We show that both << darapladib >> and a novel class of structurally distinct carbamate inhibitors inactivate [[ Lp-PLA(2) ]] in mouse tissues and human cell lines with high selectivity.


We show that both darapladib and a novel class of structurally distinct << carbamate >> inhibitors inactivate [[ Lp-PLA(2) ]] in mouse tissues and human cell lines with high selectivity.


Sepracor in the US is developing arformoterol [R,R-formoterol], a single isomer form of the << beta(2)-adrenoceptor >> agonist [[ formoterol ]] [eformoterol].


Sepracor in the US is developing arformoterol [R,R-formoterol], a single isomer form of the << beta(2)-adrenoceptor >> agonist formoterol [[[ eformoterol ]]].


Nitric oxide products of << VP-16 >> displayed significantly diminished [[ topoisomerase II ]]-dependent cleavage of DNA and cytotoxicity to human HL-60 leukemia cells.


Consistent with these locations, << N-ethylmaleimide >>, an inhibitor of [[ ACS4 ]], inhibited ACS activity 47% in MAM and 28% in endoplasmic reticulum.


Consistent with these locations, << N-ethylmaleimide >>, an inhibitor of ACS4, inhibited [[ ACS ]] activity 47% in MAM and 28% in endoplasmic reticulum.


<< Troglitazone >>, a second [[ ACS4 ]] inhibitor, inhibited ACS activity <10% in microsomes and mitochondria and 45% in MAM.


<< Troglitazone >>, a second ACS4 inhibitor, inhibited [[ ACS ]] activity <10% in microsomes and mitochondria and 45% in MAM.


<< Triacsin C >>, a competitive inhibitor of both [[ ACS1 ]] and ACS4, inhibited ACS activity similarly in endoplasmic reticulum, MAM, and mitochondria, suggesting that a hitherto unidentified triacsin-sensitive ACS is present in mitochondria.


<< Triacsin C >>, a competitive inhibitor of both ACS1 and [[ ACS4 ]], inhibited ACS activity similarly in endoplasmic reticulum, MAM, and mitochondria, suggesting that a hitherto unidentified triacsin-sensitive ACS is present in mitochondria.


<< Triacsin C >>, a competitive inhibitor of both ACS1 and ACS4, inhibited [[ ACS ]] activity similarly in endoplasmic reticulum, MAM, and mitochondria, suggesting that a hitherto unidentified triacsin-sensitive ACS is present in mitochondria.


Re-feeding normal chow or a high << sucrose >> diet for 24 h after a 48-h fast increased both [[ ACS1 ]] and ACS4 protein expression 1.5-2.0-fold, consistent with inhibition studies.


Re-feeding normal chow or a high << sucrose >> diet for 24 h after a 48-h fast increased both ACS1 and [[ ACS4 ]] protein expression 1.5-2.0-fold, consistent with inhibition studies.


These results suggest that << ACS1 >> and ACS4 may be linked to [[ triacylglycerol ]] synthesis.


These results suggest that ACS1 and << ACS4 >> may be linked to [[ triacylglycerol ]] synthesis.


The << tyrosine kinase >> inhibitor [[ ZD1839 ]] ("Iressa") inhibits HER2-driven signaling and suppresses the growth of HER2-overexpressing tumor cells.


The tyrosine kinase inhibitor << ZD1839 >> ("Iressa") inhibits [[ HER2 ]]-driven signaling and suppresses the growth of HER2-overexpressing tumor cells.


The tyrosine kinase inhibitor ZD1839 ("<< Iressa >>") inhibits HER2-driven signaling and suppresses the growth of [[ HER2 ]]-overexpressing tumor cells.


The << tyrosine kinase >> inhibitor ZD1839 ("[[ Iressa ]]") inhibits HER2-driven signaling and suppresses the growth of HER2-overexpressing tumor cells.


The tyrosine kinase inhibitor ZD1839 ("<< Iressa >>") inhibits [[ HER2 ]]-driven signaling and suppresses the growth of HER2-overexpressing tumor cells.


The << tyrosine kinase >>[[ tyrosine ]] kinase inhibitor ZD1839 ("Iressa") inhibits HER2-driven signaling and suppresses the growth of HER2-overexpressing tumor cells.


<< ZD1839 >> ("Iressa"), a quinazoline [[ tyrosine kinase ]] inhibitor selective for the EGFR, has shown good activity in preclinical studies and in the early phase of clinical trials.


<< ZD1839 >> ("Iressa"), a quinazoline tyrosine kinase inhibitor selective for the [[ EGFR ]], has shown good activity in preclinical studies and in the early phase of clinical trials.


ZD1839 ("<< Iressa >>"), a quinazoline [[ tyrosine kinase ]] inhibitor selective for the EGFR, has shown good activity in preclinical studies and in the early phase of clinical trials.


ZD1839 ("<< Iressa >>"), a quinazoline tyrosine kinase inhibitor selective for the [[ EGFR ]], has shown good activity in preclinical studies and in the early phase of clinical trials.


ZD1839 ("Iressa"), a << quinazoline tyrosine >>[[ tyrosine kinase ]] inhibitor selective for the EGFR, has shown good activity in preclinical studies and in the early phase of clinical trials.


Growth inhibition of these tumor cell lines was associated with the dephosphorylation of EGFR, HER2, and HER3, accompanied by the loss of association of HER3 with << phosphatidylinositol 3-kinase >>[[ phosphatidylinositol ]] 3-kinase, and down-regulation of Akt activity.


These studies suggest that HER2-overexpressing tumors are particularly susceptible to the inhibition of HER family << tyrosine kinase >>[[ tyrosine ]] kinase signaling and suggest novel strategies to treat these particularly aggressive tumors.


[Pharmacological effects of a << mu-opioid receptor >> antagonist [[ naltrexone ]] on alcohol dependence].


In many countries, a << mu-opioid receptor >> antagonist [[ naltrexone ]] has been used in the treatment of alcohol dependence.


RESULTS: In drug discrimination studies, << lisuride >> fully mimicked the [[ 5-HT(1A) ]] agonist LY 293284, only partially substituted for LSD and DOI, and failed to substitute for (+)-amphetamine.


RESULTS: In drug discrimination studies, lisuride fully mimicked the << 5-HT(1A) >> agonist [[ LY 293284 ]], only partially substituted for LSD and DOI, and failed to substitute for (+)-amphetamine.


Only pMPPI [<< 4-iodo-N-[2-[4-(methoxyphenyl)-1-piperazinyl]ethyl]-N-2-pyridynyl-benzamide hydrochloride >>], a selective [[ 5-HT(1A) ]] antagonist, was effective in inhibiting all 5-HT syndrome behaviors produced by lisuride, whereas pMPPI was without effect on any behavior induced by LSD.


Lisuride dose dependently decreased body temperature in rats with a potency similar to that of the selective << 5-HT(1A) >> agonist [[ LY 293284 ]].


<< Bupropion >>, an efficacious antidepressant and smoking cessation agent, inhibits dopamine and norepinephrine transporters ([[ DAT ]] and NET, respectively).


<< Bupropion >>, an efficacious antidepressant and smoking cessation agent, inhibits dopamine and norepinephrine transporters (DAT and [[ NET ]], respectively).


To eliminate the interaction of << bupropion >> with [[ DAT ]] or NET, nomifensine or desipramine, respectively, was included in the superfusion buffer.


To eliminate the interaction of << bupropion >> with DAT or [[ NET ]], nomifensine or desipramine, respectively, was included in the superfusion buffer.


Thus, << bupropion >> acts as an antagonist at alpha3beta2* and alpha3beta4* nAChRs in rat striatum and hippocampus, respectively, across the same concentration range that inhibits [[ DAT ]] and NET function.


Thus, << bupropion >> acts as an antagonist at alpha3beta2* and alpha3beta4* nAChRs in rat striatum and hippocampus, respectively, across the same concentration range that inhibits DAT and [[ NET ]] function.


The combination of << nAChR >> and transporter inhibition produced by [[ bupropion ]] may contribute to its clinical efficacy as a smoking cessation agent.


<< Nitrogen >>-containing bisphosphonates induce apoptosis of hematopoietic tumor cells via inhibition of Ras signaling pathways and [[ Bim ]]-mediated activation of the intrinsic apoptotic pathway.


Nitrogen-containing << bisphosphonates >> induce apoptosis of hematopoietic tumor cells via inhibition of Ras signaling pathways and [[ Bim ]]-mediated activation of the intrinsic apoptotic pathway.


<< Nitrogen >>-containing bisphosphonates induce apoptosis of hematopoietic tumor cells via inhibition of [[ Ras ]] signaling pathways and Bim-mediated activation of the intrinsic apoptotic pathway.


Nitrogen-containing << bisphosphonates >> induce apoptosis of hematopoietic tumor cells via inhibition of [[ Ras ]] signaling pathways and Bim-mediated activation of the intrinsic apoptotic pathway.


<< Nitrogen >>-containing bisphosphonates (N-BPs) induce apoptosis in tumor cells by inhibiting the prenylation of small [[ G-proteins ]].


Nitrogen-containing << bisphosphonates >> (N-BPs) induce apoptosis in tumor cells by inhibiting the prenylation of small [[ G-proteins ]].


Nitrogen-containing bisphosphonates (<< N >>-BPs) induce apoptosis in tumor cells by inhibiting the prenylation of small [[ G-proteins ]].


Nitrogen-containing bisphosphonates (N-<< BPs >>) induce apoptosis in tumor cells by inhibiting the prenylation of small [[ G-proteins ]].


Furthermore, << N >>-BPs decreased the levels of phosphorylated extracellular signal-regulated kinase (ERK) and mTOR via suppression of Ras prenylation and enhanced [[ Bim ]] expression.


Furthermore, N-<< BPs >> decreased the levels of phosphorylated extracellular signal-regulated kinase (ERK) and mTOR via suppression of Ras prenylation and enhanced [[ Bim ]] expression.


Furthermore, << N >>-BPs decreased the levels of [[ phosphorylated extracellular signal-regulated kinase ]] (ERK) and mTOR via suppression of Ras prenylation and enhanced Bim expression.


Furthermore, << N >>-BPs decreased the levels of phosphorylated extracellular signal-regulated kinase ([[ ERK ]]) and mTOR via suppression of Ras prenylation and enhanced Bim expression.


Furthermore, << N >>-BPs decreased the levels of phosphorylated extracellular signal-regulated kinase (ERK) and [[ mTOR ]] via suppression of Ras prenylation and enhanced Bim expression.


Furthermore, N-<< BPs >> decreased the levels of [[ phosphorylated extracellular signal-regulated kinase ]] (ERK) and mTOR via suppression of Ras prenylation and enhanced Bim expression.


Furthermore, N-<< BPs >> decreased the levels of phosphorylated extracellular signal-regulated kinase ([[ ERK ]]) and mTOR via suppression of Ras prenylation and enhanced Bim expression.


Furthermore, N-<< BPs >> decreased the levels of phosphorylated extracellular signal-regulated kinase (ERK) and [[ mTOR ]] via suppression of Ras prenylation and enhanced Bim expression.


Furthermore, << N >>-BPs decreased the levels of phosphorylated extracellular signal-regulated kinase (ERK) and mTOR via suppression of [[ Ras ]] prenylation and enhanced Bim expression.


Furthermore, N-<< BPs >> decreased the levels of phosphorylated extracellular signal-regulated kinase (ERK) and mTOR via suppression of [[ Ras ]] prenylation and enhanced Bim expression.


The present results indicated that << N >>-BPs induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of [[ caspase-9 ]] and caspase-3, and enhancing Bim expression through inhibition of the Ras/MEK/ERK and Ras/mTOR pathways.


The present results indicated that << N >>-BPs induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and [[ caspase-3 ]], and enhancing Bim expression through inhibition of the Ras/MEK/ERK and Ras/mTOR pathways.


The present results indicated that N-<< BPs >> induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of [[ caspase-9 ]] and caspase-3, and enhancing Bim expression through inhibition of the Ras/MEK/ERK and Ras/mTOR pathways.


The present results indicated that N-<< BPs >> induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and [[ caspase-3 ]], and enhancing Bim expression through inhibition of the Ras/MEK/ERK and Ras/mTOR pathways.


The present results indicated that << N >>-BPs induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing [[ Bim ]] expression through inhibition of the Ras/MEK/ERK and Ras/mTOR pathways.


The present results indicated that N-<< BPs >> induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing [[ Bim ]] expression through inhibition of the Ras/MEK/ERK and Ras/mTOR pathways.


The present results indicated that << N >>-BPs induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the [[ Ras ]]/MEK/ERK and Ras/mTOR pathways.


The present results indicated that << N >>-BPs induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the Ras/[[ MEK ]]/ERK and Ras/mTOR pathways.


The present results indicated that << N >>-BPs induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the Ras/MEK/[[ ERK ]] and Ras/mTOR pathways.


The present results indicated that << N >>-BPs induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the Ras/MEK/ERK and [[ Ras ]]/mTOR pathways.


The present results indicated that << N >>-BPs induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the Ras/MEK/ERK and Ras/[[ mTOR ]] pathways.


The present results indicated that N-<< BPs >> induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the [[ Ras ]]/MEK/ERK and Ras/mTOR pathways.


The present results indicated that N-<< BPs >> induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the Ras/[[ MEK ]]/ERK and Ras/mTOR pathways.


The present results indicated that N-<< BPs >> induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the Ras/MEK/[[ ERK ]] and Ras/mTOR pathways.


The present results indicated that N-<< BPs >> induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the Ras/MEK/ERK and [[ Ras ]]/mTOR pathways.


The present results indicated that N-<< BPs >> induce apoptosis by decreasing the mitochondrial transmembrane potential, increasing the activation of caspase-9 and caspase-3, and enhancing Bim expression through inhibition of the Ras/MEK/ERK and Ras/[[ mTOR ]] pathways.


The reduction of << P2X3 >> expression levels was reversed by the proteasomal inhibitor [[ MG-132 ]].


We investigated the involvement of the farnesoid X receptor (FXR), a nuclear receptor for bile acids, in the << chenodeoxycholic acid >> (CDCA)-induced expression of [[ Cdx2 ]] and MUC2 in normal rat gastric epithelial cells (RGM-1 cells).


We investigated the involvement of the farnesoid X receptor (FXR), a nuclear receptor for bile acids, in the << chenodeoxycholic acid >> (CDCA)-induced expression of Cdx2 and [[ MUC2 ]] in normal rat gastric epithelial cells (RGM-1 cells).


We investigated the involvement of the farnesoid X receptor (FXR), a nuclear receptor for bile acids, in the chenodeoxycholic acid (<< CDCA >>)-induced expression of [[ Cdx2 ]] and MUC2 in normal rat gastric epithelial cells (RGM-1 cells).


We investigated the involvement of the farnesoid X receptor (FXR), a nuclear receptor for bile acids, in the chenodeoxycholic acid (<< CDCA >>)-induced expression of Cdx2 and [[ MUC2 ]] in normal rat gastric epithelial cells (RGM-1 cells).


RGM-1 cells were treated with << CDCA >> or GW4064, an [[ FXR ]] agonist, in the presence or absence of guggulsterone, an FXR antagonist.


RGM-1 cells were treated with CDCA or << GW4064 >>, an [[ FXR ]] agonist, in the presence or absence of guggulsterone, an FXR antagonist.


RGM-1 cells were treated with CDCA or GW4064, an FXR agonist, in the presence or absence of << guggulsterone >>, an [[ FXR ]] antagonist.


<< CDCA >> induced dose-dependent expression of [[ Cdx2 ]] and MUC2 at both the mRNA and protein levels.


<< CDCA >> induced dose-dependent expression of Cdx2 and [[ MUC2 ]] at both the mRNA and protein levels.


The maximum stimulation of << Cdx2 >> and MUC2 mRNA induced by [[ CDCA ]] was observed at 3 h and by 6 h, respectively.


The maximum stimulation of Cdx2 and << MUC2 >> mRNA induced by [[ CDCA ]] was observed at 3 h and by 6 h, respectively.


The effects of CDCA and GW4064 on expression of << Cdx2 >> and MUC2 were abolished by [[ guggulsterone ]].


The effects of CDCA and GW4064 on expression of Cdx2 and << MUC2 >> were abolished by [[ guggulsterone ]].


<< Mazindol >> analogues as potential inhibitors of the [[ cocaine binding site ]] at the dopamine transporter.


<< Mazindol >> analogues as potential inhibitors of the cocaine binding site at the [[ dopamine transporter ]].


Mazindol analogues as potential inhibitors of the cocaine binding site at the << dopamine transporter >>[[ dopamine ]] transporter.


Several active analogues were also evaluated for their ability to block uptake of DA, << 5-HT >>, and NE and inhibit binding of [(125)I] RTI-55 at HEK-hDAT, HEK-[[ hSERT ]], and HEK-hNET cells.


Several active analogues were also evaluated for their ability to block uptake of DA, 5-HT, and << NE >> and inhibit binding of [(125)I] RTI-55 at HEK-hDAT, HEK-hSERT, and HEK-[[ hNET ]] cells.


Several active analogues were also evaluated for their ability to block uptake of << DA >>, 5-HT, and NE and inhibit binding of [(125)I] RTI-55 at HEK-[[ hDAT ]], HEK-hSERT, and HEK-hNET cells.


<< Glyphosate >> affects aromatic amino acid biosynthesis by inhibiting [[ 5-enolpyruvylshikimate-3-phosphate synthase ]] (EPSPS).


<< Glyphosate >> affects aromatic amino acid biosynthesis by inhibiting 5-enolpyruvylshikimate-3-phosphate synthase ([[ EPSPS ]]).


<< Glufosinate >> inhibits [[ glutamine synthetase ]] and blocks biosynthesis of glutamine.


Glufosinate inhibits << glutamine synthetase >> and blocks biosynthesis of [[ glutamine ]].


Mechanisms of Glucose Lowering of << Dipeptidyl Peptidase-4 >> Inhibitor [[ Sitagliptin ]] When Used Alone or With Metformin in Type 2 Diabetes: A double-tracer study.


Upon co-exposure to V(5+) and << TCDD >>, V(5+) significantly potentiated the TCDD-mediated induction of the [[ Cyp1a1 ]], Cyp1a2, and Cyp1b1 mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to V(5+) and << TCDD >>, V(5+) significantly potentiated the TCDD-mediated induction of the Cyp1a1, [[ Cyp1a2 ]], and Cyp1b1 mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to V(5+) and << TCDD >>, V(5+) significantly potentiated the TCDD-mediated induction of the Cyp1a1, Cyp1a2, and [[ Cyp1b1 ]] mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to << V(5+) >> and TCDD, V(5+) significantly potentiated the TCDD-mediated induction of the [[ Cyp1a1 ]], Cyp1a2, and Cyp1b1 mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to << V(5+) >> and TCDD, V(5+) significantly potentiated the TCDD-mediated induction of the Cyp1a1, [[ Cyp1a2 ]], and Cyp1b1 mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to << V(5+) >> and TCDD, V(5+) significantly potentiated the TCDD-mediated induction of the Cyp1a1, Cyp1a2, and [[ Cyp1b1 ]] mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to V(5+) and TCDD, << V(5+) >> significantly potentiated the TCDD-mediated induction of the [[ Cyp1a1 ]], Cyp1a2, and Cyp1b1 mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to V(5+) and TCDD, << V(5+) >> significantly potentiated the TCDD-mediated induction of the Cyp1a1, [[ Cyp1a2 ]], and Cyp1b1 mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to V(5+) and TCDD, << V(5+) >> significantly potentiated the TCDD-mediated induction of the Cyp1a1, Cyp1a2, and [[ Cyp1b1 ]] mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to V(5+) and TCDD, V(5+) significantly potentiated the << TCDD >>-mediated induction of the [[ Cyp1a1 ]], Cyp1a2, and Cyp1b1 mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to V(5+) and TCDD, V(5+) significantly potentiated the << TCDD >>-mediated induction of the Cyp1a1, [[ Cyp1a2 ]], and Cyp1b1 mRNA, protein, and catalytic activity levels at 24 h.


Upon co-exposure to V(5+) and TCDD, V(5+) significantly potentiated the << TCDD >>-mediated induction of the Cyp1a1, Cyp1a2, and [[ Cyp1b1 ]] mRNA, protein, and catalytic activity levels at 24 h.


In vitro, V(5+) decreased the << TCDD >>-mediated induction of [[ Cyp1a1 ]] mRNA, protein, and catalytic activity levels.


In vitro, << V(5+) >> decreased the TCDD-mediated induction of [[ Cyp1a1 ]] mRNA, protein, and catalytic activity levels.


Furthermore, V(5+) significantly inhibited the << TCDD >>-induced [[ AhR ]]-dependent luciferase activity.


Furthermore, << V(5+) >> significantly inhibited the TCDD-induced [[ AhR ]]-dependent luciferase activity.


<< V(5+) >> also increased [[ serum hemoglobin ]] (Hb) levels in animals treated for 24 h.


<< V(5+) >> also increased serum hemoglobin ([[ Hb ]]) levels in animals treated for 24 h.


Upon treatment of isolated hepatocytes with Hb alone or in the presence of << TCDD >>, there was an increase in the [[ AhR ]]-dependent luciferase activity.


<< GCS >> therapy results in reduced mRNA expression of [[ interleukin-4 ]] (IL-4) and IL-5 in cells from bronchoalveolar lavage (BAL) but not of IFN-gamma.


<< GCS >> therapy results in reduced mRNA expression of interleukin-4 ([[ IL-4 ]]) and IL-5 in cells from bronchoalveolar lavage (BAL) but not of IFN-gamma.


<< GCS >> therapy results in reduced mRNA expression of interleukin-4 (IL-4) and [[ IL-5 ]] in cells from bronchoalveolar lavage (BAL) but not of IFN-gamma.


In vitro studies with blood-derived T cells, however, show inhibition of all three << cytokines >> by [[ GCS ]].


Dexamethasone (<< DEX >>) inhibited the anti-CD3-induced production of [[ IL-4 ]], IL-5 and IFN-gamma in all 20 clones tested.


Dexamethasone (<< DEX >>) inhibited the anti-CD3-induced production of IL-4, [[ IL-5 ]] and IFN-gamma in all 20 clones tested.


Dexamethasone (<< DEX >>) inhibited the anti-CD3-induced production of IL-4, IL-5 and [[ IFN-gamma ]] in all 20 clones tested.


<< Dexamethasone >> (DEX) inhibited the anti-CD3-induced production of [[ IL-4 ]], IL-5 and IFN-gamma in all 20 clones tested.


<< Dexamethasone >> (DEX) inhibited the anti-CD3-induced production of IL-4, [[ IL-5 ]] and IFN-gamma in all 20 clones tested.


<< Dexamethasone >> (DEX) inhibited the anti-CD3-induced production of IL-4, IL-5 and [[ IFN-gamma ]] in all 20 clones tested.


Dexamethasone (<< DEX >>) inhibited the anti-[[ CD3 ]]-induced production of IL-4, IL-5 and IFN-gamma in all 20 clones tested.


<< Dexamethasone >> (DEX) inhibited the anti-[[ CD3 ]]-induced production of IL-4, IL-5 and IFN-gamma in all 20 clones tested.


<< DEX >> enhanced the ratio [[ IFN-gamma ]]/IL-4 (mean +/- SEM: control, 28.7 +/- 17.6; with 10-7 M DEX, 55.0 +/- 27.5, P<0.005).


<< DEX >> enhanced the ratio IFN-gamma/[[ IL-4 ]] (mean +/- SEM: control, 28.7 +/- 17.6; with 10-7 M DEX, 55.0 +/- 27.5, P<0.005).


Interestingly, two categories of clones were distinguished based on the effects of GCS on IL-2 production and IL-2R alpha expression and proliferation; 1) In low IL-2 producers DEX blocked IL-2 production and decreased IL-2R alpha expression and proliferation; 2) In high IL-2 producers << DEX >> inhibited IL-2 production partially and enhanced [[ IL-2R alpha ]] expression and proliferation.


Interestingly, two categories of clones were distinguished based on the effects of GCS on IL-2 production and IL-2R alpha expression and proliferation; 1) In low IL-2 producers << DEX >> blocked [[ IL-2 ]] production and decreased IL-2R alpha expression and proliferation; 2) In high IL-2 producers DEX inhibited IL-2 production partially and enhanced IL-2R alpha expression and proliferation.


Interestingly, two categories of clones were distinguished based on the effects of GCS on IL-2 production and IL-2R alpha expression and proliferation; 1) In low IL-2 producers << DEX >> blocked IL-2 production and decreased [[ IL-2R alpha ]] expression and proliferation; 2) In high IL-2 producers DEX inhibited IL-2 production partially and enhanced IL-2R alpha expression and proliferation.


Interestingly, two categories of clones were distinguished based on the effects of GCS on IL-2 production and IL-2R alpha expression and proliferation; 1) In low IL-2 producers DEX blocked IL-2 production and decreased IL-2R alpha expression and proliferation; 2) In high IL-2 producers << DEX >> inhibited [[ IL-2 ]] production partially and enhanced IL-2R alpha expression and proliferation.


In conclusion, the production of << IL-4 >> and IL-5 by T-cell clones (derived either from BAL or blood) was more sensitive to inhibition by [[ DEX ]] than that of IFN-gamma, which may account for the therapeutic effects of glucocorticosteroids in patients with asthma.


In conclusion, the production of IL-4 and << IL-5 >> by T-cell clones (derived either from BAL or blood) was more sensitive to inhibition by [[ DEX ]] than that of IFN-gamma, which may account for the therapeutic effects of glucocorticosteroids in patients with asthma.


In conclusion, the production of IL-4 and IL-5 by T-cell clones (derived either from BAL or blood) was more sensitive to inhibition by << DEX >> than that of [[ IFN-gamma ]], which may account for the therapeutic effects of glucocorticosteroids in patients with asthma.


Pregnane X Receptor Mediates Dyslipidemia Induced by the << HIV Protease >> Inhibitor [[ Amprenavir ]] in Mice.


In the present study, we identified << amprenavir >>, a widely used HIV PI, as a potent [[ PXR ]]-selective agonist.


<< Amprenavir >> efficiently activated [[ PXR ]] and induced PXR target gene expression in vitro and in vivo.


<< Amprenavir >> efficiently activated PXR and induced [[ PXR ]] target gene expression in vitro and in vivo.


<< Amprenavir >>-mediated [[ PXR ]] activation stimulated the expression of several key intestinal genes involved in lipid homeostasis.


Anti-diabetic Activity of Swertiamarin is due to an Active Metabolite, << Gentianine >>, that Upregulates [[ PPAR-γ ]] Gene Expression in 3T3-L1 cells.


<< Swertiamarin >> treatment had no significant effect on adipogenesis, or the mRNA expression of PPAR-γ and GLUT-4; however, there was a significant increase in the mRNA expression of [[ adiponectin ]].


On the other hand, treatment with << gentianine >> significantly increased adipogenesis, which was associated with a significant increase in the mRNA expression of [[ PPAR-γ ]], GLUT-4 and adiponectin.


On the other hand, treatment with << gentianine >> significantly increased adipogenesis, which was associated with a significant increase in the mRNA expression of PPAR-γ, [[ GLUT-4 ]] and adiponectin.


On the other hand, treatment with << gentianine >> significantly increased adipogenesis, which was associated with a significant increase in the mRNA expression of PPAR-γ, GLUT-4 and [[ adiponectin ]].


<< Jaspamide >> also inhibited other channels including [[ Cav1.2 ]], Cav3.2, and HCN2; however, the Kv11.1 (hERG) channel was minimally affected.


<< Jaspamide >> also inhibited other channels including Cav1.2, [[ Cav3.2 ]], and HCN2; however, the Kv11.1 (hERG) channel was minimally affected.


<< Jaspamide >> also inhibited other channels including Cav1.2, Cav3.2, and [[ HCN2 ]]; however, the Kv11.1 (hERG) channel was minimally affected.


Treatment with << carvedilol >> reversed both protein and mRNA of HIF-1alpha, VEGF, BNP, and [[ NGF-beta ]] to the baseline values.


Treatment with << carvedilol >> reversed both protein and mRNA of [[ HIF-1alpha ]], VEGF, BNP, and NGF-beta to the baseline values.


Treatment with << carvedilol >> reversed both protein and mRNA of HIF-1alpha, [[ VEGF ]], BNP, and NGF-beta to the baseline values.


Treatment with << carvedilol >> reversed both protein and mRNA of HIF-1alpha, VEGF, [[ BNP ]], and NGF-beta to the baseline values.


Increased immunohistochemical labeling of << HIF-1alpha >>, VEGF, and BNP in the ventricular myocardium was observed in the shunt group and [[ carvedilol ]] again normalized the labeling.


Increased immunohistochemical labeling of HIF-1alpha, << VEGF >>, and BNP in the ventricular myocardium was observed in the shunt group and [[ carvedilol ]] again normalized the labeling.


Increased immunohistochemical labeling of HIF-1alpha, VEGF, and << BNP >> in the ventricular myocardium was observed in the shunt group and [[ carvedilol ]] again normalized the labeling.


Treatment with << carvedilol >> is associated with a reversal of abnormal regulation of [[ HIF-1alpha ]] and VEGF in the failing ventricular myocardium.


Treatment with << carvedilol >> is associated with a reversal of abnormal regulation of HIF-1alpha and [[ VEGF ]] in the failing ventricular myocardium.


These effects were fully counteracted by dietary << phenolics >> which inhibited ROS overproduction and GSH consumption, rendered the reactive transcription of glutathione-associated enzymes unnecessary and blocked the intracellular signals leading to the overexpression and rearrangement of [[ p66Shc ]] signalling molecule.


The enzyme requires PLP and divalent cations such as Ca(2+), Mg(2+), or Mn(2+), but not ATP, whereas mammalian << serine racemase >> activity is increased by [[ ATP ]].


In kidneys, stimulation of adenylyl cyclase causes egress of cAMP, conversion of cAMP to << AMP >> by ecto-[[ phosphodiesterase ]], and metabolism of AMP to adenosine by ecto-5'-nucleotidase.


In kidneys, stimulation of adenylyl cyclase causes egress of cAMP, conversion of cAMP to AMP by ecto-phosphodiesterase, and metabolism of AMP to << adenosine >> by [[ ecto-5'-nucleotidase ]].


In kidneys, stimulation of adenylyl cyclase causes egress of cAMP, conversion of << cAMP >> to AMP by ecto-[[ phosphodiesterase ]], and metabolism of AMP to adenosine by ecto-5'-nucleotidase.


In kidneys, stimulation of adenylyl cyclase causes egress of cAMP, conversion of cAMP to AMP by ecto-phosphodiesterase, and metabolism of << AMP >> to adenosine by [[ ecto-5'-nucleotidase ]].


A broad-spectrum << phosphodiesterase >> (PDE) inhibitor ([[ 1,3-isobutyl-1-methylxanthine ]], 300 microM, n=6) and an ecto-phosphodiesterase inhibitor (1,3-dipropyl-8-p-sulfophenylxanthine, 1 mM, n=6) significantly attenuated cAMP-induced AMP secretion by 60 and 74%, respectively.


A broad-spectrum phosphodiesterase (<< PDE >>) inhibitor ([[ 1,3-isobutyl-1-methylxanthine ]], 300 microM, n=6) and an ecto-phosphodiesterase inhibitor (1,3-dipropyl-8-p-sulfophenylxanthine, 1 mM, n=6) significantly attenuated cAMP-induced AMP secretion by 60 and 74%, respectively.


Blockade of PDE1 (8-methoxymethyl-3-isobutyl-1-methylxanthine, 100 microM), PDE2 [erythro-9-(2-hydroxy-3-nonyl)adenine, 30 microM], << PDE3 >> ([[ milrinone ]], 10 microM; cGMP, 10 microM), PDE4 (Ro 20-1724 [4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one], 100 microM), PDE5 and PDE6 (zaprinast, 30 microM), and PDE7 [BRL-50481 (5-nitro-2,N,N-trimethylbenzenesulfonamide), 10 microM] did not alter renal ecto-phosphodiesterase activity.


Blockade of << PDE1 >> ([[ 8-methoxymethyl-3-isobutyl-1-methylxanthine ]], 100 microM), PDE2 [erythro-9-(2-hydroxy-3-nonyl)adenine, 30 microM], PDE3 (milrinone, 10 microM; cGMP, 10 microM), PDE4 (Ro 20-1724 [4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one], 100 microM), PDE5 and PDE6 (zaprinast, 30 microM), and PDE7 [BRL-50481 (5-nitro-2,N,N-trimethylbenzenesulfonamide), 10 microM] did not alter renal ecto-phosphodiesterase activity.


Blockade of PDE1 (8-methoxymethyl-3-isobutyl-1-methylxanthine, 100 microM), << PDE2 >> [[[ erythro-9-(2-hydroxy-3-nonyl)adenine ]], 30 microM], PDE3 (milrinone, 10 microM; cGMP, 10 microM), PDE4 (Ro 20-1724 [4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one], 100 microM), PDE5 and PDE6 (zaprinast, 30 microM), and PDE7 [BRL-50481 (5-nitro-2,N,N-trimethylbenzenesulfonamide), 10 microM] did not alter renal ecto-phosphodiesterase activity.


Blockade of PDE1 (8-methoxymethyl-3-isobutyl-1-methylxanthine, 100 microM), PDE2 [erythro-9-(2-hydroxy-3-nonyl)adenine, 30 microM], PDE3 (milrinone, 10 microM; cGMP, 10 microM), << PDE4 >> (Ro 20-1724 [[[ 4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one ]]], 100 microM), PDE5 and PDE6 (zaprinast, 30 microM), and PDE7 [BRL-50481 (5-nitro-2,N,N-trimethylbenzenesulfonamide), 10 microM] did not alter renal ecto-phosphodiesterase activity.


Blockade of PDE1 (8-methoxymethyl-3-isobutyl-1-methylxanthine, 100 microM), PDE2 [erythro-9-(2-hydroxy-3-nonyl)adenine, 30 microM], PDE3 (milrinone, 10 microM; cGMP, 10 microM), PDE4 (Ro 20-1724 [4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one], 100 microM), << PDE5 >> and PDE6 ([[ zaprinast ]], 30 microM), and PDE7 [BRL-50481 (5-nitro-2,N,N-trimethylbenzenesulfonamide), 10 microM] did not alter renal ecto-phosphodiesterase activity.


Blockade of PDE1 (8-methoxymethyl-3-isobutyl-1-methylxanthine, 100 microM), PDE2 [erythro-9-(2-hydroxy-3-nonyl)adenine, 30 microM], PDE3 (milrinone, 10 microM; cGMP, 10 microM), PDE4 (Ro 20-1724 [4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one], 100 microM), PDE5 and << PDE6 >> ([[ zaprinast ]], 30 microM), and PDE7 [BRL-50481 (5-nitro-2,N,N-trimethylbenzenesulfonamide), 10 microM] did not alter renal ecto-phosphodiesterase activity.


Blockade of PDE1 (8-methoxymethyl-3-isobutyl-1-methylxanthine, 100 microM), PDE2 [erythro-9-(2-hydroxy-3-nonyl)adenine, 30 microM], PDE3 (milrinone, 10 microM; cGMP, 10 microM), PDE4 (Ro 20-1724 [4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one], 100 microM), PDE5 and PDE6 (zaprinast, 30 microM), and << PDE7 >> [[[ BRL-50481 ]] (5-nitro-2,N,N-trimethylbenzenesulfonamide), 10 microM] did not alter renal ecto-phosphodiesterase activity.


Blockade of PDE1 (8-methoxymethyl-3-isobutyl-1-methylxanthine, 100 microM), PDE2 [erythro-9-(2-hydroxy-3-nonyl)adenine, 30 microM], PDE3 (milrinone, 10 microM; cGMP, 10 microM), PDE4 (Ro 20-1724 [4-(3-butoxy-4-methoxybenzyl)imidazolidin-2-one], 100 microM), PDE5 and PDE6 (zaprinast, 30 microM), and << PDE7 >> [BRL-50481 ([[ 5-nitro-2,N,N-trimethylbenzenesulfonamide ]]), 10 microM] did not alter renal ecto-phosphodiesterase activity.


Administration of a concentration (100 microM) of << dipyridamole >> that blocks [[ PDE8 ]] inhibited ecto-phosphodiesterase activity (by 44%).


Administration of a concentration (100 microM) of << dipyridamole >> that blocks PDE8 inhibited ecto-[[ phosphodiesterase ]] activity (by 44%).


However, a lower concentration of << dipyridamole >> (3 microM) that blocks [[ PDE9 ]], PDE10, and PDE11, but not PDE8, did not inhibit ecto-phosphodiesterase activity.


However, a lower concentration of << dipyridamole >> (3 microM) that blocks PDE9, [[ PDE10 ]], and PDE11, but not PDE8, did not inhibit ecto-phosphodiesterase activity.


However, a lower concentration of << dipyridamole >> (3 microM) that blocks PDE9, PDE10, and [[ PDE11 ]], but not PDE8, did not inhibit ecto-phosphodiesterase activity.


These data support the conclusion that renal ecto-<< phosphodiesterase >> activity is not mediated by PDE1, PDE2, PDE3, PDE4, PDE5, PDE6, PDE7, PDE9, PDE10, or PDE11 and is inhibited by high concentrations of [[ dipyridamole ]].


<< Ambrisentan >> is an [[ endothelin type A (ET(A))-selective receptor ]] antagonist that is metabolized primarily by glucuronidation but also undergoes oxidative metabolism by CYP3A4.


<< Ambrisentan >> is an endothelin type A (ET(A))-selective receptor antagonist that is metabolized primarily by glucuronidation but also undergoes oxidative metabolism by [[ CYP3A4 ]].


The potential for << ketoconazole >>, the archetypal strong inhibitor of [[ CYP3A4 ]], to alter the pharmacokinetic profile of ambrisentan and its oxidative metabolite, 4-hydroxymethyl ambrisentan, was assessed in an open-label, nonrandomized, 2-period, single-sequence study in 16 healthy men.


In summary, << ketoconazole >> had no clinically significant effect on the pharmacokinetics or safety profile of ambrisentan; therefore, no changes in ambrisentan dose should be necessary when the drug is administered concomitantly with known [[ CYP3A4 ]] inhibitors.


Although << glutathione S-transferase omega 1 >> (GSTO1) and arsenic methyltransferase have been shown or thought to catalyze [[ DMAs(V) ]] reduction, their role in DMAs(V) reduction in vivo, or in cell extracts is uncertain.


Although glutathione S-transferase omega 1 (GSTO1) and << arsenic methyltransferase >> have been shown or thought to catalyze [[ DMAs(V) ]] reduction, their role in DMAs(V) reduction in vivo, or in cell extracts is uncertain.


Pretreatment of rats with glutathione (GSH) depletors (phorone or BSO) delayed the elimination of DMAs(V) and the accumulation of RBC-bound DMAs, whereas the indirect << methyltransferase >> inhibitor periodate-oxidized [[ adenosine ]] was without effect.


Although << thioredoxin reductase >> (TRR) inhibitors ([[ aurothioglucose ]] and Sb(III)) inhibited cytosolic DMAs(V) reduction, recombinant rat TRR plus NADPH, alone or when added to the cytosol, failed to support DMAs(V) reduction.


Although thioredoxin reductase (<< TRR >>) inhibitors ([[ aurothioglucose ]] and Sb(III)) inhibited cytosolic DMAs(V) reduction, recombinant rat TRR plus NADPH, alone or when added to the cytosol, failed to support DMAs(V) reduction.


Although << thioredoxin reductase >> (TRR) inhibitors (aurothioglucose and [[ Sb(III) ]]) inhibited cytosolic DMAs(V) reduction, recombinant rat TRR plus NADPH, alone or when added to the cytosol, failed to support DMAs(V) reduction.


Although thioredoxin reductase (<< TRR >>) inhibitors (aurothioglucose and [[ Sb(III) ]]) inhibited cytosolic DMAs(V) reduction, recombinant rat TRR plus NADPH, alone or when added to the cytosol, failed to support DMAs(V) reduction.


The << kinase >> activity of EGFR was little inhibited by [[ TT-B ]] in a cell-free system.


The kinase activity of << EGFR >> was little inhibited by [[ TT-B ]] in a cell-free system.


<< Sorafenib >> (BAY 43-9006, Nexavar), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and [[ tyrosine kinases ]] VEGFR/PDGFR in tumor vasculature.


<< Sorafenib >> (BAY 43-9006, Nexavar), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and tyrosine kinases [[ VEGFR ]]/PDGFR in tumor vasculature.


<< Sorafenib >> (BAY 43-9006, Nexavar), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and tyrosine kinases VEGFR/[[ PDGFR ]] in tumor vasculature.


<< Sorafenib >> (BAY 43-9006, Nexavar), a dual-action inhibitor that targets [[ RAF ]]/MEK/ERK pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


<< Sorafenib >> (BAY 43-9006, Nexavar), a dual-action inhibitor that targets RAF/[[ MEK ]]/ERK pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


<< Sorafenib >> (BAY 43-9006, Nexavar), a dual-action inhibitor that targets RAF/MEK/[[ ERK ]] pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


Sorafenib (<< BAY 43-9006 >>, Nexavar), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and [[ tyrosine kinases ]] VEGFR/PDGFR in tumor vasculature.


Sorafenib (<< BAY 43-9006 >>, Nexavar), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and tyrosine kinases [[ VEGFR ]]/PDGFR in tumor vasculature.


Sorafenib (<< BAY 43-9006 >>, Nexavar), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and tyrosine kinases VEGFR/[[ PDGFR ]] in tumor vasculature.


Sorafenib (<< BAY 43-9006 >>, Nexavar), a dual-action inhibitor that targets [[ RAF ]]/MEK/ERK pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


Sorafenib (<< BAY 43-9006 >>, Nexavar), a dual-action inhibitor that targets RAF/[[ MEK ]]/ERK pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


Sorafenib (<< BAY 43-9006 >>, Nexavar), a dual-action inhibitor that targets RAF/MEK/[[ ERK ]] pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


Sorafenib (BAY 43-9006, << Nexavar >>), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and [[ tyrosine kinases ]] VEGFR/PDGFR in tumor vasculature.


Sorafenib (BAY 43-9006, << Nexavar >>), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and tyrosine kinases [[ VEGFR ]]/PDGFR in tumor vasculature.


Sorafenib (BAY 43-9006, << Nexavar >>), a dual-action inhibitor that targets RAF/MEK/ERK pathway in tumor cells and tyrosine kinases VEGFR/[[ PDGFR ]] in tumor vasculature.


Sorafenib (BAY 43-9006, << Nexavar >>), a dual-action inhibitor that targets [[ RAF ]]/MEK/ERK pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


Sorafenib (BAY 43-9006, << Nexavar >>), a dual-action inhibitor that targets RAF/[[ MEK ]]/ERK pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


Sorafenib (BAY 43-9006, << Nexavar >>), a dual-action inhibitor that targets RAF/MEK/[[ ERK ]] pathway in tumor cells and tyrosine kinases VEGFR/PDGFR in tumor vasculature.


A novel class of << biaryl urea >> that inhibits [[ C-RAF ]] kinase was discovered using a combination of medicinal and combinatorial chemistry approaches.


A novel class of << biaryl urea >> that inhibits C-RAF [[ kinase ]] was discovered using a combination of medicinal and combinatorial chemistry approaches.


<< Sorafenib >> inhibited the [[ kinase ]] activity of both C-RAF and B-RAF (wild type and V600E mutant).


<< Sorafenib >> inhibited the kinase activity of both [[ C-RAF ]] and B-RAF (wild type and V600E mutant).


<< Sorafenib >> inhibited the kinase activity of both C-RAF and [[ B-RAF ]] (wild type and V600E mutant).


<< Sorafenib >> inhibited the kinase activity of both C-RAF and B-RAF (wild type and [[ V600E ]] mutant).


Further characterization of << sorafenib >> revealed that this molecule was a multikinase inhibitor that targeted the [[ vascular endothelial growth factor receptor ]] family (VEGFR-2 and VEGFR-3) and platelet-derived growth factor receptor family (PDGFR-beta and Kit), which play key roles in tumor progression and angiogenesis.


Further characterization of << sorafenib >> revealed that this molecule was a multikinase inhibitor that targeted the vascular endothelial growth factor receptor family ([[ VEGFR-2 ]] and VEGFR-3) and platelet-derived growth factor receptor family (PDGFR-beta and Kit), which play key roles in tumor progression and angiogenesis.


Further characterization of << sorafenib >> revealed that this molecule was a multikinase inhibitor that targeted the vascular endothelial growth factor receptor family (VEGFR-2 and [[ VEGFR-3 ]]) and platelet-derived growth factor receptor family (PDGFR-beta and Kit), which play key roles in tumor progression and angiogenesis.


Further characterization of << sorafenib >> revealed that this molecule was a multikinase inhibitor that targeted the vascular endothelial growth factor receptor family (VEGFR-2 and VEGFR-3) and [[ platelet-derived growth factor receptor ]] family (PDGFR-beta and Kit), which play key roles in tumor progression and angiogenesis.


Further characterization of << sorafenib >> revealed that this molecule was a multikinase inhibitor that targeted the vascular endothelial growth factor receptor family (VEGFR-2 and VEGFR-3) and platelet-derived growth factor receptor family ([[ PDGFR-beta ]] and Kit), which play key roles in tumor progression and angiogenesis.


Further characterization of << sorafenib >> revealed that this molecule was a multikinase inhibitor that targeted the vascular endothelial growth factor receptor family (VEGFR-2 and VEGFR-3) and platelet-derived growth factor receptor family (PDGFR-beta and [[ Kit ]]), which play key roles in tumor progression and angiogenesis.


Thus, << sorafenib >> may inhibit tumor growth by a dual mechanism, acting either directly on the tumor (through inhibition of [[ Raf ]] and Kit signaling) and/or on tumor angiogenesis (through inhibition of VEGFR and PDGFR signaling).


Thus, << sorafenib >> may inhibit tumor growth by a dual mechanism, acting either directly on the tumor (through inhibition of Raf and [[ Kit ]] signaling) and/or on tumor angiogenesis (through inhibition of VEGFR and PDGFR signaling).


Thus, << sorafenib >> may inhibit tumor growth by a dual mechanism, acting either directly on the tumor (through inhibition of Raf and Kit signaling) and/or on tumor angiogenesis (through inhibition of [[ VEGFR ]] and PDGFR signaling).


Thus, << sorafenib >> may inhibit tumor growth by a dual mechanism, acting either directly on the tumor (through inhibition of Raf and Kit signaling) and/or on tumor angiogenesis (through inhibition of VEGFR and [[ PDGFR ]] signaling).


<< Rapamycin >> inhibits [[ proteinase ]] and selected peptidase activities of the catalytic core proteasome at low micromolar concentrations.


<< Rapamycin >> inhibits proteinase and selected [[ peptidase ]] activities of the catalytic core proteasome at low micromolar concentrations.


<< Rapamycin >> inhibits proteinase and selected peptidase activities of the catalytic core [[ proteasome ]] at low micromolar concentrations.


Ten IU/mL urokinase was also incubated with pooled plasma of stroke patients, that was previously oxidized with the singlet oxygen (1O2) donor << chloramine T >> (CT), to destroy [[ plasmatic PAI-1 ]] and alpha2-antiplasmin.


Ten IU/mL urokinase was also incubated with pooled plasma of stroke patients, that was previously oxidized with the singlet oxygen (1O2) donor << chloramine T >> (CT), to destroy plasmatic PAI-1 and alpha2-anti[[ plasmin ]].


Ten IU/mL urokinase was also incubated with pooled plasma of stroke patients, that was previously oxidized with the singlet oxygen (1O2) donor chloramine T (<< CT >>), to destroy [[ plasmatic PAI-1 ]] and alpha2-antiplasmin.


Ten IU/mL urokinase was also incubated with pooled plasma of stroke patients, that was previously oxidized with the singlet oxygen (1O2) donor chloramine T (<< CT >>), to destroy plasmatic PAI-1 and alpha2-anti[[ plasmin ]].


Ten IU/mL urokinase was also incubated with pooled plasma of stroke patients, that was previously oxidized with the << singlet oxygen >> (1O2) donor chloramine T (CT), to destroy [[ plasmatic PAI-1 ]] and alpha2-antiplasmin.


Ten IU/mL urokinase was also incubated with pooled plasma of stroke patients, that was previously oxidized with the singlet oxygen (<< 1O2 >>) donor chloramine T (CT), to destroy [[ plasmatic PAI-1 ]] and alpha2-antiplasmin.


For determination of << plasmin >> activity, 10 microL thereof was incubated with 150 microL 1.5 M [[ arginine ]], pH 8.7, and 100 microL 20 mM CT preoxidized (15 minutes 37 degrees C) pooled normal citrate buffered EDTA-plasma for 30 minutes (37 degrees C).


For determination of [<< PA >>+Pli]-activity, [[ arginine ]] was added after this incubation.


For determination of [PA+<< Pli >>]-activity, [[ arginine ]] was added after this incubation.


<< KCNK1 >>, a member of the family of two-pore K(+) ion channels, is specifically induced in the livers of male mice after [[ phenobarbital ]] treatment.


KCNK1, a member of the family of two-pore << K(+) ion channels >>, is specifically induced in the livers of male mice after [[ phenobarbital ]] treatment.


Here, we have determined the molecular mechanism of this male-specific activation of the Kcnk1 gene and characterized << KCNK1 >> as a [[ phenobarbital ]]-inducible antihyperplasia factor.


Here, we have determined the molecular mechanism of this male-specific activation of the << Kcnk1 >> gene and characterized KCNK1 as a [[ phenobarbital ]]-inducible antihyperplasia factor.


Upon activation by << phenobarbital >>, [[ nuclear receptor ]] CAR binds the 97-bp response element (-2441/-2345) within the Kcnk1 promoter.


Upon activation by << phenobarbital >>, nuclear receptor [[ CAR ]] binds the 97-bp response element (-2441/-2345) within the Kcnk1 promoter.


These results indicate that << phenobarbital >> treatment induces [[ KCNK1 ]] to elicit a male-specific and growth-suppressing signal.


<< Methylphenidate >>, an inhibitor of [[ dopamine and norepinephrine transporters ]] (DAT and NET, respectively), is a standard treatment for ADHD.


<< Methylphenidate >>, an inhibitor of dopamine and norepinephrine transporters ([[ DAT ]] and NET, respectively), is a standard treatment for ADHD.


<< Methylphenidate >>, an inhibitor of dopamine and norepinephrine transporters (DAT and [[ NET ]], respectively), is a standard treatment for ADHD.


<< Methylphenidate >> increased [[ DAT ]] Vmax in SHR mPFC and decreased DAT Vmax in WKY OFC.


<< Methylphenidate >> increased DAT Vmax in SHR mPFC and decreased [[ DAT ]] Vmax in WKY OFC.


Also, << methylphenidate >> decreased [[ DAT ]] Km in WIS OFC.


Thus, the increase in mPFC << DAT >> function was an SHR-specific long term consequence of [[ methylphenidate ]] treatment during adolescence, which may be responsible for the treatment-induced alterations in behavior including the observed increases in cocaine self-administration.


OBJECTIVE: To evaluate the extent of human cyclooxygenase-1 (COX-1) inhibition by << meloxicam >>, which has been reported to preferentially inhibit [[ cyclooxygenase-2 ]] (COX-2).


OBJECTIVE: To evaluate the extent of human cyclooxygenase-1 (COX-1) inhibition by << meloxicam >>, which has been reported to preferentially inhibit cyclooxygenase-2 ([[ COX-2 ]]).


OBJECTIVE: To evaluate the extent of << human cyclooxygenase-1 >> (COX-1) inhibition by [[ meloxicam ]], which has been reported to preferentially inhibit cyclooxygenase-2 (COX-2).


OBJECTIVE: To evaluate the extent of human cyclooxygenase-1 (<< COX-1 >>) inhibition by [[ meloxicam ]], which has been reported to preferentially inhibit cyclooxygenase-2 (COX-2).


The effects of << meloxicam >> were compared with those of diclofenac, a nonselective [[ COX ]] inhibitor.


The effects of meloxicam were compared with those of << diclofenac >>, a nonselective [[ COX ]] inhibitor.


METHODS: << COX-1 >> inhibition was determined by measuring thromboxane B2 (TXB2)-generation from clotting whole blood ex vivo after single oral doses of 7.5 and 15 mg [[ meloxicam ]] and 75 mg diclofenac and at steady state (15 mg meloxicam daily and 150 mg diclofenac daily).


METHODS: << COX-1 >> inhibition was determined by measuring thromboxane B2 (TXB2)-generation from clotting whole blood ex vivo after single oral doses of 7.5 and 15 mg meloxicam and 75 mg [[ diclofenac ]] and at steady state (15 mg meloxicam daily and 150 mg diclofenac daily).


METHODS: << COX-1 >> inhibition was determined by measuring thromboxane B2 (TXB2)-generation from clotting whole blood ex vivo after single oral doses of 7.5 and 15 mg meloxicam and 75 mg diclofenac and at steady state (15 mg [[ meloxicam ]] daily and 150 mg diclofenac daily).


METHODS: << COX-1 >> inhibition was determined by measuring thromboxane B2 (TXB2)-generation from clotting whole blood ex vivo after single oral doses of 7.5 and 15 mg meloxicam and 75 mg diclofenac and at steady state (15 mg meloxicam daily and 150 mg [[ diclofenac ]] daily).


Thus our data suggest that the << COX-2 >> preference of [[ meloxicam ]] observed in vitro may not result in clinical advantages when the higher dose of 15 mg is needed.


Inhibition of angiogenesis and invasion by << DMBT >> is mediated by downregulation of [[ VEGF ]] and MMP-9 through Akt pathway in MDA-MB-231 breast cancer cells.


Inhibition of angiogenesis and invasion by << DMBT >> is mediated by downregulation of VEGF and [[ MMP-9 ]] through Akt pathway in MDA-MB-231 breast cancer cells.


Inhibition of angiogenesis and invasion by << DMBT >> is mediated by downregulation of VEGF and MMP-9 through [[ Akt ]] pathway in MDA-MB-231 breast cancer cells.


Gelatin zymography showed that << DMBT >> inhibited secretion and activity of [[ MMP-9 ]].


Western blotting demonstrated that << DMBT >> effectively suppressed the expression of [[ VEGF ]], p-VEGFR-2, p-EGFR, and p-Akt.


Western blotting demonstrated that << DMBT >> effectively suppressed the expression of VEGF, [[ p-VEGFR-2 ]], p-EGFR, and p-Akt.


Western blotting demonstrated that << DMBT >> effectively suppressed the expression of VEGF, p-VEGFR-2, [[ p-EGFR ]], and p-Akt.


Western blotting demonstrated that << DMBT >> effectively suppressed the expression of VEGF, p-VEGFR-2, p-EGFR, and [[ p-Akt ]].


These results suggested that << DMBT >> could inhibit invasion and angiogenesis by downregulation of [[ VEGF ]]and MMP-9, resulting from the inhibition of Akt pathway.


These results suggested that << DMBT >> could inhibit invasion and angiogenesis by downregulation of VEGFand [[ MMP-9 ]], resulting from the inhibition of Akt pathway.


These results suggested that << DMBT >> could inhibit invasion and angiogenesis by downregulation of VEGFand MMP-9, resulting from the inhibition of [[ Akt ]] pathway.


Expression of L-type pyruvate kinase (<< L-PK >>) is upregulated in the liver by dietary [[ carbohydrate ]].


Expression of << L-type pyruvate kinase >> (L-PK) is upregulated in the liver by dietary [[ carbohydrate ]].


<< Felbamate >> block of recombinant [[ N-methyl-D-aspartate receptors ]]: selectivity for the NR2B subunit.


<< Felbamate >> block of recombinant N-methyl-D-aspartate receptors: selectivity for the [[ NR2B ]] subunit.


The anticonvulsant << felbamate >> blocks [[ N-methyl-D-asparate (NMDA) receptors ]] but fails to exhibit the neurobehavioral toxicity characteristic of other NMDA receptor antagonists.


The anticonvulsant << felbamate >> blocks N-methyl-D-asparate (NMDA) receptors but fails to exhibit the neurobehavioral toxicity characteristic of other [[ NMDA receptor ]] antagonists.


To investigate the possibility that felbamate's favorable toxicity profile could be related to NMDA receptor subtype selectivity, we examined the specificity of << felbamate >> block of recombinant [[ NMDA receptors ]] composed of the NR1a subunit and various NR2 subunits.


To investigate the possibility that felbamate's favorable toxicity profile could be related to NMDA receptor subtype selectivity, we examined the specificity of << felbamate >> block of recombinant NMDA receptors composed of the [[ NR1a ]] subunit and various NR2 subunits.


To investigate the possibility that felbamate's favorable toxicity profile could be related to NMDA receptor subtype selectivity, we examined the specificity of << felbamate >> block of recombinant NMDA receptors composed of the NR1a subunit and various [[ NR2 ]] subunits.


<< Felbamate >> produced a rapid, concentration-dependent block of currents evoked by 50 microM NMDA and 10 microM glycine in human embryonic kidney 293 cells expressing the [[ rat NR1a ]] subunit, and either the NR2A, NR2B or NR2C subunits; the IC50 values for block were 2.6, 0.52 and 2.4 mM, respectively (holding potential, - 60 mV).


<< Felbamate >> produced a rapid, concentration-dependent block of currents evoked by 50 microM NMDA and 10 microM glycine in human embryonic kidney 293 cells expressing the rat NR1a subunit, and either the [[ NR2A ]], NR2B or NR2C subunits; the IC50 values for block were 2.6, 0.52 and 2.4 mM, respectively (holding potential, - 60 mV).


<< Felbamate >> produced a rapid, concentration-dependent block of currents evoked by 50 microM NMDA and 10 microM glycine in human embryonic kidney 293 cells expressing the rat NR1a subunit, and either the NR2A, [[ NR2B ]] or NR2C subunits; the IC50 values for block were 2.6, 0.52 and 2.4 mM, respectively (holding potential, - 60 mV).


<< Felbamate >> produced a rapid, concentration-dependent block of currents evoked by 50 microM NMDA and 10 microM glycine in human embryonic kidney 293 cells expressing the rat NR1a subunit, and either the NR2A, NR2B or [[ NR2C ]] subunits; the IC50 values for block were 2.6, 0.52 and 2.4 mM, respectively (holding potential, - 60 mV).


The higher affinity of << felbamate >> block of [[ NMDA receptors ]] containing the NR2B subunit could be accounted for by more rapid association and slower dissociation from these sites.


The higher affinity of << felbamate >> block of NMDA receptors containing the [[ NR2B ]] subunit could be accounted for by more rapid association and slower dissociation from these sites.


We conclude that << felbamate >> exhibits modest selectivity for [[ NMDA receptors ]] composed of NR1a/NR2B subunits.


We conclude that << felbamate >> exhibits modest selectivity for NMDA receptors composed of [[ NR1a ]]/NR2B subunits.


We conclude that << felbamate >> exhibits modest selectivity for NMDA receptors composed of NR1a/[[ NR2B ]] subunits.


This selectivity could, in part, account for the more favorable clinical profile of << felbamate >> in comparison with [[ NMDA receptor ]] antagonists that do not show subunit selectivity.


In four (10 %) patients the peak << ACTH >>-stimulated [[ cortisol ]] values were lower than 18 μg/dL.


<< ACTH >>-stimulated peak [[ cortisol ]], delta cortisol, and delta DHEA-S levels are decreased during hyperthyroidism, probably due to increased turnover.


<< ACTH >>-stimulated peak cortisol, [[ delta cortisol ]], and delta DHEA-S levels are decreased during hyperthyroidism, probably due to increased turnover.


<< ACTH >>-stimulated peak cortisol, delta cortisol, and [[ delta DHEA ]]-S levels are decreased during hyperthyroidism, probably due to increased turnover.


Previously, we showed that the << human kappa-opioid receptor >> (hkor) stably expressed in Chinese hamster ovary (CHO) cells underwent down-regulation after prolonged [[ U50,488H ]] treatment.


Previously, we showed that the human kappa-opioid receptor (<< hkor >>) stably expressed in Chinese hamster ovary (CHO) cells underwent down-regulation after prolonged [[ U50,488H ]] treatment.


<< U50, 488H >> caused a significant down-regulation of the [[ hkor ]], although etorphine did not.


Expression of the dominant negative mutants arrestin-2(319-418) or dynamin I-K44A significantly reduced << U50,488H >>-induced down-regulation of the [[ hkor ]].


Coexpression of GRK2 or GRK2 and arrestin-2 permitted << etorphine >> to induce down-regulation of the [[ hkor ]], although expression of arrestin-2 or dynamin I alone did not.


Expression of the dominant negative mutants << rab5A >>-N133I or rab7-N125I blunted [[ U50,488H ]]-induced down-regulation.


Expression of the dominant negative mutants rab5A-<< N133I >> or rab7-N125I blunted [[ U50,488H ]]-induced down-regulation.


Expression of the dominant negative mutants rab5A-N133I or << rab7 >>-N125I blunted [[ U50,488H ]]-induced down-regulation.


Expression of the dominant negative mutants rab5A-N133I or rab7-<< N125I >> blunted [[ U50,488H ]]-induced down-regulation.


Pretreatment with lysosomal enzyme inhibitors [(2S, 3S)trans-epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester or chloroquine] or proteasome inhibitors (<< proteasome >> inhibitor I, [[ MG-132 ]], or lactacystin) decreased the extent of U50,488H-induced down-regulation.


Pretreatment with lysosomal enzyme inhibitors [(2S, 3S)trans-epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester or chloroquine] or proteasome inhibitors (<< proteasome >> inhibitor I, MG-132, or [[ lactacystin ]]) decreased the extent of U50,488H-induced down-regulation.


These results indicate that << U50,488H >>-induced down-regulation of the [[ hkor ]] involves GRK-, arrestin-2-, dynamin-, rab5-, and rab7-dependent mechanisms and receptors seem to be trafficked to lysosomes and proteasomes for degradation.


Thus, << U50,488H >>-induced internalization and down-regulation of the [[ hkor ]] share initial common mechanisms.


In Alexander cells, only when they were transfected with FXR+RXR, << GW4064 >> caused up-regulation of [[ SHP ]] and OSTβ, and a down-regulation of CYP27A1.


In Alexander cells, only when they were transfected with FXR+RXR, << GW4064 >> caused up-regulation of SHP and [[ OSTβ ]], and a down-regulation of CYP27A1.


In Alexander cells, only when they were transfected with FXR+RXR, << GW4064 >> caused up-regulation of SHP and OSTβ, and a down-regulation of [[ CYP27A1 ]].


Moreover, GCs have a synergistic effect on << GW4064 >>-induced [[ FXR ]] activation, whereas chenodeoxycholate and GW4064 have an additive effect.


Kinetic parameters for << PAM >> inactivation by [[ 4-oxo-5-acetamido-6-phenyl-hex-2-enoic acid and 4-oxo-5-acetamido-6-(2-thienyl)-hex-2-enoic acid ]] were obtained by using both the conventional dilution assay method and the more complex progress curve method.


Stereochemical studies established that << PAM >> inactivation by [[ 4-oxo-5-acetamido-6-(2-thienyl)-hex-2-enoic acid ]] is stereospecific with respect to the moiety at the P(2) position, which is consistent with previous results with substrates and reversible inhibitors.


In contrast, << 2, 4-dioxo-5-acetamido-6-phenylhexanoic acid >>, which is a competitive inhibitor with respect to ascorbate, exhibits a low degree of stereospecificity in binding to the ascorbate sites of both [[ PAM ]] and dopamine-beta-hydroxylase.


In contrast, << 2, 4-dioxo-5-acetamido-6-phenylhexanoic acid >>, which is a competitive inhibitor with respect to ascorbate, exhibits a low degree of stereospecificity in binding to the ascorbate sites of both PAM and [[ dopamine-beta-hydroxylase ]].


Five classes of chalcogenopyrylium dyes (CGPs) were examined for their ability to modulate transport of << [(3)H]estradiol glucuronide >> (E217βG) (a prototypical [[ MRP ]] substrate) into MRP-enriched inside-out membrane vesicles.


Five classes of chalcogenopyrylium dyes (CGPs) were examined for their ability to modulate transport of [(3)H]estradiol glucuronide (<< E217βG >>) (a prototypical [[ MRP ]] substrate) into MRP-enriched inside-out membrane vesicles.


Sixteen of 34 << CGPs >> inhibited [[ MRP1 ]]-mediated E217βG uptake by >50% (IC50's 0.7-7.6 μM).


Sixteen of 34 CGPs inhibited << MRP1 >>-mediated [[ E217βG ]] uptake by >50% (IC50's 0.7-7.6 μM).


When tested in the intact cells, only 4 of 16 << CGPs >> (at 10 μM) inhibited [[ MRP1 ]]-mediated calcein efflux by >50% (III-1, V-3, -4, -6) while a fifth (I-5) inhibited efflux by just 23%.


When tested in the intact cells, only 4 of 16 CGPs (at 10 μM) inhibited << MRP1 >>-mediated [[ calcein ]] efflux by >50% (III-1, V-3, -4, -6) while a fifth (I-5) inhibited efflux by just 23%.


These five << CGPs >> also inhibited [(3)H]E217βG uptake by [[ MRP4 ]].


These five CGPs also inhibited << [(3)H]E217βG >> uptake by [[ MRP4 ]].


<< Gemfibrozil >>, a lipid-lowering drug, inhibits the induction of [[ nitric-oxide synthase ]] in human astrocytes.


Gemfibrozil, a lipid-lowering drug, inhibits the induction of << nitric-oxide synthase >>[[ nitric-oxide ]] synthase in human astrocytes.


<< Gemfibrozil >>, a lipid-lowering drug, inhibited cytokine-induced production of NO and the expression of [[ inducible nitric-oxide synthase ]] (iNOS) in human U373MG astroglial cells and primary astrocytes.


<< Gemfibrozil >>, a lipid-lowering drug, inhibited cytokine-induced production of NO and the expression of inducible nitric-oxide synthase ([[ iNOS ]]) in human U373MG astroglial cells and primary astrocytes.


<< Gemfibrozil >>, a lipid-lowering drug, inhibited [[ cytokine ]]-induced production of NO and the expression of inducible nitric-oxide synthase (iNOS) in human U373MG astroglial cells and primary astrocytes.


Gemfibrozil, a lipid-lowering drug, inhibited cytokine-induced production of << NO >> and the expression of [[ inducible nitric-oxide synthase ]] (iNOS) in human U373MG astroglial cells and primary astrocytes.


Gemfibrozil, a lipid-lowering drug, inhibited cytokine-induced production of << NO >> and the expression of inducible nitric-oxide synthase ([[ iNOS ]]) in human U373MG astroglial cells and primary astrocytes.


Gemfibrozil, a lipid-lowering drug, inhibited cytokine-induced production of NO and the expression of << inducible nitric-oxide synthase >>[[ nitric-oxide ]] synthase (iNOS) in human U373MG astroglial cells and primary astrocytes.


Gemfibrozil, a lipid-lowering drug, inhibited cytokine-induced production of NO and the expression of inducible << nitric-oxide >> synthase ([[ iNOS ]]) in human U373MG astroglial cells and primary astrocytes.


Similar to << gemfibrozil >>, clofibrate, another fibrate drug, also inhibited the expression of [[ iNOS ]].


Similar to gemfibrozil, << clofibrate >>, another fibrate drug, also inhibited the expression of [[ iNOS ]].


Similar to gemfibrozil, clofibrate, another << fibrate >> drug, also inhibited the expression of [[ iNOS ]].


Inhibition of human iNOS promoter-driven luciferase activity by << gemfibrozil >> in cytokine-stimulated U373MG astroglial cells suggests that this compound inhibits the transcription of [[ iNOS ]].


Inhibition of << human iNOS promoter >>-driven luciferase activity by [[ gemfibrozil ]] in cytokine-stimulated U373MG astroglial cells suggests that this compound inhibits the transcription of iNOS.


Since << gemfibrozil >> is known to activate [[ peroxisome proliferator-activated receptor-alpha ]] (PPAR-alpha), we investigated the role of PPAR-alpha in gemfibrozil-mediated inhibition of iNOS.


Since << gemfibrozil >> is known to activate peroxisome proliferator-activated receptor-alpha ([[ PPAR-alpha ]]), we investigated the role of PPAR-alpha in gemfibrozil-mediated inhibition of iNOS.


Since gemfibrozil is known to activate peroxisome proliferator-activated receptor-alpha (PPAR-alpha), we investigated the role of << PPAR-alpha >> in [[ gemfibrozil ]]-mediated inhibition of iNOS.


Since gemfibrozil is known to activate peroxisome proliferator-activated receptor-alpha (PPAR-alpha), we investigated the role of PPAR-alpha in << gemfibrozil >>-mediated inhibition of [[ iNOS ]].


<< Gemfibrozil >> induced [[ peroxisome proliferator-responsive element ]] (PPRE)-dependent luciferase activity, which was inhibited by the expression of DeltahPPAR-alpha, the dominant-negative mutant of human PPAR-alpha.


<< Gemfibrozil >> induced peroxisome proliferator-responsive element ([[ PPRE ]])-dependent luciferase activity, which was inhibited by the expression of DeltahPPAR-alpha, the dominant-negative mutant of human PPAR-alpha.


However, DeltahPPAR-alpha was unable to abrogate << gemfibrozil >>-mediated inhibition of [[ iNOS ]] suggesting that gemfibrozil inhibits iNOS independent of PPAR-alpha.


However, DeltahPPAR-alpha was unable to abrogate gemfibrozil-mediated inhibition of iNOS suggesting that << gemfibrozil >> inhibits [[ iNOS ]] independent of PPAR-alpha.


Interestingly, << gemfibrozil >> strongly inhibited the activation of [[ NF-kappaB ]], AP-1, and C/EBPbeta but not that of GAS in cytokine-stimulated astroglial cells.


Interestingly, << gemfibrozil >> strongly inhibited the activation of NF-kappaB, [[ AP-1 ]], and C/EBPbeta but not that of GAS in cytokine-stimulated astroglial cells.


Interestingly, << gemfibrozil >> strongly inhibited the activation of NF-kappaB, AP-1, and [[ C/EBPbeta ]] but not that of GAS in cytokine-stimulated astroglial cells.


These results suggest that << gemfibrozil >> inhibits the induction of [[ iNOS ]] probably by inhibiting the activation of NF-kappaB, AP-1, and C/EBPbeta and that gemfibrozil, a prescribed drug for humans, may further find its therapeutic use in neuroinflammatory diseases.


These results suggest that << gemfibrozil >> inhibits the induction of iNOS probably by inhibiting the activation of [[ NF-kappaB ]], AP-1, and C/EBPbeta and that gemfibrozil, a prescribed drug for humans, may further find its therapeutic use in neuroinflammatory diseases.


These results suggest that << gemfibrozil >> inhibits the induction of iNOS probably by inhibiting the activation of NF-kappaB, [[ AP-1 ]], and C/EBPbeta and that gemfibrozil, a prescribed drug for humans, may further find its therapeutic use in neuroinflammatory diseases.


These results suggest that << gemfibrozil >> inhibits the induction of iNOS probably by inhibiting the activation of NF-kappaB, AP-1, and [[ C/EBPbeta ]] and that gemfibrozil, a prescribed drug for humans, may further find its therapeutic use in neuroinflammatory diseases.


OBJECTIVES: The aim of this study was to determine whether cocaine's sympathomimetic actions can be reversed by a potent centrally acting << alpha2 adrenergic receptor >> (AR) agonist ([[ dexmedetomidine ]]).


OBJECTIVES: The aim of this study was to determine whether cocaine's sympathomimetic actions can be reversed by a potent centrally acting alpha2 adrenergic receptor (<< AR >>) agonist ([[ dexmedetomidine ]]).


The inhibitory effect of << sodium nitroprusside >> on [[ HIF-1 ]] activation is not dependent on nitric oxide-soluble guanylyl cyclase pathway.


We demonstrate that among the three nitrates, only << SNP >> inhibits [[ HIF-1 ]] activation in response to hypoxia.


<< SNP >> inhibits the accumulation of HIF-1alpha, the regulatory subunit of HIF-1, and the transcriptional activation of [[ HIF-1alpha ]] via a mechanism that is not dependent on either NO or soluble guanylate cyclase.


<< SNP >> inhibits the accumulation of [[ HIF-1alpha ]], the regulatory subunit of HIF-1, and the transcriptional activation of HIF-1alpha via a mechanism that is not dependent on either NO or soluble guanylate cyclase.


<< SNP >> inhibits the accumulation of HIF-1alpha, the regulatory subunit of [[ HIF-1 ]], and the transcriptional activation of HIF-1alpha via a mechanism that is not dependent on either NO or soluble guanylate cyclase.


<< Indomethacin >> activates [[ carbonic anhydrase ]] and antagonizes the effect of the specific carbonic anhydrase inhibitor acetazolamide, by a direct mechanism of action.


<< Indomethacin >> activates carbonic anhydrase and antagonizes the effect of the specific [[ carbonic anhydrase ]] inhibitor acetazolamide, by a direct mechanism of action.


Indomethacin activates << carbonic anhydrase >> and antagonizes the effect of the specific carbonic anhydrase inhibitor [[ acetazolamide ]], by a direct mechanism of action.


Indomethacin activates carbonic anhydrase and antagonizes the effect of the specific << carbonic anhydrase >> inhibitor [[ acetazolamide ]], by a direct mechanism of action.


RESULTS: << Indomethacin >>, in vitro and in vivo. induces an increase in erythorcyte [[ CA I ]] and CA II activity.


RESULTS: << Indomethacin >>, in vitro and in vivo. induces an increase in erythorcyte CA I and [[ CA II ]] activity.


<< Acetazolamide >>, a specific inhibitor of [[ CA ]], reduces the activity of CA I and CA II from red cells.


<< Acetazolamide >>, a specific inhibitor of CA, reduces the activity of [[ CA I ]] and CA II from red cells.


<< Acetazolamide >>, a specific inhibitor of CA, reduces the activity of CA I and [[ CA II ]] from red cells.


<< Indomethacin >> completely antagonizes [[ CA ]] activity, i.e. abolishes the inhibitory effect of acetazolamide on CA.


<< Indomethacin >> completely antagonizes CA activity, i.e. abolishes the inhibitory effect of acetazolamide on [[ CA ]].


Indomethacin completely antagonizes << CA >> activity, i.e. abolishes the inhibitory effect of [[ acetazolamide ]] on CA.


Indomethacin completely antagonizes CA activity, i.e. abolishes the inhibitory effect of << acetazolamide >> on [[ CA ]].


CONCLUSIONS: Our results show that << indomethacin >>, a known cyclooxygenase (COX) inhibitor, is also an activator of [[ CA ]].


CONCLUSIONS: Our results show that << indomethacin >>, a known [[ cyclooxygenase ]] (COX) inhibitor, is also an activator of CA.


CONCLUSIONS: Our results show that << indomethacin >>, a known cyclooxygenase ([[ COX ]]) inhibitor, is also an activator of CA.


Our data also prove that << indomethacin >> is not only an activator of [[ CA ]] but also antagonizes the effect of acetazolamide, a specific inhibitor of this enzyme.


Our data also prove that indomethacin is not only an activator of << CA >> but also antagonizes the effect of [[ acetazolamide ]], a specific inhibitor of this enzyme.


In view of the role of CA in acid-base balance as well as the fact that an increase or decrease in its activity is accompanied by an increase or decrease in intra- and extracellular pH, our results suggest that: firstly, << CA >> activation induced by [[ indomethacin ]] might cause changes in COX activity; secondly, PGs are synthetized as a consequence of the changes in COX activity, a hypothesis that requires further study.


The acetylcholinesterase (<< AChE >>) and butyrylcholinesterase (BuChE) inhibitory activities of a series of [[ pyrano[2,3-b]quinolines ]] (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and << butyrylcholinesterase >> (BuChE) inhibitory activities of a series of [[ pyrano[2,3-b]quinolines ]] (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The << acetylcholinesterase >> (AChE) and butyrylcholinesterase (BuChE) inhibitory activities of a series of [[ pyrano[2,3-b]quinolines ]] (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and butyrylcholinesterase (<< BuChE >>) inhibitory activities of a series of [[ pyrano[2,3-b]quinolines ]] (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (<< AChE >>) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [[ [1,8]naphthyridines ]] (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and << butyrylcholinesterase >> (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [[ [1,8]naphthyridines ]] (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The << acetylcholinesterase >> (AChE) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [[ [1,8]naphthyridines ]] (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and butyrylcholinesterase (<< BuChE >>) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [[ [1,8]naphthyridines ]] (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (<< AChE >>) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), [[ 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines ]] (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and << butyrylcholinesterase >> (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), [[ 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines ]] (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The << acetylcholinesterase >> (AChE) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), [[ 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines ]] (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and butyrylcholinesterase (<< BuChE >>) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), [[ 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines ]] (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (<< AChE >>) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ [[ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine ]] (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and << butyrylcholinesterase >> (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ [[ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine ]] (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The << acetylcholinesterase >> (AChE) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ [[ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine ]] (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and butyrylcholinesterase (<< BuChE >>) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ [[ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine ]] (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (<< AChE >>) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), [[ 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline ]] (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and << butyrylcholinesterase >> (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), [[ 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline ]] (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The << acetylcholinesterase >> (AChE) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), [[ 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline ]] (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (AChE) and butyrylcholinesterase (<< BuChE >>) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), [[ 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline ]] (15)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine (16) are described.


The acetylcholinesterase (<< AChE >>) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ [[ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine ]] (16) are described.


The acetylcholinesterase (AChE) and << butyrylcholinesterase >> (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ [[ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine ]] (16) are described.


The << acetylcholinesterase >> (AChE) and butyrylcholinesterase (BuChE) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ [[ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine ]] (16) are described.


The acetylcholinesterase (AChE) and butyrylcholinesterase (<< BuChE >>) inhibitory activities of a series of pyrano[2,3-b]quinolines (2, 3), [1,8]naphthyridines (5, 6), 4-amino-2,3-diaryl-5,6,7,8-tetrahydrofuro[2,3-b]quinolines (11-13)/ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]furo[2,3-b]pyridine (14), 4-amino-5,6,7,8-tetrahydro-2,3-diphenylthieno[2,3-b]quinoline (15)/ [[ 4-amino-6,7,8,9-tetrahydro-2,3-diphenyl-5H-cyclohepta[e]thieno[2,3-b]pyridine ]] (16) are described.


These compounds are competitive and, in a few cases, non-competitive inhibitors for << AChE >>, the most potent being compound (14), though three-fold less active than [[ tacrine ]].


The << BuChE >> inhibitory activity is only significant in compounds 11 and 14, ten-fold less active than [[ tacrine ]].


<< Juglone >>, isolated from Juglans mandshurica Maxim, induces apoptosis via down-regulation of [[ AR ]] expression in human prostate cancer LNCaP cells.


Moreover, we found that << juglone >> significantly inhibited the expression levels of [[ androgen receptor ]] (AR) and prostate-specific antigen (PSA) in a dose-dependent manner, as well as abrogated up-regulation of AR and PSA genes with and/or without dihydrotestosterone (DHT).


Moreover, we found that << juglone >> significantly inhibited the expression levels of androgen receptor ([[ AR ]]) and prostate-specific antigen (PSA) in a dose-dependent manner, as well as abrogated up-regulation of AR and PSA genes with and/or without dihydrotestosterone (DHT).


Moreover, we found that << juglone >> significantly inhibited the expression levels of androgen receptor (AR) and [[ prostate-specific antigen ]] (PSA) in a dose-dependent manner, as well as abrogated up-regulation of AR and PSA genes with and/or without dihydrotestosterone (DHT).


Moreover, we found that << juglone >> significantly inhibited the expression levels of androgen receptor (AR) and prostate-specific antigen ([[ PSA ]]) in a dose-dependent manner, as well as abrogated up-regulation of AR and PSA genes with and/or without dihydrotestosterone (DHT).


Moreover, we found that << juglone >> significantly inhibited the expression levels of androgen receptor (AR) and prostate-specific antigen (PSA) in a dose-dependent manner, as well as abrogated up-regulation of [[ AR ]] and PSA genes with and/or without dihydrotestosterone (DHT).


Moreover, we found that << juglone >> significantly inhibited the expression levels of androgen receptor (AR) and prostate-specific antigen (PSA) in a dose-dependent manner, as well as abrogated up-regulation of AR and [[ PSA ]] genes with and/or without dihydrotestosterone (DHT).


Take together, our results demonstrated that << juglone >> might induce the apoptosis in LNCaP cell via down-regulation of [[ AR ]] expression.


<< Astemizole >>, a potent [[ histamine H1-receptor ]] antagonist: effect in allergic rhinoconjunctivitis, on antigen and histamine induced skin weal responses and relationship to serum levels.


The efficacy of << astemizole >>, a new, long acting, oral [[ histamine H1-receptor ]] antagonist was compared to placebo for the treatment of allergic rhinitis and conjunctivitis during the grass pollen season of 1982.


<< Tacrine >>, the first of the [[ cholinesterase ]] inhibitors to undergo extensive trials for this purpose, was associated with significant adverse effects including hepatotoxicity.


Other << cholinesterase >> inhibitors, including [[ rivastigmine ]], with superior properties in terms of specificity of action and low risk of adverse effects, have now been introduced.


<< 5-(N,N-dimethyl)-amiloride >> (50 microM; DMA), a concentration that selectively inhibits the [[ NHE ]] isoforms NHE1 and NHE2, but not NHE3, did not affect DBS.


<< 5-(N,N-dimethyl)-amiloride >> (50 microM; DMA), a concentration that selectively inhibits the NHE isoforms [[ NHE1 ]] and NHE2, but not NHE3, did not affect DBS.


<< 5-(N,N-dimethyl)-amiloride >> (50 microM; DMA), a concentration that selectively inhibits the NHE isoforms NHE1 and [[ NHE2 ]], but not NHE3, did not affect DBS.


<< 5-(N,N-dimethyl)-amiloride >> (50 microM; DMA), a concentration that selectively inhibits the NHE isoforms NHE1 and NHE2, but not [[ NHE3 ]], did not affect DBS.


5-(N,N-dimethyl)-amiloride (50 microM; << DMA >>), a concentration that selectively inhibits the [[ NHE ]] isoforms NHE1 and NHE2, but not NHE3, did not affect DBS.


5-(N,N-dimethyl)-amiloride (50 microM; << DMA >>), a concentration that selectively inhibits the NHE isoforms [[ NHE1 ]] and NHE2, but not NHE3, did not affect DBS.


5-(N,N-dimethyl)-amiloride (50 microM; << DMA >>), a concentration that selectively inhibits the NHE isoforms NHE1 and [[ NHE2 ]], but not NHE3, did not affect DBS.


5-(N,N-dimethyl)-amiloride (50 microM; << DMA >>), a concentration that selectively inhibits the NHE isoforms NHE1 and NHE2, but not [[ NHE3 ]], did not affect DBS.


Nevertheless, 3 mM << DMA >>, a higher concentration that inhibits [[ NHE1 ]], NHE2, and NHE3, significantly increased DBS.


Nevertheless, 3 mM << DMA >>, a higher concentration that inhibits NHE1, [[ NHE2 ]], and NHE3, significantly increased DBS.


Nevertheless, 3 mM << DMA >>, a higher concentration that inhibits NHE1, NHE2, and [[ NHE3 ]], significantly increased DBS.


Moreover, << S1611 >> and S3226, both specific inhibitors of [[ NHE3 ]] only, or perfusion with Na+-free solutions, dose dependently increased DBS, as measured by pH-stat and CO2-sensitive electrode, without affecting intracellular pH.


Moreover, S1611 and << S3226 >>, both specific inhibitors of [[ NHE3 ]] only, or perfusion with Na+-free solutions, dose dependently increased DBS, as measured by pH-stat and CO2-sensitive electrode, without affecting intracellular pH.


Nevertheless, coperfusion with 0.1 and 0.3 mM << 5-nitro-2-(3-phenylpropylamino) benzoic acid >>, which inhibits the [[ cystic fibrosis transmembrane conductor regulator ]] (CFTR), dose dependently inhibited S3226-induced DBS.


Nevertheless, coperfusion with 0.1 and 0.3 mM << 5-nitro-2-(3-phenylpropylamino) benzoic acid >>, which inhibits the cystic fibrosis transmembrane conductor regulator ([[ CFTR ]]), dose dependently inhibited S3226-induced DBS.


In conclusion, only specific apical NHE3 inhibition increased DBS, whereas prostaglandin synthesis, Na+-HCO3- cotransporter activation, or intracellular << HCO3 >>- formation by [[ carbonic anhydrase ]] was not involved.


Mechanisms limiting distribution of the << threonine-protein kinase B-RaF >>(V600E) inhibitor [[ dabrafenib ]] to the brain: implications for the treatment of melanoma brain metastases.


Mechanisms limiting distribution of the threonine-protein kinase B-RaF(<< V600E >>) inhibitor [[ dabrafenib ]] to the brain: implications for the treatment of melanoma brain metastases.


In vitro accumulation studies conducted in Madin-Darby canine kidney II cells indicate that << dabrafenib >> is an avid substrate for both [[ P-gp ]] and BCRP.


In vitro accumulation studies conducted in Madin-Darby canine kidney II cells indicate that << dabrafenib >> is an avid substrate for both P-gp and [[ BCRP ]].


Further, compared with << vemurafenib >>, another [[ BRAF ]](V600E) inhibitor, dabrafenib showed greater brain penetration with a similar dose.


Further, compared with << vemurafenib >>, another BRAF([[ V600E ]]) inhibitor, dabrafenib showed greater brain penetration with a similar dose.


Since the original discovery of << azoles >> analogs as [[ PXR ]] antagonists, we have preliminarily defined an important PXR antagonist pharmacophore and developed less-toxic PXR antagonists.


Since the original discovery of << azoles >> analogs as PXR antagonists, we have preliminarily defined an important [[ PXR ]] antagonist pharmacophore and developed less-toxic PXR antagonists.


Since the original discovery of << azoles >> analogs as PXR antagonists, we have preliminarily defined an important PXR antagonist pharmacophore and developed less-toxic [[ PXR ]] antagonists.


Activation of endogenous << somatostatin receptor subtype 2 >> (sst2) by [[ somatostatin-14 ]] or activation of transiently transfected rat D2 dopamine receptors (rD2(long)) by quinpirole had no effect.


Activation of endogenous somatostatin receptor subtype 2 (<< sst2 >>) by [[ somatostatin-14 ]] or activation of transiently transfected rat D2 dopamine receptors (rD2(long)) by quinpirole had no effect.


Activation of endogenous somatostatin receptor subtype 2 (sst2) by somatostatin-14 or activation of transiently transfected << rat D2 dopamine receptors >> (rD2(long)) by [[ quinpirole ]] had no effect.


Activation of endogenous somatostatin receptor subtype 2 (sst2) by somatostatin-14 or activation of transiently transfected rat D2 dopamine receptors (<< rD2 >>(long)) by [[ quinpirole ]] had no effect.


In contrast, in the same system, << N >>-type currents, formed from transiently transfected alpha(1B)/alpha(2)delta-1/beta(3), showed strong [[ G-protein ]]-mediated inhibition.


Levels of << Cx43 >> protein were also decreased in a dose- and time-dependent manner following [[ antofine ]] treatment.


Co-treatment of astrocytes with antofine and the intracellular Ca(2+) chelator << BAPTA-AM >> prevented downregulation of [[ Cx43 ]] and inhibition of GJIC.


Co-treatment of astrocytes with << antofine >> and the intracellular Ca(2+) chelator BAPTA-AM prevented downregulation of [[ Cx43 ]] and inhibition of GJIC.


Moreover, co-treatment with << antofine >> and a specific PKCβ inhibitor prevented endocytosis of gap junctions, downregulation of [[ Cx43 ]], and inhibition of GJIC.


Taken together, these findings indicate that << antofine >> induces Cx43 gap junction disassembly by the [[ PKCβ ]] signaling pathway.


<< Torasemide >> inhibits [[ angiotensin II ]]-induced vasoconstriction and intracellular calcium increase in the aorta of spontaneously hypertensive rats.


Isometric contraction induced by a submaximal concentration of << Ang II >> (10(-7) mol/L) was reduced in a dose-dependent way by [[ torasemide ]] (IC(50)=0.5+/-0.04 micromol/L).


The stimulatory effect of [Ca(2+)](i) induced by a submaximal concentration of << Ang II >> (10(-7) mol/L) was blocked by [[ torasemide ]] (IC(50)=0.5+/-0.3 nmol/L).


Our findings suggest that << torasemide >> blocks the vasoconstrictor action of [[ Ang II ]] in vitro.


This action can be related to the ability of << torasemide >> to block the increase of [Ca(2+)](i) induced by [[ Ang II ]] in VSMCs.


Among the isolated compounds, << trans-dihydromorin >> (8), oxyresveratrol (9), and steppogenin (12) were found to exhibit significant [[ tyrosinase ]] inhibition activities.


Among the isolated compounds, trans-dihydromorin (8), << oxyresveratrol >> (9), and steppogenin (12) were found to exhibit significant [[ tyrosinase ]] inhibition activities.


Among the isolated compounds, trans-dihydromorin (8), oxyresveratrol (9), and << steppogenin >> (12) were found to exhibit significant [[ tyrosinase ]] inhibition activities.


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), << 17-phenyl-trinor-PGE2 >> (an EP1-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit [[ HVA Ca2+ channels ]] was sulprostone>PGE2, PGE1>STA2>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, << STA2 >> (a stable analogue of thromboxane A2), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit [[ HVA Ca2+ channels ]] was sulprostone>PGE2, PGE1>STA2>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, STA2 (a stable analogue of << thromboxane A2 >>), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit [[ HVA Ca2+ channels ]] was sulprostone>PGE2, PGE1>STA2>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and << sulprostone >> (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit [[ HVA Ca2+ channels ]] was sulprostone>PGE2, PGE1>STA2>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit << HVA Ca2+ channels >> was [[ sulprostone ]]>PGE2, PGE1>STA2>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit << HVA Ca2+ channels >> was sulprostone>[[ PGE2 ]], PGE1>STA2>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit << HVA Ca2+ channels >> was sulprostone>PGE2, [[ PGE1 ]]>STA2>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit << HVA Ca2+ channels >> was sulprostone>PGE2, PGE1>[[ STA2 ]]>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit << HVA Ca2+ channels >> was sulprostone>PGE2, PGE1>STA2>>[[ 17-phenyl-trinor-PGE2 ]].


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), << 17-phenyl-trinor-PGE2 >> (an [[ EP1 ]]-selective agonist) and sulprostone (an EP3-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit HVA Ca2+ channels was sulprostone>PGE2, PGE1>STA2>>17-phenyl-trinor-PGE2.


Prostaglandin E1, E2, STA2 (a stable analogue of thromboxane A2), 17-phenyl-trinor-PGE2 (an EP1-selective agonist) and << sulprostone >> (an [[ EP3 ]]-selective agonist) inhibited the HVA Ca2+ current (HVA ICa) dose-dependently, and the rank order of potency to inhibit HVA Ca2+ channels was sulprostone>PGE2, PGE1>STA2>>17-phenyl-trinor-PGE2.