Natural and Bioinspired Phenolic Compounds as Tyrosinase Inhibitors for the Treatment of Skin Hyperpigmentation: Recent Advances

The Protective Role of Melanin Against UV Damage in Human Skin ^†

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An Updated Review of Tyrosinase Inhibitors

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A comprehensive review on tyrosinase inhibitors

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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 · see citing works

Crystal Structure of <i>Agaricus bisporus</i> Mushroom Tyrosinase: Identity of the Tetramer Subunits and Interaction with Tropolone

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 · see citing works

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 · see citing works

THE CHEMISTRY OF MELANIN

Mason, H. S. (1948) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35614-x · Cited by 621 · see citing works

A Chemist's View of Melanogenesis

Ito, S. (2003) · Pigment Cell Research · doi:10.1034/j.1600-0749.2003.00037.x · Cited by 508 · see citing works

Tyrosinase: The four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation

Ramsden, C. A., & Riley, P. A. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.02.048 · Cited by 368 · see citing works

New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins

Olivares, C., & Solano, F. (2009) · Pigment Cell &amp; Melanoma Research · doi:10.1111/j.1755-148x.2009.00636.x · Cited by 312 · see citing works

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 · see citing works

The Tyrosinase-tyrosine Reaction

Raper, H. S. (1927) · Biochemical Journal · doi:10.1042/bj0210089 · Cited by 308 · see citing works

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 294 · see citing works

A new enzymatic function in the melanogenic pathway. The 5,6-dihydroxyindole-2-carboxylic acid oxidase activity of tyrosinase-related protein-1 (TRP1).

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 · see citing works

Inhibition of Human Tyrosinase Requires Molecular Motifs Distinctively Different from Mushroom Tyrosinase

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 · see citing works

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 · see citing works

Bioactive Constituents of<i>Glycyrrhiza uralensis</i>(Licorice): Discovery of the Effective Components of a Traditional Herbal Medicine

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 · see citing works

Melanocytes and Their DiseasesPreprint

Yamaguchi, Y., & Hearing, V. J. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a017046 · Cited by 240 · see citing works

The patterns of melanosome distribution in keratinocytes of human skin as one determining factor of skin colour

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 · see citing works

Upregulation of Melanogenesis and Tyrosinase Activity: Potential Agents for Vitiligo

Niu, C., & Aisa, H. A. (2017) · Molecules · doi:10.3390/molecules22081303 · Cited by 186 · see citing works

The antityrosinase and antioxidant activities of flavonoids dominated by the number and location of phenolic hydroxyl groups

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 · see citing works

Discovery of Highly Potent Tyrosinase Inhibitor, T1, with Significant Anti-Melanogenesis Ability by zebrafish in vivo Assay and Computational Molecular Modeling

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 · see citing works

Functionalized Carbon Quantum Dots with Dopamine for Tyrosinase Activity Monitoring and Inhibitor Screening: In Vitro and Intracellular Investigation

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 · see citing works

Effective Tyrosinase Inhibition by Thiamidol Results in Significant Improvement of Mild to Moderate Melasma

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 · see citing works

Melanins and Melanosomes

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“Fifty Shades” of Black and Red or How Carboxyl Groups Fine Tune Eumelanin and Pheomelanin Properties

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 · see citing works

Condensed 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 · see citing works

Melanogenesis Inhibitors

Kumari, S., Thng, S. T. G., Verma, N. K., & Gautam, H. (2018) · Acta Dermato Venereologica · doi:10.2340/00015555-3002 · Cited by 134 · see citing works

Effect of apigenin-7-glucoside, genkwanin and naringenin on tyrosinase activity and melanin synthesis in B16F10 melanoma cells

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 · see citing works

Characterization of glabridin/hydroxypropyl-β-cyclodextrin inclusion complex with robust solubility and enhanced bioactivity

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 · see citing works

On the Metal Cofactor in the Tyrosinase Family

Solano, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020633 · Cited by 118 · see citing works

Acquired hyperpigmentations

Cestari, T. F., Dantas, L. D. P., & Boza, J. C. (2014) · Anais Brasileiros de Dermatologia · doi:10.1590/abd1806-4841.20142353 · Cited by 104 · see citing works

Skin targeting of curcumin solid lipid nanoparticles-engrossed topical gel for the treatment of pigmentation and irritant contact dermatitis

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 · see citing works

Synthesis, kinetic mechanism and docking studies of vanillin derivatives as inhibitors of mushroom tyrosinase

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 · see citing works

Melanosome Distribution in Keratinocytes in Different Skin Types: Melanosome Clusters Are Not Degradative Organelles

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 · see citing works

Tyrosinase inhibitory constituents from a polyphenol enriched fraction of rose oil distillation wastewater

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 · see citing works

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 · see citing works

Skin Delivery and in Vitro Biological Evaluation of Trans-Resveratrol-Loaded Solid Lipid Nanoparticles for Skin Disorder Therapies

Rigon, R. B., Fachinetti, N., Severino, P. B., Santana, M. H. A., & Chorilli, M. (2016) · Molecules · doi:10.3390/molecules21010116 · Cited by 95 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 87 · see citing works

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 · see citing works

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 82 · see citing works

Biochemical Characterization of Ferulic Acid and Caffeic Acid Which Effectively Inhibit Melanin Synthesis via Different Mechanisms in B16 Melanoma Cells

Maruyama, H., Kawakami, F., Lwin, T., Imai, M., & Shamsa, F. (2018) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00892 · Cited by 81 · see citing works

Pigmentation Disorders: Diagnosis and Management.

Plensdorf, S., Livieratos, M., & Dada, N. (2017) · PubMed · Cited by 81 · see citing works

Biophenols: Enzymes (β-secretase, Cholinesterases, histone deacetylase and tyrosinase) inhibitors from olive (Olea europaea L.)

Omar, S. H., Scott, C., Hamlin, A. S., & Obied, H. K. (2018) · Fitoterapia · doi:10.1016/j.fitote.2018.05.011 · Cited by 80 · see citing works

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 · see citing works

Kinetic and in silico studies of novel hydroxy-based thymol analogues as inhibitors of mushroom tyrosinase

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 · see citing works

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 · see citing works

Avocado Proanthocyanidins as a Source of Tyrosinase Inhibitors: Structure Characterization, Inhibitory Activity, and Mechanism

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 · see citing works

Molecular docking studies and biological evaluation of chalcone based pyrazolines as tyrosinase inhibitors and potential anticancer agents

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 · see citing works

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 · see citing works

Structure of Melanins

Ito, S., Wakamatsu, K., d’Ischia, M., Napolitano, A., & Pezzella, A. (2011) · doi:10.1002/9783527636150.ch6 · Cited by 74 · see citing works

Anti-melanogenesis properties of condensed tannins from Vigna angularis seeds with potent antioxidant and DNA damage protection activities

Chai, 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 · see citing works

Synthesis of cinnamic amide derivatives and their anti-melanogenic effect in α-MSH-stimulated B16F10 melanoma cells

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 · see citing works

Tyrosinase 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 · see citing works

Carvacrol derivatives as mushroom tyrosinase inhibitors; synthesis, kinetics mechanism and molecular docking studies

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 · see citing works

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 70 · see citing works

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 · see citing works

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 &amp; Medicinal Chemistry · doi:10.1016/j.bmc.2017.05.009 · Cited by 68 · see citing works

Characterization of a New Flavone and Tyrosinase Inhibition Constituents from the Twigs of Morus alba L.

Zhang, L., Tao, G., Chen, J., & Zheng, Z. (2016) · Molecules · doi:10.3390/molecules21091130 · Cited by 67 · see citing works

Sesquiterpenoids and 2-(2-phenylethyl)chromones respectively acting as α-glucosidase and tyrosinase inhibitors from agarwood of an Aquilaria plant

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 · see citing works

New insights into highly potent tyrosinase inhibitors based on 3-heteroarylcoumarins: Anti-melanogenesis and antioxidant activities, and computational molecular modeling studies

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 · see citing works

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 · see citing works

Antityrosinase and antioxidant properties of mung bean seed proanthocyanidins: Novel insights into the inhibitory mechanism

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 · see citing works

Inhibition of tyrosinase by cherimoya pericarp proanthocyanidins: Structural characterization, inhibitory activity and mechanism

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 · see citing works

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 · see citing works

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 · see citing works

A convenient screening method to differentiate phenolic skin whitening tyrosinase inhibitors from leukoderma-inducing phenols

Ito, S., & Wakamatsu, K. (2015) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2015.07.007 · Cited by 62 · see citing works

Integrated study of the mechanism of tyrosinase inhibition by baicalein using kinetic, multispectroscopic and computational simulation analyses

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 62 · see citing works

Cyanidin-3-O-glucoside inhibits different enzymes involved in central nervous system pathologies and type-2 diabetes

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 · see citing works

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 · see citing works

Isolation of Flavonoids and Flavonoid Glycosides from Myrsine africana and Their Inhibitory Activities against Mushroom Tyrosinase

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 · see citing works

Design, synthesis and evaluation of cinnamic acid ester derivatives as mushroom tyrosinase inhibitors

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 · see citing works

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 57 · see citing works

Isoorientin derived from Gentiana veitchiorum Hemsl. flowers inhibits melanogenesis by down-regulating MITF-induced tyrosinase expression

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 · see citing works

Identification of tyrosinase specific inhibitors from Xanthium strumarium fruit extract using ultrafiltration-high performance liquid chromatography

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 · see citing works

Plumbagin Suppresses α-MSH-Induced Melanogenesis in B16F10 Mouse Melanoma Cells by Inhibiting Tyrosinase Activity

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 · see citing works

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 · see citing works

Correlation between the Potency of Flavonoids on Mushroom Tyrosinase Inhibitory Activity and Melanin Synthesis in Melanocytes

Promden, W., Viriyabancha, W., Monthakantirat, O., Umehara, K., Noguchi, H., & De‐Eknamkul, W. (2018) · Molecules · doi:10.3390/molecules23061403 · Cited by 54 · see citing works

A Potent Tyrosinase Inhibitor, (E)-3-(2,4-Dihydroxyphenyl)-1-(thiophen-2-yl)prop-2-en-1-one, with Anti-Melanogenesis Properties in α-MSH and IBMX-Induced B16F10 Melanoma Cells

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 · see citing works

The tyrosinase inhibitory effects of isoxazolone derivatives with a (Z)-β-phenyl-α, β-unsaturated carbonyl scaffold

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 · see citing works

Screening of tyrosinase inhibitors by capillary electrophoresis with immobilized enzyme microreactor and molecular docking

Cheng, M., & Chen, Z. (2016) · Electrophoresis · doi:10.1002/elps.201600367 · Cited by 52 · see citing works

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 · see citing works

Development of highly potent melanogenesis inhibitor by in vitro, in vivo and computational studies

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Identification of Anti-Melanogenesis Constituents from Morus alba L. Leaves

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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 · see citing works

Proanthocyanidins Extracted from Rhododendron pulchrum Leaves as Source of Tyrosinase Inhibitors: Structure, Activity, and Mechanism

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Inhibitory kinetics of novel 2,3-dihydro-1H-inden-1-one chalcone-like derivatives on mushroom tyrosinase

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 · see citing works

Anti-Melanogenic Potentials of Nanoparticles from Calli of Resveratrol-Enriched Rice against UVB-Induced Hyperpigmentation in Guinea Pig Skin

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 · see citing works

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 · see citing works

Design, synthesis, and antimelanogenic effects of (2-substituted phenyl-1,3-dithiolan-4-yl)methanol derivatives

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 · see citing works

6-Methoxy-3,4-dihydronaphthalenone Chalcone-like Derivatives as Potent Tyrosinase Inhibitors and Radical Scavengers

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 · see citing works

(2E,5E)-2,5-Bis(3-hydroxy-4-methoxybenzylidene) cyclopentanone Exerts Anti-Melanogenesis and Anti-Wrinkle Activities in B16F10 Melanoma and Hs27 Fibroblast Cells

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 · see citing works

Spinosin is a flavonoid in the seed of Ziziphus jujuba that prevents skin pigmentation in a human skin model

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 · see citing works

Hair Dyes Resorcinol and Lawsone Reduce Production of Melanin in Melanoma Cells by Tyrosinase Activity Inhibition and Decreasing Tyrosinase and Microphthalmia-Associated Transcription Factor (MITF) Expression

Lee, S.-M., Chen, Y.-S., Lin, C., & Chen, K.-H. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16011495 · Cited by 22 · see citing works

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 · see citing works

Conjugation with Dihydrolipoic Acid Imparts Caffeic Acid Ester Potent Inhibitory Effect on Dopa Oxidase Activity of Human Tyrosinase

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 · see citing works

3-hydroxycoumarin loaded vesicles for recombinant human tyrosinase inhibition in topical applications

Schlich, 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 · see citing works

β-Lactoglobulin Peptide Fragments Conjugated with Caffeic Acid Displaying Dual Activities for Tyrosinase Inhibition and Antioxidant Effect

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 · see citing works

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 · see citing works

Anti-melanogenesis and antigenotoxic activities of eriodictyol in murine melanoma (B16-F10) and primary human keratinocyte cells

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 · see citing works

Identification of 3′-hydroxygenistein as a potent melanogenesis inhibitor from biotransformation of genistein by recombinant Pichia pastoris

Ding, H., Chiang, C.-M., Tzeng, W.-M., & Chang, T. (2015) · Process Biochemistry · doi:10.1016/j.procbio.2015.06.007 · Cited by 20 · see citing works

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 · see citing works

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 · see citing works

Integrated kinetic studies and computational analysis on naphthyl chalcones as mushroom tyrosinase inhibitors

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 · see citing works

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 · see citing works

Magnetic solid-phase extraction coupled with HPLC-Q-TOF-MS for rapid analysis of tyrosinase binders from San-Bai decoction by Box–Behnken statistical design

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 · see citing works

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 · see citing works

Phenolic compounds from the leaves of Breynia officinalis and their tyrosinase and melanogenesis inhibitory activities

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 · see citing works

Mushroom Tyrosinase-Based Enzyme Inhibition Assays Are Not Suitable for Bioactivity-Guided Fractionation of Extracts

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 18 · see citing works

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 · see citing works

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 · see citing works

Molecular design of potent, hydrophilic tyrosinase inhibitors based on the natural dihydrooxyresveratrol skeleton

Tanaka, Y., Suzuki, M. S., Kodachi, Y., & Nihei, K. (2018) · Carbohydrate Research · doi:10.1016/j.carres.2018.11.006 · Cited by 18 · see citing works

Structure Elucidation and Evaluation of Antioxidant and Tyrosinase Inhibitory Effect and Mechanism of Proanthocyanidins from Leaf and Fruit of Leucaena Leucocephala

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 · see citing works

Evaluation of the Structure and Biological Activities of Condensed Tannins from Acanthus ilicifolius Linn and Their Effect on Fresh-Cut Fuji Apples

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 · see citing works

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 · see citing works

Flavokawains B and C, melanogenesis inhibitors, isolated from the root of Piper methysticum and synthesis of analogs

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 · see citing works

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 · see citing works

Chemical constituents of Piper aduncum and their inhibitory effects on soluble epoxide hydrolase and tyrosinase

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 · see citing works

Bioactive Phenolic Compounds From Agri-Food Wastes: An Update on Green and Sustainable Extraction Methodologies

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 · see citing works

Skin Pigmentation Types, Causes and Treatment—A Review

Thawabteh, A. M., Jibreen, A., Karaman, D., Thawabteh, A., & Karaman, R. (2023) · Molecules · doi:10.3390/molecules28124839 · Cited by 233 · see citing works

Natural and synthetic flavonoid derivatives as new potential tyrosinase inhibitors: a systematic review

Obaid, R. J., Mughal, E. U., Naeem, N., Sadiq, A., Alsantali, R. I., Jassas, R. S., Moussa, Z., & Ahmed, S. A. (2021) · RSC Advances · doi:10.1039/d1ra03196a · Cited by 200 · see citing works

Recent Advances in Research on Polyphenols: Effects on Microbiota, Metabolism, and Health

Rajha, H. N., Paule, A., Aragonès, G., Barbosa, M., Caddeo, C., Debs, E., Dinkova, R., Eckert, G. P., Fontana, A., Gebrayel, P., et al. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202100670 · Cited by 96 · see citing works

Licorice (Glycyrrhiza glabra, G. uralensis, and G. inflata) and Their Constituents as Active Cosmeceutical Ingredients

Cerulli, A., Masullo, M., Montoro, P., & Piacente, S. (2022) · Cosmetics · doi:10.3390/cosmetics9010007 · Cited by 83 · see citing works

Natural tyrosinase enzyme inhibitors: A path from melanin to melanoma and its reported pharmacological activities

Logesh, R., Prasad, S. R., Chipurupalli, S., Robinson, N., & Mohankumar, S. K. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188968 · Cited by 89 · see citing works

Green synthesis of silver nanoparticles using aqueous extracts of three Sideritis species from Turkey and evaluations bioactivity potentials

Ceylan, R., Demırbas, A., Öçsoy, İ., & Aktümsek, A. (2021) · Sustainable Chemistry and Pharmacy · doi:10.1016/j.scp.2021.100426 · Cited by 71 · see citing works

Natural Phenolic Compounds for Health, Food and Cosmetic Applications

Panzella, L. (2020) · Antioxidants · doi:10.3390/antiox9050427 · Cited by 68 · see citing works

Condensed Tannins, a Viable Solution To Meet the Need for Sustainable and Effective Multifunctionality in Food Packaging: Structure, Sources, and Properties

Panzella, L., & Napolitano, A. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c07229 · Cited by 67 · see citing works

A Melanin-Related Phenolic Polymer with Potent Photoprotective and Antioxidant Activities for Dermo-Cosmetic Applications

Liberti, D., Alfieri, M. L., Monti, D. M., Panzella, L., & Napolitano, A. (2020) · Antioxidants · doi:10.3390/antiox9040270 · Cited by 62 · see citing works

Metabolomic Profile and Antioxidant/Anti-Inflammatory Effects of Industrial Hemp Water Extract in Fibroblasts, Keratinocytes and Isolated Mouse Skin Specimens

di Giacomo, V., Recinella, L., Chiavaroli, A., Orlando, G., Cataldi, A., Rapino, M., Valerio, V. D., Politi, M., Antolini, M. D., Acquaviva, A., et al. (2021) · Antioxidants · doi:10.3390/antiox10010044 · Cited by 57 · see citing works

Phenolic Compounds and Antioxidant Capacity of Sea Cucumber (Cucumaria frondosa) Processing Discards as Affected by High-Pressure Processing (HPP)

Hossain, A., Yeo, J., Dave, D., & Shahidi, F. (2022) · Antioxidants · doi:10.3390/antiox11020337 · Cited by 57 · see citing works

Structure and inhibition mechanism of some synthetic compounds and phenolic derivatives as tyrosinase inhibitors: review and new insight

Vaezi, M. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2069157 · Cited by 57 · see citing works

Dermal Drug Delivery of Phytochemicals with Phenolic Structure via Lipid-Based Nanotechnologies

Gugleva, V., Ivanova, N. A., Sotirova, Y., & Andonova, V. (2021) · Pharmaceuticals · doi:10.3390/ph14090837 · Cited by 54 · see citing works

Pecan (Carya illinoinensis (Wagenh.) K. Koch) Nut Shell as an Accessible Polyphenol Source for Active Packaging and Food Colorant Stabilization

Moccia, F., Salazar, S. A., Berg, A.-L., Setaro, B., Micillo, R., Pizzo, E., Weber, F., Gámez‐Meza, N., Schieber, A., Cerruti, P., et al. (2020) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.0c00356 · Cited by 48 · see citing works

Antioxidant Properties of Agri-Food Byproducts and Specific Boosting Effects of Hydrolytic Treatments

Moccia, F., Salazar, S. A., Verotta, L., Caneva, E., Giovando, S., D’Errico, G., Panzella, L., d’Ischia, M., & Napolitano, A. (2020) · Antioxidants · doi:10.3390/antiox9050438 · Cited by 47 · see citing works

Hyperpigmentation: Looking beyond hydroquinone

Charoo, N. A. (2022) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.14746 · Cited by 44 · see citing works

Antioxidant and Tyrosinase Inhibitory Properties of an Aqueous Extract of Garcinia atroviridis Griff. ex. T. Anderson Fruit Pericarps

Chatatikun, M., Supjaroen, P., Promlat, P., Chantarangkul, C., Waranuntakul, S., Nawarat, J., Tangpong, J., & Chiabchalard, A. (2020) · Pharmacognosy Journal · doi:10.5530/pj.2020.12.12 · Cited by 41 · see citing works

Anti-tyrosinase and antioxidant activity of meroterpene bakuchiol from Psoralea corylifolia (L.)

Cariola, A., Chami, M. E., Granatieri, J., & Valgimigli, L. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.134953 · Cited by 39 · see citing works

Evaluation of bioactive constituents of Garcinia indica (kokum) as a potential source of hydroxycitric acid, anthocyanin, and phenolic compounds

Singh, P., Roy, T. K., Chaturvedi, K., Tripathi, P. C., Kumar, P., & Shivashankara, K. S. (2021) · LWT · doi:10.1016/j.lwt.2021.112999 · Cited by 39 · see citing works

Analysis of Kojic Acid Derivatives as Competitive Inhibitors of Tyrosinase: A Molecular Modeling Approach

Cardoso, R., Valente, R. P. D. P., da Costa, C. H. S., Júnior, J. L. D. S. G. V., da Costa, K. S., de Molfetta, F. A., & Alves, C. N. (2021) · Molecules · doi:10.3390/molecules26102875 · Cited by 36 · see citing works

The UHPLC-QTOF-MS Phenolic Profiling and Activity of Cydonia oblonga Mill. Reveals a Promising Nutraceutical Potential

Zhang, L., Rocchetti, G., Zengin, G., Ak, G., Saber, F. R., Montesano, D., & Lucini, L. (2021) · Foods · doi:10.3390/foods10061230 · Cited by 35 · see citing works

Determination of Phenolic Content, Antioxidant Activity, and Tyrosinase Inhibitory Effects of Functional Cosmetic Creams Available on the Thailand Market

Mapoung, S., Semmarath, W., Arjsri, P., Umsumarng, S., Srisawad, K., Thippraphan, P., Yodkeeree, S., & Limtrakul, P. (2021) · Plants · doi:10.3390/plants10071383 · Cited by 40 · see citing works

Phenolic profiles of Atlantic sea cucumber (Cucumaria frondosa) tentacles and their biological properties

Hossain, A., Senadheera, T. R. L., Dave, D., & Shahidi, F. (2022) · Food Research International · doi:10.1016/j.foodres.2022.112262 · Cited by 35 · see citing works

Simultaneous loading of (−)-epigallocatechin gallate and ferulic acid in chitosan-based nanoparticles as effective antioxidant and potential skin-whitening agents

Li, G., Lee, Y., Lu, X., Chen, J., Liu, N., Qiu, C., & Wang, Y. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.07.242 · Cited by 31 · see citing works

Emergent properties of melanin-inspired peptide/RNA condensates

Netzer, A., Katzir, I., Leshem, A. B., Weitman, M., & Lampel, A. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2310569120 · Cited by 29 · see citing works

Determination of tyrosinase-cyanidin-3-O-glucoside and (−/+)-catechin binding modes reveal mechanistic differences in tyrosinase inhibition

Lee, K. E., Bharadwaj, S., Sahoo, A. K., Yadava, U., & Kang, S. G. (2021) · Scientific Reports · doi:10.1038/s41598-021-03569-1 · Cited by 31 · see citing works

Origanum syriacum Phytochemistry and Pharmacological Properties: A Comprehensive Review

Mesmar, J. E., Abdallah, R., Badran, A., Maresca, M., & Baydoun, E. (2022) · Molecules · doi:10.3390/molecules27134272 · Cited by 29 · see citing works

Utilization of the zebrafish model to unravel the harmful effects of biomass burning during Amazonian wildfires

Babić, S., Čižmek, L., Maršavelski, A., Malev, O., Pflieger, M., Strunjak‐Perović, I., Popović, N. T., Čož‐Rakovac, R., & Trebše, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-81789-1 · Cited by 28 · see citing works

Cosmeceuticals: A Newly Expanding Industry in South Africa

Gebashe, F. C., Naidoo, D., Amoo, S. O., & Masondo, N. A. (2022) · Cosmetics · doi:10.3390/cosmetics9040077 · Cited by 31 · see citing works

From by-products to new application opportunities: the enhancement of the leaves deriving from the fruit plants for new potential healthy products

Regolo, L., Giampieri, F., Battino, M. A., Díaz, Y. A., Mezzetti, B., Elexpuru-Zabaleta, M., Pérez-Oleaga, C. M., Pifarré, K. T., & Mazzoni, L. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1083759 · Cited by 34 · see citing works

Harnessing the chemical composition and anti-oxidant, anti-enzymatic, and anti-cancer activities of two Corydalis species (C. erdelii and C. solida) by using in vitro and in silico analysis

Duran, T., Peron, G., Zancato, M., Zengin, G., Çetiz, M. V., Bouyahya, A., Ahmed, S., Yıldıztugay, E., Dall’Acqua, S., Kljakić, A. C., et al. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.104762 · Cited by 27 · see citing works

Comprehensive bioactivity and chemical characterization of the endemic plant Scorzonera hieraciifolia Hayek extracts: A promising source of bioactive compounds

Dall’Acqua, S., Ak, G., Sut, S., Zengin, G., Yıldıztugay, E., Mahomoodally, M. F., Sinan, K. I., & Lobine, D. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109371 · Cited by 27 · see citing works

Pickering emulsions stabilized by chitosan-flaxseed gum-hyaluronic acid nanoparticles for controlled topical release of ferulic acid

Li, G., Li, J., Lee, Y., Qiu, C., Zeng, X., & Wang, Y. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128086 · Cited by 26 · see citing works

Antioxidant activity, anti-tyrosinase activity, molecular docking studies, and molecular dynamic simulation of active compounds found in nipa palm vinegar

Chatatikun, M., Tedasen, A., Pattaranggoon, N. C., Palachum, W., Chuaijit, S., Mudpan, A., Pruksaphanrat, S., Sohbenalee, S., Yamasaki, K., & Klangbud, W. K. (2023) · PeerJ · doi:10.7717/peerj.16494 · Cited by 25 · see citing works

Effects of Maturity and Thermal Treatment on Phenolic Profiles and In Vitro Health-Related Properties of Sacha Inchi Leaves

Kittibunchakul, S., Hudthagosol, C., Sanporkha, P., Sapwarobol, S., Suttisansanee, U., & Sahasakul, Y. (2022) · Plants · doi:10.3390/plants11111515 · Cited by 24 · see citing works

Antioxidant and anti-tyrosinase activities of quercetin-loaded olive oil nanoemulsion as potential formulation for skin hyperpigmentation

Silva, C. C., Benati, R. B., Massaro, T. N. C., Pereira, K. C., Gaspar, L. R., & Marcato, P. D. (2022) · Journal of Dispersion Science and Technology · doi:10.1080/01932691.2022.2116715 · Cited by 23 · see citing works

Tripeptides conjugated with thiosemicarbazones: new inhibitors of tyrosinase for cosmeceutical use

Ledwoń, P., Goldeman, W., Hałdys, K., Jewgiński, M., Calamai, G., Rossowska, J., Papini, A. M., Rovero, P., & Latajka, R. (2023) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2023.2193676 · Cited by 23 · see citing works

Tyrosinase Inhibition and Kinetic Details of Puerol A Having But-2-Enolide Structure from Amorpha fruticosa

Kim, J. H., Jang, D. H., Lee, K. W., Kim, K. D., Shah, A. B., Zhumanova, K., & Park, K. H. (2020) · Molecules · doi:10.3390/molecules25102344 · Cited by 23 · see citing works

Flavonoid Glycosides from Ziziphus jujuba var. inermis (Bunge) Rehder Seeds Inhibit α-Melanocyte-Stimulating Hormone-Mediated Melanogenesis

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In silico and in vitro studies of novel derivatives of tyrosol and raspberry ketone as the mushroom tyrosinase inhibitors

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