AXL Is an Essential Factor and Therapeutic Target for Metastatic Ovarian Cancer

New functions for the matrix metalloproteinases in cancer progression

Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108 · see citing works

Matrix Metalloproteinase Inhibitors and Cancer—Trials and Tribulations

Coussens, L. M., Fingleton, B., & Matrisian, L. M. (2002) · Science · doi:10.1126/science.1067100 · Cited by 2,761 · see citing works

The Origin and Pathogenesis of Epithelial Ovarian Cancer: A Proposed Unifying Theory

Kurman, R. J., & Shih, I. (2010) · The American Journal of Surgical Pathology · doi:10.1097/pas.0b013e3181cf3d79 · Cited by 1,850 · see citing works

Tumor Self-Seeding by Circulating Cancer Cells

Kim, M.-Y., Oskarsson, T., Acharyya, S., Nguyen, D. X., Zhang, X. H.-F., Norton, L., & Massagué, J. (2009) · Cell · doi:10.1016/j.cell.2009.11.025 · Cited by 1,335 · see citing works

TAM Receptor Tyrosine Kinases: Biologic Functions, Signaling, and Potential Therapeutic Targeting in Human Cancer

Linger, R. M. A., Keating, A. K., Earp, H. S., & Graham, D. K. (2008) · Advances in cancer research · doi:10.1016/s0065-230x(08)00002-x · Cited by 750 · see citing works

axl, a transforming gene isolated from primary human myeloid leukemia cells, encodes a novel receptor tyrosine kinase.

O’Bryan, J. P., Frye, R. A., Cogswell, P. C., Neubauer, A., Kitch, B., Prokop, C. A., Espinosa, R., Beau, M. M. L., Earp, H. S., & Liu, E. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.10.5016 · Cited by 746 · see citing works

Homeostatic Regulation of the Immune System by Receptor Tyrosine Kinases of the Tyro 3 Family

Lu, Q., & Lemke, G. (2001) · Science · doi:10.1126/science.1061663 · Cited by 699 · see citing works

Axl is an essential epithelial-to-mesenchymal transition-induced regulator of breast cancer metastasis and patient survival

Gjerdrum, C., Tiron, C., Høiby, T., Stefansson, I., Haugen, H., Sandal, T., Collett, K., Li, S., McCormack, E., Gjertsen, B. T., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909333107 · Cited by 594 · see citing works

Illuminating the metastatic process

Sahai, E. A. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2229 · Cited by 566 · see citing works

R428, a Selective Small Molecule Inhibitor of Axl Kinase, Blocks Tumor Spread and Prolongs Survival in Models of Metastatic Breast Cancer

Holland, S. J., Pan, A., Franci, C., Hu, Y., Chang, B. Y., Li, W., Duan, M., Torneros, A., Yu, J., Heckrodt, T. J., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2997 · Cited by 554 · see citing works

Targeting phosphoinositide 3-kinase—Moving towards therapy

Marone, R., Cmiljanović, V., Giese, B., & Wymann, M. P. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.10.003 · Cited by 548 · see citing works

Identification of the Product of Growth Arrest-specific Gene 6 as a Common Ligand for Axl, Sky, and Mer Receptor Tyrosine Kinases*

Nagata, K., Ohashi, K., Nakano, T., Arita, H., Zong, C., Hanafusa, H., & Mizuno, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.47.30022 · Cited by 541 · see citing works

Ovarian Cancer Metastasis: Integrating insights from disparate model organisms

Naora, H., & Montell, D. J. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1611 · Cited by 538 · see citing works

Mechanisms of transcoelomic metastasis in ovarian cancer

Tan, D. S. P., Agarwal, R., & Kaye, S. B. (2006) · The Lancet Oncology · doi:10.1016/s1470-2045(06)70939-1 · Cited by 521 · see citing works

Tyro-3 family receptors are essential regulators of mammalian spermatogenesis

Lu, Q., Gore, M., Zhang, Q., Camenisch, T., Boast, S., Casagranda, F., Lai, C., Skinner, M. K., Klein, R., Matsushima, G. K., et al. (1999) · Nature · doi:10.1038/19554 · Cited by 514 · see citing works

Deficiency or inhibition of Gas6 causes platelet dysfunction and protects mice against thrombosis

Angelillo-Scherrer, A., de Frutos, P. G., Aparicio, C., Melis, E., Savi, P., Lupu, F., Arnout, J., Dewerchin, M., Hoylaerts, M. F., Herbert, J.-M., et al. (2001) · Nature Medicine · doi:10.1038/84667 · Cited by 441 · see citing works

Frequent activation of AKT2 and induction of apoptosis by inhibition of phosphoinositide-3-OH kinase/Akt pathway in human ovarian cancer

Yuan, Z. Q., Sun, M., Feldman, R. I., Wang, G., Xiaoling, M., Jiang, C. C., Coppola, D., Nicosia, S. V., & Cheng, J. Q. (2000) · Oncogene · doi:10.1038/sj.onc.1203598 · Cited by 385 · see citing works

Expression of Angiogenesis-Related Genes and Progression of Human Ovarian Carcinomas in Nude Mice

Yoneda, J., Kuniyasu, H., Price, J. E., Bucana, C. D., Fidler, I. J., & Crispens, M. A. (1998) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/90.6.447 · Cited by 375 · see citing works

Precursor lesions of ovarian epithelial malignancy

Feeley, K. M., & Wells, M. L. (2001) · Histopathology · doi:10.1046/j.1365-2559.2001.01042.x · Cited by 351 · see citing works

Expression Profiling of Serous Low Malignant Potential, Low-Grade, and High-Grade Tumors of the Ovary

Bonome, T., Lee, J.-Y., Park, D.-C., Radonovich, M., Pise-Masison, C. A., Brady, J. N., Gardner, G. J., Hao, K., Wong, W. H., Barrett, J. C., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-2240 · Cited by 315 · see citing works

Axl as a potential therapeutic target in cancer: role of Axl in tumor growth, metastasis and angiogenesis

Li, Y., Ye, X., Tan, C., Hongo, J. A., Zha, J., Liu, J., Kallop, D. Y., Ludlam, M. J. C., & Pei, L. (2009) · Oncogene · doi:10.1038/onc.2009.212 · Cited by 289 · see citing works

Expression of Axl in Lung Adenocarcinoma and Correlation with Tumor Progression

Shinh, Y.-S., Lai, C.-Y., Kao, Y.-R., Shiah, S., Chu, Y., Lee, H., & Wu, C. (2005) · Neoplasia · doi:10.1593/neo.05640 · Cited by 274 · see citing works

Comparative evaluation of the antitumor activity of antiangiogenic proteins delivered by gene transfer

Kuo, C. J., Farnebo, F. A., Yu, E. Y., Christofferson, R. H. B., Swearingen, R. A., Carter, R., von Recum, H. A., Yuan, J., Kamihara, J., Flynn, E. A., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081615298 · Cited by 268 · see citing works

Twist mediates suppression of inflammation by type I IFNs and Axl

Sharif, M. N., Šošić, D., Rothlin, C. V., Kelly, E., Lemke, G., Olson, E. N., & Ivashkiv, L. B. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051725 · Cited by 251 · see citing works

Dominant-negative inhibition of the Axl receptor tyrosine kinase suppresses brain tumor cell growth and invasion and prolongs survival

Vajkoczy, P., Knyazev, P. G., Kunkel, A., Capelle, H., Behrndt, S., von Tengg‐Kobligk, H., Kiessling, F. M., Eichelsbacher, U., Essig, M., Read, T., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510923103 · Cited by 239 · see citing works

Receptor tyrosine kinase AXL is induced by chemotherapy drugs and overexpression of AXL confers drug resistance in acute myeloid leukemia

Hong, C., Lay, J., Huang, J.-S., Cheng, A., Tang, J., Lin, M., Lai, G., & Chuang, S. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.04.017 · Cited by 234 · see citing works

axl , a Transforming Gene Isolated from Primary Human Myeloid Leukemia Cells, Encodes a Novel Receptor Tyrosine Kinase

O’Bryan, J. P., Frye, R. A., Cogswell, P. C., Neubauer, A., Kitch, B., Prokop, C. A., Espinosa, R., Beau, M. M. L., Earp, H. S., & Liu, E. T. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.10.5016-5031.1991 · Cited by 232 · see citing works

AXL Is a Potential Target for Therapeutic Intervention in Breast Cancer Progression

Zhang, Y., Knyazev, P. G., Cheburkin, Y. V., Sharma, K., Knyazev, Y. P., Őrfi, L., Szabadkai, I., Daub, H., Kéri, G., & Ullrich, A. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-2661 · Cited by 214 · see citing works

The Axl receptor tyrosine kinase confers an adverse prognostic influence in pancreatic cancer and represents a new therapeutic target

Koorstra, J.-B. M., Karikari, C. A., Feldmann, G., Bisht, S., Rojas, P. L., Offerhaus, G. J. A., Alvarez, H., & Maitra, A. (2009) · Cancer Biology & Therapy · doi:10.4161/cbt.8.7.7923 · Cited by 208 · see citing works

Multiple Roles for the Receptor Tyrosine Kinase Axl in Tumor Formation

Holland, S. J., Powell, M. J., Franci, C., Chan, E. W., Friera, A. M., Atchison, R. E., McLaughlin, J. R., Swift, S. E., Pali, E. S., Yam, G. C., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0993 · Cited by 201 · see citing works

GAS6 Induces Axl-mediated Chemotaxis of Vascular Smooth Muscle Cells

Fridell, Y.-W. C., Villa, J., Attar, E. C., & Liu, E. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.7123 · Cited by 195 · see citing works

Axl promotes cell invasion by inducing MMP-9 activity through activation of NF-κB and Brg-1

Tai, K.-Y., Shieh, Y.-S., Lee, C.-S., Shiah, S., & Wu, C.-W. (2008) · Oncogene · doi:10.1038/onc.2008.57 · Cited by 170 · see citing works

Natural killer cell differentiation driven by Tyro3 receptor tyrosine kinases

Caraux, A., Lu, Q., Fernandez, N. C., Riou, S., Santo, J. P. D., Raulet, D. H., Lemke, G., & Roth, C. (2006) · Nature Immunology · doi:10.1038/ni1353 · Cited by 157 · see citing works

The role of genetic abnormalities of PTEN and the phosphatidylinositol 3-kinase pathway in breast and ovarian tumorigenesis, prognosis, and therapy

Mills, G. B., Lu, Y., Fang, X., Wang, H., Eder, A., Mao, M., Swaby, R., Cheng, K. W., Stokoe, D., Siminovitch, K., et al. (2001) · Seminars in Oncology · doi:10.1016/s0093-7754(01)90290-8 · Cited by 134 · see citing works

AKT2, a member of the protein kinase B family, is activated by growth factors, v-Ha-ras, and v-src through phosphatidylinositol 3-kinase in human ovarian epithelial cancer cells.

Liu, A. X., Testa, J. R., Hamilton, T. C., Jove, R., Nicosia, S. V., & Cheng, J. Q. (1998) · PubMed · Cited by 130 · see citing works

Expression of the receptor protein-tyrosine kinases Tyro-3, Axl, and Mer in the developing rat central nervous system

Prieto, A. L., Weber, J. L., & Lai, C. (2000) · The Journal of Comparative Neurology · doi:10.1002/1096-9861(20000918)425:2 · Cited by 119 · see citing works

Sulfasalazine Suppresses Drug Resistance and Invasiveness of Lung Adenocarcinoma Cells Expressing AXL

Lay, J., Hong, C., Huang, J.-S., Yang, Y.-Y., Pao, C.-Y., Liu, C.-H., Lai, Y.-P., Lai, G., Cheng, A., Su, I., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3191 · Cited by 114 · see citing works

Role of Gas6 in erythropoiesis and anemia in mice

Angelillo‐Scherrer, A., Burnier, L., Lambrechts, D., Fish, R. J., Tjwa, M., Plaisance, S., Sugamele, R., DeMol, M., Martínez-Soria, E., Maxwell, P. H., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci30375 · Cited by 100 · see citing works

Soluble receptor-mediated selective inhibition of VEGFR and PDGFRβ signaling during physiologic and tumor angiogenesis

Kuhnert, F., Tam, B. Y. Y., Sennino, B., Gray, J. T., Yuan, J., Jocson, A., Nayak, N. R., Mulligan, R. C., McDonald, D. M., & Kuo, C. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803194105 · Cited by 97 · see citing works

Crystal Structure of a C-terminal Fragment of Growth Arrest-specific Protein Gas6

Sasaki, T., Knyazev, P. G., Cheburkin, Y. V., Göhring, W., Tisi, D., Ullrich, A., Timpl, R., & Hohenester, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207340200 · Cited by 91 · see citing works

Gonadotropins Activate Proteolysis and Increase Invasion through Protein Kinase A and Phosphatidylinositol 3-Kinase Pathways in Human Epithelial Ovarian Cancer Cells

Choi, J., Choi, K., Auersperg, N., & Leung, P. C. K. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-1785 · Cited by 73 · see citing works

Identification of genes associated with ovarian cancer metastasis using microarray expression analysis

Lancaster, J. M., Dressman, H. K., Clarke, J., Sayer, R. A., Martino, M. A., Cragun, J. M., Henriott, A., Gray, J., Sutphen, R., Elahi, A. H., et al. (2006) · International Journal of Gynecological Cancer · doi:10.1111/j.1525-1438.2006.00660.x · Cited by 67 · see citing works

Increased staining for phosphorylated AKT and nuclear factor‐κB p65 and their relationship with prognosis in epithelial ovarian cancer

Guo, R., Qiao, Y., Zhou, Y., Li, L., Shi, H., & Chen, K. (2008) · Pathology International · doi:10.1111/j.1440-1827.2008.02306.x · Cited by 60 · see citing works

Inflammation: A hidden path to breaking the spell of ovarian cancer

Shan, W., & Liu, J. (2009) · Cell Cycle · doi:10.4161/cc.8.19.9590 · Cited by 59 · see citing works

Adhesion-Related Kinase Induction of Migration Requires Phosphatidylinositol-3-Kinase and Ras Stimulation of Rac Activity in Immortalized Gonadotropin-Releasing Hormone Neuronal Cells

Nielsen‐Preiss, S. M., Allen, M. P., Xu, M., Linseman, D. A., Pawlowski, J. E., Bouchard, R. J., Varnum, B. C., Heidenreich, K. A., & Wierman, M. E. (2007) · Endocrinology · doi:10.1210/en.2007-0039 · Cited by 59 · see citing works

New agents for the treatment of ovarian cancer: the next generation

Dupont, J., Aghajanian, C. A., Sabbatini, P. J., & Spriggs, D. R. (2005) · International Journal of Gynecological Cancer · doi:10.1111/j.1525-1438.2005.00443.x · Cited by 11 · see citing works

Hypoxic control of metastasis

Rankin, E. B., & Giaccia, A. J. (2016) · Science · doi:10.1126/science.aaf4405 · Cited by 1,340 · see citing works

Biomarkers for the early diagnosis of hepatocellular carcinoma

Tsuchiya, N. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i37.10573 · Cited by 571 · see citing works

AXL receptor tyrosine kinase as a promising anti-cancer approach: functions, molecular mechanisms and clinical applications

Zhu, C., Wei, Y., & Wei, X. (2019) · Molecular Cancer · doi:10.1186/s12943-019-1090-3 · Cited by 498 · see citing works

Targeting MET and AXL overcomes resistance to sunitinib therapy in renal cell carcinoma

Zhou, L., Liu, X.-D., Sun, M., Zhang, X., German, P., Bai, S., Ding, Z., Tannir, N. M., Wood, C. G., Matin, S. F., et al. (2015) · Oncogene · doi:10.1038/onc.2015.343 · Cited by 400 · see citing works

AXL induces epithelial-to-mesenchymal transition and regulates the function of breast cancer stem cells

Asiedu, M. K., Beauchamp‐Perez, F., Ingle, J. N., Behrens, M. D., Radisky, D. C., & Knutson, K. L. (2013) · Oncogene · doi:10.1038/onc.2013.57 · Cited by 302 · see citing works

Direct regulation of GAS6/AXL signaling by HIF promotes renal metastasis through SRC and MET

Rankin, E. B., Fuh, K. C., Castellini, L., Viswanathan, K., Finger, E. C., Diep, A. N., LaGory, E. L., Kariolis, M. S., Chan, A., Lindgren, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404848111 · Cited by 269 · see citing works

Targeting Axl and Mer Kinases in Cancer

Verma, A. R., Warner, S. L., Vankayalapati, H., Bearss, D. J., & Sharma, S. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0116 · Cited by 226 · see citing works

AXL Mediates Resistance to Cetuximab Therapy

Brand, T. M., Iida, M., Stein, A. P., Corrigan, K. L., Braverman, C. M., Luthar, N., Toulany, M., Gill, P. S., Salgia, R., Kimple, R. J., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0294 · Cited by 198 · see citing works

AXL kinase as a novel target for cancer therapy

Wu, X., Liu, X., Koul, S., Lee, C. Y., Zhang, Z., & Halmos, B. (2014) · Oncotarget · doi:10.18632/oncotarget.2542 · Cited by 191 · see citing works

METTL3 promotes ovarian carcinoma growth and invasion through the regulation of AXL translation and epithelial to mesenchymal transition

Hua, W., Zhao, Y., Jin, X., Yu, D., He, J., Xie, D., & Duan, P. (2018) · Gynecologic Oncology · doi:10.1016/j.ygyno.2018.09.015 · Cited by 193 · see citing works

Axl as a mediator of cellular growth and survival

Axelrod, H. D., & Pienta, K. J. (2014) · Oncotarget · doi:10.18632/oncotarget.2422 · Cited by 190 · see citing works

AXL-Driven EMT State as a Targetable Conduit in Cancer

Antony, J., & Huang, R. Y. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0392 · Cited by 182 · see citing works

The Receptor Tyrosine Kinase AXL in Cancer Progression

Rankin, E. B., & Giaccia, A. J. (2016) · Cancers · doi:10.3390/cancers8110103 · Cited by 170 · see citing works

Receptor tyrosine kinase Axl is required for resistance of leukemic cells to FLT3-targeted therapy in acute myeloid leukemia

Park, I.-K., Mundy-Bosse, B. L., Whitman, S. P., Zhang, X., Warner, S. L., Bearss, D. J., Blum, W. G., Marcucci, G., & Caligiuri, M. A. (2015) · Leukemia · doi:10.1038/leu.2015.147 · Cited by 163 · see citing works

The receptor tyrosine kinase Axl in cancer: Biological functions and therapeutic implications

Paccez, J. D., Vogelsang, M., Parker, M. I., & Zerbini, L. F. (2013) · International Journal of Cancer · doi:10.1002/ijc.28246 · Cited by 148 · see citing works

The Receptor Tyrosine Kinase AXL Is Required at Multiple Steps of the Metastatic Cascade during HER2-Positive Breast Cancer Progression

Goyette, M.-A., Duhamel, S., Aubert, L., Pelletier, A., Savage, P., Thibault, M.-P., Johnson, R. M., Carmeliet, P., Basik, M., Gaboury, L. A., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.019 · Cited by 144 · see citing works

An engineered Axl 'decoy receptor' effectively silences the Gas6-Axl signaling axis

Kariolis, M. S., Miao, Y. R., Jones, D. S., Kapur, S., Mathews, I. I., Giaccia, A. J., & Cochran, J. R. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1636 · Cited by 143 · see citing works

The receptor tyrosine kinase Axl is an essential regulator of prostate cancer proliferation and tumor growth and represents a new therapeutic target

Paccez, J. D., Vasques, G. J., Correa, R. G., de Vasconcellos, J. F., Duncan, K., Gu, X., Bhasin, M., Libermann, T. A., & Zerbini, L. F. (2012) · Oncogene · doi:10.1038/onc.2012.89 · Cited by 141 · see citing works

GAS6 Receptor Status Is Associated with Dormancy and Bone Metastatic Tumor Formation

Taichman, R. S., Patel, L. R., Bedenis, R., Wang, J., Weidner, S., Schumann, T., Yumoto, K., Berry, J. E., Shiozawa, Y., & Pienta, K. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0061873 · Cited by 133 · see citing works

Ultrasensitive tumour-penetrating nanosensors of protease activity

Kwon, E. J., Dudani, J. S., & Bhatia, S. N. (2017) · Nature Biomedical Engineering · doi:10.1038/s41551-017-0054 · Cited by 131 · see citing works

Molecular Pathways: AXL, a Membrane Receptor Mediator of Resistance to Therapy

Scaltriti, M., Elkabets, M., & Baselga, J. M. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-1458 · Cited by 123 · see citing works

Molecular Pathways: Receptor Ectodomain Shedding in Treatment, Resistance, and Monitoring of Cancer

Miller, M. A., Sullivan, R. J., & Lauffenburger, D. A. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-0869 · Cited by 125 · see citing works

The HIF target MAFF promotes tumor invasion and metastasis through IL11 and STAT3 signaling

Moon, E. J., Mello, S. S., Li, C. G., Chi, J., Thakkar, K. N., Kirkland, J. G., LaGory, E. L., Lee, I. J., Diep, A. N., Miao, Y. R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24631-6 · Cited by 128 · see citing works

AXL Is a Logical Molecular Target in Head and Neck Squamous Cell Carcinoma

Brand, T. M., Iida, M., Stein, A. P., Corrigan, K. L., Braverman, C. M., Coan, J. P., Pearson, H. E., Bahrar, H., Fowler, T. L., Bednarz, B. P., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2648 · Cited by 119 · see citing works

ONO-7475, a Novel AXL Inhibitor, Suppresses the Adaptive Resistance to Initial EGFR-TKI Treatment in EGFR -Mutated Non–Small Cell Lung Cancer

Okura, N., Nishioka, N., Yamada, T., Taniguchi, H., Tanimura, K., Katayama, Y., Yoshimura, A., Watanabe, S., Kikuchi, T., Shiotsu, S., et al. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-19-2321 · Cited by 120 · see citing works

Fra-1 controls motility of bladder cancer cells via transcriptional upregulation of the receptor tyrosine kinase AXL

Sayan, E., Stanford, R., Vickery, R., Grigorenko, E. V., Diesch, J., Kulbicki, K., Edwards, R., Pal, R., Greaves, P., Jariel‐Encontre, I., et al. (2011) · Oncogene · doi:10.1038/onc.2011.336 · Cited by 119 · see citing works

The GAS6-AXL signaling network is a mesenchymal (Mes) molecular subtype–specific therapeutic target for ovarian cancer

Antony, J., Tan, T. Z., Kelly, Z. L., Low, J. J. H., Choolani, M. A., Recchi, C., Gabra, H., Thiery, J. P., & Huang, R. Y. (2016) · Science Signaling · doi:10.1126/scisignal.aaf8175 · Cited by 118 · see citing works

Inhibition of the GAS6/AXL pathway augments the efficacy of chemotherapies

Kariolis, M. S., Miao, Y. R., Diep, A. N., Nash, S. E., Olcina, M. M., Jiang, D., Jones, D. S., Kapur, S., Mathews, I. I., Koong, A. C., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci85610 · Cited by 108 · see citing works

Gas6/Axl mediates tumor cell apoptosis, migration and invasion and predicts the clinical outcome of osteosarcoma patients

Han, J., Tian, R., Yong, B., Luo, C., Tan, P., Shen, J., & Peng, T. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.05.019 · Cited by 109 · see citing works

Inhibition of the receptor tyrosine kinase Axl impedes activation of the FLT3 internal tandem duplication in human acute myeloid leukemia: implications for Axl as a potential therapeutic target

Park, I., Mishra, A., Chandler, J. C., Whitman, S. P., Marcucci, G., & Caligiuri, M. A. (2013) · Blood · doi:10.1182/blood-2012-07-444018 · Cited by 108 · see citing works

Preclinical validation of AXL receptor as a target for antibody-based pancreatic cancer immunotherapy

Leconet, W., Larbouret, C., Chardès, T., Thomas, G., Neiveyans, M., Busson, M., Jarlier, M., Radosevic‐Robin, N., Pugnière, M., Bernex, F., et al. (2013) · Oncogene · doi:10.1038/onc.2013.487 · Cited by 107 · see citing works

Axl-EGFR receptor tyrosine kinase hetero-interaction provides EGFR with access to pro-invasive signalling in cancer cells

Vouri, M., Croucher, D. R., Kennedy, S. P., An, Q., Pilkington, G. J., & Hafizi, S. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.66 · Cited by 106 · see citing works

Activation of TYRO3/AXL Tyrosine Kinase Receptors in Thyroid Cancer

Avilla, E., Guarino, V., Visciano, C., Liotti, F., Svelto, M., Krishnamoorthy, G., Franco, R., & Melillo, R. M. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2186 · Cited by 103 · see citing works

The GAS6-AXL signaling pathway triggers actin remodeling that drives membrane ruffling, macropinocytosis, and cancer-cell invasion

Zdżalik-Bielecka, D., Poświata, A., Kozik, K., Jastrzębski, K., Schink, K. O., Brewińska‐Olchowik, M., Piwocka, K., Stenmark, H., & Miączyńska, M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024596118 · Cited by 103 · see citing works

Migration/Invasion of Malignant Gliomas and Implications for Therapeutic Treatment

Liu, C.-A., Chang, C., Hsueh, K.-W., Su, H.-L., Chiou, T., Lin, S., & Harn, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041115 · Cited by 102 · see citing works

Axl inhibition induces the antitumor immune response which can be further potentiated by PD-1 blockade in the mouse cancer models

Guo, Z., Li, Y., Zhang, D., & Ma, J. (2017) · Oncotarget · doi:10.18632/oncotarget.21125 · Cited by 99 · see citing works

TAM family kinases as therapeutic targets at the interface of cancer and immunity

DeRyckere, D., Huelse, J. M., Earp, H. S., & Graham, D. K. (2023) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-023-00813-7 · Cited by 98 · see citing works

Therapeutic Targeting of the Gas6/Axl Signaling Pathway in Cancer

Tanaka, M., & Siemann, D. W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189953 · Cited by 94 · see citing works

Pyruvate uptake is increased in highly invasive ovarian cancer cells under anoikis conditions for anaplerosis, mitochondrial function, and migration

Caneba, C. A., Bellancé, N., Yang, L., Pabst, L., & Nagrath, D. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00151.2012 · Cited by 94 · see citing works

The EZH2 inhibitor GSK343 suppresses cancer stem-like phenotypes and reverses mesenchymal transition in glioma cells

Yu, T., Wang, Y., Hu, Q., Wu, W., Wu, Y., Wei, W., Han, D., You, Y., Lin, N., & Liu, N. (2017) · Oncotarget · doi:10.18632/oncotarget.21311 · Cited by 93 · see citing works

AXL signaling in cancer: from molecular insights to targeted therapies

Yadav, M., Sharma, A., Patne, K., Tabasum, S., Suryavanshi, J., Rawat, L., Machaalani, M., Eid, M., Singh, R. P., Choueiri, T. K., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02121-7 · Cited by 96 · see citing works

The Role of the Receptor Tyrosine Kinase Axl in Carcinogenesis and Development of Therapeutic Resistance: An Overview of Molecular Mechanisms and Future Applications

Wium, M., Ajayi-Smith, A. F., Paccez, J. D., & Zerbini, L. F. (2021) · Cancers · doi:10.3390/cancers13071521 · Cited by 81 · see citing works

Polarization of tumor-associated macrophages and Gas6/Axl signaling in oral squamous cell carcinoma

Chiu, K., Lee, C.-H., Liu, S.-Y., Chou, Y., Huang, R., Huang, S., & Shieh, Y. (2015) · Oral Oncology · doi:10.1016/j.oraloncology.2015.04.004 · Cited by 79 · see citing works

AXL Receptor Tyrosine Kinase as a Promising Therapeutic Target Directing Multiple Aspects of Cancer Progression and Metastasis

Goyette, M.-A., & Côté, J. (2022) · Cancers · doi:10.3390/cancers14030466 · Cited by 79 · see citing works

Therapeutic targeting of the functionally elusive TAM receptor family

Miao, Y. R., Rankin, E. B., & Giaccia, A. J. (2023) · Nature Reviews Drug Discovery · doi:10.1038/s41573-023-00846-8 · Cited by 84 · see citing works

Therapeutic Targeting of AXL Receptor Tyrosine Kinase Inhibits Tumor Growth and Intraperitoneal Metastasis in Ovarian Cancer Models

Kanlikilicer, P., Özpolat, B., Aslan, B., Bayraktar, R., Gürbüz, N., Rodriguez‐Aguayo, C., Bayraktar, E., Denizli, M., González-Villasana, V., Ivan, C., et al. (2017) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2017.06.023 · Cited by 77 · see citing works

Homing of Cancer Cells to the Bone

Mishra, A., Shiozawa, Y., Pienta, K. J., & Taichman, R. S. (2011) · Cancer Microenvironment · doi:10.1007/s12307-011-0083-6 · Cited by 76 · see citing works

TWIST1 drives cisplatin resistance and cell survival in an ovarian cancer model, via upregulation of GAS6, L1CAM, and Akt signalling

Roberts, C. M., Tran, M. A., Pitruzzello, M. C., Wen, W. X., Loeza, J., Dellinger, T. H., Mor, G., & Glackin, C. A. (2016) · Scientific Reports · doi:10.1038/srep37652 · Cited by 72 · see citing works

Targeted Axl Inhibition Primes Chronic Lymphocytic Leukemia B Cells to Apoptosis and Shows Synergistic/Additive Effects in Combination with BTK Inhibitors

Sinha, S., Boysen, J. C., Nelson, M., Secreto, C. R., Warner, S. L., Bearss, D. J., Lesnick, C. E., Shanafelt, T. D., Kay, N. E., & Ghosh, A. K. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1892 · Cited by 74 · see citing works

Axl inhibitors as novel cancer therapeutic agents

Shen, Y., Chen, X., He, J., Liao, D., & Zu, X. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.02.033 · Cited by 71 · see citing works

Cancer stem-like cells enriched with CD29 and CD44 markers exhibit molecular characteristics with epithelial–mesenchymal transition in squamous cell carcinoma

Geng, S., Guo, Y., Wang, Q., Li, L., & Wang, J. (2012) · Archives of Dermatological Research · doi:10.1007/s00403-012-1260-2 · Cited by 72 · see citing works

The Dual Role of TAM Receptors in Autoimmune Diseases and Cancer: An Overview

Wium, M., Paccez, J. D., & Zerbini, L. F. (2018) · Cells · doi:10.3390/cells7100166 · Cited by 68 · see citing works

Epithelial-to-mesenchymal transition: lessons from development, insights into cancer and the potential of EMT-subtype based therapeutic intervention

Antony, J., Thiery, J. P., & Huang, R. Y. (2019) · Physical Biology · doi:10.1088/1478-3975/ab157a · Cited by 68 · see citing works

Treatment of Ovarian Cancer Beyond PARP Inhibition: Current and Future Options

Garg, V., & Oza, A. M. (2023) · Drugs · doi:10.1007/s40265-023-01934-0 · Cited by 69 · see citing works

Global phosphotyrosine survey in triple-negative breast cancer reveals activation of multiple tyrosine kinase signaling pathways

Wu, X., Zahari, M. S., Ma, B., Liu, R., Renuse, S., Sahasrabuddhe, N. A., Chen, L., Chaerkady, R., Kim, M., Zhong, J., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5020 · Cited by 66 · see citing works

MERTK Mediates Intrinsic and Adaptive Resistance to AXL-targeting Agents

McDaniel, N. K., Cummings, C. T., Iida, M., Huelse, J. M., Pearson, H. E., Vasileiadi, E., Parker, R. E., Orbuch, R. A., Ondracek, O. J., Welke, N. B., et al. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-1239 · Cited by 66 · see citing works

Implications of Hypoxia in Breast Cancer Metastasis to Bone

Gilkes, D. M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17101669 · Cited by 63 · see citing works

Targeting Axl favors an antitumorigenic microenvironment that enhances immunotherapy responses by decreasing Hif-1α levels

Goyette, M.-A., Elkholi, I. E., Apcher, C., Kuasne, H., Rothlin, C. V., Muller, W. J., Richard, D. E., Park, M., Gratton, J., & Côté, J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2023868118 · Cited by 64 · see citing works

4-Oxo-1,4-dihydroquinoline-3-carboxamide Derivatives as New Axl Kinase Inhibitors

Tan, L., Zhang, Z., Gao, D., Luo, J., Tu, Z., Li, Z., Peng, L., Ren, X., & Ding, K. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00608 · Cited by 61 · see citing works

METTL3 promotes the initiation and metastasis of ovarian cancer by inhibiting CCNG2 expression via promoting the maturation of pri-microRNA-1246

Bi, X., Lv, X., Liu, D. J., Guo, H., Yao, G., Wang, L., Liang, X., & Yang, Y. (2021) · Cell Death Discovery · doi:10.1038/s41420-021-00600-2 · Cited by 61 · see citing works

The histone demethylase KDM4B regulates peritoneal seeding of ovarian cancer

Wilson, C. B., Qiu, L., Hong, Y., Karnik, T., Tadros, G., Mau, B., Ma, T., Mu, Y., New, J., Louie, R. J., et al. (2016) · Oncogene · doi:10.1038/onc.2016.412 · Cited by 59 · see citing works

Erratum to: Cancer stem-like cells enriched with CD29 and CD44 markers exhibit molecular characteristics with epithelial–mesenchymal transition in squamous cell carcinoma

Geng, S., Guo, Y., Wang, Q., Li, L., & Wang, J. (2017) · Archives of Dermatological Research · doi:10.1007/s00403-017-1737-0 · Cited by 59 · see citing works

GAS6 expression identifies high-risk adult AML patients: potential implications for therapy

Whitman, S. P., Kohlschmidt, J., Maharry, K. S., Volinia, S., Mrózek, K., Nicolet, D., Schwind, S., Becker, H., Metzeler, K. H., Mendler, J. H., et al. (2013) · Leukemia · doi:10.1038/leu.2013.371 · Cited by 58 · see citing works

MAPK Activation Predicts Poor Outcome and the MEK Inhibitor, Selumetinib, Reverses Antiestrogen Resistance in ER-Positive High-Grade Serous Ovarian Cancer

Hew, K. E., Miller, P. C., El‐Ashry, D., Sun, J., Besser, A. H., Ince, T. A., Gu, M., Wei, Z., Zhang, G., Brafford, P. A., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-0534 · Cited by 58 · see citing works

High expression of CDC6 is associated with accelerated cell proliferation and poor prognosis of epithelial ovarian cancer

Deng, Y., Jiang, L., Wang, Y., Xi, Q., Zhong, J., Liu, J., Yang, S., Liu, R., Wang, J., Huang, M., et al. (2015) · Pathology - Research and Practice · doi:10.1016/j.prp.2015.09.014 · Cited by 56 · see citing works

MERTK controls melanoma cell migration and survival and differentially regulates cell behavior relative to AXL

Tworkoski, K., Platt, J. T., Bacchiocchi, A., Bosenberg, M., Boggon, T. J., & Stern, D. F. (2013) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12110 · Cited by 56 · see citing works

The Development of AXL Inhibitors in Lung Cancer: Recent Progress and Challenges

Sang, Y. B., Kim, J.-H., Kim, C.-G., Hong, M. H., Kim, H. R., Cho, B. C., & Lim, S. M. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.811247 · Cited by 56 · see citing works

Molecular Mechanism of 17-Allylamino-17-demethoxygeldanamycin (17-AAG)-induced AXL Receptor Tyrosine Kinase Degradation

Krishnamoorthy, G. P., Guida, T., Alfano, L., Avilla, E., Santoro, M. M., Carlomagno, F., & Melillo, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.439422 · Cited by 55 · see citing works

GAS6/AXL Inhibition Enhances Ovarian Cancer Sensitivity to Chemotherapy and PARP Inhibition through Increased DNA Damage and Enhanced Replication Stress

Mullen, M. M., Lomonosova, E., Toboni, M. D., Oplt, A., Cybulla, E., Blachut, B., Zhao, P., Noia, H., Wilke, D., Rankin, E. B., et al. (2021) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-21-0302 · Cited by 53 · see citing works

AXL Receptor in Cancer Metastasis and Drug Resistance: When Normal Functions Go Askew

Auyez, A., Sayan, E., Kriajevska, M. V., & Tulchinsky, E. M. (2021) · Cancers · doi:10.3390/cancers13194864 · Cited by 50 · see citing works

Promotion of Glioblastoma Cell Motility by Enhancer of Zeste Homolog 2 (EZH2) Is Mediated by AXL Receptor Kinase

Ott, M., Litzenburger, U. M., Sahm, F., Rauschenbach, K. J., Tudoran, R., Hartmann, C. J., Márquez, V. E., von Deimling, A., Wick, W., & Platten, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047663 · Cited by 52 · see citing works

Therapeutic Inhibition of the Receptor Tyrosine Kinase AXL Improves Sensitivity to Platinum and Taxane in Ovarian Cancer

Quinn, J. M., Greenwade, M. M., Palisoul, M. L., Opara, G., Massad, K., Guo, L., Zhao, P., Beck-Noia, H., Hagemann, I. S., Hagemann, A. R., et al. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-0537 · Cited by 52 · see citing works

Curcumin-induced downregulation of Axl receptor tyrosine kinase inhibits cell proliferation and circumvents chemoresistance in non-small lung cancer cells

KIM, K.-C., Baek, S., & Lee, C. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.3216 · Cited by 51 · see citing works

Small molecule inhibition of Axl receptor tyrosine kinase potently suppresses multiple malignant properties of glioma cells

Vouri, M., An, Q., Birt, M., Pilkington, G. J., & Hafizi, S. (2015) · Oncotarget · doi:10.18632/oncotarget.3952 · Cited by 49 · see citing works

Anticancer effect of luteolin is mediated by downregulation of TAM receptor tyrosine kinases, but not interleukin-8, in non-small cell lung cancer cells

Lee, Y. J., Lim, T., Han, M. S., Lee, S. H., Baek, S., Nan, H., & Lee, C. (2016) · Oncology Reports · doi:10.3892/or.2016.5336 · Cited by 49 · see citing works

Axl signaling is an important mediator of tumor angiogenesis

Tanaka, M., & Siemann, D. W. (2019) · Oncotarget · doi:10.18632/oncotarget.26882 · Cited by 48 · see citing works

Reversal of Cisplatin Resistance by Epigallocatechin Gallate Is Mediated by Downregulation of Axl and Tyro 3 Expression in Human Lung Cancer Cells

Kim, K.-C., & Lee, C. (2014) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2014.18.1.61 · Cited by 47 · see citing works

RNA m6A methylation regulators in ovarian cancer

Guo, J., Zheng, J., Zhang, H., & Tong, J. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02318-8 · Cited by 47 · see citing works

Implication of the Receptor Tyrosine Kinase AXL in Head and Neck Cancer Progression

von Mäßenhausen, A., Brägelmann, J., Billig, H., Thewes, B., Queisser, A., Vogel, W., Kristiansen, G., Schröck, A., Bootz, F., Brossart, P., et al. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms18010007 · Cited by 46 · see citing works

Bioinformatics analysis to screen the key prognostic genes in ovarian cancer

Li, L., Cai, S., Liu, S., Feng, H., & Zhang, J. (2017) · Journal of Ovarian Research · doi:10.1186/s13048-017-0323-6 · Cited by 45 · see citing works

Metformin targets Axl and Tyro3 receptor tyrosine kinases to inhibit cell proliferation and overcome chemoresistance in ovarian cancer cells

Kim, N., Lee, H., & Lee, C. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.3004 · Cited by 45 · see citing works

Gene Expression Profiles of the NCI-60 Human Tumor Cell Lines Define Molecular Interaction Networks Governing Cell Migration Processes

Kohn, K. W., Zeebèrg, B. R., Reinhold, W. C., Sunshine, M., Luna, A., & Pommier, Y. G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035716 · Cited by 40 · see citing works

Carvacrol Targets AXL to Inhibit Cell Proliferation and Migration in Non-small Cell Lung Cancer Cells

Jung, C. Y., Kim, S., & Lee, C. (2018) · Anticancer Research · doi:10.21873/anticanres.12219 · Cited by 38 · see citing works

AXL Controls Directed Migration of Mesenchymal Triple-Negative Breast Cancer Cells

Zajac, O., Leclère, R., Nicolas, A., Meseure, D., Marchiò, C., Vincent‐Salomon, A., Roman‐Roman, S., Schoumacher, M., & Dubois, T. (2020) · Cells · doi:10.3390/cells9010247 · Cited by 37 · see citing works

p85β regulates autophagic degradation of AXL to activate oncogenic signaling

Rao, L., Mak, V. C. Y., Zhou, Y., Zhang, D., Li, X., Fung, C. C. Y., Sharma, R., Gu, C., Lu, Y., Tipoe, G. L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16061-7 · Cited by 38 · see citing works

Phase 1b study of AVB-500 in combination with paclitaxel or pegylated liposomal doxorubicin platinum-resistant recurrent ovarian cancer

Fuh, K. C., Bookman, M. A., Liu, J. F., Coleman, R. L., Herzog, T. J., Thaker, P. H., Monk, B. J., Anderson, R., McIntyre, G., Rangwala, R. A., et al. (2021) · Gynecologic Oncology · doi:10.1016/j.ygyno.2021.08.020 · Cited by 37 · see citing works

Meta-Analysis of Microarray Data IdentifiesGAS6Expression as an Independent Predictor of Poor Survival in Ovarian Cancer

Buehler, M., Tse, B. W.-C., Leboucq, A., Jacob, F., Caduff, R. F., Fink, D. A., Goldstein, D. R., & Heinzelmann-Schwarz, V. A. (2013) · BioMed Research International · doi:10.1155/2013/238284 · Cited by 37 · see citing works

Soluble AXL: A Possible Circulating Biomarker for Neurofibromatosis Type 1 Related Tumor Burden

Johansson, G., Peng, P.-C., Huang, P.-Y., Chien, H., Hua, K., Kuo, M., Chen, C., & Lee, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115916 · Cited by 36 · see citing works

Gene of the month: Axl

Brown, M., Black, J. R., Sharma, R., Stebbing, J., & Pinato, D. J. (2016) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2016-203629 · Cited by 37 · see citing works

The tumour suppressor OPCML promotes AXL inactivation by the phosphatase PTPRG in ovarian cancer

Antony, J., Zanini, E., Kelly, Z., Tan, T. Z., Karali, E., Alomary, M. N., Jung, Y., Nixon, K., Cunnea, P., Fotopoulou, C., et al. (2018) · EMBO Reports · doi:10.15252/embr.201745670 · Cited by 36 · see citing works

Functional roles of enhancer of zeste homolog 2 in gliomas

Yin, Y., Qiu, S., & Peng, Y. (2015) · Gene · doi:10.1016/j.gene.2015.09.080 · Cited by 35 · see citing works

Targeting MERTK and AXL in EGFR Mutant Non-Small Cell Lung Cancer

Yan, D., Earp, H. S., DeRyckere, D., & Graham, D. K. (2021) · Cancers · doi:10.3390/cancers13225639 · Cited by 35 · see citing works

Aptamers as Potential Therapeutic Tools for Ovarian Cancer: Advancements and Challenges

Szymanowski, W., Szymanowska, A., Bielawska, A., Lopez‐Berestein, G., Rodriguez‐Aguayo, C., & Amero, P. (2023) · Cancers · doi:10.3390/cancers15215300 · Cited by 34 · see citing works

Novel Axl-driven signaling pathway and molecular signature characterize high-grade ovarian cancer patients with poor clinical outcome

Rea, K., Pinciroli, P., Sensi, M., Alciato, F., Bisarò, B., Lozneanu, L., Raspagliesi, F., Centritto, F., Cabodi, S., Defilippi, P., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5087 · Cited by 34 · see citing works

Inhibition of the Receptor Tyrosine Kinase AXL Restores Paclitaxel Chemosensitivity in Uterine Serous Cancer

Palisoul, M. L., Quinn, J. M., Schepers, E. J., Hagemann, I. S., Guo, L., Reger, K., Hagemann, A. R., McCourt, C. K., Thaker, P. H., Powell, M. A., et al. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0587 · Cited by 33 · see citing works

Therapeutic activity of DCC‐2036, a novel tyrosine kinase inhibitor, against triple‐negative breast cancer patient‐derived xenografts by targeting AXL/MET

Shen, Y., Zhang, W., Liu, J., He, J., Cao, R., Chen, X., Peng, X., Xu, H., Zhao, Q., Zhong, J., et al. (2018) · International Journal of Cancer · doi:10.1002/ijc.31915 · Cited by 34 · see citing works

Axl and prostasin are biomarkers for prognosis of ovarian adenocarcinoma

Chen, P., Li, Q., & Yang, Z. (2013) · Annals of Diagnostic Pathology · doi:10.1016/j.anndiagpath.2013.01.005 · Cited by 33 · see citing works

AXL modulates extracellular matrix protein expression and is essential for invasion and metastasis in endometrial cancer

Divine, L. M., Nguyen, M. R., Meller, E. H., Desai, R. A., Arif, B., Rankin, E. B., Bligard, K. H., Meyerson, C., Hagemann, I. S., Massad, M., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.12637 · Cited by 32 · see citing works

Inactivation of GSK3β and activation of NF-κB pathway via Axl represents an important mediator of tumorigenesis in esophageal squamous cell carcinoma

Paccez, J. D., Duncan, K., Vava, A., Correa, R. G., Libermann, T. A., Parker, M. I., & Zerbini, L. F. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-04-0868 · Cited by 32 · see citing works

Receptor Tyrosine Kinases in Osteosarcoma: Not Just the Usual Suspects

Rettew, A. N., Getty, P. J., & Greenfield, E. M. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-04843-7_3 · Cited by 30 · see citing works

Genetic inactivation of the receptor tyrosine kinase AXL inhibits invasion and metastasis in metastatic endometrial cancer

Divine, L. M., Lohrey, A. K., Nguyen, M. R., Meller, E. H., Massad, M., Powell, M. A., Mutch, D. G., McCourt, C. K., Rankin, E. B., & Fuh, K. C. (2016) · Gynecologic Oncology · doi:10.1016/j.ygyno.2016.04.415

Therapeutic Targeting of AXL Receptor Tyrosine Kinase Inhibits Tumor Growth and Intraperitoneal Metastasis in Ovarian Cancer Models

Kanlikilicer, P., Özpolat, B., Aslan, B., Bayraktar, R., Gürbüz, N., Rodriguez‐Aguayo, C., Bayraktar, E., Denizli, M., González-Villasana, V., Ivan, C., et al. (2017) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2017.06.023 · Cited by 77 · see citing works

Abstract IA012: Targeting AXL in platinum-resistant ovarian cancer: from the lab bench to Phase 3 trial

Fuh, K. C. (2024) · Cancer Research · doi:10.1158/1538-7445.ovarian23-ia012 · Cited by 1 · see citing works

The metastatic role of AXL, a receptor tyrosine kinase, in a genetically engineered mouse model of metastatic, endometrioid ovarian cancer

Fuh, K. C., Rankin, E. B., Wu, C., Diep, A. N., & Giaccia, A. J. (2015) · Gynecologic Oncology · doi:10.1016/j.ygyno.2015.01.139

The role of the receptor tyrosine kinase, AXL, in metastatic endometrial cancer

Divine, L. M., Gibson, A. A., Longmore, G. D., & Fuh, K. C. (2015) · Gynecologic Oncology · doi:10.1016/j.ygyno.2015.07.072