Stonik, V. Marine natural products: A way to new drugs. Acta Nat.2, 15–25 (2009).
Carroll, A. R., Copp, B. R., Davis, R. A., Keyzers, R. A. & Prinsep, M. R. Marine natural products. Nat. Prod. Rep.36(1), 122–173 (2019).
Berlinck, R. G. S., Bertonha, A. F., Takaki, M. & Rodriguez, J. P. G. The chemistry and biology of guanidine natural products. Nat. Prod. Rep.34(11), 1264–1301 (2017).
Shi, Y., Moazami, Y. & Pierce, J. G. Structure, synthesis and biological properties of the pentacyclic guanidinium alkaloids. Biorg. Med. Chem.25(11), 2817–2824 (2017).
Berlinck, R. G. S. et al. The chemistry and biology of organic guanidine derivatives. Nat. Prod. Rep.27(12), 1871–1907 (2010).
Abbas, S. et al. Advancement into the arctic region for bioactive sponge secondary metabolites. Mar. Drugs9(11), 2423–2437 (2011).
Berlinck, R. G. S., Trindade-Silva, A. E. & Santos, M. F. C. The chemistry and biology of organic guanidine derivatives. Nat. Prod. Rep.29(12), 1382–1406 (2012).
Dyshlovoy, S. et al. Marine alkaloid Monanchocidin A induces lysosome membrane permeabilization and overcomes cisplatin resistance in germ cell tumor cells. Oncol. Res. Treat.37, 4–5 (2014).
Dyshlovoy, S. A. et al. Guanidine alkaloids from the marine sponge Monanchora pulchra show cytotoxic properties and prevent EGF-induced neoplastic transformation in vitro. Mar. Drugs14(7), 133 (2016).
Kashman, Y. et al. Ptilomycalin A: A novel polycyclic guanidine alkaloid of marine origin. J. Am. Chem. Soc.111(24), 8925–8926 (1989).
Tabakmakher, K. M. et al. Monanchomycalin C, a new pentacyclic guanidine alkaloid from the Far-Eastern marine sponge Monanchora pulchra. Nat. Prod. Commun.8(10), 1399–1402 (2013).
Guzii, A. G. et al. Monanchocidin: A new apoptosis-inducing polycyclic guanidine alkaloid from the marine sponge Monanchora pulchra. Org. Lett.12(19), 4292–4295 (2010).
Dyshlovoy, S. A. et al. Marine alkaloid Monanchocidin A overcomes drug resistance by induction of autophagy and lysosomal membrane permeabilization. Oncotarget6(19), 17328–17341 (2015).
Dyshlovoy, S. A. et al. Anti-migratory activity of marine alkaloid monanchocidin A: Proteomics-based discovery and confirmation. Proteomics16(10), 1590–1603 (2016).
Aron, Z. D., Pietraszkiewicz, H., Overman, L. E., Valeriote, F. & Cuevas, C. Synthesis and anticancer activity of side chain analogs of the crambescidin alkaloids. Biorg. Med. Chem. Lett.14(13), 3445–3449 (2004).
Roel, M. et al. Marine guanidine alkaloids crambescidins inhibit tumor growth and activate intrinsic apoptotic signaling inducing tumor regression in a colorectal carcinoma zebrafish xenograft model. Oncotarget7(50), 83071–83087 (2016).
Aoki, S., Kong, D., Matsui, K. & Kobayashi, M. Erythroid differentiation in K562 chronic myelogenous cells induced by crambescidin 800, a pentacyclic guanidine alkaloid. Anticancer Res.24(4), 2325–2330 (2004).
Berlinck, R. G. et al. Polycyclic guanidine alkaloids from the marine sponge Crambe crambe and Ca++ channel blocker activity of crambescidin 816. J. Nat. Prod.56(7), 1007–1015 (1993).
Martin, V. et al. Differential effects of crambescins and crambescidin 816 in voltage-gated sodium, potassium and calcium channels in neurons. Chem. Res. Toxicol.26(1), 169–178 (2013).
Rubiolo, J. A. et al. Mechanism of cytotoxic action of crambescidin-816 on human liver-derived tumour cells. Br. J. Pharmacol.171(7), 1655–1667 (2014).
Shubina, L. K. et al. Monanchoxymycalin C with anticancer properties, new analogue of crambescidin 800 from the marine sponge Monanchora pulchra. Nat. Prod. Res.33(10), 1415–1422 (2017).
Dyshlovoy, S. et al. Frondoside A induces AIF-associated caspase-independent apoptosis in Burkitt’s lymphoma cells. Leuk. Lymphoma
Dyshlovoy, S. A. et al. The marine triterpene glycoside frondoside A induces p53-independent apoptosis and inhibits autophagy in urothelial carcinoma cells. BMC Cancer17(1), 93 (2017).
Dyshlovoy, S. A. et al. The marine triterpene glycoside frondoside A exhibits activity in vitro and in vivo in prostate cancer. Int. J. Cancer138, 2450–2465 (2016).
Dyshlovoy, A. S. et al. Successful targeting of the warburg effect in prostate cancer by glucose-conjugated 1,4-naphthoquinones. Cancers11(11), 1690 (2019).
Arni, S. et al. Ex vivo multiplex profiling of protein tyrosine kinase activities in early stages of human lung adenocarcinoma. Oncotarget8(40), 68599–68613 (2017).
Chou, T.-C. Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies. Pharmacol. Rev.58(3), 621–681 (2006).
Chou, T.-C. Drug combination studies and their synergy quantification using the Chou–Talalay method. Cancer Res.70(2), 440–446 (2010).
Dyshlovoy, S. A. et al. Inspired by sea urchins: Warburg effect mediated selectivity of novel synthetic non-glycoside 1,4-naphthoquinone-6S-glucose conjugates in prostate cancer. Mar. Drugs18(5), 251 (2020).
Sampson, N., Neuwirt, H., Puhr, M., Klocker, H. & Eder, I. E. In vitro model systems to study androgen receptor signaling in prostate cancer. Endocr. Relat. Cancer20(2), R49-64 (2013).
Nelson, P. S. Targeting the androgen receptor in prostate cancer: A resilient foe. N. Engl. J. Med.371(11), 1067–1069 (2014).
Polverino, A. J. & Patterson, S. D. Selective activation of caspases during apoptotic induction in HL-60 cells. Effects of a tetrapeptide inhibitor. J. Biol. Chem.272(11), 7013–7021 (1997).
King, K. L., Jewell, C. M., Bortner, C. D. & Cidlowski, J. A. 28S ribosome degradation in lymphoid cell apoptosis: Evidence for caspase and Bcl-2-dependent and -independent pathways. Cell Death Differ.7(10), 994–1001 (2000).
Dhillon, A. S., Hagan, S., Rath, O. & Kolch, W. MAP kinase signalling pathways in cancer. Oncogene26(22), 3279–3290 (2007).
Struve, N. et al. EGFRvIII upregulates DNA mismatch repair resulting in increased temozolomide sensitivity of MGMT promoter methylated glioblastoma. Oncogene39(15), 3041–3055 (2020).
Rodríguez-Berriguete, G. et al. MAP kinases and prostate cancer. J. Signal Transduct.2012, 169170–169170 (2012).
Kamm, K. E. & Stull, J. T. The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu. Rev. Pharmacol. Toxicol.25, 593–620 (1985).
Tohtong, R., Phattarasakul, K., Jiraviriyakul, A. & Sutthiphongchai, T. Dependence of metastatic cancer cell invasion on MLCK-catalyzed phosphorylation of myosin regulatory light chain. Prostate Cancer Prostat. Dis.6(3), 212–216 (2003).
Xiong, Y. et al. Myosin light chain kinase: A potential target for treatment of inflammatory diseases. Front. Pharmacol.8, 292 (2017).
Hayashi, S. et al. Identification and characterization of RPK118, a novel sphingosine kinase-1-binding protein. J. Biol. Chem.277(36), 33319–33324 (2002).
Liu, L. et al. RPK118, a PX domain-containing protein, interacts with peroxiredoxin-3 through pseudo-kinase domains. Mol. Cells19(1), 39–45 (2005).
Greenman, C. et al. Patterns of somatic mutation in human cancer genomes. Nature446(7132), 153–158 (2007).
Schiebel, K. et al. Abnormal XY interchange between a novel isolated protein kinase gene, PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males and (Y−)XY females. Hum. Mol. Genet.6(11), 1985–1989 (1997).
Liu, J. & Lin, A. Role of JNK activation in apoptosis: A double-edged sword. Cell Res.15(1), 36–42 (2005).
Zhang, S. et al. c-Jun N-terminal kinase mediates hydrogen peroxide-induced cell death via sustained poly(ADP-ribose) polymerase-1 activation. Cell Death Differ.14(5), 1001–1010 (2007).
Li, X. et al. Targeting mitochondrial reactive oxygen species as novel therapy for inflammatory diseases and cancers. J. Hematol. Oncol.6, 19 (2013).
Lord, C. J. & Ashworth, A. PARP inhibitors: Synthetic lethality in the clinic. Science355(6330), 1152–1158 (2017).
Samatar, A. A. & Poulikakos, P. I. Targeting RAS-ERK signalling in cancer: Promises and challenges. Nat. Rev. Drug Discov.13(12), 928–942 (2014).
Gross, S., Rahal, R., Stransky, N., Lengauer, C. & Hoeflich, K. P. Targeting cancer with kinase inhibitors. J. Clin. Investig.125(5), 1780–1789 (2015).
Bode, A. M. & Dong, Z. The functional contrariety of JNK. Mol. Carcinog.46(8), 591–598 (2007).
Xu, R. & Hu, J. The role of JNK in prostate cancer progression and therapeutic strategies. Biomed. Pharmacother.121, 109679 (2020).
Yang, Y.-M. et al. C-Jun NH2-terminal kinase mediates proliferation and tumor growth of human prostate carcinoma. Clin. Cancer Res.9(1), 391 (2003).
Hu, J., Wang, G. & Sun, T. Dissecting the roles of the androgen receptor in prostate cancer from molecular perspectives. Tumour Biol.39(5), 1010428317692259 (2017).
Liu, P.-Y. et al. Regulation of androgen receptor expression by Z-isochaihulactone mediated by the JNK signaling pathway and might be related to cytotoxicity in prostate cancer. Prostate73(5), 531–541 (2013).
Tang, F. et al. Androgen via p21 inhibits tumor necrosis factor alpha-induced JNK activation and apoptosis. J. Biol. Chem.284(47), 32353–32358 (2009).
Shimada, K., Nakamura, M., Ishida, E., Kishi, M. & Konishi, N. Requirement of c-jun for testosterone-induced sensitization to N-(4-hydroxyphenyl)retinamide-induced apoptosis. Mol. Carcinog.36(3), 115–122 (2003).
Lorenzo, P. I. & Saatcioglu, F. Inhibition of apoptosis in prostate cancer cells by androgens is mediated through downregulation of c-jun N-terminal kinase activation. Neoplasia10(5), 418–428 (2008).
Hübner, A. et al. JNK and PTEN cooperatively control the development of invasive adenocarcinoma of the prostate. Proc. Natl. Acad. Sci.109(30), 12046 (2012).
Zhang, P. et al. Expressions of JNK and p-JNK in advanced prostate cancer and their clinical implications. Zhonghua Nan Ke Xue23(4), 309–314 (2017).
Guo, J. et al. Differential sensitization of different prostate cancer cells to apoptosis. Genes Cancer1(8), 836–846 (2010).
Gupta, K. et al. Green tea polyphenols induce p53-dependent and p53-independent apoptosis in prostate cancer cells through two distinct mechanisms. PLoS ONE7(12), e52572 (2012).
Guo, Y.-x et al. Jungermannenone A and B induce ROS- and cell cycle-dependent apoptosis in prostate cancer cells in vitro. Acta Pharmacol. Sin.37(6), 814–824 (2016).
Li, R. et al. Capilliposide C derived from Lysimachia capillipes Hemsl inhibits growth of human prostate cancer PC3 cells by targeting caspase and MAPK pathways. Int. Urol. Nephrol.46(7), 1335–1344 (2014).
Li, X., Shen, X., Xu, J., Li, X. & Ma, S. Hydration properties of the alite–ye’elimite cement clinker synthesized by reformation. Constr. Build. Mater.99, 254–259 (2015).
Koh, D. W., Dawson, T. M. & Dawson, V. L. Mediation of cell death by poly(ADP-ribose) polymerase-1. Pharmacol. Res.52(1), 5–14 (2005).
Braicu, C. et al. A comprehensive review on MAPK: A promising therapeutic target in cancer. Cancers11(10), 1618 (2019).
Khandrika, L. et al. Hypoxia-associated p38 mitogen-activated protein kinase-mediated androgen receptor activation and increased HIF-1α levels contribute to emergence of an aggressive phenotype in prostate cancer. Oncogene28(9), 1248–1260 (2009).
Nickols, N. G. et al. MEK-ERK signaling is a therapeutic target in metastatic castration resistant prostate cancer. Prostate Cancer Prostat. Dis.22(4), 531–538 (2019).