References
- V. J. Hearing, Biochemical control of melanogenesis and melanosomal organization, J. Investig. Dermatol. Symp. Proc., 4, 24 (1999). https://doi.org/10.1038/sj.jidsp.5640176
- M. Tsatmali, J. Ancans, and A. J. Thody, Melanocyte function and its control by melanocortin peptides, J. Histochem. Cytochem., 50, 125 (2002). https://doi.org/10.1177/002215540205000201
- A. K. Gupta, M. D. Gover, K. N. Nouri, and S. Taylor, The treatment of melasma: a review of clinical trials, J. Am. Acad. Dermatol., 55, 1048 (2006). https://doi.org/10.1016/j.jaad.2006.02.009
- S. R. Dalton, T. L. Gardner, L. F. Libow, and D. M. Elston, Contiguous lesions in lentigo maligna, J. Am. Acad. Dermatol., 52, 859 (2005). https://doi.org/10.1016/j.jaad.2004.11.063
- S.-Y. SeO, V. K. Sharma, and N. Sharma, Mushroom Tyrosinase: Recent Prospects, J. Agric. Food Chem., 51, 2837 (2003). https://doi.org/10.1021/jf020826f
- Y.-J. Kim and H. Uyama, Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future, Cell. Mol. Life Sci., 62, 1707 (2005). https://doi.org/10.1007/s00018-005-5054-y
- V. D. Marmol and F. Beermann, Tyrosinase and related proteins in mammalian pigmentation, FEBS Lett., 381, 165 (1996). https://doi.org/10.1016/0014-5793(96)00109-3
- C. J. Smith, K. B. O'Hare, and J. C. Alle, Selective cybtoxicity of hydroquinone for melanoma derived cells is mediated by tyrosinase activity but independent of melanin content, Pigment Cell Res., 1, 386 (1988). https://doi.org/10.1111/j.1600-0749.1988.tb00140.x
- K-K. Song, H. Huang, P. Han, C-L. Zhang, Y. Shi, and Q-X. Chen, Inhibitory effects of cis- and trans-isomers of 3,5-dihydroxystilbene on the activity of mushroom tyrosinase, Biochem. Biophys. Res. Commun., 342, 1147 (2006). https://doi.org/10.1016/j.bbrc.2005.12.229
-
N. Fujimoto, H. Watanabe, T. Nakatani, G. Roy, and A. Ito, Induction of thyroid tumours in (C57BL/6N
${\times}$ C3H/N)F1 mice by oral administration of kojic acid, Food Chem. Toxicol., 36, 697 (1998). https://doi.org/10.1016/S0278-6915(98)00030-1 - A. M. Korner and J. Pawelek, Dopachrome Conversion: A Possible Control Point in Melanin Biosynthesis, J. Invest. Dermatol., 75, 192 (1980). https://doi.org/10.1111/1523-1747.ep12522650
- Y. Mishima, S. Hatta, Y. Ohyama, and M. Inazu, Induction of melanogenesis suppression: cellular pharmacology and mode of differential action, Pigment Cell Res., 1, 367 (1988). https://doi.org/10.1111/j.1600-0749.1988.tb00136.x
- K. Maeda and M. Fukuda, Arbutin: mechanism of its depigmenting action in human melanocyte culture, J. Pharmacol. Exp. Ther., 276, 765 (1996).
- L. M. Liu, L. Chen, R. H. Wang, Q. Yang, X. G. Weng, and L. Wang, Study on finger-print of Cortex Fraxini with HPLC, Zhongguo Zhongyao Zazhi, 33, 2932 (2008).
- H. Wang, Y. Dou, J. Tian, F. Li, S. Wang, and Z. Wang, Research on medical specialty of traditional Chinese medicines using dot-Immunoblotting method based on polyclonal antibody prepared from traditional Chinese medicines with hot/cold nature, Zhongguo Zhongyao Zazhi, 34, 438 (2009).
- Y. Masamoto, H. Ando, Y. Murata, Y. Shimoishi, M. Tada, and K. Takahata, Mushroom tyrosinase inhibitory activity of esculetin isolated from seeds of Euphorbia lathyris L., Biosci. Biotechnol. Biochem., 67(3), 631 (2003). https://doi.org/10.1271/bbb.67.631
- A. N. Jain, Surflex: fully automatic flexible molecular docking using a molecular similarity-based search engine, J. Med. Chem., 46, 499 (2003). https://doi.org/10.1021/jm020406h
- Y. Matoba, T. Kumagai, A. Yamamoto, H. Yoshitsu, and M. Sugiyama, Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis, J. Biol. Chem., 281, 8981 (2006). https://doi.org/10.1074/jbc.M509785200