Cited by 429Genomics and Rare DiseasesProtein Kinase Regulation and GTPase SignalingProtein Tyrosine Phosphatases

The DOI matches its Crossref record; 126 of the 126 references it cites were found in a registry or an index.

Kinase mutations in human disease: interpreting genotype–phenotype relationships

Lahiry, Piya, Torkamani, Ali, Schork, Nicholas J., Hegele, Robert A.·2010·Nature Reviews Genetics

Open this paper in CoChat — free account

Abstract

Protein kinases are one of the largest families of evolutionarily related proteins and comprise one of the most abundant gene families in humans. Here we survey kinase gene mutations from the perspective of human disease phenotypes and further analyse the structural features of mutant kinases, including mutational hotspots. Our evaluation of the genotype-phenotype relationship across 915 human kinase mutations - that underlie 67 single-gene diseases, mainly inherited developmental and metabolic disorders and also certain cancers - enhances our understanding of the role of kinases in development, kinase dysfunction in pathogenesis and kinases as potential targets for therapy.

Integrity signals

Registry

Crossref · 10.1038/nrg2707

Cites

126 of 126 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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

Show all 125 references

Sorted by citations

Angiogenic signaling pathways and anti-angiogenic therapy for cancer
Liu, Z., Chen, H., Zheng, L., Sun, L., & Shi, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01460-1 · Cited by 1,486
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
Trends in kinase drug discovery: targets, indications and inhibitor design
Attwood, M. M., Fabbro, D., Sokolov, A. V., Knapp, S., & Schiöth, H. B. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00252-y · Cited by 850
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
The potential health effects of dietary phytoestrogens
Rietjens, I. M. C. M., Louisse, J., & Beekmann, K. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13622 · Cited by 512
The functional landscape of the human phosphoproteome
Ochoa, D., Jarnuczak, A. F., Viéitez, C., Gehre, M., Soucheray, M., Mateus, A., Kleefeldt, A. A., Hill, A., Garcia-Alonso, L., Stein, F., et al. (2020) · Nature Biotechnology · doi:10.1038/s41587-019-0344-3 · Cited by 491
Statistical analysis strategies for association studies involving rare variants
Bansal, V., Libiger, O., Torkamani, A., & Schork, N. J. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2867 · Cited by 455
Self-citation
Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery
Papaleo, E., Saladino, G., Lambrughi, M., Lindorff‐Larsen, K., Gervasio, F. L., & Nussinov, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00623 · Cited by 434
Ten things you should know about protein kinases: IUPHAR R eview 14
Fabbro, D., Cowan‐Jacob, S. W., & Möbitz, H. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13096 · Cited by 365
Advances in covalent kinase inhibitors
Abdeldayem, A., Raouf, Y. S., Constantinescu, S. N., Moriggl, R., & Gunning, P. T. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00720b · Cited by 337
Mapping differential interactomes by affinity purification coupled with data-independent mass spectrometry acquisition
Lambert, J.-P., Ivosev, G., Couzens, A. L., Larsen, B., Taipale, M., Lin, Z.-Y., Zhong, Q., Lindquist, S., Vidal, M., Aebersold, R., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2702 · Cited by 318
Small Molecule Kinase Inhibitor Drugs (1995–2021): Medical Indication, Pharmacology, and Synthesis
Ayala-Aguilera, C. C., Valero, T., Lorente‐Macías, Á., Baillache, D. J., Croke, S., & Unciti‐Broceta, A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00963 · Cited by 294
iSNO-AAPair: incorporating amino acid pairwise coupling into PseAAC for predicting cysteineS-nitrosylation sites in proteins
Xu, Y., Shao, X., Wu, L., Deng, N.-Y., & Chou, K. (2013) · PeerJ · doi:10.7717/peerj.171 · Cited by 272
Conformational states dynamically populated by a kinase determine its function
Xie, T., Saleh, T., Rossi, P., & Kalodimos, C. G. (2020) · Science · doi:10.1126/science.abc2754 · Cited by 266
Protein kinase signaling networks in cancer
Brognard, J., & Hunter, T. R. (2010) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2010.10.012 · Cited by 246
Overcoming ABC transporter-mediated multidrug resistance: The dual role of tyrosine kinase inhibitors as multitargeting agents
Beretta, G. L., Cassinelli, G., Pennati, M., Zuco, V., & Gatti, L. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.07.062 · Cited by 239
The Protein Interaction Landscape of the Human CMGC Kinase Group
Varjosalo, M. T., Keskitalo, S., van Drogen, A., Nurkkala, H., Vichalkovski, A., Aebersold, R. H., & Gstaiger, M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.027 · Cited by 235
Systematic Analysis of Protein Phosphorylation Networks From Phosphoproteomic Data
Song, C., Ye, M., Liu, Z., Cheng, H., Jiang, X., Han, G., Songyang, Z., Tan, Y., Wang, H., Ren, J. M., et al. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.012625 · Cited by 196
Mechanisms of drug resistance in kinases
Barouch‐Bentov, R., & Sauer, K. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2011.546344 · Cited by 192
Global proteomic assessment of the classical protein-tyrosine phosphatome and “Redoxome”
Karisch, R., Fernandez, M., Taylor, P., Virtanen, C., St-Germain, J. R., Jin, L. L., Harris, I. S., Mori, J., Mak, T. W., Senis, Y. A., et al. (2011) · Cell · doi:10.1016/j.cell.2011.07.020 · Cited by 179
A Structurally-Validated Multiple Sequence Alignment of 497 Human Protein Kinase Domains
Modi, V., & Dunbrack, R. L. (2019) · Scientific Reports · doi:10.1038/s41598-019-56499-4 · Cited by 171
Taking aim at Mer and Axl receptor tyrosine kinases as novel therapeutic targets in solid tumors
Linger, R. M. A., Keating, A. K., Earp, H. S., & Graham, D. K. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.515980 · Cited by 171
Biological targets and mechanisms of action of natural products from marine cyanobacteria
Salvador‐Reyes, L. A., & Luesch, H. (2015) · Natural Product Reports · doi:10.1039/c4np00104d · Cited by 168
Unlocking the Transcriptomes of Two Carcinogenic Parasites, Clonorchis sinensis and Opisthorchis viverrini
Young, N. D., Campbell, B. E., Hall, R. S., Jex, A. R., Cantacessi, C., Laha, T., Sohn, W., Sripa, B., Loukas, A. C., Brindley, P. J., et al. (2010) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0000719 · Cited by 151
Molecular hybrids: A five-year survey on structures of multiple targeted hybrids of protein kinase inhibitors for cancer therapy
Soltan, O. M., Shoman, M. E., Abdel‐Aziz, S. A., Narumi, A., Konno, H., & Abdel‐Aziz, M. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113768 · Cited by 150
INstruct: a database of high-quality 3D structurally resolved protein interactome networks
Meyer, M. J., Das, J., Wang, X., & Yu, H. (2013) · Bioinformatics · doi:10.1093/bioinformatics/btt181 · Cited by 144
Superbinder SH2 Domains Act as Antagonists of Cell Signaling
Kaneko, T., Huang, H., Cao, X., Li, X., Li, C., Voss, C., Sidhu, S. S., & Li, S. S. ‐. (2012) · Science Signaling · doi:10.1126/scisignal.2003021 · Cited by 137
A Pan-Cancer Catalogue of Cancer Driver Protein Interaction Interfaces
Porta‐Pardo, E., García‐Alonso, L., Hrabe, T., Dopazo, J., & Godzik, A. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004518 · Cited by 127
Role of Non Receptor Tyrosine Kinases in Hematological Malignances and its Targeting by Natural Products
Siveen, K. S., Prabhu, K. S., Achkar, I. W., Kuttikrishnan, S., Shyam, S., Khan, A. Q., Merhi, M., Dermime, S., & Shahab Uddin, M. S. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0788-y · Cited by 137
Unraveling the Anticancer Effect of Curcumin and Resveratrol
Pavan, A. R., Silva, G., Jornada, D. H., Chiba, D. E., Fernandes, G., Chin, C. M., & dos Santos, J. L. (2016) · Nutrients · doi:10.3390/nu8110628 · Cited by 130
Determining Cysteines Available for Covalent Inhibition Across the Human Kinome
Zhao, Z., Liu, Q., Bliven, S. E., Xie, L., & Bourne, P. E. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01815 · Cited by 128
Kinase Inhibitors and Kinase-Targeted Cancer Therapies: Recent Advances and Future Perspectives
Li, J., Chen, G., Zhou, H., Liu, J., Xia, X., Ha, W., Jiang, Y., Liu, Q., & Xiong, H. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25105489 · Cited by 135
Recent Advances and New Strategies in Targeting Plk1 for Anticancer Therapy
Lee, K. S., Burke, T. R., Park, J., Bang, J. K., & Lee, E. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.013 · Cited by 127
Cancer Risk Among Patients With Myotonic Muscular Dystrophy
Gadalla, S. M., Lund, M., Pfeiffer, R. M., Gørtz, S., Mueller, C. M., Moxley, R. T., Kristinsson, S. Y., Björkholm, M., Shebl, F. M., Hilbert, J. E., et al. (2011) · JAMA · doi:10.1001/jama.2011.1796 · Cited by 122
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases
Buljan, M., Ciuffa, R., van Drogen, A., Vichalkovski, A., Mehnert, M., Rosenberger, G., Lee, S., Varjosalo, M. T., Pernas, L. E., Spegg, V., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.001 · Cited by 118
The Human Kinome and Kinase Inhibition
Duong‐Ly, K. C., & Peterson, J. R. (2013) · Current Protocols in Pharmacology · doi:10.1002/0471141755.ph0209s60 · Cited by 116
Molecular Spies in Action: Genetically Encoded Fluorescent Biosensors Light up Cellular Signals
Gest, A. M. M., Sahan, A. Z., Zhong, Y., Lin, W., Mehta, S., & Zhang, J. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00293 · Cited by 112
Chemical and biology of sulfur fluoride exchange (SuFEx) click chemistry for drug discovery
Lucas, S. W., Qin, R. Z., Rakesh, K. P., Kumar, K. S. S., & Qin, H. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106227 · Cited by 109
Global and Site-Specific Effect of Phosphorylation on Protein Turnover
Wu, C., Ba, Q., Lu, D., Li, W., Šalovská, B., Hou, P., Mueller, T., Rosenberger, G., Gao, E., Di, Y., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.10.025 · Cited by 97
Genetic Code Expansion in Animals
Brown, W., Liu, J., & Deiters, A. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00520 · Cited by 94
DYRK1A: a down syndrome-related dual protein kinase with a versatile role in tumorigenesis
Laham, A. J., Saber-Ayad, M. M., & El‐Awady, R. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03626-4 · Cited by 95
Compounds from Natural Sources as Protein Kinase Inhibitors
Baier, A., & Szyszka, R. (2020) · Biomolecules · doi:10.3390/biom10111546 · Cited by 96
Raman Spectroscopy to Diagnose Alzheimer’s Disease and Dementia with Lewy Bodies in Blood
Paraskevaidi, M., Morais, C. L. M., Halliwell, D. E., Mann, D. M. A., Allsop, D., Martin‐Hirsch, P. L., & Martin, F. L. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00198 · Cited by 90
Phosphotyrosine recognition domains: the typical, the atypical and the versatile
Kaneko, T., Joshi, R., Feller, S. M., & Li, S. S. ‐. (2012) · Cell Communication and Signaling · doi:10.1186/1478-811x-10-32 · Cited by 93
Receptor tyrosine kinases: biological functions and anticancer targeted therapy
Zhang, N., & Li, Y. (2023) · MedComm · doi:10.1002/mco2.446 · Cited by 97
Receptor tyrosine kinase mutations in developmental syndromes and cancer: two sides of the same coin
McDonell, L. M., Kernohan, K. D., Boycott, K. M., & Sawyer, S. L. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv254 · Cited by 86
Phosphoproteomic Analysis of Neonatal Regenerative Myocardium Revealed Important Roles of Checkpoint Kinase 1 via Activating Mammalian Target of Rapamycin C1/Ribosomal Protein S6 Kinase b-1 Pathway
Fan, Y., Cheng, Y., Li, Y., Chen, B., Wang, Z., Wei, T., Zhang, H., Guo, Y., Wang, Q., Wei, Y., et al. (2020) · Circulation · doi:10.1161/circulationaha.119.040747 · Cited by 86
A subcellular map of the human kinome
Zhang, H., Cao, X., Tang, M., Zhong, G., Si, Y., Li, H., Zhu, F., Liao, Q., Li, L., Zhao, J., et al. (2021) · eLife · doi:10.7554/elife.64943 · Cited by 88
Phosphorylation‐Responsive Membrane Transport of Peptides
Peng, S., Barba‐Bon, A., Pan, Y., Nau, W. M., Guo, D., & Hennig, A. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201707979 · Cited by 80
Comprehensive Analysis of Constraint on the Spatial Distribution of Missense Variants in Human Protein Structures
Sivley, R. M., Kropski, J., Sheehan, J., Cogan, J., Dou, X., Blackwell, T. S., Phillips, J., Meiler, J., Bush, W. S., & Capra, J. A. (2018) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2018.01.017 · Cited by 76
dbPAF: an integrative database of protein phosphorylation in animals and fungi
Ullah, S., Lin, S., Xu, Y., Deng, W., Ma, L., Zhang, Y. W., Liu, Z., & Xue, Y. (2016) · Scientific Reports · doi:10.1038/srep23534 · Cited by 77
Evolution of protein kinase substrate recognition at the active site
Bradley, D. T. C., & Beltrão, P. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000341 · Cited by 75
Kinase Inhibitors as Underexplored Antiviral Agents
García-Cárceles, J., Caballero, E., Gil, C., & Martínez, A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00302 · Cited by 75
Germline mutations in ABL1 cause an autosomal dominant syndrome characterized by congenital heart defects and skeletal malformations
Wang, X., Charng, W., Chen, C., Rosenfeld, J. A., Shamsi, A. A., Al‐Gazali, L., McGuire, M., Mew, N. A., Arnold, G. L., Qu, C., et al. (2017) · Nature Genetics · doi:10.1038/ng.3815 · Cited by 74
Lost Branches on the Tree of Life
Drew, B. T., Gazis, R. O., Cabezas, P., Swithers, K. S., Deng, J., Rodriguez, R., Katz, L. A., Crandall, K. A., Hibbett, D. S., & Soltis, P. S. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001636 · Cited by 70
Manipulation of Endogenous Kinase Activity in Living Cells Using Photoswitchable Inhibitory Peptides
Yi, J. J., Wang, H., Vilela, M., Danuser, G. M., & Hahn, K. M. (2014) · ACS Synthetic Biology · doi:10.1021/sb5001356 · Cited by 73
DFGmodel: Predicting Protein Kinase Structures in Inactive States for Structure-Based Discovery of Type-II Inhibitors
Ung, P. M. U., & Schlessinger, A. (2014) · ACS Chemical Biology · doi:10.1021/cb500696t · Cited by 75
Exploiting polypharmacology for improving therapeutic outcome of kinase inhibitors (KIs): An update of recent medicinal chemistry efforts
Ma, X., Lv, X., & Zhang, J. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.11.049 · Cited by 71
A Combined Approach Reveals a Regulatory Mechanism Coupling Src’s Kinase Activity, Localization, and Phosphotransferase-Independent Functions
Ahler, E., Register, A. C., Chakraborty, S., Fang, L., Dieter, E. M., Sitko, K. A., Vidadala, R. S. R., Trevillian, B. M., Golkowski, M. G., Gelman, H., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.02.003 · Cited by 74
Spatiotemporally resolved subcellular phosphoproteomics
Liu, Y., Zeng, R., Wang, R., Weng, Y., Wang, R., Zou, P., & Chen, P. R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2025299118 · Cited by 68
De Novo Missense Substitutions in the Gene Encoding CDK8, a Regulator of the Mediator Complex, Cause a Syndromic Developmental Disorder
Calpena, E., Hervieu, A., Kaserer, T., Swagemakers, S. M. A., Goos, J. A. C., Adeniji-Popoola, O., Ortiz-Ruiz, M. J., Barbaro‐Dieber, T., Bownass, L., Brilstra, E. H., et al. (2019) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2019.02.006 · Cited by 64
A novel signalling screen demonstrates that CALR mutations activate essential MAPK signalling and facilitate megakaryocyte differentiation
Kollmann, K., Warsch, W., Arias, C. G., Nice, F. L., Avezov, E., Milburn, J. V., Li, J., Dimitropoulou, D., Biddie, S. C., Wang, M., et al. (2016) · Leukemia · doi:10.1038/leu.2016.280 · Cited by 62
MICAL-1 Is a Negative Regulator of MST-NDR Kinase Signaling and Apoptosis
Zhou, Y., Adolfs, Y., Pijnappel, W. W. M. P., Fuller, S. J., van der Schors, R. C., Li, K. W., Sugden, P. H., Smit, A. B., Hergovich, A., & Pasterkamp, R. J. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01389-10 · Cited by 64
A Summary of Computational Resources for Protein Phosphorylation
Xue, Y., Gao, X., Cao, J., Liu, Z., Jin, C., Wen, L., Yao, X., & Ren, J. M. (2010) · Current Protein and Peptide Science · doi:10.2174/138920310791824138 · Cited by 61
Recent developments in receptor tyrosine kinase inhibitors: A promising mainstay in targeted cancer therapy
Kumar, R., Goel, H., Solanki, R., Rawat, L., Tabasum, S., Tanwar, P., Pal, S., & Sabarwal, A. (2024) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2024.100195 · Cited by 65
ProKinO: A Unified Resource for Mining the Cancer Kinome
McSkimming, D. I., Dastgheib, S., Talevich, E., Narayanan, A., Katiyar, S., Taylor, S. S., Kochut, K. J., & Kannan, N. (2014) · Human Mutation · doi:10.1002/humu.22726 · Cited by 56
Silmitasertib (CX-4945), a Clinically Used CK2-Kinase Inhibitor with Additional Effects on GSK3β and DYRK1A Kinases: A Structural Perspective
Grygier, P., Pustelny, K., Nowak, J., Golik, P., Popowicz, G. M., Plettenburg, O., Dubin, G., Menezes, F., & Czarna, A. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01887 · Cited by 64
Epidermal Growth Factor Receptor Tyrosine Kinase Inhibitors in Cancer: Current Use and Future Prospects
Dickerson, H., Diab, A. I., & Musaimi, O. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251810008 · Cited by 68
Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases
Meharena, H. S., Fan, X., Ahuja, L. G., Keshwani, M. M., McClendon, C. L., Chen, A. M., Adams, J. A., & Taylor, S. S. (2016) · PLoS Biology · doi:10.1371/journal.pbio.2000127 · Cited by 56
Chemotherapy Induced Cardiotoxicity: A State of the Art Review on General Mechanisms, Prevention, Treatment and Recent Advances in Novel Therapeutics
Abdul‐Rahman, T., Dunham, A. J., Huang, H., Bukhari, S. M. A., Mehta, A., Awuah, W. A., Ede-Imafidon, D., Cantu‐Herrera, E., Talukder, S., Joshi, A. M., et al. (2023) · Current Problems in Cardiology · doi:10.1016/j.cpcardiol.2023.101591 · Cited by 59
How Reactive are Druggable Cysteines in Protein Kinases?
Awoonor‐Williams, E., & Rowley, C. N. (2018) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00454 · Cited by 57
MAPK pathway and B cells overactivation in multiple sclerosis revealed by phosphoproteomics and genomic analysis
Kotelnikova, E. A., Kiani, N. A., Messinis, D. E., Pertsovskaya, I., Pliaka, V., Bernardo-Faura, M., Rinas, M., Vila, G., Zubizarreta, I., Pulido-Valdeolivas, I., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818347116 · Cited by 58
Exploring Polypharmacology in Drug Discovery and Repurposing Using the CANDO Platform
Chopra, G., & Samudrala, R. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160325121943 · Cited by 55
EKPD: a hierarchical database of eukaryotic protein kinases and protein phosphatases
Wang, Y., Liu, Z., Cheng, H., Gao, T., Pan, Z., Yang, Q., Guo, A., & Xue, Y. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1121 · Cited by 55
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 International Edition · doi:10.1002/anie.201411040 · Cited by 54
Receptor tyrosine kinases in PI3K signaling: The therapeutic targets in cancer
Jiang, W., & Ji, M. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.03.006 · Cited by 55
Analysis of protein phosphorylation using Phos-tag gels
O’Donoghue, L., & Smolenski, A. (2022) · Journal of Proteomics · doi:10.1016/j.jprot.2022.104558 · Cited by 50
AKTivation mechanisms
Cole, P. A., Chu, N. K., Salguero, A. L., & Bae, H. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.02.004 · Cited by 52
Insights into the binding mode of MEK type-III inhibitors. A step towards discovering and designing allosteric kinase inhibitors across the human kinome
Zhao, Z., Xie, L., & Bourne, P. E. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179936 · Cited by 48
Methods to monitor classical protein‐tyrosine phosphatase oxidation
Karisch, R., & Neel, B. G. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08626.x · Cited by 46
Arena3D: visualizing time-driven phenotypic differences in biological systems
Secrier, M., Pavlopoulos, G. A., Aerts, J. A., & Schneider, R. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-45 · Cited by 49
Nanomedicine of tyrosine kinase inhibitors
Šmídová, V., Michálek, P., Goliášová, Z., Eckschlager, T., Hodek, P., Adam, V., & Heger, Z. (2020) · Theranostics · doi:10.7150/thno.48662 · Cited by 49
Insights into Aurora-A Kinase Activation Using Unnatural Amino Acids Incorporated by Chemical Modification
Rowan, F. C., Richards, M., Bibby, R. A., Thompson, A., Bayliss, R. W., & Blagg, J. (2013) · ACS Chemical Biology · doi:10.1021/cb400425t · Cited by 46
Correlates of tumor development in patients with myotonic dystrophy
Das, M., Moxley, R. T., Hilbert, J. E., Martens, W. B., Letren, L., Greene, M. H., & Gadalla, S. M. (2012) · Journal of Neurology · doi:10.1007/s00415-012-6476-8 · Cited by 45
Comparison of FDA Approved Kinase Targets to Clinical Trial Ones: Insights from Their System Profiles and Drug-Target Interaction Networks
Xu, J., Wang, P., Yang, H. J., Zhou, J., Li, Y., Li, X., Xue, W., Yu, C., Tian, Y., & Zhu, F. (2016) · BioMed Research International · doi:10.1155/2016/2509385 · Cited by 45
Ultrasensitive Detection of Enzymatic Activity Using Single Molecule Arrays
Wang, X., Ogata, A. F., & Walt, D. R. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c06599 · Cited by 44
Overexpression of MICAL2, a novel tumor-promoting factor, accelerates tumor progression through regulating cell proliferation and EMT
Cai, Y., Lu, J., & Tang, F. (2018) · Journal of Cancer · doi:10.7150/jca.22355 · Cited by 41
Development and Applications of Chimera Platforms for Tyrosine Phosphorylation
Pergu, R., Shoba, V. M., Chaudhary, S. K., Godage, D. N. P. M., Deb, A., Singha, S., Dhawa, U., Singh, P. R., Anokhina, V. S., Singh, S., et al. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00200 · Cited by 41
DYRK1B mutations associated with metabolic syndrome impair the chaperone-dependent maturation of the kinase domain
Jhaisha, S. A., Widowati, E. W., Kii, I., Sonamoto, R., Knapp, S., Papadopoulos, C., & Becker, W. B. (2017) · Scientific Reports · doi:10.1038/s41598-017-06874-w · Cited by 41
Genetic and pharmacological inhibition of TTK impairs pancreatic cancer cell line growth by inducing lethal chromosomal instability
Stratford, J. K., Yan, F., Hill, R. A., Major, M. B., Graves, L. M., Der, C. J., & Yeh, J. J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174863 · Cited by 38
High-Throughput Assessment of Kinome-Wide Activation States
Schmidlin, T., Debets, D. O., van Gelder, C. A. G. H., Stecker, K. E., Rontogianni, S., van den Eshof, B. L., Kemper, K., Lips, E. H., van den Biggelaar, M., Peeper, D. S., et al. (2018) · Cell Systems · doi:10.1016/j.cels.2019.08.005 · Cited by 36
Molecular mechanisms of resistance to kinase inhibitors in thyroid cancers
Hofmann, M.-C. C., Kunnimalaiyaan, M., Wang, J. R., Busaidy, N. L., Sherman, S. I., Lai, S. Y., Zafereo, M., & Cabanillas, M. E. (2022) · Endocrine Related Cancer · doi:10.1530/erc-22-0129 · Cited by 39
Emerging Roles of DYRK Kinases in Embryogenesis and Hedgehog Pathway Control
Singh, R. K., & Lauth, M. (2017) · Journal of Developmental Biology · doi:10.3390/jdb5040013 · Cited by 37
Role of tyrosine kinases in bladder cancer progression: an overview
Zangouei, A. S., Barjasteh, A. H., Rahimi, H. R., Mojarrad, M., & Moghbeli, M. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00625-7 · Cited by 37
Inhibitory Member of the Apoptosis-stimulating Proteins of the p53 Family (iASPP) Interacts with Protein Phosphatase 1 via a Noncanonical Binding Motif
Llanos, S., Royer, C., Lu, M. M., Bergamaschi, D., Lee, W. H., & Lü, X. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.270751 · Cited by 35
A New Challenging and Promising Era of Tyrosine Kinase Inhibitors
Cui, J. J. (2014) · ACS Medicinal Chemistry Letters · doi:10.1021/ml500091p · Cited by 36
Disruption of protein function by pathogenic mutations: common and uncommon mechanisms
Taipale, M. (2018) · Biochemistry and Cell Biology · doi:10.1139/bcb-2018-0007 · Cited by 35
Kinome‐Wide Profiling Prediction of Small Molecules
Sorgenfrei, F. A., Fulle, S., & Merget, B. (2017) · ChemMedChem · doi:10.1002/cmdc.201700180 · Cited by 36
Strategy toward Kinase-Selective Drug Discovery
Zhang, M., Liu, Y., Jang, H., & Nussinov, R. (2023) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c01171 · Cited by 35

Authors: Lahiry, P., Torkamani, A., Schork, N. J., & Hegele, R. A.
Affiliations: Western University (CA)
Scripps Research Institute (US)
Corresponding author: Hegele, Robert A.
ORCID: Lahiry, Piya
Torkamani, Ali
Schork, Nicholas J.
Hegele, Robert A.
Venue: Nature Reviews Genetics
Publisher: Springer Science and Business Media LLC
Published: 2010-01
Volume: 11
Issue: 1
Pages: 60-74
ISSN: 1471-0056 (ISSN-L)
1471-0064
DOI: 10.1038/nrg2707
OpenAlex: W2095492902
Cited by: 420
References: 125
Citations by year: 2026: 20 · 2025: 23 · 2024: 37 · 2023: 36 · 2022: 22 · 2021: 31 · 2020: 29 · 2019: 22 · 2018: 29 · 2017: 37 · 2016: 30 · 2015: 17 · 2014: 19 · 2013: 22 · 2012: 20
FWCI: 1.43
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Reviews Genetics (publishedVersion)
PubMed (publishedVersion)
Scholarship@Western (Western University) (submittedVersion)
Funders: Canadian Institutes of Health Research
National Center for Research Resources (UL1RR025774, U54RR02504-01)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords: protein kinases, kinase mutations, genotype-phenotype correlation, mutational hotspots, structure-function relationship, inborn errors of metabolism, developmental disorders, cancer, therapeutic target
MeSH terms: Animals, Disease Models, Animal, DNA Mutational Analysis, Multigene Family, Genotype, Humans, Models, Biological, Models, Genetic, Models, Molecular, Mutation, Neoplasms, Phenotype, Phosphotransferases, Germ-Line Mutation, Genetic Diseases, Inborn

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Kinase mutations in human disease: interpreting genotype–phenotype relationships

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks