Cited by 3,738PI3K/AKT/mTOR signaling in cancerProtein Kinase Regulation and GTPase SignalingMetabolism, Diabetes, and Cancer

The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.

Oncogenic kinase signalling.

Blume-Jensen, Peter, Hunter, Tony·2001·Nature

DOI 10.1038/35077225

Open this paper in CoChat — free account

Abstract

Protein-tyrosine kinases (PTKs) are important regulators of intracellular signal-transduction pathways mediating development and multicellular communication in metazoans. Their activity is normally tightly controlled and regulated. Perturbation of PTK signalling by mutations and other genetic alterations results in deregulated kinase activity and malignant transformation. The lipid kinase phosphoinositide 3-OH kinase (PI(3)K) and some of its downstream targets, such as the protein-serine/threonine kinases Akt and p70 S6 kinase (p70S6K), are crucial effectors in oncogenic PTK signalling. This review emphasizes how oncogenic conversion of protein kinases results from perturbation of the normal autoinhibitory constraints on kinase activity and provides an update on our knowledge about the role of deregulated PI(3)K/Akt and mammalian target of rapamycin/p70S6K signalling in human malignancies.

Integrity signals

Registry

Crossref · 10.1038/35077225

Cites

93 of 93 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 hallmarks of cancer
Hanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219
Cell Signaling by Receptor Tyrosine Kinases
Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929
Efficacy and Safety of a Specific Inhibitor of the BCR-ABL Tyrosine Kinase in Chronic Myeloid Leukemia
Druker, B. J., Talpaz, M., Resta, D. J., Peng, B., Buchdunger, E., Ford, J., Lydon, N., Kantarjian, H. M., Capdeville, R., Ohno-Jones, S., et al. (2001) · New England Journal of Medicine · doi:10.1056/nejm200104053441401 · Cited by 5,237
Gain-of-Function Mutations of c- kit in Human Gastrointestinal Stromal Tumors
Hirota, S., Isozaki, K., Moriyama, Y., Hashimoto, K., Nishida, T., Ishiguro, S., Kawano, K., Hanada, M., Kurata, A., Takeda, M., et al. (1998) · Science · doi:10.1126/science.279.5350.577 · Cited by 4,487
Cellular survival: a play in three Akts
Datta, S. R., Brunet, A., & Greenberg, M. E. (1999) · Genes & Development · doi:10.1101/gad.13.22.2905 · Cited by 4,216
STATs and Gene Regulation
Darnell, J. E. (1997) · Science · doi:10.1126/science.277.5332.1630 · Cited by 3,979
Cell Signaling by Receptor Tyrosine Kinases
Schlessinger, J. (2000) · Cell · doi:10.1016/s0092-8674(00)00114-8 · Cited by 3,774
Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr–Abl positive cells
Druker, B. J., Tamura, S., Buchdunger, E., Ohno-Jones, S., Segal, G. M., Fanning, S., Zimmermann, J., & Lydon, N. (1996) · Nature Medicine · doi:10.1038/nm0596-561 · Cited by 3,652
Activity of a Specific Inhibitor of the BCR-ABL Tyrosine Kinase in the Blast Crisis of Chronic Myeloid Leukemia and Acute Lymphoblastic Leukemia with the Philadelphia Chromosome
Druker, B. J., Sawyers, C. L., Kantarjian, H., Resta, D. J., Reese, S. F., Ford, J. M., Capdeville, R., & Talpaz, M. (2001) · New England Journal of Medicine · doi:10.1056/nejm200104053441402 · Cited by 2,713
Signaling—2000 and Beyond
Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586
Self-citation

Flagged first, then by citations

Show all 93 references

Research works printed but not linked: 3

Blume-Jensen, P. & Hunter, T. in Encyclopedia of Cancer (ed. Bertino, J. R.) (Academic, San Diego, in the press).
Blume-Jensen, P. & Hunter, T. in Cancer Research - An Encyclopedic Reference (ed. Schwab, M.) (Springer, in the press).
Blume-Jensen, P. & Hunter, T. in Encyclopedia of Cancer (ed. Bertino, J. R.) (Academic, San Diego, in the press).

Sorted by citations

Items 601–700 of 1,008

Oncogenic Kinase–Induced PKM2 Tyrosine 105 Phosphorylation Converts Nononcogenic PKM2 to a Tumor Promoter and Induces Cancer Stem–like Cells
Zhou, Z., Li, M., Zhang, L., Zhao, H., Şahin, Ö., Chen, J., Zhao, J. J., Songyang, Z., & Yu, D. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-2726 · Cited by 102
Src Signaling Regulates Completion of Abscission in Cytokinesis through ERK/MAPK Activation at the Midbody
Kasahara, K., Nakayama, Y., Nakazato, Y., Ikeda, K., Kuga, T., & Yamaguchi, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608396200 · Cited by 102
Parallel Phosphatidylinositol-3 Kinase and p42/44 Mitogen-Activated Protein Kinase Signaling Pathways Subserve the Mitogenic and Antiapoptotic Actions of Insulin-Like Growth Factor I in Osteoblastic Cells
Grey, A. B., Chen, Q., Xu, X., Callon, K. E., & Cornish, J. (2003) · Endocrinology · doi:10.1210/en.2003-0350 · Cited by 102
Genetic alterations in juvenile nasopharyngeal angiofibromas
Coutinho‐Camillo, C. M., Brentani, M. M., & Nagai, M. A. (2008) · Head & Neck · doi:10.1002/hed.20775 · Cited by 102
Structure-Based Optimization of Novel Azepane Derivatives as PKB Inhibitors
Breitenlechner, C. B., Wegge, T., Berillon, L., Graul, K., Marzenell, K., Friebe, W.-G., Thomas, U., Schumacher, R., Huber, R., Engh, R. A., et al. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm0310479 · Cited by 102
Possible roles of insulin signaling in osteoblasts
Pramojanee, S. N., Phimphilai, M., Chattipakorn, N., & Chattipakorn, S. C. (2014) · Endocrine Research · doi:10.3109/07435800.2013.879168 · Cited by 109
Ror2 as a Therapeutic Target in Cancer
Debebe, Z., & Rathmell, W. K. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.01.010 · Cited by 101
Crizotinib (PF‐02341066) reverses multidrug resistance in cancer cells by inhibiting the function of P‐glycoprotein
Zhou, W., Zhang, X., Cheng, C., Wang, F., Wang, X., Liang, Y.-J., To, K. K. W., Wang, Z., Huang, H., & Fu, L. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.01849.x · Cited by 100
Vascular endothelial growth factor receptors: Molecular mechanisms of activation and therapeutic potentials
Rahimi, N. (2006) · Experimental Eye Research · doi:10.1016/j.exer.2006.03.019 · Cited by 106
Involvement of Pin1 induction in epithelial–mesenchymal transition of tamoxifen‐resistant breast cancer cells
Kim, M. R., Choi, H., Cho, K. B., Kim, H. S., & Kang, K. W. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01260.x · Cited by 100
Integration of A Deep Learning Classifier with A Random Forest Approach for Predicting Malonylation Sites
Chen, Z., He, N., Huang, Y., Qin, W. T., Liu, X., & Li, L. (2018) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2018.08.004 · Cited by 102
The ATP‐Binding Site of Protein Kinase CK2 Holds a Positive Electrostatic Area and Conserved Water Molecules
Battistutta, R., Mazzorana, M., Cendron, L., Bortolato, A., Sarno, S., Kazimierczuk, Z., Zanotti, G., Moro, S., & Pinna, L. A. (2007) · ChemBioChem · doi:10.1002/cbic.200700307 · Cited by 102
Critical Role for TrkB Kinase Function in Anoikis Suppression, Tumorigenesis, and Metastasis
Geiger, T. R., & Peeper, D. S. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0121 · Cited by 100
Molecular Pathogenesis of Lymphangioleiomyomatosis
Juvet, S., McCormack, F. X., Kwiatkowski, D. J., & Downey, G. P. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0372tr · Cited by 100
The Raison D'Être of Constitutively Active Protein Kinases: The Lesson of CK2
Pinna, L. A. (2003) · Accounts of Chemical Research · doi:10.1021/ar020164f · Cited by 100
Nuclear Signaling by Receptor Tyrosine Kinases: The First Robin of Spring
Schlessinger, J., & Lemmon, M. A. (2006) · Cell · doi:10.1016/j.cell.2006.09.013 · Cited by 98
Cytokine-Induced Signaling Networks Prioritize Dynamic Range over Signal Strength
Janes, K. A., Reinhardt, H. C., & Yaffe, M. B. (2008) · Cell · doi:10.1016/j.cell.2008.08.034 · Cited by 99
Receptor Tyrosine Kinase Signaling and Targeting in Glioblastoma Multiforme
Tilak, M., Holborn, J., New, L. A., Lalonde, J., & Jones, N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041831 · Cited by 105
Characterization of a Peptide Inhibitor of Janus Kinase 2 That Mimics Suppressor of Cytokine Signaling 1 Function
Flowers, L. O., Johnson, H. M., Mujtaba, M. G., Ellis, M. R., Haider, S. M. I., & Subramaniam, P. S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.12.7510 · Cited by 99
Exression and PI3K/AKT Pathway in Gastric Cancer and its Blockade Suppresses Tumor Growth and Metastasis
Ye, B., Jiang, L.-L., Xu, H.-T., Zhou, D., & Zs, L. (2012) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463201202500309 · Cited by 100
Probing the kinome in real time with fluorescent peptides
Gonzalez‐Vera, J. A. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15198c · Cited by 99
On the nature of low- and high-affinity EGF receptors on living cells
Özcan, F., Klein, P., Lemmon, M. A., Lax, I., & Schlessinger, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601469103 · Cited by 99
Complex Regulation of the Cyclin-Dependent Kinase Inhibitor p27kip1 in Thyroid Cancer Cells by the PI3K/AKT Pathway
Motti, M. L., Califano, D., Troncone, G., Marco, C. D., Migliaccio, I., Palmieri, E. A., Pezzullo, L., Palombini, L., Fusco, A., & Viglietto, G. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62295-x · Cited by 100
TSH-activated signaling pathways in thyroid tumorigenesis
Rivas, M., & Santisteban, P. (2003) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2003.10.029 · Cited by 99
Src Kinase Conformational Activation: Thermodynamics, Pathways, and Mechanisms
Yang, S., & Roux, B. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000047 · Cited by 98
Insulin-like Growth Factor-I Inhibits Transcriptional Responses of Transforming Growth Factor-β by Phosphatidylinositol 3-Kinase/Akt-dependent Suppression of the Activation of Smad3 but Not Smad2
Song, K. W., Cornelius, S. C., Reiß, M., & Danielpour, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304583200 · Cited by 98
Gain and loss of phosphorylation sites in human cancer
Predrag Radivojac, A., Baenziger, P. H., Kann, M. G., Mort, M. E., Hahn, M. W., & Mooney, S. D. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btn267 · Cited by 104
Differential Regulation of Akt Kinase Isoforms by the Members of the TCL1 Oncogene Family
Laine, J. T., Künstle, G., Obata, T., & Noguchi, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107069200 · Cited by 98
Induction and patterning of neuronal development, and its connection to cell cycle control
Bally‐Cuif, L., & Hammerschmidt, M. (2003) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(03)00015-1 · Cited by 102
Breakdown of endocytosis in the oncogenic activation of receptor tyrosine kinases
Abella, J. V., & Park, M. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90857.2008 · Cited by 97
VEGF in Tumor Progression and Targeted Therapy
Chekhonin, V. P., Shein, S. A., Korchagina, A. A., & Gurina, O. I. (2013) · Current Cancer Drug Targets · doi:10.2174/15680096113139990074 · Cited by 99
Protein Tyrosine Kinases: Their Roles and Their Targeting in Leukemia
Bhanumathy, K. K., Amrutha, B., Vizeacoumar, F. S., Vizeacoumar, F. J., Freywald, A., & Giambra, V. (2021) · Cancers · doi:10.3390/cancers13020184 · Cited by 97
Functional Deregulation of KIT
Cruse, G., Metcalfe, D. D., & Olivera, A. (2014) · Immunology and Allergy Clinics of North America · doi:10.1016/j.iac.2014.01.002 · Cited by 97
Tamoxifen through GPER upregulates aromatase expression: a novel mechanism sustaining tamoxifen-resistant breast cancer cell growth
Catalano, S., Giordano, C., Panza, S., Chemi, F., Bonofiglio, D., Lanzino, M., Rizza, P., Romeo, F., Fuqua, S. A. W., Maggiolini, M., et al. (2014) · Breast Cancer Research and Treatment · doi:10.1007/s10549-014-3017-4 · Cited by 97
Element and molecular mass spectrometry—an emerging analytical dream team in the life sciences
Wind, M., & Lehmann, W. D. (2004) · Journal of Analytical Atomic Spectrometry · doi:10.1039/b309482k · Cited by 97
AEG-1/MTDH/LYRIC
Emdad, L., Das, S. K., Dasgupta, S., Hu, B., Sarkar, D., & Fisher, P. B. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-401676-7.00003-6 · Cited by 96
Concepts and consequences of Eph receptor clustering
Janes, P. W., Nievergall, E., & Lackmann, M. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.01.001 · Cited by 96
Pathway specificity for Met signalling
Comoglio, P. M. (2001) · Nature Cell Biology · doi:10.1038/35083116 · Cited by 96
Optimal Sox-based fluorescent chemosensor design for serine/threonine protein kinases
Shults, M. D., Carrico-Moniz, D., & Imperiali, B. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.03.003 · Cited by 96
ESCRTs and human disease
Saksena, S., & Emr, S. D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370167 · Cited by 94
Tyrosine Phosphatase-ε Activates Src and Supports the Transformed Phenotype of Neu-induced Mammary Tumor Cells
Gil-Henn, H., & Elson, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210273200 · Cited by 96
The role of Eph receptors and ephrin ligands in colorectal cancer
Herath, N. I., & Boyd, A. (2009) · International Journal of Cancer · doi:10.1002/ijc.25147 · Cited by 96
On the Origins of Enzyme Inhibitor Selectivity and Promiscuity: A Case Study of Protein Kinase Binding to Staurosporine
Tanramluk, D., Schreyer, A. M., Pitt, W. R., & Blundell, T. L. (2009) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2009.00832.x · Cited by 96
Fibroblast growth factor receptor 2 gene amplification status and its clinicopathologic significance in gastric carcinoma
Jung, E.-J., Jung, E., Min, S. Y., Kim, M. A., & Kim, W. H. (2012) · Human Pathology · doi:10.1016/j.humpath.2011.12.002 · Cited by 98
Oncogenic signaling pathways associated with immune evasion and resistance to immune checkpoint inhibitors in cancer
Kobayashi, Y., Lim, S., & Yamaguchi, H. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.11.011 · Cited by 96
Role and Significance of c-KIT Receptor Tyrosine Kinase in Cancer: A Review
Sheikh, E., Tran, T. T., Vranić, S., Levy, A., & Bonfil, R. D. (2022) · Bosnian Journal of Basic Medical Sciences · doi:10.17305/bjbms.2021.7399 · Cited by 105
Online Nanoflow Multidimensional Fractionation for High Efficiency Phosphopeptide Analysis
Ficarro, S. B., Zhang, Y., Carrasco-Alfonso, M. J., Garg, B. K., Adelmant, G., Webber, J. T., Luckey, C. J., & Marto, J. A. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o111.011064 · Cited by 95
Reciprocal regulation of MelCAM and AKT in human melanoma
Li, G., Kalabis, J., Xu, X., Meier, F. E., Oka, M., Bogenrieder, T., & Herlyn, M. (2003) · Oncogene · doi:10.1038/sj.onc.1206819 · Cited by 98
Regulation of the Nonreceptor Tyrosine Kinase Brk by Autophosphorylation and by Autoinhibition
Qiu, H., & Miller, W. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203877200 · Cited by 94
The receptor tyrosine kinase ROR1 – An oncofetal antigen for targeted cancer therapy
Hojjat‐Farsangi, M., Moshfegh, A., Daneshmanesh, A. H., Khan, A. S., Mikaelsson, E., Österborg, A., & Mellstedt, H. (2014) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2014.07.005 · Cited by 97
Treatment of herpesvirus associated primary effusion lymphoma with intracavity cidofovir
Luppi, M., Trovato, R., Barozzi, P., Vallisa, D., Rossi, G., Re, A., Ravazzini, L., Potenza, L., Riva, G., Morselli, M., et al. (2005) · Leukemia · doi:10.1038/sj.leu.2403646 · Cited by 94
Selective PDZ protein-dependent stimulation of phosphatidylinositol 3-kinase by the adenovirus E4-ORF1 oncoprotein
Frese, K. K., Lee, S. S., Thomas, D. L., Latorre, I. J., Weiss, R. S., Glaunsinger, B. A., & Javier, R. T. (2003) · Oncogene · doi:10.1038/sj.onc.1206151 · Cited by 94
Functional Profiling of Receptor Tyrosine Kinases and Downstream Signaling in Human Chondrosarcomas Identifies Pathways for Rational Targeted Therapy
Zhang, Y., van Oosterwijk, J. G., Sicińska, E., Moss, S., Remillard, S. P., van Wezel, T., Bühnemann, C., Hassan, A. B., Demetri, G. D., Bovée, J. V. M. G., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-3647 · Cited by 101
Proteomics study of oxidative stress and Src kinase inhibition in H9C2 cardiomyocytes: a cell model of heart ischemia–reperfusion injury and treatment
Chou, H., Chen, Y., Lee, T., Wu, F.-S., Chan, H.-T., Lyu, P. C., Timms, J. F., & Chan, H. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.001 · Cited by 92
Tyrosine-phosphorylated bacterial effector proteins: the enemies within
Backert, S., & Selbach, M. (2005) · Trends in Microbiology · doi:10.1016/j.tim.2005.08.002 · Cited by 93
Nucleophosmin-anaplastic lymphoma kinase of anaplastic large-cell lymphoma recruits, activates, and uses pp60c-src to mediate its mitogenicity
Cussac, D. (2003) · Blood · doi:10.1182/blood-2003-04-1038 · Cited by 93
Rapid trafficking of c-Src, a non-palmitoylated Src-family kinase, between the plasma membrane and late endosomes/lysosomes
Kasahara, K., Nakayama, Y., Kihara, A., Matsuda, D., Ikeda, K., Kuga, T., Fukumoto, Y., Igarashi, Y., & Yamaguchi, N. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2007.05.001 · Cited by 93
Application of LC/MS to proteomics studies: current status and future prospects
Chen, G., & Pramanik, B. N. (2009) · Drug Discovery Today · doi:10.1016/j.drudis.2009.02.007 · Cited by 94
Dynamic Profiling of the Post-translational Modifications and Interaction Partners of Epidermal Growth Factor Receptor Signaling after Stimulation by Epidermal Growth Factor Using Extended Range Proteomic Analysis (ERPA)
Wu, S., Kim, J., Bandle, R., Liotta, L. A., Petricoin, E. F., & Karger, B. L. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600105-mcp200 · Cited by 93
Chromosomal amplification of leucine-rich repeat kinase-2 (LRRK2) is required for oncogenic MET signaling in papillary renal and thyroid carcinomas
Looyenga, B. D., Furge, K. A., Dykema, K. J., Koeman, J. M., Swiatek, P. J., Giordano, T. J., West, A. B., Resau, J. H., Teh, B. T., & MacKeigan, J. P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012500108 · Cited by 99
Imatinib inhibits c-Kit-induced hypoxia-inducible factor-1α activity and vascular endothelial growth factor expression in small cell lung cancer cells
Litz, J., & Krystal, G. W. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0503 · Cited by 93
Human cytomegalovirus induces cellular tyrosine kinase signaling and promotes glioma cell invasiveness
Cobbs, C., Soroceanu, L., Denham, S., Zhang, W., Britt, W. J., Pieper, R. O., & Kraus, M. H. (2007) · Journal of Neuro-Oncology · doi:10.1007/s11060-007-9423-2 · Cited by 93
AEG-1/MTDH/LYRIC
Sarkar, D., & Fisher, P. B. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-401676-7.00002-4 · Cited by 91
Apoptotic Pathways in Tumor Progression and Therapy
Melet, A., Song, K., Bucur, O., Jagani, Z., Grassian, A. R., & Khosravi‐Far, R. (2007) · Advances in experimental medicine and biology · doi:10.1007/978-1-4020-6554-5_4 · Cited by 92
Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins
Howard, P. L., Chia, M. C., Rizzo, S. D., Liu, F., & Pawson, T. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934711100 · Cited by 92
Expression of the Receptor Tyrosine Kinase Axl Promotes Ocular Melanoma Cell Survival
van Ginkel, P. R., Gee, R. L., Shearer, R. L., Subramanian, L., Walker, T. M., Albert, D. M., Meisner, L. F., Varnum, B. C., & Polans, A. S. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-0245 · Cited by 96
Blocking Myristoylation of Src Inhibits Its Kinase Activity and Suppresses Prostate Cancer Progression
Kim, S., Alsaidan, O. A., Goodwin, O. Y., Li, Q., Sulejmani, E., Han, Z. H., Bai, A., Albers, T., Beharry, Z. M., Zheng, Y. G., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0981 · Cited by 91
Beyond controlling cell size: functional analyses of S6K in tumorigenesis
Wu, X., Xie, W., Xie, W., Wei, W., & Guo, J. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05081-4 · Cited by 96
Negative regulation of receptor tyrosine kinases: unexpected links to c-Cbl and receptor ubiquitylation
Rubin, C., Gur, G., & Yarden, Y. (2005) · Cell Research · doi:10.1038/sj.cr.7290268 · Cited by 91
Akt/PTEN Signaling Mediates Estrogen-Dependent Proliferation of Primordial Germ Cells in Vitro
Moe-Behrens, G. H. G., Klinger, F. G., Eskild, W., Grotmol, T., Haugen, T. B., & Felici, M. D. (2003) · Molecular Endocrinology · doi:10.1210/me.2003-0006 · Cited by 91
Correlation of KIT and platelet-derived growth factor receptor α mutations with gene activation and expression profiles in gastrointestinal stromal tumors
Kang, H. J., Nam, S. W., Kim, H., Rhee, H., Kim, N.-G., Kim, H., Hyung, W. J., Noh, S. H., Kim, J.-H., Yun, C., et al. (2004) · Oncogene · doi:10.1038/sj.onc.1208358 · Cited by 91
Unique Activation Mechanism of Protein Kinase CK2
Sarno, S., Ghisellini, P., & Pinna, L. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200486200 · Cited by 91
A Unique Protein Phosphatase with Kelch-Like Domains (PPKL) in Plasmodium Modulates Ookinete Differentiation, Motility and Invasion
Guttery, D. S., Poulin, B., Ferguson, D. J. P., Szöőr, B., Wickstead, B., Carroll, P. L., Ramakrishnan, C., Brady, D., Patzewitz, E., Straschil, U., et al. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002948 · Cited by 91
Quantitative methods for the analysis of protein phosphorylation in drug development
Olive, D. M. (2004) · Expert Review of Proteomics · doi:10.1586/14789450.1.3.327 · Cited by 91
Prognostic relevance of activated Akt kinase in node-negative breast cancer: a clinicopathological study of 99 cases
Schmitz, K. J., Otterbach, F., Callies, R., Levkau, B., Hölscher, M., Hoffmann, O. I., Grabellus, F., Kimmig, R., Schmid, K. W., & Baba, H. A. (2003) · Modern Pathology · doi:10.1038/modpathol.3800002 · Cited by 91
Use of proteomic analysis to monitor responses to biological therapies
Espina, V. A., Dettloff, K. A., Cowherd, S., Petricoin, E. F., & Liotta, L. A. (2004) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.4.1.83 · Cited by 91
Identification of Akt Association and Oligomerization Domains of the Akt Kinase Coactivator TCL1
Künstle, G., Laine, J. T., Pierron, G., Kagami, S., Nakajima, H., Hoh, F., Roumestand, C., Stern, M., & Noguchi, M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1513-1525.2002 · Cited by 91
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
Src-mediated regulation of E-cadherin and EMT in pancreatic cancer
Nagathihalli, N. S. (2012) · Frontiers in bioscience · doi:10.2741/4037 · Cited by 90
The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases
Shah, N. H., Amacher, J. F., Nocka, L. M., & Kuriyan, J. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1495173 · Cited by 91
Molecular signaling regulating anchorage-independent growth of cancer cells.
Wang, L. (2004) · PubMed · Cited by 92
Oncogenic targeting of an activated tyrosine kinase to the Golgi apparatus in a glioblastoma
Charest, A., Kheifets, V., Park, J., Lane, K. M., McMahon, K., Nutt, C. L., & Housman, D. E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242741799 · Cited by 90
Tyrosine kinase inhibitor STI-571/Gleevec down-regulates the β-catenin signaling activity
Zhou, L., An, N., Haydon, R. C., Zhou, Q., Cheng, H., Peng, Y., Jiang, W., Luu, H. H., Vanichakarn, P., Szatkowski, J. P., et al. (2003) · Cancer Letters · doi:10.1016/s0304-3835(03)00013-2 · Cited by 91
Protein-tyrosine kinase CAKβ/PYK2 is activated by binding Ca2+/calmodulin to FERM F2 α2 helix and thus forming its dimer
Kohno, T., Matsuda, E., Sasaki, H., & Sasaki, T. (2008) · Biochemical Journal · doi:10.1042/bj20070665 · Cited by 90
The Rab2A GTPase Promotes Breast Cancer Stem Cells and Tumorigenesis via Erk Signaling Activation
Luo, M., Gong, C., Chen, C.-H., Hu, H., Huang, P., Zheng, M., Yao, Y., Wei, S., Wulf, G. M., Lieberman, J., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.002 · Cited by 91
Tyrosine Residues in Phospholipase Cγ2 Essential for the Enzyme Function in B-cell Signaling
Rodriguez, R., Matsuda, M., Perišić, O., Bravo, J., Paul, A., Jones, N. P., Light, Y., Swann, K., Williams, R. L., & Katan, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107577200 · Cited by 90
Current targeted therapies in the treatment of advanced colorectal cancer: a review
Moriarity, A., O’Sullivan, J., Kennedy, J., Mehigan, B., & McCormick, P. (2016) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758834016646734 · Cited by 87
A Robust Error Model for iTRAQ Quantification Reveals Divergent Signaling between Oncogenic FLT3 Mutants in Acute Myeloid Leukemia
Zhang, Y., Askenazi, M., Jiang, J., Luckey, C. J., Griffin, J. D., & Marto, J. A. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900452-mcp200 · Cited by 89
Alk and Ltk ligands are essential for iridophore development in zebrafish mediated by the receptor tyrosine kinase Ltk
Mo, E. S., Cheng, Q., Reshetnyak, A. V., Schlessinger, J., & Nicoli, S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710254114 · Cited by 91
Regulation of glycosaminoglycan structure and atherogenesis
Ballinger, M. L., Nigro, J., Frontanilla, K. V., Dart, A. M., & Little, P. J. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-3389-4 · Cited by 89
Sprouty and cancer: The first terms report
Lo, T. L., Fong, C. W., Yusoff, P., McKie, A. B., Chua, M., Leung, H. Y., & Guy, G. R. (2006) · Cancer Letters · doi:10.1016/j.canlet.2005.12.032 · Cited by 89
Postgenomic global analysis of translational control induced by oncogenic signaling
Rajasekhar, V. K., & Holland, E. C. (2004) · Oncogene · doi:10.1038/sj.onc.1207546 · Cited by 90
Lymphoblastic leukemia/lymphoma in mice overexpressing the Mer (MerTK) receptor tyrosine kinase
Keating, A. K., Salzberg, D. B., Sather, S., Liang, X., Nickoloff, S., Anwar, A., DeRyckere, D., Hill, K. K., Joung, D., Sawczyn, K. K., et al. (2006) · Oncogene · doi:10.1038/sj.onc.1209633 · Cited by 89
Mining the Tumor Phosphoproteome for Cancer Markers
Lim, Y. P. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-2243 · Cited by 88
Cross-talk between IGF-I and TGF-β signaling pathways
Danielpour, D., & SONG, K. (2005) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2005.09.007 · Cited by 91
Dual phosphoproteomics and chemical proteomics analysis of erlotinib and gefitinib interference in acute myeloid leukemia cells
Weber, C. K., Schreiber, T. B., & Daub, H. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.11.004 · Cited by 88
ROCK1 as a potential therapeutic target in osteosarcoma
Liu, X., Choy, E., Hornicek, F. J., Yang, S., Cao, Y., Harmon, D. C., Mankin, H. J., & Duan, Z. (2011) · Journal of Orthopaedic Research® · doi:10.1002/jor.21403 · Cited by 88
Novel targets of Akt, p21, and MDM2
Zhou, B. P., & Hung, M. (2002) · Seminars in Oncology · doi:10.1016/s0093-7754(02)70128-0 · Cited by 88
Kinase requirements in human cells: I. Comparing kinase requirements across various cell types
Grueneberg, D. A., Degot, S., Pearlberg, J., Li, W., Davies, J. E., Baldwin, A. E., Endege, W. O., Doench, J. G., Sawyer, J., Hu, Y., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808019105 · Cited by 88
Transcription factors and cancer: an overview
Nebert, D. W. (2002) · Toxicology · doi:10.1016/s0300-483x(02)00269-x · Cited by 88

Authors: Blume-Jensen, P., & Hunter, T.
Affiliations: Salk Institute for Biological Studies (US)
ORCID: Hunter, Tony
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2001-05-01
Volume: 411
Issue: 6835
Pages: 355-365
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/35077225
OpenAlex: W1639582946
Cited by: 3,738
References: 93
Citations by year: 2026: 48 · 2025: 69 · 2024: 87 · 2023: 102 · 2022: 103 · 2021: 114 · 2020: 121 · 2019: 118 · 2018: 105 · 2017: 119 · 2016: 131 · 2015: 156 · 2014: 186 · 2013: 185 · 2012: 200
FWCI: 12.95
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: tyrosine kinase, oncogenic signaling, signal transduction, phosphatidylinositol 3-kinase, Akt, p70 S6 kinase, mTOR, kinase autoinhibition, malignant transformation, human malignancies
MeSH terms: Animals, Humans, Mutation, Neoplasms, Oncogenes, Protein-Tyrosine Kinases, Signal Transduction, Oncogene Proteins, Retroviridae Proteins, Oncogenic, Phosphatidylinositol 3-Kinases, Ribosomal Protein S6 Kinases, Receptor Protein-Tyrosine Kinases, Oncogene Protein v-akt

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

Oncogenic kinase signalling.

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