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Volumn 10, Issue 6, 2009, Pages 2440-2475

An updated review of tyrosinase inhibitors

Author keywords

Browning; Inhibitors; Melanogenesis; Tyrosinase

Indexed keywords

CHALCONE; COUMARIN; ENZYME INHIBITOR; EUMELANIN; KOJIC ACID; MELANIN; POLYPHENOL; STILBENE DERIVATIVE; TYROSINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 67649668609     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms10062440     Document Type: Review
Times cited : (1239)

References (170)
  • 1
    • 0000537283 scopus 로고
    • The anaerobic oxidases
    • Raper, H.S. The anaerobic oxidases. Physiol. Rev. 1928, 8, 245-282.
    • (1928) Physiol. Rev. , vol.8 , pp. 245-282
    • Raper, H.S.1
  • 2
    • 0002518418 scopus 로고
    • The chemistry of melanin. III. Mechanism of the oxidation of trihydroxyphenylalanine by tyrosinase
    • Mason, H.S. The chemistry of melanin. III. Mechanism of the oxidation of trihydroxyphenylalanine by tyrosinase. J. Biol. Chem. 1948, 172, 83-99.
    • (1948) J. Biol. Chem. , vol.172 , pp. 83-99
    • Mason, H.S.1
  • 3
    • 0030722720 scopus 로고    scopus 로고
    • Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase
    • Cooksey, C.J.; Garratt, P.J.; Land, E.J.; Pavel, S.; Ramsden, C.A.; Riley, P.A.; Smit N.P.M. Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase. J. Biol. Chem. 1997, 272, 26226-26235.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26226-26235
    • Cooksey, C.J.1    Garratt, P.J.2    Land, E.J.3    Pavel, S.4    Ramsden, C.A.5    Riley, P.A.6    Smit, N.P.M.7
  • 6
    • 0039448182 scopus 로고    scopus 로고
    • Review: Enzymatic browning in minimally processed fruit and vegetables
    • Artés, F.; Castañer, M.; Gil, M.I. Review: enzymatic browning in minimally processed fruit and vegetables. J. Agric. Food Chem. 1998, 4, 377-389.
    • (1998) J. Agric. Food Chem. , vol.4 , pp. 377-389
    • Artés, F.1    Castañer, M.2    Gil, M.I.3
  • 8
    • 23844545621 scopus 로고    scopus 로고
    • Tyrosinase inhibitors from natural and synthetic sources: Structure, inhibition mechanism and perspective for the future
    • Kim, Y.J.; Uyama, H. Tyrosinase inhibitors from natural and synthetic sources: structure, inhibition mechanism and perspective for the future. Cell. Mol. Life Sci. 2005, 62, 1707-1723.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1707-1723
    • Kim, Y.J.1    Uyama, H.2
  • 9
    • 34548614908 scopus 로고    scopus 로고
    • Naturally occurring tyrosinase inhibitors: Mechanism and applications in skin health, cosmetics and agriculture industries
    • Parvez, S.; Kang, M.; Chung, H.S.; Bae, H. Naturally occurring tyrosinase inhibitors: mechanism and applications in skin health, cosmetics and agriculture industries. Phytother. Res. 2007, 21, 805-816.
    • (2007) Phytother. Res. , vol.21 , pp. 805-816
    • Parvez, S.1    Kang, M.2    Chung, H.S.3    Bae, H.4
  • 10
    • 0038580778 scopus 로고    scopus 로고
    • Chemical and instrumental approaches to treat hyperpigmentation
    • DOI 10.1034/j.1600-0749.2003.00029.x
    • Briganti, S.; Camera, E.; Picardo, M. Chemical and instrumental approaches to treat hyperpigmentation. Pigment Cell Res. 2003, 16, 101-110. (Pubitemid 36596955)
    • (2003) Pigment Cell Research , vol.16 , Issue.2 , pp. 101-110
    • Briganti, S.1    Camera, E.2    Picardo, M.3
  • 11
    • 23344450642 scopus 로고    scopus 로고
    • Review of skin-lightening agents
    • Rendon, M.I.; Gaviria, J.I. Review of skin-lightening agents. Dermatol. Surg. 2005, 31, 886-889.
    • (2005) Dermatol. Surg. , vol.31 , pp. 886-889
    • Rendon, M.I.1    Gaviria, J.I.2
  • 12
    • 36649036991 scopus 로고    scopus 로고
    • Skin lightening preparations and the hydroquinone controversy
    • Draelos, Z.D. Skin lightening preparations and the hydroquinone controversy. Dermatol. Ther. 2007, 20, 308-313.
    • (2007) Dermatol. Ther. , vol.20 , pp. 308-313
    • Draelos, Z.D.1
  • 14
    • 33750538670 scopus 로고    scopus 로고
    • Hypopigmenting agents: An updated review on biological, chemical and clinical aspects
    • DOI 10.1111/j.1600-0749.2006.00334.x
    • Solano, F.; Briganti, S.; Picardo, M.; Ghanem, G. Hypopigmenting agents: an updated review on biological, chemical and clinical aspects. Pigment Cell Res. 2006, 19, 550-571. (Pubitemid 44674109)
    • (2006) Pigment Cell Research , vol.19 , Issue.6 , pp. 550-571
    • Solano, F.1    Briganti, S.2    Picardo, M.3    Ghanem, G.4
  • 15
    • 33947327697 scopus 로고    scopus 로고
    • Approaches to identify inhibitors of melanin biosynthesis via the quality control of tyrosinase
    • Ando, H.; Kondoh, H.; Ichihashi, M.; Hearing, V.J. Approaches to identify inhibitors of melanin biosynthesis via the quality control of tyrosinase. J. Invest. Dermatol. 2007, 127, 751-761.
    • (2007) J. Invest. Dermatol. , vol.127 , pp. 751-761
    • Ando, H.1    Kondoh, H.2    Ichihashi, M.3    Hearing, V.J.4
  • 16
    • 41349106224 scopus 로고    scopus 로고
    • The use of botanical extracts as topical skin-lightening agents for the improvement of skin pigmentation disorders
    • Zhu, W.; Gao, J. The use of botanical extracts as topical skin-lightening agents for the improvement of skin pigmentation disorders. J. Investig. Dermatol. Symp. Proc. 2008, 13, 20-24.
    • (2008) J. Investig. Dermatol. Symp. Proc. , vol.13 , pp. 20-24
    • Zhu, W.1    Gao, J.2
  • 19
    • 0035999729 scopus 로고    scopus 로고
    • Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects
    • Sugumaran, M. Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Pigment Cell. Res. 2002, 15, 2-9.
    • (2002) Pigment Cell. Res. , vol.15 , pp. 2-9
    • Sugumaran, M.1
  • 20
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba, Y.; Kumagai, T.; Yamamoto, A.; Yoshitsu, H.; Sugiyama, M. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 2006, 281, 8981-8990.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 21
    • 33645065115 scopus 로고    scopus 로고
    • Tyrosinase maturation through the mammalian secretory pathway: Bringing color to life
    • Wang, N.; Hebert, D.N. Tyrosinase maturation through the mammalian secretory pathway: bringing color to life. Pigment Cell Res. 2006, 19, 3-18.
    • (2006) Pigment Cell Res. , vol.19 , pp. 3-18
    • Wang, N.1    Hebert, D.N.2
  • 23
    • 0036016301 scopus 로고    scopus 로고
    • Molecular anatomy of tyrosinase and its related proteins: Beyond the histidine-bound metal catalytic center
    • DOI 10.1034/j.1600-0749.2002.02012.x
    • García-Borron, J.C.; Solano, F. Molecular anatomy of tyrosinase and its related proteins: Beyond the histidine bound metal catalytic center. Pigment Cell Res. 2002, 15, 162-173. (Pubitemid 34608974)
    • (2002) Pigment Cell Research , vol.15 , Issue.3 , pp. 162-173
    • Garcia-Borron, J.C.1    Solano, F.2
  • 24
    • 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.; Solomon, E.I. Substrate analogue binding to the coupled binuclear copper active site in tyrosinase. J. Am. Chem. 1985, 107, 4015-4027.
    • (1985) J. Am. Chem. , 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
  • 25
    • 33751500842 scopus 로고
    • Inhibition mechanism of kojic acid on polyphenol oxidase
    • Chen, J.S.; Wei, C.; Marshall, M.R. Inhibition mechanism of kojic acid on polyphenol oxidase. J. Agric. Food Chem. 1991, 39, 1897-1901.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1897-1901
    • Chen, J.S.1    Wei, C.2    Marshall, M.R.3
  • 26
    • 0028597093 scopus 로고
    • Kojic acid, a cosmetic skin whitening agent, is a slow-binding inhibitor of catecholase activity of tyrosinase
    • Cabanes, J.; Chazarra, S.; García-Carmona, F. Kojic acid, a cosmetic skin whitening agent, is a slow-binding inhibitor of catecholase activity of tyrosinase. J. Pharm. Pharmacol. 1994, 46, 982-985.
    • (1994) J. Pharm. Pharmacol. , vol.46 , pp. 982-985
    • Cabanes, J.1    Chazarra, S.2    García-Carmona, F.3
  • 27
    • 0032855966 scopus 로고    scopus 로고
    • Slow-binding inhibition of mushroom (Agaricus bisporus) tyrosinase isoforms by tropolone
    • Espín, J.C.; Wichers, H.J. Slow-binding inhibition of mushroom (Agaricus bisporus) tyrosinase isoforms by tropolone. J. Agric. Food Chem. 1999, 47, 2638-2644.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 2638-2644
    • Espín, J.C.1    Wichers, H.J.2
  • 29
    • 0034736046 scopus 로고    scopus 로고
    • Advances in flavonoid research since 1992
    • Harborne, J.B.; Williams, C.A. Advances in flavonoid research since 1992. Phytochemistry 2000, 55, 481-504.
    • (2000) Phytochemistry , vol.55 , pp. 481-504
    • Harborne, J.B.1    Williams, C.A.2
  • 30
    • 0344994605 scopus 로고    scopus 로고
    • Flavonols from saffron flower: Tyrosinase inhibitory activity and inhibition mechanism
    • Kubo, I.; Kinst-Hori, I. Flavonols from saffron flower: tyrosinase inhibitory activity and inhibition mechanism. J. Agric. Food Chem. 1999, 47, 4121-4125.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4121-4125
    • Kubo, I.1    Kinst-Hori, I.2
  • 31
    • 0033933718 scopus 로고    scopus 로고
    • Flavonols from Heterotheca inuloides: Tyrosinase inhibitory activity and structural criteria
    • Kubo, I.; Kinst-Hori, I.; Chaudhuri, S.K.; Kubo, Y.; Sánchez, Y.; Ogura, T. Flavonols from Heterotheca inuloides: tyrosinase inhibitory activity and structural criteria. Bioorg. Med. Chem. 2000, 8, 1749-1755.
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 1749-1755
    • Kubo, I.1    Kinst-Hori, I.2    Chaudhuri, S.K.3    Kubo, Y.4    Sánchez, Y.5    Ogura, T.6
  • 32
    • 0037644565 scopus 로고    scopus 로고
    • Inhibitory effects of some flavonoids on the activity of mushroom tyrosinase
    • Xie, L.P.; Chen, Q.X.; Huang, H.; Wang, H.Z.; Zhang, R.Q. Inhibitory effects of some flavonoids on the activity of mushroom tyrosinase. Biochemistry 2003, 68, 487-491.
    • (2003) Biochemistry , vol.68 , pp. 487-491
    • Xie, L.P.1    Chen, Q.X.2    Huang, H.3    Wang, H.Z.4    Zhang, R.Q.5
  • 33
    • 0029111821 scopus 로고
    • Studies of cuticle drugs from natural sources. III. Inhibitory effect of Myrica rubra on melanin biosynthesis
    • Matsuda, H.; Higashino, M.; Chen, W.; Tosa, H.; Iinuma, M.; Kubo, M. Studies of cuticle drugs from natural sources. III. Inhibitory effect of Myrica rubra on melanin biosynthesis. Biol. Pharm. Bull. 1995, 18, 1148-1150.
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 1148-1150
    • Matsuda, H.1    Higashino, M.2    Chen, W.3    Tosa, H.4    Iinuma, M.5    Kubo, M.6
  • 34
    • 65649098315 scopus 로고    scopus 로고
    • Two new flavonol glycosides from Lamium amplexicaule L. and their in vitro free radical scavenging and tyrosinase inhibitory activities
    • Nugroho, A.; Choi, J.K.; Park, J.H.; Lee, K.T.; Cha, B.C.; Park, H.J. Two new flavonol glycosides from Lamium amplexicaule L. and their in vitro free radical scavenging and tyrosinase inhibitory activities. Planta Med. 2009, 75, 364-366.
    • (2009) Planta Med. , vol.75 , pp. 364-366
    • Nugroho, A.1    Choi, J.K.2    Park, J.H.3    Lee, K.T.4    Cha, B.C.5    Park, H.J.6
  • 35
    • 33846974360 scopus 로고    scopus 로고
    • Inhibitory effects of 5,6,7-trihydroxyflavones on tyrosinase
    • Gao, H.; Nishida, J.; Saito, S.; Kawabata, J. Inhibitory effects of 5,6,7-trihydroxyflavones on tyrosinase. Molecules 2007, 12, 86-97.
    • (2007) Molecules , vol.12 , pp. 86-97
    • Gao, H.1    Nishida, J.2    Saito, S.3    Kawabata, J.4
  • 36
    • 33847728947 scopus 로고    scopus 로고
    • Tyrosinase inhibitory effects and inhibition mechanisms of nobiletin and hesperidin from citrus peel crude extracts
    • Zhang, C.; Lu, Y.; Tao, L.; Tao, X.; Su, X.; Wei, D. Tyrosinase inhibitory effects and inhibition mechanisms of nobiletin and hesperidin from citrus peel crude extracts. J. Enzyme Inhib. Med. Chem. 2007, 22, 83-90.
    • (2007) J. Enzyme Inhib. Med. Chem. , vol.22 , pp. 83-90
    • Zhang, C.1    Lu, Y.2    Tao, L.3    Tao, X.4    Su, X.5    Wei, D.6
  • 38
    • 0036690366 scopus 로고    scopus 로고
    • Mulberroside F isolated from the leaves of Morus alba inhibits melanin biosynthesis
    • Lee, S.H.; Choi, S.Y.; Kim, H.; Hwang, J.S.; Lee, B.G.; Gao, J.J.; Kim, S.Y. Mulberroside F isolated from the leaves of Morus alba inhibits melanin biosynthesis. Biol. Pharm. Bull. 2002, 25, 1045-1048.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 1045-1048
    • Lee, S.H.1    Choi, S.Y.2    Kim, H.3    Hwang, J.S.4    Lee, B.G.5    Gao, J.J.6    Kim, S.Y.7
  • 39
    • 56449121507 scopus 로고    scopus 로고
    • Inhibitory effects on mushroom tyrosinase by flavones from the stem barks of Morus lhou (S.) Koidz
    • Ryu, Y.B.; Ha, T.J.; Curtis-Long, M.J.; Ryu, H.W.; Gal, S.W.; Park, K.H. Inhibitory effects on mushroom tyrosinase by flavones from the stem barks of Morus lhou (S.) Koidz. J. Enzyme Inhib. Med. Chem. 2008, 23, 922-930.
    • (2008) J. Enzyme Inhib. Med. Chem. , vol.23 , pp. 922-930
    • Ryu, Y.B.1    Ha, T.J.2    Curtis-Long, M.J.3    Ryu, H.W.4    Gal, S.W.5    Park, K.H.6
  • 42
    • 33748351202 scopus 로고    scopus 로고
    • Inhibitory effect of artocarpanone from Artocarpus heterophyllus on melanin biosynthesis
    • Arung, E.T.; Shimizu, K.; Kondo, R. Inhibitory effect of artocarpanone from Artocarpus heterophyllus on melanin biosynthesis. Biol. Pharm. Bull. 2006, 29, 1966-1969.
    • (2006) Biol. Pharm. Bull. , vol.29 , pp. 1966-1969
    • Arung, E.T.1    Shimizu, K.2    Kondo, R.3
  • 43
    • 57549099265 scopus 로고    scopus 로고
    • Isolation of tyrosinase inhibitors from Artocarpus heterophyllus and use of its extract as antibrowning agent
    • Zheng, Z.P.; Cheng, K.W.; To, J.T.; Li, H.; Wang, M. Isolation of tyrosinase inhibitors from Artocarpus heterophyllus and use of its extract as antibrowning agent. Mol. Nutr. Food Res. 2008, 52, 1530-1538.
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. 1530-1538
    • Zheng, Z.P.1    Cheng, K.W.2    To, J.T.3    Li, H.4    Wang, M.5
  • 44
    • 33847614832 scopus 로고    scopus 로고
    • Identification of tyrosinase inhibitors from Marrubium velutinum and Marrubium cylleneum
    • Karioti, A.; Protopappa, A.; Megoulas, N.; Skaltsa, H. Identification of tyrosinase inhibitors from Marrubium velutinum and Marrubium cylleneum. Bioorg. Med. Chem. 2007, 15, 2708-2714.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 2708-2714
    • Karioti, A.1    Protopappa, A.2    Megoulas, N.3    Skaltsa, H.4
  • 45
    • 33244460034 scopus 로고    scopus 로고
    • Flavonoids as mushroom tyrosinase inhibitors: A fluorescence quenching study
    • Kim, D.; Park, J.; Kim, J.; Han, C.; Yoon, J.; Kim, N.; Seo, J.; Lee, C. Flavonoids as mushroom tyrosinase inhibitors: A fluorescence quenching study. J. Agric. Food Chem. 2006, 54, 935-941.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 935-941
    • Kim, D.1    Park, J.2    Kim, J.3    Han, C.4    Yoon, J.5    Kim, N.6    Seo, J.7    Lee, C.8
  • 46
    • 33847652922 scopus 로고    scopus 로고
    • Inhibitory compound of tyrosinase activity from the sprout of Polygonum hydropiper L. (Benitade)
    • Miyazawa, M.; Tamura, N. Inhibitory compound of tyrosinase activity from the sprout of Polygonum hydropiper L. (Benitade). Biol. Pharm. Bull. 2007, 30, 595-597.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 595-597
    • Miyazawa, M.1    Tamura, N.2
  • 47
    • 52649114815 scopus 로고    scopus 로고
    • Flavonoids, taxifolin and luteolin attenuate cellular melanogenesis despite increasing tyrosinase protein levels
    • An, S.M.; Kim, H.J.; Kim, J.E.; Boo, Y.C. Flavonoids, taxifolin and luteolin attenuate cellular melanogenesis despite increasing tyrosinase protein levels. Phytother. Res. 2008, 22, 1200-1207.
    • (2008) Phytother. Res. , vol.22 , pp. 1200-1207
    • An, S.M.1    Kim, H.J.2    Kim, J.E.3    Boo, Y.C.4
  • 48
    • 15244355251 scopus 로고    scopus 로고
    • Screening for tyrosinase inhibitors among extracts of seashore plants and identification of potent inhibitors from Garcinia subelliptica
    • DOI 10.1271/bbb.69.197
    • Masuda, T.; Yamashita, D.; Takeda, Y.; Yonemori, S. Screening for tyrosinase inhibitors among extracts of seashore plants and identification of potent inhibitors from Garcinia subelliptica. Biosci. Biotechnol., Biochem. 2005, 69, 197-201. (Pubitemid 40383500)
    • (2005) Bioscience, Biotechnology and Biochemistry , vol.69 , Issue.1 , pp. 197-201
    • Masuda, T.1    Yamashita, D.2    Takeda, Y.3    Yonemori, S.4
  • 49
    • 0032239708 scopus 로고    scopus 로고
    • The Inhibitory Effect of Glabridin from Licorice Extracts on Melanogenesis and Inflammation
    • Yokota, T.; Nishio, H.; Kubota, Y.; Mizoguchi, M. The inhibitory effect of glabridin from licorice extracts on melanogenesis and inflammation. Pigment Cell Res. 1998, 11, 355-361. (Pubitemid 128531532)
    • (1998) Pigment Cell Research , vol.11 , Issue.6 , pp. 355-361
    • Yokota, T.1    Nishio, H.2    Kubota, Y.3    Mizoguchi, M.4
  • 50
    • 0037467028 scopus 로고    scopus 로고
    • Glabrene and isoliquiritigenin as tyrosinase inhibitors from Licorice roots
    • Nerya, O.; Vaya, J.; Musa, R.; Izrael, S.; Ben-Arie, R.; Tamir, S. Glabrene and isoliquiritigenin as tyrosinase inhibitors from Licorice roots. J. Agric. Food Chem. 2003, 51, 1201-1207.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 1201-1207
    • Nerya, O.1    Vaya, J.2    Musa, R.3    Izrael, S.4    Ben-Arie, R.5    Tamir, S.6
  • 51
    • 24944508196 scopus 로고    scopus 로고
    • Identification of tyrosinase inhibitors from Glycyrrhiza uralensis
    • DOI 10.1055/s-2005-871232
    • Kim, H.J.; Seo, S.H.; Lee, B.G.; Lee, Y.S. Identification of tyrosinase inhibitors from Glycyrrhiza uralensis. Planta Med. 2005, 71, 785-787. (Pubitemid 41306205)
    • (2005) Planta Medica , vol.71 , Issue.8 , pp. 785-787
    • Kim, H.J.1    Seo, S.H.2    Lee, B.-G.3    Lee, Y.S.4
  • 52
    • 27644444019 scopus 로고    scopus 로고
    • Identifying 6,7,4'-trihydroxyisoflavone as a potent tyrosinase inhibitor
    • Chang, T.S.; Ding, H.Y.; Lin, H.C. Identifying 6,7,4'- trihydroxyisoflavone as a potent tyrosinase inhibitor. Biosci. Biotechnol., Biochem. 2005, 69, 1999-2001.
    • (2005) Biosci. Biotechnol., Biochem. , vol.69 , pp. 1999-2001
    • Chang, T.S.1    Ding, H.Y.2    Lin, H.C.3
  • 53
    • 34447633916 scopus 로고    scopus 로고
    • Tyrosinase inhibitors isolated from soygerm koji fermented with Aspergillus oryzae BCRC 32288
    • Chang, T.S.; Ding, H.Y.; Tai, S.S.K.; Wu, C.Y. Tyrosinase inhibitors isolated from soygerm koji fermented with Aspergillus oryzae BCRC 32288. Food Chem. 2007, 105, 1430-1438.
    • (2007) Food Chem. , vol.105 , pp. 1430-1438
    • Chang, T.S.1    Ding, H.Y.2    Tai, S.S.K.3    Wu, C.Y.4
  • 54
    • 33947600591 scopus 로고    scopus 로고
    • Two potent suicide substrates of mushroom tyrosinase: 7, 8, 4′-trihydroxyisoflavone and 5, 7, 8,4′-tetrahydroxyisoflavone
    • Chang, T. S. Two potent suicide substrates of mushroom tyrosinase: 7, 8, 4′-trihydroxyisoflavone and 5, 7, 8,4′-tetrahydroxyisoflavone. J. Agric. Food Chem. 2007, 55, 2010-2015.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 2010-2015
    • Chang, T.S.1
  • 56
    • 50249109395 scopus 로고    scopus 로고
    • Inhibitory effect of dalbergioidin isolated from the trunk of Lespedeza cyrtobotrya on melanin biosynthesis
    • Baek, S.; Kim, J.; Kim, D.; Lee, C.; Kim, J.; Chung, D.K.; Lee, C. Inhibitory effect of dalbergioidin isolated from the trunk of Lespedeza cyrtobotrya on melanin biosynthesis. J. Microbiol. Biotechnol. 2008, 18, 874-879.
    • (2008) J. Microbiol. Biotechnol. , vol.18 , pp. 874-879
    • Baek, S.1    Kim, J.2    Kim, D.3    Lee, C.4    Kim, J.5    Chung, D.K.6    Lee, C.7
  • 57
    • 60749086012 scopus 로고    scopus 로고
    • Inhibitory effects of calycosin isolated from the root of Astragalus membranaceus on melanin biosynthesis
    • Kim, J.H.; Kim, M.R.; Lee, E.S.; Lee, C.H. Inhibitory effects of calycosin isolated from the root of Astragalus membranaceus on melanin biosynthesis. Biol. Pharm. Bull. 2009, 32, 264-268.
    • (2009) Biol. Pharm. Bull. , vol.32 , pp. 264-268
    • Kim, J.H.1    Kim, M.R.2    Lee, E.S.3    Lee, C.H.4
  • 58
    • 26244463344 scopus 로고    scopus 로고
    • Isolation and identification of flavonoids in licorice and a study of their inhibitory effects on tyrosinase
    • Fu, B.; Li, H.; Wang, X.; Lee, F.S.; Cui, S. Isolation and identification of flavonoids in licorice and a study of their inhibitory effects on tyrosinase. J. Agric. Food Chem. 2005, 53, 7408-7414.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 7408-7414
    • Fu, B.1    Li, H.2    Wang, X.3    Lee, F.S.4    Cui, S.5
  • 59
    • 2142754392 scopus 로고    scopus 로고
    • Tyrosinase inhibitory prenylated flavonoids from Sophora flavescens
    • Kim, S.J.; Son, K.H.; Chang, H.W.; Kang, S.S.; Kim, H.P. Tyrosinase inhibitory prenylated flavonoids from Sophora flavescens. Biol. Pharm. Bull. 2003, 26, 1348-1350.
    • (2003) Biol. Pharm. Bull. , vol.26 , pp. 1348-1350
    • Kim, S.J.1    Son, K.H.2    Chang, H.W.3    Kang, S.S.4    Kim, H.P.5
  • 60
    • 38049049927 scopus 로고    scopus 로고
    • Inhibitory effect of kurarinol, kuraridinol, and trifolirhizin from Sophora flavescens on tyrosinase and melanin synthesis
    • Hyun, S.K.; Lee, W.H.; Jeong, da.M.; Kim, Y.; Choi, J.S. Inhibitory effect of kurarinol, kuraridinol, and trifolirhizin from Sophora flavescens on tyrosinase and melanin synthesis. Biol. Pharm. Bull. 2008, 31, 154-158.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 154-158
    • Hyun, S.K.1    Lee, W.H.2    Jeong, Da.M.3    Kim, Y.4    Choi, J.S.5
  • 61
    • 59949085461 scopus 로고    scopus 로고
    • Inhibitory effect of 2,4,2',4'-tetrahydroxy-3-(3-methyl-2-butenyl)- chalcone on tyrosinase activity and melanin biosynthesis
    • Zhang, X.; Hu, X.; Hou, A.; Wang. H. Inhibitory effect of 2,4,2',4'-tetrahydroxy-3-(3-methyl-2-butenyl)-chalcone on tyrosinase activity and melanin biosynthesis. Biol. Pharm. Bull. 2009, 32, 86-90.
    • (2009) Biol. Pharm. Bull. , vol.32 , pp. 86-90
    • Zhang, X.1    Hu, X.2    Hou, A.3    Wang, H.4
  • 62
    • 0033975767 scopus 로고    scopus 로고
    • Inhibition of tyrosinase by flavonoids, stilbenes and related 4- Substituted resorcinols: Structure-activity investigations
    • DOI 10.1055/s-2000-11113
    • Shimizu, K.; Kondo, R.; Sakai, K. Inhibition of tyrosinase by flavonoids, stilbenes and related 4-substituted resorcinols: structure-activity investigations. Planta Med. 2000, 66, 11-15. (Pubitemid 30097272)
    • (2000) Planta Medica , vol.66 , Issue.1 , pp. 11-15
    • Shimizu, K.1    Kondo, R.2    Sakai, K.3
  • 63
    • 7444229216 scopus 로고    scopus 로고
    • Inhibitory effects of hexylresorcinol and dodecylresorcinol on mushroom (Agaricus bisporus) tyrosinase
    • DOI 10.1023/B:JOPC.0000020080.21417.ff
    • Chen, Q.X.; Ke, L.N.; Song, K.K.; Huang, H.; Liu, X.D. Inhibitory effects of hexylresorcinol and dodecylresorcinol on mushroom (Agaricus bisporus) tyrosinase. Protein J. 2004, 23, 135-141. (Pubitemid 41399336)
    • (2004) Protein Journal , vol.23 , Issue.2 , pp. 135-141
    • Chen, Q.-X.1    Ke, L.-N.2    Song, K.-K.3    Huang, H.4    Liu, X.-D.5
  • 64
    • 3042522850 scopus 로고    scopus 로고
    • Chalcones as potent tyrosinase inhibitors: The effect of hydroxyl positions and numbers
    • DOI 10.1016/j.phytochem.2004.04.016, PII S0031942204001797
    • Nerya, O.; Musa, R.; Khatib, S.; Tamir, S.; Vaya, J. Chalcones as potent tyrosinase inhibitors: the effect of hydroxyl positions and numbers. Phytochemistry 2004, 65, 1389-1395. (Pubitemid 38844723)
    • (2004) Phytochemistry , vol.65 , Issue.10 , pp. 1389-1395
    • Nerya, O.1    Musa, R.2    Khatib, S.3    Tamir, S.4    Vaya, J.5
  • 65
    • 10444280081 scopus 로고    scopus 로고
    • Chalcones as potent tyrosinase inhibitors: The importance of a 2,4-substituted resorcinol moiety
    • Khatib, S.; Nerya, O.; Musa, R.; Shmuel, M.; Tamir, S.; Vaya, J. Chalcones as potent tyrosinase inhibitors: the importance of a 2,4-substituted resorcinol moiety. Bioorg. Med. Chem. 2005, 13, 433-441.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 433-441
    • Khatib, S.1    Nerya, O.2    Musa, R.3    Shmuel, M.4    Tamir, S.5    Vaya, J.6
  • 66
    • 33846933805 scopus 로고    scopus 로고
    • Synthesis and evalution of 2′,4′,6′-trihydroxychalcones as a new class of tyrosine inhibitors
    • Jun, N.; Hong, G.; Jun, K. Synthesis and evalution of 2′,4′,6′-trihydroxychalcones as a new class of tyrosine inhibitors. Bioorg. Med. Chem. 2007, 15, 2396-2402.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 2396-2402
    • Jun, N.1    Hong, G.2    Jun, K.3
  • 67
  • 68
    • 34250205541 scopus 로고    scopus 로고
    • Enhanced substituted resorcinol hydrophobicity augments tyrosinase inhibition potency
    • Khatib, S.; Nerya, O.; Musa, R.; Tamir, S.; Peter, T.; Vaya, J. Enhanced substituted resorcinol hydrophobicity augments tyrosinase inhibition potency. J. Med. Chem. 2007, 50, 2676-2681.
    • (2007) J. Med. Chem. , vol.50 , pp. 2676-2681
    • Khatib, S.1    Nerya, O.2    Musa, R.3    Tamir, S.4    Peter, T.5    Vaya, J.6
  • 69
    • 0037013315 scopus 로고    scopus 로고
    • Oxyresveratrol and hydroxystilbene compounds. Inhibitory effect on tyrosinase and mechanism of action
    • Kim, Y.M.; Yun, J.; Lee, C.K.; Lee, H.; Min, K.R.; Kim, Y. Oxyresveratrol and hydroxystilbene compounds. Inhibitory effect on tyrosinase and mechanism of action. J. Biol. Chem. 2002, 277, 16340-16344.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16340-16344
    • Kim, Y.M.1    Yun, J.2    Lee, C.K.3    Lee, H.4    Min, K.R.5    Kim, Y.6
  • 70
    • 0141940128 scopus 로고    scopus 로고
    • A new stilbene with tyrosinase inhibitory activity form Chlorophora excelsa
    • Kuniyoshi, S.; Seiji, Y.; Ryuichiro, K. A new stilbene with tyrosinase inhibitory activity form Chlorophora excelsa. Chem. Pharm. Bull. 2003, 51, 318-319.
    • (2003) Chem. Pharm. Bull. , vol.51 , pp. 318-319
    • Kuniyoshi, S.1    Seiji, Y.2    Ryuichiro, K.3
  • 72
    • 36148983487 scopus 로고    scopus 로고
    • Piceatannol inhibits melanogenesis by its antioxidative actions
    • Yokozawa, T.; Kim, Y.J. Piceatannol inhibits melanogenesis by its antioxidative actions. Biol. Pharm. Bull. 2007, 30, 2007-2011.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 2007-2011
    • Yokozawa, T.1    Kim, Y.J.2
  • 74
    • 33644890708 scopus 로고    scopus 로고
    • Inhibitory effects of cis- And trans-isomers of 3,5-dihydroxystilbene on the activity of mushroom tyrosinase
    • Song, K.K.; Huang, H.; Han, P.; Zhang, C.L.; Shi, Y.; Chen, Q.X. Inhibitory effects of cis- and trans-isomers of 3,5-dihydroxystilbene on the activity of mushroom tyrosinase. Biochem. Biophys. Res. Commun. 2006, 342, 1147-1151.
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 1147-1151
    • Song, K.K.1    Huang, H.2    Han, P.3    Zhang, C.L.4    Shi, Y.5    Chen, Q.X.6
  • 75
    • 33748766664 scopus 로고    scopus 로고
    • Chemical transformations of oxyresveratrol (trans-2,4,3′,5′- tetrahydroxystilbene) into a potent tyrosinase inhibitor and a strong cytotoxic agent
    • Likhitwitayawuid, K.; Sornsute, A.; Sritularak, B.; Ploypradith, P. Chemical transformations of oxyresveratrol (trans-2,4,3′,5′- tetrahydroxystilbene) into a potent tyrosinase inhibitor and a strong cytotoxic agent. Bioorg. Med. Chem. Lett. 2006, 16, 5650-5653.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 5650-5653
    • Likhitwitayawuid, K.1    Sornsute, A.2    Sritularak, B.3    Ploypradith, P.4
  • 76
    • 52049096125 scopus 로고    scopus 로고
    • Molecular design of potent tyrosinase inhibitors having the bibenzyl skeleton
    • Oozeki, H.; Tajima, R.; Nihei, K. Molecular design of potent tyrosinase inhibitors having the bibenzyl skeleton. Bioorg. Med. Chem. Lett. 2008, 18, 5252-5254.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5252-5254
    • Oozeki, H.1    Tajima, R.2    Nihei, K.3
  • 78
    • 33846070701 scopus 로고    scopus 로고
    • Syntheses of hydroxy substituted 2-phenyl-naphthalenes as inhibitors of tyrosinase
    • Song, S.; Lee, H.; Jin, Y.; Ha, Y.M.; Bae, S.; Chung, H.Y.; Suh, H. Syntheses of hydroxy substituted 2-phenyl-naphthalenes as inhibitors of tyrosinase. Bioorg. Med. Chem. Lett. 2007, 17, 461-464.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 461-464
    • Song, S.1    Lee, H.2    Jin, Y.3    Ha, Y.M.4    Bae, S.5    Chung, H.Y.6    Suh, H.7
  • 79
    • 34548635092 scopus 로고    scopus 로고
    • 4-(6-Hydroxy-2-naphthyl)-1,3-bezendiol: A potent, new tyrosinase inhibitor
    • Ha, Y.M.; Chung, S.W.; Song, S.; Lee, H.; Suh, H.; Chung, H.Y. 4-(6-Hydroxy-2-naphthyl)-1,3-bezendiol: a potent, new tyrosinase inhibitor. Biol. Pharm. Bull. 2007, 30, 1711-1715.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 1711-1715
    • Ha, Y.M.1    Chung, S.W.2    Song, S.3    Lee, H.4    Suh, H.5    Chung, H.Y.6
  • 80
    • 0036783677 scopus 로고    scopus 로고
    • Modulation of melanogenesis by aloesin: A competitive inhibitor of tyrosinase
    • Jones, K.; Hughes, J.; Hong, M.; Jia, Q.; Orndorff, S. Modulation of melanogenesis by aloesin: a competitive inhibitor of tyrosinase. Pigment Cell Res. 2002, 15, 335-340.
    • (2002) Pigment Cell Res. , vol.15 , pp. 335-340
    • Jones, K.1    Hughes, J.2    Hong, M.3    Jia, Q.4    Orndorff, S.5
  • 83
    • 57349084222 scopus 로고    scopus 로고
    • Umbelliferone and esculetin: Inhibitors or substrates for polyphenol oxidases?
    • Sollai, F.; Zucca, P.; Sanjust, E.; Steri, D.; Resciqno, A. Umbelliferone and esculetin: inhibitors or substrates for polyphenol oxidases? Biol. Pharm. Bull. 2008, 31, 2187-2193.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 2187-2193
    • Sollai, F.1    Zucca, P.2    Sanjust, E.3    Steri, D.4    Resciqno, A.5
  • 84
    • 16644381707 scopus 로고    scopus 로고
    • Tyrosinase-inhibitory furanocoumarin from Angelica dahurica
    • Piao, X.L.; Baek, S.H.; Park, M.K.; Park, J.H. Tyrosinase-inhibitory furanocoumarin from Angelica dahurica. Biol. Pharm. Bull. 2004, 27, 1144-1146.
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 1144-1146
    • Piao, X.L.1    Baek, S.H.2    Park, M.K.3    Park, J.H.4
  • 85
    • 17444421649 scopus 로고    scopus 로고
    • Tyrosinase inhibitors from Rhododendron collettianum and their structure-activity relationship (SAR) studies
    • Ahmad, V.U.; Ullah, F.; Hussain, J.; Farooq, U.; Zubair, M.; Khan, M.T.; Choudhary, M.I. Tyrosinase inhibitors from Rhododendron collettianum and their structure-activity relationship (SAR) studies. Chem. Pharm. Bull. 2004, 52, 1458-1461.
    • (2004) Chem. Pharm. Bull. , vol.52 , pp. 1458-1461
    • Ahmad, V.U.1    Ullah, F.2    Hussain, J.3    Farooq, U.4    Zubair, M.5    Khan, M.T.6    Choudhary, M.I.7
  • 86
    • 0037070326 scopus 로고    scopus 로고
    • Tyrosinase inhibitors of Pulsatilla cernua root-derived materials
    • Lee, H.S. Tyrosinase inhibitors of Pulsatilla cernua root-derived materials. J. Agric. Food Chem. 2002, 50, 1400-1403.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 1400-1403
    • Lee, H.S.1
  • 88
    • 0032983350 scopus 로고    scopus 로고
    • 2-Hydroxy-4-methoxybenzaldehyde: A potent tyrosinase inhibitor from African medicinal plants
    • Kubo, I.; Kinst-Hori, I. 2-Hydroxy-4-methoxy benzaldehyde: a potent tyrosinase inhibitor from African medicinal plants. Planta Med. 1999, 65, 19-22. (Pubitemid 29077422)
    • (1999) Planta Medica , vol.65 , Issue.1 , pp. 19-22
    • Kubo, I.1    Kinst-Hori, I.2
  • 89
    • 0032771906 scopus 로고    scopus 로고
    • Tyrosinase inhibitory p-coumaric acid from ginseng leaves
    • Lim, J.Y.; Ishiguro, K.; Kubo, I. Tyrosinase inhibitory p-coumaric acid from ginseng leaves. Phytother. Res. 1999, 13, 371-375.
    • (1999) Phytother. Res. , vol.13 , pp. 371-375
    • Lim, J.Y.1    Ishiguro, K.2    Kubo, I.3
  • 90
    • 3242797244 scopus 로고    scopus 로고
    • In vitro antioxidative effects and tyrosinase inhibitory activities of seven hydroxycinnamoyl derivatives in green coffee beans
    • Iwai, K.; Kishimoto, N.; Kakino, Y.; Mochida, K.; Fujita, T. In vitro antioxidative effects and tyrosinase inhibitory activities of seven hydroxycinnamoyl derivatives in green coffee beans. J. Agric. Food Chem. 2004, 52, 4893-4898.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4893-4898
    • Iwai, K.1    Kishimoto, N.2    Kakino, Y.3    Mochida, K.4    Fujita, T.5
  • 92
    • 0001397165 scopus 로고    scopus 로고
    • Tyrosinase inhibitors from cumin
    • Kubo, I.; Kinst-Hori, I. Tyrosinase inhibitors from cumin. J. Agric. Food Chem. 1998, 46, 5338-5341.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 5338-5341
    • Kubo, I.1    Kinst-Hori, I.2
  • 93
    • 0033230675 scopus 로고    scopus 로고
    • Tyrosinase inhibitory activity of the olive oil flavor compounds
    • Kubo, I.; Kinst-Hori, I. Tyrosinase inhibitory activity of the olive oil flavor compounds. J. Agric. Food Chem. 1999, 47, 4574-4578.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4574-4578
    • Kubo, I.1    Kinst-Hori, I.2
  • 94
    • 0028176278 scopus 로고
    • Inhibitor binding to the binuclear active site of tyrosinase: Temperature, pH, and solvent deuterium isotope effects
    • DOI 10.1021/bi00185a010
    • Conrad, J.S.; Dawso, S.R.; Hubbard, E.R.; Meyers, T.E.; Strothkamp, K.G. Inhibitor binding to the binuclear active site of tyrosinase: temperature, pH and solvent deuterium isotope effects. Biochemistry 1994, 33, 5739-5744. (Pubitemid 24184575)
    • (1994) Biochemistry , vol.33 , Issue.19 , pp. 5739-5744
    • Conrad, J.S.1    Dawso, S.R.2    Hubbard, E.R.3    Meyers, T.E.4    Strothkamp, K.G.5
  • 97
    • 26444558025 scopus 로고    scopus 로고
    • Inhibitory effects of salicylic acid family compounds on the diphenolase activity of mushroom tyrosinase
    • DOI 10.1016/j.foodchem.2005.01.042, PII S030881460500124X
    • Zhang, J.P.; Chen, Q.X.; Song, K.K.; Xie, J.J. Inhibitory effects of salicylic acid family compounds on the diphenolase activity of mushroom tyrosinase. Food Chem. 2006, 95, 579-584. (Pubitemid 41436428)
    • (2006) Food Chemistry , vol.95 , Issue.4 , pp. 579-584
    • Zhang, J.-P.1    Chen, Q.-X.2    Song, K.-K.3    Xie, J.-J.4
  • 98
    • 34547758423 scopus 로고    scopus 로고
    • Functional interaction of diphenols with polyphenol oxidase. Molecular determinants of substrate/inhibitor specificity
    • Kanade, S.R.; Suhas, V.L.; Chandra, N.; Gowda, L.R. Functional interaction of diphenols with polyphenol oxidase. Molecular determinants of substrate/inhibitor specificity. FEBS J. 2007, 274, 4177-4187.
    • (2007) FEBS J. , vol.274 , pp. 4177-4187
    • Kanade, S.R.1    Suhas, V.L.2    Chandra, N.3    Gowda, L.R.4
  • 99
    • 36148935223 scopus 로고    scopus 로고
    • Tyrosinase inhibitory activity of ethanol extracts from medicinal and edible plants cultivated in Okinawa and identification of a water-soluble inhibitor from the leaves of Nandina domestica
    • DOI 10.1271/bbb.70249
    • Masuda, T.; Fujita, N.; Odaka, Y.; Takeda, Y.; Yonemori, S.; Nakamoto, K.; Kuninaga, H. Tyrosinase inhibitory activity of ethanol extracts from medicinal and edible plants cultivated in okinawa and identification of a water-soluble inhibitor from the leaves of Nandina domestica. Biosci. Biotechnol., Biochem. 2007, 71, 2316-2320. (Pubitemid 350113094)
    • (2007) Bioscience, Biotechnology and Biochemistry , vol.71 , Issue.9 , pp. 2316-2320
    • Masuda, T.1    Fujita, N.2    Odaka, Y.3    Takeda, Y.4    Yonemori, S.5    Nakamoto, K.6    Kuninaga, H.7
  • 100
    • 16644381151 scopus 로고    scopus 로고
    • A sphingolipid and tyrosinase inhibitors from the fruiting body of Phellinus linteus
    • Kang, H.S.; Choi, J.H.; Cho, W.K.; Park, J.C.; Choi, J.S. A sphingolipid and tyrosinase inhibitors from the fruiting body of Phellinus linteus. Arch. Pharm. Res. 2004, 27, 742-750.
    • (2004) Arch. Pharm. Res. , vol.27 , pp. 742-750
    • Kang, H.S.1    Choi, J.H.2    Cho, W.K.3    Park, J.C.4    Choi, J.S.5
  • 102
    • 22544467498 scopus 로고    scopus 로고
    • Inhibitory effects of 4-vinylbenzaldehyde and 4-vinylbenzoic acid on the activity of mushroom tyrosinase
    • Song, K.K.; Chen, Q.X.; Wang, Q.; Qiu, L.; Huang, H. Inhibitory effects of 4-vinylbenzaldehyde and 4-vinylbenzoic acid on the activity of mushroom tyrosinase. J. Enzyme Inhib. Med. Chem. 2005, 20, 239-243.
    • (2005) J. Enzyme Inhib. Med. Chem. , vol.20 , pp. 239-243
    • Song, K.K.1    Chen, Q.X.2    Wang, Q.3    Qiu, L.4    Huang, H.5
  • 103
    • 47249118378 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship studies of mushroom tyrosinase inhibitors
    • Xue, C.B.; Luo, W.C.; Ding, Q.; Liu, S.Z.; Gao, X.X. Quantitative structure-activity relationship studies of mushroom tyrosinase inhibitors. J. Comput. Aided. Mol. Des. 2008, 22, 299-309.
    • (2008) J. Comput. Aided. Mol. Des. , vol.22 , pp. 299-309
    • Xue, C.B.1    Luo, W.C.2    Ding, Q.3    Liu, S.Z.4    Gao, X.X.5
  • 104
    • 0344307448 scopus 로고    scopus 로고
    • Inhibitory effects on mushroom tyrosinase by some alkylbenzaldehydes
    • Chen, Q.X.; Song, K.K.; Wang, Q.; Huang, H. Inhibitory effects on mushroom tyrosinase by some alkylbenzaldehydes. J. Enzyme Inhib. Med. Chem. 2003, 18, 491-496.
    • (2003) J. Enzyme Inhib. Med. Chem. , vol.18 , pp. 491-496
    • Chen, Q.X.1    Song, K.K.2    Wang, Q.3    Huang, H.4
  • 105
    • 1642575094 scopus 로고    scopus 로고
    • 2-Hydroxy-4-isopropylbenzaldehyde, a potent partial tyrosinase inhibitor
    • Nihei, K.; Yamagiwa, Y.; Kamikawa, T.; Kubo, I. 2-Hydroxy-4- isopropylbenzaldehyde, a potent partial tyrosinase inhibitor. Bioorg. Med. Chem. Lett. 2004, 14, 681-683.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 681-683
    • Nihei, K.1    Yamagiwa, Y.2    Kamikawa, T.3    Kubo, I.4
  • 106
    • 0034957357 scopus 로고    scopus 로고
    • Hydroxy- Or methoxy-substituted benzaldoximes and benzaldehyde-O- alkyloximes as tyrosinase inhibitors
    • Lev, J.P.; Bertram, H.J. Hydroxy- or methoxy-substituted benzaldoximes and benzaldehyde-O-alkyloximes as tyrosinase inhibitors. Bioorg. Med. Chem. 2001, 9, 1879-1885.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 1879-1885
    • Lev, J.P.1    Bertram, H.J.2
  • 107
    • 33846648506 scopus 로고    scopus 로고
    • 3D-QSAR and molecular docking studites of benzaldehyde thiosemicarbazone, benzaldehyde, benzoic acid, and their derivatives as phenoloxidase inhibitors
    • Xue, C.B.; Zhang, L.; Luo, W.C.; Xie, X.Y.; Jiang, L.; Xiao, T. 3D-QSAR and molecular docking studites of benzaldehyde thiosemicarbazone, benzaldehyde, benzoic acid, and their derivatives as phenoloxidase inhibitors. Bioorg. Med. Chem. 2007, 15, 2006-2015.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 2006-2015
    • Xue, C.B.1    Zhang, L.2    Luo, W.C.3    Xie, X.Y.4    Jiang, L.5    Xiao, T.6
  • 110
    • 0037402359 scopus 로고    scopus 로고
    • Molecular design of antibrowning agents: Antioxidative tyrosinase inhibitors
    • DOI 10.1016/S0308-8146(02)00418-1, PII S0308814602004181
    • Kubo, I.; Chen, Q.X.; Nihei, K. Molecular design of antibrowning agents: antioxidative tyrosinase inhibitors. Food Chem. 2003, 81, 241-247. (Pubitemid 36411728)
    • (2003) Food Chemistry , vol.81 , Issue.2 , pp. 241-247
    • Kubo, I.1    Chen, Q.-X.2    Nihei, K.-I.3
  • 111
    • 2142856722 scopus 로고    scopus 로고
    • Depigmenting activity and low cytotoxicity of alkoxy benzoates or alkoxy cinnamte in cultured melanocytes
    • Kang, H.H.; Rho, H.S.; Hwang, J.S.; Oh, S.G. Depigmenting activity and low cytotoxicity of alkoxy benzoates or alkoxy cinnamte in cultured melanocytes. Chem. Pharm. Bull. 2003, 51, 1085-1088.
    • (2003) Chem. Pharm. Bull. , vol.51 , pp. 1085-1088
    • Kang, H.H.1    Rho, H.S.2    Hwang, J.S.3    Oh, S.G.4
  • 112
    • 59149085366 scopus 로고    scopus 로고
    • Molecular docking studies and anti-tyrosinase activity of Thai mango seed kernel extract
    • Nithitanakool, S.; Pithayanukul, P.; Bavovada, R.; Saparpakorn, P. Molecular docking studies and anti-tyrosinase activity of Thai mango seed kernel extract. Molecules 2009, 14, 257-265.
    • (2009) Molecules , vol.14 , pp. 257-265
    • Nithitanakool, S.1    Pithayanukul, P.2    Bavovada, R.3    Saparpakorn, P.4
  • 115
    • 84895195113 scopus 로고    scopus 로고
    • Tyrosinase inhibitors isolated from the roots of Paeonia suffruticosa
    • In press
    • Ding, H.Y.; Lin, H.C.; Chang, T.S. Tyrosinase inhibitors isolated from the roots of Paeonia suffruticosa. J. Cosmet. Sci. In press.
    • J. Cosmet. Sci.
    • Ding, H.Y.1    Lin, H.C.2    Chang, T.S.3
  • 117
    • 39149123777 scopus 로고    scopus 로고
    • Tyrosinase inhibitors and sesquiterpene diglycosides from Guioa villosa
    • DOI 10.1055/s-2007-993780
    • Maqid, A.A.; Voutquenne-Nazabadioko, L.; Bontemps, G.; Litaudon, M.; Lavaud, C. Tyrosinase inhibitors and sesquiterpene diglycosides from Guioa villosa. Planta Med. 2008, 74, 55-60. (Pubitemid 351251384)
    • (2008) Planta Medica , vol.74 , Issue.1 , pp. 55-60
    • Magid, A.A.1    Voutquenne-Nazabadioko, L.2    Bontemps, G.3    Litaudon, M.4    Lavaud, C.5
  • 118
    • 38949129695 scopus 로고    scopus 로고
    • Identification of geranic acid, a tyrosinase inhibitor in lemongrass (Cymbopogon citratus)
    • DOI 10.1021/jf072893l
    • Masuda, T.; Odaka, Y.; Oqawa, N.; Nakamoto, K.; Kuninaqa, H. Identification of geranic acid, a tyrosinase inhibitor in lemongrass (Cymbopogon citratus). J. Agric. Food Chem. 2008, 56, 597-601. (Pubitemid 351212591)
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.2 , pp. 597-601
    • Masuda, T.1    Odaka, Y.2    Ogawa, N.3    Nakamoto, K.4    Kuninaga, H.5
  • 119
  • 121
    • 30344474608 scopus 로고    scopus 로고
    • Tyrosinase inhibitory cycloartane type triterpenoids from the methanol extract of the whole plant of Amberboa ramosa Jafri and their structure-activity relationship
    • Khan, M.T.; Khan, S.B.; Ather, A. Tyrosinase inhibitory cycloartane type triterpenoids from the methanol extract of the whole plant of Amberboa ramosa Jafri and their structure-activity relationship. Bioorg. Med. Chem. 2006, 14, 938-943.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 938-943
    • Khan, M.T.1    Khan, S.B.2    Ather, A.3
  • 123
    • 36549027860 scopus 로고    scopus 로고
    • Tyrosinase inhibitory pentacyclic triterpenes and analgesic and spasmolytic activities of methanol extracts of Rhododendron collettianum
    • Ullah, F.; Hussain, H.; Hussain, J.; Bukhari, I.A.; Khan, M.T.; Choudhary, M.I.; Gilani, A.H.; Ahmad, V.U. Tyrosinase inhibitory pentacyclic triterpenes and analgesic and spasmolytic activities of methanol extracts of Rhododendron collettianum. Phytother. Res. 2007, 21, 1076-1081.
    • (2007) Phytother. Res. , vol.21 , pp. 1076-1081
    • Ullah, F.1    Hussain, H.2    Hussain, J.3    Bukhari, I.A.4    Khan, M.T.5    Choudhary, M.I.6    Gilani, A.H.7    Ahmad, V.U.8
  • 124
    • 17444431916 scopus 로고    scopus 로고
    • Atta-ur-Rahman. Alkaloids of Aconitum laeve and their anti-inflammatory antioxidant and tyrosinase inhibition activities
    • Shaheen, F.; Ahmad, M.; Khan, M.T.; Jalil, S.; Ejaz, A.; Sultankhodjaev, M.N.; Arfan, M.; Choudhary, M.I.; Atta-ur-Rahman. Alkaloids of Aconitum laeve and their anti-inflammatory antioxidant and tyrosinase inhibition activities. Phtochemistry 2005, 66, 935-940.
    • (2005) Phtochemistry , vol.66 , pp. 935-940
    • Shaheen, F.1    Ahmad, M.2    Khan, M.T.3    Jalil, S.4    Ejaz, A.5    Sultankhodjaev, M.N.6    Arfan, M.7    Choudhary, M.I.8
  • 125
    • 20144363745 scopus 로고    scopus 로고
    • Tyrosinase inhibition studies of diterpenoid alkaloids and their derivatives: Structure-activity relationships
    • Sultankhodzhaev, M.N.; Khan, M.T.; Moin, M.; Choudhary, M.I.; Atta-ur-Rahman. Tyrosinase inhibition studies of diterpenoid alkaloids and their derivatives: structure-activity relationships. Nat. Prod. Res. 2005, 19, 517-522.
    • (2005) Nat. Prod. Res. , vol.19 , pp. 517-522
    • Sultankhodzhaev, M.N.1    Khan, M.T.2    Moin, M.3    Choudhary, M.I.4    Atta-ur-Rahman5
  • 126
    • 1642424273 scopus 로고    scopus 로고
    • Antityrosinase principles and constituents of the petals of Crocus sativus
    • Li, C.Y.; Lee, E.J.; Wu, T.S. Antityrosinase principles and constituents of the petals of Crocus sativus. J. Nat. Prod. 2004, 67, 437-440.
    • (2004) J. Nat. Prod. , vol.67 , pp. 437-440
    • Li, C.Y.1    Lee, E.J.2    Wu, T.S.3
  • 127
    • 52149084387 scopus 로고    scopus 로고
    • New tyrosinase inhibitory sesquiterpenes from Chloranthus henryi
    • Wu, B.; He, S.; Wu, X.D.; Pan, Y.J. New tyrosinase inhibitory sesquiterpenes from Chloranthus henryi. Chem. Biodivers. 2008, 5, 1298-1303.
    • (2008) Chem. Biodivers. , vol.5 , pp. 1298-1303
    • Wu, B.1    He, S.2    Wu, X.D.3    Pan, Y.J.4
  • 128
    • 45249085705 scopus 로고    scopus 로고
    • Complex sesquiterpenoids with tyrosinase inhibitory activity from the leaves of Chloranthus tianmushanensis
    • Wu, B.; Chen, J.; Qu, H.; Cheng, Y. Complex sesquiterpenoids with tyrosinase inhibitory activity from the leaves of Chloranthus tianmushanensis. J. Nat. Prod. 2008, 75, 877-880.
    • (2008) J. Nat. Prod. , vol.75 , pp. 877-880
    • Wu, B.1    Chen, J.2    Qu, H.3    Cheng, Y.4
  • 129
    • 24944498881 scopus 로고    scopus 로고
    • Microbial transformation of 17alpha-ethynyl- And 17alpha-ethylsteroids, and tyrosinase inhibitory activity of transformed products
    • Choudhary, M.I.; Sultan, S.; Khan, M.T.; Atta-ur-Rahman. Microbial transformation of 17alpha-ethynyl- and 17alpha-ethylsteroids, and tyrosinase inhibitory activity of transformed products. Steroids 2005, 70, 798-802.
    • (2005) Steroids , vol.70 , pp. 798-802
    • Choudhary, M.I.1    Sultan, S.2    Khan, M.T.3    Atta-ur-Rahman4
  • 130
    • 42949111608 scopus 로고    scopus 로고
    • Anthraquinones from Polygonum cuspidatum as tyrosinase inhibitors for dermal use
    • Leu, Y.L.; Hwang, T.L.; Hu, J.W.; Fang, J.Y. Anthraquinones from Polygonum cuspidatum as tyrosinase inhibitors for dermal use. Phytother. Res. 2008, 22, 552-556.
    • (2008) Phytother. Res. , vol.22 , pp. 552-556
    • Leu, Y.L.1    Hwang, T.L.2    Hu, J.W.3    Fang, J.Y.4
  • 131
    • 34248356669 scopus 로고    scopus 로고
    • Tyrosinase inhibitory and antileishmanial constituents from the rhizomes of Paris polyphylla
    • Devkota, K.P.; Khan, M.T.; Ranjit, R.; Lannang, A.M.; Samreen; Choudhary, M.I. Tyrosinase inhibitory and antileishmanial constituents from the rhizomes of Paris polyphylla. Nat. Prod. Res. 2007, 21, 321-327.
    • (2007) Nat. Prod. Res. , vol.21 , pp. 321-327
    • Devkota, K.P.1    Khan, M.T.2    Ranjit, R.3    Lannang, A.M.4    Samreen5    Choudhary, M.I.6
  • 132
    • 32844456498 scopus 로고    scopus 로고
    • Tyrosinase inhibitory lignans from the methanol extract of the roots of Vitex negundo Linn. and their structure-activity relationship
    • DOI 10.1016/j.phymed.2004.09.001, PII S0944711305001212
    • Azhar-Ul-Haq; Malik, A.; Khan, M.T.; Anwar-Ul-Haq; Khan, S.B.; Ahmad, A.; Choudhary, M.I. Tyrosinase inhibitory lignans from the methanol extract of the roots of Vitex negundo Linn. and their structure-activity relationship. Phytomedicine 2006, 13, 255-260. (Pubitemid 43255325)
    • (2006) Phytomedicine , vol.13 , Issue.4 , pp. 255-260
    • Azhar-Ul-Haq1    Malik, A.2    Khan, M.T.H.3    Anwar-Ul-Haq4    Khan, S.B.5    Ahmad, A.6    Choudhary, M.I.7
  • 133
    • 13744255495 scopus 로고    scopus 로고
    • Tyrosinase inhibitors isolated from the edible brown alga Ecklonia stolonifera
    • Kang, H.S.; Kim, H.R.; Byun, D.S.; Son, B.W.; Nam, T.J.; Choi, J.S. Tyrosinase inhibitors isolated from the edible brown alga Ecklonia stolonifera. Arch. Pham. Res. 2004, 27, 1226-1232.
    • (2004) Arch. Pham. Res. , vol.27 , pp. 1226-1232
    • Kang, H.S.1    Kim, H.R.2    Byun, D.S.3    Son, B.W.4    Nam, T.J.5    Choi, J.S.6
  • 134
    • 21144434818 scopus 로고    scopus 로고
    • Myrothenones a and B, cyclopentenone derivatives with tyrosinase inhibitory activity from the marine-derived fungus Myrothecium sp
    • Li, X.; Kim, M.K.; Lee, U.; Kim, S.K.; Kang, J.S.; Choi, H.D.; Son, B.W. Myrothenones A and B, cyclopentenone derivatives with tyrosinase inhibitory activity from the marine-derived fungus Myrothecium sp. Chem. Pharm. Bull. 2005, 53, 453-455.
    • (2005) Chem. Pharm. Bull. , vol.53 , pp. 453-455
    • Li, X.1    Kim, M.K.2    Lee, U.3    Kim, S.K.4    Kang, J.S.5    Choi, H.D.6    Son, B.W.7
  • 135
    • 48849102560 scopus 로고    scopus 로고
    • Purification and determination of the chemical structure of the tyrosinase inhibitor produced by Trichoderma viride strain H1-7 from a marine environment
    • Tsuchiya, T.; Yamada, K.; Minoura, K.; Miyamoto, K.; Usami ,Y.; Kobayashi, T.; Hamada-Sato, N.; Imada, C.; Tsujibo, H. Purification and determination of the chemical structure of the tyrosinase inhibitor produced by Trichoderma viride strain H1-7 from a marine environment. Biol. Pharm. Bull. 2008, 31, 1618-1620.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 1618-1620
    • Tsuchiya, T.1    Yamada, K.2    Minoura, K.3    Miyamoto, K.4    Usami, Y.5    Kobayashi, T.6    Hamada-Sato, N.7    Imada, C.8    Tsujibo, H.9
  • 136
    • 0036009142 scopus 로고    scopus 로고
    • The crystal structure of catechol oxidase: New insight into the function of type-3 copper proteins
    • Gerdemann, C.; Eicken, C.; Krebs, B. The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins. Acc. Chem. Res. 2002, 35, 183-191.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 183-191
    • Gerdemann, C.1    Eicken, C.2    Krebs, B.3
  • 137
    • 44649198318 scopus 로고    scopus 로고
    • Analogues of N-hydroxy-N′-phenylthiourea and N-hydroxy-N′- phenylurea as inhibitors of tyrosinase and melanin formation
    • Criton, M.; Le Mellay-Hamon V. Analogues of N-hydroxy-N′- phenylthiourea and N-hydroxy-N′-phenylurea as inhibitors of tyrosinase and melanin formation. Bioorg. Med. Chem. Lett. 2008, 18, 3607-3610.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 3607-3610
    • Criton, M.1    Le Mellay-Hamon, V.2
  • 138
    • 60749098532 scopus 로고    scopus 로고
    • Phenylethylamide and phenylmethylamide derivatives as new tyrosinase inhibitors
    • Le Mellay-Hamon V.; Criton, M. Phenylethylamide and phenylmethylamide derivatives as new tyrosinase inhibitors. Biol. Pharm. Bull. 2009, 32, 301-303.
    • (2009) Biol. Pharm. Bull. , vol.32 , pp. 301-303
    • Le Mellay-Hamon, V.1    Criton, M.2
  • 139
    • 57749084378 scopus 로고    scopus 로고
    • Synthesis of tyrosinase inhibitory (4-oxo-4H-pyran-2-yl)acrylic acid ester derivatives
    • Kang, S.S.; Kim, H.J.; Jin, C.; Lee, Y.S. Synthesis of tyrosinase inhibitory (4-oxo-4H-pyran-2-yl)acrylic acid ester derivatives. Bioorg. Med. Chem. Lett. 2009, 19, 188-191.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 188-191
    • Kang, S.S.1    Kim, H.J.2    Jin, C.3    Lee, Y.S.4
  • 140
    • 0142092755 scopus 로고    scopus 로고
    • Inhibitory effects of cupferron on the monophenolase and diphenolase activity of mushroom tyrosinase
    • Xie, L.P.; Chen, Q.X.; Huang, H.; Liu, X.D.; Chen, H.T.; Zhang, R.Q. Inhibitory effects of cupferron on the monophenolase and diphenolase activity of mushroom tyrosinase. Int. J. Biochem. Cell Biol. 2003, 35, 1658-1666.
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 1658-1666
    • Xie, L.P.1    Chen, Q.X.2    Huang, H.3    Liu, X.D.4    Chen, H.T.5    Zhang, R.Q.6
  • 141
    • 0034997903 scopus 로고    scopus 로고
    • Synthesis of N-substituted N-nitrosohydroxylamines as inhibitors of mushroom tyrosinase
    • Shiino, M.; Watanabe, Y.; Umezawa, K. Synthesis of N-substituted N-nitrosohydroxylamines as inhibitors of mushroom tyrosinase. Bioorg. Med. Chem. 2001, 9, 1233-1240.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 1233-1240
    • Shiino, M.1    Watanabe, Y.2    Umezawa, K.3
  • 142
    • 0037394181 scopus 로고    scopus 로고
    • Synthesis of tyrosinase inhibitory activity of novel N-hydroxybenzyl-N- nitrosohydroxylamines
    • Shiino, M.; Watanabe, Y.; Umezawa, K. Synthesis of tyrosinase inhibitory activity of novel N-hydroxybenzyl-N-nitrosohydroxylamines. Bioorg. Chem. 2003, 31, 129-135.
    • (2003) Bioorg. Chem. , vol.31 , pp. 129-135
    • Shiino, M.1    Watanabe, Y.2    Umezawa, K.3
  • 143
    • 39349085018 scopus 로고    scopus 로고
    • pH-dependent inhibition of mushroom tyrosinase by N-substituted N-nitrosohydroxylamines
    • Shiino, M.; Watanabe,Y.; Umezawa, K. pH-dependent inhibition of mushroom tyrosinase by N-substituted N-nitrosohydroxylamines. J. Enzyme Inhib. Med. Chem. 2008, 23, 16-20.
    • (2008) J. Enzyme Inhib. Med. Chem. , vol.23 , pp. 16-20
    • Shiino, M.1    Watanabe, Y.2    Umezawa, K.3
  • 145
    • 17444374605 scopus 로고    scopus 로고
    • Structure-activity relationships of tyrosinase inhibitory combinatorial library of 2,5-disubstituted-1,3,4-oxadiazole analogues
    • Khan, M.T.; Choudhary, M.I.; Khan, K.M.; Rani, M.; Atta-ur-Rahman. Structure-activity relationships of tyrosinase inhibitory combinatorial library of 2,5-disubstituted-1,3,4-oxadiazole analogues. Bioorg. Med. Chem. 2005, 13, 3385-3395.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 3385-3395
    • Khan, M.T.1    Choudhary, M.I.2    Khan, K.M.3    Rani, M.4    Atta-ur-Rahman5
  • 146
    • 33746031797 scopus 로고    scopus 로고
    • Oxazolones: New tyrosinase inhibitors; synthesis and their structure-activity relationships
    • Khan, K.M.; Mughal, U.R.; Khan, M.T.; Zia-Ullah; Perveen, S.; Choudhary, M.I. Oxazolones: new tyrosinase inhibitors; synthesis and their structure-activity relationships. Bioorg. Med. Chem. 2006, 14, 6027-6033.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 6027-6033
    • Khan, K.M.1    Mughal, U.R.2    Khan, M.T.3    Zia-Ullah4    Perveen, S.5    Choudhary, M.I.6
  • 148
    • 1842865269 scopus 로고    scopus 로고
    • Inhibitory effects of 1,3-selenazol-4-one derivatives on mushroom tyrosinase
    • Koketsu, M.; Choi, S.Y.; Ishihara, H.; Lim, B.O.; Kim, H.; Kim, S.Y. Inhibitory effects of 1,3-selenazol-4-one derivatives on mushroom tyrosinase. Chem. Pharm. Bull. 2002, 50, 1594-1596.
    • (2002) Chem. Pharm. Bull. , vol.50 , pp. 1594-1596
    • Koketsu, M.1    Choi, S.Y.2    Ishihara, H.3    Lim, B.O.4    Kim, H.5    Kim, S.Y.6
  • 151
    • 19444376688 scopus 로고    scopus 로고
    • 4,4'-Dihydroxybiphenyl as a new potent tyrosinase inhibitor
    • Kim, Y.J.; No, J.K.; Lee, J.H.; Chung, H.Y. 4,4'-Dihydroxybiphenyl as a new potent tyrosinase inhibitor. Biol. Pharm. Bull. 2005, 28, 323-327.
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 323-327
    • Kim, Y.J.1    No, J.K.2    Lee, J.H.3    Chung, H.Y.4
  • 152
    • 33747434820 scopus 로고    scopus 로고
    • Biphenyl glycosides from the fruit of Pyracantha fortuneana
    • Dai, Y.; Zhou, G.X.; Kurihara, H.; Ye, W.C.; Yao, X.S. Biphenyl glycosides from the fruit of Pyracantha fortuneana. J. Nat. Prod. 2006, 69, 1022-1024.
    • (2006) J. Nat. Prod. , vol.69 , pp. 1022-1024
    • Dai, Y.1    Zhou, G.X.2    Kurihara, H.3    Ye, W.C.4    Yao, X.S.5
  • 153
    • 29844441290 scopus 로고    scopus 로고
    • Inhibition of melanogenic activity by 4,4′-dihydroxybiphenyl in melanoma cells
    • No, J.K.; Kim, Y.J.; Lee, J.S.; Chung, H.Y. Inhibition of melanogenic activity by 4,4′-dihydroxybiphenyl in melanoma cells. Biol. Pharm. Bull. 2006, 29, 14-16.
    • (2006) Biol. Pharm. Bull. , vol.29 , pp. 14-16
    • No, J.K.1    Kim, Y.J.2    Lee, J.S.3    Chung, H.Y.4
  • 154
    • 24944433492 scopus 로고    scopus 로고
    • Potent inhibitory effects of N-aryl S-alkylthiocarbamate derivatives on the dopa oxidase activity of mushroom tyrosinase
    • Lee, K.H.; Koketsu, M.; Choi, S.Y.; Lee, K.J.; Lee, P.; Ishihara, H.; Kim, S.Y. Potent inhibitory effects of N-aryl S-alkylthiocarbamate derivatives on the dopa oxidase activity of mushroom tyrosinase. Chem. Pharm. Bull. 2005, 53, 747-749.
    • (2005) Chem. Pharm. Bull. , vol.53 , pp. 747-749
    • Lee, K.H.1    Koketsu, M.2    Choi, S.Y.3    Lee, K.J.4    Lee, P.5    Ishihara, H.6    Kim, S.Y.7
  • 155
    • 23844534499 scopus 로고    scopus 로고
    • Isolation of a natural antioxidant, dehydrozingerone from Zingiber officinale and synthesis of its analogues for recognition of effective antioxidant and antityrosinase agents
    • Kuo, P.C.; Damu, A.G.; Cherng, C.Y.; Jeng, J.F.; Teng, C.M.; Lee, E.J.; Wu, T.S. Isolation of a natural antioxidant, dehydrozingerone from Zingiber officinale and synthesis of its analogues for recognition of effective antioxidant and antityrosinase agents. Arch. Pharm. Res. 2005, 28, 518-528.
    • (2005) Arch. Pharm. Res. , vol.28 , pp. 518-528
    • Kuo, P.C.1    Damu, A.G.2    Cherng, C.Y.3    Jeng, J.F.4    Teng, C.M.5    Lee, E.J.6    Wu, T.S.7
  • 156
    • 0023739543 scopus 로고
    • Kinetics of substrate reaction during irreversible modification of enzyme activity
    • Tsou, C.L. Kinetics of substrate reaction during irreversible modification of enzyme activity. Adv. Enzymol. Relat. Areas. Mol. Biol. 1988, 61, 381-436.
    • (1988) Adv. Enzymol. Relat. Areas. Mol. Biol. , vol.61 , pp. 381-436
    • Tsou, C.L.1
  • 157
    • 0035847062 scopus 로고    scopus 로고
    • Effect of captopril on mushroom tyrosinase activity in vitro
    • Espín, J.C.; Wichers, H.J. Effect of captopril on mushroom tyrosinase activity in vitro. Biochim. Biophys. Acta. 2001, 1544, 289-300.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 289-300
    • Espín, J.C.1    Wichers, H.J.2
  • 158
    • 0019124480 scopus 로고
    • Inactivation of dopamine?-monooxygenase by hydrogen peroxide and by ascorbate
    • Skotland, T.; Ljones, T. Inactivation of dopamine ?-monooxygenase by hydrogen peroxide and by ascorbate. Arch. Biochem. Biophys. 1980, 201, 81-87.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 81-87
    • Skotland, T.1    Ljones, T.2
  • 159
    • 0037880763 scopus 로고
    • Inactivation of mushroom tyrosinase by hydrogen peroxide
    • Andrawis, A.; Kahn, V. Inactivation of mushroom tyrosinase by hydrogen peroxide. Phytochemistry 1985, 24, 397-405.
    • (1985) Phytochemistry , vol.24 , pp. 397-405
    • Andrawis, A.1    Kahn, V.2
  • 160
    • 34548558789 scopus 로고    scopus 로고
    • A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutations
    • DOI 10.1111/j.1600-0749.2007.00405.x
    • Schweikardt, T.; Olivares, C.; Solano, F.; Jaenicke, E.; Garcia-Borron, J.C.; Decker, H. A three-dimensional model of mammalian tyrosinase active site accounting for loss of function mutations. Pigment Cell Res. 2007, 20, 394-401. (Pubitemid 47390119)
    • (2007) Pigment Cell Research , vol.20 , Issue.5 , pp. 394-401
    • Schweikardt, T.1    Olivares, C.2    Solano, F.3    Jaenicke, E.4    Garcia-Borron, J.C.5    Decker, H.6
  • 161
    • 0344307515 scopus 로고    scopus 로고
    • Inactivation Kinetics of Mushroom Tyrosinase by Cetylpyridinium Chloride
    • DOI 10.1023/B:JOPC.0000005464.36961.9c
    • Chen, Q.X.; Huang, H.; Kubo, I. Inactivation kinetics of mushroom tyrosinase by cetylpyridinium chloride. J. Protein Chem. 2003, 22, 481-487. (Pubitemid 37516778)
    • (2003) Journal of Protein Chemistry , vol.22 , Issue.5 , pp. 481-487
    • Chen, Q.-X.1    Huang, H.2    Kubo, I.3
  • 162
    • 25844438379 scopus 로고    scopus 로고
    • Irreversibly inhibitory kinetics of 3,5-dihydroxyphenyl decanoate on mushroom (Agaricus bisporus) tyrosinase
    • Qiu, L.; Chen, Q.X.; Wang, Q.; Huang, H.; Song, K.K. Irreversibly inhibitory kinetics of 3,5-dihydroxyphenyl decanoate on mushroom (Agaricus bisporus) tyrosinase. Bioorg. Med. Chem. 2005, 13, 6206-6211.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 6206-6211
    • Qiu, L.1    Chen, Q.X.2    Wang, Q.3    Huang, H.4    Song, K.K.5
  • 163
    • 34249998986 scopus 로고    scopus 로고
    • Inhibitory effect of p-hydroxybenzyl alcohol on tyrosinase activity and melanogenesis
    • Liu, S.H.; Pan, I.H.; Chu, I.M. Inhibitory effect of p-hydroxybenzyl alcohol on tyrosinase activity and melanogenesis. Biol. Pharm. Bull. 2007, 30, 1135-1139.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 1135-1139
    • Liu, S.H.1    Pan, I.H.2    Chu, I.M.3
  • 164
    • 33644925290 scopus 로고    scopus 로고
    • Hen egg white lysozyme as an inhibitor of mushroom tyrosinase
    • Li, B.; Huang, Y.; Paskewitz, S.M. Hen egg white lysozyme as an inhibitor of mushroom tyrosinase. FEBS Lett. 2006, 580, 1877-1882.
    • (2006) FEBS Lett. , vol.580 , pp. 1877-1882
    • Li, B.1    Huang, Y.2    Paskewitz, S.M.3
  • 165
    • 7744231644 scopus 로고    scopus 로고
    • Substrate share in the suicide inactivation of mushroom tyrosinase
    • Haghbeen, K.; Saboury, A.A.; Karbassi, F. Substrate share in the suicide inactivation of mushroom tyrosinase. Biochim. Biophys. Acta 2004, 1675, 139-146.
    • (2004) Biochim. Biophys. Acta , vol.1675 , pp. 139-146
    • Haghbeen, K.1    Saboury, A.A.2    Karbassi, F.3
  • 166
    • 0021875282 scopus 로고
    • Kinetics of suicide substrates. Practical procedures for determining parameters
    • Waley, S.G. Kinetics of suicide substrate: practical procedures for determining parameters. Biochem. J. 1985, 227, 843-849. (Pubitemid 15044661)
    • (1985) Biochemical Journal , vol.227 , Issue.3 , pp. 843-849
    • Waley, S.G.1
  • 168
    • 38449116139 scopus 로고    scopus 로고
    • The mechanism of suicide-inactivation of tyrosinase: A substrate structure investigation
    • Land, E.J.; Ramsden. C.A.; Riley, P.A. The mechanism of suicide-inactivation of tyrosinase: a substrate structure investigation. Tohoku J. Exp. Med. 2007, 212, 341-348.
    • (2007) Tohoku J. Exp. Med. , vol.212 , pp. 341-348
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3
  • 169
    • 59849124373 scopus 로고    scopus 로고
    • Evidence consistent with the requirement of cresolase activity for suicide inactivation of tyrosinase
    • Land, E.J.; Ramsden, C.A.; Riley, P.A.; Stratford, M.R. Evidence consistent with the requirement of cresolase activity for suicide inactivation of tyrosinase. Tohoku J. Exp. Med. 2008, 216, 231-238.
    • (2008) Tohoku J. Exp. Med. , vol.216 , pp. 231-238
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3    Stratford, M.R.4
  • 170
    • 84895144248 scopus 로고    scopus 로고
    • 8-Hydroxydaidzein is unstable in alkaline solutions
    • In press
    • Chang, T.S. 8-Hydroxydaidzein is unstable in alkaline solutions. J. Cosmet. Sci. In press.
    • J. Cosmet. Sci.
    • Chang, T.S.1


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