PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31345746-3 2019 A mushroom tyrosinase inhibitory assay showed compounds 1a (36.71 +- 2.14% inhibition) and 1j (25.99 +- 2.77% inhibition) inhibited tyrosinase more than the other eight NAB derivatives and kojic acid (21.56 +- 2.93% inhibition), and docking studies indicated 1a (-6.9 kcal/mole) and 1j (-7.5 kcal/mole) had stronger binding affinities for tyrosinase than kojic acid (-5.7 kcal/mole). kojic acid 189-199 tyrosinase Mus musculus 132-142 34443550-2 2021 Seven of the twelve derivatives showed stronger inhibitory activity than kojic acid against mushroom tyrosinase. kojic acid 73-83 tyrosinase Mus musculus 101-111 34356311-2 2021 Among the compounds synthesized, compounds 1-3 showed greater inhibitory activity than kojic acid (IC50 = 18.27 +- 0.89 muM); IC50 = 3.70 +- 0.51 muM for 1; IC50 = 3.05 +- 0.95 muM for 2; and IC50 = 5.00 +- 0.38 muM for 3, and found to be competitive tyrosinase inhibitors. kojic acid 87-97 tyrosinase Mus musculus 251-261 33640246-0 2021 The natural-based optimization of kojic acid conjugated to different thio-quinazolinones as potential anti-melanogenesis agents with tyrosinase inhibitory activity. kojic acid 34-44 tyrosinase Mus musculus 133-143 33640246-4 2021 All the synthesized compounds were screened for their anti-tyrosinase activity and all derivatives displayed better potency than kojic acid as the positive control. kojic acid 129-139 tyrosinase Mus musculus 59-69 31345746-3 2019 A mushroom tyrosinase inhibitory assay showed compounds 1a (36.71 +- 2.14% inhibition) and 1j (25.99 +- 2.77% inhibition) inhibited tyrosinase more than the other eight NAB derivatives and kojic acid (21.56 +- 2.93% inhibition), and docking studies indicated 1a (-6.9 kcal/mole) and 1j (-7.5 kcal/mole) had stronger binding affinities for tyrosinase than kojic acid (-5.7 kcal/mole). kojic acid 189-199 tyrosinase Mus musculus 132-142 31345746-3 2019 A mushroom tyrosinase inhibitory assay showed compounds 1a (36.71 +- 2.14% inhibition) and 1j (25.99 +- 2.77% inhibition) inhibited tyrosinase more than the other eight NAB derivatives and kojic acid (21.56 +- 2.93% inhibition), and docking studies indicated 1a (-6.9 kcal/mole) and 1j (-7.5 kcal/mole) had stronger binding affinities for tyrosinase than kojic acid (-5.7 kcal/mole). kojic acid 355-365 tyrosinase Mus musculus 132-142 31345746-3 2019 A mushroom tyrosinase inhibitory assay showed compounds 1a (36.71 +- 2.14% inhibition) and 1j (25.99 +- 2.77% inhibition) inhibited tyrosinase more than the other eight NAB derivatives and kojic acid (21.56 +- 2.93% inhibition), and docking studies indicated 1a (-6.9 kcal/mole) and 1j (-7.5 kcal/mole) had stronger binding affinities for tyrosinase than kojic acid (-5.7 kcal/mole). kojic acid 355-365 tyrosinase Mus musculus 132-142 30892163-7 2019 RESULTS: The tyrosinase inhibitory concentration (IC50) for tested compounds was observed between the range of 68 to 0.0029 microg/ml with lowest IC50 value of compound 5c which outperforms than reference arbutin and kojic acid. kojic acid 217-227 tyrosinase Mus musculus 13-23 30856375-6 2019 A docking simulation using tyrosinase indicated that the four cinnamamides exceeded the binding affinity of kojic acid, and bound more strongly to the active site of tyrosinase. kojic acid 108-118 tyrosinase Mus musculus 27-37 30856375-6 2019 A docking simulation using tyrosinase indicated that the four cinnamamides exceeded the binding affinity of kojic acid, and bound more strongly to the active site of tyrosinase. kojic acid 108-118 tyrosinase Mus musculus 166-176 31027707-5 2019 Our mushroom tyrosinase inhibitory results were supported by our docking study, which showed compound 1c (-7.2 kcal/mole) exhibited stronger binding affinity for mushroom tyrosinase than kojic acid (-5.7 kcal/mole). kojic acid 187-197 tyrosinase Mus musculus 13-23 31027707-5 2019 Our mushroom tyrosinase inhibitory results were supported by our docking study, which showed compound 1c (-7.2 kcal/mole) exhibited stronger binding affinity for mushroom tyrosinase than kojic acid (-5.7 kcal/mole). kojic acid 187-197 tyrosinase Mus musculus 171-181 30554432-5 2019 Based on in silico docking simulation, 5-HMT had a greater binding affinity than kojic acid with a different binding conformation in the tyrosinase catalytic site. kojic acid 81-91 tyrosinase Mus musculus 137-147 30414415-1 2019 Novel kojic acid derivatives (KADs) with the potential ability to inhibit tyrosinase were synthesized and were further identified by Q-Exactive, IR and NMR. kojic acid 6-16 tyrosinase Mus musculus 74-84 30347330-11 2019 Among the nine compounds that inhibited mushroom tyrosinase more potently at 25 muM than kojic acid, four cinnamic amides 4, 5, 9, and 14 showed 3-fold greater tyrosinase inhibitory activity than kojic acid. kojic acid 89-99 tyrosinase Mus musculus 49-59 30347330-11 2019 Among the nine compounds that inhibited mushroom tyrosinase more potently at 25 muM than kojic acid, four cinnamic amides 4, 5, 9, and 14 showed 3-fold greater tyrosinase inhibitory activity than kojic acid. kojic acid 89-99 tyrosinase Mus musculus 160-170 30347330-11 2019 Among the nine compounds that inhibited mushroom tyrosinase more potently at 25 muM than kojic acid, four cinnamic amides 4, 5, 9, and 14 showed 3-fold greater tyrosinase inhibitory activity than kojic acid. kojic acid 196-206 tyrosinase Mus musculus 49-59 30347330-12 2019 The docking simulation using tyrosinase indicated that these four cinnamic amides (-6.2 to -7.9 kcal/mol) bind to the active site of tyrosinase with stronger binding affinity than kojic acid (-5.7 kcal/mol). kojic acid 180-190 tyrosinase Mus musculus 29-39 30347330-12 2019 The docking simulation using tyrosinase indicated that these four cinnamic amides (-6.2 to -7.9 kcal/mol) bind to the active site of tyrosinase with stronger binding affinity than kojic acid (-5.7 kcal/mol). kojic acid 180-190 tyrosinase Mus musculus 133-143 29907470-6 2018 In silico docking simulation supported binding of 1m (-7.6 kcal/mol) to the active site of tyrosinase with stronger affinity than kojic acid (-5.7 kcal/mol). kojic acid 130-140 tyrosinase Mus musculus 91-101 30366788-7 2018 Docking simulation with tyrosinase revealed that these three cinnamamides, 4, 9, and 10, bind to the active site of tyrosinase more strongly than kojic acid. kojic acid 146-156 tyrosinase Mus musculus 24-34 30366788-7 2018 Docking simulation with tyrosinase revealed that these three cinnamamides, 4, 9, and 10, bind to the active site of tyrosinase more strongly than kojic acid. kojic acid 146-156 tyrosinase Mus musculus 116-126 30410332-1 2018 Introduction: Kojic monooleate (KMO) is an ester derived from a fungal metabolite of kojic acid with monounsaturated fatty acid, oleic acid, which contains tyrosinase inhibitor to treat skin disorders such as hyperpigmentation. kojic acid 85-95 tyrosinase Mus musculus 156-166 26500815-7 2015 The effects are comparable, and sometimes even better, than that of kojic acid, a well known tyrosinase inhibitor used for reference. kojic acid 68-78 tyrosinase Mus musculus 93-103 27829416-13 2016 The results were comparable to that of the standard tyrosinase inhibitor (kojic acid). kojic acid 74-84 tyrosinase Mus musculus 52-62 27746633-0 2016 Kojic Acid Peptide: A New Compound with Anti-Tyrosinase Potential. kojic acid 0-10 tyrosinase Mus musculus 45-55 27746633-6 2016 Further, the tyrosinase activities of the Kojic acid and Kojic acid peptides were compared. kojic acid 42-52 tyrosinase Mus musculus 13-23 27746633-6 2016 Further, the tyrosinase activities of the Kojic acid and Kojic acid peptides were compared. kojic acid 57-67 tyrosinase Mus musculus 13-23 27746633-8 2016 RESULTS: Maximum tyrosinase activity was measured by Kojic acid peptides. kojic acid 53-63 tyrosinase Mus musculus 17-27 27746633-10 2016 CONCLUSION: It was observed that this newly synthesized Kojic acid peptide is stable and potent to inhibit the tyrosinase activity and melanin content of B16F10 mouse melanoma cells without exhibiting cell toxicity. kojic acid 56-66 tyrosinase Mus musculus 111-121 27655047-7 2016 Tyrosinase enzymatic activity was determined for each batch, providing the percentage of enzyme inhibition and IC50 values obtained by constructing dose-response curves and compared to kojic acid, a well-known tyrosinase inhibitor. kojic acid 185-195 tyrosinase Mus musculus 0-10 25126713-7 2014 p-Decylaminophenol (3) was the most potent agent examined, showing significant inhibition of B16 tyrosinase activities at concentrations less than what was required to achieve a similar level of inhibition by the well-known tyrosinase inhibitor, kojic acid. kojic acid 246-256 tyrosinase Mus musculus 224-234 26235587-7 2015 As an underlying mechanism, docking simulation showed that compared to kojic acid, a well-known competitive tyrosinase inhibitor which forms a hydrogen bond and aromatic interaction with tyrosinase, MHY2081 has stronger affinity with tyrosinase by forming three hydrogen bonds and a hydrophobic interaction with residues of tyrosinase. kojic acid 71-81 tyrosinase Mus musculus 108-118 26235587-7 2015 As an underlying mechanism, docking simulation showed that compared to kojic acid, a well-known competitive tyrosinase inhibitor which forms a hydrogen bond and aromatic interaction with tyrosinase, MHY2081 has stronger affinity with tyrosinase by forming three hydrogen bonds and a hydrophobic interaction with residues of tyrosinase. kojic acid 71-81 tyrosinase Mus musculus 187-197 26235587-7 2015 As an underlying mechanism, docking simulation showed that compared to kojic acid, a well-known competitive tyrosinase inhibitor which forms a hydrogen bond and aromatic interaction with tyrosinase, MHY2081 has stronger affinity with tyrosinase by forming three hydrogen bonds and a hydrophobic interaction with residues of tyrosinase. kojic acid 71-81 tyrosinase Mus musculus 187-197 26235587-7 2015 As an underlying mechanism, docking simulation showed that compared to kojic acid, a well-known competitive tyrosinase inhibitor which forms a hydrogen bond and aromatic interaction with tyrosinase, MHY2081 has stronger affinity with tyrosinase by forming three hydrogen bonds and a hydrophobic interaction with residues of tyrosinase. kojic acid 71-81 tyrosinase Mus musculus 187-197 23291747-2 2013 Most of the compounds (3-5) exhibited higher inhibitory effects than kojic acid (IC(50) = 49.08 microM), a representative tyrosinase inhibitor. kojic acid 69-79 tyrosinase Mus musculus 122-132 23812774-3 2013 MHY498 was more potent than the well-known tyrosinase inhibitor, kojic acid (mean IC50 = 22.79 muM). kojic acid 65-75 tyrosinase Mus musculus 43-53 23812774-5 2013 Docking models showed that the binding affinity of MHY498 to tyrosinase was higher than that of kojic acid, and docking simulation results indicated that the tyrosinase binding moieties of MHY498 and kojic acid were similar. kojic acid 96-106 tyrosinase Mus musculus 158-168 23812774-5 2013 Docking models showed that the binding affinity of MHY498 to tyrosinase was higher than that of kojic acid, and docking simulation results indicated that the tyrosinase binding moieties of MHY498 and kojic acid were similar. kojic acid 200-210 tyrosinase Mus musculus 61-71 23812774-5 2013 Docking models showed that the binding affinity of MHY498 to tyrosinase was higher than that of kojic acid, and docking simulation results indicated that the tyrosinase binding moieties of MHY498 and kojic acid were similar. kojic acid 200-210 tyrosinase Mus musculus 158-168 23743286-2 2013 The IC50 value of MHY1556 was 0.50muM which was significantly lower than that of kojic acid (IC50=53.95muM), which is a well-known tyrosinase inhibitor and was used as a positive control in this study. kojic acid 81-91 tyrosinase Mus musculus 131-141 23007519-5 2013 In light of bans of previously proven and popular skin whitening cosmetic ingredients such as hydroquinone and kojic acid, use of miRNAs that target and silence tyrosinase expression may present a novel and promising cosmetic approach to achieve skin whitening. kojic acid 111-121 tyrosinase Mus musculus 161-171 23149255-3 2012 (E)-4-((4-Hydroxyphenylimino)methyl)benzene-1,2-diol exhibited the most potent and non-competitive inhibition on mushroom tyrosinase showing an IC(50) of 17.22 +- 0.38 muM and being more effective than kojic acid (51.11 +- 1.42 muM). kojic acid 202-212 tyrosinase Mus musculus 122-132 22498140-5 2012 RESULTS: The novel compound, 3-DBP, showed an inhibitory effect against mushroom tyrosinase (IC50=0.53 muM), which indicated that it was more potent than the well-known tyrosinase inhibitor kojic acid (IC50=8.2 muM). kojic acid 190-200 tyrosinase Mus musculus 169-179 21957050-3 2011 Previously, we reported that kojic acid-amino acid amide (KA-AA-NH(2)) showed enhanced tyrosinase inhibitory activity compared with kojic acid alone, but this was not observed in a cell test because of poor cell permeability. kojic acid 29-39 tyrosinase Mus musculus 87-97 17827726-5 2007 HNB inhibited mushroom tyrosinase with an IC(50) value of 0.07 microM, which is more potent than the anti-tyrosinase activity of kojic acid (IC(50)=38.24), a well-known tyrosinase inhibitor. kojic acid 129-139 tyrosinase Mus musculus 106-116 20057943-4 2009 In contrast, a standard tyrosinase inhibitor, kojic acid, showed 69.9% and 71.3% of control in cellular tyrosinase and melanogenesis activity, respectively, at a concentration as high as 100 microM. kojic acid 46-56 tyrosinase Mus musculus 24-34 20057943-4 2009 In contrast, a standard tyrosinase inhibitor, kojic acid, showed 69.9% and 71.3% of control in cellular tyrosinase and melanogenesis activity, respectively, at a concentration as high as 100 microM. kojic acid 46-56 tyrosinase Mus musculus 104-114 20619644-2 2010 5HNB inhibited mushroom tyrosinase with an IC(50) value of 2.95 microM, which is more potent than the well-known anti-tyrosinase activity of kojic acid (IC(50)=38.24). kojic acid 141-151 tyrosinase Mus musculus 118-128 19122286-2 2009 TMBC inhibited the L-dopa oxidase activity of mushroom tyrosinase with an IC(50) value of 0.95+/-0.04 microM, which was more potent than kojic acid (IC(50)=24.88+/-1.13 microM), a well-known tyrosinase inhibitor. kojic acid 137-147 tyrosinase Mus musculus 55-65 17827726-5 2007 HNB inhibited mushroom tyrosinase with an IC(50) value of 0.07 microM, which is more potent than the anti-tyrosinase activity of kojic acid (IC(50)=38.24), a well-known tyrosinase inhibitor. kojic acid 129-139 tyrosinase Mus musculus 106-116 11864987-4 2002 Oxyresveratrol showed potent inhibitory effect with an IC(50) value of 1.2 microm on mushroom tyrosinase activity, which was 32-fold stronger inhibition than kojic acid, a depigmenting agent used as the cosmetic material with skin-whitening effect and the medical agent for hyperpigmentation disorders. kojic acid 158-168 tyrosinase Mus musculus 94-104 12723623-2 2003 Gnetol (IC50, 4.5 microM) was stronger than kojic acid (IC50, 139 microM) as a standard inhibitor for murine tyrosinase activity. kojic acid 44-54 tyrosinase Mus musculus 109-119 9690341-2 1998 The extract of Artocarpus incisus showed the strongest tyrosinase inhibitory activity which was equivalent to kojic acid. kojic acid 110-120 tyrosinase Mus musculus 55-65 10630104-8 1999 Kojic acid exhibited KEIS and KEI values of 2.4 x 10(-5) M and 2.2 x 10(-5) M on mushroom tyrosinase and those of 8.9 x 10(-5) M and 7.2 x 10(-5) M on murine tyrosinase, respectively. kojic acid 0-10 tyrosinase Mus musculus 90-100 10630104-8 1999 Kojic acid exhibited KEIS and KEI values of 2.4 x 10(-5) M and 2.2 x 10(-5) M on mushroom tyrosinase and those of 8.9 x 10(-5) M and 7.2 x 10(-5) M on murine tyrosinase, respectively. kojic acid 0-10 tyrosinase Mus musculus 158-168