1 |
R. A. Spritz and G. H. Andersen, Genetics of vitiligo, Dermatol. Clin., 35(2), 245 (2017).
DOI
|
2 |
J. D. Simon, D. Peles, K. Wakamatsu, and S. Ito, Current challenges in understanding melanogenesis: bridging chemistry, biological control, morphology, and function, Pigment Cell Melanoma Res., 22(5), 563 (2009).
DOI
|
3 |
C. Olivares and F. Solano, New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins, Pigment Cell Melanoma Res., 22(6), 750 (2009).
DOI
|
4 |
A. Slominski, D. J. Tobin, S. Shibahara, and J. Wortsman, Melanin pigmentation in mammalian skin and its hormonal regulation, Physiol. Rev., 84(4), 1155 (2004).
DOI
|
5 |
Y. C. Boo, p-coumaric acid as an active ingredient in cosmetics: a review focusing on its antimelanogenic effects, Antioxidants, 8(8), 275 (2019).
DOI
|
6 |
C. Niu and H. A. Aisa, Upregulation of melanogenesis and tyrosinase activity: potential agents for vitiligo, Molecules, 22(8), 1303 (2017).
DOI
|
7 |
Y. C. Boo, Emerging strategies to protect the skin from ultraviolet rays using plant-derived materials, Antioxidants, 9(7), 637 (2020).
DOI
|
8 |
K. D. Haltaufderhyde and E. Oancea, Genome-wide transcriptome analysis of human epidermal melanocytes, Genomics, 104(6 Pt B), 482 (2014).
DOI
|
9 |
M. V. Schiaffino, Signaling pathways in melanosome biogenesis and pathology, Int. J. Biochem. Cell Biol., 42(7), 1094 (2010).
DOI
|
10 |
M. B. C. Maymone, H. H. Neamah, E. A. Secemsky, and N. A. Vashi, Correlating the dermatology life quality index and skin discoloration impact evaluation questionnaire tools in disorders of hyperpigmentation, J. Dermatol., 45(3), 361 (2018).
DOI
|
11 |
Y. C. Boo, Human skin lightening efficacy of resveratrol and its analogs: from in vitro studies to cosmetic applications, Antioxidants, 8(9), 332 (2019).
DOI
|
12 |
M. Ramos-e-Silva, L. R. Celem, S. Ramos-e-Silva, and A. P. Fucci-da-Costa, Anti-aging cosmetics: Facts and controversies, Clin. Dermatol., 31(6), 750 (2013).
DOI
|
13 |
Y. C. Boo, Up- or downregulation of melanin synthesis using amino acids, peptides, and their analogs, Biomedicines, 8(9), 322 (2020).
DOI
|
14 |
M. S. H an, X. Che, G. H . Cho, H . R. Park, K. E. Lim, N. R. Park, J. S. Jin, Y. K. Jung, J. H. Jeong, I. K. Lee, S. Kato, and J. Y. Choi, Functional cooperation between vitamin D receptor and Runx2 in vitamin D-induced vascular calcification, Plos One, 8(12), e83584 (2013).
DOI
|
15 |
K. H. Kim, T. R. Lee, and E. G. Cho, SH3BP4, a novel pigmentation gene, is inversely regulated by miR-125b and MITF, Exp. Mol. Med., 49(8), e367 (2017).
DOI
|
16 |
H . Song, Y. J. Hwang, J. W. Ha, and Y. C. Boo, Screening of an epigenetic drug library identifies 4-((hydroxyamino) carbonyl)-N-(2-hydroxyethyl)-N-phenyl -benzeneacetamide that reduces melanin synthesis by inhibiting tyrosinase activity independently of epigenetic mechanisms, Int. J. Mol. Sci., 21(13), 4589 (2020).
DOI
|
17 |
R. I. Glazer, K. D. Hartman, M. C. Knode, M. M. Richard, P. K. Chiang, C. K. Tseng, and V. E. Marquez, 3-Deazaneplanocin: a new and potent inhibitor of S-adenosylhomocysteine hydrolase and its effects on human promyelocytic leukemia cell line HL-60, Biochem. Biophys. Res. Commun., 135(2), 688 (1986).
DOI
|
18 |
J. Selhub, Homocysteine metabolism, Annu. Rev. Nutr., 19, 217 (1999).
DOI
|
19 |
J. K. Seok, S. W. Lee, J. Choi, Y. M. Kim, and Y. C. Boo, Identification of novel antimelanogenic hexapeptides via positional scanning of a synthetic peptide combinatorial library, Exp. Dermatol., 26(8), 742 (2017).
DOI
|
20 |
R. Ganceviciene, A. I. Liakou, A. Theodoridis, E. Makrantonaki, and C. C. Zouboulis, Skin anti-aging strategies, Dermatoendocrinol., 4(3), 308 (2012).
DOI
|
21 |
P. T. Rose, Pigmentary disorders, Med. Clin. North. Am., 93(6), 1225 (2009).
DOI
|
22 |
S. Yokoyama, E. Feige, L. L. Poling, C. Levy, H. R. Widlund, M. Khaled, A. L. Kung, and D. E. Fisher, Pharmacologic suppression of MITF expression via HDAC inhibitors in the melanocyte lineage, Pigment Cell Melanoma Res., 21(4), 457 (2008).
DOI
|
23 |
V. D. Callender, S. St Surin-Lord, E. C. Davis, and M. Maclin, Postinflammatory hyperpigmentation: etiologic and therapeutic considerations, Am. J. Clin. Dermatol., 12(2), 87 (2011).
DOI
|
24 |
P. Ganju, S. Nagpal, M. H. Mohammed, P. Nishal Kumar, R. Pandey, V. T. Natarajan, S. S. Mande, and R. S. Gokhale, Microbial community profiling shows dysbiosis in the lesional skin of vitiligo subjects, Sci. Rep., 6, 18761 (2016).
DOI
|
25 |
T. Pillaiyar, V. Namasivayam, M. Manickam, and S. H. Jung, Inhibitors of melanogenesis: an updated review, J. Med. Chem., 61(17), 7395 (2018).
DOI
|
26 |
A. Hayden, P. W. M. Johnson, G. Packham, and S. J. Crabb, S-adenosylhomocysteine hydrolase inhibition by 3-deazaneplanocin A analogues induces anti-cancer effects in breast cancer cell lines and synergy with both histone deacetylase and HER2 inhibition, Breast Cancer Res. Treat., 127(1), 109 (2011).
DOI
|
27 |
M. Soejima and Y. Koda, Population differences of two coding SNPs in pigmentation-related genes SLC24A5 and SLC45A2, Int. J. Legal Med., 121(1), 36 (2007).
DOI
|
28 |
J. B. Cheng and R. J. Cho, Genetics and epigenetics of the skin meet deep sequence, J. Invest. Dermatol., 132(3 Pt 2), 923 (2012).
DOI
|
29 |
J. S. Shin, H. S. Jeong, M. K. Kim, H. Y. Yun, K. J. Baek, N. S. Kwon, and D. S. Kim, The DNA methylation inhibitor 5-azacytidine decreases melanin synthesis by inhibiting CREB phosphorylation, Pharmazie, 70(10), 646 (2015).
|
30 |
K. H. Kim, B. H. Bin, J. Kim, S. E. Dong, P. J. Park, H. Choi, B. J. Kim, S. J. Yu, H. Kang, H. H. Kang, E. G. Cho, and T. R. Lee, Novel inhibitory function of miR-125b in melanogenesis, Pigment Cell Melanoma Res., 27(1), 140 (2014).
DOI
|
31 |
A. Garcia-Jimenez, J. A. Teruel-Puche, J. Berna, J. N. Rodriguez-Lopez, J. Tudela, and F. Garcia-Canovas, Action of tyrosinase on alpha and beta-arbutin: A kinetic study, PLoS One, 12(5), e0177330 (2017).
DOI
|
32 |
R. Yang, Y. Zheng, L. Li, S. Liu, M. Burrows, Z. Wei, A. Nace, M. Herlyn, R. Cui, W. Guo, G. Cotsarelis, and X. Xu, Direct conversion of mouse and human fibroblasts to functional melanocytes by defined factors, Nat. Commun., 5, 5807 (2014).
DOI
|
33 |
K. J. Livak and T. D. Schmittgen, Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCt method, Methods, 25(4), 402 (2001).
DOI
|
34 |
S. M. An, J. S. Koh, and Y. C. Boo, Inhibition of melanogenesis by tyrosinase siRNA in human melanocytes, BMB Rep., 42(3), 178 (2009).
DOI
|
35 |
J. H. Kim, J. K. Seok, Y. M. Kim, and Y. C. Boo, Identification of small peptides and glycinamide that inhibit melanin synthesis using a positional scanning synthetic peptide combinatorial library, Br. J. Dermatol., 181(1), 128 (2019).
DOI
|
36 |
S. A. Altman, L. Randers, and G. Rao, Comparison of trypan blue-dye exclusion and fluorometric assays for mammalian-cell viability determinations, Biotechnol. Prog., 9(6), 671 (1993).
DOI
|
37 |
S. W. Lee, J. H. Kim, H. Song, J. K. Seok, S. S. Hong, and Y. C. Boo, Luteolin 7-sulfate attenuates melanin synthesis through inhibition of CREB- and MITF-mediated tyrosinase expression, Antioxidants, 8(4), 87 (2019).
DOI
|
38 |
G. Y. Seo, Y. Ha, A. H. Park, O. W. Kwon, and Y. J. Kim, Leathesia difformis extract inhibits alpha-MSH-induced melanogenesis in B16F10 cells via down-regulation of CREB signaling pathway, Int. J. Mol. Sci., 20(3), 536 (2019).
DOI
|
39 |
K. B. Seamon, W. Padgett, and J. W. Daly, Forskolin: unique diterpene activator of adenylate cyclase in membranes and in intact cells, Proc. Natl. Acad. Sci. U S A, 78(6), 3363 (1981).
DOI
|
40 |
J. A. D'Orazio, T. Nobuhisa, R. Cui, M. Arya, M. Spry, K. Wakamatsu, V. Igras, T. Kunisada, S. R. Granter, E. K. Nishimura, S. Ito, and D. E. Fisher, Topical drug rescue strategy and skin protection based on the role of Mc1r in UV-induced tanning, Nature, 443(7109), 340 (2006).
DOI
|
41 |
S. Singh, U. Singh, and S. S. Pandey, Increased level of serum homocysteine in vitiligo, J. Clin. Lab. Anal., 25(2), 110 (2011).
DOI
|
42 |
T. B. Miranda, C. C. Cortez, C. B. Yoo, G. N. Liang, M. Abe, T. K. Kelly, V. E. Marquez, and P. A. Jones, DZNep is a global histone methylation inhibitor that reactivates developmental genes not silenced by DNA methylation, Mol. Cancer Ther., 8(6), 1579 (2009).
DOI
|
43 |
F. Liu, D. Barsyte-Lovejoy, F. L. Li, Y. Xiong, V. Korboukh, X. P. Huang, A. Allali-Hassani, W. P. Janzen, B. L. Roth, S. V. Frye, C. H. Arrowsmith, P. J. Brown, M. Vedadi, and J. Jin, Discovery of an in vivo chemical probe of the lysine methyltransferases G9a and GLP, J. Med. Chem., 56(21), 8931 (2013).
DOI
|
44 |
R. Dey-Rao and A. A. Sinha, Interactome analysis of gene expression profile reveals potential novel key transcriptional regulators of skin pathology in vitiligo, Genes Immun., 17(1), 30 (2016).
DOI
|
45 |
O. Reish, D. Townsend, S. A. Berry, M. Y. Tsai, and R. A. King, Tyrosinase inhibition due to interaction of homocysteine with copper - the mechanism for reversible hypopigmentation in homocystinuria due to cystathionine beta-synthase deficiency, Am. J. Hum. Genet., 57(1), 127 (1995).
|
46 |
J. Silverberg, and N. Silverberg, Serum homocysteine is associated with extent of vitiligo vulgaris, J. Am. Acad. Dermatol., 64(2), Ab142 (2011).
|
47 |
T. Y. Tsai, C. Y. Kuo, and Y. C. Huang, Serum homocysteine, folate, and vitamin B-12 levels in patients with vitiligo and their potential roles as disease activity biomarkers: A systematic review and meta-analysis, J. Am. Acad. Dermatol., 80(3), 646 (2019).
DOI
|
48 |
J. Chen, T. Zhuang, J. Chen, Y. Tian, X. Yi, Q. Ni, W. Zhang, P. Song, Z. Jian, L. Liu, T. Cui, K. Li, T. Gao, C. Li, and S. Li, Homocysteine induces melanocytes apoptosis via PERK-eIF2alpha-CHOP pathway in vitiligo, Clin. Sci. (Lond), 134(10), 1127 (2020).
DOI
|
49 |
Z. Y. Lu, H . R. Salwen, J. U. Raj, and Q. W. Yang, Histone lysine methyltransferase EHMT2 is involved in proliferation, apoptosis, and DNA methylation of human neuroblastoma cells, Cancer Res., 72((2012).
|