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palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
palmitic acid + reduced acceptor + O2
palmitoleic acid + acceptor + H2O
preferred substrate
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palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
palmitoyl-CoA + AH2 + O2
palmitoleoyl-CoA + A + H2O
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palmitoyl-CoA + ferrocytochrome b5 + O2
palmitoleoyl-CoA + ferricytochrome b5 + H2O
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palmitoyl-CoA + NADH + H+ + O2
palmitoleoyl-CoA + NAD+ + H2O
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palmitoyl-CoA + NADH + O2
palmitoleoyl-CoA + NAD+ + H2O
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stearate + reduced acceptor + O2
oleate + acceptor + H2O
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stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
stearoyl-CoA + ferrocytochrome b5 + O2
oleoyl-CoA + ferricytochrome b5 + H2O
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stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
stearoyl-CoA + NADH + H+ + O2
oleoyl-CoA + NAD+ + H2O
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stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
stearoyl-CoA + NADPH + H+ + O2
oleoyl-CoA + NADP+ + H2O
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additional information
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palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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?
stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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?
palmitoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
palmitoleoyl-CoA + 2 ferricytochrome b5 + 2 H2O
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?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
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?
stearoyl-CoA + AH2 + O2
oleoyl-CoA + A + H2O
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?
stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
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stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
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rate-limiting enzyme involved in the synthesis of monounsaturated fatty acids, deficiency of isozyme SCD1 leads to activation of the metabolic pathways that promote fatty acid beta-oxidation in mice, enzyme regulation in the heart in a hormone-dependent fashion, overview
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stearoyl-CoA + ferrocytochrome b5 + O2 + H+
oleoyl-CoA + ferricytochrome b5 + H2O
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stearoyl-CoA desaturase 2 is uniquely and absolutely required for adipogenesis, SCD2 also controls the maintenance of adipocyte-specific gene expression in fully differentiated 3T3-L1 adipocytes, including the expression of SCD1, polysome profile analysis, overview
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stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
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stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
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preferred substrate for SCD1
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?
stearoyl-CoA + NADH + O2
oleoyl-CoA + NAD+ + H2O
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Scd-/- and wild-type mice are fed with 20% high fat diets, fat-free basal mix is supplemented with 20% by weight of tristearin or triolein and 1% by weight corn oil
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additional information
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enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
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additional information
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enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
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additional information
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enzyme SCD1 catalyzes the formation of a cis-double bond between the 9th and 10th carbons of stearoyl- or palmitoyl-CoA. The reaction requires molecular oxygen, which is activated by a diiron center, and cytochrome b5, which regenerates the di-iron center
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additional information
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in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
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additional information
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in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
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additional information
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in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
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additional information
?
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in addition to molecular oxygen, the SCD1 reaction requires NAD(P)H, cytochrome b5 reductase, and cytochrome b5 through which the electrons flow to SCD and then to molecular O2, which is reduced to H2O
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additional information
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SCD1 catalyses the DELTA9 desaturation of 12-19 carbon saturated fatty acids to monounsaturated fatty acids
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additional information
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SCD2 and SCD3 preferentially utilize palmitoyl-CoA
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additional information
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rate-limiting enzyme in the biosynthesis of monounsaturated fatty acids
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additional information
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mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
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additional information
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mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
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additional information
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mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
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additional information
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mouse SCD3 isoform preferentially catalyzes palmitoleate synthesis
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additional information
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wild-type isozyme SCD3 is an exclusive 16:0 desaturase, while SCD3 enzyme mutant I112A/E113L is also active with stearoyl-CoA
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additional information
?
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wild-type isozyme SCD3 is an exclusive 16:0 desaturase, while SCD3 enzyme mutant I112A/E113L is also active with stearoyl-CoA
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additional information
?
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wild-type isozyme SCD3 is an exclusive 16:0 desaturase, while SCD3 enzyme mutant I112A/E113L is also active with stearoyl-CoA
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2-(1-((2,2-difluorocyclopropyl)methyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
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2-(1-(1-(4-fluorophenyl)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
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2-(1-(2-(4-fluorophenoxy)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
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2-(1-(3,5-difluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
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2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-imidazol-4-yl)methyl)thiazole-5-carboxamide
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2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-pyrazol-4-yl)methyl)thiazole-5-carboxamide
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2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((2-methylthiazol-5-yl)methyl)thiazole-5-carboxamide
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2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((3-methyl-1H-pyrazol-5-yl)methyl)-thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((5-methylpyrazin-2-yl)methyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((6-(trifluoromethyl)pyridin-3-yl)methyl)-thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-2-ylmethyl)thiazole-5-carboxamide
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2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-4-ylmethyl)thiazole-5-carboxamide
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2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(piperidin-3-ylmethyl)thiazole-5-carboxamide trifluoroacetic acid salt
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2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(thiazol-2-ylmethyl)thiazole-5-carboxamide
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2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
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2-(1-(cyclopropylmethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
-
2-benzamido-4-methyl-N-phenylthiazole-5-carboxamide
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3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-((1-methyl-1H-pyrazol-4-yl)methyl)-1H-pyrazole-5-carboxamide
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3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(oxazol-4-ylmethyl)-1H-pyrazole-5-carboxamide
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3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)-1H-pyrazole-5-carboxamide
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3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-4-ylmethyl)-1H-pyrazole-5-carboxamide
-
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-methyl-1H-pyrazole-5-carboxamide
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4-methyl-2-(5-oxo-1-((5-(trifluoromethyl)furan-2-yl)methyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
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4-methyl-2-(5-oxo-1-(4,4,4-trifluorobutyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
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4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
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4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
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N-((1H-pyrazol-3-yl)methyl)-2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
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N-benzyl-2-(3-(4-fluorobenzyl)-2-oxoimidazolidin-1-yl)-4-methylthiazole-5-carboxamide
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(2E)-3-(4-methoxyphenyl)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]prop-2-enamide
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2-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)-1,3-thiazole-5-carboxamide
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MF-152
2-hydroxy-N-[2-[3-methyl-2-oxo-7-[[3-(trifluoromethyl)benzyl]amino]quinoxalin-1(2H)-yl]ethyl]acetamide
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CVT-12,012
3,4-bis(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3,4-dimethoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3,4-dimethyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2,2-dihydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2,3-dihydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2-hydroxy-2-methylpropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2-hydroxyethoxy)-4-(2-methoxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2-hydroxyethoxy)-4-methoxy-N-(5-[[3-(trifluoromethyl)phenyl]carbonyl]-1,3-thiazol-2-yl)benzamide
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3-(2-hydroxyethoxy)-4-methoxy-N-methyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2-hydroxyethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
-
highly potent and orally bioavailable thiazole-based SCD-1 inhibitor
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethoxy)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3,4-thiadiazol-2-yl]benzamide
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3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]thiophen-2-yl]benzamide
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3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)phenoxy]-1,3-thiazol-2-yl]benzamide
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3-(2-hydroxyethoxy)-4-methoxy-N-{5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl}benzamide
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3-(2-hydroxyethoxy)-4-morpholin-4-yl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2-hydroxyethoxy)-4-[(methylsulfonyl)amino]-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(2-hydroxyethoxy)-N-(5-[hydroxy[3-(trifluoromethyl)phenyl]methyl]-1,3-thiazol-2-yl)-4-methoxybenzamide
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-
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
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3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
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3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-fluorophenoxy)piperidin-1-yl]pyridazine
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-
3-(3-hydroxypropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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3-(3-methyl-1,2,4-oxadiazol-5-yl)-6-[4-[2-(phenoxymethyl)phenoxy]piperidin-1-yl]pyridazine
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-
3-(4-phenoxypiperidin-1-yl)-6-(5-propyl-1,2,4-oxadiazol-3-yl)pyridazine
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-
3-(4-phenoxypiperidin-1-yl)-6-[5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl]pyridazine
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-
3-(5-benzyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
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3-(5-benzyl-1,3,4-oxadiazol-2-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
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-
3-(5-methyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
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-
3-methoxy-4-(2-morpholin-4-ylethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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-
3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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-
3-[4-(2-benzylphenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
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-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(1H-imidazol-1-yl)pyridazine
-
-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
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-
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-4H-1,2,4-triazol-3-yl)pyridazine
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-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(1H-pyrrol-1-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(1H-tetrazol-5-yl)pyridazine
-
-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
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-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3,5-dimethyl-1H-pyrazol-1-yl)pyridazine
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-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
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-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,2,4-oxadiazol-3-yl)pyridazine
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-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-furan-3-ylpyridazine
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-
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-pyridin-3-ylpyridazine
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-
4-(2-bromophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chloro-4-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chloro-5-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chloro-6-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-phenylpiperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-(1H-imidazol-2-yl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-(ethylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-chlorophenoxy)-N-[3-[(1-methylethyl)carbamoyl]phenyl]piperidine-1-carboxamide
-
-
4-(2-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(2-hydroxyethoxy)-3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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-
4-(2-methoxyphenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(3-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
-
-
4-(acetylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-(diethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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4-(dimethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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4-(ethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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-
4-ethoxy-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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-
4-ethylamino-3-(2-hydroxyethoxy)-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
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4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
4-[2-(dimethylamino)ethoxy]-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
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6-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
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-
6-[4-[(4-fluorophenyl)carbonyl]piperidin-1-yl]-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
-
-
cis-9,trans-11 conjugated linoleic acid
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-
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethoxy)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
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N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-[4-(phenylcarbonyl)piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methoxyphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
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-
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-pyridin-4-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-thiophen-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-hydroxy-2-thiophen-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-(2-phenylethyl)-4-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)benzamide
-
-
N-(2-phenylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-2-carboxamide
-
-
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-3-carboxamide
-
-
N-(3-carbamoylphenyl)-4-(2-chlorophenoxy)piperidine-1-carboxamide
-
-
N-[(2R)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-[(2S)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
-
-
N-[2-(2-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-(3-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-(4-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
-
-
N-[2-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-5-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[3-(2-hydroxyethoxy)-4-methoxyphenyl]-5-[3-(trifluoromethyl)benzyl]-1,3-thiazole-2-carboxamide
-
-
N-[3-(3,4-dichlorobenzyl)-4-oxo-3,4-dihydroquinazolin-6-yl]-2-hydroxyacetamide
-
CVT-11,563
N-[3-(methylcarbamoyl)phenyl]-4-(2-methylphenoxy)piperidine-1-carboxamide
-
-
N-[3-(methylcarbamoyl)phenyl]-4-phenoxypiperidine-1-carboxamide
-
-
N-[3-(tert-butylcarbamoyl)phenyl]-4-(2-chlorophenoxy)piperidine-1-carboxamide
-
-
N-[5-(2,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,4-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,4-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3,5-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-chloro-4-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-chlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-fluoro-4-methylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-(3-tert-butylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
-
-
N-[5-[4-fluoro-3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
-
-
[2-methoxy-4-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
-
-
[2-methoxy-5-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
-
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
-
potent and orally efficacious SCD-1 inhibitor
additional information
inhibition of SCD1 leads to reduction in lipid accumulation
-
additional information
inhibition of SCD1 leads to reduction in lipid accumulation
-
additional information
inhibition of SCD1 leads to reduction in lipid accumulation
-
additional information
inhibition of SCD1 leads to reduction in lipid accumulation
-
additional information
synthesis and structure-activity relationships of a series of triazolone derivatives as enzyme inhibitors, overview
-
additional information
-
design and synthesis of piperidine-aryl urea-based stearoyl-CoA desaturase1 inhibitors, overview
-
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.
0.000055
2-(1-((2,2-difluorocyclopropyl)methyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.00003
2-(1-(1-(4-fluorophenyl)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000015
2-(1-(2-(4-fluorophenoxy)ethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000019
2-(1-(3,5-difluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000027
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-imidazol-4-yl)methyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000019
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((1-methyl-1H-pyrazol-4-yl)methyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000024
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((2-methylthiazol-5-yl)methyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000009
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((3-methyl-1H-pyrazol-5-yl)methyl)-thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000015
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((5-methylpyrazin-2-yl)methyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.001722
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-((6-(trifluoromethyl)pyridin-3-yl)methyl)-thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000022
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000012
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(oxazol-4-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.01
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(piperidin-3-ylmethyl)thiazole-5-carboxamide trifluoroacetic acid salt
Mus musculus
pH and temperature not specified in the publication
0.000022
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.00002
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000012
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(thiazol-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000065
2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000098
2-(1-(cyclopropylmethyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methyl-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000147
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-((1-methyl-1H-pyrazol-4-yl)methyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000165
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(oxazol-4-ylmethyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000023
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000007
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.002673
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-4-ylmethyl)-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000385
3-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-N-methyl-1H-pyrazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000007
4-methyl-2-(5-oxo-1-((5-(trifluoromethyl)furan-2-yl)methyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000021
4-methyl-2-(5-oxo-1-(4,4,4-trifluorobutyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000014
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-2-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000016
4-methyl-2-(5-oxo-1-(4-(trifluoromethyl)benzyl)-1H-1,2,4-triazol-4(5H)-yl)-N-(pyridin-3-ylmethyl)thiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000046
N-((1H-pyrazol-3-yl)methyl)-2-(1-(4-fluorobenzyl)-5-oxo-1H-1,2,4-triazol-4(5H)-yl)-4-methylthiazole-5-carboxamide
Mus musculus
pH and temperature not specified in the publication
0.000002
(2E)-3-(4-methoxyphenyl)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]prop-2-enamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000022
3,4-bis(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000076
3,4-dimethoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.008218
3,4-dimethyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00217
3-(2,2-dihydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.009999
3-(2-hydroxy-2-methylpropoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
IC50 above 0.009999 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000003
3-(2-hydroxyethoxy)-4-(2-methoxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.001
3-(2-hydroxyethoxy)-4-methoxy-N-(5-[[3-(trifluoromethyl)phenyl]carbonyl]-1,3-thiazol-2-yl)benzamide
Mus musculus
-
IC50 above 0.001 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000836
3-(2-hydroxyethoxy)-4-methoxy-N-methyl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
3-(2-hydroxyethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
Mus musculus
-
in 250 mM sucrose, 150 mM KCl, 40 mM NaF, 5 mM MgCl2, 100 mM sodium phosphate, pH 7.4, at 37°C
0.000003
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethoxy)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00001
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3,4-thiadiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000076
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)benzyl]thiophen-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.001
3-(2-hydroxyethoxy)-4-methoxy-N-[5-[3-(trifluoromethyl)phenoxy]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
IC50 above 0.001 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000006
3-(2-hydroxyethoxy)-4-morpholin-4-yl-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.009999
3-(2-hydroxyethoxy)-4-[(methylsulfonyl)amino]-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
IC50 above 0.009999 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000276
3-(2-hydroxyethoxy)-N-(5-[hydroxy[3-(trifluoromethyl)phenyl]methyl]-1,3-thiazol-2-yl)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.00001
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.000026
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
Mus musculus
-
pH 7.5
0.0000074
3-(3-benzyl-1,2,4-oxadiazol-5-yl)-6-[4-(2-fluorophenoxy)piperidin-1-yl]pyridazine
Mus musculus
-
pH 7.5
0.000085
3-(3-methyl-1,2,4-oxadiazol-5-yl)-6-[4-[2-(phenoxymethyl)phenoxy]piperidin-1-yl]pyridazine
Mus musculus
-
pH 7.5
0.00133
3-(4-phenoxypiperidin-1-yl)-6-(5-propyl-1,2,4-oxadiazol-3-yl)pyridazine
Mus musculus
-
pH 7.5
0.00082
3-(4-phenoxypiperidin-1-yl)-6-[5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl]pyridazine
Mus musculus
-
pH 7.5
0.00004
3-(5-benzyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.000012
3-(5-benzyl-1,3,4-oxadiazol-2-yl)-6-[4-(2-chlorophenoxy)piperidin-1-yl]pyridazine
Mus musculus
-
pH 7.5
0.00022
3-(5-methyl-1,2,4-oxadiazol-3-yl)-6-(4-phenoxypiperidin-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.000528
3-methoxy-4-(2-morpholin-4-ylethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000193
3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000053
3-[4-(2-benzylphenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
Mus musculus
-
pH 7.5
0.000004
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(1H-imidazol-1-yl)pyridazine
Mus musculus
-
below, pH 7.5
0.0000045
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-1,3,4-oxadiazol-2-yl)pyridazine
Mus musculus
-
pH 7.5
0.000004
3-[4-(2-chloro-5-fluorophenoxy)piperidin-1-yl]-6-(5-methyl-4H-1,2,4-triazol-3-yl)pyridazine
Mus musculus
-
pH 7.5
0.00001
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(1H-pyrrol-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.00037
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(1H-tetrazol-5-yl)pyridazine
Mus musculus
-
pH 7.5
0.00002
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(2-methyl-1H-imidazol-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.000032
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3,5-dimethyl-1H-pyrazol-1-yl)pyridazine
Mus musculus
-
pH 7.5
0.00002
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(3-methyl-1,2,4-oxadiazol-5-yl)pyridazine
Mus musculus
-
pH 7.5
0.00001
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-(5-methyl-1,2,4-oxadiazol-3-yl)pyridazine
Mus musculus
-
pH 7.5
0.000092
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-furan-3-ylpyridazine
Mus musculus
-
pH 7.5
0.000004
3-[4-(2-chlorophenoxy)piperidin-1-yl]-6-pyridin-3-ylpyridazine
Mus musculus
-
below, pH 7.5
0.000004
4-(2-bromophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
below
0.000006
4-(2-chloro-4-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.000004
4-(2-chloro-5-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
below
0.00033
4-(2-chloro-6-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.00059
4-(2-chlorophenoxy)-N-phenylpiperidine-1-carboxamide
Mus musculus
-
-
0.00001
4-(2-chlorophenoxy)-N-[3-(1H-imidazol-2-yl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.000008
4-(2-chlorophenoxy)-N-[3-(3-methyl-1,2,4-oxadiazol-5-yl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.000008
4-(2-chlorophenoxy)-N-[3-(ethylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.000004
4-(2-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
below
0.00081
4-(2-chlorophenoxy)-N-[3-[(1-methylethyl)carbamoyl]phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.000098
4-(2-fluorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.000003
4-(2-hydroxyethoxy)-3-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000081
4-(2-methoxyphenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.00002
4-(3-chlorophenoxy)-N-[3-(methylcarbamoyl)phenyl]piperidine-1-carboxamide
Mus musculus
-
-
0.000008
4-(acetylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000004
4-(diethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000007
4-(dimethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000004
4-(ethylamino)-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
4-ethoxy-3-(2-hydroxyethoxy)-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]benzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000004
4-ethylamino-3-(2-hydroxyethoxy)-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
Mus musculus
-
in 250 mM sucrose, 150 mM KCl, 40 mM NaF, 5 mM MgCl2, 100 mM sodium phosphate, pH 7.4, at 37°C
0.000005
6-methoxy-N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000074
6-[4-[(4-fluorophenyl)carbonyl]piperidin-1-yl]-N-(2-hydroxy-2-phenylethyl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000005
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethoxy)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000002
N-(2-hydroxy-2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperidin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000153
N-(2-hydroxy-2-phenylethyl)-6-[4-(phenylcarbonyl)piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000052
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methoxyphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000007
N-(2-hydroxy-2-phenylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000095
N-(2-hydroxy-2-pyridin-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000037
N-(2-hydroxy-2-pyridin-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000034
N-(2-hydroxy-2-pyridin-4-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000007
N-(2-hydroxy-2-thiophen-2-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000003
N-(2-hydroxy-2-thiophen-3-ylethyl)-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.00015
N-(2-phenylethyl)-4-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)benzamide
Mus musculus
-
-
0.00037
N-(2-phenylethyl)-5-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-2-carboxamide
Mus musculus
-
-
0.000006
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000194
N-(2-phenylethyl)-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridine-3-carboxamide
Mus musculus
-
-
0.00001
N-(3-carbamoylphenyl)-4-(2-chlorophenoxy)piperidine-1-carboxamide
Mus musculus
-
-
0.000025
N-[(2R)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000066
N-[(2S)-2-hydroxy-2-phenylethyl]-6-(4-[[2-(trifluoromethyl)phenyl]carbonyl]piperazin-1-yl)pyridazine-3-carboxamide
Mus musculus
-
-
0.000009
N-[2-(2-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000005
N-[2-(3-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000007
N-[2-(4-fluorophenyl)-2-hydroxyethyl]-6-[4-[(2-methylphenyl)carbonyl]piperidin-1-yl]pyridazine-3-carboxamide
Mus musculus
-
-
0.000044
N-[2-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-5-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000049
N-[3-(2-hydroxyethoxy)-4-methoxyphenyl]-5-[3-(trifluoromethyl)benzyl]-1,3-thiazole-2-carboxamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000017
N-[3-(methylcarbamoyl)phenyl]-4-(2-methylphenoxy)piperidine-1-carboxamide
Mus musculus
-
-
0.00037
N-[3-(methylcarbamoyl)phenyl]-4-phenoxypiperidine-1-carboxamide
Mus musculus
-
-
0.01
N-[3-(tert-butylcarbamoyl)phenyl]-4-(2-chlorophenoxy)piperidine-1-carboxamide
Mus musculus
-
above
0.000009
N-[5-(2,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000008
N-[5-(3,4-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
N-[5-(3,4-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000007
N-[5-(3,5-dichlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000001
N-[5-(3,5-difluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000001
N-[5-(3-chloro-4-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000001
N-[5-(3-chlorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000022
N-[5-(3-fluoro-4-methylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.000002
N-[5-(3-fluorobenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.001307
N-[5-(3-tert-butylbenzyl)-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000006
N-[5-[3,5-bis(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.01
N-[5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]naphthalene-2-carboxamide
Mus musculus
-
IC50 above 0.01 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
0.0000002
N-[5-[4-fluoro-3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]-3-(2-hydroxyethoxy)-4-methoxybenzamide
Mus musculus
-
in 100 mM sodium phosphate, pH 7.4, at 37°C
0.009999
[2-methoxy-5-([5-[3-(trifluoromethyl)benzyl]-1,3-thiazol-2-yl]carbamoyl)phenoxy]acetic acid
Mus musculus
-
IC50 above 0.009999 mM, in 100 mM sodium phosphate, pH 7.4, at 37°C
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evolution
isozymes SCD1 and SCD3 share 89% primary sequence identity, but they yield remarkably different total fatty acid profiles in the recombinant yeast host cells, likely reflecting differences in their preferences for reaction with 16:0 and 18:0 substrates
evolution
isozymes SCD1 and SCD3 share 89% primary sequence identity, but they yield remarkably different total fatty acid profiles in the recombinant yeast host cells, likely reflecting differences in their preferences for reaction with 16:0 and 18:0 substrates
malfunction
-
stearoyl-CoA desaturase 1 deficiency is coupled with an extreme cold sensitivity and significantly increased skin inflammation
malfunction
dysregulation of stearoyl-CoA desaturase 1 likely contributes to obesity associated metabolic disturbances. Effect of genetic ablation of SCD1 in 3T3-L1 adipocytes on membrane microdomain lipid composition at the species-specific level, overview. 90% reduction in scd1 mRNA expression, caused by siRNA expression, leads to altered cellular lipid composition, SCD1 knockout modifies the acyl chain composition of lipids, as well as the lipid composition per se of membrane microdomains in 3T3-L1 adipocytes.The effects of SCD1 knockout are not limited to alterations in 16:0 and 18:0 fatty acids. Cholesterol content is unchanged although decreases in other lipids result in cholesterol accounting for a higher proportion of lipid in the membranes. This is associated with decreased membrane lateral diffusion. An increased ratio of 24:0 to 24:1 in ceramide, mono- and dihexosylceramide, and sphingomyelin likely also contributes to this decrease in lateral diffusion. Lipidomic profiling is targeted to specific membrane microdomains, overview. A decrease in phospholipids containing arachidonic acid is observed. Given the high degree of structural flexibility of this acyl chain this will influence membrane lateral diffusion, and is likely responsible for the transcriptional activation of Lands' cycle enzymes lpcat3 and mboat7
malfunction
inhibition of SCD1 activity represents a potential novel approach for the treatment of metabolic diseases such as obesity, type 2 diabetes and dyslipidemia, as well as skin diseases, acne and cancer
malfunction
loss of SCD-1 activity induces complex changes in the fatty acid composition of membrane lipids which are not restricted to the MUFA/SFA ratio. SCD-1 deficiency induces insulin signaling in peripheral tissues, namely phosphorylation of insulin receptor and insulin receptor substrates (IRS)1 and 2. Association of IRS isoforms with the regulatory subunit of phosphatidylinositol-3-kinase (PI3K) promotes the synthesis of phosphatidylinositol-3,4,5-trisphoshates (PIP3) as membrane anchor sites for the serine/threonine kinase Akt. SCD-1 inhibition suppressed starvation-induced autophagy in mouse embryonic fibroblasts and palmitate-induced autophagy in rat pancreatic beta-cells apparently by disturbing autophagosome-lysosome fusion
malfunction
reduced SCD1 activity in the liver causes endoplasmic reticulum stress that is only normalized by exogenous or endogenous oleate but not palmitoleate. SCD1 deficiency-mediated glucose uptake in skeletal muscle and brown adipose tissue feeds toward glycogen synthesis. Localized and systemic SCD1 deficiency increases glucose uptake in white adipose tissue through apparently different mechanisms involving GLUT1 and GLUT4, respectively. Liver-specific SCD1 KO mice exhibit different phenotypes compared to skin-specific SCD1 KO mice, suggesting that SCD1 products, monounsaturated fatty acids, carry out different functions in different tissues. Global SCD1 KO mice are protected against high carbohydrate diet and high fat diet-induced adiposity and hepatic steatosis. Liver-specific SCD1 knockout mice fed high-fat diet show a significant reduction of white adipose tissue weights compared with control mice. Hepatic SCD1 deficiency causes a significant reduction in hepatic lipogenic gene expression and reduced de novo lipogenesis associated with reduced hepatic triglyceride secretion. Skin-specific knockout mice show protection against high-fat diet-induced adiposity along with increased energy expenditure expected to be sufficient to counter increased calorie intake associated with feeding high-fat diet. In addition, similar to SCD1 global KO mice, skin-specific KO mice are hyperphagic and maintain lean phenotype accompanied by protection against extended high-fat diet feeding-induced insulin resistance. Skin-specific KO mice exhibit increased cold sensitivity and died within 3 h of cold exposure due to hypoglycemia. SCD1 isozyme-specific knockout phenotypes with respect to the other isozymes, detailed overview
malfunction
siRNA against SCD1 exacerbates the apoptosis
metabolism
isozyme SCD1 has a role in adipogenesis and lipid biosynthesis
metabolism
stearoyl-CoA desaturase-1 (SCD1) plays an important role in lipid metabolism
metabolism
survival and stress-activated signaling pathways are regulated by SCD-1, molecular link between SCD-1 activity and cell signaling, overview
metabolism
the enzyme is involved in the metabolism of free fatty acids
physiological function
stearoyl-CoA desaturase (SCD) introduces the first double bond into saturated fatty acyl-CoAs. Since the monounsaturated products of SCD are key precursors of membrane phospholipids, cholesterol esters, and triglycerides, SCD is pivotal in fatty acid metabolism
physiological function
stearoyl-CoA desaturase (SCD), the central enzyme in the biosynthesis of monounsaturated fatty acids, introduces a cis-DELTA9 double bond into saturated fatty acids. SCD-1 induces adaptive stress signaling that maintains cellular persistence and fosters survival and cellular functionality under distinct pathological conditions. Function, regulation, structure and mechanism of SCD-1, molecular mechanisms and potential lipid factors that link SCD-1 activity with initial signal transduction, overview. SCD-1 is the major isoenzyme responsible for monounsaturated fatty acid biosynthesis in most rodent tissues. SCD-1 is critical for cell proliferation, especially in hyperproliferative cells, such as cancer cells. Another mechanism bywhich SCD-1 modulates overall lipid metabolism depends on the negative regulation of the lipogenic transcription factor SREBP-1c, thereby reducing lipid biosynthesis and enhancing beta-oxidation of fatty acids. SCD-1 has a dual function in the regulation of autophagy by either promoting or inhibiting autophagy depending on the experimental settings and stress conditions
physiological function
stearoyl-CoA desaturase 1 is a lipogenic enzyme important for the regulation of membrane lipid homeostasis. The enzyme catalyses the insertion of a cis double bond in 12-19 carbon saturated fatty acids, thereby converting them to monounsaturated fatty acids. Through this activity, SCD1 helps to regulate the ratio of saturated to monounsaturated acyl chains in membrane lipids influencingmembrane fluidity and functionality, both essential for maintaining cellular integrity. Adaptive homeostatic mechanisms to ensure partial maintenance of the biophysical properties of membranes likely occur at a post-transcriptional level
physiological function
stearoyl-CoA desaturase-1, SCD1, is an enzyme that desaturates satruated fatty acids (SFA), converting them to monounsaturated fatty acids (MUFAs), leading to the formation of neutral lipid droplets. SCD1 activity protects cells against lipotoxicity-mediated apoptosis in proximal tubular cells. In culture, retrovirus-mediated overexpression of SCD1 or MUFA treatment significantly ameliorates saturated fatty acid-induced apoptosis in proximal tubular epithelial cells by enhancing intracellular lipid droplet formation. Both overexpression of SCD1 and monounsaturated fatty acid treatment reduces SFA-induced apoptosis via reducing endoplasmic reticulum stress in cultured proximal tubular epithelial cells
physiological function
stearoyl-coenzyme A desaturase 1 (SCD1) is a central regulator of fuel metabolism. SCD1 catalyzes the synthesis of monounsaturated fatty acids (MUFAs), mainly oleate and palmitoleate, which are important in controlling weight gain in response to feeding high carbohydrate diets, role of SCD1 isoform in the regulation of lipid and glucose metabolism in metabolic tissues. SCD1 products, oleate and palmitoleate, have different metabolic properties. Palmitoleate reduces hepatic lipogenesis and improves insulin sensitivity, while oleate promotes ectopic fat accumulation and increases glucose intolerance. Hepatic oleate, but not palmitoleate, regulates body weight. Exercise increases SCD1 activity in skeletal muscle, indicating increased fatty acid synthesis, and is proposed to be protective against weight gain
metabolism
-
SCD is critical in the biosynthesis of triglycerides, cholesterol esters, wax esters, and 1-alkyl-2,3-diacylglycerol
metabolism
-
stearoyl-CoA desaturase 1 is the rate-limiting enzyme in the biosynthesis of monounsaturated fatty acids and a risk factor of diabetes
metabolism
-
the enzyme is necessary for proper liver, adipose tissue, and skeletal muscle lipid metabolism
physiological function
-
absence of stearoyl-CoA desaturase-1 leads to chronic inflammation of the skin and increased susceptibility to atherosclerosis, while also increasing plasma inflammatory markers, but does not promote dextran sulfate sodium-induced acute colitis
physiological function
-
mice lacking Scd1 are protected from obesity and insulin resistance and are characterized by decreased fatty acid synthesis and increased fatty acid oxidation
physiological function
-
mice with a skin-specific deletion of SCD1 (SKO) have significantly increased energy expenditure, are protected from high fat diet-induced obesity, and display marked sebaceous gland hypoplasia and depletion of sebaceous lipids. SKO mice display severe cold intolerance because of rapid depletion of fuel substrates, including hepatic glycogen, to maintain core body temperature. Unlike mice globally deficient in SCD1, SKO mice have an intact hepatic lipogenic response to acute high carbohydrate feeding
physiological function
-
SCD-1 knockout mice show reduced body adiposity, increased insulin sensitivity, leanness, increased metabolic rate, and resistance to diet-induced obesity
physiological function
-
SCD1 knockout mice on the methionine-choline-deficient diet have decreased steatosis and markedly increased hepatocellular apoptosis, liver injury, and fibrosis compared with the SCD-expressing mice
physiological function
-
Scd1 null mice are more susceptible to dextran sulfate sodium treatment than wild type mice, while oleic acid feeding and in vivo SCD1 rescue with SCD1 adenovirus alleviates the dextran sulfate sodium-induced phenotype
physiological function
-
enzyme expression is important in regulating lipid bilayer fluidity, increasing triglyceride formation, and enabling lipogenesis and may protect against saturated fatty acids-induced lipotoxicity
physiological function
-
skin stearoyl-CoA desaturase 1 regulates skin integrity and energy balance
physiological function
stearoyl-CoA desaturase (SCD) introduces the first double bond into saturated fatty acyl-CoAs. Since the monounsaturated products of SCD are key precursors of membrane phospholipids, cholesterol esters, and triglycerides, SCD is pivotal in fatty acid metabolism
additional information
stearoyl-CoA desaturase-1 (SCD1) expression level significantly decreases in the kidneys of high-fat diet (HFD)-induced diabetic mice, compared with non-diabetic mice
additional information
structure-function analysis and catalytic mechanism of SCD-1, overview. SCD-1 consists of a cytosolic domain containing a di-metal active center and four alpha-helices forming a tight hydrophobic core, which is situated in the endoplasmic reticulum membrane. Acyl-CoA substrates bind to the surface of the cytoplasmic domain by forming multiple hydrogen bonds via the adenosine group, the panthothenate group and the carbonyl-group of the fatty acid. The substrate is fixed by ionic interactions between the phosphates of CoA and a positively charged surface of the enzyme and by a cation-Pi-interaction between adenosine and Lys194. The acyl-chain enters a hydrophobic tunnel extending to the interface of the cytoplasmic and transmembrane domain. The substrate tunnel has a kink, which is considered to hold the substrate and thereby determining regiospecificity of the enzyme and cis-conformation of the product. The catalytic center for dehydrogenation is located adjacent to the kink in the hydrophobic tunnel and adjacent to carbons 9 and 10 of stearoyl-CoA
additional information
the structure of isozyme SCD1 shows a fold comprising four transmembrane helices capped by a cytosolic domain, and a plausible pathway for lateral substrate access and product egress. The acyl chain of the bound stearoyl-CoA is enclosed in a tunnel buried in the cytosolic domain, and the geometry of the tunnel and configuration of the bound acyl chain provide a structural basis for the regioselectivity and stereospecificity of the desaturation reaction. The dimetal center is coordinated by a unique configuration of nine conserved histidine residues that implies a potentially distinct metal center and mechanism for oxygen activation, isozyme SCD1 structure analysis and modelling, overview. In SCD1, Ala108, Leu109, Ala288 and Val289 line the distal end of the substrate binding channel, Ala115 is near the position of double bond formation, while Gln277 and Ser278 are on the cytoplasmic surface opposite to the CoA binding site. Structural role of Arg249
additional information
the structure of isozyme SCD1 shows a fold comprising four transmembrane helices capped by a cytosolic domain, and a plausible pathway for lateral substrate access and product egress. The acyl chain of the bound stearoyl-CoA is enclosed in a tunnel buried in the cytosolic domain, and the geometry of the tunnel and configuration of the bound acyl chain provide a structural basis for the regioselectivity and stereospecificity of the desaturation reaction. The dimetal center is coordinated by a unique configuration of nine conserved histidine residues that implies a potentially distinct metal center and mechanism for oxygen activation, isozyme SCD1 structure analysis and modelling, overview. In SCD1, Ala108, Leu109, Ala288 and Val289 line the distal end of the substrate binding channel, Ala115 is near the position of double bond formation, while Gln277 and Ser278 are on the cytoplasmic surface opposite to the CoA binding site. Structural role of Arg249
additional information
-
the structure of isozyme SCD1 shows a fold comprising four transmembrane helices capped by a cytosolic domain, and a plausible pathway for lateral substrate access and product egress. The acyl chain of the bound stearoyl-CoA is enclosed in a tunnel buried in the cytosolic domain, and the geometry of the tunnel and configuration of the bound acyl chain provide a structural basis for the regioselectivity and stereospecificity of the desaturation reaction. The dimetal center is coordinated by a unique configuration of nine conserved histidine residues that implies a potentially distinct metal center and mechanism for oxygen activation, isozyme SCD1 structure analysis and modelling, overview. In SCD1, Ala108, Leu109, Ala288 and Val289 line the distal end of the substrate binding channel, Ala115 is near the position of double bond formation, while Gln277 and Ser278 are on the cytoplasmic surface opposite to the CoA binding site. Structural role of Arg249
additional information
in SCD3, Ile112, Glu113, Ser292 and Met293 line the distal end of the substrate binding channel, Val119 is near the position of double bond formation, while Asp281 and Pro282 are on the cytoplasmic surface opposite to the CoA binding site
additional information
in SCD3, Ile112, Glu113, Ser292 and Met293 line the distal end of the substrate binding channel, Val119 is near the position of double bond formation, while Asp281 and Pro282 are on the cytoplasmic surface opposite to the CoA binding site
additional information
-
in SCD3, Ile112, Glu113, Ser292 and Met293 line the distal end of the substrate binding channel, Val119 is near the position of double bond formation, while Asp281 and Pro282 are on the cytoplasmic surface opposite to the CoA binding site
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C222S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
C233S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
C322S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
C92S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
C92S/C97S/C222S/C322S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity 5fold increased compared with cells transfected with the empty vector, clear ER pattern
C97S
-
with Myc epitope tagged to the C terminus, expressed in HeLa cells, actitivity comparable to that of the wild-type
I112A/E113L
site-directed mutagenesis, the mutation is able to convert isozyme SCD3 from exclusively a 16:0 desaturase into a predominantly 18:0 desaturase
V119A/D281Q/P282S E113L
site-directed mutagenesis, the mutation of the residues which are located away from the end of the substrate tunnel, causes no change in the reaction specificity of isozyme SCD3
additional information
leptin-deficient obese ob/ob mice lacking SCD1 showed markedly reduced adiposity, despite higher food intake
additional information
leptin-deficient obese ob/ob mice lacking SCD1 showed markedly reduced adiposity, despite higher food intake
additional information
leptin-deficient obese ob/ob mice lacking SCD1 showed markedly reduced adiposity, despite higher food intake
additional information
leptin-deficient obese ob/ob mice lacking SCD1 showed markedly reduced adiposity, despite higher food intake
additional information
mice with targeted disruption in the SCD1 gene have increased energy expenditure, reduced body adiposity, increased insulin sensitivity and are resistant to diet-induced obesity
additional information
mice with targeted disruption in the SCD1 gene have increased energy expenditure, reduced body adiposity, increased insulin sensitivity and are resistant to diet-induced obesity
additional information
mice with targeted disruption in the SCD1 gene have increased energy expenditure, reduced body adiposity, increased insulin sensitivity and are resistant to diet-induced obesity
additional information
mice with targeted disruption in the SCD1 gene have increased energy expenditure, reduced body adiposity, increased insulin sensitivity and are resistant to diet-induced obesity
additional information
SCD1 -/- mice have a decrease in cellular levels of malonyl-CoA in the liver
additional information
SCD1 -/- mice have a decrease in cellular levels of malonyl-CoA in the liver
additional information
SCD1 -/- mice have a decrease in cellular levels of malonyl-CoA in the liver
additional information
SCD1 -/- mice have a decrease in cellular levels of malonyl-CoA in the liver
additional information
SCD1 deficiency attenuates fasting-induced liver steatosis in peroxisome proliferator-activated receptor alpha-deficient mice
additional information
SCD1 deficiency attenuates fasting-induced liver steatosis in peroxisome proliferator-activated receptor alpha-deficient mice
additional information
SCD1 deficiency attenuates fasting-induced liver steatosis in peroxisome proliferator-activated receptor alpha-deficient mice
additional information
SCD1 deficiency attenuates fasting-induced liver steatosis in peroxisome proliferator-activated receptor alpha-deficient mice
additional information
SCD1 deficiency corrects the hypometabolic phenotype and hepatic steatosis of ob/ob mice
additional information
SCD1 deficiency corrects the hypometabolic phenotype and hepatic steatosis of ob/ob mice
additional information
SCD1 deficiency corrects the hypometabolic phenotype and hepatic steatosis of ob/ob mice
additional information
SCD1 deficiency corrects the hypometabolic phenotype and hepatic steatosis of ob/ob mice
additional information
SCD1 deficiency increases the rate of beta-oxidation in liver, skeletal muscle and brown adipose tissue
additional information
SCD1 deficiency increases the rate of beta-oxidation in liver, skeletal muscle and brown adipose tissue
additional information
SCD1 deficiency increases the rate of beta-oxidation in liver, skeletal muscle and brown adipose tissue
additional information
SCD1 deficiency increases the rate of beta-oxidation in liver, skeletal muscle and brown adipose tissue
additional information
SCD1-deficient mice show significantly higher total and resting oxygen consumption than littermate controls
additional information
SCD1-deficient mice show significantly higher total and resting oxygen consumption than littermate controls
additional information
SCD1-deficient mice show significantly higher total and resting oxygen consumption than littermate controls
additional information
SCD1-deficient mice show significantly higher total and resting oxygen consumption than littermate controls
additional information
generation of global and tissue specific SCD1 knockout mice, phenotypes, detailed overview
additional information
generation of global and tissue specific SCD1 knockout mice, phenotypes, detailed overview
additional information
generation of global and tissue specific SCD1 knockout mice, phenotypes, detailed overview
additional information
generation of global and tissue specific SCD1 knockout mice, phenotypes, detailed overview
additional information
scd1 gene silencing by siRNA resulting in 90% reduction in scd1 mRNA expression, ceramide spectrum in the mutant, membrane microdomain lipid and acyl chain composition are altered in SCD1 knockdown mutant cells, phenotype, overview. Short range lateral diffusion, using 1-pyrenedecanoic acid, is highly reduced in mutant cell membranes. SCD1 knockout activates the expression of enzymes involved in the remodelling of phospholipids
additional information
siRNA-mediated downregulation of stearoyl-coenzyme A desaturase-1 (SCD1) in diabetic proximal tubular epithelial cells
additional information
-
activities of enzymes with HA epitope tagged to the N terminus and Myc epitope tagged to the C terminus expressed in HeLa cells are 23fold and 39fold higher than in cells transfected with an empty vector, acitivities of enzymes with HA epitope after amino acid 93 and 138 additionally Myc epitope tagged to the C terminus are 5.5fold and 5.9fold higher than in cells transfected with an empty vector, respectively
additional information
-
Myc epitope at the C terminus and additional HA epitope at predicted loops, after amino acid 93, 138 or 241
additional information
-
no activity when HA epitope is inserted after amino acid 241
additional information
-
SCD1 knockout mice show reduced levels of fatty acid transport proteins and lipid content on the heart, as well as decreased fatty acid beta-oxidation and a downregulated peroxisome proliferator-activated receptor-alpha, PPARalpha, pathway, the signalling pathways involved in glucose transport are affected, phenotype, overview
additional information
-
silencing of SCD1 does not downregulate 3T3-L1 cell differentiation or gene expression, inhibition of adipogenesis caused by SCD2 depletion is associated with a decrease in peroxisome proliferator-activated receptor alpha mRNA and protein, whereas in mature adipocytes loss of SCD2 diminishes PPARalpha protein levels, with little change in mRNA levels and protein translation levels
additional information
generation of liver-specific SCD3 knockout mice, phenotype. Partial restoration of endogenous palmitoleate levels in the liver through overexpression of mouse wild-type SCD3 isoform
additional information
generation of liver-specific SCD3 knockout mice, phenotype. Partial restoration of endogenous palmitoleate levels in the liver through overexpression of mouse wild-type SCD3 isoform
additional information
generation of liver-specific SCD3 knockout mice, phenotype. Partial restoration of endogenous palmitoleate levels in the liver through overexpression of mouse wild-type SCD3 isoform
additional information
generation of liver-specific SCD3 knockout mice, phenotype. Partial restoration of endogenous palmitoleate levels in the liver through overexpression of mouse wild-type SCD3 isoform
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Miyazaki, M.; Kim, H.J.; Man, W.C.; Ntambi, J.M.
Oleoyl-CoA is the major de novo product of stearoyl-CoA desaturase 1 gene isoform and substrate for the biosynthesis of the Harderian gland 1-alkyl-2,3-diacylglycerol
J. Biol. Chem.
276
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2001
Mus musculus
brenda
Miyazaki, M.; Jacobson, M.J.; Man, W.C.; Cohen, P.; Asilmaz, E.; Friedman, J.M.; Ntambi, J.M.
Identification and characterization of murine SCD4, a novel heart-specific stearoyl-CoA desaturase isoform regulated by leptin and dietary factors
J. Biol. Chem.
278
33904-33911
2003
Mus musculus (P13011), Mus musculus
brenda
Jiang, G.; Li, Z.; Liu, F.; Ellsworth, K.; Dallas-Yang, Q.; Wu, M.; Ronan, J.; Esau, C.; Murphy, C.; Szalkowski, D.; Bergeron, R.; Doebber, T.; Zhang, B.B.
Prevention of obesity in mice by antisense oligonucleotide inhibitors of stearoyl-CoA desaturase-1
J. Clin. Invest.
115
1030-1038
2005
Mus musculus
brenda
Biddinger, S.B.; Almind, K.; Miyazaki, M.; Kokkotou, E.; Ntambi, J.M.; Kahn, C.R.
Effects of diet and genetic background on sterol regulatory element-binding protein-1c, stearoyl-CoA desaturase 1, and the development of the metabolic syndrome
Diabetes
54
1314-1323
2005
Mus musculus
brenda
Biddinger, S.B.; Miyazaki, M.; Boucher, J.; Ntambi, J.M.; Kahn, C.R.
Leptin suppresses stearoyl-CoA desaturase 1 by mechanisms independent of insulin and sterol regulatory element-binding protein-1c
Diabetes
55
2032-2041
2006
Mus musculus
brenda
Dobrzyn, P.; Dobrzyn, A.
Stearoyl-CoA desaturase: a new therapeutic target of liver steatosis
Drug Develop. Res.
67
643-650
2006
Mus musculus (P13011), Mus musculus (P13516), Mus musculus (Q6T707), Mus musculus (Q99PL7)
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brenda
Mutch, D.M.; Grigorov, M.; Berger, A.; Fay, L.B.; Roberts, M.A.; Watkins, S.M.; Williamson, G.; German, J.B.
An integrative metabolism approach identifies stearoyl-CoA desaturase as a target for an arachidonate-enriched diet
FASEB J.
19
599-601
2005
Mus musculus (P13011), Mus musculus (P13516), Mus musculus (Q99PL7), Mus musculus, Mus musculus Rj:NMRI (P13011), Mus musculus Rj:NMRI (P13516), Mus musculus Rj:NMRI (Q99PL7)
brenda
Man, W.C.; Miyazaki, M.; Chu, K.; Ntambi, J.M.
Membrane topology of mouse stearoyl-CoA desaturase 1
J. Biol. Chem.
281
1251-1260
2006
Mus musculus
brenda
Sampath, H.; Miyazaki, M.; Dobrzyn, A.; Ntambi, J.M.
Stearoyl-CoA desaturase-1 mediates the pro-lipogenic effects of dietary saturated fat
J. Biol. Chem.
282
2483-2493
2007
Mus musculus
brenda
Flowers, M.T.; Miyazaki, M.; Liu, X.; Ntambi, J.M.
Probing the role of stearoyl-CoA desaturase-1 in hepatic insulin resistance
J. Clin. Invest.
116
1478-1481
2006
Mus musculus
brenda
Gutierrez-Juarez, R.; Pocai, A.; Mulas, C.; Ono, H.; Bhanot, S.; Monia, B.P.; Rossetti, L.
Critical role of stearoyl-CoA desaturase-1 (SCD1) in the onset of diet-induced hepatic insulin resistance
J. Clin. Invest.
116
1686-1695
2006
Mus musculus, Rattus norvegicus, Mus musculus C57/BL6J
brenda
Dobrzyn, A.; Dobrzyn, P.
Stearoyl-CoA desaturase - a new player in skeletal muscle metabolism regulation
J. Physiol. Pharmacol.
57 Suppl 10
31-42
2006
Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Dobrzyn, A.; Ntambi, J.M.
Stearoyl-CoA desaturase as a new drug target for obesity treatment
Obes. Rev.
6
169-174
2005
Mus musculus
brenda
Dobrzyn, P.; Sampath, H.; Dobrzyn, A.; Miyazaki, M.; Ntambi, J.M.
Loss of stearoyl-CoA desaturase 1 inhibits fatty acid oxidation and increases glucose utilization in the heart
Am. J. Physiol. Endocrinol. Metab.
294
E357-E364
2008
Mus musculus
brenda
Xin, Z.; Zhao, H.; Serby, M.D.; Liu, B.; Liu, M.; Szczepankiewicz, B.G.; Nelson, L.T.; Smith, H.T.; Suhar, T.S.; Janis, R.S.; Cao, N.; Camp, H.S.; Collins, C.A.; Sham, H.L.; Surowy, T.K.; Liu, G.
Discovery of piperidine-aryl urea-based stearoyl-CoA desaturase 1 inhibitors
Bioorg. Med. Chem. Lett.
18
4298-4302
2008
Homo sapiens, Mus musculus
brenda
Christianson, J.L.; Nicoloro, S.; Straubhaar, J.; Czech, M.P.
Stearoyl-CoA desaturase 2 is required for peroxisome proliferator-activated receptor gamma expression and adipogenesis in cultured 3T3-L1 cells
J. Biol. Chem.
283
2906-2916
2008
Mus musculus
brenda
Liu, G.; Lynch, J.K.; Freeman, J.; Liu, B.; Xin, Z.; Zhao, H.; Serby, M.D.; Kym, P.R.; Suhar, T.S.; Smith, H.T.; Cao, N.; Yang, R.; Janis, R.S.; Krauser, J.A.; Cepa, S.P.; Beno, D.W.; Sham, H.L.; Collins, C.A.; Surowy, T.K.; Camp, H.S.
Discovery of potent, selective, orally bioavailable stearoyl-CoA desaturase 1 inhibitors
J. Med. Chem.
50
3086-3100
2007
Homo sapiens, Mus musculus
brenda
Paton, C.M.; Ntambi, J.M.
Biochemical and physiological function of stearoyl-CoA desaturase
Am. J. Physiol. Endocrinol. Metab.
297
E28-E37
2009
Mus musculus
brenda
Macdonald, M.L.; Bissada, N.; Vallance, B.A.; Hayden, M.R.
Absence of stearoyl-CoA desaturase-1 does not promote DSS-induced acute colitis
Biochim. Biophys. Acta
1791
1166-1172
2009
Mus musculus
brenda
Flowers, M.T.; Ntambi, J.M.
Stearoyl-CoA desaturase and its relation to high-carbohydrate diets and obesity
Biochim. Biophys. Acta
1791
85-91
2009
Mus musculus
brenda
Uto, Y.; Ogata, T.; Harada, J.; Kiyotsuka, Y.; Ueno, Y.; Miyazawa, Y.; Kurata, H.; Deguchi, T.; Watanabe, N.; Takagi, T.; Wakimoto, S.; Okuyama, R.; Abe, M.; Kurikawa, N.; Kawamura, S.; Yamato, M.; Osumi, J.
Novel and potent inhibitors of stearoyl-CoA desaturase-1. Part I: Discovery of 3-(2-hydroxyethoxy)-4-methoxy-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide
Bioorg. Med. Chem. Lett.
19
4151-4158
2009
Homo sapiens, Mus musculus
brenda
Uto, Y.; Ogata, T.; Kiyotsuka, Y.; Miyazawa, Y.; Ueno, Y.; Kurata, H.; Deguchi, T.; Yamada, M.; Watanabe, N.; Takagi, T.; Wakimoto, S.; Okuyama, R.; Konishi, M.; Kurikawa, N.; Kono, K.; Osumi, J.
Novel and potent inhibitors of stearoyl-CoA desaturase-1. Part II: Identification of 4-ethylamino-3-(2-hydroxyethoxy)-N-[5-(3-trifluoromethylbenzyl)thiazol-2-yl]benzamide and its biological evaluation
Bioorg. Med. Chem. Lett.
19
4159-4166
2009
Homo sapiens, Mus musculus
brenda
Uto, Y.; Ogata, T.; Kiyotsuka, Y.; Ueno, Y.; Miyazawa, Y.; Kurata, H.; Deguchi, T.; Watanabe, N.; Konishi, M.; Okuyama, R.; Kurikawa, N.; Takagi, T.; Wakimoto, S.; Ohsumi, J.
Novel benzoylpiperidine-based stearoyl-CoA desaturase-1 inhibitors: Identification of 6-[4-(2-methylbenzoyl)piperidin-1-yl]pyridazine-3-carboxylic acid (2-hydroxy-2-pyridin-3-ylethyl)amide and its plasma triglyceride-lowering effects in Zucker fatty rats
Bioorg. Med. Chem. Lett.
20
341-345
2010
Homo sapiens, Mus musculus
brenda
Chen, C.; Shah, Y.M.; Morimura, K.; Krausz, K.W.; Miyazaki, M.; Richardson, T.A.; Morgan, E.T.; Ntambi, J.M.; Idle, J.R.; Gonzalez, F.J.
Metabolomics reveals that hepatic stearoyl-CoA desaturase 1 downregulation exacerbates inflammation and acute colitis
Cell Metab.
7
135-147
2008
Mus musculus
brenda
Sampath, H.; Flowers, M.T.; Liu, X.; Paton, C.M.; Sullivan, R.; Chu, K.; Zhao, M.; Ntambi, J.M.
Skin-specific deletion of stearoyl-CoA desaturase-1 alters skin lipid composition and protects mice from high fat diet-induced obesity
J. Biol. Chem.
284
19961-19973
2009
Mus musculus
brenda
Li, Z.Z.; Berk, M.; McIntyre, T.M.; Feldstein, A.E.
Hepatic lipid partitioning and liver damage in nonalcoholic fatty liver disease: role of stearoyl-CoA desaturase
J. Biol. Chem.
284
5637-5644
2009
Mus musculus
brenda
Stamatikos, A.D.; Paton, C.M.
Role of stearoyl-CoA desaturase-1 in skeletal muscle function and metabolism
Am. J. Physiol. Endocrinol. Metab.
305
E767-E775
2013
Mus musculus
brenda
Yokoyama, S.; Hosoi, T.; Ozawa, K.
Stearoyl-CoA desaturase 1 (SCD1) is a key factor mediating diabetes in MyD88-deficient mice
Gene
497
340-343
2012
Mus musculus
brenda
Sampath, H.; Ntambi, J.M.
The role of Stearoyl-CoA desaturase-1 in skin integrity and whole body energy balance
J. Biol. Chem.
289
2482-2488
2014
Mus musculus
brenda
Koeberle, A.; Loeser, K.; Thuermer, M.
Stearoyl-CoA desaturase-1 and adaptive stress signaling
Biochim. Biophys. Acta
1861
1719-1726
2016
Homo sapiens (O00767), Mus musculus (P13516)
brenda
Sun, S.; Zhang, Z.; Pokrovskaia, N.; Chowdhury, S.; Jia, Q.; Chang, E.; Khakh, K.; Kwan, R.; McLaren, D.G.; Radomski, C.C.; Ratkay, L.G.; Fu, J.; Dales, N.A.; Winther, M.D.
Discovery of triazolone derivatives as novel, potent stearoyl-CoA desaturase-1 (SCD1) inhibitors
Bioorg. Med. Chem.
23
455-465
2015
Homo sapiens (O00767), Mus musculus (P13516)
brenda
Iwai, T.; Kume, S.; Chin-Kanasaki, M.; Kuwagata, S.; Araki, H.; Takeda, N.; Sugaya, T.; Uzu, T.; Maegawa, H.; Araki, S.I.
Stearoyl-CoA desaturase-1 protects cells against lipotoxicity-mediated apoptosis in proximal tubular cells
Int. J. Mol. Sci.
17
E1868
2016
Mus musculus (P13516)
brenda
Bai, Y.; McCoy, J.G.; Levin, E.J.; Sobrado, P.; Rajashankar, K.R.; Fox, B.G.; Zhou, M.
X-ray structure of a mammalian stearoyl-CoA desaturase
Nature
524
252-256
2015
Mus musculus (P13516), Mus musculus (Q99PL7), Mus musculus
brenda
Rodriguez-Cuenca, S.; Whyte, L.; Hagen, R.; Vidal-Puig, A.; Fuller, M.
Stearoyl-CoA desaturase 1 Is a key determinant of membrane lipid composition in 3T3-L1 adipocytes
PLoS ONE
11
e0162047
2016
Mus musculus (P13516)
brenda
ALJohani, A.M.; Syed, D.N.; Ntambi, J.M.
Insights into stearoyl-CoA desaturase-1 regulation of systemic metabolism
Trends Endocrinol. Metab.
28
831-842
2017
Homo sapiens (O00767), Homo sapiens (Q86SK9), Mus musculus (P13011), Mus musculus (P13516), Mus musculus (Q8BNZ5), Mus musculus (Q8CFY4)
brenda