC Research Notes · doi:10.1186/s13104-017-2428-9 · Cited by 10

Phosphoproteomics Meets Chemical Genetics: Approaches for Global Mapping and Deciphering the Phosphoproteome

Jurcik, J., Siváková, B., Čipáková, I., Selicky, T., Stupenova, E., Jurcik, M., Osadská, M., Baráth, P., & Čipák, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207637 · Cited by 10

The unusual mechanism of inhibition of the p90 ribosomal S6 kinase (RSK) by flavonol rhamnosides

Utepbergenov, D., & Derewenda, Z. S. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.03.018 · Cited by 7

SHP2 ablation mitigates osteoarthritic cartilage degeneration by promoting chondrocyte anabolism through SOX9

Wang, L., Yang, H., Wang, C., Wang, M., Huang, J., Nyunt, T., Osorio, C., Sun, S., Pacifici, M., Lefebvre, V., et al. (2024) · The FASEB Journal · doi:10.1096/fj.202400642r · Cited by 7

Kinase–inhibitor binding affinity prediction with pretrained graph encoder and language model

Guo, X., Ran, Z., & Li, F. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf338 · Cited by 7

wKinMut: An integrated tool for the analysis and interpretation of mutations in human protein kinases

Izarzugaza, J. M. G., Vázquez, M., del Pozo, Á., & Valencia, A. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-345 · Cited by 7

Combination Kinase Inhibitor Treatment Suppresses Rift Valley Fever Virus Replication

Bell, T. M., Espina, V. A., Lundberg, L., Pinkham, C., Brahms, A., Carey, B. D., Lin, S., Dahal, B., Lehman, C. W., de la Fuente, C., et al. (2018) · Viruses · doi:10.3390/v10040191 · Cited by 7

KSP: an integrated method for predicting catalyzing kinases of phosphorylation sites in proteins

Ma, H., Li, G., & Su, Z. (2020) · BMC Genomics · doi:10.1186/s12864-020-06895-2 · Cited by 7

Multi-omics analysis identifies drivers of protein phosphorylationPreprint

Zhang, T., Keele, G. R., Gyuricza, I. G., Vincent, M. J., Brunton, C., Bell, T. A., Hock, P., Shaw, G. D., Munger, S. C., de Villena, F. P., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.03.494740 · Cited by 7

Analysis of DYRK1B, PPARG, and CEBPB Expression Patterns in Adipose-Derived Stem Cells from Patients Carrying DYRK1B R102C and Healthy Individuals During Adipogenesis

Armanmehr, A., Khamirani, H. J., Zoghi, S., & Dianatpour, M. (2022) · Metabolic Syndrome and Related Disorders · doi:10.1089/met.2021.0140 · Cited by 6

Impact of protein and small molecule interactions on kinase conformations

Kugler, V., Schwaighofer, S., Feichtner, A., Enzler, F., Fleischmann, J., Strich, S. L., Schwarz, S., Wilson, R., Tschaikner, P., Troppmair, J., et al. (2024) · eLife · doi:10.7554/elife.94755 · Cited by 6

Chemical coverage of human biological pathways

Kwak, H. A., Liu, L., Tredup, C., Röhm, S., Prinos, P., Böttcher, J., & Schapira, M. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104144 · Cited by 6

Site-Specific Competitive Kinase Inhibitor Target Profiling Using Phosphonate Affinity Tags

van Bergen, W., Nederstigt, A. E., Heck, A. J. R., & Baggelaar, M. P. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.100906 · Cited by 6

PTPN11 in cartilage development, adult homeostasis, and diseases

Yang, W., & Lefebvre, V. (2025) · Bone Research · doi:10.1038/s41413-025-00425-0 · Cited by 8

Typical and atypical domain combinations in human protein kinases: functions, disease causing mutations and conservation in other primates

Rakshambikai, R., Malini, M., Mutharasu, G., & Srinivasan, N. (2015) · RSC Advances · doi:10.1039/c4ra11685b · Cited by 6

Identification of phosphorylated small ORF-encoded peptides in Hep3B cells by LC/MS/MS

Peng, M., Zhou, Y., & Wan, C. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105214 · Cited by 6

Protein sector analysis for the clustering of disease-associated mutations

Guevara-Coto, J. A., Schwartz, C. E., & Wang, L. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-s11-s4 · Cited by 6

Phosphoproteomics-Based Characterization of Prostaglandin E2 Signaling in T Cells

Lone, A. M., & Taskén, K. (2021) · Molecular Pharmacology · doi:10.1124/molpharm.120.000170 · Cited by 6

Validation of ion mobility spectrometry ‐ mass spectrometry as a screening tool to identify type II kinase inhibitors of FGFR1 kinase

Beeston, H. S., Klein, T., Norman, R. A., Tucker, J. A., Anderson, M., Ashcroft, A. E., & Holdgate, G. A. (2021) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.9130 · Cited by 6

Recent Advances in Pyrazole-based Protein Kinase Inhibitors as Emerging Therapeutic Targets

Çetin, A. (2023) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/0113862073252211231024182817 · Cited by 5

Improved Methods for Recording Accurate Collision Cross Sections Using Cyclic Ion Mobility-Mass Spectrometry

Makey, D. M., Langridge, D., Richardson, K., Schroeder, R., Ujma, J., Giles, K., & Ruotolo, B. T. (2026) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.6c00022 · Cited by 5

Allosteric changes in the conformational landscape of Src kinase upon substrate binding

Chong, S., Oshima, H., & Sugita, Y. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168871 · Cited by 5

Rapid Identification of Inhibitors and Prediction of Ligand Selectivity for Multiple Proteins: Application to Protein Kinases

Ma, Z., Huang, S., Cheng, F., & Zou, X. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00016 · Cited by 5

Innovative strategies for measuring kinase activity to accelerate the next wave of novel kinase inhibitors

Veth, T. S., Kannegieter, N. M., de Graaf, E. L., Ruijtenbeek, R., Joore, J., Ressa, A., & Altelaar, M. A. F. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.103907 · Cited by 5

Stimulation of insulin secretion induced by low 4-cresol dose involves the RPS6KA3 signalling pathway

Brial, F., Puel, G., Gonzalez, L., Russick, J., Auld, D. S., Lathrop, M. G., Poirier, R., Matsuda, F., & Gauguier, D. (2024) · PLoS ONE · doi:10.1371/journal.pone.0310370 · Cited by 5

Cyclic Peptides as Protein Kinase Modulators and Their Involvement in the Treatment of Diverse Human Diseases

Alcantar, L. M., Hernández-Padilla, L., Díaz-Pérez, A. L., Villalón-Magallán, L. G., Durán-Maldonado, M. X., Díaz‐Pérez, C., Campos-Morales, M. E., Figueroa-Guzmán, C., & Campos‐García, J. (2024) · Kinases and Phosphatases · doi:10.3390/kinasesphosphatases2040023 · Cited by 5

KIF18A Is a Novel Target of JNK1/c‐Jun Signaling Pathway Involved in Cervical Tumorigenesis

Wang, Y., Zhou, B., Lian, X., Yu, S., Huang, B., Wu, X., Wen, L., & Zhu, C. (2025) · Journal of Cellular Physiology · doi:10.1002/jcp.31516 · Cited by 5

Putting a bit into the polo-box domain of polo-like kinase 1

Park, J., Kim, T.-S., Meng, L., Bang, J. K., Kim, B. Y., & Lee, K. S. (2015) · Journal of Analytical Science & Technology · doi:10.1186/s40543-015-0069-y · Cited by 5

Development of the first model of a phosphorylated, ATP/Mg 2+ -containing B-Raf monomer by molecular dynamics simulations: a tool for structure-based design

Previtali, V., Trujillo, C., Boisson, J.-C., Khartabil, H. K., Hénon, É., & Rozas, I. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp05038k · Cited by 5

Tumor-Targeting Agents

Chakraborty, D., Das, A., & Bal, C. S. (2021) · Springer eBooks · doi:10.1007/978-3-030-81261-4_9 · Cited by 5

Real‐Time Monitoring of Phosphorylation Kinetics with Self‐Assembled Nano‐oscillators

Fang, Y., Chen, S., Wang, W., Shan, X., & Tao, N. J. (2015) · Angewandte Chemie · doi:10.1002/ange.201411040 · Cited by 5

Kinase Inhibitor Drugs

Wu, P., & Choudhary, A. (2018) · Wiley eBooks · doi:10.1002/9783527808694.ch3 · Cited by 5

Revitalizing PI3K Inhibitors for PET/CT Imaging and Radionuclide Therapy of Multiple Cancers

Huang, H., Peng, S., Zuo, Q., Zhang, S., Wu, J., Zhang, Y., Chen, X., Lu, Q., Hu, Q., Jiang, S., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03583 · Cited by 4

Illuminating the dark kinome: utilizing multiplex peptide activity arrays to functionally annotate understudied kinases

Hamoud, A.-R. A., Alganem, K., Hanna, S., Morran, M. P., Henkel, N., Imami, A. S., Ryan, W. G., Sahay, S., Pulvender, P., Kunch, A., et al. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01868-4 · Cited by 4

Protein tyrosine phosphatase delta is a STAT3-phosphatase and suppressor of metabolic liver disease

Suarez, A. A. R., Jühling, F., Moehlin, J., Mailly, L., Virzì, A., Brignon, N., Durand, S. C., Oudot, M. A., Schaeffer, E., Martin, R., et al. (2025) · eGastroenterology · doi:10.1136/egastro-2024-100159 · Cited by 6

Novel Small Molecule Inhibitors of Cyclin-dependent Kinases as Anticancer Agents

Srivastava, N., & Saxena, A. K. (2025) · Current Medicinal Chemistry · doi:10.2174/0109298673331685241205180307 · Cited by 5

Identification of Novel Kinase–Transcription Factor–mRNA–miRNA Regulatory Network in Nasopharyngeal Carcinoma by Bioinformatics Analysis

Gao, L., Zhou, L., & Huang, X. (2021) · International Journal of General Medicine · doi:10.2147/ijgm.s327657 · Cited by 4

Comparative Atomistic Insights on Apo and ATP-I1171N/S/T in Nonsmall-Cell Lung Cancer

Balasundaram, A., & Doss, C. G. P. (2023) · ACS Omega · doi:10.1021/acsomega.3c05785 · Cited by 4

Cancer Biology and the Principles of Targeted Cancer Drug Discovery

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