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These findings suggest that << S1P >> activates the [[ PI3K ]]/Akt signaling pathway leading to the promotion of nuclear translocation of β-catenin in osteoblast-like cells, resulting in the upregulation of osteoptotegerin and osteoblast differentiation markers including alkaline phosphatase, probably relating to the inhibition of osteoclast formation and the mineralization, respectively.

These findings suggest that << S1P >> activates the PI3K/[[ Akt ]] signaling pathway leading to the promotion of nuclear translocation of β-catenin in osteoblast-like cells, resulting in the upregulation of osteoptotegerin and osteoblast differentiation markers including alkaline phosphatase, probably relating to the inhibition of osteoclast formation and the mineralization, respectively.

These findings suggest that << S1P >> activates the PI3K/Akt signaling pathway leading to the promotion of nuclear translocation of [[ β-catenin ]] in osteoblast-like cells, resulting in the upregulation of osteoptotegerin and osteoblast differentiation markers including alkaline phosphatase, probably relating to the inhibition of osteoclast formation and the mineralization, respectively.

These findings suggest that << S1P >> activates the PI3K/Akt signaling pathway leading to the promotion of nuclear translocation of β-catenin in osteoblast-like cells, resulting in the upregulation of [[ osteoptotegerin ]] and osteoblast differentiation markers including alkaline phosphatase, probably relating to the inhibition of osteoclast formation and the mineralization, respectively.

These findings suggest that << S1P >> activates the PI3K/Akt signaling pathway leading to the promotion of nuclear translocation of β-catenin in osteoblast-like cells, resulting in the upregulation of osteoptotegerin and osteoblast differentiation markers including [[ alkaline phosphatase ]], probably relating to the inhibition of osteoclast formation and the mineralization, respectively.

<< Plerixafor >>, a [[ CXCR4 ]] antagonist for the mobilization of hematopoietic stem cells.

<< Plerixafor >> (AMD3100, Genzyme Corporation) is a bicyclam molecule that antagonizes the binding of the chemokine [[ stromal cell-derived factor-1 ]] (SDF-1) to its cognate receptor CXCR4.

<< Plerixafor >> (AMD3100, Genzyme Corporation) is a bicyclam molecule that antagonizes the binding of the chemokine stromal cell-derived factor-1 ([[ SDF-1 ]]) to its cognate receptor CXCR4.

<< Plerixafor >> (AMD3100, Genzyme Corporation) is a bicyclam molecule that antagonizes the binding of the chemokine stromal cell-derived factor-1 (SDF-1) to its cognate receptor [[ CXCR4 ]].

<< Plerixafor >> (AMD3100, Genzyme Corporation) is a bicyclam molecule that antagonizes the binding of the [[ chemokine ]] stromal cell-derived factor-1 (SDF-1) to its cognate receptor CXCR4.

Plerixafor (<< AMD3100 >>, Genzyme Corporation) is a bicyclam molecule that antagonizes the binding of the chemokine [[ stromal cell-derived factor-1 ]] (SDF-1) to its cognate receptor CXCR4.

Plerixafor (<< AMD3100 >>, Genzyme Corporation) is a bicyclam molecule that antagonizes the binding of the chemokine stromal cell-derived factor-1 ([[ SDF-1 ]]) to its cognate receptor CXCR4.

Plerixafor (<< AMD3100 >>, Genzyme Corporation) is a bicyclam molecule that antagonizes the binding of the chemokine stromal cell-derived factor-1 (SDF-1) to its cognate receptor [[ CXCR4 ]].

Plerixafor (<< AMD3100 >>, Genzyme Corporation) is a bicyclam molecule that antagonizes the binding of the [[ chemokine ]] stromal cell-derived factor-1 (SDF-1) to its cognate receptor CXCR4.

Plerixafor (AMD3100, Genzyme Corporation) is a << bicyclam >> molecule that antagonizes the binding of the chemokine [[ stromal cell-derived factor-1 ]] (SDF-1) to its cognate receptor CXCR4.

Plerixafor (AMD3100, Genzyme Corporation) is a << bicyclam >> molecule that antagonizes the binding of the chemokine stromal cell-derived factor-1 ([[ SDF-1 ]]) to its cognate receptor CXCR4.

Plerixafor (AMD3100, Genzyme Corporation) is a << bicyclam >> molecule that antagonizes the binding of the chemokine stromal cell-derived factor-1 (SDF-1) to its cognate receptor [[ CXCR4 ]].

Plerixafor (AMD3100, Genzyme Corporation) is a << bicyclam >> molecule that antagonizes the binding of the [[ chemokine ]] stromal cell-derived factor-1 (SDF-1) to its cognate receptor CXCR4.

This stimulation was attenuated by the << Pak >> inhibitor [[ 2,2'-dihydroxy-1,1'-dinaphthyldisulfide ]] (IPA3) or dominant-negative Pak1.

This stimulation was attenuated by the << Pak >> inhibitor 2,2'-dihydroxy-1,1'-dinaphthyldisulfide ([[ IPA3 ]]) or dominant-negative Pak1.

Chronic insulin (24 h) activates NHE3 through the classic << phosphatidylinositol 3-kinase >>-serum- and glucocorticoid-dependent kinase 1 (PI3K-SGK1) pathway as insulin stimulates SGK1 phosphorylation and the insulin effect can be blocked by the PI3K inhibitor [[ wortmannin ]] or a dominant-negative SGK1.

Chronic insulin (24 h) activates NHE3 through the classic phosphatidylinositol 3-kinase-serum- and glucocorticoid-dependent kinase 1 (<< PI3K >>-SGK1) pathway as insulin stimulates SGK1 phosphorylation and the insulin effect can be blocked by the PI3K inhibitor [[ wortmannin ]] or a dominant-negative SGK1.

Chronic insulin (24 h) activates NHE3 through the classic phosphatidylinositol 3-kinase-serum- and glucocorticoid-dependent kinase 1 (PI3K-SGK1) pathway as insulin stimulates SGK1 phosphorylation and the insulin effect can be blocked by the << PI3K >> inhibitor [[ wortmannin ]] or a dominant-negative SGK1.

Results showed that neonatal << quinpirole >> treatment induced [[ D2 ]] priming that was eliminated by olanzapine treatment.

Results showed that neonatal quinpirole treatment induced << D2 >> priming that was eliminated by [[ olanzapine ]] treatment.

Brain tissue analyses revealed that neonatal quinpirole treatment produced a significant decrease in hippocampal << NGF >>, BDNF and ChAT that was eliminated by [[ olanzapine ]] treatment.

Brain tissue analyses revealed that neonatal quinpirole treatment produced a significant decrease in hippocampal NGF, << BDNF >> and ChAT that was eliminated by [[ olanzapine ]] treatment.

Brain tissue analyses revealed that neonatal quinpirole treatment produced a significant decrease in hippocampal NGF, BDNF and << ChAT >> that was eliminated by [[ olanzapine ]] treatment.

Brain tissue analyses revealed that neonatal << quinpirole >> treatment produced a significant decrease in hippocampal [[ NGF ]], BDNF and ChAT that was eliminated by olanzapine treatment.

Brain tissue analyses revealed that neonatal << quinpirole >> treatment produced a significant decrease in hippocampal NGF, [[ BDNF ]] and ChAT that was eliminated by olanzapine treatment.

Brain tissue analyses revealed that neonatal << quinpirole >> treatment produced a significant decrease in hippocampal NGF, BDNF and [[ ChAT ]] that was eliminated by olanzapine treatment.

Neonatal << quinpirole >> treatment produced a significant decrease in [[ BDNF ]] and ChAT in the frontal cortex that was unaffected by olanzapine treatment.

Neonatal << quinpirole >> treatment produced a significant decrease in BDNF and [[ ChAT ]] in the frontal cortex that was unaffected by olanzapine treatment.

These results show that << olanzapine >> eliminates [[ D2 receptor ]] priming and cognitive impairment and also alleviates decreases in neurotrophins and acetylcholinergic markers produced by D2 priming in the hippocampus.

Suppression of << Src >>/ERK and GSK-3/β-catenin signaling by [[ pinosylvin ]] inhibits the growth of human colorectal cancer cells.

Suppression of Src/<< ERK >> and GSK-3/β-catenin signaling by [[ pinosylvin ]] inhibits the growth of human colorectal cancer cells.

Suppression of Src/ERK and << GSK-3 >>/β-catenin signaling by [[ pinosylvin ]] inhibits the growth of human colorectal cancer cells.

Suppression of Src/ERK and GSK-3/<< β-catenin >> signaling by [[ pinosylvin ]] inhibits the growth of human colorectal cancer cells.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of [[ p21 ]](WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21([[ WAF1 ]]/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/[[ CIP1 ]]) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/CIP1) and [[ p53 ]].

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of [[ cyclin D1 ]], cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, [[ cyclin E ]], cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, [[ cyclin A ]], cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, [[ cyclin dependent kinase 2 ]] (CDK2), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 ([[ CDK2 ]]), CDK4, c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), [[ CDK4 ]], c-Myc, and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, [[ c-Myc ]], and retinoblastoma protein (pRb), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and [[ retinoblastoma protein ]] (pRb), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> inhibited the proliferation of HCT 116 cells by arresting transition of cell cycle from G1 to S phase along with the downregulation of cyclin D1, cyclin E, cyclin A, cyclin dependent kinase 2 (CDK2), CDK4, c-Myc, and retinoblastoma protein ([[ pRb ]]), and the upregulation of p21(WAF1/CIP1) and p53.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in f[[ ocal adhesion kinase ]] (FAK)/c-Src/extracellular signal-regulated kinase (ERK) signaling, and phosphoinositide 3-kinase (PI3K)/Akt/ glycogen synthase kinase 3β (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase ([[ FAK ]])/c-Src/extracellular signal-regulated kinase (ERK) signaling, and phosphoinositide 3-kinase (PI3K)/Akt/ glycogen synthase kinase 3β (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase (FAK)/[[ c-Src ]]/extracellular signal-regulated kinase (ERK) signaling, and phosphoinositide 3-kinase (PI3K)/Akt/ glycogen synthase kinase 3β (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase (FAK)/c-Src/[[ extracellular signal-regulated kinase ]] (ERK) signaling, and phosphoinositide 3-kinase (PI3K)/Akt/ glycogen synthase kinase 3β (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase (FAK)/c-Src/extracellular signal-regulated kinase ([[ ERK ]]) signaling, and phosphoinositide 3-kinase (PI3K)/Akt/ glycogen synthase kinase 3β (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase (FAK)/c-Src/extracellular signal-regulated kinase (ERK) signaling, and [[ phosphoinositide 3-kinase ]] (PI3K)/Akt/ glycogen synthase kinase 3β (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase (FAK)/c-Src/extracellular signal-regulated kinase (ERK) signaling, and phosphoinositide 3-kinase ([[ PI3K ]])/Akt/ glycogen synthase kinase 3β (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase (FAK)/c-Src/extracellular signal-regulated kinase (ERK) signaling, and phosphoinositide 3-kinase (PI3K)/[[ Akt ]]/ glycogen synthase kinase 3β (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase (FAK)/c-Src/extracellular signal-regulated kinase (ERK) signaling, and phosphoinositide 3-kinase (PI3K)/Akt/ [[ glycogen synthase kinase 3β ]] (GSK-3β) signaling pathway.

<< Pinosylvin >> was also found to attenuate the activation of proteins involved in focal adhesion kinase (FAK)/c-Src/extracellular signal-regulated kinase (ERK) signaling, and phosphoinositide 3-kinase (PI3K)/Akt/ glycogen synthase kinase 3β ([[ GSK-3β ]]) signaling pathway.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of [[ β-catenin ]], one of downstream molecules of PI3K/Akt/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, ID2, survivin, cyclin D1, MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of [[ PI3K ]]/Akt/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, ID2, survivin, cyclin D1, MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/[[ Akt ]]/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, ID2, survivin, cyclin D1, MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/Akt/[[ GSK-3β ]] signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, ID2, survivin, cyclin D1, MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/Akt/GSK-3β signaling, and these events led to the sequential downregulation of [[ β-catenin ]]-mediated transcription of target genes including BMP4, ID2, survivin, cyclin D1, MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/Akt/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including [[ BMP4 ]], ID2, survivin, cyclin D1, MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/Akt/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, [[ ID2 ]], survivin, cyclin D1, MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/Akt/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, ID2, [[ survivin ]], cyclin D1, MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/Akt/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, ID2, survivin, [[ cyclin D1 ]], MMP7, and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/Akt/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, ID2, survivin, cyclin D1, [[ MMP7 ]], and c-Myc.

Subsequently, << pinosylvin >> suppressed the nuclear translocation of β-catenin, one of downstream molecules of PI3K/Akt/GSK-3β signaling, and these events led to the sequential downregulation of β-catenin-mediated transcription of target genes including BMP4, ID2, survivin, cyclin D1, MMP7, and [[ c-Myc ]].

Overall, higher alcohol production was reduced by << ammonium >> supplementation, and this can be correlated with a general downregulation of genes encoding [[ decarboxylases ]] and dehydrogenases of the Ehrlich pathway.

Overall, higher alcohol production was reduced by << ammonium >> supplementation, and this can be correlated with a general downregulation of genes encoding decarboxylases and [[ dehydrogenases ]] of the Ehrlich pathway.

Novel analgesic/anti-inflammatory agents: 1,5-diarylpyrrole nitrooxyalkyl ethers and related compounds as << cyclooxygenase-2 >> inhibiting [[ nitric oxide ]] donors.

Novel analgesic/anti-inflammatory agents: << 1,5-diarylpyrrole nitrooxyalkyl ethers >> and related compounds as [[ cyclooxygenase-2 ]] inhibiting nitric oxide donors.

New classes of << pyrrole >>-derived nitrooxyalkyl inverse esters, carbonates, and ethers (7-10) as [[ COX-2 ]] selective inhibitors and NO donors were synthesized and are herein reported.

New classes of pyrrole-derived << nitrooxyalkyl >> inverse esters, carbonates, and ethers (7-10) as [[ COX-2 ]] selective inhibitors and NO donors were synthesized and are herein reported.

New classes of pyrrole-derived nitrooxyalkyl inverse << esters >>, carbonates, and ethers (7-10) as [[ COX-2 ]] selective inhibitors and NO donors were synthesized and are herein reported.

New classes of pyrrole-derived nitrooxyalkyl inverse esters, << carbonates >>, and ethers (7-10) as [[ COX-2 ]] selective inhibitors and NO donors were synthesized and are herein reported.

New classes of pyrrole-derived nitrooxyalkyl inverse esters, carbonates, and << ethers >> (7-10) as [[ COX-2 ]] selective inhibitors and NO donors were synthesized and are herein reported.

<< Nitrooxy >> derivatives showed NO-dependent vasorelaxing properties, while most of the compounds proved to be very potent and selective [[ COX-2 ]] inhibitors in in vitro experimental models.

The clinical profile of the << angiotensin II receptor >> blocker [[ eprosartan ]].

In clinical trials << eprosartan >> has proven to be at least as effective as the [[ ACE ]] inhibitor enalapril in reducing BP, but with a significantly lower incidence of side effects.

A significant decrease of << aspartate aminotransferase >>, alanine aminotransferase, lactate dehydrogenase (LDH) activities and glutathione (GSH) levels and an increase of malondialdehyde (MDA) quantity was observed after [[ CCl4 ]] and PC administration alone.

A significant decrease of aspartate aminotransferase, << alanine aminotransferase >>, lactate dehydrogenase (LDH) activities and glutathione (GSH) levels and an increase of malondialdehyde (MDA) quantity was observed after [[ CCl4 ]] and PC administration alone.

A significant decrease of aspartate aminotransferase, alanine aminotransferase, << lactate dehydrogenase >> (LDH) activities and glutathione (GSH) levels and an increase of malondialdehyde (MDA) quantity was observed after [[ CCl4 ]] and PC administration alone.

A significant decrease of aspartate aminotransferase, alanine aminotransferase, lactate dehydrogenase (<< LDH >>) activities and glutathione (GSH) levels and an increase of malondialdehyde (MDA) quantity was observed after [[ CCl4 ]] and PC administration alone.

In the CCl4 hepatotoxicity model, pre-treatment with PSM or << silymarin >> resulted in significantly increased activities of [[ ethylmorphine-N-demethylase ]] and aniline 4-hydroxylase activity and cytochrome P450, compared to the CCl4 only group.

In the CCl4 hepatotoxicity model, pre-treatment with PSM or << silymarin >> resulted in significantly increased activities of ethylmorphine-N-demethylase and [[ aniline 4-hydroxylase ]] activity and cytochrome P450, compared to the CCl4 only group.

In the CCl4 hepatotoxicity model, pre-treatment with PSM or << silymarin >> resulted in significantly increased activities of ethylmorphine-N-demethylase and aniline 4-hydroxylase activity and [[ cytochrome P450 ]], compared to the CCl4 only group.

In the CCl4 hepatotoxicity model, pre-treatment with PSM or silymarin resulted in significantly increased activities of << ethylmorphine-N-demethylase >> and aniline 4-hydroxylase activity and cytochrome P450, compared to the [[ CCl4 ]] only group.

In the CCl4 hepatotoxicity model, pre-treatment with PSM or silymarin resulted in significantly increased activities of ethylmorphine-N-demethylase and << aniline 4-hydroxylase >> activity and cytochrome P450, compared to the [[ CCl4 ]] only group.

In the CCl4 hepatotoxicity model, pre-treatment with PSM or silymarin resulted in significantly increased activities of ethylmorphine-N-demethylase and aniline 4-hydroxylase activity and << cytochrome P450 >>, compared to the [[ CCl4 ]] only group.

In vitro inhibition of << diacylglycerol acyltransferase >> by [[ prenylflavonoids ]] from Sophora flavescens.

Four prenylflavonoids, kurarinone ( 1), a chalcone of 1, << kuraridin >> ( 2), kurarinol ( 3), kushenol H ( 4) and kushenol K ( 5) isolated from the roots of Sophora flavescens were investigated for their inhibitory effects on [[ diacylglycerol acyltransferase ]] (DGAT).

Four prenylflavonoids, kurarinone ( 1), a chalcone of 1, << kuraridin >> ( 2), kurarinol ( 3), kushenol H ( 4) and kushenol K ( 5) isolated from the roots of Sophora flavescens were investigated for their inhibitory effects on diacylglycerol acyltransferase ([[ DGAT ]]).

Four prenylflavonoids, kurarinone ( 1), a chalcone of 1, kuraridin ( 2), << kurarinol >> ( 3), kushenol H ( 4) and kushenol K ( 5) isolated from the roots of Sophora flavescens were investigated for their inhibitory effects on [[ diacylglycerol acyltransferase ]] (DGAT).

Four prenylflavonoids, kurarinone ( 1), a chalcone of 1, kuraridin ( 2), << kurarinol >> ( 3), kushenol H ( 4) and kushenol K ( 5) isolated from the roots of Sophora flavescens were investigated for their inhibitory effects on diacylglycerol acyltransferase ([[ DGAT ]]).

Four prenylflavonoids, kurarinone ( 1), a chalcone of 1, kuraridin ( 2), kurarinol ( 3), << kushenol H >> ( 4) and kushenol K ( 5) isolated from the roots of Sophora flavescens were investigated for their inhibitory effects on [[ diacylglycerol acyltransferase ]] (DGAT).