References
- Ahmad, N., Badshah, S. L., Junaid, M., Rehman, A. U., Muhammad, A., & Khan, K. (2020). Structural insights into the Zika virus NS1 protein inhibition using a computational approach. Journal of Biomolecular Structure and Dynamics, 38. https://doi.org/https://doi.org/10.1080/07391102.2020.1759453.
- Bousquet, P. F., Brana, M. F., Conlon, D., Fitzgerald, K. M., Perron, D., Cocchiaro, C., Miller, R., Moran, M., George, J., Quian, X. D., Keilhauer, G., & Romerdahl, C. A. (1995). Preclinical evaluation of LU 79553: A novel bis-naphthalimide with potent antitumor activity. Cancer Research, 55(5), 1176–1180. doi: https://doi.org/10.1007/BF01517352
- Brana, M. F., Cacho, M., Garcia, M. A., Pascual-Teresa, B., Ramos, A., Dominguez, M. T., Pozuelo, J. M., Abradelo, C., Rey-Stolle, M. F., Yuste, M., Banez-Coronel, M., & Lacal, J. C. (2004). New analogues of amonafide and elinafide, containing aromatic heterocycles: Synthesis, antitumor activity, molecular modeling, and DNA binding properties. Journal of Medicinal Chemistry, 47(6), 1391–1399. https://doi.org/https://doi.org/10.1021/jm0308850
- Chung, T., Mark, I., Navneet, K., Cynthia, B., Jean-Guy, D., Laurenc, V. K., & Otto 4th, P. (2008). A drosophila model to identify polyamine − drug conjugates that target the polyamine transporter in an intact epithelium. Journal of Medicinal Chemistry, 51, 324–330. doi: https://doi.org/10.1021/jm701198s.
- Dai, F. J., Li, Q., Wang, Y. X., Ge, C. C., Feng, C. Y., Xie, S. Q., He, H. Y., Xu, X. J., & Wang, C. J. (2017). Design, synthesis, and biological evaluation of mitochondria-targeted flavone-naphthalimide-polyamine conjugates with antimetastatic activity. Journal of Medicinal Chemistry, 60(5), 2071–2083. https://doi.org/https://doi.org/10.1021/acs.jmedchem.6b01846
- Deng, N., Dai, W., & Levy, R. M. (2013). How kinetics within the unfolded state affects protein folding: An analysis based on markov state models and an ultra-long MD trajectory. The Journal of Physical Chemistry. B, 117(42), 12787–12799. https://doi.org/https://doi.org/10.1021/jp401962k
- Fang, J., & Holmgren, A. (2006). Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo. Journal of the American Chemical Society, 128(6), 1879–1885. https://doi.org/https://doi.org/10.1021/ja057358l
- Han, S. (2007). Molecular dynamics simulations of thioredoxin with S-glutathiolated cysteine-73. Biochemical and Biophysical Research Communications, 362(2), 532–537. https://doi.org/https://doi.org/10.1016/j.bbrc.2007.08.037
- Jana, S., Ghosh, S., Dalapati, S., & Guchhait, N. (2012). Exploring structural change of protein bovine serum albumin by external perturbation using extrinsic fluorescence probe: Spectroscopic measurement, molecular docking and molecular dynamics simulation. Photochemistry and Photobiology Sciences, 11(2), 323–332. https://doi.org/https://doi.org/10.1039/C1PP05180F
- Li, M., Wang, Y., Zhang, J., Xie, S., Wang, C., & Wu, Y. (2016). Synthesis and biological evaluation of novel aromatic imide-polyamine conjugates. Molecules, 21(12), 1637. https://doi.org/10.3390/molecules21121637.
- Malviya, V. K., Liu, P. Y., Alberts, D. S., Surwit, E. A., Craig, J. B., & Hannigan, E. V. (1992). Evaluation of amonafide in cervical cancer, Phase II: A SWOG study. American Journal of Clinical Oncology, 15(1), 41–44. https://doi.org/https://doi.org/10.1097/00000421-199202000-00009
- Quaquebeke, E. V., Mahieu, T., Dumont, P., Dewelle, J., Ribaucour, F., Simon, G., Sauvage, S., Gaussin, J. F., Tuti, J., Yazidi, M. E., Vynckt, F. V., Mijatovic, T., Lefranc, F., Darro, F., & Kiss, R. (2007). 2, 2, 2-Trichloro-N- ({2-[2-(dimethylamino)ethyl]-1, 3-dioxo-2, 3-dihydro-1H benzo[de]isoquinolin-5-yl}carbamoyl)- acetamide (UNBS3157), a novel nonhematotoxic naphthalimide derivative with potent antitumor activity. Journal of Medicinal Chemistry, 50(17), 4122–4134. https://doi.org/https://doi.org/10.1021/jm070315q
- Robert, A., Casero, J., & Patrick, M. W. (2001). Terminally alkylated polyamine analogues as chemotherapeutic agents. Journal of Medicinal Chemistry, 44(1), 1–26. https://doi.org/https://doi.org/10.1021/jm000084m
- Satish, L., Millan, S., Bera, K., Mohapatra, S., & Sahoo, H. (2017). A spectroscopic and molecular dynamics simulation approach towards the stabilizing effect of ammonium-based ionic liquids on bovine serum albumin. New Journal of Chemistry, 41(19), 10712–10722. https://doi.org/https://doi.org/10.1039/C7NJ02900D
- Tian, Z. Y., Xie, S. Q., Du, Y. W., Ma, Y. F., Zhao, J., Gao, W. Y., & Wang, C. J. (2009). Synthesis, cytotoxicity and apoptosis of naphthalimide polyamine conjugates as antitumor agents. European Journal of Medicinal Chemistry, 44(1), 393–399. https://doi.org/https://doi.org/10.1016/j.ejmech.2008.02.044
- Tian, Z.-Y., Xie, S. Q., Mei, Z.-H., Zhao, J., Gao, W. Y., & Wang, C. J. (2009). Conjugation of substituted naphthalimides to polyamines as cytotoxic agents targeting the Akt/mTOR signal pathway. Organic & Biomolecular Chemistry, 7(22), 4651–4560. https://doi.org/https://doi.org/10.1039/b912685f
- Wang, Y. X., Zhang, X. B., Zhao, J., Xie, S. Q., & Wang, C. J. (2012). Nonhematotoxic naphthalene diimide modified by polyamine: Synthesis and biological evaluation. Journal of Medicinal Chemistry, 55(7), 3502–3512. https://doi.org/https://doi.org/10.1021/jm300168w
- Wu, D.-H., Lim, S. C., Dong, Y. H., Wu, J., Tao, F., Zhou, L., Zhang, L. H., & Song, H. W. (2012). Structural basis of substrate binding specificity revealed by the crystal structures of polyamine receptors SpuD and SpuE from pseudomonas aeruginosa. Journal of Molecular Biology, 416(5), 697–712. https://doi.org/https://doi.org/10.1016/j.jmb.2012.01.010