Cited by 845Cancer Mechanisms and TherapyProtein Kinase Regulation and GTPase SignalingMechanisms of cancer metastasis

The DOI matches its Crossref record; 171 of the 171 references it cites were found in a registry or an index.

Src family kinases in tumor progression and metastasis

Summy, Justin M., Gallick, Gary E.·2003·Cancer and Metastasis Reviews

Open this paper in CoChat — free account

Abstract

The Src family of non-receptor protein tyrosine kinases plays critical roles in a variety of cellular signal transduction pathways, regulating such diverse processes as cell division, motility, adhesion, angiogenesis, and survival. Constitutively activated variants of Src family kinases, including the viral oncoproteins v-Src and v-Yes, are capable of inducing malignant transformation of a variety of cell types. Src family kinases, most notably although not exclusively c-Src, are frequently overexpressed and/or aberrantly activated in a variety of epithelial and non-epithelial cancers. Activation is very common in colorectal and breast cancers, and somewhat less frequent in melanomas, ovarian cancer, gastric cancer, head and neck cancers, pancreatic cancer, lung cancer, brain cancers, and blood cancers. Further, the extent of increased Src family activity often correlates with malignant potential and patient survival. Activation of Src family kinases in human cancers may occur through a variety of mechanisms and is frequently a critical event in tumor progression. Exactly how Src family kinases contribute to individual tumors remains to be defined completely, however they appear to be important for multiple aspects of tumor progression, including proliferation, disruption of cell/cell contacts, migration, invasiveness, resistance to apoptosis, and angiogenesis. This review details the evidence for Src family activation in human tumors, and emphasizes possible consequences to tumor progression. Given the ability of Src and its family members to participate in so many aspects of tumor progression and metastasis, Src family kinases are attractive targets for future anti-cancer therapeutics.

Integrity signals

Registry

Crossref · 10.1023/a:1023772912750

Cites

171 of 171 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?

CELLULAR FUNCTIONS REGULATED BY SRC FAMILY KINASES
Thomas, S. Μ., & Brugge, J. S. (1997) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.13.1.513 · Cited by 2,537
Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
Hunter, T. R., & Sefton, B. M. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1311 · Cited by 2,333
Three-dimensional structure of the tyrosine kinase c-Src
Xu, W., Harrison, S. C., & Eck, M. J. (1997) · Nature · doi:10.1038/385595a0 · Cited by 1,432
DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA
STEHELIN, D., VARMUS, H. E., BISHOP, J. M., & VOGT, P. K. (1976) · Nature · doi:10.1038/260170a0 · Cited by 1,321 · cited 2×
“Through then very tedious molecular approaches, Bishop and Varmus [3] demonstrated that the viral Src gene (v-src) had as its progenitor a normal cellular gene (proto-oncogene) c-src, an experiment largely responsible for the awarding of the”
Background
Regulation, substrates and functions of src
Brown, M. T., & Cooper, J. A. (1996) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(96)00003-0 · Cited by 1,193
Crystal structure of the Src family tyrosine kinase Hck
Sicheri, F., Moarefi, I., & Kuriyan, J. (1997) · Nature · doi:10.1038/385602a0 · Cited by 1,171
A SARCOMA OF THE FOWL TRANSMISSIBLE BY AN AGENT SEPARABLE FROM THE TUMOR CELLS
Rous, P. (1911) · Journal of Experimental Medicine · doi:10.1084/jem.13.4.397 · Cited by 1,051
Tyrosine kinase/p21ras/MAP‐kinase pathway activation by estradiol‐receptor complex in MCF‐7 cells.
Migliaccio, A., Domenico, M. D., Castoria, G., de Falco, A., Bontempo, P., Nola, E., & Auricchio, F. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00471.x · Cited by 950
Identification of a transformation-specific antigen induced by an avian sarcoma virus
Brugge, J. S., & Erikson, R. L. (1977) · Nature · doi:10.1038/269346a0 · Cited by 889
Role of Src expression and activation in human cancer
Irby, R., & Yeatman, T. J. (2000) · Oncogene · doi:10.1038/sj.onc.1203912 · Cited by 878

Show all 171 references

Items 201–300 of 845

c-Src Regulates Constitutive and EGF-mediated VEGF Expression in Pancreatic Tumor Cells Through Activation of Phosphatidyl Inositol-3 Kinase and p38 MAPK
Summy, J. M., Trevino, J. G., Baker, C. H., & Gallick, G. E. (2005) · Pancreas · doi:10.1097/01.mpa.0000178280.50534.0c · Cited by 62
Self-citation
Novel therapeutic approaches to the treatment of metastatic breast cancer
Fernández, Y., Cueva, J. F., Palomo, A. G., Ramos, M., Juan, A. D., Calvo, L., García-Mata, J., García‐Teijido, P., Peláez, I., & García‐Estévez, L. (2009) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2009.10.001 · Cited by 61
Effects of Src inhibitors on cell growth and epidermal growth factor receptor and MET signaling in gefitinib‐resistant non‐small cell lung cancer cells with acquired MET amplification
Yoshida, T., Okamoto, I., Okamoto, W., Hatashita, E., Yamada, Y., Kuwata, K., Nishio, K., Fukuoka, M., Janne, P. A., & Nakagawa, K. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01368.x · Cited by 61
Protein tyrosine phosphatases as novel targets in breast cancer therapy
Nunes‐Xavier, C. E., Martín-Pérez, J., Elson, A., & Pulido, R. (2013) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2013.06.001 · Cited by 61
Antitumor Activity of Targeting Src Kinases in Endothelial and Myeloid Cell Compartments of the Tumor Microenvironment
Liang, W. P., Kujawski, M., Wu, J., Lu, J., Herrmann, A., Loera, S., Yen, Y., Lee, F., Yu, H., Wen, W. X., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-1486 · Cited by 61
Cooperative action of tamoxifen and c-Src inhibition in preventing the growth of estrogen receptor–positive human breast cancer cells
Herynk, M. H., Beyer, A. R., Cui, Y., Weiss, H. L., Anderson, E., Green, T. P., & Fuqua, S. A. W. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0394 · Cited by 61
Drug resistance in ovarian cancer: The emerging importance of gene transcription and spatio-temporal regulation of resistance
Richardson, A., & Kaye, S. B. (2005) · Drug Resistance Updates · doi:10.1016/j.drup.2005.09.001 · Cited by 61
Oncogenic signaling by tyrosine kinases of the SRC family in advanced colorectal cancer.
Sirvent, A., Bénistant, C., & Roche, S. (2012) · Europe PMC (PubMed Central) · Cited by 61
Src Phosphorylates Ezrin at Tyrosine 477 and Induces a Phosphospecific Association between Ezrin and a Kelch-Repeat Protein Family Member
Heiska, L., & Carpén, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411353200 · Cited by 62
Expression of Src and FAK in Hepatocellular Carcinoma and the Effect of Src Inhibitors on Hepatocellular Carcinoma In Vitro
Lau, G., Lau, G. M. G., Yu, G., Gelman, I. H., Gutowski, A., Hangauer, D. G., & Fang, J. W. S. (2008) · Digestive Diseases and Sciences · doi:10.1007/s10620-008-0519-0 · Cited by 60
AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts
Zhang, J., Park, S. I., Artime, M. C., Summy, J. M., Shah, A. N., Bomser, J. A., Dorfleutner, A., Flynn, D. C., & Gallick, G. E. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30710 · Cited by 60
Self-citation
Leukocyte cell-derived chemotaxin 2 antagonizes MET receptor activation to suppress hepatocellular carcinoma vascular invasion by protein tyrosine phosphatase 1B recruitment
Chen, C.-K., Yang, C., Hua, K., Ho, M., Johansson, G., Jeng, Y., Chen, C., Chen, M.-W., Lee, W.-J., Su, J.-L., et al. (2013) · Hepatology · doi:10.1002/hep.26738 · Cited by 63
Src Inhibitors in Lung Cancer: Current Status and Future Directions
Rothschild, S. I., Gautschi, O. P., Haura, E. B., & Johnson, F. M. (2010) · Clinical Lung Cancer · doi:10.3816/clc.2010.n.030 · Cited by 59
Proteomics study of serum exosomes from papillary thyroid cancer patients
Luo, D., Zhan, S., Xia, W., Huang, L., Ge, W., & Wang, T. (2018) · Endocrine Related Cancer · doi:10.1530/erc-17-0547 · Cited by 59
Castration-Resistant Prostate Cancer Bone Metastasis Response Measured by 18 F-Fluoride PET After Treatment with Dasatinib and Correlation with Progression-Free Survival: Results from American College of Radiology Imaging Network 6687
Yu, E. Y., Duan, F., Muzi, M., Deng, X., Chin, B. B., Alumkal, J. J., Taplin, M., Taub, J., Herman, B., Higano, C. S., et al. (2015) · Journal of Nuclear Medicine · doi:10.2967/jnumed.114.146936 · Cited by 58
Apoptosis-Inducing Effects of Two Anthraquinones from Hedyotis diffusa WILLD.
Shi, Y., Wang, C.-H., & Gong, X. (2008) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.31.1075 · Cited by 58
The application of click chemistry in the synthesis of agents with anticancer activity
Sheng, J., Ma, N., Wang, Y., Ye, W., & Zhao, B. (2015) · Drug Design Development and Therapy · doi:10.2147/dddt.s56038 · Cited by 58
Involvement of adaptor protein Crk in malignant feature of human ovarian cancer cell line MCAS
Linghu, H., Tsuda, M., Makino, Y., Sakai, M., Watanabe, T., Ichihara, S., Sawa, H., Nagashima, K., Mochizuki, N., & Tanaka, S. (2006) · Oncogene · doi:10.1038/sj.onc.1209398 · Cited by 57
TRPM7 is required for ovarian cancer cell growth, migration and invasion
Wang, J., Liao, Q., Zhang, Y., Zhou, H., Luo, C., Tang, J., Wang, Y., Tang, Y., Zhao, M., Zhao, X., et al. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.10.118 · Cited by 58
Beyond adhesion: emerging roles for integrins in control of the tumor microenvironment
Longmate, W. M., & DiPersio, C. M. (2017) · F1000Research · doi:10.12688/f1000research.11877.1 · Cited by 57
The role of Src family kinases in growth and migration of glioma stem cells
Han, X., Zhang, W., Yang, X., Wheeler, C. G., Langford, C. P., Wu, L., Filippova, N., Friedman, G. K., Ding, Q., Fathallah‐Shaykh, H. M., et al. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2432 · Cited by 56
C-Src-mediated RANKL-induced breast cancer cell migration by activation of the ERK and Akt pathway
Zhang, L., Teng, Y., Zhang, Y., LIU, J., Xu, L., Qu, J., Hou, K., Yang, X., Liu, Y., & Qu, X. (2011) · Oncology Letters · doi:10.3892/ol.2011.487 · Cited by 57
Paxillin-Y118 phosphorylation contributes to the control of Src-induced anchorage-independent growth by FAK and adhesion
Sachdev, S., Bu, Y., & Gelman, I. H. (2009) · BMC Cancer · doi:10.1186/1471-2407-9-12 · Cited by 56
Understanding Micrometastatic Disease and Anoikis Resistance in Ewing Family of Tumors and Osteosarcoma
Strauss, S. J., Ng, T., Mendoza‐Naranjo, A., Whelan, J., & Sorensen, P. H. B. (2010) · The Oncologist · doi:10.1634/theoncologist.2010-0093 · Cited by 60
Src-mediated regulation of the PI3K pathway in advanced papillary and anaplastic thyroid cancer
Beadnell, T. C., Nassar, K. W., Rose, M. M., Clark, E. G., Danysh, B. P., Hofmann, M.-C. C., Pozdeyev, N. V., & Schweppe, R. E. (2018) · Oncogenesis · doi:10.1038/s41389-017-0015-5 · Cited by 57
YES1: A Novel Therapeutic Target and Biomarker in Cancer
Garmendia, I., Redín, E., Montuenga, L. M., & Calvo, A. (2022) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0958 · Cited by 53
Integrin αvβ3 Controls Activity and Oncogenic Potential of Primed c-Src
Huveneers, S., van den Bout, I., Sonneveld, P., Sancho, A., Sonnenberg, A., & Danen, E. H. J. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3654 · Cited by 55
Silencing of galectin-3 represses osteosarcoma cell migration and invasion through inhibition of FAK/Src/Lyn activation and β-catenin expression and increases susceptibility to chemotherapeutic agents.
Park, G.-B., Kim, D., Kim, Y., Lee, H.-K., Kim, C.-W., & Hur, D. (2015) · International Journal of Oncology · doi:10.3892/ijo.2014.2721 · Cited by 54
Lessons learned from gene expression profiling of cutaneous T-cell lymphoma
Dulmage, B., & Geskin, L. J. (2013) · British Journal of Dermatology · doi:10.1111/bjd.12578 · Cited by 52
RSK in tumorigenesis: Connections to steroid signaling
Eisinger‐Mathason, T. S. K., Andrade, J., & Lannigan, D. A. (2010) · Steroids · doi:10.1016/j.steroids.2009.12.010 · Cited by 59
Targeted agents to reverse resistance to endocrine therapy in metastatic breast cancer: Where are we now and where are we going?
Fedele, P., Calvani, N., Marino, A., Orlando, L., Schiavone, P., Quaranta, A., & Cinieri, S. (2012) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2012.03.004 · Cited by 55
Targeting Lyn inhibits tumor growth and metastasis in Ewing's sarcoma
Guan, H., Zhou, Z., Gallick, G. E., Jia, S.-F., Morales, J., Sood, A. K., Corey, S. J., & Kleinerman, E. S. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0058 · Cited by 55
Self-citation
The importance of non-nuclear AR signaling in prostate cancer progression and therapeutic resistance
Zarif, J. C., & Miranti, C. K. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.01.013 · Cited by 59
Combating head and neck cancer metastases by targeting Src using multifunctional nanoparticle-based saracatinib
Lang, L., Shay, C., Xiong, Y., Thakkar, P., Chemmalakuzhy, R., Wang, X., & Teng, Y. (2018) · Journal of Hematology & Oncology · doi:10.1186/s13045-018-0623-3 · Cited by 55
CEACAM6 Cross-linking Induces Caveolin-1-dependent, Src-mediated Focal Adhesion Kinase Phosphorylation in BxPC3 Pancreatic Adenocarcinoma Cells
Duxbury, M. S., Ito, H., Ashley, S. W., & Whang, E. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402051200 · Cited by 55
Retracted
Dual function of focal adhesion kinase in regulating integrin‐induced MMP‐2 and MMP‐9 release by human T lymphoid cells
Segarra, M., Vilardell, C., Matsumoto, K., Esparza, J., Lozano, E., Serra‐Pages, C., Urbano-Márquez, A., Yamada, K. M., & Cid, M. C. (2005) · The FASEB Journal · doi:10.1096/fj.04-3574fje · Cited by 54
Challenges and Opportunities in Developing Targeted Therapies for Triple Negative Breast Cancer
Chapdelaine, A. G., & Sun, G. (2023) · Biomolecules · doi:10.3390/biom13081207 · Cited by 58
Src, chemoresistance and epithelial to mesenchymal transition: are they related?
Shah, A. N., & Gallick, G. E. (2007) · Anti-Cancer Drugs · doi:10.1097/cad.0b013e32801265d7 · Cited by 54
Self-citation
Developing lipophilic aromatic halogenated fused systems with specific ring orientations, leading to potent anticancer analogs and targeting the c-Src Kinase enzyme
Ahmed, H. E. A., El-Nassag, M. A. A., Hassan, A. A. E.-H., Mohamed, H. M., Halawa, A. H., Okasha, R. M., Ihmaid, S. K., El-Gilil, S. M. A., Khattab, E. S. A. E. H., Fouda, A. M., et al. (2019) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2019.03.012 · Cited by 54
Ligand‐independent activation of MET through IGF‐1/IGF‐1R signaling
Varkaris, A. S., Gaur, S., Parikh, N. U., Song, J. H., Dayyani, F., Jin, J., Logothetis, C. J., & Gallick, G. E. (2013) · International Journal of Cancer · doi:10.1002/ijc.28169 · Cited by 53
Self-citation
A Fra‐1‐dependent, matrix metalloproteinase driven EGFR activation promotes human lung epithelial cell motility and invasion
Adiseshaiah, P. P., Vaz, M. J., Machireddy, N., Kalvakolanu, D. V., & Reddy, S. P. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21410 · Cited by 53
A phase II trial of the Src kinase inhibitor saracatinib (AZD0530) in patients with metastatic or locally advanced gastric or gastro esophageal junction (GEJ) adenocarcinoma: a trial of the PMH phase II consortium
MacKay, H. J., Au, H., McWhirter, E., Alcindor, T., Jarvi, A., MacAlpine, K., Wang, L. E., Wright, J. J., & Oza, A. M. (2011) · Investigational New Drugs · doi:10.1007/s10637-011-9650-4 · Cited by 53
Targeted treatments in colorectal cancer: state of the art and future perspectives
Arnold, D., & Seufferlein, T. (2010) · Gut · doi:10.1136/gut.2009.196006 · Cited by 54
Src Kinase Phosphorylates RUNX3 at Tyrosine Residues and Localizes the Protein in the Cytoplasm
Goh, Y., Cinghu, S., Hong, E. T. H., Lee, Y., Kim, J., Jang, J., Li, Y., Chi, X., Lee, K., Wee, H., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.071381 · Cited by 53
Improving the prognosis for patients with glioblastoma: the rationale for targeting Src
de Groot, J., & Milano, V. (2009) · Journal of Neuro-Oncology · doi:10.1007/s11060-009-9916-2 · Cited by 54
Simultaneous Expression of Caveolin-1 and E-Cadherin in Ovarian Carcinoma Cells Stabilizes Adherens Junctions through Inhibition of src-Related Kinases
Miotti, S., Tomassetti, A., Facetti, I., Sanna, E., Berno, V., & Canevari, S. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61228-x · Cited by 52
SLAP displays tumour suppressor functions in colorectal cancer via destabilization of the SRC substrate EPHA2
Naudin, C., Sirvent, A., Leroy, C., Larive, R. M., Simon, V., Pannequin, J., Bourgaux, J., Pierre, J., Robert, B., Hollande, F., et al. (2014) · Nature Communications · doi:10.1038/ncomms4159 · Cited by 57
miR-205 is frequently downregulated in prostate cancer and acts as a tumor suppressor by inhibiting tumor growth.
Wang, N., Li, Q., Feng, N., Cheng, G., Guan, Z.-L., Wang, Y., Qin, C., Yin, C., & Hua, L. X. (2013) · Asian Journal of Andrology · doi:10.1038/aja.2013.80 · Cited by 59
Interleukin-1β activates focal adhesion kinase and Src to induce matrix metalloproteinase-9 production and invasion of MCF-7 breast cancer cells
Mon, N. N., Senga, T., & Ito, S. (2016) · Oncology Letters · doi:10.3892/ol.2016.5521 · Cited by 52
Tyrosine kinase inhibitors and gemcitabine: New treatment options in pancreatic cancer?
Kleespies, A., Jauch, K. ‐., & Bruns, C. J. (2006) · Drug Resistance Updates · doi:10.1016/j.drup.2006.02.002 · Cited by 52
Src activation of Stat3 is an independent requirement from NF-κB activation for constitutive IL-8 expression in human pancreatic adenocarcinoma cells
Trevino, J. G., Gray, M. J., Nawrocki, S. T., Summy, J. M., Lesslie, D. P., Evans, D. B., Sawyer, T. K., Shakespeare, W. C., Watowich, S. S., Chiao, P. J., et al. (2006) · Angiogenesis · doi:10.1007/s10456-006-9038-9 · Cited by 52
Self-citation
Novel advances in pancreatic cancer treatment
Vulfovich, M., & Rocha-Lima, C. S. (2008) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.8.6.993 · Cited by 51
Desmoglein 3: A Help or a Hindrance in Cancer Progression?
Brown, L., & Wan, H. (2015) · Cancers · doi:10.3390/cancers7010266 · Cited by 53
Cell growth, global phosphotyrosine elevation, and c-Met phosphorylation through Src family kinases in colorectal cancer cells
Emaduddin, M., Bicknell, D. C., Bodmer, W. F., & Feller, S. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712176105 · Cited by 50
Rosmarinic acid inhibits cell proliferation, migration, and invasion and induces apoptosis in human glioma cells
Liu, Y., Xu, X., Tang, H., Pan, Y., Hu, B., & Huang, G. (2021) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2021.4900 · Cited by 50
Ableson kinases negatively regulate invadopodia function and invasion in head and neck squamous cell carcinoma by inhibiting an HB-EGF autocrine loop
Hayes, K. E., Walk, E. L., Ammer, A. G., Kelley, L., Martin, K. H., & Weed, S. A. (2012) · Oncogene · doi:10.1038/onc.2012.513 · Cited by 50
Engineered kinase activation reveals unique morphodynamic phenotypes and associated trafficking for Src family isoforms
Chu, P.-H., Tsygankov, D., Berginski, M. E., Dağliyan, O., Gomez, S. M., Elston, T. C., Karginov, A. V., & Hahn, K. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404487111 · Cited by 50
Lipid Raft–Specific Knockdown of Src Family Kinase Activity Inhibits Cell Adhesion and Cell Cycle Progression of Breast Cancer Cells
Hitosugi, T., Sato, M., Sasaki, K., & Umezawa, Y. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4539 · Cited by 50
Role of erbB3 receptors in cancer therapeutic resistance
Lee, Y., Ma, J., Lyu, H., Huang, J., Kim, A., & Liu, B. (2014) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt150 · Cited by 52
Binding Sites of Anticancer Drugs on Human Serum Albumin (HSA): A Review
Molaei, P., Mahaki, H., Manoochehri, H., & Tanzadehpanah, H. (2022) · Protein and Peptide Letters · doi:10.2174/0929866529666220426124834 · Cited by 47
Oncolytic reovirus induces intracellular redistribution of Ras to promote apoptosis and progeny virus release
Garant, K. A., Shmulevitz, M., Pan, L., Daigle, R., Ahn, D.-G., Gujar, S. A., & Lee, P. W. K. (2015) · Oncogene · doi:10.1038/onc.2015.136 · Cited by 47
Redox Regulation of Cancer Metastasis: Molecular Signaling and Therapeutic Opportunities
Yang, W., Zou, L., Huang, C., & Lei, Y. (2014) · Drug Development Research · doi:10.1002/ddr.21216 · Cited by 48
HBx protein induces EMT through c-Src activation in SMMC-7721 hepatoma cell line
Yang, S. Z., Zhang, L. D., Zhang, Y., Xiong, Y., Zhang, Y., Li, H. L., Li, X. W., & Jia, D. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.079 · Cited by 48
Nanomechanical Property Maps of Breast Cancer Cells As Determined by Multiharmonic Atomic Force Microscopy Reveal Syk-Dependent Changes in Microtubule Stability Mediated by MAP1B
Krisenko, M. O., Cartagena‐Rivera, A. X., Raman, A., & Geahlen, R. L. (2014) · Biochemistry · doi:10.1021/bi500325n · Cited by 50
PI3K activation is required for PMA-directed activation of cSrc by AFAP-110
Walker, V. G., Ammer, A. G., Cao, Z., Clump, A. C., Jiang, B., Kelley, L. C., Weed, S. A., Zot, H. G., & Flynn, D. C. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00525.2006 · Cited by 48
SRC Signaling in Cancer and Tumor Microenvironment
Caner, A., Aşık, E., & Özpolat, B. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-47189-7_4 · Cited by 51
Reduced tumor growth in a mouse model of schizophrenia, lacking the dopamine transporter
Asada, M., Ebihara, S., Numachi, Y., Okazaki, T., Yamanda, S., Ikeda, K., Yasuda, H., Sora, I., & Arai, H. (2008) · International Journal of Cancer · doi:10.1002/ijc.23562 · Cited by 47
Shear stress induces internalization of E‐cadherin and invasiveness in metastatic oesophageal cancer cells by a Src‐dependent pathway
Lawler, K., O’Sullivan, G. C., Long, A., & Kenny, D. J. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2009.01160.x · Cited by 47
Src family kinases, HCK and FGR, associate with local inflammation and tumour progression in colorectal cancer
Roseweir, A. K., Powell, A. G. M. T., Horstman, S. L., Inthagard, J., Park, J. H., McMillan, D., Horgan, P. G., & Edwards, J. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.01.007 · Cited by 48
Phytochemicals inhibit migration of triple negative breast cancer cells by targeting kinase signaling
Thakuri, P. S., Gupta, M., Singh, S. K., Joshi, R., Glasgow, E. F., Lekan, A. A., Agarwal, S., Luker, G. D., & Tavana, H. (2020) · BMC Cancer · doi:10.1186/s12885-019-6479-2 · Cited by 49
Functional dissection of transformation by c‐Src and v‐Src
Oneyama, C., Hikita, T., Nada, S., & Okada, M. (2007) · Genes to Cells · doi:10.1111/j.1365-2443.2007.01145.x · Cited by 48
The Adaptor Protein Tom1L1 Is a Negative Regulator of Src Mitogenic Signaling Induced by Growth Factors
Franco, M., Furstoss, O., Simon, V., Benistant, C., Hong, W. J., & Roche, S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1932-1947.2006 · Cited by 47
Discovery of [7-(2,6-dichlorophenyl)-5-methylbenzo [1,2,4]triazin-3-yl]-[4-(2-pyrrolidin-1-ylethoxy)phenyl]amine—a potent, orally active Src kinase inhibitor with anti-tumor activity in preclinical assays
Noronha, G., Barrett, K., Boccia, A., Brodhag, T., Cao, J., Chow, C. P., Dneprovskaia, E., Doukas, J., Fine, R., Gong, X., et al. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.11.006 · Cited by 49
Pathobiology and management of prostate cancer-induced bone pain: recent insights and future treatments
Muralidharan, A., & Smith, M. T. (2013) · Inflammopharmacology · doi:10.1007/s10787-013-0183-7 · Cited by 46
Src: Marker or Actor in Prostate Cancer Aggressiveness
Vlaeminck-Guillem, V., Gillet, G., & Rimokh, R. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00222 · Cited by 42
Epigenetic silencing of the ubiquitin ligase subunit FBXL7 impairs c-SRC degradation and promotes epithelial-to-mesenchymal transition and metastasis
Moro, L., Simoneschi, D., Kurz, E., Arbini, A., Jang, S., Guaragnella, N., Giannattasio, S., Wang, W., Chen, Y., Pires, G., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0560-6 · Cited by 45
Reversion-induced LIM interaction with Src reveals a novel Src inactivation cycle
Zhang, Y., Tu, Y., Zhao, J., Chen, K., & Wu, C. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810155 · Cited by 46
Regulation of VCP/p97 demonstrates the critical balance between cell death and epithelial-mesenchymal transition (EMT) downstream of ER stress
Shah, P. P., & Beverly, L. J. (2015) · Oncotarget · doi:10.18632/oncotarget.3918 · Cited by 45
The large GTPase dynamin2: A new player in connexin 43 gap junction endocytosis, recycling and degradation
Gilleron, J., Carette, D., Fiorini, C., Dompierre, J., Macia, E., Denizot, J., Segretain, D., & Pointis, G. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2011.04.014 · Cited by 45
Reusable amperometric biosensor for measuring protein tyrosine kinase activity.
Wang, C.-L., Wei, L.-Y., Yuan, C., & Hwang, K. (2012) · Analytical Chemistry · doi:10.1021/ac202369d · Cited by 41
Micro RNA ‐27b suppresses tumor progression by regulating ARFGEF 1 and focal adhesion signaling
Matsuyama, R., Okuzaki, D., Okada, M., & Oneyama, C. (2015) · Cancer Science · doi:10.1111/cas.12834 · Cited by 45
E2F1 silencing inhibits migration and invasion of osteosarcoma cells via regulating DDR1 expression
Wang, Z., Sun, X., Bao, Y., Mo, J., Du, H., Hu, J., & Zhang, X. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4165 · Cited by 45
Pyrazolo–pyrimidine‐derived c‐Src inhibitor reduces angiogenesis and survival of squamous carcinoma cells by suppressing vascular endothelial growth factor production and signaling
Donnini, S., Monti, M., Castagnini, C., Solito, R., Botta, M., Schenone, S., Giachetti, A., & Ziche, M. (2006) · International Journal of Cancer · doi:10.1002/ijc.22410 · Cited by 45
Resequencing and copy number analysis of the human tyrosine kinase gene family in poorly differentiated gastric cancer
Kubo, T., Kuroda, Y., Shimizu, H., Kokubu, A., Okada, N., Hosoda, F., Arai, Y., Nakamura, Y., Taniguchi, H., Yanagihara, K., et al. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp206 · Cited by 45
Growth factor receptor-Src-mediated suppression of GRK6 dysregulates CXCR4 signaling and promotes medulloblastoma migration
Yuan, L., Zhang, H., Liu, J., Rubin, J. B., Cho, Y., Shu, H. G., Schniederjan, M., & MacDonald, T. J. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-18 · Cited by 44
DGKA interacts with SRC/FAK to promote the metastasis of non-small cell lung cancer
Fu, L., Deng, R., Huang, Y., Yang, X., Jiang, N., Zhou, J., Lin, C., Chen, S., Wu, L., Cui, Q., et al. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215585 · Cited by 43
Activation of c-Src and Fyn Kinases by Protein-tyrosine Phosphatase RPTPα Is Substrate-specific and Compatible with Lipid Raft Localization
Vacaresse, N., Møller, B. K., Danielsen, E. M., Okada, M., & Sap, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807964200 · Cited by 44
Identification of 7-Phenylaminothieno- [3,2-b]pyridine-6-carbonitriles as a New Class of Src Kinase Inhibitors
Boschelli, D. H., Wu, B., Sosa, A. C. B., Durutlic, H., Ye, F., Raifeld, Y. E., Golas, J. M., & Boschelli, F. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049237m · Cited by 45
Luteinization of porcine preovulatory follicles leads to systematic changes in follicular gene expression
Agca, C., Ries, J. E., Kolath, S. J., Kim, J.-H., Forrester, L. J., Antoniou, E., Whitworth, K. M., Mathialagan, N., Springer, G. K., Prather, R. S., et al. (2006) · Reproduction · doi:10.1530/rep.1.01163 · Cited by 45
Specific Oncogenic Activity of the Src-Family Tyrosine Kinase c-Yes in Colon Carcinoma Cells
Sancier, F., Dumont, A., Sirvent, A., de Plater, L., Edmonds, T., David, G., Jan, M., de Montrion, C., Cogé, F., Léonce, S., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017237 · Cited by 43
Role of Akt2 in regulation of metastasis suppressor 1 expression and colorectal cancer metastasis
Agarwal, E., Robb, C. M., Smith, L., Brattain, M. G., Wang, J., Black, J. D., & Chowdhury, S. (2017) · Oncogene · doi:10.1038/onc.2016.460 · Cited by 43
Elongation factor-2 kinase (eEF-2K) expression is associated with poor patient survival and promotes proliferation, invasion and tumor growth of lung cancer
Bircan, A., Gürbüz, N., Pataer, A., Caner, A., Kahraman, N., Bayraktar, E., Bayraktar, R., Erdoğan, M. A., Kabil, N. N., & Özpolat, B. (2018) · Lung Cancer · doi:10.1016/j.lungcan.2018.07.027 · Cited by 44
Enhanced Anticancer Activity of Nanoformulation of Dasatinib against Triple-Negative Breast Cancer
Bahman, F., Pittalà, V., Haider, M. A., & Greish, K. F. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11060559 · Cited by 41
Apigenin Inhibits NNK-Induced Focal Adhesion Kinase Activation in Pancreatic Cancer Cells
Pham, H., Chen, M. F., Takahashi, H., King, J. C., Reber, H. A., Hines, O. J., Pandol, S., & Eibl, G. (2012) · Pancreas · doi:10.1097/mpa.0b013e31824d64d9 · Cited by 43
Src kinase inhibitors: an emerging therapeutic treatment option for prostate cancer
Edwards, J. (2010) · Expert Opinion on Investigational Drugs · doi:10.1517/13543781003789388 · Cited by 44
Inhibitors of Protein Tyrosine Phosphatase PTP1B With Anticancer Potential
Kostrzewa, T., Styszko, J., Górska‐Ponikowska, M., Śledziński, T., & Kuban‐Jankowska, A. (2019) · Anticancer Research · doi:10.21873/anticanres.13481 · Cited by 42
Fibroblast growth factor-2 stimulates proliferation of human adipose-derived stem cells via Src activation
Ma, Y., Kakudo, N., Morimoto, N., Lai, F., Taketani, S., & Kusumoto, K. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1462-z · Cited by 42
Inhibitors of ABL and the ABL-T315I Mutation
Noronha, G., Cao, J., Chow, C. P., Dneprovskaia, E., Fine, R., Hood, J. D., Kang, X., Klebansky, B., Lohse, D., Mak, C., et al. (2008) · Current Topics in Medicinal Chemistry · doi:10.2174/156802608784911635 · Cited by 42
Saracatinib (AZD0530) is a potent modulator of ABCB1‐mediated multidrug resistancein vitroandin vivo
Liu, K., He, J., Su, X., Sim, H., Xie, J., Chen, X.-G., Wang, F., Liang, Y.-J., Singh, S., Sodani, K. S., et al. (2012) · International Journal of Cancer · doi:10.1002/ijc.27649 · Cited by 41
Deregulated Expression of SRC, LYN and CKB Kinases by DNA Methylation and Its Potential Role in Gastric Cancer Invasiveness and Metastasis
Mello, A. A., Leal, M. F., REY, J. A., Pinto, G. R., Lamarão, L. M., Montenegro, R. C., Alves, A. P. N. N., de Assumpção, P. P., Borges, B. D. N., Smith, M. D. A. C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140492 · Cited by 41

Authors: Summy, J. M., & Gallick, G. E.
Affiliations: The University of Texas MD Anderson Cancer Center (US)
Corresponding author: Gallick, Gary E.
Venue: Cancer and Metastasis Reviews
Publisher: Springer Science and Business Media LLC
Published: 2003-12
Volume: 22
Issue: 4
Pages: 337-358
ISSN: 0167-7659 (ISSN-L)
1573-7233
DOI: 10.1023/a:1023772912750
OpenAlex: W1589166971
Cited by: 827
References: 171
Citations by year: 2026: 15 · 2025: 15 · 2024: 17 · 2023: 17 · 2022: 26 · 2021: 27 · 2020: 26 · 2019: 35 · 2018: 32 · 2017: 28 · 2016: 32 · 2015: 37 · 2014: 64 · 2013: 55 · 2012: 49
FWCI: 4.32
Type: journal article
Language: en
Open access: closed
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: Cancer and Metastasis Reviews (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ca065527-07)
National Cancer Institute (U54CA090810, 2 R01 CA65527)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Mechanisms and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mechanisms of cancer metastasis
Keywords: Src family kinases, Src kinase, non-receptor tyrosine kinase, tumor progression, metastasis, constitutive kinase activation, v-Src, malignant transformation, cell migration and invasion, angiogenesis, apoptosis resistance, cancer therapeutics, colorectal cancer, breast cancer, melanoma, lung cancer
MeSH terms: Enzyme Activation, Humans, Neoplasm Metastasis, Neoplasms, Neovascularization, Pathologic, Signal Transduction, Disease Progression, src-Family Kinases

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

Src family kinases in tumor progression and metastasis

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