卵巢癌正在成為對女性的威脅，78% 被診斷出患有卵巢癌的女性在診斷後至少存活 1 年。 更糟的是，癌症復發和抗藥性的可能性很高。 Hyptolide 作為一種天然化合物，已被證明具有抗發炎、抗菌作用，最新研究發現它還具有抗癌作用。 Hyptolide 的有效特性為治療卵巢癌（包括化療抗藥性的病例）提供了潛在的解決方案。 然而，Hyptolide在化療抗藥性卵巢癌中的作用尚未得到證實，且Hyptolide誘導細胞死亡的機制仍不清楚。 在這項研究中，我們的目的是弄清楚 Hyptolide 對卵巢癌細胞系的影響，包括野生型、順鉑抗藥性和紫杉醇抗藥性細胞系。 我們也研究了 Hyptolide 治療的潛在機制。 結果表明，無論卵巢癌細胞係是否具有化療抗藥性，Hyptolide 都會抑制其細胞活力。 細胞凋亡的機制是由內質網壓力透過GRP78和ATF6的活化所介導的。 在對順鉑化療抗藥性的細胞系中，Hyptolide 可以透過活化 GSK3β 並促進 β-catenin 的細胞質定位（由 Src 抑制介導）來增加 E-cadherin。 此外，在順鉑化療抗藥性細胞系中，海普托利特和順鉑聯合治療顯示出協同作用，增強細胞凋亡。 此外，Hyptolide 增強了順鉑的細胞攝取，同時減少了其外流，如順鉑化療抗藥性細胞系中 ABCG2 和 P-gp 標記物的調節所示。 總之，我們的研究結果表明，hyptolide 透過誘導 ER 壓力介導的細胞死亡並克服順鉑化療抗藥性，具有作為替代化療藥物的潛力。 這種效應歸因於其活化 GSK3β 和增加 E-鈣黏蛋白作為間質上皮轉化 (MET) 的雙重作用。

Ovarian cancer is emerging as a threat to women, and 78% of women diagnosed with ovarian cancer live for at least 1 year after diagnosis. Even worse, there is a high chance of cancer relapse and drug resistance. Hyptolide, as a natural compound, has been revealed to act as an anti-inflammatory and antibacterial agent, and the latest research discovers that it acts as an anticancer agent. The potent properties of hyptolide offer a potential solution to treat ovarian cancer, including cases with chemo-resistance. However, the effect of hyptolide in chemo-resistant ovarian cancer has not been demonstrated, and the mechanism underlying hyptolide to induce cell death is still unclear. In this research, we aim to figure out the effect of hyptolide on ovarian cancer cell lines, including wild-type, cisplatin-resistant, and paclitaxel-resistant lines. We also investigate the underlying mechanism of hyptolide treatment. The results showed that hyptolide inhibited cell viability in ovarian cancer cell lines regardless of their chemo-resistance. The mechanism of apoptosis was mediated by ER stress with the activation of GRP78 and ATF6. In the cisplatin chemo-resistant cell lines, hyptolide could increase E-cadherin by activating GSK3β and facilitating cytoplasm localization of β-catenin, which is mediated by Src inhibition. Furthermore, the combined therapy involving hyptolide and cisplatin in cisplatin chemo-resistant cell lines demonstrated a synergistic effect, enhancing cell apoptosis. Additionally, hyptolide augmented the cellular uptake of cisplatin while reducing its efflux, as indicated by the modulation of ABCG2 and P-gp markers in the cisplatin chemo-resistant cell line. In conclusion, our findings suggest that hyptolide has the potential as an alternative chemotherapeutic agent by inducing cell death mediated through ER stress and overcoming cisplatin chemoresistance. This effect is attributed to its dual action of activating GSK3β and increasing E-cadherin as a mesenchymal-epithelial transition (MET).

Ackers, I., & Malgor, R. (2018). Interrelationship of canonical and non-canonical Wnt signalling pathways in chronic metabolic diseases. Diab Vasc Dis Res, 15(1), 3-13. doi:10.1177/1479164117738442
Adachi, Y., Yamamoto, K., Okada, T.,et al. (2008). ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct Funct, 33(1), 75-89. doi:10.1247/csf.07044
Alvi, Q., Baloch, G. M., Chinna, K., & Dabbagh, A. (2020). Lifestyle and reproductive health: the aetiology of ovarian cancer in Pakistan. F1000Res, 9, 901. doi:10.12688/f1000research.24866.1
Baghal-Sadriforoush, S., Bagheri, M., Abdi Rad, I., & Sotoodeh Nejadnematalahi, F. (2022). PI3K Inhibition Sensitize the Cisplatin-resistant Human Ovarian Cancer Cell OVCAR3 by Induction of Oxidative Stress. Rep Biochem Mol Biol, 10(4), 675-685. doi:10.52547/rbmb.10.4.675
Baldwin, L. A., Huang, B., Miller, R. W., Tucker, T., et al. (2012). Ten-year relative survival for epithelial ovarian cancer. Obstetrics & Gynecology, 120(3), 612-618. doi: 10.1097/AOG.0b013e318264f794
Bañuelos-Hernández, A. E., Mendoza-Espinoza, J. A., Pereda-Miranda, R., & Cerda-García- Rojas, C. M. (2014). Studies of (−)-Pironetin Binding to α-Tubulin: Conformation, Docking, and Molecular Dynamics. The Journal of Organic Chemistry, 79(9), 3752- 3764. doi:10.1021/jo500420j
Barbosa, C., Aquino, P., Ribeiro-Júnior, K., Moura, F., et al. (2012). Cytotoxic and antitumor activities of Hyptis pectinata (Sambacaitá) extract. Pharmacologyonline, 3, 70-74.
Bayat Mokhtari, R., Homayouni, T. S., Baluch, N., et al. (2017). Combination therapy in combating cancer. Oncotarget, 8(23), 38022-38043. doi:10.18632/oncotarget.16723
Benedeković, G., Kovačević, I., Popsavin, M., et al. (2016). New antitumour agents with α,β-unsaturated δ-lactone scaffold: Synthesis and antiproliferative activity of (−)-cleistenolide and analogues. Bioorganic & Medicinal Chemistry Letters, 26(14), 3318-3321. doi:10.1016/j.bmcl.2016.05.044
Bispo, M., Mourão, R., Franzotti, E. M., Bomfim, K. B. R., et al. (2001). Antinociceptive and antiedematogenic effects of the aqueous extract of Hyptis pectinata leaves in experimental animals. Journal of Ethnopharmacology, 76, 81-86. doi:10.1016/S0378-8741(01)00172-6
Brett M. Reid, J. B. P., and Thomas A. Sellers. (2017). Epidemiology of ovarian cancer: a review. Cancer biology and medicine, 14, 9–32. doi: 10.20892/j.issn.2095- 3941.2016.0084
Brewer, H. R., Chadeau-Hyam, M., Johnson, E., et al. (2023). Cancer Loyalty Card Study (CLOCS): feasibility outcomes for an observational case–control study focusing on the patient interval in ovarian cancer. BMJ Open, 13(6), e066022. Retrieved from https://bmjopen.bmj.com/content/bmjopen/13/6/e066022.full.pdf. doi:10.1136/bmjopen-2022-066022
Carter, J. S., & Downs, L. S., Jr. (2011). Ovarian Cancer Tests and Treatment. Female Patient (Parsippany), 36(4), 30-35.
Chakraborty, T., & Purkait, S. (2008). Total synthesis of hyptolide. Tetrahedron Letters - TETRAHEDRON LETT, 49, 5502-5504. doi:10.1016/j.tetlet.2008.07.033
Chockley, P. J., & Keshamouni, V. G. (2016). Immunological Consequences of Epithelial-Mesenchymal Transition in Tumor Progression. J Immunol, 197(3), 691-698. doi:10.4049/jimmunol.1600458
Claudio Hetz, K. Z., Randal J Kaufman. (2020). Mechanisms, regulation and functions of the unfolded protein response. Nature reviews molecular cell biology, 21, 421-438. doi:doi.org/10.1038/s41580-020-0250-z
Cubillos-Ruiz, X. C. J. R. (2021). Endoplasmic reticulum stress signals in the tumour and its microenvironment. Nature Reviews Cancer, 21, 71-88. doi:doi.org/10.1038/s41568-020- 00312-2
Duda, P., Akula, S. M., Abrams, S. L., Steelman, L., et al. (2020). Targeting GSK3 and Associated Signaling Pathways Involved in Cancer. Cells, 9(5). doi:10.3390/cells9051110
Fagotto, F. (2013). Looking beyond the Wnt pathway for the deep nature of betacatenin. EMBO Rep., 14:4, 22–33. doi:10.1038/embor.2013.45
Fruman, D. A., & Rommel, C. (2014). PI3K and cancer: lessons, challenges and opportunities. Nature reviews Drug discovery, 13(2), 140-156. doi:10.1038/nrd4204
Hagen, T., & Vidal-Puig, A. (2002). Characterisation of the phosphorylation of β-catenin at the GSK-3 priming site Ser45. Biochemical and Biophysical Research Communications, 294(2), 324-328. doi:10.1016/
Hankey, W., Frankel, W. L., & Groden, J. (2018). Functions of the APC tumor suppressor protein dependent and independent of canonical WNT signaling: implications for therapeutic targeting. Cancer Metastasis Rev, 37(1), 159-172. doi:10.1007/s10555-017-9725-6
Huang, J., Zhang, L., Greshock, J., Colligon, T. A., et al. (2011). Frequent genetic abnormalities of the PI3K/AKT pathway in primary ovarian cancer predict patient outcome. Genes, Chromosomes and cancer, 50(8), 606-618. doi:10.1002/gcc.20883
Irtegun, S., Wood, R. J., Ormsby, A. R., Mulhern, T. D., & Hatters, D. M. (2013). Tyrosine 416 is phosphorylated in the closed, repressed conformation of c-Src. PloS one, 8(7), e71035. doi:10.1371/journal.pone.0071035
Iurlaro, R., & Muñoz-Pinedo, C. (2016). Cell death induced by endoplasmic reticulum stress.
Febs j, 283(14), 2640-2652. doi:10.1111/febs.13598
JA McCubrey, L. S., FE Bertrand, NM Davis, et al. (2014). Multifaceted roles of GSK-3 and Wnt/b-catenin in hematopoiesis and leukemogenesis: opportunities for therapeutic intervention. Leukemia, 28, 15-33. doi: 10.1038/leu.2013.184
Jing Tian, R. L., and Quanxin Qu. (2017). Role of endoplasmic reticulum stress on cisplatin resistance in ovarian carcinoma. Oncology letter, 13, 1437-1443. doi:10.3892/ol.2017.5580
Jintao Lin, T. S., Cong Li, Weifeng Mao. (2020). GSK-3β in DNA repair, apoptosis, and resistance of chemotherapy, radiotherapy of cancer. Molecular Cell Research, 1867. doi:10.1016/j.bbamcr.2020.118659
Junjie Huang, W. C. C., Chun Ho Ngai, Veeleah Lok, et al. (2022). Worldwide Burden, Risk Factors, and Temporal Trends of Ovarian Cancer: A Global Study. Cancers, 14. doi:10.3390/cancers14092230
Jurj, A., Ionescu, C., Berindan-Neagoe, I., & Braicu, C. (2022). The extracellular matrix alteration, implication in modulation of drug resistance mechanism: friends or foes? Journal of Experimental & Clinical Cancer Research, 41(1), 276. Retrieved from https://doi.org/10.1186/s13046-022-02484-1. doi:10.1186/s13046-022-02484-1
Kalluri, R., & Weinberg, R. A. (2009). The basics of epithelial-mesenchymal transition. J Clin Invest, 119(6), 1420-1428. doi:10.1172/jci39104
Karni, R., Gus, Y., Dor, Y., Meyuhas, O., & Levitzki, A. (2005). Active Src elevates the expression of beta-catenin by enhancement of cap-dependent translation. Mol Cell Biol, 25(12), 5031-5039. doi:10.1128/mcb.25.12.5031-5039.2005
Lee, J., & Kim, M.-S. (2007). The role of GSK3 in glucose homeostasis and the development of insulin resistance. Diabetes Research and Clinical Practice, 77(3, Supplement), S49-S57. doi: 10.1016/j.diabres.2007.01.033
Levine, D. A., Bogomolniy, F., Yee, C. J., Lash, A., Barakat, R. R., Borgen, P. I., & Boyd, J. (2005). Frequent mutation of the PIK3CA gene in ovarian and breast cancers. Clinical Cancer Research, 11(8), 2875-2878. doi:10.1158/0008-5472.CAN-04-2933
Lisboa, A. C. C. D., Mello, I. C. M., Nunes, R. S., Dos Santos, M. A., et al. (2006). Antinociceptive effect of Hyptis pectinata leaves extracts. Fitoterapia, 77 6, 439-442.
Liu, X., Zhou, X. Q., Shang, X. W., Wang, L., et al. (2020). Inhibition of chemotherapy-related breast tumor EMT by application of redox-sensitive siRNA delivery system CSO-ss-SA/siRNA along with doxorubicin treatment. J Zhejiang Univ Sci B, 21(3), 218-233. doi:10.1631/jzus.B1900468
Min, J. K., Park, H. S., Lee, Y. B., et al. (2022). Cross-Talk between Wnt Signaling and Src Tyrosine Kinase. Biomedicines, 10(5). doi:10.3390/biomedicines10051112
Mislav Glibo, A. S., Valentina Karin-Kujundzic, Ivanka Bekavac Vlatkovic, et al. (2021). The role of glycogen synthase kinase 3 (GSK3) in cancer with emphasis on ovarian cancer development and progression: A comprehensive review. Basic Medical Science., 21. doi:10.17305/bjbms.2020.5036
Mo, W., & Zhang, J. T. (2012). Human ABCG2: structure, function, and its role in multidrug resistance. Int J Biochem Mol Biol, 3(1), 1-27.
Peng, D. J., Wang, J., Zhou, J. Y., & Wu, G. S. (2010). Role of the Akt/mTOR survival pathway in cisplatin resistance in ovarian cancer cells. Biochem Biophys Res Commun, 394(3), 600-605. doi:10.1016/j.bbrc.2010.03.029
Petrova, Y. I., Schecterson, L., & Gumbiner, B. M. (2016). Roles for E-cadherin cell surface regulation in cancer. Mol Biol Cell, 27(21), 3233-3244. doi:10.1091/mbc.E16-01- 0058
Melchinger, P., & Garcia, B. M. (2023). Mitochondria are midfield players in steroid synthesis. Int J Biochem Cell Biol, 160, 106431. doi:10.1016/j.biocel.2023.106431
Meldolesi, J., & Pozzan, T. (1998). The endoplasmic reticulum Ca2+ store: a view from the lumen. Trends Biochem Sci, 23(1), 10-14. doi:10.1016/s0968-0004(97)011432
Miyano, T., Suzuki, A., & Sakamoto, N. (2021). Hyperosmotic stress induces epithelial-mesenchymal transition through rearrangements of focal adhesions in tubular epithelial cells. PloS one, 16(12), e0261345. doi:10.1371/journal.pone.0261345
Morin, PJ. (1999). Beta-catenin signaling and cancer. Bioessay, 21(12). doi: 10.1002/(SICI)1521-1878(199912)22:1<1021::AID-BIES6>3.0.CO;2-P
Nishimura, H., Nakamura, O., Yamagami, Y., Mori, M., et al. (2016). GSK-3 inhibitor inhibits cell proliferation and induces apoptosis in human osteosarcoma cells. Oncol Rep, 35(4), 2348-2354. doi:10.3892/or.2016.4565
Prat, J. (2014). Staging classification for cancer of the ovary, fallopian tube, and peritoneum. International Journal of Gynecology & Obstetrics, 124(1), 1-5. doi: doi.org/10.1016/j.ijgo.2013.10.001
Qin, K., Yu, M., Fan, J., Wang, H., et al. (2024). Canonical and noncanonical Wnt signaling: Multilayered mediators, signaling mechanisms, and major signaling crosstalk. Genes & Diseases, 11(1), 103-134. doi:10.1016/j.gendis
Rao, R. V., & Bredesen, D. E. (2004). Misfolded proteins, endoplasmic reticulum stress, and neurodegeneration. Curr Opin Cell Biol, 16(6), 653-662. doi:10.1016/j.ceb.2004.09.012
Raj Kumar Yadav, S.-W. C., Hyung-Ryong Kim, and Han Jung Chae. (2014). Endoplasmic Reticulum Stress and Cancer. Journal of Cancer Prevention, 19, 75-88. doi: 10.15430/JCP.2014.19.2.75
Raymundo, L. J., Guilhon, C. C., Alviano, D. S., Matheus, et al. (2011). Characterisation of the anti-inflammatory and antinociceptive activities of the Hyptis pectinata (L.) Poit essential oil. Journal Ethnopharmacol, 134(3), 725-732. doi:10.1016/j.jep.2011.01.027
Rebecca C. Arend, A. I. L.-J., J. Michael Straughn Jr., Donald J. Buchsbaum. (2013). The Wnt/β-catenin pathway in ovarian cancer: A review. Gynecologic Oncology, 131(3), 772-229. doi:10.1016/j.ygyno.2013.09.034
Rinne, N., Christie, E. L., Ardasheva, A., Kwok, C. H., Demchenko, N, et al (2021). Targeting the PI3K/AKT/mTOR pathway in epithelial ovarian cancer, therapeutic treatment options for platinum-resistant ovarian cancer. Cancer Drug Resist, 4(3), 573-595. doi:10.20517/cdr.2021.05
Rozpedek, W., Pytel, D., Mucha, B., Leszczynska, H., Diehl, J. A., & Majsterek, I. (2016). The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress. Curr Mol Med, 16(6), 533-544. doi:10.2174/1566524016666160523143937
Sachin Gopalkrishna Pai, B. A. C., Jose Mauricio Mota, Ricardo Costa, et al. (2017). Wnt/beta-catenin pathway: modulating anticancer immune response. Journal of Hematology & Oncology, 10 (1). doi:doi: 10.1186/s13045-017- 0471-6
Sano, R., & Reed, J. C. (2013). ER stress-induced cell death mechanisms. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1833(12), 3460-3470. doi:10.1016/j.bbamcr
Shan-Shan Li, J. M., and Alice S. T. Wong. (2018). Chemoresistance in ovarian cancer: exploiting cancer stem cell metabolism. Journal Gynecol Oncology, 29. doi: 10.3802/jgo.2018.29.e32
Sheema Hashem, T. A. A., Sabah Akhtar, Sabah Nisar, Geetanjali Sageena, et al. (2022). Targeting cancer signaling pathways by natural products: Exploring promising anti-cancer agents. Biomedicine & Pharmacotherapy, 150 (1). doi:10.1016/j.biopha.2022.113054
Sheng, Y. H., Leu, W. J., Chen, C. N., Hsu,et al. (2020). The (+)-Brevipolide H Displays Anticancer Activity against Human Castration-Resistant Prostate Cancer: The Role of Oxidative Stress and Akt/mTOR/p70S6K-Dependent Pathways in G1 Checkpoint Arrest and Apoptosis. MDPI:Molecules, 25(12). doi:10.3390/molecules25122929
Shin, M., McGowan, A., DiNatale, G. J., Chiramanewong, T., Cai, T., & Connor, R. E. (2017). Hsp72 Is an Intracellular Target of the α,β-Unsaturated Sesquiterpene Lactone, Parthenolide. ACS Omega, 2(10), 7267-7274. doi:10.1021/acsomega.7b00954
Santana, F. R., Luna-Dulcey, L., Antunes, V. U., Tormena, et al. (2020). Evaluation of the cytotoxicity on breast cancer cells of extracts and compounds isolated from Hyptis pectinata (L.) poit. Natural Product Research, 34(1), 102-109. doi:10.1080/14786419.2019.1628747
Siegel, R., Ma, J., Zou, Z., & Jemal, A. (2014). Cancer statistics, 2014. CA: a cancer journal for clinicians, 64(1), 9-29. doi:10.3322/caac.21208
Siwecka, N., Rozpędek-Kamińska, W., Wawrzynkiewicz, A., et al. (2021). The Structure, Activation, and Signaling of IRE1 and Its Role in Determining Cell Fate. Biomedicines, 9(2). doi:10.3390/biomedicines9020156
Son, H., & Moon, A. (2010). Epithelial-mesenchymal Transition and Cell Invasion. Toxicol Res, 26(4), 245-252. doi:10.5487/tr.2010.26.4.245
Song, W. J., Song, E. A., Jung, M. S., Choi, S. H., et al. (2015). Phosphorylation and inactivation of glycogen synthase kinase 3β (GSK3β) by dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A). Journal Biology Chemistry, 290(4), 2321-2333. doi:10.1074/jbc.M114.594952
Stronach, E. A., Chen, M., Maginn, E. N., Agarwal, R., Mills, G. B., Wasan, H., & Gabra,
H. (2011). DNA-PK mediates AKT activation and apoptosis inhibition in clinically acquired platinum resistance. Neoplasia, 13(11). doi:10.1593/neo.111032
Suzery, M., Cahyono, B., & Amalina, N. (2020). Antiproliferative and apoptosis effect of hyptolide from Hyptis pectinata (L.) Poit on human breast cancer cells ARTICLE INFO. Journal of Applied Pharmaceutical Science, 10, 1-006. doi:10.7324/JAPS.2020.102001
Tam, S. Y., Wu, V. W. C., & Law, H. K. W. (2020). Hypoxia-Induced Epithelial-Mesenchymal Transition in Cancers: HIF-1α and Beyond. Front Oncol, 10, 486. doi:10.3389/fonc.2020.00486
Tomas Valenta, G. H., and Konrad Baslera. (2012). The many faces and functions of β- catenin. The Embo Journal, 31, 2714-2736. doi: 10.1038/emboj.2012.150
Vu Hong Loan Nguyen, R. H., Stefanie Bernaudo, and Chun Peng. (2019). Wnt/β-catenin signaling in ovarian cancer: Insights into its hyperactivation and function in tumorigenesis. Journal Ovarian Research, 12(122). doi:doi.org/10.1186/s13048-019- 0596-z
Wang, M., Wey, S., Zhang, Y., Ye, R., & Lee, A. S. (2009). Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders. Antioxid Redox Signal, 11(9), 2307-2316. doi:10.1089/ars.2009.2485
Wen-Tai Chiu, Y.-F. H., Huei-Yu Tsai, Chien-Chin Chen, et al. (2015). FOXM1 confers to epithelial-mesenchymal transition, stemness, and chemoresistance in epithelial ovarian carcinoma cells. Oncogene, 6 (4).
Xu, Y., Yu, H., Qin, H., Kang, J., Yu, C., et al. (2012). Inhibition of autophagy enhances cisplatin cytotoxicity through endoplasmic reticulum stress in human cervical cancer cells. Cancer Letters, 314(2), 232-243. doi:10.1016/j.canlet.2011.09.034
Xue-Li Pang, G. H., Yang-Bo Liu, Yan Wang, and Bo Zhang. (2013). Endoplasmic reticulum stress sensitizes human esophageal cancer cells to radiation. World Journal of Gastroenterol, 19, 1736-1748. doi:10.3748/wjg.v19.i11.1736
Yang, J., Antin, P., Berx, G., Blanpain, C., Brabletz, T., Bronner, M (2020). Guidelines and definitions for research on epithelial–mesenchymal transition. Nature Reviews Molecular Cell Biology, 21(6), 341-352. doi:10.1038/s41580-020-0237-9
Yang, J., & Weinberg, R. A. (2008). Epithelial-mesenchymal transition: at the crossroads of development and tumor metastasis. Developmental cell, 14(6), 818-829. doi:10.1016/j.devcel.2008.05.009
Yang, S.-m., Huang, C., Li, X.-f., et al. (2013). miR-21 confers cisplatin resistance in gastric cancer cells by regulating PTEN. Toxicology, 306, 162-168.
Yokoi, A., Minami, M., Hashimura, M., Oguri, Y., et al. (2022). PTEN overexpression and nuclear β-catenin stabilization promote morular differentiation through induction of epithelial-mesenchymal transition and cancer stem cell-like properties in endometrial carcinoma. Cell Commun Signal, 20(1), 181. doi:10.1186/s12964-022-00999-w
Zeng, G., Apte, U., Micsenyi, A., Bell, A., & Monga, S. P. (2006). Tyrosine residues 654 and 670 in beta-catenin are crucial in the regulation of Met-beta-catenin interactions. Exp Cell Res, 312(18), 3620-3630. doi:10.1016/j.yexcr.2006.08.003
Zhan, Y., Chen, Z., Li, Y., He, A., He, S., et al. (2018). Long non-coding RNA DANCR promotes malignant phenotypes of bladder cancer cells by modulating the miR-149/MSI2 axis as a ceRNA. J Exp Clin Cancer Res, 37(1), 273. doi:10.1186/s13046-018-0921-1
Zhou, Z., Edil, B. H., & Li, M. (2023). Combination therapies for cancer: challenges and opportunities. BMC Medicine, 21(1), 171. doi:10.1186/s12916-023-02852-4