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(14S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + ?
(13S,14S)-epoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
-
-
-
?
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + O2
(11S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + (14S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + (17S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
-
-
-
?
5S,15S-dihydroperoxyeicosatetraenoic acid + O2
lipoxin B4
-
-
-
?
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
-
-
?
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(12S)-12-hydroperoxyicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
linoleate + O2
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
(14S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + ?
(13S,14S)-epoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
-
-
-
?
4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + O2
(11S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + (14S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid + (17S)-hydroperoxy-4Z,7Z,10Z,12E,16Z,19Z-docosahexaenoic acid
-
-
-
?
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
-
-
?
5S-hydroperoxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + 5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
-
-
?
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,12S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
-
-
?
5S-hydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid + O2
5S,15S-dihydroxy-6E,8Z,10E,14Z-eicosatetraenoic acid
-
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-12-hydroperoxyicosa-5,8,11,13-tetraenoate + (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
arachidonate + O2
(6E,8Z,11Z,14Z)-(5S)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
-
-
-
-
?
arachidonic acid + O2
(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid
-
-
the mutant enzyme A416G converts arachidonic acid to (11R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid and (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoic acid in a 1.5:1 ratio
-
?
arachidonic acid + O2
15S-hydroperoxy-5Z,8Z,11Z,13E-eicosatetraenoic acid
-
-
-
-
?
arachidonic acid + O2
?
-
-
-
-
?
eicosapentaenoic acid + O2
15-hydroxyeicosapentaenoic acid
-
-
-
-
?
linoleate + O2
(9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
linoleic acid + O2
13-hydroperoxy-(9Z,11E)-linoleic acid
-
-
-
-
?
linoleic acid + O2
13-hydroxylinoleic acid
linoleic acid + O2
13-S-hydroxyoctadecadienoic acid
-
both 15-LOX-1, 15-LOX-2 reacts with linoleic acid poorly
-
-
?
lipoic acid + O2
?
-
-
-
-
r
additional information
?
-
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
best substrate
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
671247, 672376, 672543, 672899, 672902, 673030, 675201, 675909, 676263, 676923, 676925, 676927, 677239, 685266, 685525, 685526, 685584, 686173, 687052, 687235, 688159, 688509, 688751, 712712 -
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
and small amounts of (5Z,8Z,10E,14Z)-12-hydro(pero)xy-5,8,10,14-icosatetraenoic acid
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
15-hydroperoxy-5,8,11,13-eicosatetraenoic acid + 15-hydroxy-5,8,11,13-eicosatetraenoic acid
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
formation of 15S-hydroxyeicosatetraenoic acid and 12S-hydroxyeicosatetraenoic acid in a ratio of 12:1, double oxygenation products 14R,15S-dihydroxyeicosatetraenoic acid and various 8,15-dihydroxyeicosatetraenoic acids are also produced
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
ratio of 15-lipoxygenation to 12-lipoxygenation is 9:1 for the wild-type enzyme and the mutant enzymes V104I, L397M and Q431R. The ratio of 15-lipoxygenation to 12-lipoxygenation is 1:1 for the mutant enzymes V104/L397M/M418V/Q431R, L397M/M418V/Q431R, L397M/M418V and M418V
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
15-hydroxyeicosatetraenoic acid and 12-hydroxyeicosatetraenoic acid in a ratio of 8.6:1
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
further metabolized to (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate, 15-HETE, has no effect on the spontaneous and lipopolysaccharide-stimulated growth of leukemic blasts
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
-
the bifunctional enzyme also forms (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate, the product of 12-LO activity, EC 1.13.11.31, in a ratio of 9:1 15(S)-HPETE to 12(S)-HPETE, further reduced to the correspondent (S)-hydroxy fatty acids, in eosinophils, overview, the bifunctional enzyme also forms (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate, the product of 12-LO activity, EC 1.13.11.31, in a ratio of 9:1 15(S)-HPETE to 12(S)HPETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
is further metabolized to (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate, i.e. 15(S)-HETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells, it could be a suppressor of prostate cancer development, which functions by restricting cell cycle progression
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
catalyzes enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is implicated in inflammatory disorders, 15-lipoxygenase is induced in atherosclerosis and can oxidize low-density lipoprotein to its atherogenic form
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
alternative splicing of 15S-lipoxygenase provides a further level of regulation of fatty acid metabolism
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
12/15LO protein levels and activity are increased in pathologically affected regions of Alzheimers disease brains, enzyme inhibition causes a decrease in amyloid-beta protein, 12/15LO influences amyloid-beta protein precursor protein metabolism, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
15-lipoxygenase type-1 is a prooxidant enzyme, which is expressed in asthmatic lungs leading to formation of pro- and anti-inflammatory mediators, overview
the product is further metabolized to 15(S)-hydroxyeicosatetranoic acid and 15-ketoeicosatetraenoic acid, the latter is the main product, pathway and mechanism, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
15-LOX2 in NHP cells is positively regulated by Sp1 and negatively regulated by Sp3, but 15-LOX2 expression in NHP cells is not directly regulated by androgen/androgen receptor, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
arachidonic acid is metabolized by the 15-lipoxygenase-1 pathway to the vasodilatory eicosanoids hydroxyepoxyeicosatrienoic acid and trihydroxyeicosatrienoic acid
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
arachidonic acid metabolization by lipoxygenases, overview
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is involved in acetylsalicylic acid-triggered production of 15(S)-hydroxyeicosatetranoic acid, 15(S)-HETE, in sensitive asthmatic patients, acetylsalicylate-tolerant asthma patients show reduced 15-LO activity
is metabolized to 15(S)-hydroxyeicosatetranoic, i.e. 15(S)-HETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme modifies high density lipoprotein 3, the major and most antiatherogenic HDL subfraction, and impairs anti-inflammatory activity of the lipoprotein, which, after modification, fails to inhibit TNFalpha-mediated mRNA and protein induction of adhesion molecules and monocyte chemoattractant protein-1, MCP-1, in endothelial cells, overview
is metabolized to 15(S)-hydroxyeicosatetranoic, i.e. 15(S)-HETE
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
immunohistochemic assay
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
preferred substrate of isozyme 15-hLO-2, reaction of EC 1.13.11.33
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
regioselective oxidation is achieved through control over the position of hydrogen atom abstraction by the geometry and size of the enzyme active site and through control by the protein over the interaction of molecular oxygen with the generated delocalized substrate radical, analysis of catalytic mechanisms of lipoxygenases using 10,10-dideuterated arachidonic acid, 13,13-dideuterated arachidonic acid, and 0,10,13,13-d4-AA, overview
isozymes 15-hLO-1 and 15-hLO-2 also form small amounts of 11-HPETE, 8-HPETE, and 12-HPETE, the rate of 8/12-HPETE production by isozyme 15-hLO-1 with 13,13-dideuterated arachidonic acid as substrate is exeptionally high with 75% of overall production, overview
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
15-H(p)ETE is the major reaction product of 15-LOX-2 and 12/15-LOX independent of the pH
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
-
product ratio is 9 to 1
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
5fold higher affinity for arachidonic acid than for linoleic acid for 15-hLO-1
-
-
?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
-
both 15-LOX-1 and -2
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
-
preferred substrate of isozyme 15-hLO-1, reaction of EC 1.13.11.12
-
-
?
linoleic acid + O2
13-hydroxylinoleic acid
-
-
-
?
linoleic acid + O2
13-hydroxylinoleic acid
-
-
-
?
linoleic acid + O2
13-hydroxylinoleic acid
-
-
-
?
linoleic acid + O2
13-hydroxylinoleic acid
-
-
-
?
linoleic acid + O2
13-hydroxylinoleic acid
-
-
-
-
?
linoleic acid + O2
13-hydroxylinoleic acid
-
-
13-hydroperoxy-9,11-octadecadienoic acid + 13-hydroxy-9,11-octadecadienoic acid
?
linoleic acid + O2
?
-
-
-
-
?
linoleic acid + O2
?
-
4% of the activity with arachidonate
-
-
?
additional information
?
-
a bifunctional enzyme exhibiting 12-LO and 15-LO activity
-
-
?
additional information
?
-
15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type subject produces 21% 12-hydroperoxyicosatetraenoate and 79% 15-hydroperoxyicosatetraenoate
-
-
?
additional information
?
-
human 15-LOX type 1 (ALOX15) is a predominantly 15-lipoxygenating enzyme, which produces only little amounts of (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate (ratio of 9:1)
-
-
?
additional information
?
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation. Intraenzyme oxygen movement
-
-
?
additional information
?
-
-
the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation. Intraenzyme oxygen movement
-
-
?
additional information
?
-
enzyme substrate specificity, overview. The ALOX15 enzyme activity is not restricted to free polyenoic fatty acids since phospholipids and even biomembranes and lipoproteins are suitable ALOX15 substrates. The ALOX15 orthologue is capable of converting hydroperoxy fatty acids to epoxy leukotrienes. Product specificity with polyenoic acids and with complex substrates, and alteration of product specificity by substrate modification
-
-
?
additional information
?
-
-
enzyme substrate specificity, overview. The ALOX15 enzyme activity is not restricted to free polyenoic fatty acids since phospholipids and even biomembranes and lipoproteins are suitable ALOX15 substrates. The ALOX15 orthologue is capable of converting hydroperoxy fatty acids to epoxy leukotrienes. Product specificity with polyenoic acids and with complex substrates, and alteration of product specificity by substrate modification
-
-
?
additional information
?
-
prediction of reaction specificity of mammalian ALOX15 orthologues, and reaction specificity of ALOX15 orthologues during late primate evolution
-
-
?
additional information
?
-
the enzymatic peroxidation reaction consists of four consecutive steps: At first a hydrogen atom is stereoselectively abstracted from one of the bisallylic methylene-groups forming an enzyme-bound radical. Secondly one of the two associated cis-double bonds is rearranged and forms a conjugated cis-trans-diene. Consecutively a peroxy radical is produced by inserting molecular oxygen. Finally the radical is reduced by antarafacial re-inserting of a hydrogen atom. The resulting product of this peroxidation reaction depends on the respective fatty acid, which is used as a substrate
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additional information
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15-LOX2 and 15-LOX2sv-b suppress prostate tumor development, and the tumor-suppressive functions apparently do not necessarily depend on arachidonic acid-metabolizing activity and nuclear localization
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additional information
?
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15-LOX2 is a functional tumor suppressor that regulates prostate epithelial cell differentiation, senescence, and growth size, overview
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?
additional information
?
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15-LOX2 is a functional tumor suppressor that regulates prostate epithelial cell differentiation, senescence, and growth size, overview
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?
additional information
?
-
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eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in eosinophils and mast cells, metabolism of 14,15-leukotrienes in eosinophils, overview
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additional information
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a bifunctional enzyme exhibiting 15-lipoxygenase and 12-lipoxygenase, EC 1.13.11.31, activities
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additional information
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conjugated linoleic acids are no substrates for 15-LO-1 in vitro, overview
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additional information
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product distributions of lipoxygenases under various conditions, overview
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additional information
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substrate specificity of 15-hLO isozymes, the specific activity is affected by cholate and lipoxygenation reaction products, e.g. 13-hydroperoxyoctadienoic acid changes the (kcat/Km)AA/(kcat/Km)LA ratio more than 5fold for 15-hLO-1 and 3fold for 15-hLO-2, while 12-(S)-hydroperoxyeicosatetraenoic acid affects only the ratio of 15-hLO-1 more than 5fold. In addition, 13-(S)-hydroxyoctadecadienoic acid and 12-(S)-hydroxyeicosatetraenoic acid also affect substrate specificity, indicating that iron oxidation is not responsible for the change in the (kcat/Km)AA/(kcat/Km)LA ratio, residues R402, F414, F352, I417, and M418 are located at the active site and involved in catalysis, presence of a product-activated, allosteric regulatory site for both 15-hLO isozymes, competitive substrate capture experiments, overview
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additional information
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15-LOX-2 does not oxygenate (5Z,8Z,11Z,14Z)-nonadeca-5,8,11,14-tetraene-1,19-dioic acid at various pH
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additional information
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15LO1 interacts with PEBP1 (phosphatidylethanolamine-binding protein)
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additional information
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15-LOX is a non-heme iron-containing dioxygenase that oxygenates polyunsaturated fatty acids (PUFA) containing cis,cis-1,4-pentadiene moieties
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additional information
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specificity of phospholipid binding by 15-LOX-2, overview
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
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linoleic acid + O2
(9Z,11E)-(13S)-13-hydroperoxy-octadeca-9,11-dienoate
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additional information
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
best substrate
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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-
further metabolized to (5Z,8Z,11Z,13E)-(15S)-15-hydroxyeicosa-5,8,11,13-tetraenoate, 15-HETE, has no effect on the spontaneous and lipopolysaccharide-stimulated growth of leukemic blasts
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?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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the bifunctional enzyme also forms (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyeicosa-5,8,10,14-tetraenoate, the product of 12-LO activity, EC 1.13.11.31, in a ratio of 9:1 15(S)-HPETE to 12(S)-HPETE, further reduced to the correspondent (S)-hydroxy fatty acids, in eosinophils, overview
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?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
-
the enzyme is regulated pretranslational, translational and posttranslational
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells, it could be a suppressor of prostate cancer development, which functions by restricting cell cycle progression
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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catalyzes enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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the enzyme is implicated in inflammatory disorders, 15-lipoxygenase is induced in atherosclerosis and can oxidize low-density lipoprotein to its atherogenic form
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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alternative splicing of 15S-lipoxygenase provides a further level of regulation of fatty acid metabolism
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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12/15LO protein levels and activity are increased in pathologically affected regions of Alzheimers disease brains, enzyme inhibition causes a decrease in amyloid-beta protein, 12/15LO influences amyloid-beta protein precursor protein metabolism, overview
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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15-lipoxygenase type-1 is a prooxidant enzyme, which is expressed in asthmatic lungs leading to formation of pro- and anti-inflammatory mediators, overview
the product is further metabolized to 15(S)-hydroxyeicosatetranoic acid and 15-ketoeicosatetraenoic acid, the latter is the main product, pathway and mechanism, overview
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?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
15-LOX2 in NHP cells is positively regulated by Sp1 and negatively regulated by Sp3, but 15-LOX2 expression in NHP cells is not directly regulated by androgen/androgen receptor, overview
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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arachidonic acid is metabolized by the 15-lipoxygenase-1 pathway to the vasodilatory eicosanoids hydroxyepoxyeicosatrienoic acid and trihydroxyeicosatrienoic acid
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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arachidonic acid metabolization by lipoxygenases, overview
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arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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the enzyme is involved in acetylsalicylic acid-triggered production of 15(S)-hydroxyeicosatetranoic acid, 15(S)-HETE, in sensitive asthmatic patients, acetylsalicylate-tolerant asthma patients show reduced 15-LO activity
is metabolized to 15(S)-hydroxyeicosatetranoic, i.e. 15(S)-HETE
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?
arachidonate + O2
(5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyeicosa-5,8,11,13-tetraenoate
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the enzyme modifies high density lipoprotein 3, the major and most antiatherogenic HDL subfraction, and impairs anti-inflammatory activity of the lipoprotein, which, after modification, fails to inhibit TNFalpha-mediated mRNA and protein induction of adhesion molecules and monocyte chemoattractant protein-1, MCP-1, in endothelial cells, overview
is metabolized to 15(S)-hydroxyeicosatetranoic, i.e. 15(S)-HETE
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?
additional information
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15-lipoxygenating ALOX15 orthologs exhibit significantly higher lipoxin-synthesizing capacities than 12-lipoxygenating. Product pattern of primate ALOX15 orthologues, overview. The wild-type subject produces 21% 12-hydroperoxyicosatetraenoate and 79% 15-hydroperoxyicosatetraenoate
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additional information
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human 15-LOX type 1 (ALOX15) is a predominantly 15-lipoxygenating enzyme, which produces only little amounts of (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate (ratio of 9:1)
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additional information
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the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation. Intraenzyme oxygen movement
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additional information
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the major reaction products are identified as(8S,15S,5Z,9E,11Z,13E)-8,15-dihydroperoxy-5,9,11,13-eicosatetraenoic acid (8S,15S-DiHpETE) and (5S,15S,6E,8Z,11Z,13E)-5,15-dihydroperoxy-6,8,11,13-eicosatetraenoic acid (5S,15S-DiHPETE) and the stereochemistry of the reaction is compatible with an inverse substrate orientation. Intraenzyme oxygen movement
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additional information
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15-LOX2 and 15-LOX2sv-b suppress prostate tumor development, and the tumor-suppressive functions apparently do not necessarily depend on arachidonic acid-metabolizing activity and nuclear localization
-
-
?
additional information
?
-
15-LOX2 is a functional tumor suppressor that regulates prostate epithelial cell differentiation, senescence, and growth size, overview
-
-
?
additional information
?
-
-
15-LOX2 is a functional tumor suppressor that regulates prostate epithelial cell differentiation, senescence, and growth size, overview
-
-
?
additional information
?
-
-
eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in eosinophils and mast cells, metabolism of 14,15-leukotrienes in eosinophils, overview
-
-
?
additional information
?
-
-
15LO1 interacts with PEBP1 (phosphatidylethanolamine-binding protein)
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?
additional information
?
-
15-LOX is a non-heme iron-containing dioxygenase that oxygenates polyunsaturated fatty acids (PUFA) containing cis,cis-1,4-pentadiene moieties
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(3-chlorobenzoyl)-N-(2-chlorophenyl)-1H-pyrazole-3-carboxamide
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1-acetyl-N-(3,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
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1-benzyl-N-(2-chlorophenyl)-1H-pyrazole-3-carboxamide
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1-[(2H-1,3-benzodioxol-5-yl)carbamothioyl]-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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3-(4-bromophenyl)-6-(4-chlorophenyl)-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
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3-(4-bromophenyl)-6-(4-chlorophenyl)-N-cyclohexylimidazo[2,1-b][1,3]thiazol-5-amine
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3-(4-bromophenyl)-N-cyclohexyl-6-(2-nitrophenyl)imidazo[2,1-b][1,3]thiazol-5-amine
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3-(4-methoxyphenyl)-6-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
protective activity of compound 5i against H2O2-induced cell death in differentiated PC12 cells
4,5-dichloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
4-(2-benzoylhydrazinyl)benzene-1-sulfonamide
10% inhibition
4-amino-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
4-bromo-5-chloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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4-bromo-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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4-butyl-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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4-chloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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4-chloro-N-(2-chloro-4-fluorophenyl)-5-(difluoromethyl)-1H-pyrazole-3-carboxamide
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4-chloro-N-(2-chloro-4-fluorophenyl)-5-(trifluoromethyl)-1H-pyrazole-3-carboxamide
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4-chlorophenyl 3-[(2-chlorophenyl)carbamoyl]-1H-pyrazole-1-carboxylate
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4-methyl-2-(4-methylpiperazinyl)pyrimido[4,5-b]benzothiazine
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4-[(E)-benzoyldiazenyl]benzene-1-sulfonamide
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4-[(E)-benzoyldiazenyl]benzonitrile
80% inhibition, competitive
5-(methylamino)-2-(naphthalen-1-yl)-4,5-dihydro-1,3-oxazole-4-carbonitrile
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5-amino-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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5-butyl-N3-(2-chloro-4-fluorophenyl)-N1-hexyl-1H-pyrazole-1,3-dicarboxamide
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5-chloro-2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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5-chloro-N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
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5-chloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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5-fluoro-2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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5-tert-butyl-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
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6,6a,11,11a-tetrahydro[1]benzothiopyrano[4,3-b]indole
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6-(2-bromophenyl)-N-cyclohexyl-3-phenylimidazo[2,1-b][1,3]thiazol-5-amine
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6-(2-nitrophenyl)-3-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
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6-(4-nitrophenyl)-3-phenyl-N-(2,4,4-trimethylpentan-2-yl)imidazo[2,1-b][1,3]thiazol-5-amine
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6-chloro-2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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6-chloro-2-(4,5-dichloro-1H-pyrazol-3-yl)-1,3-benzoxazole
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6-chloro-2-(5-chloro-1H-pyrazol-3-yl)-1,3-benzoxazole
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6-fluoro-2-(1H-pyrazol-3-yl)-1,3-benzoxazole
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adamantyl caffeate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.074 mM
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bornyl vanillate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.401 mM
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ethyl 6-([3-[(2-chloro-4-fluorophenyl)carbamoyl]-1H-pyrazole-1-carbonyl]amino)hexanoate
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ethyl 6-chloro-3-[(3S)-3-hydroxy-7-methyloctanoyl]-2,3-dihydro-1H-indole-2-carboxylate
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fenchyl caffeate
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.089 mM
-
N'-(4-bromophenyl)benzohydrazide
28% inhibition
N'-(4-cyanophenyl)benzohydrazide
9% inhibition
N'-(4-methoxyphenyl)benzohydrazide
73% inhibition
N'-(4-methylphenyl)benzohydrazide
93% inhibition, competitive
N'-(4-nitrophenyl)benzohydrazide
17% inhibition
N'-phenylbenzohydrazide
33% inhibition
N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
N-(2,5-dichlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1-(dimethylsulfamoyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1-(phenylacetyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1-methyl-1H-pyrazole-3-carboxamide
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N-(2-chloro-4-fluorophenyl)-1-[3-(trifluoromethyl)benzene-1-sulfonyl]-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
N-(2-chloro-4-fluorophenyl)-4,5-bis(trifluoromethyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-(trifluoromethyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-fluoro-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-iodo-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-methyl-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-methyl-5-(trimethylsilyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-nitro-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-phenyl-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-4-[(methanesulfonyl)amino]-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-(difluoromethyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-(trifluoromethyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-iodo-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-methyl-1H-pyrazole-3-carboxamide
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N-(2-chloro-4-fluorophenyl)-5-nitro-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-5-[(methanesulfonyl)amino]-1H-pyrazole-3-carboxamide
-
N-(2-chlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2-chlorophenyl)-N-methyl-1H-pyrazole-3-carboxamide
-
N-(3,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
N-(5-chloro-1,3-thiazol-2-yl)-1H-pyrazole-3-carboxamide
-
N-(5-chloropyridin-2-yl)-1H-pyrazole-3-carboxamide
-
N-(5-fluoropyridin-2-yl)-1H-pyrazole-3-carboxamide
-
N-(7-fluoroquinolin-3-yl)-1H-pyrazole-3-carboxamide
-
N-(isoquinolin-3-yl)-1H-pyrazole-3-carboxamide
-
N-(pyridin-2-yl)-1H-pyrazole-3-carboxamide
-
N-(pyridin-3-yl)-1H-pyrazole-3-carboxamide
-
N-(pyridin-4-yl)-1H-pyrazole-3-carboxamide
-
N-(quinolin-2-yl)-1H-pyrazole-3-carboxamide
-
N-(quinolin-3-yl)-1H-pyrazole-3-carboxamide
-
N-(quinolin-6-yl)-1H-pyrazole-3-carboxamide
-
N-(tert-butyl)-3-phenyl-6-(p-tolyl)imidazo[2,1-b]thiazol-5-amine
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N-(tert-butyl)-6-(4-chlorophenyl)-3-phenylimidazo[2,1-b]thiazol-5-amine
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N-(tert-butyl)-6-(4-methoxyphenyl)-3-phenylimidazo[2,1-b]thiazol-5-amine
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N-(tert-butyl)-6-(4-nitrophenyl)-3-phenylimidazo[2,1-b]thiazol-5-amine
-
N-benzyl-1H-pyrazole-3-carboxamide
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N-cyclohexyl-6-(2-fluorophenyl)-3-phenylimidazo[2,1-b][1,3]thiazol-5-amine
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N-cyclohexyl-6-(4-methoxyphenyl)-3-phenylimidazo[2,1-b][1,3]thiazol-5-amine
-
N-cyclohexyl-6-(4-nitrophenyl)-3-phenylimidazo[2,1-b][1,3]thiazol-5-amine
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N-phenyl-1H-pyrazole-3-carboxamide
-
N-[4-(trifluoromethyl)phenyl]-1H-pyrazole-3-carboxamide
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N-[4-fluoro-2-(trifluoromethyl)phenyl]-1H-pyrazole-3-carboxamide
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N1-(2H-1,3-benzodioxol-5-yl)-N-3-(2-chloro-4-fluorophenyl)-1H-pyrazole-1,3-dicarboxamide
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N1-butyl-N3-(2-chlorophenyl)-N3-methyl-1H-pyrazole-1,3-dicarboxamide
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N3-(2,2-difluoro-2H-1,3-benzodioxol-4-yl)-N1-hexyl-5-methyl-1H-pyrazole-1,3-dicarboxamide
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N3-(2-chloro-4-fluorophenyl)-N1-hexyl-4-methyl-1H-pyrazole-1,3-dicarboxamide
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N3-(2-chloro-4-fluorophenyl)-N1-pentyl-1H-pyrazole-1,3-dicarboxamide
-
N3-(2-chlorophenyl)-N1,N1-dimethyl-1H-pyrazole-1,3-dicarboxamide
-
nordihydroguaiaretic acid
-
phenyl[(E)-phenyldiazenyl]methanone
87% inhibition
stylosin
IC50 value of cytotoxicity against PC-3 cells, 24 h, is 0.101 mM
-
[(E)-(4-bromophenyl)diazenyl](phenyl)methanone
44% inhibition
[(E)-(4-methoxyphenyl)diazenyl](phenyl)methanone
19% inhibition
[(E)-(4-methylphenyl)diazenyl](phenyl)methanone
44% inhibition
[(E)-(4-nitrophenyl)diazenyl](phenyl)methanone
34% inhibition
(Z)-9-octadecenyl sulfate
-
allosteric inhibition
1-phenyl-2-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)-1H-imidazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
-
11-thialinoleic acid
-
is a noncompetitive inhibitor of 15-lipoxygenase-1 with respect to arachidonate or linoleic acid as substrates. Presence of inhibitor does not alter the product distribution for 15-lipoxygenase-1. It does not change the regioselectivity of 15-lipoxygenase-1
2,3,4,5-tetrabromo-6-(2,4-dibromophenoxy)phenol
-
IC50: 0.0018 mM
2,3,4,5-tetrabromo-6-(3,5-dibromo-2-hydroxyphenoxy)phenol
-
IC50: 0.00079 mM
2,3,5-tribromo-6-(3,5-dibromo-2-hydroxyphenoxy)phenol
-
IC50: 0.0022 mM
2,4-dibromo-6-(2,4-dibromo-6-methoxyphenoxy)phenol
-
IC50: 0.01 mM
2,4-Dibromophenol
-
IC50: 0.034 mM
2,6-dibromo-4-[1-(3-bromo-4-hydroxyphenyl)-1-methylethyl]phenol
-
IC50: 0.005 mM
2-(4-chlorophenyl)-5-cyclohexyl-1,3,4-oxadiazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
2-([4-[(4-fluorobenzyl)oxy]butyl]sulfanyl)-5-(naphthalen-1-yl)-1,3,4-oxadiazole
-
-
2-alkyl benzopyran-4-ones
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
2-alkyl-6-hydroxy-4-H-benzopyran-4-one
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
2-phenyl-3-[3-(pyridin-3-yl)-4,5-dihydro-1H-pyrazol-5-yl]-1H-indole
molecular docking, compound is stabilized in the catalytic pocket of enzyme by pi-cation interaction with the catalytic Fe+ and formation of one hydrogen bond with Ile 676 amino acid
-
2-[[(4-bromophenyl)methyl]sulfanyl]-1-phenyl-1H-imidazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
-
2-[[(4-ethylphenyl)methyl]sulfanyl]-1-phenyl-1H-imidazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
-
3'-chloro-7,8-dihydroxyisoflavone
-
weak inhibition of isozyme 15-hLO-2
3,4,6,8-tetrabromooxanthren-1-ol
-
IC50: 0.0009 mM
3,4,6-tribromo-2-(2,4-dibromophenoxy)phenol
-
IC50: 0.005 mM
3,4-dibromo-2-(5-bromo-2-hydroxyphenoxy)phenol
-
IC50: 0.011 mM
3,6,8-tribromooxanthren-1-ol
-
IC50: 0.0008 mM
3-hydroxy-H-benzopyran-4-one derivatives
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
3-[3-bromo-5-(2,6-dibromo-4-{2-[2-(3-bromo-4-hydroxy-phenyl)-ethylcarbamoyl]-2-[(E)-hydroxyimino]-ethyl}-phenoxy)-4-methyl-phenyl]-N-[(E)-2-(3,5-dibromo-4-hydroxy-phenyl)-vinyl]-2-[(E)-hydroxyimino]-propionamide
-
IC50: 0.059 mM
3-[[(4-methylphenyl)methyl]sulfanyl]-1-phenyl-1H-1,2,4-triazole
mixed-type inhibitor, performs as potent inhibitor in a HEK-293 cell-based assay and binds in the U-shaped channel of 15-Lox-2
-
4',6,7-trihydroxyisoflavan
-
-
4',6,7-trihydroxyisoflavanone
-
weak inhibition of isozyme 15-hLO-2
4',6,7-trihydroxyisoflavone
-
weak inhibition of isozyme 15-hLO-2
4'-chloro-7,8-dihydroxyisoflavone
-
weak inhibition of isozyme 15-hLO-2
4,4'-propane-2,2-diylbis(2,6-dibromophenol)
-
IC50: 0.004 mM
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)butyl)-4-fluorobenzoate
-
-
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)methyl)-benzyl-4-fluorobenzoate
-
-
4-(2-chlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-(5-(1H-indol-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(2-chlorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(2-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(2-methoxyphenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(3-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(3-hydroxynaphthalen-2-yl)-1,3,4-oxadiazol-2-ylthio)-but-2-ynyl-4-fluorobenzoate
-
low solubility
4-(5-(4-chlorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(4-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(furan-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylamino)but-2-ynyl-thiophene-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-yn-1-ol
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-1H-indole-4-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-benzofuran-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-thiophene-2-carboxylate
-
-
4-(5-(naphthalen-1-yl)-1,3,4-thiadiazol-2-ylthio)but-2-ynyl-thiophene-2-carboxylate
-
low solubility
4-(5-(quinolin-5-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-(thiophen-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-(5-phenyl-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
-
4-allyl-2-methoxyphenyl 1-adamantanecarboxylate
-
-
4-allyl-2-methoxyphenyl 1-cyclohexanecarboxylate
-
-
4-allyl-2-methoxyphenyl 2-chlorobenzoate
-
-
4-allyl-2-methoxyphenyl 2-fluorobenzoate
-
-
4-allyl-2-methoxyphenyl 2-methylbenzoate
-
-
4-allyl-2-methoxyphenyl 2-pyridinecarboxylate
-
-
4-allyl-2-methoxyphenyl 3-chlorobenzoate
-
-
4-allyl-2-methoxyphenyl 3-fluorobenzoate
-
-
4-allyl-2-methoxyphenyl 3-methoxybenzoate
-
-
4-allyl-2-methoxyphenyl 3-methylbenzoate
-
-
4-allyl-2-methoxyphenyl 4-chlorobenzoate
-
-
4-allyl-2-methoxyphenyl 4-fluorobenzoate
-
-
4-allyl-2-methoxyphenyl 4-methoxybenzoate
-
-
4-allyl-2-methoxyphenyl 4-methylbenzoate
-
-
4-allyl-2-methoxyphenyl benzoate
-
-
4-allyl-2-methoxyphenyl isonicotinate
-
-
4-allyl-2-methoxyphenyl nicotinate
-
-
4-Bromophenol
-
IC50: 0.055 mM
4-butyl-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
-
-
4-pentyl-N-(2-[2-phenyl-5-[4-(trifluoromethyl)phenyl]-1H-imidazol-4-yl]ethyl)benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyrazin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-3-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-pyridin-4-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[2-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
-
-
4-pentyl-N-[3-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)propyl]benzenesulfonamide
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1H-imidazole-4-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2,4-difluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluoropyridine-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-methoxybenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trichlorothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trifluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4-difluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chloro-1-benzothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chlorothiophene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-fluorobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(difluoromethoxy)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(methylsulfonyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(triazan-2-yl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethoxy)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-bromobenzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-chloro-3-(trifluoromethyl)benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-[(trifluoromethyl)sulfanyl]benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl benzoate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclobutanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopentanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopropanecarboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl furan-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl naphthalene-2-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl thiophene-3-carboxylate
-
-
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]butyl 4-fluorobenzoate
-
-
4-[[5-(naphthalen-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-fluorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-chlorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-fluorobenzoate
-
-
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-methoxybenzoate
-
-
5,8,11,14-Eicosatetraynoic acid
6,11-dihydro[1]benzothiopyrano[4,3-b]indole
-
PD146176
6,7-dihydroxy-2-t-butylbenzopyran-4-one
-
weak inhibition of isozyme 15-hLO-2
6,7-dihydroxy-3',4'-methylenedioxyisoflavan
-
-
6,7-dihydroxy-3'-methylisoflavan
-
-
6,7-dihydroxy-3'-methylisoflavanone
-
weak inhibition of isozyme 15-hLO-2
6,7-dihydroxy-4'-methoxyisoflavan
-
-
6,7-dihydroxy-4'-methoxyisoflavanone
-
weak inhibition of isozyme 15-hLO-2
6,7-dihydroxyisoflavones
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
6-hydroxy-2-pentyl-4H-benzopyran-4-one
-
weak inhibition of isozyme 15-hLO-2
6-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]-1-phenylhexan-1-one
-
low solubility
7,8-dihydroxy-3',4'-dimethoxyisoflavan
-
-
7,8-dihydroxy-3'-methylisoflavone
-
weak inhibition of isozyme 15-hLO-2
7,8-dihydroxy-3'-trifluoromethylisoflavone
-
weak inhibition of isozyme 15-hLO-2
7,8-dihydroxy-4'-methoxyisoflavan
-
-
7,8-dihydroxy-4'-methylisoflavan
-
-
7,8-dihydroxy-4'-methylisoflavone
-
weak inhibition of isozyme 15-hLO-2
7,8-dihydroxyisoflavone
-
weak inhibition of isozyme 15-hLO-2
7-hydroxy-H-benzopyran-4-one derivatives
-
weak inhibition of isozymes 15-hLO-1 and 15-hLO-2
alpha-mangostin
-
NSC30552, a natural product, caspase-3 pathway inhibitor, performs selective inhibition of 12-LO
apigenin
-
IC50: 0.0034 mM without Triton X-100, IC50: 0.0003 mM in the presence of 0.01% Triton X-100
arachidonic acid
-
autoinactivates 15-hLO-1 to a much greater extent than linoleic acid at high substrate concentrations. No autoinactivation at low substrate concentrations
bestatin 7
-
IC50: 0.027 mM
cinnamyl 3,4-dihydroxy-cyanocinnamate
-
CDC
conjugated linoleic acids
-
conjugated linoleic acids may function as inhibitors of 15-LO-1 activity in macrophages/in vivo, overview
-
eicosatetraynoic acid
-
-
GATA-6
-
inhibits non-steroidal anti-inflammatory drugs-induced transcription of 15-LOX-1 in colorectal cancer cells
-
glucocorticoid
-
inhibits induction in monocytes
-
interferon-gamma
-
inhibits induction in monocytes
-
michellamine B
-
NSC661755, potent but non-selective inhibitor, a natural anti-viral agent
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N-(4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol)-2-ylthio)but-2-ynyl-thiophene-2-carboxamide
-
-
N-ethyl-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-[(3R)-1-(1-methyl-1-phenylethyl)pyrrolidin-3-yl]sulfamide
-
-
N-ethyl-N-[(3R)-1-[1-(4-fluorophenyl)ethyl]pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]sulfamide
-
-
N-[(3R)-1-(3,4-dichlorobenzyl)pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methylsulfamide
-
-
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-methylbenzenesulfonamide
-
-
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-(2-cyclopropyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-(2-methyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-(2-tert-butyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(2-methyl-1,3-thiazol-4-yl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(3-nitrophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(4-chlorophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(4-methoxyphenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[2-(4-methylphenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[5-(3-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[5-(4-fluorophenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-phenylpiperazine-1-sulfonamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
-
-
N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-4-pentylpiperazine-1-sulfonamide
-
-
N-[3-(2,5-diphenyl-1H-imidazol-4-yl)propyl]-4-pentylbenzenesulfonamide
-
-
neodysidenin
-
natural product from marine sponge Dysidea herbacea from Papua New Guinea, extraction and purification, overview, steady-state inhibition kinetics, competitive mode of inhibition, selective for 12-LO
nor-dihydro-guaiaretic acid
-
-
nordihydroguaiaretic acid
NSC172033
-
a synthetic compound from the NCI library
NSC292213
-
a synthetic compound from the NCI library
NSC617570
-
a synthetic compound from the NCI library
4,5-dichloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
4,5-dichloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
-
5,8,11,14-Eicosatetraynoic acid
-
-
5,8,11,14-Eicosatetraynoic acid
-
0.0009 mM, 50% inhibition
5,8,11,14-Eicosatetraynoic acid
-
inhibits reaction of linoleic acid
baicalein
-
-
baicalein
-
potent inhibitor, IC50: 0.0016 mM without Triton X-100, IC50: 0.038 mM in the presence of 0.01% Triton X-100
caffeic acid
-
specific inhibition of 15-LO
caffeic acid
-
specific inhibitor of 15-LOX-1
linoleic acid
-
autoinactivates 15-hLO-1 to a much greater extent than linoleic acid at high substrate concentrations. No autoinactivation at low substrate concentrations
linoleic acid
-
fully deuterated, the mode of inhibition, in the presence of 13-(S)-hydroxyoctadecadienoic acid, changes from mixed-type inhibition to competitive inhibition
nordihydroguaiaretic acid
-
-
nordihydroguaiaretic acid
-
IC50: 0.00011 mM
nordihydroguaiaretic acid
-
0.002 mM, 50% inhibition
siRNA
-
-
-
siRNA
-
knockdown of 15-LOX-2 expression, decreases chemokine ligand CXCL10 secretion from hypoxic macrophages and reduces T cell migration and CD69 expression
-
additional information
3-substituted pyrazoles and 4-substituted triazoles as inhibitors of human 15-lipoxygenase-1, overview. The 1N-substituent is not essential for activity or selectivity. Additional halogen substituents on the pyrazole ring increase activity. Further development leads to triazole-4-carboxanilides and 2-(3-pyrazolyl) benzoxazoles, which are potent and selective 15-LOX-1 inhibitors
-
additional information
certain oxazole-4-carbonitrile based LOX inhibitors share a high inhibitory potency for human and mouse ALOX15 but hardly inhibit other mammalian LOX-isoforms
-
additional information
-
certain oxazole-4-carbonitrile based LOX inhibitors share a high inhibitory potency for human and mouse ALOX15 but hardly inhibit other mammalian LOX-isoforms
-
additional information
imidazo[2,1-b]thiazole derivatives as inhibitors of 15-lipoxygenase, synthesis and evaluation of series of 3,6-diphenylimidazo[2,1-b]thiazol-5-amine derivatives, docking study, overview
-
additional information
N-substituted pyrazole-3-carboxamides as inhibitors of human 15-lipoxygenase, overview. No inhibition by 7h and 10a
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additional information
synthesis and evaluation of benzoylhydrazides and their diazene derivatives as inhibitors of 15-lipoxygenase, overview
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additional information
stylosin and some similar synthetic monoterpenoids show inhibitory effects on 15-LOX. A strong positive correlation is observed between 15-LOX inhibition potential and cytotoxicity of the compounds with apoptosis being the predominant mechanism of induced cell death
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additional information
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stylosin and some similar synthetic monoterpenoids show inhibitory effects on 15-LOX. A strong positive correlation is observed between 15-LOX inhibition potential and cytotoxicity of the compounds with apoptosis being the predominant mechanism of induced cell death
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additional information
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the enzyme undergoes suicidal inactivation, during fatty acid oxygenation
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additional information
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IC50 above 0.1 mM: compound 1a, compound 1b, compound 1d, compound 1e, compound 1g
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additional information
15-LOX2 in NHP cells is negatively regulated by Sp3
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additional information
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15-LOX2 in NHP cells is negatively regulated by Sp3
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additional information
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comparison of structural requirements for flavonoid inhibitory potency and selectivity against platelet 12-hLO, EC 1.13.11.31, and reticulocyte 15-hLO-1 and prostate epithelial 15-hLO-2, overview, catechols are essential for high potency, isoflavones and isoflavanones tend to select against 12-hLO, isoflavans tend to select against isozyme 15-hLO-1, but few flavonoids target isozyme 15-hLO-2, molecular modeling analysis, overview
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additional information
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development of an assay method for high throughput screening of libraries for platelet-type 12-hLO selective inhibitors, four organo-mercurial compounds with NCI library IDs NSC20410, NSC268879, NSC321237, and NSC321239, are also found to be selectively inhibitory, but not pursued further due to their potentially toxic side effects, overview
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additional information
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docking studies, inhibitor binding structures, overview
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additional information
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enzyme inhibition causes a decrease in amyloid-beta protein
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additional information
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sulproston, misoprostol, and ONO-AE-248 inhibit acetylsalicylic acid-induced 15(S)-HETE production
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additional information
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synthesis and evaluation of 2,4,5-tri-substituted imidazoles, which show highly potent inhibition of 15-lipoxygenase with excellent selectivity over the lipoxygenases 5-LO, EC 1.13.11.34, and platelet 12-LO, EC 1.13.11.31
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additional information
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15-LOX-1 can be inactivated by epigenetic silencing, hypermethylation of the CpG islands of the 15-LOX-1 promoter results in its reduced transcription in cancers, e.g. lymphomas, lung, prostate and cervix cancers. Brominated phenol esters are potent 15-LOX-1 inhibitors
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additional information
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intraarticular glucocorticoid treatment does not influence the 15-LO-1 enzyme in rheumatoid arthritis tissue
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additional information
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physico-chemical state of the substrate and the complex equilibrium between fatty acid monomers, acid soaps and micelles may impact the reaction specificity of LOX-isoforms
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Abortion, Spontaneous
Reduced reproduction with increased abortion rate in transgenic mice that overexpress 15-lipoxygenase.
Adenocarcinoma
15-lipoxygenase-1 expression upregulates and activates insulin-like growth factor-1 receptor in prostate cancer cells.
Adenocarcinoma
15-lipoxygenase-2 (15-LOX-2) is expressed in benign prostatic epithelium and reduced in prostate adenocarcinoma.
Adenocarcinoma
15-Lipoxygenase-2 expression in benign and neoplastic lung: an immunohistochemical study and correlation with tumor grade and proliferation.
Adenocarcinoma
Concordant induction of 15-lipoxygenase-1 and mutant p53 expression in human prostate adenocarcinoma: correlation with Gleason staging.
Adenocarcinoma
Conditional expression of human 15-lipoxygenase-1 in mouse prostate induces prostatic intraepithelial neoplasia: the FLiMP mouse model.
Adenocarcinoma
Reduced 15-lipoxygenase-2 immunostaining in prostate adenocarcinoma: correlation with grade and expression in high-grade prostatic intraepithelial neoplasia.
Adenocarcinoma, Bronchiolo-Alveolar
15-Lipoxygenase-2 expression in benign and neoplastic lung: an immunohistochemical study and correlation with tumor grade and proliferation.
Adenoma
The critical role of 15-lipoxygenase-1 in colorectal epithelial cell terminal differentiation and tumorigenesis.
Alzheimer Disease
Synthesis and structure-activity relationship study of tacrine-based pyrano[2,3-c]pyrazoles targeting AChE/BuChE and 15-LOX.
Anemia
Interleukin-4 and -13 induce upregulation of the murine macrophage 12/15-lipoxygenase activity: evidence for the involvement of transcription factor STAT6.
Anemia
Transient experimental anemia in cholesterol-fed rabbits induces systemic overexpression of the reticulocyte-type 15-lipoxygenase and protects from aortic lipid deposition.
arachidonate 12-lipoxygenase deficiency
Partially disturbed lamellar granule secretion in mild congenital ichthyosiform erythroderma with ALOX12B mutations.
Arthritis
Enhancement of PLGF production by 15-(S)-HETE via PI3K-Akt, NF-?B and COX-2 pathways in rheumatoid arthritis synovial fibroblast.
Arthritis
Involvement of 15-lipoxygenase in the inflammatory arthritis.
Arthritis, Rheumatoid
Arachidonate 15-lipoxygenase of reticulocyte-type in human rheumatoid arthritis type B synoviocytes and modulation of its activity by proinflammatory cytokines.
Arthritis, Rheumatoid
Enhancement of PLGF production by 15-(S)-HETE via PI3K-Akt, NF-?B and COX-2 pathways in rheumatoid arthritis synovial fibroblast.
Arthritis, Rheumatoid
Involvement of 15-lipoxygenase in the inflammatory arthritis.
Asthma
12/15-Lipoxygenase deficiency protects mice from allergic airways inflammation and increases secretory IgA levels.
Asthma
15-Lipoxygenase 1 in nasal polyps promotes CCL26/eotaxin 3 expression through extracellular signal-regulated kinase activation.
Asthma
15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells.
Asthma
A Cell-based Assay for Screening Lipoxygenase Inhibitors.
Asthma
An ex vivo model of severe asthma using reconstituted human bronchial epithelium.
Asthma
COX-1 dependent biosynthesis of 15-hydroxyeicosatetraenoic acid in human mast cells.
Asthma
Expression of 15-lipoxygenase type-1 in human mast cells.
Asthma
Human 15-lipoxygenase: induction by interleukin-4 and insights into positional specificity.
Asthma
Interleukin-13-induced MUC5AC is regulated by 15-lipoxygenase 1 pathway in human bronchial epithelial cells.
Asthma
Mice lacking 12/15-lipoxygenase have attenuated airway allergic inflammation and remodeling.
Asthma
On the biosynthesis and biological role of eoxins and 15-lipoxygenase-1 in airway inflammation and Hodgkin lymphoma.
Asthma
On the biosynthesis of 15-HETE and eoxin C4 by human airway epithelial cells.
Asthma
Real-time imaging of asthmatic epithelial cells identifies migratory deficiencies under Type-2 conditions.
Atherosclerosis
15-lipoxygenase-1 prevents vascular endothelial growth factor A- and placental growth factor-induced angiogenic effects in rabbit skeletal muscles via reduction in growth factor mRNA levels, NO bioactivity, and downregulation of VEGF receptor 2 expression.
Atherosclerosis
15-Lipoxygenase-2 expression in human macrophages induces chemokine secretion and T cell migration.
Atherosclerosis
15-Lipoxygenase-mediated modification of high-density lipoproteins impairs SR-BI- and ABCA1-dependent cholesterol efflux from macrophages.
Atherosclerosis
?(9)-tetrahydrocannabinol and its major metabolite ?(9)-tetrahydrocannabinol-11-oic acid as 15-lipoxygenase inhibitors.
Atherosclerosis
Arachidonate 15-lipoxygenase type B knockdown leads to reduced lipid accumulation and inflammation in atherosclerosis.
Atherosclerosis
Association of polymorphisms in the ALOX15B gene with coronary artery disease.
Atherosclerosis
Bioprospection of anti-inflammatory phytochemicals suggests rutaecarpine and quinine as promising 15-lipoxygenase inhibitors.
Atherosclerosis
Cannabidiol-2',6'-Dimethyl Ether, a Cannabidiol Derivative, Is a Highly Potent and Selective 15-Lipoxygenase Inhibitor.
Atherosclerosis
Clues for new therapeutics in osteoporosis and periodontal disease: new roles for lipoxygenases?
Atherosclerosis
Discovery of potent and selective inhibitors of human reticulocyte 15-lipoxygenase-1.
Atherosclerosis
Expanding expression of the 5-lipoxygenase pathway within the arterial wall during human atherogenesis.
Atherosclerosis
Human 15-lipoxygenase: induction by interleukin-4 and insights into positional specificity.
Atherosclerosis
Identification of oxidatively modified lipids in atherosclerotic lesions of human aortas.
Atherosclerosis
Interleukin 4 induces transcription of the 15-lipoxygenase I gene in human endothelial cells.
Atherosclerosis
Involvement of 15-lipoxygenase in early stages of atherogenesis.
Atherosclerosis
Kinetic and structural investigations of novel inhibitors of human epithelial 15-lipoxygenase-2.
Atherosclerosis
Membrane-dependent Activities of Human 15-LOX-2 and Its Murine Counterpart: IMPLICATIONS FOR MURINE MODELS OF ATHEROSCLEROSIS.
Atherosclerosis
Mouse peritoneal macrophages contain abundant omega-6 lipoxygenase activity that is independent of interleukin-4.
Atherosclerosis
Redox inactivation of human 15-lipoxygenase by marine-derived meroditerpenes and synthetic chromanes: archetypes for a unique class of selective and recyclable inhibitors.
Atherosclerosis
The two faces of the 15-lipoxygenase in atherosclerosis.
Atherosclerosis
Tissue markers in human atherosclerotic carotid artery plaque.
Atherosclerosis
Transcriptional regulation of 15-lipoxygenase expression by promoter methylation.
Blister
Partially disturbed lamellar granule secretion in mild congenital ichthyosiform erythroderma with ALOX12B mutations.
Brain Ischemia
Brozopine Inhibits 15-LOX-2 Metabolism Pathway After Transient Focal Cerebral Ischemia in Rats and OGD/R-Induced Hypoxia Injury in PC12 Cells.
Brain Neoplasms
Substituted (E)-2-(2-benzylidenehydrazinyl)-4-methylthiazole-5-carboxylates as dual inhibitors of 15-lipoxygenase & carbonic anhydrase II: synthesis, biochemical evaluation and docking studies.
Breast Neoplasms
Inhibition of IGF-1R and lipoxygenase by nordihydroguaiaretic acid (NDGA) analogs.
Breast Neoplasms
Reduction of isoforms of 15-lipoxygenase (15-LOX)-1 and 15-LOX-2 in human breast cancer.
Breast Neoplasms
Regulation of GSK3?/Nrf2 signaling pathway modulated erastin-induced ferroptosis in breast cancer.
Carcinogenesis
15-Lipoxygenase-1 expression suppresses the invasive properties of colorectal carcinoma cell lines HCT-116 and HT-29.
Carcinogenesis
15-lipoxygenase-1 metabolites down-regulate peroxisome proliferator-activated receptor gamma via the MAPK signaling pathway.
Carcinogenesis
15-lipoxygenase-1 prevents vascular endothelial growth factor A- and placental growth factor-induced angiogenic effects in rabbit skeletal muscles via reduction in growth factor mRNA levels, NO bioactivity, and downregulation of VEGF receptor 2 expression.
Carcinogenesis
15-Lipoxygenase-2 is differentially expressed in normal and neoplastic ovary.
Carcinogenesis
Conditional expression of human 15-lipoxygenase-1 in mouse prostate induces prostatic intraepithelial neoplasia: the FLiMP mouse model.
Carcinogenesis
DNA methylation paradigm shift: 15-lipoxygenase-1 upregulation in prostatic intraepithelial neoplasia and prostate cancer by atypical promoter hypermethylation.
Carcinogenesis
Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells.
Carcinogenesis
Lipoxygenase metabolism: roles in tumor progression and survival.
Carcinogenesis
Lipoxygenase modulation to reverse carcinogenesis.
Carcinogenesis
Pharmacogenomics of cancer chemopreventive isothiocyanate compound sulforaphane in the intestinal polyps of ApcMin/+ mice.
Carcinogenesis
Polyunsaturated fatty acid metabolizing 15-Lipoxygenase-1 (15-LO-1) expression in normal and tumorigenic human bladder tissues.
Carcinogenesis
The critical role of 15-lipoxygenase-1 in colorectal epithelial cell terminal differentiation and tumorigenesis.
Carcinogenesis
Transcriptional regulation of 15-lipoxygenase expression by promoter methylation.
Carcinogenesis
What are cyclooxygenases and lipoxygenases doing in the driver's seat of carcinogenesis?
Carcinoma
15-Lipoxygenase-2 expression in benign and neoplastic lung: an immunohistochemical study and correlation with tumor grade and proliferation.
Carcinoma
15-Lipoxygenase-2 expression in benign and neoplastic sebaceous glands and other cutaneous adnexa.
Carcinoma
15-Lipoxygenase-2 gene regulation by its product 15-(S)-hydroxyeicosatetraenoic acid through a negative feedback mechanism that involves peroxisome proliferator-activated receptor gamma.
Carcinoma
15S-Hydroxyeicosatetraenoic acid activates peroxisome proliferator-activated receptor gamma and inhibits proliferation in PC3 prostate carcinoma cells.
Carcinoma
Antineoplastic effects of 15(S)-hydroxyeicosatetraenoic acid and 13-S-hydroxyoctadecadienoic acid in non-small cell lung cancer.
Carcinoma
Enhanced 15-lipoxygenase activity and elevated eicosanoid production in kidney tumor microenvironment contribute to the inflammation and immune suppression.
Carcinoma
Interferon-gamma-induced 15-lipoxygenase-2 expression in normal human epidermal keratinocytes and a pathogenic link to psoriasis vulgaris.
Carcinoma
Opposing effects of 15-lipoxygenase-1 and -2 metabolites on MAPK signaling in prostate. Alteration in peroxisome proliferator-activated receptor gamma.
Carcinoma
Reduced 15-lipoxygenase-2 immunostaining in prostate adenocarcinoma: correlation with grade and expression in high-grade prostatic intraepithelial neoplasia.
Carcinoma
Reduced expression of 15-lipoxygenase 2 in human head and neck carcinomas.
Carcinoma
Regulation of 15-lipoxygenase expression by cytokines.
Carcinoma
Substituted (E)-2-(2-benzylidenehydrazinyl)-4-methylthiazole-5-carboxylates as dual inhibitors of 15-lipoxygenase & carbonic anhydrase II: synthesis, biochemical evaluation and docking studies.
Carcinoma
Synergistic effect of 15-lipoxygenase 2 and radiation in killing head-and-neck cancer.
Carcinoma
The modification of ferroptosis and abnormal lipometabolism through overexpression and knockdown of potential prognostic biomarker perilipin2 in gastric carcinoma.
Carcinoma
Transgenic expression of 15-lipoxygenase 2 (15-LOX2) in mouse prostate leads to hyperplasia and cell senescence.
Carcinoma
Tumor microenvironment determines drug efficacy in vitro - apoptotic and anti-inflammatory effects of 15-lipoxygenase metabolite, 13-HpOTrE.
Carcinoma, Hepatocellular
15-Lipoxygenase-1/15-hydroxyeicosatetraenoic acid promotes hepatocellular cancer cells growth through protein kinase B and heat shock protein 90 complex activation.
Carcinoma, Non-Small-Cell Lung
Antineoplastic effects of 15(S)-hydroxyeicosatetraenoic acid and 13-S-hydroxyoctadecadienoic acid in non-small cell lung cancer.
Carcinoma, Squamous Cell
Interferon-gamma-induced 15-lipoxygenase-2 expression in normal human epidermal keratinocytes and a pathogenic link to psoriasis vulgaris.
Carcinoma, Squamous Cell
Reduced expression of 15-lipoxygenase 2 in human head and neck carcinomas.
Carcinoma, Squamous Cell
Tumor microenvironment determines drug efficacy in vitro - apoptotic and anti-inflammatory effects of 15-lipoxygenase metabolite, 13-HpOTrE.
Cardiovascular Diseases
A Cell-based Assay for Screening Lipoxygenase Inhibitors.
Ciliary Motility Disorders
[Molecular genetic mechanisms of teratozoospermia].
Colonic Neoplasms
15-lipoxygenase-1 metabolites down-regulate peroxisome proliferator-activated receptor gamma via the MAPK signaling pathway.
Colorectal Neoplasms
15-lipoxygenase-1 metabolites down-regulate peroxisome proliferator-activated receptor gamma via the MAPK signaling pathway.
Colorectal Neoplasms
Evaluation of the activity and localization of 15-lipoxygenase-1 after introduction into human colorectal carcinoma Caco-2 cells.
Colorectal Neoplasms
Expression of 15-lipoxygenase-1 in human colorectal cancer.
Colorectal Neoplasms
Expression of 15-lipoxygenase-1 is regulated by histone acetylation in human colorectal carcinoma.
Communicable Diseases
Immunoregulatory role of 15-lipoxygenase in the pathogenesis of bacterial keratitis.
Coronary Artery Disease
Lipoxygenase pathways in atherogenesis.
Coronary Artery Disease
Oxidative Stress in the Male Germline: A Review of Novel Strategies to Reduce 4-Hydroxynonenal Production.
Coronary Artery Disease
The two faces of the 15-lipoxygenase in atherosclerosis.
Cystic Fibrosis
Kinetic and structural investigations of novel inhibitors of human epithelial 15-lipoxygenase-2.
Cystic Fibrosis
Novel keto-phospholipids are generated by monocytes and macrophages, detected in cystic fibrosis, and activate peroxisome proliferator-activated receptor-?.
Cystic Fibrosis
Reduced 15-lipoxygenase 2 and lipoxin A4/leukotriene B4 ratio in children with cystic fibrosis.
Dermatitis, Exfoliative
Partially disturbed lamellar granule secretion in mild congenital ichthyosiform erythroderma with ALOX12B mutations.
Encephalomalacia
Lipoxygenase activity in the brain regions of young chicks: isolation and some properties.
Eosinophilia
15-Lipoxygenase 1 in nasal polyps promotes CCL26/eotaxin 3 expression through extracellular signal-regulated kinase activation.
Erythema
The eicosanoid response to high dose UVR exposure of individuals prone and resistant to sunburn.
Erythema
The sunburn response in human skin is characterized by sequential eicosanoid profiles that may mediate its early and late phases.
Esophageal Neoplasms
Reduced 15S-lipoxygenase-2 expression in esophageal cancer specimens and cells and upregulation in vitro by the cyclooxygenase-2 inhibitor, NS398.
Glioblastoma
Influence of Lipoxygenase Inhibition on Glioblastoma Cell Biology.
Glioma
Increased invasion of malignant gliomas after 15-LO-1 and HSV-tk/ganciclovir combination gene therapy.
Granuloma
PPAR? is critical for Mycobacterium tuberculosis induction of Mcl-1 and limitation of human macrophage apoptosis.
Hematologic Neoplasms
15-Lipoxygenases in cancer: A double-edged sword?
Herpes Zoster
Vascular endothelial tight junctions and barrier function are disrupted by 15(S)-hydroxyeicosatetraenoic acid partly via protein kinase C ?-mediated zona occludens-1 phosphorylation at threonine 770/772.
Hodgkin Disease
Metabolism of anandamide into eoxamides by 15-lipoxygenase-1 and glutathione transferases.
Hodgkin Disease
On the biosynthesis and biological role of eoxins and 15-lipoxygenase-1 in airway inflammation and Hodgkin lymphoma.
Hypercholesterolemia
Hypercholesterolemia enhances 15-lipoxygenase-mediated vasorelaxation and acetylcholine-induced hypotension.
Hypertension, Pulmonary
Hypoxia promotes rabbit pulmonary artery smooth muscle cells proliferation through a 15-LOX-2 product 15(S)-hydroxyeicosatetraenoic acid.
Hypertension, Pulmonary
Positive feedback-loop of telomerase reverse transcriptase and 15-lipoxygenase-2 promotes pulmonary hypertension.
Hypotension
15-Lipoxygenase metabolites contribute to age-related reduction in acetylcholine-induced hypotension in rabbits.
Hypotension
Endothelial 15-lipoxygenase-1 overexpression increases acetylcholine-induced hypotension and vasorelaxation in rabbits.
Hypoxia, Brain
Inhibition of 15-lipoxygenase (15-LOX) reverses hypoxia-induced down-regulation of potassium channels Kv1.5 and Kv2.1Inhibition of 15-lipoxygenase (15-LOX) reverses hypoxia-induced down-regulation of potassium channels Kv1.5 and Kv2.1.
Ichthyosiform Erythroderma, Congenital
Partially disturbed lamellar granule secretion in mild congenital ichthyosiform erythroderma with ALOX12B mutations.
Ichthyosis
Partially disturbed lamellar granule secretion in mild congenital ichthyosiform erythroderma with ALOX12B mutations.
Infections
Cell-autonomous induction of functional tumor suppressor 15-lipoxygenase 2 (15-LOX2) contributes to replicative senescence of human prostate progenitor cells.
Infections
Chronic infection during placental malaria is associated with up-regulation of cycloxygenase-2.
Infections
PPAR? is critical for Mycobacterium tuberculosis induction of Mcl-1 and limitation of human macrophage apoptosis.
Keratosis, Actinic
Interferon-gamma-induced 15-lipoxygenase-2 expression in normal human epidermal keratinocytes and a pathogenic link to psoriasis vulgaris.
Kidney Neoplasms
Tumor-associated macrophages mediate immunosuppression in the renal cancer microenvironment by activating the 15-lipoxygenase-2 pathway.
Leukemia
Arachidonate 15-lipoxygenase is required for chronic myeloid leukemia stem cell survival.
Leukemia
Tumor microenvironment determines drug efficacy in vitro - apoptotic and anti-inflammatory effects of 15-lipoxygenase metabolite, 13-HpOTrE.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Arachidonate 15-lipoxygenase is required for chronic myeloid leukemia stem cell survival.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Effect of 15-lipoxygenase metabolites, 15-(S)-HPETE and 15-(S)-HETE on chronic myelogenous leukemia cell line K-562: reactive oxygen species (ROS) mediate caspase-dependent apoptosis.
Liver Diseases, Alcoholic
Hepatic overproduction of 13-HODE due to ALOX15 upregulation contributes to alcohol-induced liver injury in mice.
Lung Neoplasms
15-Lipoxygenase-2/15(S)-hydroxyeicosatetraenoic acid regulates cell proliferation and metastasis via the STAT3 pathway in lung adenocarcinoma.
Lupus Erythematosus, Systemic
Ku autoantigen (DNA helicase) is required for interleukins-13/-4-induction of 15-lipoxygenase-1 gene expression in human epithelial cells.
Lymphoma
Beta caryophyllene and caryophyllene oxide, isolated from Aegle marmelos, as the potent anti-inflammatory agents against lymphoma and neuroblastoma cells.
Lymphoma
Differential expression of cysteinyl leukotriene receptor 1 and 15-lipoxygenase-1 in non-Hodgkin lymphomas.
Lymphoma, Large-Cell, Anaplastic
Differential expression of cysteinyl leukotriene receptor 1 and 15-lipoxygenase-1 in non-Hodgkin lymphomas.
Malaria
Chronic infection during placental malaria is associated with up-regulation of cycloxygenase-2.
Metabolic Diseases
The emerging role of COX-2, 15-LOX, and PPAR? in metabolic diseases and cancer: An introduction to novel multi-target directed ligands (MTDLs).
Multiple Sclerosis
Oxidative Stress in the Male Germline: A Review of Novel Strategies to Reduce 4-Hydroxynonenal Production.
Myocardial Ischemia
The Arachidonate 15-Lipoxygenase Enzyme Product 15-HETE Is Present in Heart Tissue from Patients with Ischemic Heart Disease and Enhances Clot Formation.
Nasal Polyps
15-Lipoxygenase 1 in nasal polyps promotes CCL26/eotaxin 3 expression through extracellular signal-regulated kinase activation.
Nasal Polyps
Inhibition of arachidonate 15-lipoxygenase reduces the epithelial-mesenchymal transition in eosinophilic chronic rhinosinusitis with nasal polyps.
Nasal Polyps
Predictive significance of arachidonate 15-lipoxygenase for eosinophilic chronic rhinosinusitis with nasal polyps.
Neoplasm Metastasis
15-Lipoxygenase-1 expression suppresses the invasive properties of colorectal carcinoma cell lines HCT-116 and HT-29.
Neoplasm Metastasis
DNA methylation paradigm shift: 15-lipoxygenase-1 upregulation in prostatic intraepithelial neoplasia and prostate cancer by atypical promoter hypermethylation.
Neoplasm Metastasis
Inhibition of carcinogenesis in transgenic mouse models over-expressing 15-lipoxygenase in the vascular wall under the control of murine preproendothelin-1 promoter.
Neoplasm Metastasis
Reduction of isoforms of 15-lipoxygenase (15-LOX)-1 and 15-LOX-2 in human breast cancer.
Neoplasm Metastasis
The effect of 15-lipoxygenase-1 expression on cancer cells.
Neoplasms
15-lipoxygenase 2 (15-LOX2) is a functional tumor suppressor that regulates human prostate epithelial cell differentiation, senescence, and growth (size).
Neoplasms
15-Lipoxygenase inhibitors: a patent review.
Neoplasms
15-lipoxygenase-1 expression upregulates and activates insulin-like growth factor-1 receptor in prostate cancer cells.
Neoplasms
15-Lipoxygenase-1 has anti-tumorigenic effects in colorectal cancer.
Neoplasms
15-lipoxygenase-1 metabolites down-regulate peroxisome proliferator-activated receptor gamma via the MAPK signaling pathway.
Neoplasms
15-lipoxygenase-2 (15-LOX-2) is expressed in benign prostatic epithelium and reduced in prostate adenocarcinoma.
Neoplasms
15-Lipoxygenase-2 expression in benign and neoplastic lung: an immunohistochemical study and correlation with tumor grade and proliferation.
Neoplasms
15-Lipoxygenase-2 gene regulation by its product 15-(S)-hydroxyeicosatetraenoic acid through a negative feedback mechanism that involves peroxisome proliferator-activated receptor gamma.
Neoplasms
15-Lipoxygenase-2 is differentially expressed in normal and neoplastic ovary.
Neoplasms
15-Lipoxygenase-2/15(S)-hydroxyeicosatetraenoic acid regulates cell proliferation and metastasis via the STAT3 pathway in lung adenocarcinoma.
Neoplasms
15-Lipoxygenases and its metabolites 15(S)-HETE and 13(S)-HODE in the development of non-small cell lung cancer.
Neoplasms
15-Lipoxygenases in cancer: A double-edged sword?
Neoplasms
15S-Lipoxygenase-2 mediates arachidonic acid-stimulated adhesion of human breast carcinoma cells through the activation of TAK1, MKK6, and p38 MAPK.
Neoplasms
A Cell-based Assay for Screening Lipoxygenase Inhibitors.
Neoplasms
A high throughput screen identifies potent and selective inhibitors to human epithelial 15-lipoxygenase-2.
Neoplasms
Antineoplastic effects of 15(S)-hydroxyeicosatetraenoic acid and 13-S-hydroxyoctadecadienoic acid in non-small cell lung cancer.
Neoplasms
Cell-autonomous induction of functional tumor suppressor 15-lipoxygenase 2 (15-LOX2) contributes to replicative senescence of human prostate progenitor cells.
Neoplasms
Concordant induction of 15-lipoxygenase-1 and mutant p53 expression in human prostate adenocarcinoma: correlation with Gleason staging.
Neoplasms
Conditional expression of human 15-lipoxygenase-1 in mouse prostate induces prostatic intraepithelial neoplasia: the FLiMP mouse model.
Neoplasms
Cooperative induction of 15-lipoxygenase in rheumatoid synovial cells by IL-4 and proinflammatory cytokines.
Neoplasms
Differential expression of cysteinyl leukotriene receptor 1 and 15-lipoxygenase-1 in non-Hodgkin lymphomas.
Neoplasms
Discovery of potent and selective inhibitors of human reticulocyte 15-lipoxygenase-1.
Neoplasms
Distinct effects of annexin A7 and p53 on arachidonate lipoxygenation in prostate cancer cells involve 5-lipoxygenase transcription.
Neoplasms
Downregulation of 15-lipoxygenase 2 by glucocorticoid receptor in prostate cancer cells.
Neoplasms
Downregulation of vascular endothelial growth factor and induction of tumor dormancy by 15-lipoxygenase-2 in prostate cancer.
Neoplasms
Effects of Ursolic Acid and its Analogues on Soybean 15-Lipoxygenase Activity and the Proliferation Rate of A human Gastric Tumour Cell Line.
Neoplasms
Evidence that Sp1 positively and Sp3 negatively regulate and androgen does not directly regulate functional tumor suppressor 15-lipoxygenase 2 (15-LOX2) gene expression in normal human prostate epithelial cells.
Neoplasms
Expanding the anticancer potential of 1,2,3-triazoles via simultaneously targeting Cyclooxygenase-2, 15-lipoxygenase and tumor-associated carbonic anhydrases.
Neoplasms
Fish oil supplementation inhibits NNK-induced lung carcinogenesis in the A/J mouse.
Neoplasms
Gamma tocopherol upregulates the expression of 15-S-HETE and induces growth arrest through a PPAR gamma-dependent mechanism in PC-3 human prostate cancer cells.
Neoplasms
Increased invasion of malignant gliomas after 15-LO-1 and HSV-tk/ganciclovir combination gene therapy.
Neoplasms
Increased neuroinflammatory and arachidonic acid cascade markers, and reduced synaptic proteins, in brain of HIV-1 transgenic rats.
Neoplasms
Inhibition of carcinogenesis in transgenic mouse models over-expressing 15-lipoxygenase in the vascular wall under the control of murine preproendothelin-1 promoter.
Neoplasms
Inhibition of IGF-1R and lipoxygenase by nordihydroguaiaretic acid (NDGA) analogs.
Neoplasms
Intravitreal adenoviral 15-lipoxygenase-1 gene transfer prevents vascular endothelial growth factor A induced neovascularization in rabbit eyes.
Neoplasms
Inverse relationship between 15-lipoxygenase-2 and PPAR-gamma gene expression in normal epithelia compared with tumor epithelia.
Neoplasms
LC/ESR/MS study of pH-dependent radical generation from 15-LOX-catalyzed DPA peroxidation.
Neoplasms
Opposing effects of 15-lipoxygenase-1 and -2 metabolites on MAPK signaling in prostate. Alteration in peroxisome proliferator-activated receptor gamma.
Neoplasms
Overexpression of 15-lipoxygenase-1 in PC-3 human prostate cancer cells increases tumorigenesis.
Neoplasms
Prostate Tumor Growth and Recurrence Can Be Modulated by the omega-6:omega-3 Ratio in Diet: Athymic Mouse Xenograft Model Simulating Radical Prostatectomy.
Neoplasms
Prostate tumor growth can be modulated by dietarily targeting the 15-lipoxygenase-1 and cyclooxygenase-2 enzymes.
Neoplasms
Pulmonary Eosinophilic Granulomatosis with Polyangiitis Has IgG4 Plasma Cells and Immunoregulatory Features.
Neoplasms
Reduced 15-lipoxygenase-2 immunostaining in prostate adenocarcinoma: correlation with grade and expression in high-grade prostatic intraepithelial neoplasia.
Neoplasms
Reduced 15S-lipoxygenase-2 expression in esophageal cancer specimens and cells and upregulation in vitro by the cyclooxygenase-2 inhibitor, NS398.
Neoplasms
Reduced expression of 15-lipoxygenase 2 in human head and neck carcinomas.
Neoplasms
Reduction of isoforms of 15-lipoxygenase (15-LOX)-1 and 15-LOX-2 in human breast cancer.
Neoplasms
Role of eicosanoids in prostate cancer progression.
Neoplasms
Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants.
Neoplasms
Synergistic effect of 15-lipoxygenase 2 and radiation in killing head-and-neck cancer.
Neoplasms
The effect of 15-lipoxygenase-1 expression on cancer cells.
Neoplasms
The emerging role of COX-2, 15-LOX, and PPAR? in metabolic diseases and cancer: An introduction to novel multi-target directed ligands (MTDLs).
Neoplasms
The importance of 15-lipoxygenase inhibitors in cancer treatment.
Neoplasms
Transgenic expression of 15-lipoxygenase 2 (15-LOX2) in mouse prostate leads to hyperplasia and cell senescence.
Neoplasms
Tumor microenvironment determines drug efficacy in vitro - apoptotic and anti-inflammatory effects of 15-lipoxygenase metabolite, 13-HpOTrE.
Neoplasms
Tumor-associated macrophages mediate immunosuppression in the renal cancer microenvironment by activating the 15-lipoxygenase-2 pathway.
Neoplasms
Up-regulation of 15-lipoxygenase enzymes and products in functional and non-functional pituitary adenomas.
Neoplasms
Utility of novel 2-furanones in synthesis of other heterocyclic compounds having anti-inflammatory activity with dual COX2/LOX inhibition.
Neuroblastoma
Beta caryophyllene and caryophyllene oxide, isolated from Aegle marmelos, as the potent anti-inflammatory agents against lymphoma and neuroblastoma cells.
Osteoarthritis
Increased 15-lipoxygenase-1 expression in chondrocytes contributes to the pathogenesis of osteoarthritis.
Periodontal Diseases
Clues for new therapeutics in osteoporosis and periodontal disease: new roles for lipoxygenases?
Pituitary Neoplasms
Up-regulation of 15-lipoxygenase enzymes and products in functional and non-functional pituitary adenomas.
Pre-Eclampsia
Preeclampsia activates 15-lipoxygenase and its metabolite 15-hydroxyeicosatetraenoic acid enhances constriction in umbilical arteries.
Prostatic Hyperplasia
Transgenic expression of 15-lipoxygenase 2 (15-LOX2) in mouse prostate leads to hyperplasia and cell senescence.
Prostatic Intraepithelial Neoplasia
Conditional expression of human 15-lipoxygenase-1 in mouse prostate induces prostatic intraepithelial neoplasia: the FLiMP mouse model.
Prostatic Intraepithelial Neoplasia
Reduced 15-lipoxygenase-2 immunostaining in prostate adenocarcinoma: correlation with grade and expression in high-grade prostatic intraepithelial neoplasia.
Prostatic Neoplasms
15-lipoxygenase 2 (15-LOX2) is a functional tumor suppressor that regulates human prostate epithelial cell differentiation, senescence, and growth (size).
Prostatic Neoplasms
15-lipoxygenase metabolites of docosahexaenoic acid inhibit prostate cancer cell proliferation and survival.
Prostatic Neoplasms
15-Lipoxygenase-1-mediated metabolism of docosahexaenoic acid is required for syndecan-1 signaling and apoptosis in prostate cancer cells.
Prostatic Neoplasms
Cell-autonomous induction of functional tumor suppressor 15-lipoxygenase 2 (15-LOX2) contributes to replicative senescence of human prostate progenitor cells.
Prostatic Neoplasms
Concordant induction of 15-lipoxygenase-1 and mutant p53 expression in human prostate adenocarcinoma: correlation with Gleason staging.
Prostatic Neoplasms
DNA methylation paradigm shift: 15-lipoxygenase-1 upregulation in prostatic intraepithelial neoplasia and prostate cancer by atypical promoter hypermethylation.
Prostatic Neoplasms
Downregulation of 15-lipoxygenase 2 by glucocorticoid receptor in prostate cancer cells.
Prostatic Neoplasms
Downregulation of vascular endothelial growth factor and induction of tumor dormancy by 15-lipoxygenase-2 in prostate cancer.
Prostatic Neoplasms
Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells.
Prostatic Neoplasms
Opposing effects of 15-lipoxygenase-1 and -2 metabolites on MAPK signaling in prostate. Alteration in peroxisome proliferator-activated receptor gamma.
Prostatic Neoplasms
Prostate tumor growth can be modulated by dietarily targeting the 15-lipoxygenase-1 and cyclooxygenase-2 enzymes.
Prostatic Neoplasms
Role of eicosanoids in prostate cancer progression.
Prostatic Neoplasms
Stylosin and some of its synthetic derivatives induce apoptosis in prostate cancer cells as 15-lipoxygenase enzyme inhibitors.
Prostatic Neoplasms
Transgenic expression of 15-lipoxygenase 2 (15-LOX2) in mouse prostate leads to hyperplasia and cell senescence.
Prostatic Neoplasms
Tumor-suppressive functions of 15-Lipoxygenase-2 and RB1CC1 in prostate cancer.
Psoriasis
Interferon-gamma-induced 15-lipoxygenase-2 expression in normal human epidermal keratinocytes and a pathogenic link to psoriasis vulgaris.
Psoriasis
Lack of association of ALOX12 and ALOX15B polymorphisms with psoriasis despite altered urinary excretion of 12(S)-HETE.
Psoriasis
Modulation of Cox-1, 5-, 12- and 15-Lox by popular herbal remedies used in southern Italy against psoriasis and other skin diseases.
Psoriasis
Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes.
Skin Diseases
Modulation of Cox-1, 5-, 12- and 15-Lox by popular herbal remedies used in southern Italy against psoriasis and other skin diseases.
Squamous Cell Carcinoma of Head and Neck
Reduced expression of 15-lipoxygenase 2 in human head and neck carcinomas.
Teratozoospermia
[Molecular genetic mechanisms of teratozoospermia].
Thyroiditis
Ku autoantigen (DNA helicase) is required for interleukins-13/-4-induction of 15-lipoxygenase-1 gene expression in human epithelial cells.
Urinary Bladder Neoplasms
Polyunsaturated fatty acid metabolizing 15-Lipoxygenase-1 (15-LO-1) expression in normal and tumorigenic human bladder tissues.
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0.00398
4-[(E)-benzoyldiazenyl]benzonitrile
pH and temperature not specified in the publication
0.00081
N'-(4-methylphenyl)benzohydrazide
pH and temperature not specified in the publication
0.1
2-([4-[(4-fluorobenzyl)oxy]butyl]sulfanyl)-5-(naphthalen-1-yl)-1,3,4-oxadiazole
-
Ki above 0.1 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0006
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)butyl)-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.07
4-((5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)methyl)-benzyl-4-fluorobenzoate
-
apparent value, Ki above 0.07 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000023
4-(5-(1H-indol-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000057
4-(5-(2-chlorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000043
4-(5-(2-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000081
4-(5-(2-methoxyphenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-(5-(3-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-(5-(4-chlorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-(5-(4-fluorophenyl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.001
4-(5-(furan-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0013
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylamino)but-2-ynyl-thiophene-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0035
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-yn-1-ol
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000076
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-1H-indole-4-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000015
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-benzofuran-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000019
4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-thiophene-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00014
4-(5-(quinolin-5-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000082
4-(5-(thiophen-2-yl)-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000026
4-(5-phenyl-1,3,4-oxadiazol-2-ylthio)but-2-ynyl-4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-2-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1-benzothiophene-3-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0014
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 1H-imidazole-4-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2,4-difluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-fluoropyridine-3-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00047
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 2-methoxybenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trichlorothiophene-2-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000016
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4,5-trifluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3,4-difluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000027
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-(trifluoromethyl)benzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000031
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chloro-1-benzothiophene-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-chlorothiophene-2-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 3-fluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(difluoromethoxy)benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000033
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(methylsulfonyl)benzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000015
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(triazan-2-yl)benzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethoxy)benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-(trifluoromethyl)benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-bromobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.0001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-chloro-3-(trifluoromethyl)benzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-[(trifluoromethyl)sulfanyl]benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl benzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000085
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclobutanecarboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopentanecarboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00027
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl cyclopropanecarboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00017
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl furan-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000022
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl naphthalene-2-carboxylate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl thiophene-3-carboxylate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.000026
4-[[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]butyl 4-fluorobenzoate
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-[[5-(naphthalen-2-yl)-1,3,4-oxadiazol-2-yl]sulfanyl]but-2-yn-1-yl 4-fluorobenzoate
-
Ki less than 0.00001 mM, apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-chlorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-fluorobenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00001
4-{[5-(naphthalen-1-yl)-1,3,4-oxadiazol-2-yl]sulfanyl}but-2-yn-1-yl 4-methoxybenzoate
-
apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.00018 - 0.0011
baicalein
0.008
dysidenin
-
above, pH 7.5, recombinant isozyme 15-hLO-1
0.005 - 0.017
linoleic acid
0.002
N-(4-(5-(naphthalen-1-yl)-1,3,4-oxadiazol)-2-ylthio)but-2-ynyl-thiophene-2-carboxamide
-
apparent value, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C
0.5
neodysidenin
-
above, pH 7.5, recombinant isozyme 15-hLO-1
additional information
additional information
-
-
-
0.00018
baicalein
-
-
0.0011
baicalein
-
in the presence of 0.01% Triton X-100
0.005
linoleic acid
-
fully deuterated, in the presence of 13-(S)-hydroxyoctadecadienoic acid
0.017
linoleic acid
-
fully deuterated
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0.000032
4,5-dichloro-N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0171
4-methyl-2-(4-methylpiperazinyl)pyrimido[4,5-b]benzothiazine
Homo sapiens
pH 7.0, 25°C
-
0.00978
4-[(E)-benzoyldiazenyl]benzonitrile
Homo sapiens
pH and temperature not specified in the publication
0.0002
5-(methylamino)-2-(naphthalen-1-yl)-4,5-dihydro-1,3-oxazole-4-carbonitrile
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.00055
5-chloro-N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.000197
6,6a,11,11a-tetrahydro[1]benzothiopyrano[4,3-b]indole
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.0261
adamantyl caffeate
Homo sapiens
pH 7.0, 25°C
-
0.399
bornyl vanillate
Homo sapiens
pH 7.0, 25°C
-
0.00009
ethyl 6-chloro-3-[(3S)-3-hydroxy-7-methyloctanoyl]-2,3-dihydro-1H-indole-2-carboxylate
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
-
0.011
fenchyl caffeate
Homo sapiens
pH 7.0, 25°C
-
0.00535
N'-(4-methylphenyl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000099
N-(2,4-dichlorophenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.0001
N-(2-chloro-4-fluorophenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000025
NDGA
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00697
phenyl[(E)-phenyldiazenyl]methanone
Homo sapiens
pH and temperature not specified in the publication
0.0668
stylosin
Homo sapiens
pH 7.0, 25°C
-
0.00034
1-phenyl-2-([[4-(trifluoromethyl)phenyl]methyl]sulfanyl)-1H-imidazole
Homo sapiens
pH 7.5, 23°C
-
0.0018
2,3,4,5-tetrabromo-6-(2,4-dibromophenoxy)phenol
Homo sapiens
-
IC50: 0.0018 mM
0.00079
2,3,4,5-tetrabromo-6-(3,5-dibromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.00079 mM
0.0022
2,3,5-tribromo-6-(3,5-dibromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.0022 mM
0.01
2,4-dibromo-6-(2,4-dibromo-6-methoxyphenoxy)phenol
Homo sapiens
-
IC50: 0.01 mM
0.034
2,4-Dibromophenol
Homo sapiens
-
IC50: 0.034 mM
0.005
2,6-dibromo-4-[1-(3-bromo-4-hydroxyphenyl)-1-methylethyl]phenol
Homo sapiens
-
IC50: 0.005 mM
0.0026
2-(4-chlorophenyl)-5-cyclohexyl-1,3,4-oxadiazole
Homo sapiens
pH 7.5, 23°C
0.00053
2-[[(4-bromophenyl)methyl]sulfanyl]-1-phenyl-1H-imidazole
Homo sapiens
pH 7.5, 23°C
-
0.00087
2-[[(4-ethylphenyl)methyl]sulfanyl]-1-phenyl-1H-imidazole
Homo sapiens
pH 7.5, 23°C
-
0.0062
3'-chloro-7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0009
3,4,6,8-tetrabromooxanthren-1-ol
Homo sapiens
-
IC50: 0.0009 mM
0.005
3,4,6-tribromo-2-(2,4-dibromophenoxy)phenol
Homo sapiens
-
IC50: 0.005 mM
0.011
3,4-dibromo-2-(5-bromo-2-hydroxyphenoxy)phenol
Homo sapiens
-
IC50: 0.011 mM
0.0008
3,6,8-tribromooxanthren-1-ol
Homo sapiens
-
IC50: 0.0008 mM
0.059
3-[3-bromo-5-(2,6-dibromo-4-{2-[2-(3-bromo-4-hydroxy-phenyl)-ethylcarbamoyl]-2-[(E)-hydroxyimino]-ethyl}-phenoxy)-4-methyl-phenyl]-N-[(E)-2-(3,5-dibromo-4-hydroxy-phenyl)-vinyl]-2-[(E)-hydroxyimino]-propionamide
Homo sapiens
-
IC50: 0.059 mM
0.0031
3-[[(4-methylphenyl)methyl]sulfanyl]-1-phenyl-1H-1,2,4-triazole
Homo sapiens
pH 7.5, 23°C
-
0.00051 - 0.071
4',6,7-trihydroxyisoflavan
0.0038 - 0.1
4',6,7-trihydroxyisoflavanone
0.049
4',6,7-trihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.009
4'-chloro-7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.004
4,4'-propane-2,2-diylbis(2,6-dibromophenol)
Homo sapiens
-
IC50: 0.004 mM
0.045 - 0.132
4-(2-chlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
0.055 - 0.378
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
0.036 - 0.133
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
0.055
4-Bromophenol
Homo sapiens
-
IC50: 0.055 mM
0.014 - 0.05
4-butyl-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
0.000072 - 0.000372
4-pentyl-N-(2-[2-phenyl-5-[4-(trifluoromethyl)phenyl]-1H-imidazol-4-yl]ethyl)benzenesulfonamide
0.01
4-pentyl-N-[2-(5-phenyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
above, versus substrate linoleic acid
0.00281
4-pentyl-N-[2-(5-phenyl-2-pyrazin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.00097 - 5.321
4-pentyl-N-[2-(5-phenyl-2-pyridin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
0.00056
4-pentyl-N-[2-(5-phenyl-2-pyridin-3-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000087 - 3.211
4-pentyl-N-[2-(5-phenyl-2-pyridin-4-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
0.000006 - 0.000013
4-pentyl-N-[2-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
0.000053 - 0.000396
4-pentyl-N-[3-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)propyl]benzenesulfonamide
0.018
6,7-dihydroxy-2-t-butylbenzopyran-4-one
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.00035 - 0.016
6,7-dihydroxy-3',4'-methylenedioxyisoflavan
0.00021 - 0.0083
6,7-dihydroxy-3'-methylisoflavan
0.00021 - 0.014
6,7-dihydroxy-3'-methylisoflavanone
0.00015 - 0.1
6,7-dihydroxy-4'-methoxyisoflavan
0.0016 - 0.019
6,7-dihydroxy-4'-methoxyisoflavanone
0.038
6-hydroxy-2-pentyl-4H-benzopyran-4-one
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.1
7,8-dihydroxy-3',4'-dimethoxyisoflavan
0.011
7,8-dihydroxy-3'-methylisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0083
7,8-dihydroxy-3'-trifluoromethylisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0037 - 0.1
7,8-dihydroxy-4'-methoxyisoflavan
0.0057 - 0.1
7,8-dihydroxy-4'-methylisoflavan
0.0078
7,8-dihydroxy-4'-methylisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.013
7,8-dihydroxyisoflavone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0031 - 0.05
alpha-mangostin
0.0003 - 100
apigenin
Homo sapiens
-
IC50: 0.0034 mM without Triton X-100, IC50: 0.0003 mM in the presence of 0.01% Triton X-100
0.038 - 100
baicalein
Homo sapiens
-
potent inhibitor, IC50: 0.0016 mM without Triton X-100, IC50: 0.038 mM in the presence of 0.01% Triton X-100
0.027
bestatin 7
Homo sapiens
-
IC50: 0.027 mM
0.0076 - 0.05
michellamine B
0.031 - 0.186
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
0.08 - 0.822
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
0.038 - 0.375
N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
0.01 - 0.132
N-ethyl-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-[(3R)-1-(1-methyl-1-phenylethyl)pyrrolidin-3-yl]sulfamide
0.003 - 0.75
N-ethyl-N-[(3R)-1-[1-(4-fluorophenyl)ethyl]pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]sulfamide
0.011 - 0.083
N-[(3R)-1-(3,4-dichlorobenzyl)pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methylsulfamide
0.000364 - 0.0028
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-methylbenzenesulfonamide
0.000033 - 0.000162
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
0.01
N-[2-(2-cyclopropyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
0.01
N-[2-(2-methyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
above, versus substrate linoleic acid
0.00192 - 0.01
N-[2-(2-tert-butyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
0.00072
N-[2-[2-(2-methyl-1,3-thiazol-4-yl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000099 - 0.0011
N-[2-[2-(3-nitrophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.000021 - 0.0011
N-[2-[2-(4-chlorophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.01
N-[2-[2-(4-methoxyphenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
above, versus substrate linoleic acid
0.003
N-[2-[2-(4-methylphenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000082 - 0.000531
N-[2-[5-(3-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.000059 - 0.000261
N-[2-[5-(4-fluorophenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.000014 - 0.00005
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
0.212 - 3.45
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-phenylpiperazine-1-sulfonamide
0.083 - 0.719
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
0.272 - 2.41
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
0.091 - 0.646
N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-4-pentylpiperazine-1-sulfonamide
0.00014 - 0.000914
N-[3-(2,5-diphenyl-1H-imidazol-4-yl)propyl]-4-pentylbenzenesulfonamide
0.5
neodysidenin
Homo sapiens
-
above, pH 7.5, recombinant isozyme 15-hLO-1
0.00011
nordihydroguaiaretic acid
Homo sapiens
-
IC50: 0.00011 mM
0.1
additional information
Homo sapiens
-
IC50 above 0.1 mM: compound 1a, compound 1b, compound 1d, compound 1e, compound 1g
-
0.00051
4',6,7-trihydroxyisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.071
4',6,7-trihydroxyisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-2
0.0038
4',6,7-trihydroxyisoflavanone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-2
0.1
4',6,7-trihydroxyisoflavanone
Homo sapiens
-
above, pH 7.5, 22°C, isozyme 15-hLO-1
0.045
4-(2-chlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.132
4-(2-chlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.055
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.378
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.036
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.133
4-(3,4-dichlorophenyl)-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.014
4-butyl-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.05
4-butyl-N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]piperazine-1-sulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000072
4-pentyl-N-(2-[2-phenyl-5-[4-(trifluoromethyl)phenyl]-1H-imidazol-4-yl]ethyl)benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000372
4-pentyl-N-(2-[2-phenyl-5-[4-(trifluoromethyl)phenyl]-1H-imidazol-4-yl]ethyl)benzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.00097
4-pentyl-N-[2-(5-phenyl-2-pyridin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
5.321
4-pentyl-N-[2-(5-phenyl-2-pyridin-2-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000087
4-pentyl-N-[2-(5-phenyl-2-pyridin-4-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
3.211
4-pentyl-N-[2-(5-phenyl-2-pyridin-4-yl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000006
4-pentyl-N-[2-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000013
4-pentyl-N-[2-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)ethyl]benzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000053
4-pentyl-N-[3-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)propyl]benzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000396
4-pentyl-N-[3-(5-phenyl-2-thioformyl-1H-imidazol-4-yl)propyl]benzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.00035
6,7-dihydroxy-3',4'-methylenedioxyisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.016
6,7-dihydroxy-3',4'-methylenedioxyisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-2
0.00021
6,7-dihydroxy-3'-methylisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.0083
6,7-dihydroxy-3'-methylisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-2
0.00021
6,7-dihydroxy-3'-methylisoflavanone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.014
6,7-dihydroxy-3'-methylisoflavanone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-2
0.00015
6,7-dihydroxy-4'-methoxyisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.1
6,7-dihydroxy-4'-methoxyisoflavan
Homo sapiens
-
above, pH 7.5, 22°C, isozyme 15-hLO-2
0.0016
6,7-dihydroxy-4'-methoxyisoflavanone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-2
0.019
6,7-dihydroxy-4'-methoxyisoflavanone
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.1
7,8-dihydroxy-3',4'-dimethoxyisoflavan
Homo sapiens
-
above, pH 7.5, 22°C, isozyme 15-hLO-1
0.1
7,8-dihydroxy-3',4'-dimethoxyisoflavan
Homo sapiens
-
above, pH 7.5, 22°C, isozyme 15-hLO-2
0.0037
7,8-dihydroxy-4'-methoxyisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.1
7,8-dihydroxy-4'-methoxyisoflavan
Homo sapiens
-
above, pH 7.5, 22°C, isozyme 15-hLO-2
0.0057
7,8-dihydroxy-4'-methylisoflavan
Homo sapiens
-
pH 7.5, 22°C, isozyme 15-hLO-1
0.1
7,8-dihydroxy-4'-methylisoflavan
Homo sapiens
-
above, pH 7.5, 22°C, isozyme 15-hLO-2
0.0031
alpha-mangostin
Homo sapiens
-
pH 7.5, recombinant isozyme 15-hLO-1
0.05
alpha-mangostin
Homo sapiens
-
above, pH 7.5, recombinant isozyme 15-hLO-2
0.0076
michellamine B
Homo sapiens
-
pH 7.5, recombinant isozyme 15-hLO-1
0.05
michellamine B
Homo sapiens
-
above, pH 7.5, recombinant isozyme 15-hLO-2
0.031
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate linoleic acid
0.186
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate arachidonic acid
0.08
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate linoleic acid
0.822
N'-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate arachidonic acid
0.038
N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate linoleic acid
0.375
N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methyl-N-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate arachidonic acid
0.01
N-ethyl-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-[(3R)-1-(1-methyl-1-phenylethyl)pyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate linoleic acid
0.132
N-ethyl-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-[(3R)-1-(1-methyl-1-phenylethyl)pyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate arachidonic acid
0.003
N-ethyl-N-[(3R)-1-[1-(4-fluorophenyl)ethyl]pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]sulfamide
Homo sapiens
-
versus substrate linoleic acid
0.75
N-ethyl-N-[(3R)-1-[1-(4-fluorophenyl)ethyl]pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]sulfamide
Homo sapiens
-
versus substrate arachidonic acid
0.011
N-[(3R)-1-(3,4-dichlorobenzyl)pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methylsulfamide
Homo sapiens
-
versus substrate linoleic acid
0.083
N-[(3R)-1-(3,4-dichlorobenzyl)pyrrolidin-3-yl]-N'-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-N-methylsulfamide
Homo sapiens
-
versus substrate arachidonic acid
0.000364
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-methylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.0028
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-methylbenzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000033
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000162
N-[2-(2,5-diphenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.01
N-[2-(2-cyclopropyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
above, versus substrate arachidonic acid
0.01
N-[2-(2-cyclopropyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
above, versus substrate linoleic acid
0.00192
N-[2-(2-tert-butyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.01
N-[2-(2-tert-butyl-5-phenyl-1H-imidazol-4-yl)ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
above, versus substrate arachidonic acid
0.000099
N-[2-[2-(3-nitrophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.0011
N-[2-[2-(3-nitrophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000021
N-[2-[2-(4-chlorophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.0011
N-[2-[2-(4-chlorophenyl)-5-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000082
N-[2-[5-(3-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000531
N-[2-[5-(3-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000059
N-[2-[5-(4-fluorophenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000261
N-[2-[5-(4-fluorophenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.000014
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.00005
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.212
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-phenylpiperazine-1-sulfonamide
Homo sapiens
-
versus substrate linoleic acid
3.45
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-4-phenylpiperazine-1-sulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.083
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate linoleic acid
0.719
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3R)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate arachidonic acid
0.272
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate linoleic acid
2.41
N-[2-[5-(4-methoxyphenyl)-2-phenyl-1H-imidazol-4-yl]ethyl]-N'-[(3S)-1-phenoxypyrrolidin-3-yl]sulfamide
Homo sapiens
-
versus substrate arachidonic acid
0.091
N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-4-pentylpiperazine-1-sulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.646
N-[2-[5-(4-methoxyphenyl)-2-thioformyl-1H-imidazol-4-yl]ethyl]-4-pentylpiperazine-1-sulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.00014
N-[3-(2,5-diphenyl-1H-imidazol-4-yl)propyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate linoleic acid
0.000914
N-[3-(2,5-diphenyl-1H-imidazol-4-yl)propyl]-4-pentylbenzenesulfonamide
Homo sapiens
-
versus substrate arachidonic acid
0.0094
NSC172033
Homo sapiens
-
pH 7.5, recombinant isozyme 15-hLO-1
0.05
NSC172033
Homo sapiens
-
above, pH 7.5, recombinant isozyme 15-hLO-2
0.025
NSC292213
Homo sapiens
-
pH 7.5, recombinant isozyme 15-hLO-1
0.05
NSC292213
Homo sapiens
-
above, pH 7.5, recombinant isozyme 15-hLO-2
0.05
NSC617570
Homo sapiens
-
above, pH 7.5, recombinant isozyme 15-hLO-2
0.5
NSC617570
Homo sapiens
-
above, pH 7.5, recombinant isozyme 15-hLO-1
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Ford-Hutchinson, A.W.
Arachidonate 15-lipoxygenase; characteristics and potential biological significance
Eicosanoids
4
65-74
1991
Oryctolagus cuniculus, Homo sapiens
brenda
Izumi, T.; Radmark, O.; Joernvall, H.; Samuelsson, B.
Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes
Eur. J. Biochem.
202
1231-1238
1991
Homo sapiens
brenda
Nichols, R.C.; Vanderhoek, J.Y.
Calcium regulation of the human PMN cytosolic 15-lipoxygenase
Biochim. Biophys. Acta
1085
77-81
1991
Homo sapiens
brenda
Izumi, T.; Radmark, O.; Samuelsson, B.
Purification of 15-lipoxygenase from human keukocytes, evidence for the presebce of isozymes
Adv. Prostaglandin Thromboxane Leukot. Res.
21
101-104
1990
Homo sapiens
-
brenda
Sigal, E.; Grunberger, D.; Highland, E.; Gross, C.; Dixon, R.A.F.; Craik, C.S.
Expression of cloned human reticulocyte 15-lipoxygenase and immunological evidence that 15-lipoxygenases of different cell types are related
J. Biol. Chem.
265
5113-5120
1990
Homo sapiens
brenda
Sigal, E.; Grunberger, D.; Cashman, J.R.; Craik, C.S.; Caughey, G.H.; Nadel, J.A.
Arachidonate 15-lipoxygenase from human eosinophil-enriched leukocytes: partial purification and properties
Biochem. Biophys. Res. Commun.
150
376-383
1988
Homo sapiens
brenda
Sigal, E.; Craik, C.S.; Dixon, R.A.F.; Nadel, J.A.
Cloning and expression of human arachidonate 15-lipoxygenase
Trans. Assoc. Am. Physicians
102
176-184
1989
Homo sapiens
brenda
Sigal, E.; Grunberger, D.; Craik, C.S.; Caughey, G.H.; Nadel, J.A.
Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases
J. Biol. Chem.
263
5328-5332
1988
Homo sapiens
brenda
Burrall, B.A.; Cheung, M.; Chiu, A.; Goetzel, E.J.
Enzymatic properties of the 15-lipoxygenase of human cultured keratinocytes
J. Invest. Dermatol.
91
294-297
1988
Homo sapiens
brenda
Soberman, R.J.; Harper, T.W.; Betteridge, D.; Lewis, R.A.; Austen, K.F.
Characterization and separation of the arachidonic acid 5-lipoxygenase and linoleic acid omega-6 lipoxygenase (arachidonic acid 15-lipoxygenase) of human polymorphonuclear leukocytes
J. Biol. Chem.
260
4508-4515
1985
Homo sapiens
brenda
Jung, G.; Yang, D.C.; Nakao, A.
Oxygenation of phosphatidylcholine by human polymorphonuclear leukocyte 15-lipoxygenase
Biochem. Biophys. Res. Commun.
130
559-566
1985
Homo sapiens
brenda
Sloane, D.L.; leung, R.; Craik, C.S.; Sigal, E.
A primary determinant for lipoxygenase positional specificity
Nature
354
149-1152
1991
Homo sapiens
brenda
Kuehn, H.; Heydeck, D.; Brinckman, R.; Trebus, F.
Regulation of cellular 15-lipoxygenase activity on pretranslational, translational, and posttranslational levels
Lipids
34
S273-S279
1999
Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus
-
brenda
Reddy, N.; Everhart, A.; Eling, T.; Glasgow, W.
Characterization of a 15-lipoxygenase in human breast carcinoma BT-20 cells: stimulation of 13-HODE formation by TGFa/EGF
Biochem. Biophys. Res. Commun.
231
111-116
1997
Homo sapiens
brenda
Kuehn, H.; Barnett, J.; Grunberger, D.; Baecker, P.; Chow, J.; Nguyen, B.; Bursztyn-Pettegrew, H.; Chan, H.; Sigal, E.
Overexpression, purification and characterization of human recombinant 15-lipoxygenase
Biochim. Biophys. Acta
1169
80-89
1993
Homo sapiens
brenda
Liminga, M.; Hornsten, L.; Sprecher, H.W.; Oliw, E.H.
Arachidonate 15-lipoxygenase in human corneal epithelium and 12- and 15-lipoxygenases in bovine corneal epithelium: comparison with other bovine 12-lipoxygenases
Biochim. Biophys. Acta
1210
288-296
1994
Bos taurus, Homo sapiens
brenda
Tang, S.; Bhatia, B.; Maldonado, C.J.; Yang, P.; Newman, R.A.; Liu, J.; Chandra, D.; Traag, J.; Klein, R.D.; Fischer, S.M.; Chopra, D.; Shen, J.; Zhau, H.E.; Chung, L.W.K.; Tang, D.G.
Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells
J. Biol. Chem.
277
16189-16201
2002
Homo sapiens (O15296), Homo sapiens
brenda
Kilty, I.; Logan, A.; Vickers, P.J.
Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase
Eur. J. Biochem.
266
83-93
1999
Homo sapiens
brenda
Mogul, R.; Johansen, E.; Holman, T.R.
Oleyl sulfate reveals allosteric inhibition of soybean lipoxygenase-1 and human 15-lipoxygenase
Biochemistry
39
4801-4807
2000
Homo sapiens
brenda
Schewe, T.
15-Lipoxygenase-1: A prooxidant enzyme
Biol. Chem.
383
365-374
2002
Oryctolagus cuniculus, Homo sapiens
brenda
MacMillan, D.K.; Hill, E.; Sala, A.; Sigal, E.; Shuman, T.; Henson, P.M.; Murphy, R.C.
Eosinophil 15-lipoxygenase is a leukotriene A4 synthase
J. Biol. Chem.
269
26663-26668
1994
Homo sapiens
brenda
Segraves, E.N.; Holman, T.R.
Kinetic investigations of the rate-limiting step in human 12- and 15-lipoxygenase
Biochemistry
42
5236-5243
2003
Homo sapiens
brenda
Chang, M.S.; Schneider, C.; Roberts, R.L.; Shappell, S.B.; Haselton, F.R.; Boeglin, W.E.; Brash, A.R.
Detection and subcellular localization of two 15S-lipoxygenases in human cornea
Invest. Ophthalmol. Vis. Sci.
46
849-856
2005
Homo sapiens
brenda
Bhatia, B.; Maldonado, C.J.; Tang, S.; Chandra, D.; Klein, R.D.; Chopra, D.; Shappell, S.B.; Yang, P.; Newman, R.A.; Tang, D.G.
Subcellular localization and tumor-suppressive functions of 15-lipoxygenase 2 (15-LOX2) and its splice variants
J. Biol. Chem.
278
25091-25100
2003
Homo sapiens
brenda
Segraves, E.N.; Shah, R.R.; Segraves, N.L.; Johnson, T.A.; Whitman, S.; Sui, J.K.; Kenyon, V.A.; Cichewicz, R.H.; Crews, P.; Holman, T.R.
Probing the activity differences of simple and complex brominated aryl compounds against 15-soybean, 15-human, and 12-human lipoxygenase
J. Med. Chem.
47
4060-4065
2004
Glycine max, Homo sapiens
brenda
Coffa, G.; Brash, A.R.
A single active site residue directs oxygenation stereospecificity in lipoxygenases: Stereocontrol is linked to the position of oxygenation
Proc. Natl. Acad. Sci. USA
101
15579-15584
2004
Homo sapiens
brenda
Aggarwal, N.T.; Holmes, B.B.; Cui, L.; Viita, H.; Yla-Herttuala, S.; Campbell, W.B.
Adenoviral expression of 15-lipoxygenase-1 in rabbit aortic endothelium: role in arachidonic acid-induced relaxation
Am. J. Physiol. Heart Circ. Physiol.
292
H1033-H1041
2007
Homo sapiens
brenda
Andersson, E.; Schain, F.; Svedling, M.; Claesson, H.; Forsell, P.K.
Interaction of human 15-lipoxygenase-1 with phosphatidylinositol bisphosphates results in increased enzyme activity
Biochim. Biophys. Acta
1761
1498-1505
2006
Homo sapiens
brenda
Deschamps, J.D.; Kenyon, V.A.; Holman, T.R.
Baicalein is a potent in vitro inhibitor against both reticulocyte 15-human and platelet 12-human lipoxygenases
Bioorg. Med. Chem.
14
4295-4301
2006
Homo sapiens
brenda
Shureiqi, I.; Wu, Y.; Chen, D.; Yang, X.L.; Guan, B.; Morris, J.S.; Yang, P.; Newman, R.A.; Broaddus, R.; Hamilton, S.R.; Lynch, P.; Levin, B.; Fischer, S.M.; Lippman, S.M.
The critical role of 15-lipoxygenase-1 in colorectal epithelial cell terminal differentiation and tumorigenesis
Cancer Res.
65
11486-11492
2005
Homo sapiens
brenda
Deguchi, A.; Xing, S.W.; Shureiqi, I.; Yang, P.; Newman, R.A.; Lippman, S.M.; Feinmark, S.J.; Oehlen, B.; Weinstein, I.B.
Activation of protein kinase G up-regulates expression of 15-lipoxygenase-1 in human colon cancer cells
Cancer Res.
65
8442-8447
2005
Homo sapiens
brenda
Flores, A.M.; Li, L.; McHugh, N.G.; Aneskievich, B.J.
Enzyme association with PPARgamma: evidence of a new role for 15-lipoxygenase type 2
Chem. Biol. Interact.
151
121-132
2005
Homo sapiens
brenda
Kelavkar, U.; Lin, Y.; Landsittel, D.; Chandran, U.; Dhir, R.
The yin and yang of 15-lipoxygenase-1 and delta-desaturases: Dietary omega-6 linoleic acid metabolic pathway in prostate
J. Carcinog.
5
9-9
2006
Homo sapiens
brenda
Bhattacharjee, A.; Xu, B.; Frank, D.A.; Feldman, G.M.; Cathcart, M.K.
Monocyte 15-lipoxygenase expression is regulated by a novel cytosolic signaling complex with protein kinase C delta and tyrosine-phosphorylated Stat3
J. Immunol.
177
3771-3781
2006
Homo sapiens
brenda
Kim, J.S.; Baek, S.J.; Bottone, F.G.; Sali, T.; Eling, T.E.
Overexpression of 15-lipoxygenase-1 induces growth arrest through phosphorylation of p53 in human colorectal cancer cells
Mol. Cancer Res.
3
511-517
2005
Homo sapiens
brenda
Kong, J.; Sumaroka, M.; Eastmond, D.L.; Liebhaber, S.A.
Shared stabilization functions of pyrimidine-rich determinants in the erythroid 15-lipoxygenase and alpha-globin mRNAs
Mol. Cell. Biol.
26
5603-5614
2006
Homo sapiens
brenda
Kelavkar, U.P.; Parwani, A.V.; Shappell, S.B.; Martin, W.D.
Conditional expression of human 15-lipoxygenase-1 in mouse prostate induces prostatic intraepithelial neoplasia: the FLiMP mouse model
Neoplasia
8
510-522
2006
Homo sapiens
brenda
Subbarayan, V.; Krieg, P.; Hsi, L.C.; Kim, J.; Yang, P.; Sabichi, A.L.; Llansa, N.; Mendoza, G.; Logothetis, C.J.; Newman, R.A.; Lippman, S.M.; Menter, D.G.
15-Lipoxygenase-2 gene regulation by its product 15-(S)-hydroxyeicosatetraenoic acid through a negative feedback mechanism that involves peroxisome proliferator-activated receptor gamma
Oncogene
25
6015-6025
2006
Homo sapiens
brenda
Kim, K.S.; Chun, H.S.; Yoon, J.H.; Lee, J.G.; Lee, J.H.; Yoo, J.B.
Expression of 15-lipoxygenase-1 in human nasal epithelium: its implication in mucociliary differentiation
Prostaglandins Leukot. Essent. Fatty Acids
73
77-83
2005
Homo sapiens, Mus musculus
brenda
Jiang, W.G.; Watkins, G.; Douglas-Jones, A.; Mansel, R.E.
Reduction of isoforms of 15-lipoxygenase (15-LOX)-1 and 15-LOX-2 in human breast cancer
Prostaglandins Leukot. Essent. Fatty Acids
74
235-245
2006
Homo sapiens
brenda
Sen, M.; McHugh, K.; Hutzley, J.; Philips, B.J.; Dhir, R.; Parwani, A.V.; Kelavkar, U.P.
Orthotopic expression of human 15-lipoxygenase (LO)-1 in the dorsolateral prostate of normal wild-type C57BL/6 mouse causes PIN-like lesions
Prostaglandins Other Lipid Mediat.
81
1-13
2006
Homo sapiens
brenda
Fischer, K.A.; Van Leyen, K.; Lovercamp, K.W.; Manandhar, G.; Sutovsky, M.; Feng, D.; Safranski, T.; Sutovsky, P.
15-Lipoxygenase is a component of the mammalian sperm cytoplasmic droplet
Reproduction
130
213-222
2005
Babyrousa babyrussa, Equus caballus, Homo sapiens, Mus musculus, Sus scrofa
brenda
Wang, D.; Chen, S.; Feng, Y.; Yang, Q.; Campbell, B.H.; Tang, X.; Campbell, W.B.
Reduced expression of 15-lipoxygenase 2 in human head and neck carcinomas
Tumour Biol.
27
261-273
2006
Homo sapiens
brenda
Assimes, T.L.; Knowles, J.W.; Priest, J.R.; Basu, A.; Borchert, A.; Volcik, K.A.; Grove, M.L.; Tabor, H.K.; Southwick, A.; Tabibiazar, R.; Sidney, S.; Boerwinkle, E.; Go, A.S.; Iribarren, C.; Hlatky, M.A.; Fortmann, S.P.; Myers, R.M.; Kuhn, H.; Risch, N.; Quertermous, T.
A near null variant of 12/15-LOX encoded by a novel SNP in ALOX15 and the risk of coronary artery disease
Atherosclerosis
198
136-144
2008
Homo sapiens (P16050)
brenda
Jacquot, C.; Wecksler, A.T.; McGinley, C.M.; Segraves, E.N.; Holman, T.R.; van der Donk, W.A.
Isotope sensitive branching and kinetic isotope effects in the reaction of deuterated arachidonic acids with human 12- and 15-lipoxygenases
Biochemistry
47
7295-7303
2008
Homo sapiens
brenda
Wecksler, A.T.; Kenyon, V.; Deschamps, J.D.; Holman, T.R.
Substrate specificity changes for human reticulocyte and epithelial 15-lipoxygenases reveal allosteric product regulation
Biochemistry
47
7364-7375
2008
Homo sapiens
brenda
Gulliksson, M.; Brunnstroem, A.; Johannesson, M.; Backman, L.; Nilsson, G.; Harvima, I.; Dahlen, B.; Kumlin, M.; Claesson, H.
Expression of 15-lipoxygenase type-1 in human mast cells
Biochim. Biophys. Acta
1771
1156-1165
2007
Homo sapiens
brenda
Deschamps, J.D.; Gautschi, J.T.; Whitman, S.; Johnson, T.A.; Gassner, N.C.; Crews, P.; Holman, T.R.
Discovery of platelet-type 12-human lipoxygenase selective inhibitors by high-throughput screening of structurally diverse libraries
Bioorg. Med. Chem.
15
6900-6908
2007
Homo sapiens
brenda
Vasquez-Martinez, Y.; Ohri, R.V.; Kenyon, V.; Holman, T.R.; Sepulveda-Boza, S.
Structure-activity relationship studies of flavonoids as potent inhibitors of human platelet 12-hLO, reticulocyte 15-hLO-1, and prostate epithelial 15-hLO-2
Bioorg. Med. Chem.
15
7408-7425
2007
Homo sapiens
brenda
Sadeghian, H.; Seyedi, S.M.; Saberi, M.R.; Arghiani, Z.; Riazi, M.
Design and synthesis of eugenol derivatives, as potent 15-lipoxygenase inhibitors
Bioorg. Med. Chem.
16
890-901
2008
Glycine max, Homo sapiens
brenda
Weinstein, D.S.; Liu, W.; Ngu, K.; Langevine, C.; Combs, D.W.; Zhuang, S.; Chen, C.; Madsen, C.S.; Harper, T.W.; Robl, J.A.
Discovery of selective imidazole-based inhibitors of mammalian 15-lipoxygenase: highly potent against human enzyme within a cellular environment
Bioorg. Med. Chem. Lett.
17
5115-5120
2007
Homo sapiens
brenda
Jedrzejczak-Czechowicz, M.; Lewandowska-Polak, A.; Bienkiewicz, B.; Kowalski, M.L.
Involvement of 15-lipoxygenase and prostaglandin EP receptors in aspirin-triggered 15-hydroxyeicosatetraenoic acid generation in aspirin-sensitive asthmatics
Clin. Exp. Allergy
38
1108-1116
2008
Homo sapiens
brenda
Aggarwal, N.T.; Chawengsub, Y.; Gauthier, K.M.; Viita, H.; Yla-Herttuala, S.; Campbell, W.B.
Endothelial 15-lipoxygenase-1 overexpression increases acetylcholine-induced hypotension and vasorelaxation in rabbits
Hypertension
51
246-251
2008
Homo sapiens
brenda
Stachowska, E.; Dziedziejko, V.; Safranow, K.; Jakubowska, K.; Olszewska, M.; Machalinski, B.; Chlubek, D.
Effect of conjugated linoleic acids on the activity and mRNA expression of 5- and 15-lipoxygenases in human macrophages
J. Agric. Food Chem.
55
5335-5342
2007
Homo sapiens
brenda
Pirillo, A.; Uboldi, P.; Bolego, C.; Kuhn, H.; Catapano, A.L.
The 15-lipoxygenase-modified high density lipoproteins 3 fail to inhibit the TNF-alpha-induced inflammatory response in human endothelial cells
J. Immunol.
181
2821-2830
2008
Homo sapiens
brenda
Succol, F.; Pratico, D.
A role for 12/15 lipoxygenase in the amyloid beta precursor protein metabolism
J. Neurochem.
103
380-387
2007
Homo sapiens
brenda
Vincent, C.; Fiancette, R.; Donnard, M.; Bordessoule, D.; Turlure, P.; Trimoreau, F.; Denizot, Y.
5-LOX, 12-LOX and 15-LOX in immature forms of human leukemic blasts
Leuk. Res.
32
1756-1762
2008
Homo sapiens
brenda
Feltenmark, S.; Gautam, N.; Brunnstroem, A.; Griffiths, W.; Backman, L.; Edenius, C.; Lindbom, L.; Bjoerkholm, M.; Claesson, H.E.
Eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in human Feltenmark, S.; Gautam, N.; Brunnstroem, A.; Griffiths, W.; Backman, L.; Edenius, C.; Lindbom, L.; Bjoerkholm, M.; Claesson, H.E.: Eoxins are proinflammatory arachidonic acid metabolites produced via the 15-lipoxygenase-1 pathway in human eosinophils and mast cells
Proc. Natl. Acad. Sci. USA
105
680-685
2008
Homo sapiens
brenda
Tang, D.G.; Bhatia, B.; Tang, S.; Schneider-Broussard, R.
15-Lipoxygenase 2 (15-LOX2) is a functional tumor suppressor that regulates human prostate epithelial cell differentiation, senescence, and growth (size)
Prostaglandins Other Lipid Mediat.
82
135-146
2007
Homo sapiens (O15296), Homo sapiens
brenda
Liu, C.; Xu, D.; Liu, L.; Schain, F.; Brunnstroem, A.; Bjoerkholm, M.; Claesson, H.E.; Sjoeberg, J.
15-Lipoxygenase-1 induces expression and release of chemokines in cultured human lung epithelial cells
Am. J. Physiol. Lung Cell Mol. Physiol.
297
L196-L203
2009
Homo sapiens
brenda
Zhao, J.; Maskrey, B.; Balzar, S.; Chibana, K.; Mustovich, A.; Hu, H.; Trudeau, J.B.; ODonnell, V.; Wenzel, S.E.
Interleukin-13-induced MUC5AC is regulated by 15-lipoxygenase 1 pathway in human bronchial epithelial cells
Am. J. Respir. Crit. Care Med.
179
782-790
2009
Homo sapiens
brenda
Weibel, G.L.; Joshi, M.R.; Alexander, E.T.; Zhu, P.; Blair, I.A.; Rothblat, G.H.
Overexpression of human 15(S)-lipoxygenase-1 in RAW macrophages leads to increased cholesterol mobilization and reverse cholesterol transport
Arterioscler. Thromb. Vasc. Biol.
29
837-842
2009
Homo sapiens
brenda
Chabane, N.; Zayed, N.; Benderdour, M.; Martel-Pelletier, J.; Pelletier, J.; Duval, N.; Fahmi, H.
Human articular chondrocytes express 15-lipoxygenase-1 and -2: Potential role in osteoarthritis
Arthritis Res. Ther.
11
R44
2009
Homo sapiens
brenda
Gheorghe, K.R.; Korotkova, M.; Catrina, A.I.; Backman, L.; af Klint, E.; Claesson, H.E.; Radmark, O.; Jakobsson, P.J.
Expression of 5-lipoxygenase and 15-lipoxygenase in rheumatoid arthritis synovium and effects of intraarticular glucocorticoids
Arthritis Res. Ther.
11
R83
2009
Homo sapiens
brenda
Danielsson, K.; Rydberg, E.; Ingelsten, M.; Akyuerek, L.; Jirholt, P.; Ullstroem, C.; Forsberg, G.; Boren, J.; Wiklund, O.; Hulten, L.
15-Lipoxygenase-2 expression in human macrophages induces chemokine secretion and T cell migration
Atherosclerosis
199
34-40
2008
Homo sapiens
brenda
Wecksler, A.T.; Jacquot, C.; van der Donk, W.A.; Holman, T.R.
Mechanistic investigations of human reticulocyte 15- and platelet 12-lipoxygenases with arachidonic acid
Biochemistry
48
6259-6267
2009
Homo sapiens
brenda
Wecksler, A.T.; Kenyon, V.; Garcia, N.K.; Deschamps, J.D.; van der Donk, W.A.; Holman, T.R.
Kinetic and structural investigations of the allosteric site in human epithelial 15-lipoxygenase-2
Biochemistry
48
8721-8730
2009
Homo sapiens
brenda
Walther, M.; Roffeis, J.; Jansen, C.; Anton, M.; Ivanov, I.; Kuhn, H.
Structural basis for pH-dependent alterations of reaction specificity of vertebrate lipoxygenase isoforms
Biochim. Biophys. Acta
1791
827-835
2009
Oryctolagus cuniculus, Homo sapiens, Mus musculus
brenda
Yang, Q.; Feng, Y.; Schultz, C.J.; Li, X.A.; Wu, H.; Wang, D.
Synergistic effect of 15-lipoxygenase 2 and radiation in killing head-and-neck cancer
Cancer Gene Ther.
15
323-330
2008
Homo sapiens
brenda
Mochizuki, N.; Kwon, Y.
15-Lipoxygenase-1 in the vasculature: Expanding roles in angiogenesis
Circ. Res.
102
143-145
2008
Oryctolagus cuniculus, Homo sapiens
brenda
Claesson, H.E.; Griffiths, W.J.; Brunnstroem, A.; Schain, F.; Andersson, E.; Feltenmark, S.; Johnson, H.A.; Porwit, A.; Sjoeberg, J.; Bjoerkholm, M.
Hodgkin Reed-Sternberg cells express 15-lipoxygenase-1 and are putative producers of eoxins in vivo: novel insight into the inflammatory features of classical Hodgkin lymphoma
FEBS J.
275
4222-4234
2008
Homo sapiens
brenda
Yoo, H.; Jeon, B.; Jeon, M.S.; Lee, H.; Kim, T.Y.
Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes
FEBS Lett.
582
3249-3253
2008
Homo sapiens
brenda
Zhu, H.; Glasgow, W.; George, M.D.; Chrysovergis, K.; Olden, K.; Roberts, J.D.; Eling, T.
15-lipoxygenase-1 activates tumor suppressor p53 independent of enzymatic activity
Int. J. Cancer
123
2741-2749
2008
Homo sapiens
brenda
Tang, Y.; Wang, M.T.; Chen, Y.; Yang, D.; Che, M.; Honn, K.V.; Akers, G.D.; Johnson, S.R.; Nie, D.
Downregulation of vascular endothelial growth factor and induction of tumor dormancy by 15-lipoxygenase-2 in prostate cancer
Int. J. Cancer
124
1545-1551
2009
Homo sapiens
brenda
Jacquot, C.; McGinley, C.M.; Plata, E.; Holman, T.R.; van der Donk, W.A.
Synthesis of 11-thialinoleic acid and 14-thialinoleic acid, inhibitors of soybean and human lipoxygenases
Org. Biomol. Chem.
6
4242-4252
2008
Homo sapiens
brenda
Claesson, H.E.
On the biosynthesis and biological role of eoxins and 15-lipoxygenase-1 in airway inflammation and Hodgkin lymphoma
Prostaglandins Other Lipid Mediat.
89
120-125
2009
Homo sapiens, Mus musculus, Oryctolagus cuniculus, Sus scrofa
brenda
Bhattacharya, S.; Mathew, G.; Jayne, D.G.; Pelengaris, S.; Khan, M.
15-lipoxygenase-1 in colorectal cancer: a review
Tumour Biol.
30
185-199
2009
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Rai, G.; Kenyon, V.; Jadhav, A.; Schultz, L.; Armstrong, M.; Jameson, J.B.; Hoobler, E.; Leister, W.; Simeonov, A.; Holman, T.R.; Maloney, D.J.
Discovery of potent and selective inhibitors of human reticulocyte 15-lipoxygenase-1
J. Med. Chem.
53
7392-7404
2010
Homo sapiens
brenda
Magnusson, L.U.; Lundqvist, A.; Asp, J.; Synnergren, J.; Johansson, C.T.; Palmqvist, L.; Jeppsson, A.; Hulten, L.M.
High expression of arachidonate 15-lipoxygenase and proinflammatory markers in human ischemic heart tissue
Biochem. Biophys. Res. Commun.
424
327-330
2012
Homo sapiens
brenda
Schurmann, K.; Anton, M.; Ivanov, I.; Richter, C.; Kuhn, H.; Walther, M.
Molecular basis for the reduced catalytic activity of the naturally occurring T560M mutant of human 12/15-lipoxygenase that has been implicated in coronary artery disease
J. Biol. Chem.
286
23920-23927
2011
Homo sapiens
brenda
Zhao, J.; ODonnell, V.B.; Balzar, S.; St Croix, C.M.; Trudeau, J.B.; Wenzel, S.E.
15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells
Proc. Natl. Acad. Sci. USA
108
14246-14251
2011
Homo sapiens
brenda
Droege, K.D.; Keithly, M.E.; Sanders, C.R.; Armstrong, R.N.; Thompson, M.K.
Structural dynamics of 15-lipoxygenase-2 via hydrogen-deuterium exchange
Biochemistry
56
5065-5074
2017
Homo sapiens (O15296)
brenda
Ackermann, J.A.; Hofheinz, K.; Zaiss, M.M.; Kroenke, G.
The double-edged role of 12/15-lipoxygenase during inflammation and immunity
Biochim. Biophys. Acta
1862
371-381
2017
Homo sapiens (P16050), Mus musculus (P39654)
brenda
Pelcman, B.; Sanin, A.; Nilsson, P.; Schaal, W.; Olofsson, K.; Krog-Jensen, C.; Forsell, P.; Hallberg, A.; Larhed, M.; Boesen, T.; Kromann, H.; Claesson, H.E.
N-Substituted pyrazole-3-carboxamides as inhibitors of human 15-lipoxygenase
Bioorg. Med. Chem. Lett.
25
3017-3023
2015
Homo sapiens (P16050)
brenda
Pelcman, B.; Sanin, A.; Nilsson, P.; No, K.; Schaal, W.; Oehrman, S.; Krog-Jensen, C.; Forsell, P.; Hallberg, A.; Larhed, M.; Boesen, T.; Kromann, H.; Vogensen, S.B.; Groth, T.; Claesson, H.E.
3-Substituted pyrazoles and 4-substituted triazoles as inhibitors of human 15-lipoxygenase-1
Bioorg. Med. Chem. Lett.
25
3024-3029
2015
Homo sapiens (P16050)
brenda
Tirapegui, C.; Acevedo-Fuentes, W.; Dahech, P.; Torrent, C.; Barrias, P.; Rojas-Poblete, M.; Mascayano, C.
Easy and rapid preparation of benzoylhydrazides and their diazene derivatives as inhibitors of 15-lipoxygenase
Bioorg. Med. Chem. Lett.
27
1649-1653
2017
Homo sapiens (P16050)
brenda
Tehrani, M.B.; Emami, S.; Asadi, M.; Saeedi, M.; Mirzahekmati, M.; Ebrahimi, S.M.; Mahdavi, M.; Nadri, H.; Moradi, A.; Moghadam, F.H.; Farzipour, S.; Vosooghi, M.; Foroumadi, A.; Shafiee, A.
Imidazo[2,1-b]thiazole derivatives as new inhibitors of 15-lipoxygenase
Eur. J. Med. Chem.
87
759-764
2014
Homo sapiens (P16050)
brenda
Ivanov, I.; Kuhn, H.; Heydeck, D.
Structural and functional biology of arachidonic acid 15-lipoxygenase-1 (ALOX15)
Gene
573
1-32
2015
Oryctolagus cuniculus (P12530), Oryctolagus cuniculus, Homo sapiens (P16050), Homo sapiens, Mus musculus (P39654), Mus musculus, Rattus norvegicus (Q02759)
brenda
Adel, S.; Karst, F.; Gonzalez-Lafont, A.; Pekarova, M.; Saura, P.; Masgrau, L.; Lluch, J.M.; Stehling, S.; Horn, T.; Kuhn, H.; Heydeck, D.
Evolutionary alteration of ALOX15 specificity optimizes the biosynthesis of antiinflammatory and proresolving lipoxins
Proc. Natl. Acad. Sci. USA
113
E4266-E4275
2016
Homo sapiens (P16050), Homo sapiens neanderthalensis, Homo sapiens subsp. 'Denisova', Macaca mulatta (F7EPQ4), Nomascus leucogenys (G1S6D2), Oryctolagus cuniculus (P12530), Pan paniscus, Pan troglodytes (H2QBX9), Papio anubis (A0A096P2G1), Pongo abelii (Q5RBE8), Pongo pygmaeus (Q5RBE8)
brenda
Cole, B.; Lieb, D.; Dobrian, A.; Nadler, J.
12- and 15-lipoxygenases in adipose tissue inflammation
Prostaglandins Other Lipid Mediat.
104-105
84-92
2013
Homo sapiens (P16050)
-
brenda
Green, A.R.; Freedman, C.; Tena, J.; Tourdot, B.E.; Liu, B.; Holinstat, M.; Holman, T.R.
5 S,15 S-Dihydroperoxyeicosatetraenoic Acid (5,15-diHpETE) as a lipoxin intermediate Reactivity and kinetics with human leukocyte 5-lipoxygenase, platelet 12-lipoxygenase, and reticulocyte 15-lipoxygenase-1
Biochemistry
57
6726-6734
2018
Homo sapiens (P16050), Homo sapiens
brenda
Freedman, C.; Tran, A.; Tourdot, B.E.; Kalyanaraman, C.; Perry, S.; Holinstat, M.; Jacobson, M.P.; Holman, T.R.
Biosynthesis of the maresin intermediate, 13S,14S-epoxy-DHA, by human 15-lipoxygenase and 12-lipoxygenase and its regulation through negative allosteric modulators
Biochemistry
59
1832-1844
2020
Homo sapiens (P16050), Homo sapiens (P18054), Homo sapiens
brenda
Perry, S.C.; Horn, T.; Tourdot, B.E.; Yamaguchi, A.; Kalyanaraman, C.; Conrad, W.S.; Akinkugbe, O.; Holinstat, M.; Jacobson, M.P.; Holman, T.R.
Role of human 15-lipoxygenase-2 in the biosynthesis of the lipoxin intermediate, 5S,15S-diHpETE, implicated with the altered positional specificity of human 15-lipoxygenase-1
Biochemistry
59
4118-4130
2020
Homo sapiens (O15296), Homo sapiens (P16050), Homo sapiens (P18054), Homo sapiens
brenda
Tsai, W.C.; Gilbert, N.C.; Ohler, A.; Armstrong, M.; Perry, S.; Kalyanaraman, C.; Yasgar, A.; Rai, G.; Simeonov, A.; Jadhav, A.; Standley, M.; Lee, H.W.; Crews, P.; Iavarone, A.T.; Jacobson, M.P.; Neau, D.B.; Offenbacher, A.R.; Newcomer, M.; Holman, T.R.
Kinetic and structural investigations of novel inhibitors of human epithelial 15-lipoxygenase-2
Bioorg. Med. Chem.
46
116349
2021
Homo sapiens (O15296), Homo sapiens
brenda
ElBordiny, H.S.; El-Miligy, M.M.; Kassab, S.E.; Daabees, H.; Mohamed Ali, W.A.; Abdelhamid Mohamed El-Hawash, S.
Design, synthesis, biological evaluation and docking studies of new 3-(4,5-dihydro-1H-pyrazol/isoxazol-5-yl)-2-phenyl-1H-indole derivatives as potent antioxidants and 15-lipoxygenase inhibitors
Eur. J. Med. Chem.
145
594-605
2018
Homo sapiens (O15296)
brenda
Nagasaki, T.; Schuyler, A.J.; Zhao, J.; Samovich, S.N.; Yamada, K.; Deng, Y.; Ginebaugh, S.P.; Christenson, S.A.; Woodruff, P.G.; Fahy, J.V.; Trudeau, J.B.; Stoyanovsky, D.; Ray, A.; Tyurina, Y.Y.; Kagan, V.E.; Wenzel, S.E.
15LO1 dictates glutathione redox changes in asthmatic airway epithelium to worsen type 2 inflammation
J. Clin. Invest.
132
e151685
2022
Homo sapiens (P16050)
brenda
Coppey, L.; Obrosov, A.; Shevalye, H.; Davidson, E.; Paradee, W.; Yorek, M.A.
Characterization of mice ubiquitously overexpressing human 15-lipoxygenase-1 effect of diabetes on peripheral neuropathy and treatment with menhaden oil
J. Diabetes Res.
2021
5564477
2021
Homo sapiens (P16050)
brenda
Goftari, S.N.; Sadeghian, H.; Bahrami, A.R.; Maleki, F.; Matin, M.M.
Stylosin and some of its synthetic derivatives induce apoptosis in prostate cancer cells as 15-lipoxygenase enzyme inhibitors
Naunyn Schmiedebergs Arch. Pharmacol.
392
1491-1502
2019
Homo sapiens (P16050), Homo sapiens
brenda
Archambault, A.S.; Turcotte, C.; Martin, C.; Provost, V.; Larose, M.C.; Laprise, C.; Chakir, J.; Bissonnette, E.; Laviolette, M.; Bosse, Y.; Flamand, N.
Comparison of eight 15-lipoxygenase (LO) inhibitors on the biosynthesis of 15-LO metabolites by human neutrophils and eosinophils
PLoS ONE
13
e0202424
2018
Homo sapiens (O15296), Homo sapiens (P16050), Homo sapiens
brenda