Academic literature on the topic 'Tyrosinase activity'

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Journal articles on the topic "Tyrosinase activity"

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Suwunwong, T., T. Kobkeatthawin, K. Chanawanno, N. Saewan, P. Wisitsak, and Suchada Chantrapromma. "Tyrosinase Inhibitory Activity of Pyrazole Derivatives." Advanced Materials Research 506 (April 2012): 194–97. http://dx.doi.org/10.4028/www.scientific.net/amr.506.194.

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A series of 3,5-substituted-4,5-dihydro-1H-pyrazole-1-carbothioamide derivatives were synthesized. Their structures were determined on the basis of spectroscopic data interpretation and their tyrosinase inhibitory activity was determined. The results showed that compound 2 (at 1.00 mg/mL) exhibits significant tyrosinase inhibitory activity with % inhibition of 91.866 ± 2.086 with L-tyrosine as substrate whereas compound 3 (at 1.00 mg/mL) exhibits significant tyrosinase inhibitory activity with % inhibition of 79.266 ± 0.552 and 89.593 ± 1.015 with L-tyrosine and L-DOPA as substrates. The IC50v
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Kwak, Jung-Hoon, and Yeong-Hwan Han. "Tyrosinase Inhibitory Activity of Macrolepiota procera." Korean Journal of Mycology 38, no. 2 (2010): 202–4. http://dx.doi.org/10.4489/kjm.2010.38.2.202.

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Lopez-Tejedor, David, Rafael Claveria-Gimeno, Adrian Velazquez-Campoy, Olga Abian, and Jose M. Palomo. "In Vitro Antiviral Activity of Tyrosinase from Mushroom Agaricus bisporus against Hepatitis C Virus." Pharmaceuticals 14, no. 8 (2021): 759. http://dx.doi.org/10.3390/ph14080759.

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Tyrosinases from a commercial Agaricus bisporus protein extract and directly isolated from white mushrooms were purified in order to obtaining the well-known tyrosinase from A. bisporus (TyrAB) of 45 kDa and a newly discovered 50 kDa tyrosinase isoform (Tyr50 kDa), and tested showing high antiviral activity against the hepatitis C virus for the first time. Cell toxicity and antiviral activity of tyrosinases were determined in cultured Huh 5-2 liver tumor cells transfected with a replicon system (a plasmid that includes all non-structural hepatitis C virus proteins and replicates autonomously).
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Lee, Sanggwon, Heejeong Choi, Yujin Park, et al. "Urolithin and Reduced Urolithin Derivatives as Potent Inhibitors of Tyrosinase and Melanogenesis: Importance of the 4-Substituted Resorcinol Moiety." International Journal of Molecular Sciences 22, no. 11 (2021): 5616. http://dx.doi.org/10.3390/ijms22115616.

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We previously reported (E)-β-phenyl-α,β-unsaturated carbonyl scaffold ((E)-PUSC) played an important role in showing high tyrosinase inhibitory activity and that derivatives with a 4-substituted resorcinol moiety as the β-phenyl group of the scaffold resulted in the greatest tyrosinase inhibitory activity. To examine whether the 4-substituted resorcinol moiety could impart tyrosinase inhibitory activity in the absence of the α,β-unsaturated carbonyl moiety of the (E)-PUSC scaffold, 10 urolithin derivatives were synthesized. To obtain more candidate samples, the lactone ring in synthesized urol
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Schallreuter-Wood, Karin U., and John M. Wood. "Control of Melanogenesis In the Human Epidermis by the Redox-Status of Tetrahydrobiopterins." Pteridines 6, no. 3 (1995): 101–3. http://dx.doi.org/10.1515/pteridines.1995.6.3.101.

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Summary Activity of tyrosinase directly controls melanogenesis in the human epidermis. Recently, it has been shown that the biosynthesis and recycling of (6R)L-erythro 5,6,7,8 tetrahydrobiopterin (6-BH4) plays a central role in regulating the supply of L-tyrosine, the substrate for tyrosinase. In this report, we present evidence that 6-BH4 and other tetrahydropterins, have the capacity to regulate tyrosinase activity directly by a specific uncompetitive mechanism. This fine control of tyrosinase activity/melanogenesis in the human epiidermis depends on the redox equilibrium 6-BH4 ↔ dihydropter
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Song, Hanbit, Pyung-Gang Lee, Hyun Kim, et al. "Polyphenol-Hydroxylating Tyrosinase Activity under Acidic pH Enables Efficient Synthesis of Plant Catechols and Gallols." Microorganisms 9, no. 9 (2021): 1866. http://dx.doi.org/10.3390/microorganisms9091866.

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Tyrosinase is generally known as a melanin-forming enzyme, facilitating monooxygenation of phenols, oxidation of catechols into quinones, and finally generating biological melanin. As a homologous form of tyrosinase in plants, plant polyphenol oxidases perform the same oxidation reactions specifically toward plant polyphenols. Recent studies reported synthetic strategies for large scale preparation of hydroxylated plant polyphenols, using bacterial tyrosinases rather than plant polyphenol oxidase or other monooxygenases, by leveraging its robust monophenolase activity and broad substrate speci
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Xiu-Hua, Jia, Lin Shao-Chun, Huang Bing, et al. "Tyrosinase Small Interfering RNA Effectively Suppresses Tyrosinase Gene Expression In Vitro and In Vivo." Molecular Biology International 2010 (November 4, 2010): 1–6. http://dx.doi.org/10.4061/2010/240472.

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Tyrosinase is a bifunctional enzyme which oxidizes the initial step of melanin biosynthesis, that is, conversion of tyrosine to dopa and subsequently dopa to dopaquinone. It is a glycosylated protein and a major regulator of melanogenesis. To date, many approaches have been tried to regulate tyrosinase activity and melanin content. To that end, we screened small interfering RNA sequences for sequence-inhibited tyrosinase expression in B16 cells and in C57BL/6 mice. We analyzed tyrosinase mRNA levels by quantitative real-time PCR and determined tyrosinase activity and melanin content at 24, 48,
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Pintus, Francesca, Delia Spanò, Angela Corona, and Rosaria Medda. "Antityrosinase activity ofEuphorbia characiasextracts." PeerJ 3 (October 13, 2015): e1305. http://dx.doi.org/10.7717/peerj.1305.

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Tyrosinase is a well-known key enzyme in melanin biosynthesis and its inhibitors have become increasingly important because of their potential use as hypopigmenting agents. In the present study, the anti-melanogenic effect of aqueous and ethanolic extracts fromEuphorbia characiasleaves, stems, and flowers in cell-free and cellular systems was examined. All the extracts showed inhibitory effects against mushroom tyrosinase with leaf extracts exhibiting the lowest IC50values of 24 and 97 µg/mL for aqueous and ethanolic extracts respectively. Enzyme kinetic analysis indicated that leaf aqueous ex
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Manandhar, Wagle, Seong, et al. "Phlorotannins with Potential Anti-tyrosinase and Antioxidant Activity Isolated from the Marine Seaweed Ecklonia stolonifera." Antioxidants 8, no. 8 (2019): 240. http://dx.doi.org/10.3390/antiox8080240.

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Compounds were isolated from Ecklonia stolonifera Okamura, a marine brown alga widely consumed as food. Among the isolated compounds, 974-A was demonstrated for the first time to be a potent competitive inhibitor of mushroom tyrosinase activity towards l-tyrosine and l-DOPA (IC50 values = 1.57 ± 0.08 and 3.56 ± 0.22 µM, respectively). Molecular docking simulations clarified that the hydroxyl residues of the isolated compounds formed hydrogen bonds with residues at the catalytic and allosteric sites of tyrosinase, while other residues participated in hydrophobic interactions. Moreover, 974-A, p
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OLIVARES, Concepción, Celia JIMÉNEZ-CERVANTES, José Antonio LOZANO, Francisco SOLANO, and José Carlos GARCÍA-BORRÓN. "The 5,6-dihydroxyindole-2-carboxylic acid (DHICA) oxidase activity of human tyrosinase." Biochemical Journal 354, no. 1 (2001): 131–39. http://dx.doi.org/10.1042/bj3540131.

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Melanin synthesis in mammals is catalysed by at least three enzymic proteins, tyrosinase (monophenol dihydroxyphenylalanine:oxygen oxidoreductase, EC 1.14.18.1) and tyrosinase-related proteins (tyrps) 1 and 2, whose genes map to the albino, brown and slaty loci in mice, respectively. Tyrosinase catalyses the rate-limiting generation of l-dopaquinone from l-tyrosine and is also able to oxidize l-dopa to l-dopaquinone. Conversely, mouse tyrp1, but not tyrosinase, catalyses the oxidation of the indolic intermediate 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into the corresponding 5,6-indolequi
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Dissertations / Theses on the topic "Tyrosinase activity"

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Weinel, Allison Clare. "Comparative aspects of tyrosinase activity : purification of human tyrosinase from IGR1 cells and comparison of properties with tyrosinase from Agaricus bisporus." Thesis, Brunel University, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.282921.

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Hossain, Abzal. "Inhibition of tyrosinase activity by metallothionein from Aspergillus niger." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0015/MQ55068.pdf.

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Nkabinde, Nkosana Cyril. "Synthesis and activity of tyrosinase in mouse skin melanocytes." Master's thesis, University of Cape Town, 1990. http://hdl.handle.net/11427/27178.

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Tyrosinase (E.C. 1.14.18.1) is a key enzyme in the biosynthesis of melanin. The control of melanin sythesis was explored in skin melanocytes of the following strains; wild type (C57BL/6J-C/C) (which maximally synthesize melanin at normal mammalian body temperature, Himalayan (C57BL/6J-cʰ/cʰ) (which maximally synthesize melanin at temperatures below 37°C) and albino (Balb c-c/c) (a mutant which does not synthesize melanin) The effect of a-MSH on tyrosinase activity was initially investigated. A skin culture tyrosinase assay that made it possible to measure the effect of α-MSH on the activity of
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Narli, Isil. "Activity Analysis Of Immobilized Tyrosinase In The Presence Of Different Inhibitors." Master's thesis, METU, 2006. http://etd.lib.metu.edu.tr/upload/2/12607238/index.pdf.

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ACTIVITY ANALYSIS OF IMMOBILIZED TYROSINASE ENZYME IN THE PRESENCE OF DIFFERENT INHIBITORS Narli, ISil M.Sc., Department of Chemistry Supervisor: Prof. Dr. Levent Toppare May 2006, 97 pages Immobilization of tyrosinase enzyme was performed in the matrices obtained via copolymerization of terephthalic acid bis-(2-thiophen-3-yl ethyl) ester (TATE) with pyrrole. During electrochemical polymerization of pyrrole, enzyme molecules were entrapped in the copolymer matrice. Activity measurements were performed by using Besthorn&amp<br>#8217<br>s Hydrazone method which includes spectrophotometri
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Seechurn, L. M. P. I. "The regulation of tyrosinase activity in epidermal melanocytes in the mouse." Thesis, University of Newcastle Upon Tyne, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.384020.

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Juneja, Kashmir Singh. "Tyrosinase-like activity of several Alzheimer's disease related and model peptides and their inhibition by natural antioxidants." [Tampa, Fla] : University of South Florida, 2006. http://purl.fcla.edu/usf/dc/et/SFE0001838.

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Msebele, Bongiwe. "Application of Sutherlandia flutescens in cosmetic skin industry (phytochemical fingerprinting and its activity against skin immune diseases." University of the Western Cape, 2019. http://hdl.handle.net/11394/7368.

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>Magister Scientiae - MSc<br>Hyperpigmentation disorders such as melasma, freckles and black-pigmented spots on the surface of the skin are often a result of increased over production and accumulation of melanin pigments in the skin. In melanin biogenesis, tyrosinase is the key enzyme that catalysis the synthesis of melanin, thus the most effective and easiest way to reduce melanin synthesis is by inhibiting tyrosinase. There are a large number of reported tyrosinase inhibitors, their identification and isolation from natural sources is highly important because when natural tyrosinase in
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de, la Torre Jerry James Murillo. "Effect Of Frequency On Polyphenoloxidase Activity During Moderate Electric Field Treatment." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1231859740.

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Schmitt, Marie. "CHAVIC - Valorisation de la flore Champardennaise dans le domaine du vieillissement cutané." Thesis, Reims, 2019. http://www.theses.fr/2019REIMS030.

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Ce travail présente l'étude phytochimique et l’évaluation biologique de neuf plantes récoltées en région Champagne-Ardenne afin de les valoriser dans le traitement du vieillissement cutané. Il s'agit des espèces Agrimonia eupatoria, Geum urbanum (Rosaceae), Colutea arborescens, Hippocrepis emerus, Lotus maritimus (Fabaceae), Equisetum arvense (Equisetaceae), Linaria vulgaris (Scrophulariaceae), Melampyrum sylvaticum (Orobanchaceae) et Prunella vulgaris (Lamiaceae). Les extraits bruts (MeOH, CH2Cl2, AcOEt, n-BuOH) de ces neuf plantes ont été criblés grâce à des tests d'activités antioxydantes (
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Verdoni, Marion. "Identification, caractérisations physico-chimiques et pharmacologiques de nouveaux inhibiteurs de la mélanogenèse isolés à partir de venins d'animaux : exemple de l'Argiotoxine-636." Thesis, Aix-Marseille, 2015. http://www.theses.fr/2015AIXM4720.

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La mélanogenèse engage 3 enzymes. La tyrosinase catalyse l’oxydation des 2 premiers substrats pour former la DOPAquinone. Celle-ci, en présence de cystéine peut s’y conjuguer pour produire des pheomélanines (pigments clairs). En son absence, la DOPAquinone est convertie en DOPAchrome, précurseur de la voie de synthèse des eumélanines (pigments foncés). Leur formation implique deux autres enzymes : TRP-1 et TRP-2. Un dérèglement de ce processus entraîne des dermatoses de type hyperpigmentations chez les phototypes IV à VI. Traiter ces problématiques efficacement sans effets secondaires nécessit
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Books on the topic "Tyrosinase activity"

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Keane, Noeleen Emily. Nuclear magnetic resonance studies of the human insulin receptor tyrosine kinase autophosphorylation and activity. University of Birmingham, 1994.

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Lam, Lily Po Yee. A transforming mutation induces dimerization and enhances activity of the c-kit soluble tyrosine kinase domain. National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Viegas, Muriel. The intrinsic tyrosine kinase activity of the epidermal growth factor receptor is necessary for phospholipase A2 activation. National Library of Canada = Bibliothèque nationale du Canada, 1993.

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Moussa, Raffy Cesario. The effect of seizure activity on tyrosine phosphorylation of the N-methyl-D-aspartate receptor in the hippocampus. National Library of Canada, 2002.

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Alaimo, Darrick James. Hepatic insulin receptor tyrosine kinase activity in diabetes: Modulation by assorted adenosine triphosphatases/phosphatases which copurify in partially purified preparations of the insulin receptor. s.n.], 1992.

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Pelkey, Kenneth A. Regulation of NMDAR function by tyrosine phosphorylation: The role of extracellular zinc and identification of the tyrosine phosphatase step as an endogenous regulator of NMDAR activity. 2002.

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Stafstrom, Carl E., and Thomas P. Sutula. 2-Deoxyglucose. Edited by Dominic P. D’Agostino. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190497996.003.0036.

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Metabolic regulation of excitability is increasingly appreciated as a strategy to control seizures and reduce pathogenesis. Inhibiting or bypassing glycolysis may be one way in which the ketogenic diet suppresses seizures. 2-deoxy-D-glucose (2DG) is a glucose analog that partially inhibits glycolysis and has antiseizure effects in several acute and chronic seizure models. The mechanisms underlying the acute and chronic effects of 2DG are being investigated. Preliminary studies provide evidence that the acute anticonvulsant actions of 2DG involve activity-dependent presynaptic suppression of ex
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Fleischmann, Roy. Signalling pathway inhibitors. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199642489.003.0081.

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Oral, small-molecule signalling pathway inhibitors, including ones that inhibit the JAK and SyK pathways, are currently in development for the treatment of rheumatoid arthritis (RA). Tofacitinib is an orally administered small-molecule inhibitor that targets the intracellular Janus kinase 3 and 1 (JAK1/3) molecules to a greater extent than JAK2 while baricitinib (formerly INCB028050) predominantly inhibits JAK1/2. Many of the proinflammatory cytokines implicated in the pathogenesis of RA utilize cell signalling that involves the JAK-STAT pathways and therefore inhibition of JAK-STAT signalling
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Eisen, Tim. The patient with renal cell cancer. Edited by Giuseppe Remuzzi. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0172.

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Renal cancer is the commonest malignancy of the kidney and worldwide, accounts for between 2% and 3% of the total cancer burden. The mainstay of curative treatment remains surgery. There have been significant advances in surgical technique, the most important ones being nephron-sparing surgery and laparoscopic nephrectomy. The medical treatment of advanced renal cell cancer has only improved markedly in the last decade with the development of antiangiogenic tyrosine-kinase inhibitors, inhibitors of mammalian target of rapamycin, and a diminished role for immunotherapy.Tyrosine-kinase inhibitor
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Book chapters on the topic "Tyrosinase activity"

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Robb, Donald A. "Exploiting Tyrosinase Activity in Aqueous and Nonaqueous Media." In ACS Symposium Series. American Chemical Society, 1995. http://dx.doi.org/10.1021/bk-1995-0600.ch012.

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Company, Anna. "O2 Reactivity at Model Copper Systems: Mimicking Tyrosinase Activity." In Ideas in Chemistry and Molecular Sciences. Wiley-VCH Verlag GmbH & Co. KGaA, 2010. http://dx.doi.org/10.1002/9783527630516.ch11.

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Wilke, Patrick, William L. A. Brooks, Romina Kühnle, Brent Sumerlin, and Hans G. Börner. "Activity Control of Mussel Glue Derived Enzymes: A Study on Thermoresponsive Tyrosinase-PNIPAM Conjugates." In ACS Symposium Series. American Chemical Society, 2012. http://dx.doi.org/10.1021/bk-2012-1101.ch018.

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Kremerskothen, Joachim, and Angelika Barnekow. "Non-radioactive determination of phosphotyrosine phosphatase (PTPase) activity." In Tyrosine Phosphorylation/Dephosphorylation and Downstream Signalling. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78247-3_14.

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Lee, P. L., and G. M. Clinton. "Serum Tyrosine Kinase Activity and Neoplastic Disease." In Endocrine Therapy and Growth Regulation of Breast Cancer. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-83638-1_5.

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Cool, D. E., and J. J. Blum. "Protein tyrosine phosphatase activity in Leishmania donovani." In Reversible Protein Phosphorylation in Cell Regulation. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2600-1_13.

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Walls, Chad, Bo Zhou, and Zhong-Yin Zhang. "Activity-Based Protein Profiling of Protein Tyrosine Phosphatases." In Methods in Molecular Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-281-6_27.

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Tautz, Lutz, and Eduard A. Sergienko. "High-Throughput Screening for Protein Tyrosine Phosphatase Activity Modulators." In Methods in Molecular Biology. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-562-0_14.

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Zigmond, R. E., and N. Y. Ip. "Cholinergic and Peptidergic Regulation of Ganglionic Tyrosine Hydroxylase Activity." In Advances in Behavioral Biology. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5194-8_102.

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Weiner, N., F. L. Lee, J. C. Waymire, and M. Posiviata. "The Regulation of Tyrosine Hydroxylase Activity in Adrenergic Nervous Tissue." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720059.ch8.

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Conference papers on the topic "Tyrosinase activity"

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Ambarwati, Neneng Siti S., Berna Elya, Yesi Desmiaty, Dwi Atmanto, and Islamudin Ahmad. "Tyrosinase inhibitory activity of Garcinia xanthochymus fruit pericarp extract." In THE 2ND SCIENCE AND MATHEMATICS INTERNATIONAL CONFERENCE (SMIC 2020): Transforming Research and Education of Science and Mathematics in the Digital Age. AIP Publishing, 2021. http://dx.doi.org/10.1063/5.0041813.

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Ginting, Chrismis Novalinda, Lobianna Nadeak, and Linda Chiuman. "Activity of Rose Flower Extract and Resepthakulum as Antioxidant and Anti-tyrosinase." In International Conference on Health Informatics, Medical, Biological Engineering, and Pharmaceutical. SCITEPRESS - Science and Technology Publications, 2020. http://dx.doi.org/10.5220/0010285800170022.

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Leem, Kang-Hyun. "Effects of Myrrh extracts on the anti-wrinkle activity and anti tyrosinase activity in Hs68 human fibroblasts." In Healthcare and Nursing 2015. Science & Engineering Research Support soCiety, 2015. http://dx.doi.org/10.14257/astl.2015.104.37.

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Leem, Kang-Hyun. "Effects of Olibanum extracts on the collagenase activity and procollagen synthesis in Hs68 human fibroblasts and tyrosinase activity." In Health Care and Nursing 2015. Science & Engineering Research Support soCiety, 2015. http://dx.doi.org/10.14257/astl.2015.88.36.

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Lu, Rong, Hai-xia Ma, Wei-ping Liu, and Wen-xin Li. "Studies on quantitative structure-activity-relationship inhibitory effects of benzoic acid derivatives on tyrosinase." In 2010 4th International Conference on Bioinformatics and Biomedical Engineering (iCBBE 2010). IEEE, 2010. http://dx.doi.org/10.1109/icbbe.2010.5516550.

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Tristiyanti, Deby, Ledianasari, and Silva Oktaviani. "Inhibitory Activity of Tyrosinase Enzyme on Lotion Contains Pear (Pyrus pyrifolia (Burm.F) Nakai) Rind Extract." In 2nd Bakti Tunas Husada-Health Science International Conference (BTH-HSIC 2019). Atlantis Press, 2020. http://dx.doi.org/10.2991/ahsr.k.200523.022.

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Tai Boon Kai, Zaiton Abdul Majid, and Shafinaz Shahir. "Covalent immobilization of tyrosinase onto commercial multi-walled carbon nanotubes and its effect on enzymatic activity." In 2010 International Conference on Enabling Science and Nanotechnology (ESciNano). IEEE, 2010. http://dx.doi.org/10.1109/escinano.2010.5701046.

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Marrero-Ponce, Yovani, Gerardo Casañola-Martín, Mahmud Khan, et al. "Bond-Based 2D Quadratic Fingerprints in QSAR Studies. Virtual and In Vitro Tyrosinase Inhibitory Activity Elucidation." In The 12th International Electronic Conference on Synthetic Organic Chemistry. MDPI, 2008. http://dx.doi.org/10.3390/ecsoc-12-01278.

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Delogu, Giovanna Lucia, Antonella Fais, Carmen Picciau, et al. "Synthesis of a Serie of 2-Phenylbenzofurans. Structures with Rigid Trans-resveratrol\'s Core and Their Tyrosinase Activity." In The 16th International Electronic Conference on Synthetic Organic Chemistry. MDPI, 2012. http://dx.doi.org/10.3390/ecsoc-16-01109.

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Pittman, Debra D., Louise C. Wasley, Beth L. Murray, Jack H. Wang, and Randal J. Kaufman. "ANALYSIS OF STRUCTURAL REQUIREMENTS FOR FACTOR VIII FUNCTION USING SITE-DIRECTED MUTAGENESIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644044.

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Factor VIII (fVIII) functions in the intrinsic pathway of coagulation as the cofactor for Factor IXa proteolytic activation of Factor X. fVIII contains multiple sites which are susceptible to cleavage by thrombin, Factor Xa, and activate) protein C. Proteolytic cleavage is required for cofactor activity and may be responsible for inactivation of cofactor activity. In order to identify the role ofthe individual cleavages of fVIII in its activation and inactivation, site-directed DNA mediated mutagenesis of fVIII was performed and the altered forms of fVIII produced and characterized. Conversion
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Reports on the topic "Tyrosinase activity"

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Eom, Tae-Kil, Ekyune Kim, and Ju-Sung Kim. Inhibitory Effects of 6,6′‑bieckol from Ishige okamurae on Tyrosinase Activity and Melanin Synthesis in Mouse B16F10 Melanoma Cells. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, 2019. http://dx.doi.org/10.7546/crabs.2019.09.18.

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Drake, Justin, and Owen Witte. Identification and Targeting of Tyrosine Kinase Activity in Prostate Cancer Initiation, Progression, and Metastasis. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada595692.

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Drake, Justin, and Owen Witte. Identification and Targeting of Tyrosine Kinase Activity in Prostate Cancer Initiation, Progression, and Metastasis. Defense Technical Information Center, 2012. http://dx.doi.org/10.21236/ada575949.

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