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Natural and Bioinspired Phenolic Compounds as Tyrosinase Inhibitors for the Treatment of Skin Hyperpigmentation: Recent Advances
Open accessAbstract
One of the most common approaches for control of skin pigmentation involves the inhibition of tyrosinase, a copper-containing enzyme which catalyzes the key steps of melanogenesis. This review focuses on the tyrosinase inhibition properties of a series of natural and synthetic, bioinspired phenolic compounds that have appeared in the literature in the last five years. Both mushroom and human tyrosinase inhibitors have been considered. Among the first class, flavonoids, in particular chalcones, occupy a prominent role as natural inhibitors, followed by hydroxystilbenes (mainly resveratrol derivatives). A series of more complex phenolic compounds from a variety of sources, first of all belonging to the Moraceae family, have also been described as potent tyrosinase inhibitors. As to the synthetic compounds, hydroxycinnamic acids and chalcones again appear as the most exploited scaffolds. Several inhibition mechanisms have been reported for the described inhibitors, pointing to copper chelating and/or hydrophobic moieties as key structural requirements to achieve good inhibition properties. Emerging trends in the search for novel skin depigmenting agents, including the development of assays that could distinguish between inhibitors and potentially toxic substrates of the enzyme as well as of formulations aimed at improving the bioavailability and hence the effectiveness of well-known inhibitors, have also been addressed.
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“Flavonoids are the most representative class among natural phenolic compounds acting as tyrosinase inhibitors [35].”
From Licorice (Glycyrrhiza glabra, G. uralensis, and G. inflata) and Their Constituents as Active Cosmeceutical Ingredients (2022) · cites this paper as [35]
In the citing paper
“This review confirmed that despite the diversity of natural inhibitors, many tyrosinase inhibitors belong to the phenolic class [35]”
From Licorice (Glycyrrhiza glabra, G. uralensis, and G. inflata) and Their Constituents as Active Cosmeceutical Ingredients (2022) · cites this paper as [35]
Citations
Cites
The Protective Role of Melanin Against UV Damage in Human Skin †
Brenner, M., & Hearing, V. J. (2008) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2007.00226.x · Cited by 1,741
An Updated Review of Tyrosinase Inhibitors
Chang, T. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10062440 · Cited by 1,555
A comprehensive review on tyrosinase inhibitors
Zolghadri, S., Bahrami, A., Khan, M. T. H., Munoz-Munoz, J., García-Molina, F., García-Cánovas, F., & Saboury, A. (2019) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1545767 · Cited by 993
Skin whitening agents: medicinal chemistry perspective of tyrosinase inhibitors
Pillaiyar, T., Manickam, M., & Namasivayam, V. (2017) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2016.1256882 · Cited by 932
Ismaya, W. T., Rozeboom, H. J., Weijn, A., Mes, J. J., Fusetti, F., Wichers, H. J., & Dijkstra, B. W. (2011) · Biochemistry · doi:10.1021/bi200395t · Cited by 872
Hypopigmenting agents: an updated review on biological, chemical and clinical aspects
Solano, F., Briganti, S., Picardo, M., & Ghanem, G. (2006) · Pigment Cell Research · doi:10.1111/j.1600-0749.2006.00334.x · Cited by 697
Mason, H. S. (1948) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35614-x · Cited by 620
A Chemist's View of Melanogenesis
Ito, S. (2003) · Pigment Cell Research · doi:10.1034/j.1600-0749.2003.00037.x · Cited by 508
Ramsden, C. A., & Riley, P. A. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.02.048 · Cited by 384
Olivares, C., & Solano, F. (2009) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2009.00636.x · Cited by 312
Inhibitors of Melanogenesis: An Updated Review
Pillaiyar, T., Namasivayam, V., Manickam, M., & Jung, S. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00967 · Cited by 309
The Tyrosinase-tyrosine Reaction
Raper, H. S. (1927) · Biochemical Journal · doi:10.1042/bj0210089 · Cited by 301
Natural, semisynthetic and synthetic tyrosinase inhibitors
Lee, S. Y., Baek, N., & Nam, T. (2015) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2015.1004058 · Cited by 298
Jiménez‐Cervantes, C., Solano, F., Kobayashi, T., Urabe, K., Hearing, V. J., Lozano, J. A., & García-Borrón, J. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32408-0 · Cited by 274
Mann, T., Gerwat, W., Batzer, J., Eggers, K., Scherner, C., Wenck, H., Stäb, F., Hearing, V. J., Röhm, K., & Kolbe, L. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2018.01.019 · Cited by 268
Melanocytes and Their DiseasesPreprint
Yamaguchi, Y., & Hearing, V. J. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a017046 · Cited by 257
Intrinsic and extrinsic regulation of human skin melanogenesis and pigmentation
Serre, C., Busuttil, V., & Botto, J.-M. (2018) · International Journal of Cosmetic Science · doi:10.1111/ics.12466 · Cited by 255
Ji, S., Li, Z., Song, W., Wang, Y., Liang, W., Li, K., Tang, S., Wang, Q., Qiao, X., Zhou, D., et al. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.5b00877 · Cited by 242
Thong, H.-Y., Jee, S., SUN, C.-C., & Boissy, R. E. (2003) · British Journal of Dermatology · doi:10.1046/j.1365-2133.2003.05473.x · Cited by 207
Upregulation of Melanogenesis and Tyrosinase Activity: Potential Agents for Vitiligo
Niu, C., & Aisa, H. A. (2017) · Molecules · doi:10.3390/molecules22081303 · Cited by 186
Ai-ren, Z., Dong, H., Yu, Y., Shu, Q., Zheng, L., Yu, X.-Y., & Cao, S. (2018) · Chinese Medicine · doi:10.1186/s13020-018-0206-9 · Cited by 177
Chen, W.-C., Tseng, T., Hsiao, N., Lin, Y., Wen, Z., Tsai, C., Lee, Y., Lin, H.-H., & Tsai, K. (2015) · Scientific Reports · doi:10.1038/srep07995 · Cited by 172
Chai, L., Zhou, J., Feng, H. X., Tang, C., Huang, Y., & Qian, Z. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b06711 · Cited by 156
Arrowitz, C., Schoelermann, A. M., Mann, T., Jiang, L. I., Weber, T. M., & Kolbe, L. (2019) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2019.02.013 · Cited by 148
Kumari, S., Thng, S. T. G., Verma, N. K., & Gautam, H. (2018) · Acta Dermato Venereologica · doi:10.2340/00015555-3002 · Cited by 138
(2011) · Wiley eBooks · doi:10.1002/9783527636150 · Cited by 138
Micillo, R., Panzella, L., Koike, K., Monfrecola, G., Napolitano, A., & D’Ischia, M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050746 · Cited by 135
Self-citationCondensed Tannins from Longan Bark as Inhibitor of Tyrosinase: Structure, Activity, and Mechanism
Chai, W., Huang, Q., Lin, M., Ou-Yang, C., Huang, W.-Y., Wang, Y., Xu, K.-L., & Feng, H. A. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b05481 · Cited by 135
Bouzaiene, N. N., Chaabane, F., Sassi, A., Ghédira, L. C., & Ghédira, K. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.11.030 · Cited by 129
Wei, Y., Zhang, J., Zhou, Y., Bei, W., Li, Y., Yuan, Q., & Liang, H. (2016) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2016.11.093 · Cited by 125
On the Metal Cofactor in the Tyrosinase Family
Solano, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020633 · Cited by 118
Cestari, T. F., Dantas, L. D. P., & Boza, J. C. (2014) · Anais Brasileiros de Dermatologia · doi:10.1590/abd1806-4841.20142353 · Cited by 104
Shrotriya, S. N., Ranpise, N. S., Satpute, P., & Vidhate, B. (2017) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2017.1373659 · Cited by 102
Ashraf, Z., Rafiq, M., Seo, S., Babar, M. M., & Zaidi, N. S. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.06.068 · Cited by 102
Hurbain, I., Romao, M., Sextius, P., Bourreau, E., Marchal, C., Bernerd, F., Duval, C., & Raposo, G. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.09.039 · Cited by 98
Solimine, J., Garo, E., Wedler, J., Rusanov, K., Fertig, O., Hamburger, M. O., Atanassov, I. I., & Butterweck, V. (2015) · Fitoterapia · doi:10.1016/j.fitote.2015.11.012 · Cited by 97
A tyrosinase with an abnormally high tyrosine hydroxylase/dopa oxidase ratio
Hernández‐Romero, D., Sánchez-Amat, A., & Solano, F. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05038.x · Cited by 96
Rigon, R. B., Fachinetti, N., Severino, P. B., Santana, M. H. A., & Chorilli, M. (2016) · Molecules · doi:10.3390/molecules21010116 · Cited by 95
Self-assembly of the oxy-tyrosinase core and the fundamental components of phenolic hydroxylation
Citek, C., Lyons, C. T., Wasinger, E. C., & Stack, T. D. P. (2012) · Nature Chemistry · doi:10.1038/nchem.1284 · Cited by 95
Crystal Structures of Copper-depleted and Copper-bound Fungal Pro-tyrosinase
Fujieda, N., Yabuta, S., Ikeda, T., Oyama, T., Muraki, N., Kurisu, G., & Itoh, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.477612 · Cited by 92
Ethosomes of Phenylethyl Resorcinol as Vesicular Delivery System for Skin Lightening Applications
Limsuwan, T., Boonme, P., Khongkow, P., & Amnuaikit, T. (2017) · BioMed Research International · doi:10.1155/2017/8310979 · Cited by 91
Synergistic Promotion on Tyrosinase Inhibition by Antioxidants
Wang, T., Hao, M., Sun, Y. X., Wang, L., Wang, H., Zhang, Y., Li, H., Zhuang, P., & Yang, Z. Y. (2018) · Molecules · doi:10.3390/molecules23010106 · Cited by 88
Characteristics and in vitro anti-skin aging activity of gallic acid loaded in cationic CTAB niosome
Chaikul, P., Khat‐udomkiri, N., Iangthanarat, K., Manosroi, J., & Manosroi, A. (2019) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2019.02.008 · Cited by 87
Glycybridins A–K, Bioactive Phenolic Compounds from Glycyrrhiza glabra
Li, K., Ji, S., Song, W., Kuang, Y., Lin, Y., Tang, S., Cui, Z.-X., Qiao, X., Yu, S., & Ye, M. (2017) · Journal of Natural Products · doi:10.1021/acs.jnatprod.6b00783 · Cited by 86
Maruyama, H., Kawakami, F., Lwin, T., Imai, M., & Shamsa, F. (2018) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00892 · Cited by 84
Pigmentation Disorders: Diagnosis and Management.
Plensdorf, S., Livieratos, M., & Dada, N. (2017) · PubMed · Cited by 81
Anti-Melanogenic Properties of Greek Plants. A Novel Depigmenting Agent from Morus alba Wood
Chaita, E., Lambrinidis, G., Cheimonidi, C., Agalou, A., Beis, D., Trougakos, I., Mikros, E., Skaltsounis, A.-L., & Aligiannis, N. (2017) · Molecules · doi:10.3390/molecules22040514 · Cited by 80
Ashraf, Z., Rafiq, M., Seo, S., Kwon, K. S., Babar, M. M., & Zaidi, N. S. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.05.031 · Cited by 79
Tyrosinase inhibition and anti-melanin generation effect of cinnamamide analogues
Ullah, S., Park, C., Ikram, M., Kang, D., Lee, S., Yang, J., Park, Y., Yoon, S., Chun, P., & Moon, H. R. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.03.001 · Cited by 78
Chai, W., Wei, M.-K., Wang, R. Y., Deng, R.-G., Zou, Z.-R., & Peng, Y. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b03099 · Cited by 77
Omar, S., Scott, C. J., Hamlin, A., & Obied, H. K. (2018) · Fitoterapia · doi:10.1016/j.fitote.2018.05.011 · Cited by 76
Qin, H., Shang, Z., Jantan, I., Tan, O. Ü., Hussain, M. A., Sher, M., & Bukhari, S. N. A. (2015) · RSC Advances · doi:10.1039/c5ra02995c · Cited by 76
Suicide inactivation of the diphenolase and monophenolase activities of tyrosinase
Muñoz-Muñoz, J., Garcı́a-Molina, F., Varón, R., Garcı́a-Ruiz, P. A., Tudela, J., Garcı́a-Cánovas, F., & Rodríguez‐López, J. N. (2010) · IUBMB Life · doi:10.1002/iub.348 · Cited by 75
Ito, S., Wakamatsu, K., d’Ischia, M., Napolitano, A., & Pezzella, A. (2011) · Wiley eBooks · doi:10.1002/9783527636150.ch6 · Cited by 74
Self-citationChai, W., Wei, Q., Deng, W., Zheng, Y., Chen, X., Huang, Q., Ou-Yang, C., & Peng, Y. (2018) · Food & Function · doi:10.1039/c8fo01979g · Cited by 74
Ullah, S., Kang, D., Lee, S., Ikram, M., Park, C., Park, Y., Yoon, S., Chun, P., & Moon, H. R. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.10.025 · Cited by 73
The Late Stages of Melanogenesis: Exploring the Chemical Facets and the Application Opportunities
Panzella, L., Ebato, A., Napolitano, A., & Koike, K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061753 · Cited by 72
Self-citationTyrosinase inhibitory activity of flavonoids from Artocarpus heterophyllous
Nguyen, H. X., Nguyen, N. T., Nguyen, M. H. K., Le, T. H., Do, T. N. V., Hưng, T. M., & Nguyen, M. T. T. (2016) · Chemistry Central Journal · doi:10.1186/s13065-016-0150-7 · Cited by 72
Ashraf, Z., Rafiq, M., Nadeem, H., Hassan, M., Afzal, S., Waseem, M., Afzal, K., & Latip, J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178069 · Cited by 72
The Mechanism of Suicide-Inactivation of Tyrosinase: A Substrate Structure Investigation
Land, E. J., Ramsden, C. A., & Riley, P. A. (2007) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.212.341 · Cited by 69
Screening for bioactive natural products from a 67-compound library of Glycyrrhiza inflata
Lin, Y., Kuang, Y., Li, K., Wang, S., Song, W., Qiao, X., Sabir, G., & Ye, M. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.05.009 · Cited by 68
Zhang, L., Tao, G., Chen, J., & Zheng, Z. (2016) · Molecules · doi:10.3390/molecules21091130 · Cited by 67
Yang, L., Yang, Y., Dong, W.-H., Li, W., Wang, P., Xue, C., Yuan, J.-Z., Chen, H., Mei, W.-L., & Dai, H. (2019) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2019.1576657 · Cited by 66
Pintus, F., Matos, M. J., Vilar, S., Hripcsak, G. M., Varela, C. L., Uriarte, E., Santana, L., Borges, F., Medda, R., Petrillo, A. D., et al. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.01.037 · Cited by 66
Melanogenesis Inhibitors: Strategies for Searching for and Evaluation of Active Compounds
Gunia‐Krzyżak, A., Popiół, J., & Marona, H. (2016) · Current Medicinal Chemistry · doi:10.2174/0929867323666160627094938 · Cited by 65
Chai, W., Ou-Yang, C., Huang, Q., Lin, M., Wang, Y., Xu, K.-L., Huang, W.-Y., & Pang, D. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.04.001 · Cited by 65
Chai, W., Lin, M., Wang, Y., Xu, K., Huang, W.-Y., Pan, D., Zou, Z.-R., & Peng, Y. (2017) · Food Research International · doi:10.1016/j.foodres.2017.07.082 · Cited by 65
Inhibitory effect of brazilein on tyrosinase and melanin synthesis: Kinetics and in silico approach
Hemachandran, H., Anantharaman, A., Mohan, S., Doss, C. G. P., Gopalakrishnan, M., Gopalakrishnan, C., & Ramamoorthy, S. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.07.064 · Cited by 63
Mechanisms underlying post-inflammatory hyperpigmentation: lessons from solar lentigo
Cardinali, G., Kovacs, D., & Picardo, M. (2012) · Annales de Dermatologie et de Vénéréologie · doi:10.1016/s0151-9638(12)70127-8 · Cited by 62
Ito, S., & Wakamatsu, K. (2015) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2015.07.007 · Cited by 62
Cásedas, G., Les, F., González‐Burgos, E., Gómez-Serranillos, M. P., Smith, C., & López, V. (2018) · South African Journal of Botany · doi:10.1016/j.sajb.2018.07.001 · Cited by 62
2-Hydroxypyridine-N-oxide-Embedded Aurones as Potent Human Tyrosinase Inhibitors
Haudecoeur, R., Carotti, M., Gouron, A., Maresca, M., Buitrago, E., Hardré, R., Bergantino, E., Jamet, H., Belle, C., Réglier, M., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00369 · Cited by 61
Guo, N., Wang, C., Shang, C., You, X. T., Zhang, L., & Liu, W. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.06.055 · Cited by 61
Kishore, N., Twilley, D., van Staden, A. B., Verma, P. K., Singh, B., Cardinali, G., Kovacs, D., Picardo, M., Kumar, V., & Lall, N. (2018) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00564 · Cited by 60
Intercellular transfer of organelles during body pigmentation
Tadokoro, R., & Takahashi, Y. (2017) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2017.05.001 · Cited by 58
Sheng, Z., Ge, S.-Y., Xu, X., Zhang, Y., Wu, P., Zhang, K., Xu, X., Li, C., Zhao, D., & Tang, X. (2018) · MedChemComm · doi:10.1039/c8md00099a · Cited by 58
Wu, Q., Wong, Z. C. F., Wang, C., Fung, A. H. Y., Wong, E. O. Y., Chan, G. K.-L., Dong, T. T.-X., Chen, Y., & Tsim, K. W. K. (2018) · Phytomedicine · doi:10.1016/j.phymed.2018.12.006 · Cited by 57
Wang, Z., Hwang, S. H., Huang, B., & Lim, S. S. (2015) · Journal of Chromatography B · doi:10.1016/j.jchromb.2015.08.030 · Cited by 56
Oh, T.-I., Yun, J.-M., Park, E., Kim, Y. S., Lee, Y.-M., & Lim, J.-H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020320 · Cited by 56
Antimelanogenic effects of luteolin 7-sulfate isolated fromPhyllospadix iwatensisMakino
Kwak, J. Y., Seok, J. K., Suh, H., Choi, Y., Hong, S. S., Kim, D. S., & Boo, Y. C. (2016) · British Journal of Dermatology · doi:10.1111/bjd.14496 · Cited by 55
Promden, W., Viriyabancha, W., Monthakantirat, O., Umehara, K., Noguchi, H., & De‐Eknamkul, W. (2018) · Molecules · doi:10.3390/molecules23061403 · Cited by 54
Kim, C. S., Noh, S. G., Park, Y., Kang, D., Chun, P., Chung, H. Y., Jung, H. J., & Moon, H. R. (2018) · Molecules · doi:10.3390/molecules23102725 · Cited by 53
Kim, S. J., Yang, J., Lee, S., Park, C., Kang, D., Akter, J., Ullah, S., Kim, Y., Chun, P., & Moon, H. R. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.05.047 · Cited by 52
Cheng, M., & Chen, Z. (2016) · Electrophoresis · doi:10.1002/elps.201600367 · Cited by 52
Comparative efficacy and safety of deoxyarbutin, a new tyrosinase-inhibiting agent.
Hamed, S., Sriwiriyanont, P., deLong, M. A., Visscher, M. O., Wickett, R. R., & Boissy, R. E. (2006) · PubMed · Cited by 51
Development of highly potent melanogenesis inhibitor by in vitro, in vivo and computational studies
Abbas, Q., Ashraf, Z., Hassan, M., Nadeem, H., Latif, M., Afzal, S., & Seo, S.-Y. (2017) · Drug Design Development and Therapy · doi:10.2147/dddt.s137550 · Cited by 51
Identification of Anti-Melanogenesis Constituents from Morus alba L. Leaves
Li, H. X., Park, J. U., Su, X. D., Kim, K. T., Kang, J. S., Kim, Y. H., Kim, Y. H., & Yang, S. Y. (2018) · Molecules · doi:10.3390/molecules23102559 · Cited by 50
Ashraf, Z., Rafiq, M., Seo, S., Babar, M. M., & Zaidi, N. S. (2015) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2014.979346 · Cited by 50
The Improvement of Skin Whitening of Phenylethyl Resorcinol by Nanostructured Lipid Carriers
Kim, B.-S., Na, Y., Choi, J., Kim, I., Lee, E. J., Kim, S.-Y., Lee, J., & Cho, C. (2017) · Nanomaterials · doi:10.3390/nano7090241 · Cited by 47
Fachinetti, N., Rigon, R. B., Eloy, J. O., Sato, M. R., dos Santos, K. C., & Chorilli, M. (2018) · AAPS PharmSciTech · doi:10.1208/s12249-018-0961-z · Cited by 47
Polyamine derivatives from the bee pollen of Quercus mongolica with tyrosinase inhibitory activity
Kim, S. B., Liu, Q., Ahn, J. H., Jo, Y. H., Turk, A., Hong, I. P., Han, S. M., Hwang, B. Y., & Lee, M. K. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.08.014 · Cited by 46
Influence of plasma-activated compounds on melanogenesis and tyrosinase activity
Ali, A., Ashraf, Z., Kumar, N., Rafiq, M., Jabeen, F., Park, J. H., Choi, K. H., Lee, S.-H., Seo, S.-Y., Choi, E. H., et al. (2016) · Scientific Reports · doi:10.1038/srep21779 · Cited by 45
Substrate share in the suicide inactivation of mushroom tyrosinase
Haghbeen, K., Saboury, A. A., & Karbassi, F. (2004) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2004.08.017 · Cited by 44
Tyrosinase inhibitory study of flavonolignans from the seeds of Silybum marianum (Milk thistle)
Kim, J. Y., Kim, J. Y., Jenis, J., Li, Z. P., Ban, Y. J., Baiseitova, A., & Park, K. H. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.03.013 · Cited by 44
Chemical constituents derived from Artocarpus xanthocarpus as inhibitors of melanin biosynthesis
Jin, Y., Lin, C.-C., Lu, T., Li, J., Chen, I., Kuo, Y., & Ko, H. (2015) · Phytochemistry · doi:10.1016/j.phytochem.2015.07.003 · Cited by 43
Uesugi, D., Hamada, H., Shimoda, K., Kubota, N., Ozaki, S., & Nagatani, N. (2016) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2016.1240606 · Cited by 43
Identification by shape-based virtual screening and evaluation of new tyrosinase inhibitors
Li, Q., Yang, H., Mo, J., Chen, Y., Wu, Y., Chen, K., Sun, Y., & Sun, H. (2018) · PeerJ · doi:10.7717/peerj.4206 · Cited by 43
Kim, B., Park, K. C., Park, J. H., Lee, C. G., Ye, S., & Park, J. Y. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.10.110 · Cited by 42
Zeng, H., Liu, Z., Hu, G.-Z., Qu, L., & Yang, R. (2018) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2018.11.045 · Cited by 42
Biochemical Mechanism of Rhododendrol-Induced Leukoderma
Ito, S., & Wakamatsu, K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020552 · Cited by 41
Xiong, S., Lim, G. T., Yin, S., Lee, J., Si, Y.-X., Yang, J., Park, Y., & Qian, G.-Y. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.10.046 · Cited by 41
Lee, J. Y., Cho, Y., Park, J. H., Ahn, E., Jeong, W., Shin, H. S., Kim, M.-S., Yang, S. H., & Oh, J. S. (2018) · Toxicology Reports · doi:10.1016/j.toxrep.2018.11.005 · Cited by 41
Inhibitory effects of compounds isolated from Lepechinia meyenii on tyrosinase
Crespo, M. I., Chabán, M. F., Lanza, P. A., Joray, M. B., Palacios, S. M., Vera, D. M. A., & Carpinella, M. C. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2019.01.019 · Cited by 41
Tofani, R., SUMIRTAPURA, Y. C., & Darijanto, S. T. (2016) · Scientia Pharmaceutica · doi:10.3390/scipharm84040634 · Cited by 40
Chai, W., Lin, M., Feng, H. A., Zou, Z.-R., & Wang, Y. (2017) · Food & Function · doi:10.1039/c6fo01320a · Cited by 40
Shang, C., Zhang, Y., You, X. T., Guo, N., Wang, Y., Yang, F., & Liu, W. (2018) · Luminescence · doi:10.1002/bio.3464 · Cited by 40
Enachi, E., Aprodu, I., Stănciuc, N., Gabriela Râpeanu, B., & Bahrim, G. E. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.01.089 · Cited by 39
Deng, Y.-T., Ge, L., Shi, Y., Li, H., Zhang, J., Mao, X., Fu, Q., Peng, W.-X., Chen, Q., & Shen, D. (2016) · Process Biochemistry · doi:10.1016/j.procbio.2016.04.022 · Cited by 39
Anti-photoageing and anti-melanogenesis activities of chrysin
Zhu, L., Lu, Y. Q., Yu, W.-G., Zhao, X., & Lü, Y. (2016) · Pharmaceutical Biology · doi:10.1080/13880209.2016.1179334 · Cited by 39
Bang, E., Noh, S., Ha, S., Jung, H. J., Kim, D. H., Lee, A. K., Hyun, M. K., Kang, D., Lee, S., Park, C., et al. (2018) · Molecules · doi:10.3390/molecules23123307 · Cited by 39
Wang, S., Chang, W.-C., Hsu, C., & Su, N. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b02442 · Cited by 38
Koirala, P., Seong, S. H., Zhou, Y., Shrestha, S., Jung, H. A., & Choi, J. S. (2018) · Molecules · doi:10.3390/molecules23061413 · Cited by 38
Design, synthesis and anti-melanogenic effect of cinnamamide derivatives
Ullah, S., Park, Y., Ikram, M., Lee, S., Park, C., Kang, D., Yang, J., Akter, J., Yoon, S., Chun, P., et al. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.10.014 · Cited by 38
Rhododenol-induced leukoderma in a mouse model mimicking Japanese skin
Abe, Y., Okamura, K., Kawaguchi, M., Hozumi, Y., Aoki, H., Kunisada, T., Ito, S., Wakamatsu, K., Matsunaga, K., & Suzuki, T. (2015) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2015.10.011 · Cited by 37
Mustapha, N., Mokdad-Bzéouich, I., Ghédira, K., Hennebelle, T., & Ghédira, L. C. (2014) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2014.11.010 · Cited by 37
Gąsowska-Bajger, B., & Wojtasek, H. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b01896 · Cited by 36
Zhou, J., Tang, Q., Wu, T., & Cheng, Z. (2016) · Phytochemical Analysis · doi:10.1002/pca.2666 · Cited by 36
Flavanoids derivatives from the root bark of Broussonetia papyrifera as a tyrosinase inhibitor
Tian, J., Liu, T.-L., Xue, J., Hong, W., Zhang, Y., Zhang, D.-X., Cui, C., Liu, M., & Niu, S.-L. (2019) · Industrial Crops and Products · doi:10.1016/j.indcrop.2019.06.008 · Cited by 36
Lee, S., Lee, D.-H., Kim, J., Um, B. H., Sung, S. H., Jeong, L. S., Kim, Y. K., & Kim, S. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.08.106 · Cited by 35
Tang, H., Cui, F., Li, H., Huang, Q., & Li, Y. (2018) · RSC Advances · doi:10.1039/c7ra12749a · Cited by 35
Kwak, J. Y., Park, S., Seok, J. K., Liu, K., & Boo, Y. C. (2015) · Archives of Dermatological Research · doi:10.1007/s00403-015-1583-x · Cited by 34
Marková, E., Kotik, M., Křenková, A., Man, P., Haudecoeur, R., Boumendjel, A., Hardré, R., Mekmouche, Y., Courvoisier‐Dezord, E., Réglier, M., et al. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b00286 · Cited by 34
Synthesis and tyrosinase inhibitory activities of 4-oxobutanoate derivatives of carvacrol and thymol
Brotzman, N., Xu, Y., Graybill, A., Cocolas, A. H., Ressler, A. J., Seeram, N. P., Ma, H., & Henry, G. E. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.11.013 · Cited by 34
What’s New in Pigmentary Disorders
Zubair, R., Lyons, A. B., Vellaichamy, G., Peacock, A., & Hamzavi, I. H. (2019) · Dermatologic Clinics · doi:10.1016/j.det.2018.12.008 · Cited by 34
Discrimination between Alternative Substrates and Inhibitors of Tyrosinase
Ortiz‐Ruiz, C. V., García‐Molina, M. D. M., Tudela, J., Tomas-Martinez, V., & Garcı́a-Cánovas, F. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf5051816 · Cited by 33
Tang, L., Zhang, W., Zhao, H. Y., & Chen, Z. (2015) · Journal of Separation Science · doi:10.1002/jssc.201500371 · Cited by 32
Kim, D. H., & Lee, J. H. (2019) · South African Journal of Botany · doi:10.1016/j.sajb.2019.03.015 · Cited by 32
Al-Amin, M., Cao, J., Naeem, M., Banna, H., Kim, M., Jung, Y., Chung, H. Y., Moon, H. R., & Yoo, J. (2016) · Drug Design Development and Therapy · doi:10.2147/dddt.s123759 · Cited by 31
Jung, H. J., Lee, M. J., Park, Y. J., Noh, S. G., Lee, A. K., Moon, K. M., Lee, E. K., Bang, E. J., Park, Y. J., Kim, S. J., et al. (2018) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2018.1445518 · Cited by 31
Ismaya, W. T., Tandrasasmita, O. M., Sundari, S., Diana, D., Lai, X., RETNONINGRUM, D. S., Dijkstra, B. W., Tjandrawinata, R. R., & Rachmawati, H. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.04.014 · Cited by 31
Swertiajaponin inhibits skin pigmentation by dual mechanisms to suppress tyrosinase
Lee, B., Moon, K. M., Lee, B.-S., Yang, J.-H., Park, K. I., Cho, W., & Yeul, J. (2017) · Oncotarget · doi:10.18632/oncotarget.20913 · Cited by 31
Son, S., Kim, H., Yun, H. Y., Kim, D. H., Ullah, S., Kim, S. J., Kim, Y., Kim, M., Yoo, J., Chun, P., et al. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.11.015 · Cited by 30
Flavonoids from the leaves and heartwoods of Artocarpus lowii King and their bioactivities
Abdullah, S. A., Jamil, S., Basar, N., Lathiff, S. M. A., & Arriffin, N. M. (2016) · Natural Product Research · doi:10.1080/14786419.2016.1222387 · Cited by 30
Resorcinol alkyl glucosides as potent tyrosinase inhibitors
Ishioka, W., Oonuki, S., Iwadate, T., & Nihei, K. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.11.029 · Cited by 30
Kang, K. H., Lee, B., Son, S., Yun, H. Y., Moon, K. M., Jeong, H. O., Kim, D. H., Lee, E. K., Choi, Y. J., Kim, D. H., et al. (2015) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-00300 · Cited by 29
Yamauchi, K., Mitsunaga, T., Itakura, Y., & Batubara, I. (2015) · Fitoterapia · doi:10.1016/j.fitote.2015.05.006 · Cited by 29
Deng, H., Lin, X.-L., He, S., Wu, G.-W., Wu, W., Yang, Y., Lin, Z. Y., Peng, H., Xia, X., & Chen, W. (2019) · Microchimica Acta · doi:10.1007/s00604-019-3451-4 · Cited by 29
4‐n‐butylresorcinol enhances proteolytic degradation of tyrosinase in B16F10 melanoma cells
Lee, S.-J., Son, Y. H., Lee, K. B., Lee, J., Kim, H. ‐., Jeong, E. M., Park, S. C., & Kim, I. (2016) · International Journal of Cosmetic Science · doi:10.1111/ics.12368 · Cited by 28
Bioassay Guided Isolation of Active Compounds from Alchemilla barbatiflora Juz.
(2017) · Records of Natural Products · doi:10.25135/rnp.07.17.07.117 · Cited by 28
Nguyen, M. T. T., Le, T. H., Nguyen, H. X., Dang, P. H., Do, T. N. V., Abe, M., Takagi, R., & Nguyen, N. T. (2017) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00453 · Cited by 28
Is DHICA the key to dopachrome tautomerase and melanocyte functions?
Panzella, L., Napolitano, A., & d’Ischia, M. (2011) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2010.00771.x · Cited by 27
Self-citationSynthesis and tyrosinase inhibition activity of trans -stilbene derivatives
Ismail, T., Shafi, S., Srinivas, J., Sarkar, D. M., Qurishi, Y., Khazir, J., Alam, M. S., & Kumar, H. M. S. (2016) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2016.01.001 · Cited by 27
Jeong, J., Liu, Q., Kim, S., Jo, Y. H., Mo, E. J., Yang, H., Song, D. H., Hwang, B., & Lee, M. H. (2015) · Molecules · doi:10.3390/molecules20058730 · Cited by 27
Glabridin smartPearls—Silica selection, production, amorphous stability and enhanced solubility
Hespeler, D., Kaltenbach, J., & Pyo, S. M. (2019) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2019.02.028 · Cited by 27
Ullah, S., Park, Y., Park, C., Lee, S., Kang, D., Yang, J., Akter, J., Chun, P., & Moon, H. R. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.04.020 · Cited by 27
Radhakrishnan, S., Shimmon, R., Conn, C., & Baker, A. T. (2015) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2015.08.005 · Cited by 26
Parisi, O. I., Malivindi, R., Amone, F., Ruffo, M., Malanchin, R., Carlomagno, F., Piangiolino, C., Nobile, V., Pezzi, V., Scrivano, L., et al. (2017) · Cosmetics · doi:10.3390/cosmetics4030028 · Cited by 26
Kamauchi, H., Noji, M., Kinoshita, K., Takanami, T., & Koyama, K. (2018) · Tetrahedron · doi:10.1016/j.tet.2018.04.033 · Cited by 26
Lu, T., Ko, H.-J., Ng, L., & Hsieh, Y. (2015) · Chemistry & Biodiversity · doi:10.1002/cbdv.201400208 · Cited by 25
Ortiz‐Ruiz, C. V., Berná, J., Rodríguez‐López, J. N., Pérez‐Ruiz, T., & Garcı́a-Cánovas, F. (2015) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b02523 · Cited by 25
2-(3, 4-dihydroxybenzylidene)malononitrile as a novel anti-melanogenic compound
Lee, B., Moon, K. M., Lim, J. S., Park, Y., Kim, D. H., Son, S., Jeong, H. O., Kim, D. H., Lee, E. K., Chung, K. W., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20690 · Cited by 25
Song, W., Qin, S.-T., Fang, F.-X., Gao, Z., Liang, D.-D., Liu, L., Tian, H., & Yang, H. (2017) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-017-2635-9 · Cited by 25
Kang, M., Park, S., Oh, S. W., Lee, S. E., Yoo, J. A., Nho, Y. H., Lee, S., Han, B. S., Cho, J. Y., & Lee, J. (2018) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2018.1459176 · Cited by 25
Isolation of tyrosinase and melanogenesis inhibitory flavonoids from Juniperus chinensis fruits
Park, S.-A., Jegal, J., Chung, K. W., Jung, H. J., Noh, S. G., Chung, H. Y., Ahn, J., Kim, J., & Yang, M. H. (2018) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2018.1511367 · Cited by 24
Crescenzi, O., Napolitano, A., Prota, G., & Peter, M. G. (1991) · Tetrahedron · doi:10.1016/s0040-4020(01)86556-x · Cited by 24
Self-citationEvaluation of Novel Chalcone Oximes as Inhibitors of Tyrosinase and Melanin Formation in B16 Cells
Radhakrishnan, S., Shimmon, R., Conn, C., & Baker, A. T. (2015) · Archiv der Pharmazie · doi:10.1002/ardp.201500298 · Cited by 24
Vandeput, M., Patris, S., Cunha‐Silva, H., Parsajoo, C., Dejaeghere, B., Martinez, J. A., & Kauffmann, J. (2017) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2017.03.156 · Cited by 24
4-n-butylresorcinol, a depigmenting agent used in cosmetics, reacts with tyrosinase
Garcia-Jimenez, A., Teruel, J. A., Ortiz‐Ruiz, C. V., Berná, J., Tudela, J., & Garcı́a-Cánovas, F. (2016) · IUBMB Life · doi:10.1002/iub.1528 · Cited by 24
Song, W., Zhu, X., Ding, X., Yang, H., Qin, S.-T., Chen, H., & Wei, S. (2016) · International Journal of Food Properties · doi:10.1080/10942912.2016.1209682 · Cited by 24
Boghrati, Z., Naseri, M., Rezaie, M., Pham, N. B., Quinn, R. J., Tayarani‐Najaran, Z., & Iranshahi, M. (2016) · Europe PMC (PubMed Central) · doi:10.22038/ijbms.2016.7460 · Cited by 24
Ha, J. H., Jeong, Y. J., Xuan, S. H., Lee, J., Park, J., & Park, S. N. (2018) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2018.04.011 · Cited by 24
Veselinović, J. B., Veselinović, A. M., Tomic, T. I., Davis, R., O’Connor, K. E., Pavić, A., & Runic, J. N. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.09.021 · Cited by 24
Isoprenylated phenolic compounds with tyrosinase inhibition from Morus nigra
Hu, X., Yu, M.-H., Yan, G., Wang, H., Hou, A., & Lei, C. (2017) · Journal of Asian Natural Products Research · doi:10.1080/10286020.2017.1350653 · Cited by 24
Anti-melanogenic activity of ellagitannin casuarictin in B16F10 mouse melanoma cells
Goenka, S., Ceccoli, J., & Simon, S. R. (2019) · Natural Product Research · doi:10.1080/14786419.2019.1636242 · Cited by 24
Chai, W., Wang, R., Wei, M.-K., Zou, Z.-R., Deng, R.-G., Liu, W., & Peng, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145483 · Cited by 23
Flavonoids from Artocarpus anisophyllus and their Bioactivities
Lathiff, S. M. A., Jemaon, N., Abdullah, S. A., & Jamil, S. (2015) · Natural Product Communications · doi:10.1177/1934578x1501000305 · Cited by 23
Preparation of tyrosinase inhibitors and antibrowning agents using green technology
Dong, X., Zhang, Y., He, J., Zhang, S., Zeng, M., Chen, J., & Zheng, Z. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.11.007 · Cited by 23
Azachalcones: A new class of potent polyphenol oxidase inhibitors
Radhakrishnan, S., Shimmon, R., Conn, C., & Baker, A. T. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.02.060 · Cited by 23
Radhakrishnan, S., Shimmon, R., Conn, C., & Baker, A. T. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.10.071 · Cited by 23
Lee, T. H., Kang, J. H., Seo, J. O., Baek, S.-H., Moh, S. H., Chae, J. K., Park, Y. U., Ko, Y. T., & Kim, S. Y. (2015) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2015.165 · Cited by 23
Chemical and bioactivity of flavanones obtained from roots of Dalea pazensis Rusby
Santi, M. D., Peralta, M. A., Mendoza, C. S., Cabrera, J. L., & Ortega, M. G. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.02.058 · Cited by 23
Kim, D. H., Kim, S. J., Ullah, S., Yun, H. Y., Chun, P., & Moon, H. R. (2017) · Drug Design Development and Therapy · doi:10.2147/dddt.s131538 · Cited by 23
Ranjbar, S., Akbari, A., Edraki, N., Khoshneviszadeh, M., Hemmatian, H., Firuzi, O., & Khoshneviszadeh, M. (2018) · Letters in Drug Design & Discovery · doi:10.2174/1570180815666180219155027 · Cited by 23
Jung, H. J., Lee, A. K., Park, Y. J., Lee, S., Kang, D., Jung, Y. S., Chung, H. Y., & Moon, H. R. (2018) · Molecules · doi:10.3390/molecules23061415 · Cited by 23
Moon, K. M., Hwang, Y., Yang, J.-H., Yeul, J., & Lee, B. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.01.044 · Cited by 23
Lee, S.-M., Chen, Y.-S., Lin, C., & Chen, K.-H. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16011495 · Cited by 22
Chemical synthesis and tyrosinase-inhibitory activity of isotachioside and its related glycosides
Matsumoto, T., Nakajima, T., Iwadate, T., & Nihei, K. (2018) · Carbohydrate Research · doi:10.1016/j.carres.2018.06.004 · Cited by 22
Micillo, R., Sirés-Campos, J., García-Borrón, J. C., Panzella, L., Napolitano, A., & Olivares, C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082156 · Cited by 22
Self-citationSchlich, M., Fornasier, M., Nieddu, M., Sinico, C., Murgia, S., & Rescigno, A. (2018) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2018.08.008 · Cited by 22
Yang, J., Lee, E., Hwang, I., Yim, D., Han, J., Lee, Y., & Kim, J. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00050 · Cited by 21
Mayr, F., Sturm, S., Ganzera, M., Waltenberger, B., Martens, S., Schwaiger, S., Schuster, D., & Stuppner, H. (2019) · Journal of Natural Products · doi:10.1021/acs.jnatprod.8b00847 · Cited by 21
Phenols displaying tyrosinase inhibition from Humulus lupulus
Kim, D. W., Woo, H. S., Kim, J. Y., Ryuk, J. A., Park, K. H., & Ko, B. (2015) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2015.1063621 · Cited by 21
Mokdad-Bzéouich, I., Chaabane, F., Nadia, M. A. N., Kilani, S., Ghedira, K., & Ghédira, L. C. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.06.022 · Cited by 20
Ding, H., Chiang, C.-M., Tzeng, W.-M., & Chang, T. (2015) · Process Biochemistry · doi:10.1016/j.procbio.2015.06.007 · Cited by 20
Rhododendrol glycosides as stereospecific tyrosinase inhibitors
Iwadate, T., & Nihei, K. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.09.014 · Cited by 20
Melanogenesis inhibitory activity of components from Salam leaf (Syzygium polyanthum) extract
Setyawati, A., Hirabayashi, K., Yamauchi, K., Hattori, H., Mitsunaga, T., Batubara, I., Heryanto, R., Hashimoto, H., & Hotta, M. (2018) · Journal of Natural Medicines · doi:10.1007/s11418-018-1171-4 · Cited by 20
Radhakrishnan, S., Shimmon, R., Conn, C., & Baker, A. T. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.08.033 · Cited by 19
Chemical Components from the Stems ofPueraria lobataand Their Tyrosinase Inhibitory Activity
Morgan, A. M. A., Jeon, M. N., Jeong, M. H., Yang, S. Y., & Kim, Y. H. (2016) · Natural Product Sciences · doi:10.20307/nps.2016.22.2.111 · Cited by 19
Tao, Y., Su, D., Du, Y., Li, W., Cai, B., Di, L., Shi, L., & Hu, L. (2016) · RSC Advances · doi:10.1039/c6ra22045b · Cited by 19
Structural and kinetic considerations on the catalysis of deoxyarbutin by tyrosinase
Garcia-Jimenez, A., Teruel, J. A., Garcı́a-Ruiz, P. A., Saura-Sanmartín, A., Berná, J., Garcı́a-Cánovas, F., & Rodríguez‐López, J. N. (2017) · PLoS ONE · doi:10.1371/journal.pone.0187845 · Cited by 19
Sasaki, A., Yamano, Y., Sugimoto, S., Otsuka, H., Matsunami, K., & Shinzato, T. (2017) · Journal of Natural Medicines · doi:10.1007/s11418-017-1148-8 · Cited by 19
Phenylethyl resorcinol smartLipids for skin brightening – Increased loading & chemical stability
Köpke, D., Müller, R. H., & Pyo, S. M. (2019) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2019.104992 · Cited by 18
Evaluation of Antimelanogenic Activity and Mechanism of Galangin in Silico and in Vivo
Chung, K. W., Jeong, H. O., Lee, E. K., Kim, S. J., Chun, P., Chung, H. Y., & Moon, H. R. (2017) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00597 · Cited by 18
Tanaka, Y., Suzuki, M. S., Kodachi, Y., & Nihei, K. (2018) · Carbohydrate Research · doi:10.1016/j.carres.2018.11.006 · Cited by 18
Chen, H., Song, W., Sun, K.-K., Du, H., & Wei, S. (2018) · Journal of Wood Chemistry and Technology · doi:10.1080/02773813.2018.1533975 · Cited by 18
Gong, C., Wang, Y., Wang, M., Su, W.-C., Wang, Q., Chen, Q., & Shi, Y. (2019) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-019-03038-6 · Cited by 18
Feruloyl Sucrose Esters from Oryza sativa Roots and Their Tyrosinase Inhibition Activity
Cho, J., Cha, B., Seo, W. D., Jeong, R., Shrestha, S., Kim, J.-Y., Kang, H., & Baek, N. (2015) · Chemistry of Natural Compounds · doi:10.1007/s10600-015-1500-8 · Cited by 17
Jeong, H.-J., Lee, C. S., Choi, J., Hong, Y. D., Shin, S. S., Park, J. S., Lee, J. H., Lee, S., Yoon, K. D., & Ko, J. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.12.082 · Cited by 17
Extract from Ceratonia siliqua Exhibits Depigmentation Properties
Lall, N., Kishore, N., Momtaz, S., Hussein, A. A., Naidoo, S., Nqephe, M., & Crampton, B. G. (2015) · Phytotherapy Research · doi:10.1002/ptr.5420 · Cited by 17
Luyen, B. T. T., Thảo, N. P., Widowati, W., Fauziah, N., Maesaroh, M., Herlina, T., & Kim, Y. H. (2016) · Medicinal Chemistry Research · doi:10.1007/s00044-016-1735-3 · Cited by 17
Flagged first, then by citations
Research works printed but not linked: 2
- Vanitha, 2017, Isolation and characterisation of mushroom tyrosinase and screening of herbal extracts for anti-tyrosinase activity, Int. J. ChemTech Res., 10, 1156
- Bourquelot, 1895, La laccase dans les champignons, Compt. Rendus., 121, 783
Cited by
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Panzella, L., Moccia, F., Nasti, R., Marzorati, S., Verotta, L., & Napolitano, A. (2020) · Frontiers in Nutrition · doi:10.3389/fnut.2020.00060 · Cited by 448
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Metadata
- Authors
- Panzella, L., & Napolitano, A.
- Affiliations
- University of Naples Federico II (IT)
- Corresponding author
- Panzella, Lucia
- Venue
- Cosmetics
- Publisher
- MDPI AG
- Published
- 2019-10-01
- Volume
- 6
- Issue
- 4
- Pages
- 57
- ISSN
- 2079-9284 (ISSN-L)
- OpenAlex
- W2977872445
- Cited by
- 208
- References
- 245
- Citations by year
- 2026: 16 · 2025: 32 · 2024: 38 · 2023: 44 · 2022: 36 · 2021: 26 · 2020: 16
- FWCI
- 10.32
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- Cosmetics (publishedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › melanin and skin pigmentation
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Bioactive natural compounds
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- tyrosinase inhibitors, hyperpigmentation, melanogenesis, phenolic compounds, chalcones, flavonoids, hydroxystilbenes, resveratrol derivatives, Moraceae, hydroxycinnamic acids, copper chelation, enzyme inhibition mechanism, bioavailability
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