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Volumn 62, Issue 3-4, 2007, Pages 227-233

Effects of salicylic acid on mushroom tyrosinase and B16 melanoma cells

Author keywords

B16 F10 melanoma cells; Salicylic acid; Tyrosinase

Indexed keywords

BASIDIOMYCOTA; MURINAE;

EID: 34547434821     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-2007-3-412     Document Type: Article
Times cited : (12)

References (15)
  • 1
    • 0028176278 scopus 로고
    • Inhibitor binding to the binuclear active site of tyrosinase: Temperature, pH, and solvent deuterium isotope effects
    • Conrad J. S., Dawso S. R., Hubbard E. R., Meyers T. E., and Strothkamp K. G. (1994), Inhibitor binding to the binuclear active site of tyrosinase: Temperature, pH, and solvent deuterium isotope effects. Biochemistry 33, 5739-5744.
    • (1994) Biochemistry , vol.33 , pp. 5739-5744
    • Conrad, J.S.1    Dawso, S.R.2    Hubbard, E.R.3    Meyers, T.E.4    Strothkamp, K.G.5
  • 2
    • 0032855966 scopus 로고    scopus 로고
    • Slow-binding inhibition of mushroom (Agaricus bisporus) tyrosinase isoforms by tropolone
    • Espín J. C. and Wichers H. J. (1999), Slow-binding inhibition of mushroom (Agaricus bisporus) tyrosinase isoforms by tropolone. J. Agric. Food Chem. 47, 2638-2644.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 2638-2644
    • Espín, J.C.1    Wichers, H.J.2
  • 3
    • 25444509223 scopus 로고    scopus 로고
    • Effects of mushroom tyrosinase on anisaldehyde
    • Ha T. J., Tamura S., and Kubo I. (2005), Effects of mushroom tyrosinase on anisaldehyde. J. Agric. Food Chem. 53, 7024-7028.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 7024-7028
    • Ha, T.J.1    Tamura, S.2    Kubo, I.3
  • 4
    • 3042591315 scopus 로고    scopus 로고
    • Down-regulation of melanogenesis by phospholipase D2 through ubiquitin proteasome-mediated degradation of tyrosinase
    • Kageyama A., Oka M., Okada T., Nakamura S., Ueyama T., Saito N., Hearing V. J., Ichihashi M., and Nishigori C. (2004), Down-regulation of melanogenesis by phospholipase D2 through ubiquitin proteasome-mediated degradation of tyrosinase. J. Biol. Chem. 279, 27774-27780.
    • (2004) J. Biol. Chem , vol.279 , pp. 27774-27780
    • Kageyama, A.1    Oka, M.2    Okada, T.3    Nakamura, S.4    Ueyama, T.5    Saito, N.6    Hearing, V.J.7    Ichihashi, M.8    Nishigori, C.9
  • 5
    • 0001397165 scopus 로고    scopus 로고
    • Tyrosinase inhibitors from cumin
    • Kubo I. and Kinst-Hori I. (1998), Tyrosinase inhibitors from cumin. J. Agric. Food Chem. 46, 5338-5341.
    • (1998) J. Agric. Food Chem , vol.46 , pp. 5338-5341
    • Kubo, I.1    Kinst-Hori, I.2
  • 6
    • 0344994605 scopus 로고    scopus 로고
    • Flavonols from saffron flower: Tyrosinase inhibitory activity and inhibition mechanisms
    • Kubo I. and Kinst-Hori I. (1999), Flavonols from saffron flower: Tyrosinase inhibitory activity and inhibition mechanisms. J. Agric. Food Chem. 47, 4121-4125.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 4121-4125
    • Kubo, I.1    Kinst-Hori, I.2
  • 7
    • 0000940559 scopus 로고
    • Molluscicides from the cashew Anacardium occidentale and their large-scale isolation
    • Kubo I., Komatsu S., and Ochi M. (1986), Molluscicides from the cashew Anacardium occidentale and their large-scale isolation. J. Agric. Food Chem. 34, 970-973.
    • (1986) J. Agric. Food Chem , vol.34 , pp. 970-973
    • Kubo, I.1    Komatsu, S.2    Ochi, M.3
  • 8
    • 0028287786 scopus 로고
    • Tyrosinase inhibitors from Anacardium occidentale fruits
    • Kubo I., Kinst-Hori I., and Yokokawa Y. (1994), Tyrosinase inhibitors from Anacardium occidentale fruits. J. Nat. Prod. 57, 545-551.
    • (1994) J. Nat. Prod , vol.57 , pp. 545-551
    • Kubo, I.1    Kinst-Hori, I.2    Yokokawa, Y.3
  • 10
    • 0030076508 scopus 로고    scopus 로고
    • Arbutin: Mechanism of its depigmenting action in human melanocyte culture
    • Maeda K. and Fukuda M. (1996), Arbutin: Mechanism of its depigmenting action in human melanocyte culture. J. Pharm. Exp. Therap. 276, 765-769.
    • (1996) J. Pharm. Exp. Therap , vol.276 , pp. 765-769
    • Maeda, K.1    Fukuda, M.2
  • 11
    • 0000838740 scopus 로고
    • Assay of catechol oxidase - a critical comparison of methods
    • Mayer A. M., Harel E., and Ben-Shaul R. (1966), Assay of catechol oxidase - a critical comparison of methods. Phytochemistry 5, 783-789.
    • (1966) Phytochemistry , vol.5 , pp. 783-789
    • Mayer, A.M.1    Harel, E.2    Ben-Shaul, R.3
  • 12
  • 13
    • 0038680412 scopus 로고    scopus 로고
    • Identification of oxidation product of arbutin in mushroom tyrosinase assay system
    • Nihei K. and Kubo I. (2003), Identification of oxidation product of arbutin in mushroom tyrosinase assay system. Bioorg. Med. Chem. Lett. 13, 2409-2412.
    • (2003) Bioorg. Med. Chem. Lett , vol.13 , pp. 2409-2412
    • Nihei, K.1    Kubo, I.2
  • 14
    • 1642461642 scopus 로고    scopus 로고
    • Effects of piperine analogues on stimulation of melanocyte proliferation and melanocyte differentiation
    • Venkatasamy R., Faas L., Young A. R., Raman A., and Hider R. C. (2004), Effects of piperine analogues on stimulation of melanocyte proliferation and melanocyte differentiation. Bioorg. Med. Chem. 12, 1905-1920.
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 1905-1920
    • Venkatasamy, R.1    Faas, L.2    Young, A.R.3    Raman, A.4    Hider, R.C.5
  • 15
    • 33845378952 scopus 로고
    • Substrate analogue binding to the coupled binuclear copper active site in tyrosinase
    • Wilcox D. E., Porras A. G., Hwang Y. T., Lerch K., Winkler M. E., and Solomon E. I. (1985), Substrate analogue binding to the coupled binuclear copper active site in tyrosinase. J. Am. Chem. Soc. 107, 4015-4027.
    • (1985) J. Am. Chem. Soc , vol.107 , pp. 4015-4027
    • Wilcox, D.E.1    Porras, A.G.2    Hwang, Y.T.3    Lerch, K.4    Winkler, M.E.5    Solomon, E.I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.