Results 41 to 50 of about 54,266 (256)

Inhibitory Effects of Urginea maritima (L.) Baker, Zhumeria majdae Rech. F. and Wendelbo and Physalis divaricata D. Don Ethanolic Extracts on Mushroom Tyrosinase

open access: yesPharmaceutical Sciences, 2016
Background: Tyrosinase is a key enzyme in melanin synthesis from tyrosine. To prevent or treat pigmentation disorders, tyrosinase inhibitors have been used increasingly for medicinal and cosmetic products.
Foroogh Namjoyan, Alireza Jahangiri, Mohammad Ebrahim Azemi, Hamideh Mousavi
doaj   +1 more source

Data in support of covalent attachment of tyrosinase onto cyanuric chloride crosslinked magnetic nanoparticles

open access: yesData in Brief, 2016
Preparation and characterization of cross linked amine-functionalized magnetic nanoparticles as an appropriate support for covalent immobilization on tyrosinase was presented in the study "Covalent immobilization of tyrosinase onto cyanuric chloride ...
Kourosh Abdollahi   +2 more
doaj   +1 more source

Advances in the Design of Genuine Human Tyrosinase Inhibitors for Targeting Melanogenesis and Related Pigmentations.

open access: yesJournal of Medicinal Chemistry, 2020
Human tyrosinase (hsTYR) is the key enzyme ensuring the conversion of L-tyrosine to dopaqui-none, thereby initiating melanin synthesis, i.e. melanogenesis.
Brayan Roulier   +2 more
semanticscholar   +1 more source

Visualization of Intracellular Tyrosinase Activity in vitro

open access: yesBio-Protocol, 2016
Melanocytes produce the melanin pigments in melanosomes and these organelles protect the skin against harmful ultraviolet rays. Tyrosinase is the key cuproenzyme which initiates the pigment synthesis using its substrate amino acid tyrosine or L-DOPA (L-3,
Riddhi Jani, Sudeshna Nag, Subba Setty
doaj   +1 more source

In vitro screening of elastase, collagenase, hyaluronidase, and tyrosinase inhibitory and antioxidant activities of 22 halophyte plant extracts for novel cosmeceuticals

open access: yes, 2020
Background Halophyte plant (HPs), a salt-resistant flora, has been reported to provide several health benefits, but the knowledge of its cosmeceutical potential is still ambiguous.
Chanipa Jiratchayamaethasakul   +9 more
semanticscholar   +1 more source

Screening of Peruvian Medicinal Plants for Tyrosinase Inhibitory Properties: Identification of Tyrosinase Inhibitors in Hypericum laricifolium Juss

open access: yesMolecules, 2017
Tyrosinase inhibitors are of far-ranging importance in cosmetics, medicinal products, and food industries. Peru is a diverse country with a wide variety of plants that may contain excellent anti-tyrosinase inhibitors. In the present study, the tyrosinase
Yanymee Nimesia Guillen Quispe   +3 more
doaj   +1 more source

Rifampicin is not an inhibitor of tyrosinase

open access: yesInternational Journal of Biological Macromolecules, 2022
Rifampicin has been previously described as an inhibitor of tyrosinase (Chai et al., Int. J. Biol. Macromol. 102 (2017) 425-430). However, rifampicin contains a p-diphenol group and compounds with such a moiety have been shown before to reduce tyrosinase-generated o-quinones.
Damian Tarasek, Hubert Wojtasek
openaire   +2 more sources

Tyrosinase inhibitors as melanoma sensitizers: Boosting therapeutic efficacy

open access: yesSupramolecular Materials
Melanoma therapy faces critical challenges due to melanin-mediated resistance mechanisms. The use of tyrosinase inhibitors to suppress tyrosinase activity and reduce melanogenesis, thereby sensitizing melanoma cells, represents a highly promising ...
Yongsheng Li, Kan Yang, Luyang Zhao
doaj   +1 more source

Hydroxamic Acid as a Potent Metal-Binding Group for Inhibiting Tyrosinase

open access: yesAntioxidants, 2022
Tyrosinase, a metalloenzyme containing a dicopper cofactor, plays a central role in synthesizing melanin from tyrosine. Many studies have aimed to identify small-molecule inhibitors of tyrosinase for pharmaceutical, cosmetic, and agricultural purposes ...
Joonhyeok Choi   +3 more
doaj   +1 more source

Copper-oxygen Dynamics in Tyrosinase Mechanism.

open access: yesAngewandte Chemie, 2020
The dinuclear copper enzyme tyrosinase activates O2  to form a (μ-η2:η2-peroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate ...
N. Fujieda   +7 more
semanticscholar   +1 more source

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