Dynamic interplay of nuclear receptors in tumor cell plasticity and drug resistance: Shifting gears in malignant transformations and applications in cancer therapeutics

1.

Hanahan, D., & Weinberg, R. A. (2011). Hallmarks of cancer: The next generation. Cell, 144(5), 646–674. https://doi.org/10.1016/j.cell.2011.02.013CrossRefPubMed

2.

Sung, H., Ferlay, J., Siegel, R. L., Laversanne, M., Soerjomataram, I., Jemal, A., et al. (2021). Global Cancer Statistics 2020: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries. CA: A Cancer Journal for Clinicians, 71(3), 209–249. https://doi.org/10.3322/caac.21660CrossRefPubMed

3.

Hanahan, D. (2022). Hallmarks of cancer: New dimensions. Cancer Discovery, 12(1), 31–46. https://doi.org/10.1158/2159-8290.CD-21-1059CrossRefPubMed

4.

Hanahan, D., & Weinberg, R. A. (2000). The hallmarks of cancer. Cell, 100(1), 57–70. https://doi.org/10.1016/s0092-8674(00)81683-9CrossRefPubMed

5.

Yuan, S., Norgard, R. J., & Stanger, B. Z. (2019). Cellular plasticity in cancer. Cancer Discov, 9(7), 837–851. https://doi.org/10.1158/2159-8290.CD-19-0015CrossRefPubMed

6.

Filip, S., Mokry, J., Horacek, J., & English, D. (2008). Stem cells and the phenomena of plasticity and diversity: A limiting property of carcinogenesis. Stem Cells Dev, 17(6), 1031–1038. https://doi.org/10.1089/scd.2007.0234CrossRefPubMed

7.

Mani, S. A., Guo, W., Liao, M. J., Eaton, E. N., Ayyanan, A., Zhou, A. Y., et al. (2008). The epithelial-mesenchymal transition generates cells with properties of stem cells. Cell, 133(4), 704–715. https://doi.org/10.1016/j.cell.2008.03.027CrossRefPubMedPubMedCentral

8.

Pastushenko, I., & Blanpain, C. (2019). EMT transition states during tumor progression and metastasis. Trends in Cell Biology, 29(3), 212–226. https://doi.org/10.1016/j.tcb.2018.12.001CrossRefPubMed

9.

Mansoori, B., Mohammadi, A., Davudian, S., Shirjang, S., & Baradaran, B. (2017). The different mechanisms of cancer drug resistance: A brief review. Adv Pharm Bull, 7(3), 339–34. https://doi.org/10.15171/apb.2017.041CrossRefPubMedPubMedCentral

10.

Bordoloi, D., Roy, N. K., Monisha, J., Padmavathi, G., & Kunnumakkara, A. B. (2016). Multi-targeted agents in cancer cell chemosensitization: What we learnt from curcumin thus far. Recent Patents on Anti-Cancer Drug Discovery, 11(1), 67–97. https://doi.org/10.2174/1574892810666151020101706CrossRefPubMed

11.

Kunnumakkara, A. B., Bordoloi, D., Sailo, B. L., Roy, N. K., Thakur, K. K., Banik, K., et al. (2019). Cancer drug development: The missing links. Experimental Biology and Medicine (Maywood, N.J.), 244(8), 663–689. https://doi.org/10.1177/1535370219839163CrossRefPubMed

12.

Longley, D. B., & Johnston, P. G. (2005). Molecular mechanisms of drug resistance. The Journal of Pathology, 205(2), 275–292. https://doi.org/10.1002/path.1706CrossRefPubMed

13.

Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schutz, G., Umesono, K., et al. (1995). The nuclear receptor superfamily: The second decade. Cell, 83(6), 835–839. https://doi.org/10.1016/0092-8674(95)90199-xCrossRefPubMedPubMedCentral

14.

Hoeck, J. D., Biehs, B., Kurtova, A. V., Kljavin, N. M., de Sousa, E. M. F., Alicke, B., et al. (2017). Stem cell plasticity enables hair regeneration following Lgr5(+) cell loss. Nature Cell Biology, 19(6), 666–676. https://doi.org/10.1038/ncb3535CrossRefPubMed

15.

Ge, Y., & Fuchs, E. (2018). Stretching the limits: From homeostasis to stem cell plasticity in wound healing and cancer. Nature Reviews Genetics, 19(5), 311–325. https://doi.org/10.1038/nrg.2018.9CrossRefPubMedPubMedCentral

16.

Brockmueller, A., Sajeev, A., Koklesova, L., Samuel, S. M., Kubatka, P., Busselberg, D., et al. (2023). Resveratrol as sensitizer in colorectal cancer plasticity. Cancer and Metastasis Reviews. https://doi.org/10.1007/s10555-023-10126-xCrossRefPubMed

17.

Shen, S., & Clairambault, J. (2020). Cell plasticity in cancer cell populations. F1000Research, 9, F1000 Faculty Rev-635. https://doi.org/10.12688/f1000research.24803.1CrossRefPubMedPubMedCentral

18.

Gupta, P. B., Pastushenko, I., Skibinski, A., Blanpain, C., & Kuperwasser, C. (2019). Phenotypic plasticity: Driver of cancer initiation, progression, and therapy resistance. Cell Stem Cell, 24(1), 65–78. https://doi.org/10.1016/j.stem.2018.11.011CrossRefPubMed

19.

Zeng, Z., Fu, M., Hu, Y., Wei, Y., Wei, X., & Luo, M. (2023). Regulation and signaling pathways in cancer stem cells: Implications for targeted therapy for cancer. Molecular Cancer, 22(1), 172. https://doi.org/10.1186/s12943-023-01877-wCrossRefPubMedPubMedCentral

20.

Reya, T., Morrison, S. J., Clarke, M. F., & Weissman, I. L. (2001). Stem cells, cancer, and cancer stem cells. Nature, 414(6859), 105–111. https://doi.org/10.1038/35102167CrossRefPubMed

21.

Dawood, S., Austin, L., & Cristofanilli, M. (2014). Cancer stem cells: implications for cancer therapy. Oncology (Williston Park, N.Y.), 28(12), 1101–1110.

22.

Al-Hajj, M., Wicha, M. S., Benito-Hernandez, A., Morrison, S. J., & Clarke, M. F. (2003). Prospective identification of tumorigenic breast cancer cells. Proc Natl Acad Sci U S A, 100(7), 3983–3988. https://doi.org/10.1073/pnas.0530291100CrossRefPubMedPubMedCentral

23.

Singh, S. K., Hawkins, C., Clarke, I. D., Squire, J. A., Bayani, J., Hide, T., et al. (2004). Identification of human brain tumour initiating cells. Nature, 432(7015), 396–401. https://doi.org/10.1038/nature03128CrossRefPubMed

24.

Beier, D., Hau, P., Proescholdt, M., Lohmeier, A., Wischhusen, J., Oefner, P. J., et al. (2007). CD133(+) and CD133(-) glioblastoma-derived cancer stem cells show differential growth characteristics and molecular profiles. Cancer Research, 67(9), 4010–4015. https://doi.org/10.1158/0008-5472.CAN-06-4180CrossRefPubMed

25.

Visvader, J. E., & Lindeman, G. J. (2008). Cancer stem cells in solid tumours: Accumulating evidence and unresolved questions. Nature Reviews Cancer, 8(10), 755–768. https://doi.org/10.1038/nrc2499CrossRefPubMed

26.

Mohan, A., Raj, R. R., Mohan, G., KP, P., & Maliekal, T. T. (2021). Reporters of cancer stem cells as a tool for drug discovery. Frontiers in Oncology, 11, 669250. https://doi.org/10.3389/fonc.2021.669250CrossRefPubMedPubMedCentral

27.

Sokol, S. Y. (2011). Maintaining embryonic stem cell pluripotency with Wnt signaling. Development, 138(20), 4341–4350. https://doi.org/10.1242/dev.066209CrossRefPubMedPubMedCentral

28.

Merchant, A. A., & Matsui, W. (2010). Targeting Hedgehog–a cancer stem cell pathway. Clinical Cancer Research, 16(12), 3130–3140. https://doi.org/10.1158/1078-0432.CCR-09-2846CrossRefPubMedPubMedCentral

29.

Zhu, Q., Shen, Y., Chen, X., He, J., Liu, J., & Zu, X. (2020). Self-renewal signalling pathway inhibitors: Perspectives on therapeutic approaches for cancer stem cells. Oncotargets and Therapy, 13, 525–540. https://doi.org/10.2147/OTT.S224465CrossRefPubMedPubMedCentral

30.

Machold, R., Hayashi, S., Rutlin, M., Muzumdar, M. D., Nery, S., Corbin, J. G., et al. (2003). Sonic hedgehog is required for progenitor cell maintenance in telencephalic stem cell niches. Neuron, 39(6), 937–950. https://doi.org/10.1016/s0896-6273(03)00561-0CrossRefPubMed

31.

Takahashi-Yanaga, F., & Kahn, M. (2010). Targeting Wnt signaling: Can we safely eradicate cancer stem cells? Clinical Cancer Research, 16(12), 3153–3162. https://doi.org/10.1158/1078-0432.CCR-09-2943CrossRefPubMed

32.

Hadjimichael, C., Chanoumidou, K., Papadopoulou, N., Arampatzi, P., Papamatheakis, J., & Kretsovali, A. (2015). Common stemness regulators of embryonic and cancer stem cells. World J Stem Cells, 7(9), 1150–1184. https://doi.org/10.4252/wjsc.v7.i9.1150CrossRefPubMedPubMedCentral

33.

Rich, J. N. (2016). Cancer stem cells: Understanding tumor hierarchy and heterogeneity. Medicine (Baltimore), 95(1 Suppl 1), S2–S7. https://doi.org/10.1097/MD.0000000000004764CrossRefPubMed

34.

Plaks, V., Kong, N., & Werb, Z. (2015). The cancer stem cell niche: How essential is the niche in regulating stemness of tumor cells? Cell Stem Cell, 16(3), 225–238. https://doi.org/10.1016/j.stem.2015.02.015CrossRefPubMedPubMedCentral

35.

Arumugam, T., Ramachandran, V., Fournier, K. F., Wang, H., Marquis, L., Abbruzzese, J. L., et al. (2009). Epithelial to mesenchymal transition contributes to drug resistance in pancreatic cancer. Cancer Research, 69(14), 5820–5828. https://doi.org/10.1158/0008-5472.CAN-08-2819CrossRefPubMedPubMedCentral

36.

Kurrey, N. K., Jalgaonkar, S. P., Joglekar, A. V., Ghanate, A. D., Chaskar, P. D., Doiphode, R. Y., et al. (2009). Snail and slug mediate radioresistance and chemoresistance by antagonizing p53-mediated apoptosis and acquiring a stem-like phenotype in ovarian cancer cells. Stem Cells, 27(9), 2059–2068. https://doi.org/10.1002/stem.154CrossRefPubMed

37.

Vega, S., Morales, A. V., Ocana, O. H., Valdes, F., Fabregat, I., & Nieto, M. A. (2004). Snail blocks the cell cycle and confers resistance to cell death. Genes & Development, 18(10), 1131–1143. https://doi.org/10.1101/gad.294104CrossRef

38.

Battula, V. L., Evans, K. W., Hollier, B. G., Shi, Y., Marini, F. C., Ayyanan, A., et al. (2010). Epithelial-mesenchymal transition-derived cells exhibit multilineage differentiation potential similar to mesenchymal stem cells. Stem Cells, 28(8), 1435–1445. https://doi.org/10.1002/stem.467CrossRefPubMed

39.

Guo, W., Keckesova, Z., Donaher, J. L., Shibue, T., Tischler, V., Reinhardt, F., et al. (2012). Slug and Sox9 cooperatively determine the mammary stem cell state. Cell, 148(5), 1015–1028. https://doi.org/10.1016/j.cell.2012.02.008CrossRefPubMedPubMedCentral

40.

Morel, A. P., Lievre, M., Thomas, C., Hinkal, G., Ansieau, S., & Puisieux, A. (2008). Generation of breast cancer stem cells through epithelial-mesenchymal transition. PLoS ONE, 3(8), e2888. https://doi.org/10.1371/journal.pone.0002888CrossRefPubMedPubMedCentral

41.

Vesuna, F., Lisok, A., Kimble, B., & Raman, V. (2009). Twist modulates breast cancer stem cells by transcriptional regulation of CD24 expression. Neoplasia, 11(12), 1318–1328. https://doi.org/10.1593/neo.91084CrossRefPubMedPubMedCentral

42.

Nieto, M. A., Huang, R. Y., Jackson, R. A., & Thiery, J. P. (2016). Emt: 2016. Cell, 166(1), 21–45. https://doi.org/10.1016/j.cell.2016.06.028CrossRefPubMed

43.

Celia-Terrassa, T., Meca-Cortes, O., Mateo, F., Martinez de Paz, A., Rubio, N., Arnal-Estape, A., et al. (2012). Epithelial-mesenchymal transition can suppress major attributes of human epithelial tumor-initiating cells. The Journal of Clinical Investigation, 122(5), 1849–1868. https://doi.org/10.1172/JCI59218CrossRefPubMedPubMedCentral

44.

Ocana, O. H., Corcoles, R., Fabra, A., Moreno-Bueno, G., Acloque, H., Vega, S., et al. (2012). Metastatic colonization requires the repression of the epithelial-mesenchymal transition inducer Prrx1. Cancer Cell, 22(6), 709–724. https://doi.org/10.1016/j.ccr.2012.10.012CrossRefPubMed

45.

Schmidt, J. M., Panzilius, E., Bartsch, H. S., Irmler, M., Beckers, J., Kari, V., et al. (2015). Stem-cell-like properties and epithelial plasticity arise as stable traits after transient Twist1 activation. Cell Reports, 10(2), 131–139. https://doi.org/10.1016/j.celrep.2014.12.032CrossRefPubMed

46.

Kunnumakkara, A. B., Bordoloi, D., Harsha, C., Banik, K., Gupta, S. C., & Aggarwal, B. B. (2017). Curcumin mediates anticancer effects by modulating multiple cell signaling pathways. Clinical Science (London, England), 131(15), 1781–1799. https://doi.org/10.1042/CS20160935CrossRef

47.

Verma, E., Kumar, A., Daimary, U. D., Parama, D., Girisa, S., Sethi, G., et al. (2021). Potential of baicalein in the prevention and treatment of cancer: A scientometric analyses based review. Journal of Functional Foods, 86, 104660.CrossRef

48.

Bhagwat, A. S., & Vakoc, C. R. (2015). Targeting transcription factors in cancer. Trends Cancer, 1(1), 53–65. https://doi.org/10.1016/j.trecan.2015.07.001CrossRefPubMedPubMedCentral

49.

Bushweller, J. H. (2019). Targeting transcription factors in cancer - from undruggable to reality. Nature Reviews Cancer, 19(11), 611–624. https://doi.org/10.1038/s41568-019-0196-7CrossRefPubMedPubMedCentral

50.

Vishnoi, K., Viswakarma, N., Rana, A., & Rana, B. (2020). Transcription factors in cancer development and therapy. Cancers, 12(8), 2296. https://doi.org/10.3390/cancers12082296CrossRefPubMedPubMedCentral

51.

Wang, L., Nanayakkara, G., Yang, Q., Tan, H., Drummer, C., Sun, Y., et al. (2017). A comprehensive data mining study shows that most nuclear receptors act as newly proposed homeostasis-associated molecular pattern receptors. Journal of Hematology & Oncology, 10(1), 168. https://doi.org/10.1186/s13045-017-0526-8CrossRef

52.

Wagner, R. T., & Cooney, A. J. (2013). Minireview: The diverse roles of nuclear receptors in the regulation of embryonic stem cell pluripotency. Molecular Endocrinology, 27(6), 864–878. https://doi.org/10.1210/me.2012-1383CrossRefPubMedPubMedCentral

53.

Sun, G., & Shi, Y. (2010). Nuclear receptors in stem cells and their therapeutic potential. Advanced Drug Delivery Reviews, 62(13), 1299–1306. https://doi.org/10.1016/j.addr.2010.08.003CrossRefPubMedPubMedCentral

54.

Jeong, Y., & Mangelsdorf, D. J. (2009). Nuclear receptor regulation of stemness and stem cell differentiation. Experimental & Molecular Medicine, 41(8), 525–537. https://doi.org/10.3858/emm.2009.41.8.091CrossRef

55.

Gangwar, S. K., Kumar, A., Jose, S., Alqahtani, M. S., Abbas, M., Sethi, G., et al. (2022). Nuclear receptors in oral cancer-Emerging players in tumorigenesis. Cancer Letters, 536, 215666. https://doi.org/10.1016/j.canlet.2022.215666CrossRefPubMed

56.

Gangwar, S. K., Kumar, A., Yap, K. C., Jose, S., Parama, D., Sethi, G., Kumar, A. P., & Kunnumakkara, A. B. (2022). Targeting nuclear receptors in lung cancer-novel therapeutic prospects. Pharmaceuticals (Basel, Switzerland), 15(5), 624. https://doi.org/10.3390/ph15050624CrossRefPubMed

57.

Jayaprakash, S., Hegde, M., Girisa, S., Alqahtani, M. S., Abbas, M., Lee, E. H. C., Yap, K. C., Sethi, G., Kumar, A. P., & Kunnumakkara, A. B. (2022). Demystifying the functional role of nuclear receptors in esophageal cancer. International Journal of Molecular Sciences, 23(18), 10952. https://doi.org/10.3390/ijms231810952CrossRefPubMedPubMedCentral

58.

Hegde, M., Girisa, S., Naliyadhara, N., Kumar, A., Alqahtani, M. S., Abbas, M., et al. (2023). Natural compounds targeting nuclear receptors for effective cancer therapy. Cancer and Metastasis Reviews, 42(3), 765–822. https://doi.org/10.1007/s10555-022-10068-wCrossRefPubMed

59.

Zhao, L., Zhou, S., & Gustafsson, J. A. (2019). Nuclear receptors: Recent drug discovery for cancer Therapies. Endocrine Reviews, 40(5), 1207–1249. https://doi.org/10.1210/er.2018-00222CrossRefPubMed

60.

Sever, R., & Glass, C. K. (2013). Signaling by nuclear receptors. Cold Spring Harbor Perspectives in Biology, 5(3), a016709. https://doi.org/10.1101/cshperspect.a016709CrossRefPubMedPubMedCentral

61.

Weikum, E. R., Liu, X., & Ortlund, E. A. (2018). The nuclear receptor superfamily: A structural perspective. Protein Science, 27(11), 1876–1892. https://doi.org/10.1002/pro.3496CrossRefPubMedPubMedCentral

62.

Scholtes, C., & Giguere, V. (2022). Transcriptional control of energy metabolism by nuclear receptors. Nature Reviews Molecular Cell Biology, 23(11), 750–770. https://doi.org/10.1038/s41580-022-00486-7CrossRefPubMed

63.

Wang, K., & Wan, Y. J. (2008). Nuclear receptors and inflammatory diseases. Experimental Biology and Medicine (Maywood, N.J.), 233(5), 496–506. https://doi.org/10.3181/0708-MR-231CrossRefPubMed

64.

Paredes, A., Santos-Clemente, R., & Ricote, M. (2021). Untangling the cooperative role of nuclear receptors in cardiovascular physiology and disease. International Journal of Molecular Sciences, 22(15), 7775. https://doi.org/10.3390/ijms22157775CrossRefPubMedPubMedCentral

65.

Manickasamy, M. K., Sajeev, A., Bharathwaj Chetty, B., Alqahtani, M. S., Abbas, M., Hegde, M., Aswani, B. S., Shakibaei, M., Sethi, G., & Kunnumakkara, A. B. (2024). Exploring the nexus of nuclear receptors in hematological malignancies. Cellular and Molecular Life Sciences: CMLS, 81(1), 78. https://doi.org/10.1007/s00018-023-05085-zCrossRefPubMed

66.

Lamouille, S., Xu, J., & Derynck, R. (2014). Molecular mechanisms of epithelial-mesenchymal transition. Nature Reviews Molecular Cell Biology, 15(3), 178–196. https://doi.org/10.1038/nrm3758CrossRefPubMedPubMedCentral

67.

Kalluri, R., & Neilson, E. G. (2003). Epithelial-mesenchymal transition and its implications for fibrosis. The Journal of Clinical Investigation, 112(12), 1776–1784. https://doi.org/10.1172/JCI20530CrossRefPubMedPubMedCentral

68.

Kalluri, R., & Weinberg, R. A. (2009). The basics of epithelial-mesenchymal transition. The Journal of Clinical Investigation, 119(6), 1420–1428. https://doi.org/10.1172/JCI39104CrossRefPubMedPubMedCentral

69.

Zeisberg, M., & Neilson, E. G. (2009). Biomarkers for epithelial-mesenchymal transitions. The Journal of Clinical Investigation, 119(6), 1429–1437. https://doi.org/10.1172/JCI36183CrossRefPubMedPubMedCentral

70.

Yang, J., & Weinberg, R. A. (2008). Epithelial-mesenchymal transition: At the crossroads of development and tumor metastasis. Developmental Cell, 14(6), 818–829. https://doi.org/10.1016/j.devcel.2008.05.009CrossRefPubMed

71.

Wilson, M. M., Weinberg, R. A., Lees, J. A., & Guen, V. J. (2020). Emerging Mechanisms by which EMT Programs Control Stemness. Trends Cancer, 6(9), 775–780. https://doi.org/10.1016/j.trecan.2020.03.011CrossRefPubMed

72.

Dongre, A., & Weinberg, R. A. (2019). New insights into the mechanisms of epithelial-mesenchymal transition and implications for cancer. Nature Reviews Molecular Cell Biology, 20(2), 69–84. https://doi.org/10.1038/s41580-018-0080-4CrossRefPubMed

73.

Goossens, S., Vandamme, N., Van Vlierberghe, P., & Berx, G. (2017). EMT transcription factors in cancer development re-evaluated: Beyond EMT and MET. Biochimica et Biophysica Acta - Reviews on Cancer, 1868(2), 584–591. https://doi.org/10.1016/j.bbcan.2017.06.006CrossRefPubMed

74.

Puisieux, A., Brabletz, T., & Caramel, J. (2014). Oncogenic roles of EMT-inducing transcription factors. Nature Cell Biology, 16(6), 488–494. https://doi.org/10.1038/ncb2976CrossRefPubMed

75.

Sanchez-Tillo, E., Liu, Y., de Barrios, O., Siles, L., Fanlo, L., Cuatrecasas, M., et al. (2012). EMT-activating transcription factors in cancer: Beyond EMT and tumor invasiveness. Cellular and Molecular Life Sciences, 69(20), 3429–3456. https://doi.org/10.1007/s00018-012-1122-2CrossRefPubMed

76.

Tse, J. C., & Kalluri, R. (2007). Mechanisms of metastasis: Epithelial-to-mesenchymal transition and contribution of tumor microenvironment. Journal of Cellular Biochemistry, 101(4), 816–829. https://doi.org/10.1002/jcb.21215CrossRefPubMed

77.

Gottardi, C. J., Wong, E., & Gumbiner, B. M. (2001). E-cadherin suppresses cellular transformation by inhibiting beta-catenin signaling in an adhesion-independent manner. Journal of Cell Biology, 153(5), 1049–1060. https://doi.org/10.1083/jcb.153.5.1049CrossRefPubMedPubMedCentral

78.

Stockinger, A., Eger, A., Wolf, J., Beug, H., & Foisner, R. (2001). E-cadherin regulates cell growth by modulating proliferation-dependent beta-catenin transcriptional activity. Journal of Cell Biology, 154(6), 1185–1196. https://doi.org/10.1083/jcb.200104036CrossRefPubMedPubMedCentral

79.

Kim, K., Lu, Z., & Hay, E. D. (2002). Direct evidence for a role of beta-catenin/LEF-1 signaling pathway in induction of EMT. Cell Biology International, 26(5), 463–476. https://doi.org/10.1006/cbir.2002.0901CrossRefPubMed

80.

Thiery, J. P. (2002). Epithelial-mesenchymal transitions in tumour progression. Nature Reviews Cancer, 2(6), 442–454. https://doi.org/10.1038/nrc822CrossRefPubMed

81.

Batlle, E., Sancho, E., Franci, C., Dominguez, D., Monfar, M., Baulida, J., et al. (2000). The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells. Nature Cell Biology, 2(2), 84–89. https://doi.org/10.1038/35000034CrossRefPubMed

82.

Cano, A., Perez-Moreno, M. A., Rodrigo, I., Locascio, A., Blanco, M. J., del Barrio, M. G., et al. (2000). The transcription factor snail controls epithelial-mesenchymal transitions by repressing E-cadherin expression. Nature Cell Biology, 2(2), 76–83. https://doi.org/10.1038/35000025CrossRefPubMed

83.

Baranwal, S., & Alahari, S. K. (2009). Molecular mechanisms controlling E-cadherin expression in breast cancer. Biochemical and Biophysical Research Communications, 384(1), 6–11. https://doi.org/10.1016/j.bbrc.2009.04.051CrossRefPubMedPubMedCentral

84.

De Craene, B., & Berx, G. (2013). Regulatory networks defining EMT during cancer initiation and progression. Nature Reviews Cancer, 13(2), 97–110. https://doi.org/10.1038/nrc3447CrossRefPubMed

85.

Droufakou, S., Deshmane, V., Roylance, R., Hanby, A., Tomlinson, I., & Hart, I. R. (2001). Multiple ways of silencing E-cadherin gene expression in lobular carcinoma of the breast. International Journal of Cancer, 92(3), 404–408. https://doi.org/10.1002/ijc.1208CrossRefPubMed

86.

Guilford, P., Hopkins, J., Harraway, J., McLeod, M., McLeod, N., Harawira, P., et al. (1998). E-cadherin germline mutations in familial gastric cancer. Nature, 392(6674), 402–405. https://doi.org/10.1038/32918CrossRefPubMed

87.

Pharoah, P. D., Guilford, P., Caldas, C., International Gastric Cancer Linkage, C. (2001). Incidence of gastric cancer and breast cancer in CDH1 (E-cadherin) mutation carriers from hereditary diffuse gastric cancer families. Gastroenterology, 121(6), 1348–135. https://doi.org/10.1053/gast.2001.29611CrossRefPubMed

88.

Peinado, H., Ballestar, E., Esteller, M., & Cano, A. (2004). Snail mediates E-cadherin repression by the recruitment of the Sin3A/histone deacetylase 1 (HDAC1)/HDAC2 complex. Molecular and Cellular Biology, 24(1), 306–319. https://doi.org/10.1128/MCB.24.1.306-319.2004CrossRefPubMedPubMedCentral

89.

Yoshiura, K., Kanai, Y., Ochiai, A., Shimoyama, Y., Sugimura, T., & Hirohashi, S. (1995). Silencing of the E-cadherin invasion-suppressor gene by CpG methylation in human carcinomas. Proc Natl Acad Sci U S A, 92(16), 7416–7419. https://doi.org/10.1073/pnas.92.16.7416CrossRefPubMedPubMedCentral

90.

Stryjewska, A., Dries, R., Pieters, T., Verstappen, G., Conidi, A., Coddens, K., et al. (2017). Zeb2 regulates cell fate at the exit from epiblast state in mouse embryonic stem cells. Stem Cells, 35(3), 611–625. https://doi.org/10.1002/stem.2521CrossRefPubMed

91.

Galvagni, F., & Neri, F. (2015). Snai1 represses Nanog to promote embryonic stem cell differentiation. Genom Data, 4, 82–83. https://doi.org/10.1016/j.gdata.2015.03.007CrossRefPubMedPubMedCentral

92.

Lin, Y., Li, X. Y., Willis, A. L., Liu, C., Chen, G., & Weiss, S. J. (2014). Snail1-dependent control of embryonic stem cell pluripotency and lineage commitment. Nature Communications, 5, 3070. https://doi.org/10.1038/ncomms4070CrossRefPubMed

93.

Paranjape, A. N., Balaji, S. A., Mandal, T., Krushik, E. V., Nagaraj, P., Mukherjee, G., et al. (2014). Bmi1 regulates self-renewal and epithelial to mesenchymal transition in breast cancer cells through Nanog. BMC Cancer, 14, 785. https://doi.org/10.1186/1471-2407-14-785CrossRefPubMedPubMedCentral

94.

Yang, M. H., Hsu, D. S., Wang, H. W., Wang, H. J., Lan, H. Y., Yang, W. H., et al. (2010). Bmi1 is essential in Twist1-induced epithelial-mesenchymal transition. Nature Cell Biology, 12(10), 982–992. https://doi.org/10.1038/ncb2099CrossRefPubMed

95.

Ye, Y., Xiao, Y., Wang, W., Yearsley, K., Gao, J. X., & Barsky, S. H. (2008). ERalpha suppresses slug expression directly by transcriptional repression. The Biochemical Journal, 416(2), 179–187. https://doi.org/10.1042/BJ20080328CrossRefPubMed

96.

Ye, Y., Xiao, Y., Wang, W., Yearsley, K., Gao, J. X., Shetuni, B., et al. (2010). ERalpha signaling through slug regulates E-cadherin and EMT. Oncogene, 29(10), 1451–1462. https://doi.org/10.1038/onc.2009.433CrossRefPubMed

97.

Barsky, S. H. (2003). Myoepithelial mRNA expression profiling reveals a common tumor-suppressor phenotype. Experimental and Molecular Pathology, 74(2), 113–122. https://doi.org/10.1016/s0014-4800(03)00011-xCrossRefPubMed

98.

Xiong, G., & Xu, R. (2022). Retinoid orphan nuclear receptor alpha (RORalpha) suppresses the epithelial-mesenchymal transition (EMT) by directly repressing Snail transcription. Journal of Biological Chemistry, 298(7), 102059. https://doi.org/10.1016/j.jbc.2022.102059CrossRefPubMedPubMedCentral

99.

Chua, H. L., Bhat-Nakshatri, P., Clare, S. E., Morimiya, A., Badve, S., & Nakshatri, H. (2007). NF-kappaB represses E-cadherin expression and enhances epithelial to mesenchymal transition of mammary epithelial cells: Potential involvement of ZEB-1 and ZEB-2. Oncogene, 26(5), 711–724. https://doi.org/10.1038/sj.onc.1209808CrossRefPubMed

100.

Huber, M. A., Azoitei, N., Baumann, B., Grunert, S., Sommer, A., Pehamberger, H., et al. (2004). NF-kappaB is essential for epithelial-mesenchymal transition and metastasis in a model of breast cancer progression. The Journal of Clinical Investigation, 114(4), 569–581. https://doi.org/10.1172/JCI21358CrossRefPubMedPubMedCentral

101.

Oh, S. K., Kim, D., Kim, K., Boo, K., Yu, Y. S., Kim, I. S., et al. (2019). RORalpha is crucial for attenuated inflammatory response to maintain intestinal homeostasis. Proc Natl Acad Sci U S A, 116(42), 21140–21149. https://doi.org/10.1073/pnas.1907595116CrossRefPubMedPubMedCentral

102.

Jiang, Y., Zhou, J., Zhao, J., Hou, D., Zhang, H., Li, L., et al. (2020). MiR-18a-downregulated RORA inhibits the proliferation and tumorigenesis of glioma using the TNF-alpha-mediated NF-kappaB signaling pathway. eBioMedicine, 52, 102651. https://doi.org/10.1016/j.ebiom.2020.102651CrossRefPubMedPubMedCentral

103.

Upadhyay, S. K., Verone, A., Shoemaker, S., Qin, M., Liu, S., Campbell, M., et al. (2013). 1,25-Dihydroxyvitamin D3 (1,25(OH)2D3) Signaling capacity and the epithelial-mesenchymal transition in non-small cell lung cancer (NSCLC): Implications for use of 1,25(OH)2D3 in NSCLC treatment. Cancers (Basel), 5(4), 1504–1521. https://doi.org/10.3390/cancers5041504CrossRefPubMed

104.

Pereira, F., Barbachano, A., Silva, J., Bonilla, F., Campbell, M. J., Munoz, A., et al. (2011). KDM6B/JMJD3 histone demethylase is induced by vitamin D and modulates its effects in colon cancer cells. Human Molecular Genetics, 20(23), 4655–4665. https://doi.org/10.1093/hmg/ddr399CrossRefPubMed

105.

Pereira, F., Barbachano, A., Singh, P. K., Campbell, M. J., Munoz, A., & Larriba, M. J. (2012). Vitamin D has wide regulatory effects on histone demethylase genes. Cell Cycle, 11(6), 1081–1089. https://doi.org/10.4161/cc.11.6.19508CrossRefPubMed

106.

Palmer, H. G., Larriba, M. J., Garcia, J. M., Ordonez-Moran, P., Pena, C., Peiro, S., et al. (2004). The transcription factor SNAIL represses vitamin D receptor expression and responsiveness in human colon cancer. Nature Medicine, 10(9), 917–919. https://doi.org/10.1038/nm1095CrossRefPubMed

107.

Choudhary, R., Li, H., Winn, R. A., Sorenson, A. L., Weiser-Evans, M. C., & Nemenoff, R. A. (2010). Peroxisome proliferator-activated receptor-gamma inhibits transformed growth of non-small cell lung cancer cells through selective suppression of Snail. Neoplasia, 12(3), 224–234. https://doi.org/10.1593/neo.91638CrossRefPubMedPubMedCentral

108.

Lefterova, M. I., Zhang, Y., Steger, D. J., Schupp, M., Schug, J., Cristancho, A., et al. (2008). PPARgamma and C/EBP factors orchestrate adipocyte biology via adjacent binding on a genome-wide scale. Genes & Development, 22(21), 2941–2952. https://doi.org/10.1101/gad.1709008CrossRef

109.

Lu, J., Du, C., Yao, J., Wu, B., Duan, Y., Zhou, L., et al. (2017). C/EBPalpha Suppresses Lung Adenocarcinoma Cell Invasion and Migration by Inhibiting beta-Catenin. Cellular Physiology and Biochemistry, 42(5), 1779–1788. https://doi.org/10.1159/000479457CrossRefPubMed

110.

Sato, A., Yamada, N., Ogawa, Y., & Ikegami, M. (2013). CCAAT/enhancer-binding protein-alpha suppresses lung tumor development in mice through the p38alpha MAP kinase pathway. PLoS ONE, 8(2), e57013. https://doi.org/10.1371/journal.pone.0057013CrossRefPubMedPubMedCentral

111.

Lourenco, A. R., Roukens, M. G., Seinstra, D., Frederiks, C. L., Pals, C. E., Vervoort, S. J., et al. (2020). C/EBPa is crucial determinant of epithelial maintenance by preventing epithelial-to-mesenchymal transition. Nature Communications, 11(1), 785. https://doi.org/10.1038/s41467-020-14556-xCrossRefPubMedPubMedCentral

112.

Lam, S. S., Mak, A. S., Yam, J. W., Cheung, A. N., Ngan, H. Y., & Wong, A. S. (2014). Targeting estrogen-related receptor alpha inhibits epithelial-to-mesenchymal transition and stem cell properties of ovarian cancer cells. Molecular Therapy, 22(4), 743–751. https://doi.org/10.1038/mt.2014.1CrossRefPubMedPubMedCentral

113.

Zhao, Y., Li, Y., Lou, G., Zhao, L., Xu, Z., Zhang, Y., et al. (2012). MiR-137 targets estrogen-related receptor alpha and impairs the proliferative and migratory capacity of breast cancer cells. PLoS ONE, 7(6), e39102. https://doi.org/10.1371/journal.pone.0039102CrossRefPubMedPubMedCentral

114.

Balaguer, F., Link, A., Lozano, J. J., Cuatrecasas, M., Nagasaka, T., Boland, C. R., et al. (2010). Epigenetic silencing of miR-137 is an early event in colorectal carcinogenesis. Cancer Research, 70(16), 6609–6618. https://doi.org/10.1158/0008-5472.CAN-10-0622CrossRefPubMedPubMedCentral

115.

Chen, Q., Chen, X., Zhang, M., Fan, Q., Luo, S., & Cao, X. (2011). miR-137 is frequently down-regulated in gastric cancer and is a negative regulator of Cdc42. Digestive Diseases and Sciences, 56(7), 2009–2016. https://doi.org/10.1007/s10620-010-1536-3CrossRefPubMed

116.

Chen, X., Wang, J., Shen, H., Lu, J., Li, C., Hu, D. N., et al. (2011). Epigenetics, microRNAs, and carcinogenesis: Functional role of microRNA-137 in uveal melanoma. Investigative Ophthalmology & Visual Science, 52(3), 1193–1199. https://doi.org/10.1167/iovs.10-5272CrossRef

117.

Kozaki, K., Imoto, I., Mogi, S., Omura, K., & Inazawa, J. (2008). Exploration of tumor-suppressive microRNAs silenced by DNA hypermethylation in oral cancer. Cancer Research, 68(7), 2094–2105. https://doi.org/10.1158/0008-5472.CAN-07-5194CrossRefPubMed

118.

Langevin, S. M., Stone, R. A., Bunker, C. H., Grandis, J. R., Sobol, R. W., & Taioli, E. (2010). MicroRNA-137 promoter methylation in oral rinses from patients with squamous cell carcinoma of the head and neck is associated with gender and body mass index. Carcinogenesis, 31(5), 864–870. https://doi.org/10.1093/carcin/bgq051CrossRefPubMedPubMedCentral

119.

Langevin, S. M., Stone, R. A., Bunker, C. H., Lyons-Weiler, M. A., LaFramboise, W. A., Kelly, L., et al. (2011). MicroRNA-137 promoter methylation is associated with poorer overall survival in patients with squamous cell carcinoma of the head and neck. Cancer, 117(7), 1454–1462. https://doi.org/10.1002/cncr.25689CrossRefPubMed

120.

Silber, J., Lim, D. A., Petritsch, C., Persson, A. I., Maunakea, A. K., Yu, M., et al. (2008). miR-124 and miR-137 inhibit proliferation of glioblastoma multiforme cells and induce differentiation of brain tumor stem cells. BMC Medicine, 6, 14. https://doi.org/10.1186/1741-7015-6-14CrossRefPubMedPubMedCentral

121.

Li, X., Chen, W., Zeng, W., Wan, C., Duan, S., & Jiang, S. (2017). microRNA-137 promotes apoptosis in ovarian cancer cells via the regulation of XIAP. British Journal of Cancer, 116(1), 66–76. https://doi.org/10.1038/bjc.2016.379CrossRefPubMed

122.

Miao, L., Yang, L., Li, R., Rodrigues, D. N., Crespo, M., Hsieh, J. T., et al. (2017). Disrupting androgen receptor signaling induces snail-mediated epithelial-mesenchymal plasticity in prostate cancer. Cancer Research, 77(11), 3101–3112. https://doi.org/10.1158/0008-5472.CAN-16-2169CrossRefPubMed

123.

Wu, K., Gore, C., Yang, L., Fazli, L., Gleave, M., Pong, R. C., et al. (2012). Slug, a unique androgen-regulated transcription factor, coordinates androgen receptor to facilitate castration resistance in prostate cancer. Molecular Endocrinology, 26(9), 1496–1507. https://doi.org/10.1210/me.2011-1360CrossRefPubMedPubMedCentral

124.

Liu, Y. N., Liu, Y., Lee, H. J., Hsu, Y. H., & Chen, J. H. (2008). Activated androgen receptor downregulates E-cadherin gene expression and promotes tumor metastasis. Molecular and Cellular Biology, 28(23), 7096–7108. https://doi.org/10.1128/MCB.00449-08CrossRefPubMedPubMedCentral

125.

Thakkar, A., Wang, B., Picon-Ruiz, M., Buchwald, P., & Ince, T. A. (2016). Vitamin D and androgen receptor-targeted therapy for triple-negative breast cancer. Breast Cancer Research and Treatment, 157(1), 77–90. https://doi.org/10.1007/s10549-016-3807-yCrossRefPubMedPubMedCentral

126.

Fernández, N. B., Sosa, S. M., Roberts, J. T., Recouvreux, M. S., Rocha-Viegas, L., Christenson, J. L., Spoelstra, N. S., Couto, F. L., Raimondi, A. R., Richer, J. K., & Rubinstein, N. (2023). RUNX1 is regulated by androgen receptor to promote cancer stem markers and chemotherapy resistance in triple negative breast cancer. Cells, 12(3), 444. https://doi.org/10.3390/cells12030444CrossRefPubMedPubMedCentral

127.

Barton, V. N., Christenson, J. L., Gordon, M. A., Greene, L. I., Rogers, T. J., Butterfield, K., et al. (2017). Androgen receptor supports an anchorage-independent, cancer stem cell-like population in triple-negative breast cancer. Cancer Research, 77(13), 3455–3466. https://doi.org/10.1158/0008-5472.CAN-16-3240CrossRefPubMedPubMedCentral

128.

Chen, L., Chang, W. C., Hung, Y. C., Chang, Y. Y., Bao, B. Y., Huang, H. C., et al. (2014). Androgen receptor increases CD133 expression and progenitor-like population that associate with cisplatin resistance in endometrial cancer cell line. Reproductive Sciences, 21(3), 386–394. https://doi.org/10.1177/1933719113497281CrossRefPubMedPubMedCentral

129.

Zhao, N., Wang, F., Ahmed, S., Liu, K., Zhang, C., Cathcart, S. J., et al. (2021). Androgen Receptor, Although Not a Specific Marker For, Is a Novel Target to Suppress Glioma Stem Cells as a Therapeutic Strategy for Glioblastoma. Frontiers in Oncology, 11, 616625. https://doi.org/10.3389/fonc.2021.616625CrossRefPubMedPubMedCentral

130.

Xiao, Y., Sun, Y., Liu, G., Zhao, J., Gao, Y., Yeh, S., et al. (2019). Androgen receptor (AR)/miR-520f-3p/SOX9 signaling is involved in altering hepatocellular carcinoma (HCC) cell sensitivity to the Sorafenib therapy under hypoxia via increasing cancer stem cells phenotype. Cancer Letters, 444, 175–187. https://doi.org/10.1016/j.canlet.2018.11.004CrossRefPubMed

131.

Jiang, L., Shan, J., Shen, J., Wang, Y., Yan, P., Liu, L., et al. (2016). Androgen/androgen receptor axis maintains and promotes cancer cell stemness through direct activation of Nanog transcription in hepatocellular carcinoma. Oncotarget, 7(24), 36814–36828. https://doi.org/10.18632/oncotarget.9192CrossRefPubMedPubMedCentral

132.

Han, H., Wang, Y., Curto, J., Gurrapu, S., Laudato, S., Rumandla, A., et al. (2022). Mesenchymal and stem-like prostate cancer linked to therapy-induced lineage plasticity and metastasis. Cell Reports, 39(1), 110595. https://doi.org/10.1016/j.celrep.2022.110595CrossRefPubMed

133.

Lu, X., Yang, F., Chen, D., Zhao, Q., Chen, D., Ping, H., et al. (2020). Quercetin reverses docetaxel resistance in prostate cancer via androgen receptor and PI3K/Akt signaling pathways. International Journal of Biological Sciences, 16(7), 1121–1134. https://doi.org/10.7150/ijbs.41686CrossRefPubMedPubMedCentral

134.

Zhifang, M., Liang, W., Wei, Z., Bin, H., Rui, T., Nan, W., et al. (2015). The androgen receptor plays a suppressive role in epithelial- mesenchymal transition of human prostate cancer stem progenitor cells. BMC Biochemistry, 16, 13. https://doi.org/10.1186/s12858-015-0042-9CrossRefPubMedPubMedCentral

135.

Bai, J. Y., Jin, B., Ma, J. B., Liu, T. J., Yang, C., Chong, Y., et al. (2021). HOTAIR and androgen receptor synergistically increase GLI2 transcription to promote tumor angiogenesis and cancer stemness in renal cell carcinoma. Cancer Letters, 498, 70–79. https://doi.org/10.1016/j.canlet.2020.10.031CrossRefPubMed

136.

Guo, C., Sun, Y., Zhai, W., Yao, X., Gong, D., You, B., et al. (2022). Hypoxia increases RCC stem cell phenotype via altering the androgen receptor (AR)-lncTCFL5-2-YBX1-SOX2 signaling axis. Cell & Bioscience, 12(1), 185. https://doi.org/10.1186/s13578-022-00912-5CrossRef

137.

Rota, S. G., Roma, A., Dude, I., Ma, C., Stevens, R., MacEachern, J., et al. (2017). Estrogen receptor beta is a novel target in acute myeloid leukemia. Molecular Cancer Therapeutics, 16(11), 2618–2626. https://doi.org/10.1158/1535-7163.MCT-17-0292CrossRefPubMed

138.

Jung, J. W., Park, S. B., Lee, S. J., Seo, M. S., Trosko, J. E., & Kang, K. S. (2011). Metformin represses self-renewal of the human breast carcinoma stem cells via inhibition of estrogen receptor-mediated OCT4 expression. PLoS ONE, 6(11), e28068. https://doi.org/10.1371/journal.pone.0028068CrossRefPubMedPubMedCentral

139.

Deng, H., Yin, L., Zhang, X. T., Liu, L. J., Wang, M. L., & Wang, Z. Y. (2014). ER-α variant ER-α36 mediates antiestrogen resistance in ER-positive breast cancer stem/progenitor cells. The Journal of Steroid Biochemistry and Molecular Biology, 144 Pt B, 417–426. https://doi.org/10.1016/j.jsbmb.2014.08.017CrossRefPubMed

140.

Lettlova, S., Brynychova, V., Blecha, J., Vrana, D., Vondrusova, M., Soucek, P., et al. (2018). MiR-301a-3p suppresses estrogen signaling by directly inhibiting ESR1 in ERalpha positive breast cancer. Cellular Physiology and Biochemistry, 46(6), 2601–2615. https://doi.org/10.1159/000489687CrossRefPubMed

141.

Alves, C. L., Elias, D., Lyng, M. B., Bak, M., & Ditzel, H. J. (2018). SNAI2 upregulation is associated with an aggressive phenotype in fulvestrant-resistant breast cancer cells and is an indicator of poor response to endocrine therapy in estrogen receptor-positive metastatic breast cancer. Breast Cancer Research, 20(1), 60. https://doi.org/10.1186/s13058-018-0988-9CrossRefPubMedPubMedCentral

142.

Wan, X., Hou, J., Liu, S., Zhang, Y., Li, W., Zhang, Y., et al. (2021). Estrogen receptor alpha mediates doxorubicin sensitivity in breast cancer cells by regulating E-cadherin. Front Cell Dev Biol, 9, 583572. https://doi.org/10.3389/fcell.2021.583572CrossRefPubMedPubMedCentral

143.

Bano, A., Stevens, J. H., Modi, P. S., Gustafsson, J. Å., & Strom, A. M. (2023). Estrogen receptor β4 regulates chemotherapy resistance and induces cancer stem cells in triple negative breast cancer. International Journal of Molecular Sciences, 24(6), 5867. https://doi.org/10.3390/ijms24065867CrossRefPubMedPubMedCentral

144.

Strillacci, A., Sansone, P., Rajasekhar, V. K., Turkekul, M., Boyko, V., Meng, F., et al. (2022). ERalpha-LBD, an isoform of estrogen receptor alpha, promotes breast cancer proliferation and endocrine resistance. NPJ Breast Cancer, 8(1), 96. https://doi.org/10.1038/s41523-022-00470-6CrossRefPubMedPubMedCentral

145.

Kwon, Y. S., Nam, K. S., & Kim, S. (2021). Tamoxifen overcomes the trastuzumab-resistance of SK-BR-3 tumorspheres by targeting crosstalk between cytoplasmic estrogen receptor alpha and the EGFR/HER2 signaling pathway. Biochemical Pharmacology, 190, 114635. https://doi.org/10.1016/j.bcp.2021.114635CrossRefPubMed

146.

Zhang, F., Peng, L., Huang, Y., Lin, X., Zhou, L., & Chen, J. (2019). Chronic BDE-47 exposure aggravates malignant phenotypes and chemoresistance by activating ERK through ERalpha and GPR30 in endometrial carcinoma. Frontiers in Oncology, 9, 1079. https://doi.org/10.3389/fonc.2019.01079CrossRefPubMedPubMedCentral

147.

Hamilton, D. H., Griner, L. M., Keller, J. M., Hu, X., Southall, N., Marugan, J., et al. (2016). Targeting estrogen receptor signaling with fulvestrant enhances immune and chemotherapy-mediated cytotoxicity of human lung cancer. Clinical Cancer Research, 22(24), 6204–6216. https://doi.org/10.1158/1078-0432.CCR-15-3059CrossRefPubMedPubMedCentral

148.

Maher, D. M., Khan, S., Nordquist, J. L., Ebeling, M. C., Bauer, N. A., Kopel, L., et al. (2015). Ormeloxifene efficiently inhibits ovarian cancer growth. Cancer Lett, 356(2), 606–612. https://doi.org/10.1016/j.canlet.2014.10.009CrossRefPubMed

149.

He, Y., Alejo, S., Venkata, P. P., Johnson, J. D., Loeffel, I., Pratap, U. P., Zou, Y., Lai, Z., Tekmal, R. R., Kost, E. R., & Sareddy, G. R. (2022). Therapeutic targeting of ovarian cancer stem cells using estrogen receptor beta agonist. International Journal of Molecular Sciences, 23(13), 7159. https://doi.org/10.3390/ijms23137159CrossRefPubMedPubMedCentral

150.

Tian, L., Peng, Y., Yang, K., Cao, J., Du, X., Liang, Z., et al. (2022). The ERalpha-NRF2 signalling axis promotes bicalutamide resistance in prostate cancer. Cell Communication and Signaling: CCS, 20(1), 178. https://doi.org/10.1186/s12964-022-00979-0CrossRefPubMedPubMedCentral

151.

Dahut, M., Fousek, K., Horn, L. A., Angstadt, S., Qin, H., Hamilton, D. H., Schlom, J., & Palena, C. (2023). Fulvestrant increases the susceptibility of enzalutamide-resistant prostate cancer cells to NK-mediated lysis. Journal for Immunotherapy of Cancer, 11(9), e007386. https://doi.org/10.1136/jitc-2023-007386CrossRefPubMedPubMedCentral

152.

Faria, M., Shepherd, P., Pan, Y., Chatterjee, S. S., Navone, N., Gustafsson, J. A., et al. (2018). The estrogen receptor variants beta2 and beta5 induce stem cell characteristics and chemotherapy resistance in prostate cancer through activation of hypoxic signaling. Oncotarget, 9(91), 36273–36288. https://doi.org/10.18632/oncotarget.26345CrossRefPubMedPubMedCentral

153.

Muduli, K., Prusty, M., Pradhan, J., Samal, A. P., Sahu, B., Roy, D. S., et al. (2023). Estrogen-related receptor alpha (ERRalpha) promotes cancer stem cell-like characteristics in breast cancer. Stem Cell Rev Rep. https://doi.org/10.1007/s12015-023-10605-2CrossRefPubMed

154.

Brindisi, M., Fiorillo, M., Frattaruolo, L., Sotgia, F., Lisanti, M. P., & Cappello, A. R. (2020). Cholesterol and mevalonate: Two metabolites involved in breast cancer progression and drug resistance through the ERRα pathway. Cells, 9(8), 1819. https://doi.org/10.3390/cells9081819CrossRefPubMedPubMedCentral

155.

Chen, H., Pan, J., Zhang, L., Chen, L., Qi, H., Zhong, M., et al. (2018). Downregulation of estrogen-related receptor alpha inhibits human cutaneous squamous cell carcinoma cell proliferation and migration by regulating EMT via fibronectin and STAT3 signaling pathways. European Journal of Pharmacology, 825, 133–142. https://doi.org/10.1016/j.ejphar.2018.02.025CrossRefPubMed

156.

Huang, J. W., Guan, B. Z., Yin, L. H., Liu, F. N., Hu, B., Zheng, Q. Y., et al. (2014). Effects of estrogen-related receptor alpha (ERRalpha) on proliferation and metastasis of human lung cancer A549 cells. Journal of Huazhong University of Science and Technology. Medical Sciences, 34(6), 875–881. https://doi.org/10.1007/s11596-014-1367-0CrossRef

157.

Chen, Y., Zhang, K., Li, Y., & He, Q. (2017). Estrogen-related receptor alpha participates transforming growth factor-beta (TGF-beta) induced epithelial-mesenchymal transition of osteosarcoma cells. Cell Adhesion & Migration, 11(4), 338–346. https://doi.org/10.1080/19336918.2016.1221567CrossRef

158.

Liu, S. L., Liang, H. B., Yang, Z. Y., Cai, C., Wu, Z. Y., Wu, X. S., et al. (2022). Gemcitabine and XCT790, an ERRalpha inverse agonist, display a synergistic anticancer effect in pancreatic cancer. International Journal of Medical Sciences, 19(2), 286–298. https://doi.org/10.7150/ijms.68404CrossRefPubMedPubMedCentral

159.

Singh, T. D., Jeong, S. Y., Lee, S. W., Ha, J. H., Lee, I. K., Kim, S. H., et al. (2015). Inverse agonist of estrogen-related receptor gamma enhances sodium iodide symporter function through mitogen-activated protein kinase signaling in anaplastic thyroid cancer cells. Journal of Nuclear Medicine, 56(11), 1690–1696. https://doi.org/10.2967/jnumed.115.160366CrossRefPubMed

160.

Di Matteo, S., Nevi, L., Costantini, D., Overi, D., Carpino, G., Safarikia, S., et al. (2019). The FXR agonist obeticholic acid inhibits the cancerogenic potential of human cholangiocarcinoma. PLoS ONE, 14(1), e0210077. https://doi.org/10.1371/journal.pone.0210077CrossRefPubMedPubMedCentral

161.

Shi, W., Wang, D., Yuan, X., Liu, Y., Guo, X., Li, J., et al. (2019). Glucocorticoid receptor-IRS-1 axis controls EMT and the metastasis of breast cancers. Journal of Molecular Cell Biology, 11(12), 1042–1055. https://doi.org/10.1093/jmcb/mjz001CrossRefPubMedPubMedCentral

162.

Sorrentino, G., Ruggeri, N., Zannini, A., Ingallina, E., Bertolio, R., Marotta, C., et al. (2017). Glucocorticoid receptor signalling activates YAP in breast cancer. Nature Communications, 8, 14073. https://doi.org/10.1038/ncomms14073CrossRefPubMedPubMedCentral

163.

Han, G. H., Yun, H., Kim, J., Chung, J. Y., Kim, J. H., & Cho, H. (2022). Overexpression of glucocorticoid receptor promotes the poor progression and induces cisplatin resistance through p38 MAP kinase in cervical cancer patients. American Journal of Cancer Research, 12(7), 3437–3454.PubMedPubMedCentral

164.

Liu, L., Han, S., Xiao, X., An, X., Gladkich, J., Hinz, U., et al. (2022). Glucocorticoid-induced microRNA-378 signaling mediates the progression of pancreatic cancer by enhancing autophagy. Cell Death & Disease, 13(12), 1052. https://doi.org/10.1038/s41419-022-05503-3CrossRef

165.

Suzuki, S., Yamamoto, M., Sanomachi, T., Togashi, K., Sugai, A., Seino, S., Yoshioka, T., Okada, M., & Kitanaka, C. (2021). Dexamethasone sensitizes cancer stem cells to gemcitabine and 5-Fluorouracil by increasing reactive oxygen species production through NRF2 Reduction. Life (Basel, Switzerland), 11(9), 885. https://doi.org/10.3390/life11090885CrossRefPubMed

166.

Martinez, S. R., Elix, C. C., Ochoa, P. T., Sanchez-Hernandez, E. S., Alkashgari, H. R., Ortiz-Hernandez, G. L., Zhang, L., & Casiano, C. A. (2023). Glucocorticoid receptor and β-Catenin interact in prostate cancer cells and their co-inhibition attenuates tumorsphere formation, stemness, and docetaxel resistance. International Journal of Molecular Sciences, 24(8), 7130. https://doi.org/10.3390/ijms24087130CrossRefPubMedPubMedCentral

167.

Zhao, X. G., Hu, J. Y., Tang, J., Yi, W., Zhang, M. Y., Deng, R., et al. (2019). miR-665 expression predicts poor survival and promotes tumor metastasis by targeting NR4A3 in breast cancer. Cell Death & Disease, 10(7), 479. https://doi.org/10.1038/s41419-019-1705-zCrossRef

168.

Shi, Z., To, S. K. Y., Zhang, S., Deng, S., Artemenko, M., Zhang, M., et al. (2021). Hypoxia-induced Nur77 activates PI3K/Akt signaling via suppression of Dicer/let-7i-5p to induce epithelial-to-mesenchymal transition. Theranostics, 11(7), 3376–3391. https://doi.org/10.7150/thno.52190CrossRefPubMedPubMedCentral

169.

Wan, P. K., Leung, T. H., Siu, M. K., Mo, X. T., Tang, H. W., Chan, K. K., et al. (2021). HPV-induced Nurr1 promotes cancer aggressiveness, self-renewal, and radioresistance via ERK and AKT signaling in cervical cancer. Cancer Letters, 497, 14–27. https://doi.org/10.1016/j.canlet.2020.09.025CrossRefPubMed

170.

Zarei, M., Shrestha, R., Johnson, S., Yu, Z., Karki, K., Vaziri-Gohar, A., et al. (2021). Nuclear Receptor 4A2 (NR4A2/NURR1) Regulates autophagy and chemoresistance in pancreatic ductal adenocarcinoma. Cancer Res Commun, 1(2), 65–78. https://doi.org/10.1158/2767-9764.crc-21-0073CrossRefPubMedPubMedCentral

171.

Zhou, H., Jiang, Y., Huang, Y., Zhong, M., Qin, D., Xie, C., et al. (2023). Therapeutic inhibition of PPARalpha-HIF1alpha-PGK1 signaling targets leukemia stem and progenitor cells in acute myeloid leukemia. Cancer Letters, 554, 215997. https://doi.org/10.1016/j.canlet.2022.215997CrossRefPubMed

172.

Tabe, Y., Konopleva, M., Kondo, Y., Contractor, R., Tsao, T., Konoplev, S., et al. (2007). PPARgamma-active triterpenoid CDDO enhances ATRA-induced differentiation in APL. Cancer Biology & Therapy, 6(12), 1967–1977. https://doi.org/10.4161/cbt.6.12.4982CrossRef

173.

Huang, G., Yin, L., Lan, J., Tong, R., Li, M., Na, F., et al. (2018). Synergy between peroxisome proliferator-activated receptor gamma agonist and radiotherapy in cancer. Cancer Science, 109(7), 2243–2255. https://doi.org/10.1111/cas.13650CrossRefPubMedPubMedCentral

174.

Haynes, H. R., Scott, H. L., Killick-Cole, C. L., Shaw, G., Brend, T., Hares, K. M., et al. (2019). shRNA-mediated PPARalpha knockdown in human glioma stem cells reduces in vitro proliferation and inhibits orthotopic xenograft tumour growth. The Journal of Pathology, 247(4), 422–434. https://doi.org/10.1002/path.5201CrossRefPubMed

175.

Ma, X. L., Sun, Y. F., Wang, B. L., Shen, M. N., Zhou, Y., Chen, J. W., et al. (2019). Sphere-forming culture enriches liver cancer stem cells and reveals Stearoyl-CoA desaturase 1 as a potential therapeutic target. BMC Cancer, 19(1), 760. https://doi.org/10.1186/s12885-019-5963-zCrossRefPubMedPubMedCentral

176.

Liu, L., Yang, Z., Xu, Y., Li, J., Xu, D., Zhang, L., et al. (2013). Inhibition of oxidative stress-elicited AKT activation facilitates PPARgamma agonist-mediated inhibition of stem cell character and tumor growth of liver cancer cells. PLoS ONE, 8(8), e73038. https://doi.org/10.1371/journal.pone.0073038CrossRefPubMedPubMedCentral

177.

Dwyer, A. R., Truong, T. H., Kerkvliet, C. P., Paul, K. V., Kabos, P., Sartorius, C. A., et al. (2021). Insulin receptor substrate-1 (IRS-1) mediates progesterone receptor-driven stemness and endocrine resistance in oestrogen receptor+ breast cancer. British Journal of Cancer, 124(1), 217–227. https://doi.org/10.1038/s41416-020-01094-yCrossRefPubMed

178.

Finlay-Schultz, J., Cittelly, D. M., Hendricks, P., Patel, P., Kabos, P., Jacobsen, B. M., et al. (2015). Progesterone downregulation of miR-141 contributes to expansion of stem-like breast cancer cells through maintenance of progesterone receptor and Stat5a. Oncogene, 34(28), 3676–3687. https://doi.org/10.1038/onc.2014.298CrossRefPubMed

179.

Recouvreux, M. S., Diaz Bessone, M. I., Taruselli, A., Todaro, L., Lago Huvelle, M. A., Sampayo, R. G., Bissell, M. J., & Simian, M. (2020). Alterations in progesterone receptor isoform balance in normal and neoplastic breast cells modulates the stem cell population. Cells, 9(9), 2074. https://doi.org/10.3390/cells9092074CrossRefPubMedPubMedCentral

180.

Planque, C., Rajabi, F., Grillet, F., Finetti, P., Bertucci, F., Gironella, M., et al. (2016). Pregnane X-receptor promotes stem cell-mediated colon cancer relapse. Oncotarget, 7(35), 56558–56573. https://doi.org/10.18632/oncotarget.10646CrossRefPubMedPubMedCentral

181.

Bansard, L., Bouvet, O., Moutin, E., Le Gall, G., Giammona, A., Pothin, E., et al. (2022). Niclosamide induces miR-148a to inhibit PXR and sensitize colon cancer stem cells to chemotherapy. Stem Cell Reports, 17(4), 835–848. https://doi.org/10.1016/j.stemcr.2022.02.005CrossRefPubMedPubMedCentral

182.

Yan, Y., Li, Z., Xu, X., Chen, C., Wei, W., Fan, M., et al. (2016). All-trans retinoic acids induce differentiation and sensitize a radioresistant breast cancer cells to chemotherapy. BMC Complementary and Alternative Medicine, 16, 113. https://doi.org/10.1186/s12906-016-1088-yCrossRefPubMedPubMedCentral

183.

Croker, A. K., & Allan, A. L. (2012). Inhibition of aldehyde dehydrogenase (ALDH) activity reduces chemotherapy and radiation resistance of stem-like ALDHhiCD44(+) human breast cancer cells. Breast Cancer Research and Treatment, 133(1), 75–87. https://doi.org/10.1007/s10549-011-1692-yCrossRefPubMed

184.

Najafzadeh, N., Mazani, M., Abbasi, A., Farassati, F., & Amani, M. (2015). Low-dose all-trans retinoic acid enhances cytotoxicity of cisplatin and 5-fluorouracil on CD44(+) cancer stem cells. Biomedicine & Pharmacotherapy, 74, 243–251. https://doi.org/10.1016/j.biopha.2015.08.019CrossRef

185.

Mao, X. M., Li, H., Zhang, X. Y., Zhou, P., Fu, Q. R., Chen, Q. E., et al. (2018). Retinoic acid receptor alpha knockdown suppresses the tumorigenicity of esophageal carcinoma via Wnt/beta-catenin pathway. Digestive Diseases and Sciences, 63(12), 3348–3358. https://doi.org/10.1007/s10620-018-5254-6CrossRefPubMed

186.

Singh, D. K., Carcamo, S., Farias, E. F., Hasson, D., Zheng, W., Sun, D., Huang, X., Cheung, J., Nobre, A. R., Kale, N., Sosa, M. S., Bernstein, E., & Aguirre-Ghiso, J. A. (2023). 5-Azacytidine- and retinoic-acid-induced reprogramming of DCCs into dormancy suppresses metastasis via restored TGF-β-SMAD4 signaling. Cell reports, 42(6), 112560. https://doi.org/10.1016/j.celrep.2023.112560CrossRefPubMed

187.

MacDonagh, L., Santiago, R. M., Gray, S. G., Breen, E., Cuffe, S., Finn, S. P., et al. (2021). Exploitation of the vitamin A/retinoic acid axis depletes ALDH1-positive cancer stem cells and re-sensitises resistant non-small cell lung cancer cells to cisplatin. Transl Oncol, 14(4), 101025. https://doi.org/10.1016/j.tranon.2021.101025CrossRefPubMedPubMedCentral

188.

Yao, W., Wang, L., Huang, H., Li, X., Wang, P., Mi, K., et al. (2020). All-trans retinoic acid reduces cancer stem cell-like cell-mediated resistance to gefitinib in NSCLC adenocarcinoma cells. BMC Cancer, 20(1), 315. https://doi.org/10.1186/s12885-020-06818-0CrossRefPubMedPubMedCentral

189.

Oh, T. G., Wang, S. M., Acharya, B. R., Goode, J. M., Graham, J. D., Clarke, C. L., et al. (2016). The Nuclear receptor, RORgamma, regulates pathways necessary for breast cancer metastasis. eBioMedicine, 6, 59–72. https://doi.org/10.1016/j.ebiom.2016.02.028CrossRefPubMedPubMedCentral

190.

Wen, Z., Chen, M., Guo, W., Guo, K., Du, P., Fang, Y., Gao, M., & Wang, Q. (2021). RORβ suppresses the stemness of gastric cancer cells by downregulating the activity of the Wnt signaling pathway. Oncology Reports, 46(2), 180. https://doi.org/10.3892/or.2021.8131CrossRefPubMedPubMedCentral

191.

Rambow, F., Rogiers, A., Marin-Bejar, O., Aibar, S., Femel, J., Dewaele, M., et al. (2018). Toward minimal residual disease-directed therapy in melanoma. Cell., 174(4), 843-855 e819. https://doi.org/10.1016/j.cell.2018.06.025CrossRefPubMed

192.

Jiang, P., Xu, C., Chen, L., Chen, A., Wu, X., Zhou, M., et al. (2018). Epigallocatechin-3-gallate inhibited cancer stem cell-like properties by targeting hsa-mir-485-5p/RXRalpha in lung cancer. Journal of Cellular Biochemistry, 119(10), 8623–8635. https://doi.org/10.1002/jcb.27117CrossRefPubMed

193.

Chavali, P. L., Saini, R. K., Zhai, Q., Vizlin-Hodzic, D., Venkatabalasubramanian, S., Hayashi, A., et al. (2014). TLX activates MMP-2, promotes self-renewal of tumor spheres in neuroblastoma and correlates with poor patient survival. Cell Death & Disease, 5(10), e1502. https://doi.org/10.1038/cddis.2014.449CrossRef

194.

Yang, D. R., Ding, X. F., Luo, J., Shan, Y. X., Wang, R., Lin, S. J., et al. (2013). Increased chemosensitivity via targeting testicular nuclear receptor 4 (TR4)-Oct4-interleukin 1 receptor antagonist (IL1Ra) axis in prostate cancer CD133+ stem/progenitor cells to battle prostate cancer. Journal of Biological Chemistry, 288(23), 16476–16483. https://doi.org/10.1074/jbc.M112.448142CrossRefPubMedPubMedCentral

195.

Pervin, S., Hewison, M., Braga, M., Tran, L., Chun, R., Karam, A., et al. (2013). Down-regulation of vitamin D receptor in mammospheres: Implications for vitamin D resistance in breast cancer and potential for combination therapy. PLoS ONE, 8(1), e53287. https://doi.org/10.1371/journal.pone.0053287CrossRefPubMedPubMedCentral

196.

Zheng, W., Duan, B., Zhang, Q., Ouyang, L., Peng, W., Qian, F., Wang, Y., & Huang, S. (2018). Vitamin D-induced vitamin D receptor expression induces tamoxifen sensitivity in MCF-7 stem cells via suppression of Wnt/β-catenin signaling. Bioscience Reports, 38(6), BSR20180595. https://doi.org/10.1042/BSR20180595CrossRefPubMedPubMedCentral

197.

Hu, P. S., Li, T., Lin, J. F., Qiu, M. Z., Wang, D. S., Liu, Z. X., et al. (2020). VDR-SOX2 signaling promotes colorectal cancer stemness and malignancy in an acidic microenvironment. Signal Transduction and Targeted Therapy, 5(1), 183. https://doi.org/10.1038/s41392-020-00230-7CrossRefPubMedPubMedCentral

198.

Liu, C., Shaurova, T., Shoemaker, S., Petkovich, M., Hershberger, P. A., & Wu, Y. (2018). Tumor-targeted nanoparticles deliver a vitamin D-based drug payload for the treatment of EGFR tyrosine kinase inhibitor-resistant lung cancer. Molecular Pharmaceutics, 15(8), 3216–3226. https://doi.org/10.1021/acs.molpharmaceut.8b00307CrossRefPubMed

199.

Jia, Z., Zhang, Y., Yan, A., Wang, M., Han, Q., Wang, K., et al. (2020). 1,25-dihydroxyvitamin D3 signaling-induced decreases in IRX4 inhibits NANOG-mediated cancer stem-like properties and gefitinib resistance in NSCLC cells. Cell Death & Disease, 11(8), 670. https://doi.org/10.1038/s41419-020-02908-wCrossRef

200.

Davey, R. A., & Grossmann, M. (2016). Androgen Receptor Structure, Function and Biology: From Bench to Bedside. Clinical Biochemist Reviews, 37(1), 3–15.PubMedPubMedCentral

201.

Fuentes, N., & Silveyra, P. (2019). Estrogen receptor signaling mechanisms. Advances in Protein Chemistry and Structural Biology, 116, 135–170. https://doi.org/10.1016/bs.apcsb.2019.01.001CrossRefPubMedPubMedCentral

202.

Polyak, K., & Weinberg, R. A. (2009). Transitions between epithelial and mesenchymal states: Acquisition of malignant and stem cell traits. Nature Reviews Cancer, 9(4), 265–273. https://doi.org/10.1038/nrc2620CrossRefPubMed

203.

Giguere, V. (2008). Transcriptional control of energy homeostasis by the estrogen-related receptors. Endocrine Reviews, 29(6), 677–696. https://doi.org/10.1210/er.2008-0017CrossRefPubMed

204.

Villena, J. A., & Kralli, A. (2008). ERRalpha: A metabolic function for the oldest orphan. Trends in Endocrinology and Metabolism, 19(8), 269–276. https://doi.org/10.1016/j.tem.2008.07.005CrossRefPubMed

205.

Schreiber, S. N., Knutti, D., Brogli, K., Uhlmann, T., & Kralli, A. (2003). The transcriptional coactivator PGC-1 regulates the expression and activity of the orphan nuclear receptor estrogen-related receptor alpha (ERRalpha). Journal of Biological Chemistry, 278(11), 9013–9018. https://doi.org/10.1074/jbc.M212923200CrossRefPubMed

206.

Tam, I. S., & Giguere, V. (2016). There and back again: The journey of the estrogen-related receptors in the cancer realm. Journal of Steroid Biochemistry and Molecular Biology, 157, 13–19. https://doi.org/10.1016/j.jsbmb.2015.06.009CrossRefPubMed

207.

Deblois, G., & Giguere, V. (2013). Oestrogen-related receptors in breast cancer: Control of cellular metabolism and beyond. Nature Reviews Cancer, 13(1), 27–36. https://doi.org/10.1038/nrc3396CrossRefPubMed

208.

Cai, Q., Lin, T., Kamarajugadda, S., & Lu, J. (2013). Regulation of glycolysis and the Warburg effect by estrogen-related receptors. Oncogene, 32(16), 2079–2086. https://doi.org/10.1038/onc.2012.221CrossRefPubMed

209.

Dufour, C. R., Wilson, B. J., Huss, J. M., Kelly, D. P., Alaynick, W. A., Downes, M., et al. (2007). Genome-wide orchestration of cardiac functions by the orphan nuclear receptors ERRalpha and gamma. Cell Metabolism, 5(5), 345–356. https://doi.org/10.1016/j.cmet.2007.03.007CrossRefPubMed

210.

Zhou, J., & Cidlowski, J. A. (2005). The human glucocorticoid receptor: One gene, multiple proteins and diverse responses. Steroids, 70(5–7), 407–417. https://doi.org/10.1016/j.steroids.2005.02.006CrossRefPubMed

211.

Davis, I. J., Hazel, T. G., Chen, R. H., Blenis, J., & Lau, L. F. (1993). Functional domains and phosphorylation of the orphan receptor Nur77. Molecular Endocrinology, 7(8), 953–964. https://doi.org/10.1210/mend.7.8.8232315CrossRefPubMed

212.

Maltais, A., & Labelle, Y. (2000). Structure and expression of the mouse gene encoding the orphan nuclear receptor TEC. DNA and Cell Biology, 19(2), 121–130. https://doi.org/10.1089/104454900314636CrossRefPubMed

213.

Paulsen, R. F., Granas, K., Johnsen, H., Rolseth, V., & Sterri, S. (1995). Three related brain nuclear receptors, NGFI-B, Nurr1, and NOR-1, as transcriptional activators. Journal of Molecular Neuroscience, 6(4), 249–255. https://doi.org/10.1007/BF02736784CrossRefPubMed

214.

Arkenbout, E. K., de Waard, V., van Bragt, M., van Achterberg, T. A., Grimbergen, J. M., Pichon, B., et al. (2002). Protective function of transcription factor TR3 orphan receptor in atherogenesis: Decreased lesion formation in carotid artery ligation model in TR3 transgenic mice. Circulation, 106(12), 1530–1535. https://doi.org/10.1161/01.cir.0000028811.03056.bfCrossRefPubMed

215.

Lim, R. W., Yang, W. L., & Yu, H. (1995). Signal-transduction-pathway-specific desensitization of expression of orphan nuclear receptor TIS1. The Biochemical Journal, 308(Pt 3), 785–789. https://doi.org/10.1042/bj3080785CrossRefPubMedPubMedCentral

216.

Nakai, A., Kartha, S., Sakurai, A., Toback, F. G., & DeGroot, L. J. (1990). A human early response gene homologous to murine nur77 and rat NGFI-B, and related to the nuclear receptor superfamily. Molecular Endocrinology, 4(10), 1438–1443. https://doi.org/10.1210/mend-4-10-1438CrossRefPubMed

217.

Winoto, A. (1997). Genes involved in T-cell receptor-mediated apoptosis of thymocytes and T-cell hybridomas. Seminars in Immunology, 9(1), 51–58. https://doi.org/10.1006/smim.1996.0053CrossRefPubMed

218.

Zetterstrom, R. H., Solomin, L., Mitsiadis, T., Olson, L., & Perlmann, T. (1996). Retinoid X receptor heterodimerization and developmental expression distinguish the orphan nuclear receptors NGFI-B, Nurr1, and Nor1. Molecular Endocrinology, 10(12), 1656–1666. https://doi.org/10.1210/mend.10.12.8961274CrossRefPubMed

219.

Berger, J., & Moller, D. E. (2002). The mechanisms of action of PPARs. Annual Review of Medicine, 53, 409–435. https://doi.org/10.1146/annurev.med.53.082901.104018CrossRefPubMed

220.

Delerive, P., Furman, C., Teissier, E., Fruchart, J., Duriez, P., & Staels, B. (2000). Oxidized phospholipids activate PPARalpha in a phospholipase A2-dependent manner. FEBS Letters, 471(1), 34–38. https://doi.org/10.1016/s0014-5793(00)01364-8CrossRefPubMed

221.

Neschen, S., Morino, K., Dong, J., Wang-Fischer, Y., Cline, G. W., Romanelli, A. J., et al. (2007). n-3 Fatty acids preserve insulin sensitivity in vivo in a peroxisome proliferator-activated receptor-alpha-dependent manner. Diabetes, 56(4), 1034–1041. https://doi.org/10.2337/db06-1206CrossRefPubMed

222.

Kliewer, S. A., Sundseth, S. S., Jones, S. A., Brown, P. J., Wisely, G. B., Koble, C. S., et al. (1997). Fatty acids and eicosanoids regulate gene expression through direct interactions with peroxisome proliferator-activated receptors alpha and gamma. Proc Natl Acad Sci U S A, 94(9), 4318–4323. https://doi.org/10.1073/pnas.94.9.4318CrossRefPubMedPubMedCentral

223.

Lo Verme, J., Fu, J., Astarita, G., La Rana, G., Russo, R., Calignano, A., et al. (2005). The nuclear receptor peroxisome proliferator-activated receptor-alpha mediates the anti-inflammatory actions of palmitoylethanolamide. Molecular Pharmacology, 67(1), 15–19. https://doi.org/10.1124/mol.104.006353CrossRefPubMed

224.

Wang, Y. X., Lee, C. H., Tiep, S., Yu, R. T., Ham, J., Kang, H., et al. (2003). Peroxisome-proliferator-activated receptor delta activates fat metabolism to prevent obesity. Cell, 113(2), 159–170. https://doi.org/10.1016/s0092-8674(03)00269-1CrossRefPubMed

225.

Stephen, R. L., Gustafsson, M. C., Jarvis, M., Tatoud, R., Marshall, B. R., Knight, D., et al. (2004). Activation of peroxisome proliferator-activated receptor delta stimulates the proliferation of human breast and prostate cancer cell lines. Cancer Research, 64(9), 3162–3170. https://doi.org/10.1158/0008-5472.can-03-2760CrossRefPubMed

226.

Lehrke, M., & Lazar, M. A. (2005). The many faces of PPARgamma. Cell, 123(6), 993–999. https://doi.org/10.1016/j.cell.2005.11.026CrossRefPubMed

227.

Medina-Gomez, G., Gray, S. L., Yetukuri, L., Shimomura, K., Virtue, S., Campbell, M., et al. (2007). PPAR gamma 2 prevents lipotoxicity by controlling adipose tissue expandability and peripheral lipid metabolism. PLoS Genetics, 3(4), e64. https://doi.org/10.1371/journal.pgen.0030064CrossRefPubMedPubMedCentral

228.

Pavek, P., & Dvorak, Z. (2008). Xenobiotic-induced transcriptional regulation of xenobiotic metabolizing enzymes of the cytochrome P450 superfamily in human extrahepatic tissues. Current Drug Metabolism, 9(2), 129–143. https://doi.org/10.2174/138920008783571774CrossRefPubMed

229.

Steven, A., Kliewer John, T., Laura, Moore, Wade Jeff, L., Staudinger Michael, A., Watson Stacey, A., Jones David, D., McKee Beverly, B., Oliver Timothy, M., Willson Rolf, H., Thomas, Zetterström, Perlmann Jürgen, M., & Lehmann,. (1998). An orphan nuclear receptor activated by pregnanes defines a novel steroid signaling pathway. Cell, 92(1), 73–82. https://doi.org/10.1016/S0092-8674(00)80900-9CrossRef

230.

Lehmann, J. M., McKee, D. D., Watson, M. A., Willson, T. M., Moore, J. T., & Kliewer, S. A. (1998). The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions. Journal of Clinical Investigation, 102(5), 1016–1023. https://doi.org/10.1172/JCI3703CrossRefPubMedPubMedCentral

231.

Ma, X., Idle, J. R., & Gonzalez, F. J. (2008). The pregnane X receptor: From bench to bedside. Expert Opinion on Drug Metabolism & Toxicology, 4(7), 895–908. https://doi.org/10.1517/17425255.4.7.895CrossRef

232.

Pavek, P. (2016). Pregnane X Receptor (PXR)-mediated gene repression and cross-talk of PXR with other nuclear receptors via coactivator interactions. Frontiers in Pharmacology, 7, 456. https://doi.org/10.3389/fphar.2016.00456CrossRefPubMedPubMedCentral

233.

McDonnell, D. P. (1995). Unraveling the human progesterone receptor signal transduction pathway Insights into antiprogestin action. Trends in Endocrinology and Metabolism, 6(4), 133–138. https://doi.org/10.1016/1043-2760(95)00065-pCrossRefPubMed

234.

Kariagina, A., Aupperlee, M. D., & Haslam, S. Z. (2008). Progesterone receptor isoform functions in normal breast development and breast cancer. Critical Reviews in Eukaryotic Gene Expression, 18(1), 11–33. https://doi.org/10.1615/critreveukargeneexpr.v18.i1.20CrossRefPubMedPubMedCentral

235.

Conneely, O. M., & Lydon, J. P. (2000). Progesterone receptors in reproduction: Functional impact of the A and B isoforms. Steroids, 65(10–11), 571–577. https://doi.org/10.1016/s0039-128x(00)00115-xCrossRefPubMed

236.

Giangrande, P. H., Pollio, G., & McDonnell, D. P. (1997). Mapping and characterization of the functional domains responsible for the differential activity of the A and B isoforms of the human progesterone receptor. Journal of Biological Chemistry, 272(52), 32889–32900. https://doi.org/10.1074/jbc.272.52.32889CrossRefPubMed

237.

Delacroix, L., Moutier, E., Altobelli, G., Legras, S., Poch, O., Choukrallah, M. A., et al. (2010). Cell-specific interaction of retinoic acid receptors with target genes in mouse embryonic fibroblasts and embryonic stem cells. Molecular and Cellular Biology, 30(1), 231–244. https://doi.org/10.1128/MCB.00756-09CrossRefPubMed

238.

Eifert, C., Sangster-Guity, N., Yu, L. M., Chittur, S. V., Perez, A. V., Tine, J. A., et al. (2006). Global gene expression profiles associated with retinoic acid-induced differentiation of embryonal carcinoma cells. Molecular Reproduction and Development, 73(7), 796–824. https://doi.org/10.1002/mrd.20444CrossRefPubMed

239.

Gudas, L. J., & Wagner, J. A. (2011). Retinoids regulate stem cell differentiation. Journal of Cellular Physiology, 226(2), 322–330. https://doi.org/10.1002/jcp.22417CrossRefPubMedPubMedCentral

240.

Dolle, P. (2009). Developmental expression of retinoic acid receptors (RARs). Nuclear Receptor Signaling, 7, e006. https://doi.org/10.1621/nrs.07006CrossRefPubMedPubMedCentral

241.

Mark, M., Ghyselinck, N. B., & Chambon, P. (2006). Function of retinoid nuclear receptors: Lessons from genetic and pharmacological dissections of the retinoic acid signaling pathway during mouse embryogenesis. Annual Review of Pharmacology and Toxicology, 46, 451–480. https://doi.org/10.1146/annurev.pharmtox.46.120604.141156CrossRefPubMed

242.

Niederreither, K., & Dolle, P. (2008). Retinoic acid in development: Towards an integrated view. Nature Reviews Genetics, 9(7), 541–553. https://doi.org/10.1038/nrg2340CrossRefPubMed

243.

Su, D., & Gudas, L. J. (2008). Gene expression profiling elucidates a specific role for RARgamma in the retinoic acid-induced differentiation of F9 teratocarcinoma stem cells. Biochemical Pharmacology, 75(5), 1129–1160. https://doi.org/10.1016/j.bcp.2007.11.006CrossRefPubMed

244.

Germain, P., Chambon, P., Eichele, G., Evans, R. M., Lazar, M. A., Leid, M., et al. (2006). International Union of Pharmacology. LXIII. Retinoid X receptors. Pharmacol Rev, 58(4), 760–772. https://doi.org/10.1124/pr.58.4.7CrossRefPubMed

245.

Hamada, K., Gleason, S. L., Levi, B. Z., Hirschfeld, S., Appella, E., & Ozato, K. (1989). H-2RIIBP, a member of the nuclear hormone receptor superfamily that binds to both the regulatory element of major histocompatibility class I genes and the estrogen response element. Proc Natl Acad Sci U S A, 86(21), 8289–8293. https://doi.org/10.1073/pnas.86.21.8289CrossRefPubMedPubMedCentral

246.

Yu, V. C., Delsert, C., Andersen, B., Holloway, J. M., Devary, O. V., Naar, A. M., et al. (1991). RXR beta: A coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements. Cell, 67(6), 1251–1266. https://doi.org/10.1016/0092-8674(91)90301-eCrossRefPubMed

247.

Mangelsdorf, D. J., Borgmeyer, U., Heyman, R. A., Zhou, J. Y., Ong, E. S., Oro, A. E., et al. (1992). Characterization of three RXR genes that mediate the action of 9-cis retinoic acid. Genes & Development, 6(3), 329–344. https://doi.org/10.1101/gad.6.3.329CrossRef

248.

Dolle, P., Fraulob, V., Kastner, P., & Chambon, P. (1994). Developmental expression of murine retinoid X receptor (RXR) genes. Mechanisms of Development, 45(2), 91–104. https://doi.org/10.1016/0925-4773(94)90023-xCrossRefPubMed

249.

Mangelsdorf, D. J., Ong, E. S., Dyck, J. A., & Evans, R. M. (1990). Nuclear receptor that identifies a novel retinoic acid response pathway. Nature, 345(6272), 224–229. https://doi.org/10.1038/345224a0CrossRefPubMed

250.

Haugen, B. R., Brown, N. S., Wood, W. M., Gordon, D. F., & Ridgway, E. C. (1997). The thyrotrope-restricted isoform of the retinoid-X receptor-gamma1 mediates 9-cis-retinoic acid suppression of thyrotropin-beta promoter activity. Molecular Endocrinology, 11(4), 481–489. https://doi.org/10.1210/mend.11.4.9905CrossRefPubMed

251.

Chiang, M. Y., Misner, D., Kempermann, G., Schikorski, T., Giguere, V., Sucov, H. M., et al. (1998). An essential role for retinoid receptors RARbeta and RXRgamma in long-term potentiation and depression. Neuron, 21(6), 1353–1361. https://doi.org/10.1016/s0896-6273(00)80654-6CrossRefPubMed

252.

Luskin, M. R., Murakami, M. A., Manalis, S. R., & Weinstock, D. M. (2018). Targeting minimal residual disease: A path to cure? Nature Reviews Cancer, 18(4), 255–263. https://doi.org/10.1038/nrc.2017.125CrossRefPubMedPubMedCentral

253.

Giguere, V., Tini, M., Flock, G., Ong, E., Evans, R. M., & Otulakowski, G. (1994). Isoform-specific amino-terminal domains dictate DNA-binding properties of ROR alpha, a novel family of orphan hormone nuclear receptors. Genes & Development, 8(5), 538–553. https://doi.org/10.1101/gad.8.5.538CrossRef

254.

Carlberg, C., Hooft van Huijsduijnen, R., Staple, J. K., DeLamarter, J. F., & Becker-Andre, M. (1994). RZRs, a new family of retinoid-related orphan receptors that function as both monomers and homodimers. Molecular Endocrinology, 8(6), 757–770. https://doi.org/10.1210/mend.8.6.7935491CrossRefPubMed

255.

Hirose, T., Smith, R. J., & Jetten, A. M. (1994). ROR gamma: The third member of ROR/RZR orphan receptor subfamily that is highly expressed in skeletal muscle. Biochemical and Biophysical Research Communications, 205(3), 1976–1983. https://doi.org/10.1006/bbrc.1994.2902CrossRefPubMed

256.

Hamilton, B. A., Frankel, W. N., Kerrebrock, A. W., Hawkins, T. L., FitzHugh, W., Kusumi, K., et al. (1996). Disruption of the nuclear hormone receptor RORalpha in staggerer mice. Nature, 379(6567), 736–739. https://doi.org/10.1038/379736a0CrossRefPubMed

257.

Steinmayr, M., Andre, E., Conquet, F., Rondi-Reig, L., Delhaye-Bouchaud, N., Auclair, N., et al. (1998). staggerer phenotype in retinoid-related orphan receptor alpha-deficient mice. Proc Natl Acad Sci U S A, 95(7), 3960–3965. https://doi.org/10.1073/pnas.95.7.3960CrossRefPubMedPubMedCentral

258.

Andre, E., Conquet, F., Steinmayr, M., Stratton, S. C., Porciatti, V., & Becker-Andre, M. (1998). Disruption of retinoid-related orphan receptor beta changes circadian behavior, causes retinal degeneration and leads to vacillans phenotype in mice. EMBO Journal, 17(14), 3867–3877. https://doi.org/10.1093/emboj/17.14.3867CrossRefPubMedPubMedCentral

259.

Andre, E., Gawlas, K., & Becker-Andre, M. (1998). A novel isoform of the orphan nuclear receptor RORbeta is specifically expressed in pineal gland and retina. Gene, 216(2), 277–283. https://doi.org/10.1016/s0378-1119(98)00348-5CrossRefPubMed

260.

Medvedev, A., Yan, Z. H., Hirose, T., Giguere, V., & Jetten, A. M. (1996). Cloning of a cDNA encoding the murine orphan receptor RZR/ROR gamma and characterization of its response element. Gene, 181(1–2), 199–206. https://doi.org/10.1016/s0378-1119(96)00504-5CrossRefPubMed

261.

Bouillon, R., Carmeliet, G., Verlinden, L., van Etten, E., Verstuyf, A., Luderer, H. F., et al. (2008). Vitamin D and human health: Lessons from vitamin D receptor null mice. Endocrine Reviews, 29(6), 726–776. https://doi.org/10.1210/er.2008-0004CrossRefPubMedPubMedCentral

262.

Pike, J. W., Meyer, M. B., Lee, S. M., Onal, M., & Benkusky, N. A. (2017). The vitamin D receptor: Contemporary genomic approaches reveal new basic and translational insights. The Journal of Clinical Investigation, 127(4), 1146–1154. https://doi.org/10.1172/JCI88887CrossRefPubMedPubMedCentral

263.

Freedland, S. J., de Almeida Luz, M., De Giorgi, U., Gleave, M., Gotto, G. T., Pieczonka, C. M., et al. (2023). Improved outcomes with enzalutamide in biochemically recurrent prostate cancer. New England Journal of Medicine, 389(16), 1453–1465. https://doi.org/10.1056/NEJMoa2303974CrossRefPubMed

264.

Sweeney, C. J., Martin, A. J., Stockler, M. R., Begbie, S., Cheung, L., Chi, K. N., et al. (2023). Testosterone suppression plus enzalutamide versus testosterone suppression plus standard antiandrogen therapy for metastatic hormone-sensitive prostate cancer (ENZAMET): An international, open-label, randomised, phase 3 trial. The lancet Oncology, 24(4), 323–334. https://doi.org/10.1016/S1470-2045(23)00063-3CrossRefPubMed

265.

Merseburger, A. S., Attard, G., Astrom, L., Matveev, V. B., Bracarda, S., Esen, A., et al. (2022). Continuous enzalutamide after progression of metastatic castration-resistant prostate cancer treated with docetaxel (PRESIDE): An international, randomised, phase 3b study. The lancet Oncology, 23(11), 1398–1408. https://doi.org/10.1016/S1470-2045(22)00560-5CrossRefPubMed

266.

Armstrong, A. J., Azad, A. A., Iguchi, T., Szmulewitz, R. Z., Petrylak, D. P., Holzbeierlein, J., et al. (2022). Improved Survival With Enzalutamide in Patients With Metastatic Hormone-Sensitive Prostate Cancer. Journal of Clinical Oncology, 40(15), 1616–1622. https://doi.org/10.1200/JCO.22.00193CrossRefPubMedPubMedCentral

267.

Josefsson, A., Jellvert, A., Holmberg, E., Brasso, K., Meidahl Petersen, P., Aaltomaa, S., et al. (2023). Effect of docetaxel added to bicalutamide in hormone-naive non-metastatic prostate cancer with rising PSA, a randomized clinical trial (SPCG-14). Acta Oncologica, 62(4), 372–380. https://doi.org/10.1080/0284186X.2023.2199940CrossRefPubMed

268.

Gu, W., Han, W., Luo, H., Zhou, F., He, D., Ma, L., et al. (2022). Rezvilutamide versus bicalutamide in combination with androgen-deprivation therapy in patients with high-volume, metastatic, hormone-sensitive prostate cancer (CHART): A randomised, open-label, phase 3 trial. The lancet Oncology, 23(10), 1249–1260. https://doi.org/10.1016/S1470-2045(22)00507-1CrossRefPubMed

269.

Penson, D. F., Armstrong, A. J., Concepcion, R. S., Agarwal, N., Olsson, C. A., Karsh, L. I., et al. (2022). Enzalutamide versus bicalutamide in patients with nonmetastatic castration-resistant prostate cancer: A prespecified subgroup analysis of the STRIVE trial. Prostate Cancer and Prostatic Diseases, 25(2), 363–365. https://doi.org/10.1038/s41391-021-00465-7CrossRefPubMed

270.

Yuan, Y., Lee, J. S., Yost, S. E., Frankel, P. H., Ruel, C., Egelston, C. A., et al. (2021). A phase II clinical trial of pembrolizumab and enobosarm in patients with androgen receptor-positive metastatic triple-negative breast cancer. The Oncologist, 26(2), 99-e217. https://doi.org/10.1002/onco.13583CrossRefPubMed

271.

Serritella, A. V., Shevrin, D., Heath, E. I., Wade, J. L., Martinez, E., Anderson, A., et al. (2022). Phase I/II trial of enzalutamide and mifepristone, a glucocorticoid receptor antagonist, for metastatic castration-resistant prostate cancer. Clinical Cancer Research, 28(8), 1549–1559. https://doi.org/10.1158/1078-0432.CCR-21-4049CrossRefPubMedPubMedCentral

272.

Cmero, M., Kurganovs, N. J., Stuchbery, R., McCoy, P., Grima, C., Ngyuen, A., Chow, K., Mangiola, S., Macintyre, G., Howard, N., Kerger, M., Dundee, P., Ruljancich, P., Clarke, D., Grummet, J., Peters, J. S., Costello, A. J., Norden, S., Ryan, A., … Corcoran, N. M. (2021). Loss of SNAI2 in prostate cancer correlates with clinical response to androgen deprivation therapy. JCO Precision Oncology, 5, PO.20.00337. https://doi.org/10.1200/PO.20.00337CrossRefPubMedPubMedCentral

273.

Eriksson, M., Eklund, M., Borgquist, S., Hellgren, R., Margolin, S., Thoren, L., et al. (2021). Low-dose tamoxifen for mammographic density reduction: A randomized controlled trial. Journal of Clinical Oncology, 39(17), 1899–1908. https://doi.org/10.1200/JCO.20.02598CrossRefPubMedPubMedCentral

274.

Hammarstrom, M., Gabrielson, M., Crippa, A., Discacciati, A., Eklund, M., Lundholm, C., et al. (2023). Side effects of low-dose tamoxifen: Results from a six-armed randomised controlled trial in healthy women. British Journal of Cancer, 129(1), 61–71. https://doi.org/10.1038/s41416-023-02293-zCrossRefPubMedPubMedCentral

275.

Baek, S. Y., Noh, W. C., Ahn, S. H., Kim, H. A., Ryu, J. M., Kim, S. I., et al. (2023). Adding ovarian suppression to tamoxifen for premenopausal women with hormone receptor-positive breast cancer after chemotherapy: An 8-year follow-up of the ASTRRA trial. Journal of Clinical Oncology, 41(31), 4864–4871. https://doi.org/10.1200/JCO.23.00557CrossRefPubMed

276.

Francis, P. A., Fleming, G. F., Lang, I., Ciruelos, E. M., Bonnefoi, H. R., Bellet, M., et al. (2023). Adjuvant endocrine therapy in premenopausal breast cancer: 12-year results from SOFT. Journal of Clinical Oncology, 41(7), 1370–1375. https://doi.org/10.1200/JCO.22.01065CrossRefPubMed

277.

Jhaveri, K., Eli, L. D., Wildiers, H., Hurvitz, S. A., Guerrero-Zotano, A., Unni, N., et al. (2023). Neratinib + fulvestrant + trastuzumab for HR-positive, HER2-negative, HER2-mutant metastatic breast cancer: Outcomes and biomarker analysis from the SUMMIT trial. Annals of Oncology, 34(10), 885–898. https://doi.org/10.1016/j.annonc.2023.08.003CrossRefPubMed

278.

Howell, S. J., Casbard, A., Carucci, M., Ingarfield, K., Butler, R., Morgan, S., et al. (2022). Fulvestrant plus capivasertib versus placebo after relapse or progression on an aromatase inhibitor in metastatic, oestrogen receptor-positive, HER2-negative breast cancer (FAKTION): Overall survival, updated progression-free survival, and expanded biomarker analysis from a randomised, phase 2 trial. The lancet Oncology, 23(7), 851–864. https://doi.org/10.1016/S1470-2045(22)00284-4CrossRefPubMedPubMedCentral

279.

Turner, N. C., Oliveira, M., Howell, S. J., Dalenc, F., Cortes, J., Gomez Moreno, H. L., et al. (2023). Capivasertib in hormone receptor-positive advanced breast cancer. New England Journal of Medicine, 388(22), 2058–2070. https://doi.org/10.1056/NEJMoa2214131CrossRefPubMed

280.

Elia, A., Saldain, L., Vanzulli, S. I., Helguero, L. A., Lamb, C. A., Fabris, V., et al. (2023). Beneficial effects of mifepristone treatment in patients with breast cancer selected by the progesterone receptor isoform ratio: Results from the MIPRA trial. Clinical Cancer Research, 29(5), 866–877. https://doi.org/10.1158/1078-0432.CCR-22-2060CrossRefPubMed

281.

Kato, S., Endoh, H., Masuhiro, Y., Kitamoto, T., Uchiyama, S., Sasaki, H., et al. (1995). Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase. Science, 270(5241), 1491–1494. https://doi.org/10.1126/science.270.5241.1491CrossRefPubMed

282.

Campbell, R. A., Bhat-Nakshatri, P., Patel, N. M., Constantinidou, D., Ali, S., & Nakshatri, H. (2001). Phosphatidylinositol 3-kinase/AKT-mediated activation of estrogen receptor alpha: A new model for anti-estrogen resistance. Journal of Biological Chemistry, 276(13), 9817–9824. https://doi.org/10.1074/jbc.M010840200CrossRefPubMed

283.

Jiang, J., Sarwar, N., Peston, D., Kulinskaya, E., Shousha, S., Coombes, R. C., et al. (2007). Phosphorylation of estrogen receptor-alpha at Ser167 is indicative of longer disease-free and overall survival in breast cancer patients. Clinical Cancer Research, 13(19), 5769–5776. https://doi.org/10.1158/1078-0432.CCR-07-0822CrossRefPubMed

284.

Sonneveld, P., Chanan-Khan, A., Weisel, K., Nooka, A. K., Masszi, T., Beksac, M., et al. (2023). Overall survival with daratumumab, bortezomib, and dexamethasone in previously treated multiple myeloma (CASTOR): A randomized, open-label, phase III trial. Journal of Clinical Oncology, 41(8), 1600–1609. https://doi.org/10.1200/JCO.21.02734CrossRefPubMed

285.

Dimopoulos, M. A., Dytfeld, D., Grosicki, S., Moreau, P., Takezako, N., Hori, M., et al. (2023). Elotuzumab plus pomalidomide and dexamethasone for relapsed/refractory multiple myeloma: Final overall survival analysis from the randomized phase II ELOQUENT-3 Trial. Journal of Clinical Oncology, 41(3), 568–578. https://doi.org/10.1200/JCO.21.02815CrossRefPubMed

286.

Derman, B. A., Kansagra, A., Zonder, J., Stefka, A. T., Grinblatt, D. L., Anderson, L. D., Jr., et al. (2022). Elotuzumab and weekly carfilzomib, lenalidomide, and dexamethasone in patients with newly diagnosed multiple myeloma without transplant intent: A phase 2 measurable residual disease-adapted study. JAMA Oncology, 8(9), 1278–1286. https://doi.org/10.1001/jamaoncol.2022.2424CrossRefPubMedPubMedCentral

287.

Costa, L. J., Chhabra, S., Medvedova, E., Dholaria, B. R., Schmidt, T. M., Godby, K. N., et al. (2023). Minimal residual disease response-adapted therapy in newly diagnosed multiple myeloma (MASTER): Final report of the multicentre, single-arm, phase 2 trial. Lancet Haematol, 10(11), e890–e901. https://doi.org/10.1016/S2352-3026(23)00236-3CrossRefPubMed

288.

Costa, L. J., Chhabra, S., Medvedova, E., Dholaria, B. R., Schmidt, T. M., Godby, K. N., et al. (2022). Daratumumab, carfilzomib, lenalidomide, and dexamethasone with minimal residual disease response-adapted therapy in newly diagnosed multiple myeloma. Journal of Clinical Oncology, 40(25), 2901–2912. https://doi.org/10.1200/JCO.21.01935CrossRefPubMed

289.

Barry, E. L., Peacock, J. L., Rees, J. R., Bostick, R. M., Robertson, D. J., Bresalier, R. S., et al. (2017). Vitamin D receptor genotype, vitamin D3 supplementation, and risk of colorectal adenomas: A randomized clinical trial. JAMA Oncology, 3(5), 628–635. https://doi.org/10.1001/jamaoncol.2016.5917CrossRefPubMedPubMedCentral

290.

Akutsu, T., Okada, S., Hirooka, S., Ikegami, M., Ohdaira, H., Suzuki, Y., et al. (2020). Effect of vitamin D on relapse-free survival in a subgroup of patients with p53 protein-positive digestive tract cancer: A post hoc analysis of the AMATERASU trial. Cancer Epidemiology, Biomarkers & Prevention, 29(2), 406–413. https://doi.org/10.1158/1055-9965.EPI-19-0986CrossRef

291.

Akiba, T., Morikawa, T., Odaka, M., Nakada, T., Kamiya, N., Yamashita, M., et al. (2018). Vitamin D supplementation and survival of patients with non-small cell lung cancer: A randomized, double-blind, placebo-controlled trial. Clinical Cancer Research, 24(17), 4089–4097. https://doi.org/10.1158/1078-0432.CCR-18-0483CrossRefPubMed

292.

Haidari, F., Abiri, B., Iravani, M., Ahmadi-Angali, K., & Vafa, M. (2020). Randomized study of the effect of vitamin D and omega-3 fatty acids cosupplementation as adjuvant chemotherapy on inflammation and nutritional status in colorectal cancer patients. J Diet Suppl, 17(4), 384–400. https://doi.org/10.1080/19390211.2019.1600096CrossRefPubMed

293.

Haidari, F., Abiri, B., Iravani, M., Ahmadi-Angali, K., & Vafa, M. (2020). Effects of vitamin D and omega-3 fatty acids co-supplementation on inflammatory factors and tumor marker cea in colorectal cancer patients undergoing chemotherapy: A randomized, double-blind, placebo-controlled clinical trial. Nutrition and Cancer, 72(6), 948–958. https://doi.org/10.1080/01635581.2019.1659380CrossRefPubMed

294.

Dalhoff, K., Dancey, J., Astrup, L., Skovsgaard, T., Hamberg, K. J., Lofts, F. J., et al. (2003). A phase II study of the vitamin D analogue Seocalcitol in patients with inoperable hepatocellular carcinoma. British Journal of Cancer, 89(2), 252–257. https://doi.org/10.1038/sj.bjc.6601104CrossRefPubMedPubMedCentral

295.

Evans, T. R., Colston, K. W., Lofts, F. J., Cunningham, D., Anthoney, D. A., Gogas, H., et al. (2002). A phase II trial of the vitamin D analogue Seocalcitol (EB1089) in patients with inoperable pancreatic cancer. British Journal of Cancer, 86(5), 680–685. https://doi.org/10.1038/sj.bjc.6600162CrossRefPubMedPubMedCentral

296.

Kutny, M. A., Alonzo, T. A., Abla, O., Rajpurkar, M., Gerbing, R. B., Wang, Y. C., et al. (2022). Assessment of arsenic trioxide and all-trans retinoic acid for the treatment of pediatric acute promyelocytic leukemia: A report from the Children’s Oncology group AAML1331 Trial. JAMA Oncology, 8(1), 79–87. https://doi.org/10.1001/jamaoncol.2021.5206CrossRefPubMed

297.

Wang, H. Y., Gong, S., Li, G. H., Yao, Y. Z., Zheng, Y. S., Lu, X. H., et al. (2022). An effective and chemotherapy-free strategy of all-trans retinoic acid and arsenic trioxide for acute promyelocytic leukemia in all risk groups (APL15 trial). Blood Cancer Journal, 12(11), 158. https://doi.org/10.1038/s41408-022-00753-yCrossRefPubMedPubMedCentral

298.

Debrock, G., Vanhentenrijk, V., Sciot, R., Debiec-Rychter, M., Oyen, R., & Van Oosterom, A. (2003). A phase II trial with rosiglitazone in liposarcoma patients. British Journal of Cancer, 89(8), 1409–1412. https://doi.org/10.1038/sj.bjc.6601306CrossRefPubMedPubMedCentral

299.

Sepmeyer, J. A., Greer, J. P., Koyama, T., & Zic, J. A. (2007). Open-label pilot study of combination therapy with rosiglitazone and bexarotene in the treatment of cutaneous T-cell lymphoma. Journal of the American Academy of Dermatology, 56(4), 584–587. https://doi.org/10.1016/j.jaad.2006.10.033CrossRefPubMed

300.

Smith, M. R., Manola, J., Kaufman, D. S., George, D., Oh, W. K., Mueller, E., et al. (2004). Rosiglitazone versus placebo for men with prostate carcinoma and a rising serum prostate-specific antigen level after radical prostatectomy and/or radiation therapy. Cancer, 101(7), 1569–1574. https://doi.org/10.1002/cncr.20493CrossRefPubMed

301.

Morita, A., Tateishi, C., Muramatsu, S., Kubo, R., Yonezawa, E., Kato, H., et al. (2020). Efficacy and safety of bexarotene combined with photo(chemo)therapy for cutaneous T-cell lymphoma. Journal of Dermatology, 47(5), 443–451. https://doi.org/10.1111/1346-8138.15310CrossRefPubMed

302.

Garon, E. B., Siegfried, J. M., Stabile, L. P., Young, P. A., Marquez-Garban, D. C., Park, D. J., et al. (2018). Randomized phase II study of fulvestrant and erlotinib compared with erlotinib alone in patients with advanced or metastatic non-small cell lung cancer. Lung Cancer, 123, 91–98. https://doi.org/10.1016/j.lungcan.2018.06.013CrossRefPubMed

Live-Webinar "Urologie und Sexualmedizin in der Praxis"

Springer Medizin

Dynamic interplay of nuclear receptors in tumor cell plasticity and drug resistance: Shifting gears in malignant transformations and applications in cancer therapeutics

Abstract

Graphical Abstract

Neu im Fachgebiet Onkologie

Bei seelischem Stress sind Checkpoint-Hemmer weniger wirksam

Antikörper mobilisiert Neutrophile gegen Krebs

Erhebliches Risiko für Kehlkopfkrebs bei mäßiger Dysplasie

15% bedauern gewählte Blasenkrebs-Therapie

Update Onkologie

Live-Webinar "Urologie und Sexualmedizin in der Praxis"

Springer Medizin

Abstract

Graphical Abstract

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

Weitere Artikel der Ausgabe 1/2024

Resveratrol as sensitizer in colorectal cancer plasticity

Cancer cell plasticity, stem cell factors, and therapy resistance: how are they linked?

Molecular panorama of therapy resistance in prostate cancer: a pre-clinical and bioinformatics analysis for clinical translation

Deciphering cellular plasticity in pancreatic cancer for effective treatments