| 1. | Hasegawa-Minato Junko, Toyoshima Masafumi, Ishibashi Masumi, et al. Novel cooperative pathway of c-Myc and Furin, a pro-protein convertase, in cell proliferation as a therapeutic target in ovarian cancers. Oncotarget. 2018; 9 (3): 3483-3496. doi:10.18632/oncotarget.23322 | ||
| 2. | Ishibashi Masumi, Toyoshima Masafumi, Zhang Xuewei, et al. Tyrosine kinase receptor TIE-1 mediates platinum resistance by promoting nucleotide excision repair in ovarian cancer. Scientific Reports. 2018; 8 (1): 13207. doi:10.1038/s41598-018-31069-2 | ||
| 3. | Zhang Xuewei, Kitatani Kazuyuki, Toyoshima Masafumi, et al. Ceramide nanoliposomes as a MLKL-dependent, necroptosis-inducing, chemotherapeutic reagent in ovarian cancer. Molecular Cancer Therapeutics. 2017; : molcanther.0173.2017. doi:10.1158/1535-7163.MCT-17-0173 | ||
| 4. | Wada M, Canals D, Adada M, et al. P38 delta MAPK promotes breast cancer progression and lung metastasis by enhancing cell proliferation and cell detachment. Oncogene. 2017; 36 (47): 6649-6657. doi:10.1038/onc.2017.274 | ||
| 5. | Kitatani Kazuyuki, Iwabuchi Kazuhisa, Snider Ashley, Riboni Laura. Sphingolipids in Inflammation: From Bench to Bedside. Mediators of Inflammation. 2016; 2016 : 1-2. doi:10.1155/2016/7602526 | ||
| 6. | Shigeta S, Toyoshima M, Kitatani K, et al. Transferrin facilitates the formation of DNA double-strand breaks via transferrin receptor 1: the possible involvement of transferrin in carcinogenesis of high-grade serous ovarian cancer. Oncogene. 2016; 35 (27): 3577-86. doi:10.1038/onc.2015.425 | ||
| 7. | Mizuno Satoshi, Ogishima Soichi, Kitatani Kazuyuki, et al. Network Analysis of a Comprehensive Knowledge Repository Reveals a Dual Role for Ceramide in Alzheimer's Disease. PloS one. 2016; 11 (2): e0148431. doi:10.1371/journal.pone.0148431 | ||
| 8. | Mashiko Satsuki, Kitatani Kazuyuki, Toyoshima Masafumi, et al. Inhibition of plasminogen activator inhibitor-1 is a potential therapeutic strategy in ovarian cancer. Cancer biology & therapy. 2015; 16 (2): 253-60. doi:10.1080/15384047.2014.1001271 | ||
| 9. | Taniguchi M, Ogiso H, Takeuchi T, et al. Lysosomal ceramide generated by acid sphingomyelinase triggers cytosolic cathepsin B-mediated degradation of X-linked inhibitor of apoptosis protein in natural killer/T lymphoma cell apoptosis. Cell death & disease. 2015; 6 : e1717. doi:10.1038/cddis.2015.82 | ||
| 10. | Kitatani Kazuyuki, Taniguchi Makoto, Okazaki Toshiro. Role of Sphingolipids and Metabolizing Enzymes in Hematological Malignancies. Molecules and cells. 2015; 38 (6): 482-95. doi:10.14348/molcells.2015.0118 | ||
| 11. | Kitatani K, Usui T, Sriraman S K, et al. Ceramide limits phosphatidylinositol-3-kinase C2β-controlled cell motility in ovarian cancer: potential of ceramide as a metastasis-suppressor lipid. Oncogene. 2015; 35 (21): 2801-2812. doi:10.1038/onc.2015.330 | ||
| 12. | Kitatani Kazuyuki, Wada Masayuki, Perry David, et al. Activation of p38 Mitogen-Activated Protein Kinase in Gaucher's Disease. PloS one. 2015; 10 (8): e0136633. doi:10.1371/journal.pone.0136633 | ||
| 13. | Perry David M, Newcomb Benjamin, Adada Mohamad, et al. Defining a role for acid sphingomyelinase in the p38/interleukin-6 pathway. The Journal of biological chemistry. 2014; 289 (32): 22401-12. doi:10.1074/jbc.M114.589648 |