Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and << SU11248 >>, the indolocarbazoles PKC412 and CEP-701, and the piperazonyl quinazoline CT53518, are potent inhibitors of [[ Flt3 ]] kinase.


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and << SU11248 >>, the indolocarbazoles PKC412 and CEP-701, and the piperazonyl quinazoline CT53518, are potent inhibitors of Flt3 [[ kinase ]].


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the << indolocarbazoles >> PKC412 and CEP-701, and the piperazonyl quinazoline CT53518, are potent inhibitors of [[ Flt3 ]] kinase.


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the << indolocarbazoles >> PKC412 and CEP-701, and the piperazonyl quinazoline CT53518, are potent inhibitors of Flt3 [[ kinase ]].


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the indolocarbazoles << PKC412 >> and CEP-701, and the piperazonyl quinazoline CT53518, are potent inhibitors of [[ Flt3 ]] kinase.


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the indolocarbazoles << PKC412 >> and CEP-701, and the piperazonyl quinazoline CT53518, are potent inhibitors of Flt3 [[ kinase ]].


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the indolocarbazoles PKC412 and << CEP-701 >>, and the piperazonyl quinazoline CT53518, are potent inhibitors of [[ Flt3 ]] kinase.


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the indolocarbazoles PKC412 and << CEP-701 >>, and the piperazonyl quinazoline CT53518, are potent inhibitors of Flt3 [[ kinase ]].


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the indolocarbazoles PKC412 and CEP-701, and the << piperazonyl quinazoline >> CT53518, are potent inhibitors of [[ Flt3 ]] kinase.


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the indolocarbazoles PKC412 and CEP-701, and the << piperazonyl quinazoline >> CT53518, are potent inhibitors of Flt3 [[ kinase ]].


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the indolocarbazoles PKC412 and CEP-701, and the piperazonyl quinazoline << CT53518 >>, are potent inhibitors of [[ Flt3 ]] kinase.


Compounds of several other structural families, including the quinoxaline AG1296, the bis(1H-2-indolyl)-1-methanone D-65476, the indolinones SU5416 and SU11248, the indolocarbazoles PKC412 and CEP-701, and the piperazonyl quinazoline << CT53518 >>, are potent inhibitors of Flt3 [[ kinase ]].


Novel mechanism of action for << hydralazine >>: induction of hypoxia-inducible factor-1alpha, [[ vascular endothelial growth factor ]], and angiogenesis by inhibition of prolyl hydroxylases.


Novel mechanism of action for << hydralazine >>: induction of [[ hypoxia-inducible factor-1alpha ]], vascular endothelial growth factor, and angiogenesis by inhibition of prolyl hydroxylases.


Novel mechanism of action for << hydralazine >>: induction of hypoxia-inducible factor-1alpha, vascular endothelial growth factor, and angiogenesis by inhibition of [[ prolyl hydroxylases ]].


<< Hydralazine >> induced rapid and transient expression of HIF-1alpha and downstream targets of HIF ([[ endothelin-1 ]], adrenomedullin, haem oxygenase 1, and vascular endothelial growth factor [VEGF]) in endothelial and smooth muscle cells and induced endothelial cell-specific proliferation.


<< Hydralazine >> induced rapid and transient expression of HIF-1alpha and downstream targets of HIF (endothelin-1, [[ adrenomedullin ]], haem oxygenase 1, and vascular endothelial growth factor [VEGF]) in endothelial and smooth muscle cells and induced endothelial cell-specific proliferation.


<< Hydralazine >> induced rapid and transient expression of HIF-1alpha and downstream targets of HIF (endothelin-1, adrenomedullin, [[ haem oxygenase 1 ]], and vascular endothelial growth factor [VEGF]) in endothelial and smooth muscle cells and induced endothelial cell-specific proliferation.


<< Hydralazine >> induced rapid and transient expression of HIF-1alpha and downstream targets of HIF (endothelin-1, adrenomedullin, haem oxygenase 1, and [[ vascular endothelial growth factor ]] [VEGF]) in endothelial and smooth muscle cells and induced endothelial cell-specific proliferation.


<< Hydralazine >> induced rapid and transient expression of HIF-1alpha and downstream targets of HIF (endothelin-1, adrenomedullin, haem oxygenase 1, and vascular endothelial growth factor [[[ VEGF ]]]) in endothelial and smooth muscle cells and induced endothelial cell-specific proliferation.


<< Hydralazine >> induced rapid and transient expression of [[ HIF-1alpha ]] and downstream targets of HIF (endothelin-1, adrenomedullin, haem oxygenase 1, and vascular endothelial growth factor [VEGF]) in endothelial and smooth muscle cells and induced endothelial cell-specific proliferation.


<< Hydralazine >> induced rapid and transient expression of HIF-1alpha and downstream targets of [[ HIF ]] (endothelin-1, adrenomedullin, haem oxygenase 1, and vascular endothelial growth factor [VEGF]) in endothelial and smooth muscle cells and induced endothelial cell-specific proliferation.


<< Hydralazine >> dose-dependently inhibited PHD activity and induced nonhydroxylated [[ HIF-1alpha ]], evidence for HIF stabilization specifically by inhibition of PHD enzyme activity.


<< Hydralazine >> dose-dependently inhibited [[ PHD ]] activity and induced nonhydroxylated HIF-1alpha, evidence for HIF stabilization specifically by inhibition of PHD enzyme activity.


<< Hydralazine >> dose-dependently inhibited PHD activity and induced nonhydroxylated HIF-1alpha, evidence for HIF stabilization specifically by inhibition of [[ PHD ]] enzyme activity.


In vivo, << hydralazine >> induced HIF-1alpha and VEGF protein in tissue extracts and elevated plasma [[ VEGF ]] levels.


In vivo, << hydralazine >> induced HIF-1alpha and [[ VEGF ]] protein in tissue extracts and elevated plasma VEGF levels.


In vivo, << hydralazine >> induced [[ HIF-1alpha ]] and VEGF protein in tissue extracts and elevated plasma VEGF levels.


Thus, << hydralazine >> activates the [[ HIF ]] pathway through inhibition of PHD activity and initiates a pro-angiogenic phenotype.


Thus, << hydralazine >> activates the HIF pathway through inhibition of [[ PHD ]] activity and initiates a pro-angiogenic phenotype.


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas << NS398 >>, carprofen, tolfenamic acid, nimesulide, and etodolac had more than 5 times greater preference for inhibiting [[ COX-2 ]] than COX-1.


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas << NS398 >>, carprofen, tolfenamic acid, nimesulide, and etodolac had more than 5 times greater preference for inhibiting COX-2 than [[ COX-1 ]].


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas NS398, << carprofen >>, tolfenamic acid, nimesulide, and etodolac had more than 5 times greater preference for inhibiting [[ COX-2 ]] than COX-1.


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas NS398, << carprofen >>, tolfenamic acid, nimesulide, and etodolac had more than 5 times greater preference for inhibiting COX-2 than [[ COX-1 ]].


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas NS398, carprofen, << tolfenamic acid >>, nimesulide, and etodolac had more than 5 times greater preference for inhibiting [[ COX-2 ]] than COX-1.


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas NS398, carprofen, << tolfenamic acid >>, nimesulide, and etodolac had more than 5 times greater preference for inhibiting COX-2 than [[ COX-1 ]].


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas NS398, carprofen, tolfenamic acid, << nimesulide >>, and etodolac had more than 5 times greater preference for inhibiting [[ COX-2 ]] than COX-1.


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas NS398, carprofen, tolfenamic acid, << nimesulide >>, and etodolac had more than 5 times greater preference for inhibiting COX-2 than [[ COX-1 ]].


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas NS398, carprofen, tolfenamic acid, nimesulide, and << etodolac >> had more than 5 times greater preference for inhibiting [[ COX-2 ]] than COX-1.


RESULTS: Aspirin, diclofenac, indomethacin, ketoprofen, meclofenamic acid, and piroxicam had little selectivity toward COX isozymes, whereas NS398, carprofen, tolfenamic acid, nimesulide, and << etodolac >> had more than 5 times greater preference for inhibiting COX-2 than [[ COX-1 ]].


CONCLUSIONS AND CLINICAL RELEVANCE: << Canine COX-2 >> was selectively inhibited by [[ etodolac ]], nimesulide, and NS398; tolfenamic acid and carprofen also appeared to be preferential COX-2 inhibitors in dogs.


CONCLUSIONS AND CLINICAL RELEVANCE: << Canine COX-2 >> was selectively inhibited by etodolac, [[ nimesulide ]], and NS398; tolfenamic acid and carprofen also appeared to be preferential COX-2 inhibitors in dogs.


CONCLUSIONS AND CLINICAL RELEVANCE: << Canine COX-2 >> was selectively inhibited by etodolac, nimesulide, and [[ NS398 ]]; tolfenamic acid and carprofen also appeared to be preferential COX-2 inhibitors in dogs.


CONCLUSIONS AND CLINICAL RELEVANCE: Canine COX-2 was selectively inhibited by etodolac, nimesulide, and NS398; << tolfenamic acid >> and carprofen also appeared to be preferential [[ COX-2 ]] inhibitors in dogs.


CONCLUSIONS AND CLINICAL RELEVANCE: Canine COX-2 was selectively inhibited by etodolac, nimesulide, and NS398; tolfenamic acid and << carprofen >> also appeared to be preferential [[ COX-2 ]] inhibitors in dogs.


<< Acarbose >> served as inhibitor of an interfering [[ acid alpha-glucosidase ]] present in neutrophils, which allowed the lysosomal enzyme implicated in Pompe disease to be selectively analyzed.


After 12 months of treatment, << carvedilol >> significantly improved all end points (plasma concentration of [[ B-type natriuretic peptide ]] [BNP] from 175 (35 to 209) to 106 (52 to 160) pg/ml, mean (95% confidence interval) p <0.01; New York Heart Association functional class from 2.37 (2.13 to 2.61) to 1.56 (1.21 to 1.91), p <0.01; exercise capacity estimated with the Specific Activity Scale from 4.75 (4.50 to 5.00) to 5.68 (5.22 to 6.14) METs, p <0.02), whereas conventional therapy did not (plasma BNP concentration from 150 (114 to 186) to 174 (100 to 248) pg/ml; New York Heart Association functional class from 2.29 (2.08 to 2.50) to 2.11 (1.73 to 2.49); exercise capacity from 4.57 (4.34 to 4.80) to 4.72 (4.41 to 5.03) METs).


After 12 months of treatment, << carvedilol >> significantly improved all end points (plasma concentration of B-type natriuretic peptide [[[ BNP ]]] from 175 (35 to 209) to 106 (52 to 160) pg/ml, mean (95% confidence interval) p <0.01; New York Heart Association functional class from 2.37 (2.13 to 2.61) to 1.56 (1.21 to 1.91), p <0.01; exercise capacity estimated with the Specific Activity Scale from 4.75 (4.50 to 5.00) to 5.68 (5.22 to 6.14) METs, p <0.02), whereas conventional therapy did not (plasma BNP concentration from 150 (114 to 186) to 174 (100 to 248) pg/ml; New York Heart Association functional class from 2.29 (2.08 to 2.50) to 2.11 (1.73 to 2.49); exercise capacity from 4.57 (4.34 to 4.80) to 4.72 (4.41 to 5.03) METs).


Univariate regression analyses showed that only the use of << carvedilol >> was correlated with the decrease in [[ plasma BNP ]] concentration (p <0.03).


<< Terbinafine >>: mode of action and properties of the [[ squalene epoxidase ]] inhibition.


<< Terbinafine >> (Lamisil) has primarily fungicidal action against many fungi as a result of its specific mechanism of [[ squalene epoxidase ]] inhibition.


Terbinafine (<< Lamisil >>) has primarily fungicidal action against many fungi as a result of its specific mechanism of [[ squalene epoxidase ]] inhibition.


<< Terbinafine >> is a potent non-competitive inhibitor of [[ squalene epoxidase ]] from Candida (Ki = 30 nM).


In contrast, inhibition of << rat liver squalene epoxidase >> only occurs at higher drug concentrations (Ki = 77 microM), and is competitive with [[ squalene ]].


Each statin induced apoA-I expression (mRNA and protein) dose-dependently: the rank order of the << apoA-I >> induction [[ pitavastatin ]] (3 microM)>simvastatin (10 microM)>atorvastatin (30 microM).


Each statin induced apoA-I expression (mRNA and protein) dose-dependently: the rank order of the << apoA-I >> induction pitavastatin (3 microM)>[[ simvastatin ]] (10 microM)>atorvastatin (30 microM).


Each statin induced apoA-I expression (mRNA and protein) dose-dependently: the rank order of the << apoA-I >> induction pitavastatin (3 microM)>simvastatin (10 microM)>[[ atorvastatin ]] (30 microM).


The induction of << apoA-I >> by statins disappeared with addition of [[ mevalonate ]], which indicates that the effect is HMG-CoA reductase inhibition-dependent.


Based on HMG-CoA reductase inhibition, pitavastatin-induced << apoA-I >> more efficiently than [[ simvastatin ]] and atorvastatin.


Based on HMG-CoA reductase inhibition, pitavastatin-induced << apoA-I >> more efficiently than simvastatin and [[ atorvastatin ]].


Based on HMG-CoA reductase inhibition, << pitavastatin >>-induced [[ apoA-I ]] more efficiently than simvastatin and atorvastatin.


Further study revealed that << pitavastatin >> increased [[ ABCA1 ]] mRNA in HMG-CoA reductase-dependent manner and that Rho and Rho kinase inhibitor (C3T and Y27632) increased apoA-I production in the HepG2 cells.


Further study revealed that pitavastatin increased ABCA1 mRNA in HMG-CoA reductase-dependent manner and that Rho and Rho kinase inhibitor (C3T and << Y27632 >>) increased [[ apoA-I ]] production in the HepG2 cells.


Further study revealed that pitavastatin increased ABCA1 mRNA in HMG-CoA reductase-dependent manner and that << Rho >> and Rho kinase inhibitor (C3T and [[ Y27632 ]]) increased apoA-I production in the HepG2 cells.


Further study revealed that pitavastatin increased ABCA1 mRNA in HMG-CoA reductase-dependent manner and that Rho and << Rho kinase >> inhibitor (C3T and [[ Y27632 ]]) increased apoA-I production in the HepG2 cells.


These results suggest that << pitavastatin >> efficiently increases [[ apoA-I ]] in the culture medium of HepG2 cells by promoting apoA-I production through inhibition of HMG-CoA reductase and suppression of Rho activity and by protecting apoA-I from catabolism through ABCA1 induction and lipidation of apoA-I.


These results suggest that << pitavastatin >> efficiently increases apoA-I in the culture medium of HepG2 cells by promoting [[ apoA-I ]] production through inhibition of HMG-CoA reductase and suppression of Rho activity and by protecting apoA-I from catabolism through ABCA1 induction and lipidation of apoA-I.


These results suggest that << pitavastatin >> efficiently increases apoA-I in the culture medium of HepG2 cells by promoting apoA-I production through inhibition of HMG-CoA reductase and suppression of Rho activity and by protecting apoA-I from catabolism through [[ ABCA1 ]] induction and lipidation of apoA-I.


These results suggest that << pitavastatin >> efficiently increases apoA-I in the culture medium of HepG2 cells by promoting apoA-I production through inhibition of HMG-CoA reductase and suppression of Rho activity and by protecting apoA-I from catabolism through ABCA1 induction and lipidation of [[ apoA-I ]].


These results suggest that << pitavastatin >> efficiently increases apoA-I in the culture medium of HepG2 cells by promoting apoA-I production through inhibition of [[ HMG-CoA reductase ]] and suppression of Rho activity and by protecting apoA-I from catabolism through ABCA1 induction and lipidation of apoA-I.


These results suggest that << pitavastatin >> efficiently increases apoA-I in the culture medium of HepG2 cells by promoting apoA-I production through inhibition of HMG-CoA reductase and suppression of [[ Rho ]] activity and by protecting apoA-I from catabolism through ABCA1 induction and lipidation of apoA-I.


MATERIALS AND METHODS: Seeking to improve efficacy against otherwise intractable end-stage pancreatic islet tumors, two << receptor tyrosine kinase >> inhibitors, [[ imatinib ]] and SU11248, were used to disrupt PDGFR-mediated pericyte support of tumor endothelial cells in concert with maximum-tolerated dose (MTD) or metronomic chemotherapy and/or VEGFR inhibition.


MATERIALS AND METHODS: Seeking to improve efficacy against otherwise intractable end-stage pancreatic islet tumors, two receptor tyrosine kinase inhibitors, << imatinib >> and SU11248, were used to disrupt [[ PDGFR ]]-mediated pericyte support of tumor endothelial cells in concert with maximum-tolerated dose (MTD) or metronomic chemotherapy and/or VEGFR inhibition.


MATERIALS AND METHODS: Seeking to improve efficacy against otherwise intractable end-stage pancreatic islet tumors, two receptor tyrosine kinase inhibitors, << imatinib >> and SU11248, were used to disrupt PDGFR-mediated pericyte support of tumor endothelial cells in concert with maximum-tolerated dose (MTD) or metronomic chemotherapy and/or [[ VEGFR ]] inhibition.


MATERIALS AND METHODS: Seeking to improve efficacy against otherwise intractable end-stage pancreatic islet tumors, two << receptor tyrosine kinase >> inhibitors, imatinib and [[ SU11248 ]], were used to disrupt PDGFR-mediated pericyte support of tumor endothelial cells in concert with maximum-tolerated dose (MTD) or metronomic chemotherapy and/or VEGFR inhibition.


MATERIALS AND METHODS: Seeking to improve efficacy against otherwise intractable end-stage pancreatic islet tumors, two receptor tyrosine kinase inhibitors, imatinib and << SU11248 >>, were used to disrupt [[ PDGFR ]]-mediated pericyte support of tumor endothelial cells in concert with maximum-tolerated dose (MTD) or metronomic chemotherapy and/or VEGFR inhibition.


MATERIALS AND METHODS: Seeking to improve efficacy against otherwise intractable end-stage pancreatic islet tumors, two receptor tyrosine kinase inhibitors, imatinib and << SU11248 >>, were used to disrupt PDGFR-mediated pericyte support of tumor endothelial cells in concert with maximum-tolerated dose (MTD) or metronomic chemotherapy and/or [[ VEGFR ]] inhibition.


RESULTS: << Imatinib >>, despite equivocal efficacy as monotherapy, reduced pericyte coverage of tumor vessels and enhanced efficacy in combination with metronomic chemotherapy or [[ VEGFR ]] inhibition.


The objective of the present study was to compare the anti-inflammatory effects of the preferential COX-2 inhibitor etodolac with the non-selective << COX >> inhibitor [[ phenylbutazone ]] in horses with lipopolysaccharide (LPS)-induced synovitis.


In addition, both drugs significantly reduced PGE2 levels (P<0.05) 6-h following LPS injection, whereas the probable << COX-1 >> prostanoid TXB2 was significantly reduced by [[ phenylbutazone ]] (P<0.05), but not etodolac.


Effect of << bosentan >> ([[ ETA ]]/ETB receptor antagonist) on metabolic changes during stress and diabetes.


Effect of << bosentan >> (ETA/[[ ETB ]] receptor antagonist) on metabolic changes during stress and diabetes.


To test this, we studied the possible effect of the << endothelin receptor >> antagonist, [[ bosentan ]] (50 and 100 mg kg(-1)) on serum glucose and insulin levels as well as on liver glycogen contents in normoglycemic stressed animals.


Pre-irradiation administration of RP-1 enhanced levels of << GSH >> induced increase in [[ complex I ]] (upto 16 h), complex I/III (4 h) complex II/III activity (upto 24 h; p < 0.01) and inhibited the radiation-induced decrease in MMP significantly (24 h; p < 0.01).


Pre-irradiation administration of RP-1 enhanced levels of << GSH >> induced increase in complex I (upto 16 h), [[ complex I/III ]] (4 h) complex II/III activity (upto 24 h; p < 0.01) and inhibited the radiation-induced decrease in MMP significantly (24 h; p < 0.01).


Pre-irradiation administration of RP-1 enhanced levels of << GSH >> induced increase in complex I (upto 16 h), complex I/III (4 h) [[ complex II/III ]] activity (upto 24 h; p < 0.01) and inhibited the radiation-induced decrease in MMP significantly (24 h; p < 0.01).


Moreover, << minocycline >> efficiently suppressed the release of [[ cytochrome c ]] from mitochondria of the liver tissues from Jo2-challenged mice.


Our results suggest that easing of Fas-triggered fulminant hepatitis by << minocycline >> may involve a mitochondrial apoptotic pathway, probably through preventing [[ cytochrome c ]] release and thereby blocking downstream caspase activation.


Our results suggest that easing of Fas-triggered fulminant hepatitis by << minocycline >> may involve a mitochondrial apoptotic pathway, probably through preventing cytochrome c release and thereby blocking downstream [[ caspase ]] activation.


Cystathionine-gamma-lyase (<< CSE >>) and cystathionine-beta-synthase (CBS) utilize L-cysteine as substrate to form [[ H2S ]].


Cystathionine-gamma-lyase (CSE) and << cystathionine-beta-synthase >> (CBS) utilize L-cysteine as substrate to form [[ H2S ]].


Cystathionine-gamma-lyase (CSE) and cystathionine-beta-synthase (<< CBS >>) utilize L-cysteine as substrate to form [[ H2S ]].


<< Cystathionine-gamma-lyase >> (CSE) and cystathionine-beta-synthase (CBS) utilize L-cysteine as substrate to form [[ H2S ]].


Cystathionine-gamma-lyase (<< CSE >>) and cystathionine-beta-synthase (CBS) utilize [[ L-cysteine ]] as substrate to form H2S.


Cystathionine-gamma-lyase (CSE) and << cystathionine-beta-synthase >> (CBS) utilize [[ L-cysteine ]] as substrate to form H2S.


Cystathionine-gamma-lyase (CSE) and cystathionine-beta-synthase (<< CBS >>) utilize [[ L-cysteine ]] as substrate to form H2S.


<< Cystathionine-gamma-lyase >> (CSE) and cystathionine-beta-synthase (CBS) utilize [[ L-cysteine ]] as substrate to form H2S.


Of these two enzymes, << cystathionine-gamma-lyase >> (CSE) is believed to be the key enzyme that forms [[ H2S ]] in the cardiovascular system.


Of these two enzymes, cystathionine-gamma-lyase (<< CSE >>) is believed to be the key enzyme that forms [[ H2S ]] in the cardiovascular system.


Also, prophylactic, as well as therapeutic, treatment with the CSE inhibitor, DL-propargylglycine (PAG), significantly reduced the severity of caerulein-induced pancreatitis and associated lung injury, as determined by 1) hyperamylasemia [plasma amylase (U/L) (control, 1204+/-59); prophylactic treatment: placebo, 10635+/-305; PAG, 7904+/-495; therapeutic treatment: placebo, 10427+/-470; PAG, 7811+/-428; P<0.05 PAG c.f. placebo; n=24 animals in each group]; 2) neutrophil sequestration in the pancreas [pancreatic << myeloperoxidase oxidase >> (MPO) activity (fold increase over control) (prophylactic treatment: placebo, 5.78+/-0.63; [[ PAG ]], 2.97+/-0.39; therapeutic treatment: placebo, 5.48+/-0.52; PAG, 3.03+/-0.47; P<0.05 PAG c.f. placebo; n=24 animals in each group)]; 3) pancreatic acinar cell injury/necrosis; 4) lung MPO activity (fold increase over control) [prophylactic treatment: placebo, 1.99+/-0.16; PAG, 1.34+/-0.14; therapeutic treatment: placebo, 2.03+/-0.12; PAG, 1.41+/-0.97; P<0.05 PAG c.f. placebo; n=24 animals in each group]; and 5) histological evidence of lung injury.


Also, prophylactic, as well as therapeutic, treatment with the CSE inhibitor, DL-propargylglycine (PAG), significantly reduced the severity of caerulein-induced pancreatitis and associated lung injury, as determined by 1) hyperamylasemia [plasma amylase (U/L) (control, 1204+/-59); prophylactic treatment: placebo, 10635+/-305; PAG, 7904+/-495; therapeutic treatment: placebo, 10427+/-470; PAG, 7811+/-428; P<0.05 PAG c.f. placebo; n=24 animals in each group]; 2) neutrophil sequestration in the pancreas [pancreatic myeloperoxidase oxidase (<< MPO >>) activity (fold increase over control) (prophylactic treatment: placebo, 5.78+/-0.63; [[ PAG ]], 2.97+/-0.39; therapeutic treatment: placebo, 5.48+/-0.52; PAG, 3.03+/-0.47; P<0.05 PAG c.f. placebo; n=24 animals in each group)]; 3) pancreatic acinar cell injury/necrosis; 4) lung MPO activity (fold increase over control) [prophylactic treatment: placebo, 1.99+/-0.16; PAG, 1.34+/-0.14; therapeutic treatment: placebo, 2.03+/-0.12; PAG, 1.41+/-0.97; P<0.05 PAG c.f. placebo; n=24 animals in each group]; and 5) histological evidence of lung injury.


Also, prophylactic, as well as therapeutic, treatment with the << CSE >> inhibitor, [[ DL-propargylglycine ]] (PAG), significantly reduced the severity of caerulein-induced pancreatitis and associated lung injury, as determined by 1) hyperamylasemia [plasma amylase (U/L) (control, 1204+/-59); prophylactic treatment: placebo, 10635+/-305; PAG, 7904+/-495; therapeutic treatment: placebo, 10427+/-470; PAG, 7811+/-428; P<0.05 PAG c.f. placebo; n=24 animals in each group]; 2) neutrophil sequestration in the pancreas [pancreatic myeloperoxidase oxidase (MPO) activity (fold increase over control) (prophylactic treatment: placebo, 5.78+/-0.63; PAG, 2.97+/-0.39; therapeutic treatment: placebo, 5.48+/-0.52; PAG, 3.03+/-0.47; P<0.05 PAG c.f. placebo; n=24 animals in each group)]; 3) pancreatic acinar cell injury/necrosis; 4) lung MPO activity (fold increase over control) [prophylactic treatment: placebo, 1.99+/-0.16; PAG, 1.34+/-0.14; therapeutic treatment: placebo, 2.03+/-0.12; PAG, 1.41+/-0.97; P<0.05 PAG c.f. placebo; n=24 animals in each group]; and 5) histological evidence of lung injury.


Also, prophylactic, as well as therapeutic, treatment with the << CSE >> inhibitor, DL-propargylglycine ([[ PAG ]]), significantly reduced the severity of caerulein-induced pancreatitis and associated lung injury, as determined by 1) hyperamylasemia [plasma amylase (U/L) (control, 1204+/-59); prophylactic treatment: placebo, 10635+/-305; PAG, 7904+/-495; therapeutic treatment: placebo, 10427+/-470; PAG, 7811+/-428; P<0.05 PAG c.f. placebo; n=24 animals in each group]; 2) neutrophil sequestration in the pancreas [pancreatic myeloperoxidase oxidase (MPO) activity (fold increase over control) (prophylactic treatment: placebo, 5.78+/-0.63; PAG, 2.97+/-0.39; therapeutic treatment: placebo, 5.48+/-0.52; PAG, 3.03+/-0.47; P<0.05 PAG c.f. placebo; n=24 animals in each group)]; 3) pancreatic acinar cell injury/necrosis; 4) lung MPO activity (fold increase over control) [prophylactic treatment: placebo, 1.99+/-0.16; PAG, 1.34+/-0.14; therapeutic treatment: placebo, 2.03+/-0.12; PAG, 1.41+/-0.97; P<0.05 PAG c.f. placebo; n=24 animals in each group]; and 5) histological evidence of lung injury.


ABCG5 and ABCG8 themselves are regulated by cholesterol via liver X receptors (<< LXRs >>), which are also activated by oxysterols and some derivatives of plant [[ sterols ]].


<< NPC1L1 >> could recently be identified as a major sterol transporter for the intestinal uptake of [[ cholesterol ]] as well as plant sterols.


NPC1L1 could recently be identified as a major << sterol transporter >> for the intestinal uptake of [[ cholesterol ]] as well as plant sterols.


<< NPC1L1 >> could recently be identified as a major sterol transporter for the intestinal uptake of cholesterol as well as plant [[ sterols ]].


NPC1L1 could recently be identified as a major << sterol transporter >> for the intestinal uptake of cholesterol as well as plant [[ sterols ]].


<< Bupropion >> has an antidepressant effect through blocking the [[ dopamine transporter ]].


In vitro studies demonstrated that the retinoid X receptor (RXR) retinoid, << bexarotene >>, at biologically relevant concentrations of 10(-6) M to 10(-8) M, upregulated both the [[ p55 ]] and p75 subunits of the IL-2R and enhanced 5- to 10-fold the susceptibility of T-cell leukemia cells to denileukin diftitox.


In vitro studies demonstrated that the retinoid X receptor (RXR) retinoid, << bexarotene >>, at biologically relevant concentrations of 10(-6) M to 10(-8) M, upregulated both the p55 and [[ p75 ]] subunits of the IL-2R and enhanced 5- to 10-fold the susceptibility of T-cell leukemia cells to denileukin diftitox.


In vitro studies demonstrated that the retinoid X receptor (RXR) retinoid, << bexarotene >>, at biologically relevant concentrations of 10(-6) M to 10(-8) M, upregulated both the p55 and p75 subunits of the [[ IL-2R ]] and enhanced 5- to 10-fold the susceptibility of T-cell leukemia cells to denileukin diftitox.


Our results demonstrate that the combination of denileukin diftitox and bexarotene is well tolerated and that even low doses (150 mg/day) of << bexarotene >> are capable of in vivo upregulation of [[ CD25 ]] expression on circulating leukemia cells.


<< PSMA >> acts as a glutamate carboxypeptidase (GCPII) on small molecule substrates, including [[ folate ]], the anticancer drug methotrexate, and the neuropeptide N-acetyl-l-aspartyl-l-glutamate.


PSMA acts as a << glutamate carboxypeptidase >> (GCPII) on small molecule substrates, including [[ folate ]], the anticancer drug methotrexate, and the neuropeptide N-acetyl-l-aspartyl-l-glutamate.


PSMA acts as a glutamate carboxypeptidase (<< GCPII >>) on small molecule substrates, including [[ folate ]], the anticancer drug methotrexate, and the neuropeptide N-acetyl-l-aspartyl-l-glutamate.


<< PSMA >> acts as a glutamate carboxypeptidase (GCPII) on small molecule substrates, including folate, the anticancer drug [[ methotrexate ]], and the neuropeptide N-acetyl-l-aspartyl-l-glutamate.


PSMA acts as a << glutamate carboxypeptidase >> (GCPII) on small molecule substrates, including folate, the anticancer drug [[ methotrexate ]], and the neuropeptide N-acetyl-l-aspartyl-l-glutamate.


PSMA acts as a glutamate carboxypeptidase (<< GCPII >>) on small molecule substrates, including folate, the anticancer drug [[ methotrexate ]], and the neuropeptide N-acetyl-l-aspartyl-l-glutamate.


<< PSMA >> acts as a glutamate carboxypeptidase (GCPII) on small molecule substrates, including folate, the anticancer drug methotrexate, and the neuropeptide [[ N-acetyl-l-aspartyl-l-glutamate ]].


PSMA acts as a << glutamate carboxypeptidase >> (GCPII) on small molecule substrates, including folate, the anticancer drug methotrexate, and the neuropeptide [[ N-acetyl-l-aspartyl-l-glutamate ]].


Elucidation of the << PSMA >> structure combined with docking studies and a proposed catalytic mechanism provides insight into the recognition of inhibitors and the natural substrate [[ N-acetyl-l-aspartyl-l-glutamate ]].


A number of selective << 5-HT3 >> antagonists have been developed including ondansetron, granisetron, tropisetron renzapride and [[ zacopride ]].


A number of selective << 5-HT3 >> antagonists have been developed including [[ ondansetron ]], granisetron, tropisetron renzapride and zacopride.


A number of selective << 5-HT3 >> antagonists have been developed including ondansetron, [[ granisetron ]], tropisetron renzapride and zacopride.


A number of selective << 5-HT3 >> antagonists have been developed including ondansetron, granisetron, [[ tropisetron ]] renzapride and zacopride.


A number of selective << 5-HT3 >> antagonists have been developed including ondansetron, granisetron, tropisetron [[ renzapride ]] and zacopride.


While the substituted << benzamide >> prokinetics (for example, metoclopramide, cisapride) also block [[ 5-HT3 ]] receptors in high concentrations, their prokinetic action is believed to be on the basis of their agonist effects on the putative 5-HT4 receptor.


While the substituted benzamide prokinetics (for example, << metoclopramide >>, cisapride) also block [[ 5-HT3 ]] receptors in high concentrations, their prokinetic action is believed to be on the basis of their agonist effects on the putative 5-HT4 receptor.


While the substituted benzamide prokinetics (for example, metoclopramide, << cisapride >>) also block [[ 5-HT3 ]] receptors in high concentrations, their prokinetic action is believed to be on the basis of their agonist effects on the putative 5-HT4 receptor.


While the substituted << benzamide >> prokinetics (for example, metoclopramide, cisapride) also block 5-HT3 receptors in high concentrations, their prokinetic action is believed to be on the basis of their agonist effects on the putative [[ 5-HT4 ]] receptor.


While the substituted benzamide prokinetics (for example, << metoclopramide >>, cisapride) also block 5-HT3 receptors in high concentrations, their prokinetic action is believed to be on the basis of their agonist effects on the putative [[ 5-HT4 ]] receptor.


While the substituted benzamide prokinetics (for example, metoclopramide, << cisapride >>) also block 5-HT3 receptors in high concentrations, their prokinetic action is believed to be on the basis of their agonist effects on the putative [[ 5-HT4 ]] receptor.


Some 5-HT3 antagonists have << 5-HT4 >> agonist activity (for example, [[ renzapride ]], zacopride) and others do not (for example, ondansetron, granisetron), while tropisetron in high concentrations is a 5-HT4 antagonist.


Some 5-HT3 antagonists have << 5-HT4 >> agonist activity (for example, renzapride, [[ zacopride ]]) and others do not (for example, ondansetron, granisetron), while tropisetron in high concentrations is a 5-HT4 antagonist.


Some << 5-HT3 >> antagonists have 5-HT4 agonist activity (for example, [[ renzapride ]], zacopride) and others do not (for example, ondansetron, granisetron), while tropisetron in high concentrations is a 5-HT4 antagonist.


Some << 5-HT3 >> antagonists have 5-HT4 agonist activity (for example, renzapride, [[ zacopride ]]) and others do not (for example, ondansetron, granisetron), while tropisetron in high concentrations is a 5-HT4 antagonist.


Some 5-HT3 antagonists have 5-HT4 agonist activity (for example, renzapride, zacopride) and others do not (for example, ondansetron, granisetron), while << tropisetron >> in high concentrations is a [[ 5-HT4 ]] antagonist.


We present our studies to demonstrate that HM74A, but not HM74, binds << niacin >> at high affinities and effectively mediates [[ Gi ]] signaling events in human embryonic kidney HEK293 cells as well as in 3T3L1 adipocytes expressing HM74A.


When cultured in YPD medium containing 15% glucose under aerobic conditions, the << KGD1 >> (alpha-ketoglutarate dehydrogenase) gene disrupted mutant produced a lower level of [[ succinate ]] than the wild-type strain, while the SDH1 (succinate dehydrogenase) gene-disrupted mutant produced an increased level of succinate.


When cultured in YPD medium containing 15% glucose under aerobic conditions, the KGD1 (<< alpha-ketoglutarate dehydrogenase >>) gene disrupted mutant produced a lower level of [[ succinate ]] than the wild-type strain, while the SDH1 (succinate dehydrogenase) gene-disrupted mutant produced an increased level of succinate.


When cultured in YPD medium containing 15% glucose under aerobic conditions, the KGD1 (alpha-ketoglutarate dehydrogenase) gene disrupted mutant produced a lower level of succinate than the wild-type strain, while the << SDH1 >> (succinate dehydrogenase) gene-disrupted mutant produced an increased level of [[ succinate ]].


When cultured in YPD medium containing 15% glucose under aerobic conditions, the KGD1 (alpha-ketoglutarate dehydrogenase) gene disrupted mutant produced a lower level of succinate than the wild-type strain, while the SDH1 (<< succinate dehydrogenase >>) gene-disrupted mutant produced an increased level of [[ succinate ]].


On the other hand, the << FUM1 >> (fumarase) gene disrupted mutant produced significantly higher levels of [[ fumarate ]] but did not form malate at all.


On the other hand, the FUM1 (<< fumarase >>) gene disrupted mutant produced significantly higher levels of [[ fumarate ]] but did not form malate at all.


When the growth condition was shifted from aerobic to anaerobic, the increased level of << succinate >> in [[ SDH1 ]] disruptants was no longer observed, whereas the decreased level of succinate in the KGD1 diruptant was still observed.


When the growth condition was shifted from aerobic to anaerobic, the increased level of succinate in SDH1 disruptants was no longer observed, whereas the decreased level of << succinate >> in the [[ KGD1 ]] diruptant was still observed.


A double mutant of the two << fumarate reductase >> isozyme genes (OSM1 and FRDS) showed a [[ succinate ]] productivity of 50% as compared to the parent when cells were incubated in glucose-buffered solution.


A double mutant of the two fumarate reductase isozyme genes (<< OSM1 >> and FRDS) showed a [[ succinate ]] productivity of 50% as compared to the parent when cells were incubated in glucose-buffered solution.


A double mutant of the two fumarate reductase isozyme genes (OSM1 and << FRDS >>) showed a [[ succinate ]] productivity of 50% as compared to the parent when cells were incubated in glucose-buffered solution.


<< Vitamin E >> and probucol significantly suppressed an increase in plasma total-cholesterol (total-C) and [[ low-density lipoprotein ]] cholesterol compared to HC-control group.


Vitamin E and << probucol >> significantly suppressed an increase in plasma total-cholesterol (total-C) and [[ low-density lipoprotein ]] cholesterol compared to HC-control group.


However, plasma high-density lipoprotein-cholesterol (HDL-C) and HDL-C/total-C ratio levels and plasma << paraoxonase >> activity were only significantly higher in [[ vitamin E ]] group after 8 weeks.


However, plasma << high-density lipoprotein >>-cholesterol (HDL-C) and HDL-C/total-C ratio levels and plasma paraoxonase activity were only significantly higher in [[ vitamin E ]] group after 8 weeks.


However, plasma high-density lipoprotein-cholesterol (<< HDL >>-C) and HDL-C/total-C ratio levels and plasma paraoxonase activity were only significantly higher in [[ vitamin E ]] group after 8 weeks.


However, plasma high-density lipoprotein-cholesterol (HDL-C) and << HDL >>-C/total-C ratio levels and plasma paraoxonase activity were only significantly higher in [[ vitamin E ]] group after 8 weeks.


Hepatic ACAT activity was significantly lower in both vitamin E and probucol groups than in HC-control group, while << HMG-CoA reductase >> activity was the highest only in the [[ probucol ]] group.


Hepatic << ACAT >> activity was significantly lower in both [[ vitamin E ]] and probucol groups than in HC-control group, while HMG-CoA reductase activity was the highest only in the probucol group.


Hepatic << ACAT >> activity was significantly lower in both vitamin E and [[ probucol ]] groups than in HC-control group, while HMG-CoA reductase activity was the highest only in the probucol group.


Hepatic mRNA expressions of << apo B-100 >> and apo C-III were significantly lower in [[ probucol ]] group than in other groups.


Hepatic mRNA expressions of apo B-100 and << apo C-III >> were significantly lower in [[ probucol ]] group than in other groups.


Vitamin E supplementation was found to alter the plasma HDL-C-related factors; meanwhile, << probucol >> supplementation was very effective in enhancing cholesterol metabolism, except for a negative effect that reduced plasma [[ HDL ]]-C concentration.


The aim of this study was to determine if macaque represents a suitable species for the pre-clinical evaluation of novel << CCR5 >> antagonists, such as [[ maraviroc ]] (UK-427,857).


The aim of this study was to determine if macaque represents a suitable species for the pre-clinical evaluation of novel << CCR5 >> antagonists, such as maraviroc ([[ UK-427,857 ]]).


<< Maraviroc >> inhibited binding of [125I]-MIP-1beta to CCR5 from macaque and human with similar potency (IC50 = 17.50 +/- 1.24 nM and 7.18 +/- 0.93 nM, respectively) and antagonised MIP-1beta induced intracellular calcium release mediated through [[ CCR5 ]] from macaque and human with similar potency (IC50 = 17.50 +/- 3.30 nM and 12.07 +/- 1.89, respectively).


However, as with the human receptor, << maraviroc >> was shown to be a high affinity, potent functional antagonist of [[ macaque CCR5 ]] thereby indicating that the macaque should be a suitable species in which to evaluate the pharmacology, safety and potential mechanism-related toxicology of novel CCR5 antagonists.


However, as with the human receptor, << maraviroc >> was shown to be a high affinity, potent functional antagonist of macaque CCR5 thereby indicating that the macaque should be a suitable species in which to evaluate the pharmacology, safety and potential mechanism-related toxicology of novel [[ CCR5 ]] antagonists.


Hence, re-expression of the p75NTR appears to partially reverse de-differentiation of prostate cancer cells by up-regulating the expression of << CRABPI >> for localized sequestration of [[ retinoids ]] that are available to newly up-regulated RAR-beta, RXR-alpha, and RXR-beta.


Its special profile of actions, especially the rise in << HDL >>-cholesterol levels induced by [[ nicotinic acid ]], is unique among the currently available pharmacological tools to treat lipid disorders.


<< Valproic acid >> selectively inhibits conversion of arachidonic acid to arachidonoyl-CoA by [[ brain microsomal long-chain fatty acyl-CoA synthetases ]]: relevance to bipolar disorder.


Valproic acid selectively inhibits conversion of arachidonic acid to << arachidonoyl-CoA >> by [[ brain microsomal long-chain fatty acyl-CoA synthetases ]]: relevance to bipolar disorder.


Valproic acid selectively inhibits conversion of << arachidonic acid >> to arachidonoyl-CoA by [[ brain microsomal long-chain fatty acyl-CoA synthetases ]]: relevance to bipolar disorder.


RATIONALE: Several drugs used to treat bipolar disorder (<< lithium >> and carbamazepine), when administered chronically to rats, reduce the turnover of arachidonic acid, but not docosahexaenoic acid, in brain phospholipids by decreasing the activity of an arachidonic acid-selective [[ phospholipase A(2) ]].


RATIONALE: Several drugs used to treat bipolar disorder (lithium and << carbamazepine >>), when administered chronically to rats, reduce the turnover of arachidonic acid, but not docosahexaenoic acid, in brain phospholipids by decreasing the activity of an arachidonic acid-selective [[ phospholipase A(2) ]].


MATERIALS AND METHODS/RESULTS: By isolating rat brain microsomal long-chain fatty acyl-CoA synthetases (Acsl), we show in vitro that << valproic acid >> is a non-competitive inhibitor of [[ Acsl ]], as it reduces the maximal velocity of the reaction without changing the affinity of the substrate for the enzyme.


CONCLUSIONS: This study shows that << valproic acid >> acts as a non-competitive inhibitor of [[ brain microsomal Acsl ]], and that inhibition is substrate-selective.


On the other hand, holocarboxylase synthetase (<< HCS >>) mRNA levels were markedly low in the deficient animals, and increased upon [[ biotin ]] injection.


On the other hand, << holocarboxylase synthetase >> (HCS) mRNA levels were markedly low in the deficient animals, and increased upon [[ biotin ]] injection.


Involvement of << COX-1 >> and up-regulated prostaglandin E synthases in phosphatidylserine liposome-induced [[ prostaglandin E2 ]] production by microglia.


Involvement of COX-1 and up-regulated << prostaglandin E synthases >> in phosphatidylserine liposome-induced [[ prostaglandin E2 ]] production by microglia.


Furthermore, PS liposome-induced PGE2 production was significantly suppressed by << indomethacin >>, a preferential [[ COX-1 ]] inhibitor, but not by NS-398, a selective COX-2 inhibitor.


Furthermore, PS liposome-induced PGE2 production was significantly suppressed by indomethacin, a preferential COX-1 inhibitor, but not by << NS-398 >>, a selective [[ COX-2 ]] inhibitor.


These observations strongly suggest that the up-regulation of terminal << PGESs >> that are preferentially coupled with COX-1, especially mPGES-2, plays the pivotal role in PS liposome-induced [[ PGE2 ]] production by microglia.


These observations strongly suggest that the up-regulation of terminal PGESs that are preferentially coupled with << COX-1 >>, especially mPGES-2, plays the pivotal role in PS liposome-induced [[ PGE2 ]] production by microglia.


These observations strongly suggest that the up-regulation of terminal PGESs that are preferentially coupled with COX-1, especially << mPGES-2 >>, plays the pivotal role in PS liposome-induced [[ PGE2 ]] production by microglia.


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-<< kinase >> inhibitors (MKIs) [[ sorafenib ]], sunitinib, and AG013736, which target multiple VEGFRs as well as PDGFR-beta.


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-kinase inhibitors (MKIs) << sorafenib >>, sunitinib, and AG013736, which target multiple [[ VEGFRs ]] as well as PDGFR-beta.


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-kinase inhibitors (MKIs) << sorafenib >>, sunitinib, and AG013736, which target multiple VEGFRs as well as [[ PDGFR-beta ]].


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-<< kinase >> inhibitors (MKIs) sorafenib, [[ sunitinib ]], and AG013736, which target multiple VEGFRs as well as PDGFR-beta.


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-kinase inhibitors (MKIs) sorafenib, << sunitinib >>, and AG013736, which target multiple [[ VEGFRs ]] as well as PDGFR-beta.


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-kinase inhibitors (MKIs) sorafenib, << sunitinib >>, and AG013736, which target multiple VEGFRs as well as [[ PDGFR-beta ]].


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-<< kinase >> inhibitors (MKIs) sorafenib, sunitinib, and [[ AG013736 ]], which target multiple VEGFRs as well as PDGFR-beta.


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-kinase inhibitors (MKIs) sorafenib, sunitinib, and << AG013736 >>, which target multiple [[ VEGFRs ]] as well as PDGFR-beta.


Significant advances in the treatment of clear-cell RCC have been derived from agents that target these pathways, including the multiple-kinase inhibitors (MKIs) sorafenib, sunitinib, and << AG013736 >>, which target multiple VEGFRs as well as [[ PDGFR-beta ]].


<< Sorafenib >> has the added advantage of inhibiting multiple different [[ Raf ]] isoforms, which enables it to target TGF-alpha/EGFR signaling and may also enhance its inhibition of VEGFR and PDGFR-beta.


<< Sorafenib >> has the added advantage of inhibiting multiple different Raf isoforms, which enables it to target [[ TGF-alpha ]]/EGFR signaling and may also enhance its inhibition of VEGFR and PDGFR-beta.


<< Sorafenib >> has the added advantage of inhibiting multiple different Raf isoforms, which enables it to target TGF-alpha/[[ EGFR ]] signaling and may also enhance its inhibition of VEGFR and PDGFR-beta.


<< Sorafenib >> has the added advantage of inhibiting multiple different Raf isoforms, which enables it to target TGF-alpha/EGFR signaling and may also enhance its inhibition of [[ VEGFR ]] and PDGFR-beta.


<< Sorafenib >> has the added advantage of inhibiting multiple different Raf isoforms, which enables it to target TGF-alpha/EGFR signaling and may also enhance its inhibition of VEGFR and [[ PDGFR-beta ]].


Low << TS >> expression levels, cytoplasmic expression pattern and C SNP arose as variables associated to longer progression-free survival (PFS) in patients treated with [[ 5FU ]].


Therefore, in the present studies, animals were rendered tolerant to the << delta-opioid receptor >>-selective agonist [D-Pen2,D-Pen5]enkephalin ([[ DPDPE ]]), and receptor binding activities were measured.


Therefore, in the present studies, animals were rendered tolerant to the << delta-opioid receptor >>-selective agonist [[ [D-Pen2,D-Pen5]enkephalin ]] (DPDPE), and receptor binding activities were measured.


Our conclusion is that chronic << DPDPE >> treatment preferentially reduces [[ delta-opioid receptor ]] binding activity.


Complementary experiments using the 5-HT3-dependent Bezold-Jarisch reflex confirmed that << amoxapine >> really acts in vivo as a [[ 5-HT3 ]] antagonist (IC50 = 50 micrograms/kg i.v.), whereas amitriptyline is essentially inactive on 5-HT3 receptors.


Competitive radioligand binding assays were performed using cells expressing either the << human serotonin (5-HT) transporter >> (hSERT) or norepinephrine (NE) transporter (hNET) with K(i) values for [[ DVS ]] of 40.2 +/- 1.6 and 558.4 +/- 121.6 nM, respectively.


Competitive radioligand binding assays were performed using cells expressing either the human serotonin (5-HT) transporter (<< hSERT >>) or norepinephrine (NE) transporter (hNET) with K(i) values for [[ DVS ]] of 40.2 +/- 1.6 and 558.4 +/- 121.6 nM, respectively.


Competitive radioligand binding assays were performed using cells expressing either the human serotonin (5-HT) transporter (hSERT) or << norepinephrine (NE) transporter >> (hNET) with K(i) values for [[ DVS ]] of 40.2 +/- 1.6 and 558.4 +/- 121.6 nM, respectively.


Competitive radioligand binding assays were performed using cells expressing either the human serotonin (5-HT) transporter (hSERT) or norepinephrine (NE) transporter (<< hNET >>) with K(i) values for [[ DVS ]] of 40.2 +/- 1.6 and 558.4 +/- 121.6 nM, respectively.


Inhibition of << [3H]5-HT >> or [3H]NE uptake by DVS for the [[ hSERT ]] or hNET produced IC50 values of 47.3 +/- 19.4 and 531.3 +/- 113.0 nM, respectively.


Inhibition of [3H]5-HT or << [3H]NE >> uptake by DVS for the hSERT or [[ hNET ]] produced IC50 values of 47.3 +/- 19.4 and 531.3 +/- 113.0 nM, respectively.


To mimic chronic selective serotonin reuptake inhibitor treatment and to block the inhibitory 5-HT(1A) autoreceptors, a << 5-HT(1A) >> antagonist, [[ N-[2-[4-(2-methoxyphenyl)-1-piperazinyl]ethyl]-N-2-pyridinylcyclo hexanecarboxamide maleate salt ]] (WAY-100635) (0.3 mg/kg s.c.), was administered with DVS (30 mg/kg orally).


To mimic chronic selective serotonin reuptake inhibitor treatment and to block the inhibitory 5-HT(1A) autoreceptors, a << 5-HT(1A) >> antagonist, N-[2-[4-(2-methoxyphenyl)-1-piperazinyl]ethyl]-N-2-pyridinylcyclo hexanecarboxamide maleate salt ([[ WAY-100635 ]]) (0.3 mg/kg s.c.), was administered with DVS (30 mg/kg orally).


The tissue RA level is maintained through a cascade of metabolic reactions where << retinal dehydrogenases >> (RALDHs) catalyze the terminal reaction of [[ RA ]] biosynthesis from retinal, a rate-limiting step.


The tissue RA level is maintained through a cascade of metabolic reactions where retinal dehydrogenases (<< RALDHs >>) catalyze the terminal reaction of [[ RA ]] biosynthesis from retinal, a rate-limiting step.


The tissue RA level is maintained through a cascade of metabolic reactions where << retinal dehydrogenases >> (RALDHs) catalyze the terminal reaction of RA biosynthesis from [[ retinal ]], a rate-limiting step.


The tissue RA level is maintained through a cascade of metabolic reactions where retinal dehydrogenases (<< RALDHs >>) catalyze the terminal reaction of RA biosynthesis from [[ retinal ]], a rate-limiting step.


Further, << cholesterol >> metabolites, predominantly the oxysterols, the natural ligands for liver X receptor (LXR), induced these genes via upregulation of [[ sterol regulatory element binding protein-1c ]] (SREBP-1c) that bound to the regulatory regions of these genes.


Further, << cholesterol >> metabolites, predominantly the oxysterols, the natural ligands for liver X receptor (LXR), induced these genes via upregulation of sterol regulatory element binding protein-1c ([[ SREBP-1c ]]) that bound to the regulatory regions of these genes.


Further, cholesterol metabolites, predominantly the << oxysterols >>, the natural ligands for liver X receptor (LXR), induced these genes via upregulation of [[ sterol regulatory element binding protein-1c ]] (SREBP-1c) that bound to the regulatory regions of these genes.


Further, cholesterol metabolites, predominantly the << oxysterols >>, the natural ligands for liver X receptor (LXR), induced these genes via upregulation of sterol regulatory element binding protein-1c ([[ SREBP-1c ]]) that bound to the regulatory regions of these genes.


Hypermethlyation of << RELN and GAD67 promoters >> can be induced by treating mice with [[ methionine ]], and these mice display brain and behavioral abnormalities similar to +/rl.


Functional and bioenergetic consequences of << AT1 >> antagonist [[ olmesartan medoxomil ]] in hearts with postinfarction LV remodeling.


Thus, severe LV dysfunction and accompanying abnormal myocardial bioenergetic phenotype were prevented by the << AT1 >> antagonist [[ olmesartan medoxomil ]].


We evaluated << imatinib >>, a [[ tyrosine kinase ]] inhibitor currently used to treat chronic myelogenous leukemia and gastrointestinal stromal tumors, as a potential drug for systemic treatment of MTC, in 2 MTC-derived cell lines expressing multiple endocrine neoplasia-associated mutant RET receptors.


RESULTS: << Imatinib >> inhibited [[ RET ]] Y1062 phosphorylation in a dose-dependent manner after 1.5 hours of exposure.


RESULTS: << Imatinib >> inhibited RET [[ Y1062 ]] phosphorylation in a dose-dependent manner after 1.5 hours of exposure.


CONCLUSIONS: << Imatinib >> inhibits RET-mediated MTC cell growth affecting [[ RET ]] protein levels in vitro in a dose-dependent manner.


CONCLUSIONS: << Imatinib >> inhibits [[ RET ]]-mediated MTC cell growth affecting RET protein levels in vitro in a dose-dependent manner.


The concentration of << imatinib >> necessary to inhibit [[ RET ]] in vitro, however, makes it impossible to conclude that imatinib monotherapy will be a good option for systemic therapy of MTC.


In eukaryotes, the most prominent Mo-enzymes are (1) << sulfite oxidase >>, which catalyzes the final step in the degradation of [[ sulfur ]]-containing amino acids and is involved in detoxifying excess sulfite, (2) xanthine dehydrogenase, which is involved in purine catabolism and reactive oxygen production, (3) aldehyde oxidase, which oxidizes a variety of aldehydes and is essential for the biosynthesis of the phytohormone abscisic acid, and in autotrophic organisms also (4) nitrate reductase, which catalyzes the key step in inorganic nitrogen assimilation.


<< Retinoid >> is a collective term for compounds which bind to and activate retinoic acid receptors (RARalpha, beta, gamma and RXRalpha, beta, gamma), members of [[ nuclear hormone receptor ]] superfamily.


<< Retinoid >> is a collective term for compounds which bind to and activate [[ retinoic acid receptors ]] (RARalpha, beta, gamma and RXRalpha, beta, gamma), members of nuclear hormone receptor superfamily.


The cholesterol-lowering drug << simvastatin >> inhibits [[ LFA-1 ]] signaling by binding to an allosteric site on CD11a (LFA-1 alpha chain), which leads to immunomodulation.


<< Simvastatin >> abolished these anti-[[ CD11a ]] mAb-induced increases in lymphocytic cholinergic activity in a manner independent of its cholesterol-lowering activity.


<< Menthol >>, popularly known for its cooling effect, activates [[ TRPM8 ]]--a cold-activated thermoTRP ion channel.


<< Menthol >>, popularly known for its cooling effect, activates TRPM8--a cold-activated [[ thermoTRP ion channel ]].


However, human physiological studies demonstrate a paradoxical role of menthol in modulation of warm sensation, and here, we show that << menthol >> also activates heat-activated [[ TRPV3 ]].


We further show that << menthol >> inhibits [[ TRPA1 ]], potentially explaining the use of menthol as an analgesic.


Similar to << menthol >>, both camphor and cinnamaldehyde (initially reported to be specific activators of [[ TRPV3 ]] and TRPA1, respectively) also modulate other thermoTRPs.


Similar to << menthol >>, both camphor and cinnamaldehyde (initially reported to be specific activators of TRPV3 and [[ TRPA1 ]], respectively) also modulate other thermoTRPs.


Similar to menthol, both << camphor >> and cinnamaldehyde (initially reported to be specific activators of [[ TRPV3 ]] and TRPA1, respectively) also modulate other thermoTRPs.


Similar to menthol, both << camphor >> and cinnamaldehyde (initially reported to be specific activators of TRPV3 and [[ TRPA1 ]], respectively) also modulate other thermoTRPs.


Similar to menthol, both camphor and << cinnamaldehyde >> (initially reported to be specific activators of [[ TRPV3 ]] and TRPA1, respectively) also modulate other thermoTRPs.


Similar to menthol, both camphor and << cinnamaldehyde >> (initially reported to be specific activators of TRPV3 and [[ TRPA1 ]], respectively) also modulate other thermoTRPs.


The glutamate-aspartate transporter << GLAST >> mediates [[ glutamate ]] uptake at inner hair cell afferent synapses in the mammalian cochlea.


The << glutamate-aspartate transporter >> GLAST mediates [[ glutamate ]] uptake at inner hair cell afferent synapses in the mammalian cochlea.


Focal application of the transporter substrate D-aspartate elicited inward currents in IPCs, which were larger in the presence of anions that permeate the transporter-associated << anion channel >> and blocked by the transporter antagonist [[ D,L-threo-beta-benzyloxyaspartate ]].


These currents were produced by << glutamate-aspartate transporters >> (GLAST) (excitatory amino acid transporter 1) because they were weakly inhibited by [[ dihydrokainate ]], an antagonist of glutamate transporter-1 (excitatory amino acid transporter 2) and were absent from IPCs in GLAST-/- cochleas.


These currents were produced by glutamate-aspartate transporters (<< GLAST >>) (excitatory amino acid transporter 1) because they were weakly inhibited by [[ dihydrokainate ]], an antagonist of glutamate transporter-1 (excitatory amino acid transporter 2) and were absent from IPCs in GLAST-/- cochleas.


These currents were produced by glutamate-aspartate transporters (GLAST) (<< excitatory amino acid transporter 1 >>) because they were weakly inhibited by [[ dihydrokainate ]], an antagonist of glutamate transporter-1 (excitatory amino acid transporter 2) and were absent from IPCs in GLAST-/- cochleas.


These currents were produced by glutamate-aspartate transporters (GLAST) (excitatory amino acid transporter 1) because they were weakly inhibited by << dihydrokainate >>, an antagonist of [[ glutamate transporter-1 ]] (excitatory amino acid transporter 2) and were absent from IPCs in GLAST-/- cochleas.


These currents were produced by glutamate-aspartate transporters (GLAST) (excitatory amino acid transporter 1) because they were weakly inhibited by << dihydrokainate >>, an antagonist of glutamate transporter-1 ([[ excitatory amino acid transporter 2 ]]) and were absent from IPCs in GLAST-/- cochleas.


Furthermore, D-aspartate-induced currents in outside-out patches from IPCs exhibited larger steady-state currents than responses elicited by << L-glutamate >>, a prominent feature of [[ GLAST ]], and examination of cochlea from GLAST-Discosoma red (DsRed) promoter reporter mice revealed that DsRed expression was restricted to IPCs and other supporting cells surrounding IHCs.


Overexpression of << proline oxidase >> induces [[ proline ]]-dependent and mitochondria-mediated apoptosis.


<< Proline oxidase >> (POX), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of proline to [[ pyrroline- 5-carboxylate ]] (P5C).


Proline oxidase (<< POX >>), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of proline to [[ pyrroline- 5-carboxylate ]] (P5C).


<< Proline oxidase >> (POX), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of proline to pyrroline- 5-carboxylate ([[ P5C ]]).


Proline oxidase (<< POX >>), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of proline to pyrroline- 5-carboxylate ([[ P5C ]]).


<< Proline oxidase >> (POX), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of [[ proline ]] to pyrroline- 5-carboxylate (P5C).


Proline oxidase (<< POX >>), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of [[ proline ]] to pyrroline- 5-carboxylate (P5C).


To further investigate the molecular basis of POX-induced apoptosis, we utilized the DLD-1.POX cells to show that cells overproducing << POX >> exhibit an [[ L-proline ]]-dependent apoptotic response.


The apoptotic effect is specific for L-proline, detectable at 0.2 mM, maximal at 1 mM, and occurs during 48-72 h following the addition of << L-proline >> to cells with maximally induced [[ POX ]].


We conclude that in the presence of << proline >>, high [[ POX ]] activity is sufficient to induce mitochondria-mediated apoptosis.


The exception was << bupropion >>, a dual [[ norepinephrine transporter ]]/dopamine transporter blocker, which tended to increase spontaneous locomotor activity.


The exception was << bupropion >>, a dual norepinephrine transporter/[[ dopamine transporter ]] blocker, which tended to increase spontaneous locomotor activity.


Coadministration of reboxetine and the << dopamine transporter >> blocker [[ GBR 12909 ]] also increased spontaneous locomotor activity.


<< Tamoxifen >> blocks the action of estrogen by binding to the ER, and possesses both [[ ER ]]-agonist and antagonist properties.


<< Fulvestrant >> is a novel ER antagonist that destroys the [[ ER ]] and its signaling pathway and is not associated with tamoxifen-like agonist effects.


<< Fulvestrant >> is a novel [[ ER ]] antagonist that destroys the ER and its signaling pathway and is not associated with tamoxifen-like agonist effects.


<< Phosphodiesterase-5 >> (PDE5) contains a catalytic domain (C domain) that hydrolyzes [[ cGMP ]] and a regulatory domain (R domain) that contains two mammalian cGMP-binding phosphodiesterase, Anabaena adenylyl cyclases, Escherichia coli FhlAs (GAFs) (A and B) and a phosphorylation site for cyclic nucleotide-dependent protein kinases (cNPKs).


Phosphodiesterase-5 (<< PDE5 >>) contains a catalytic domain (C domain) that hydrolyzes [[ cGMP ]] and a regulatory domain (R domain) that contains two mammalian cGMP-binding phosphodiesterase, Anabaena adenylyl cyclases, Escherichia coli FhlAs (GAFs) (A and B) and a phosphorylation site for cyclic nucleotide-dependent protein kinases (cNPKs).


Binding of << cGMP >> to GAF-A increases [[ cNPK ]] phosphorylation of PDE5 and improves catalytic site affinity for cGMP or inhibitors.


Binding of << cGMP >> to GAF-A increases cNPK phosphorylation of [[ PDE5 ]] and improves catalytic site affinity for cGMP or inhibitors.


K(m) values of the mutants for << cGMP >> were similar to that of full-length [[ PDE5 ]].


<< Telmisartan >> downregulates angiotensin II type 1 receptor through activation of [[ peroxisome proliferator-activated receptor gamma ]].


<< Telmisartan >> downregulates [[ angiotensin II type 1 receptor ]] through activation of peroxisome proliferator-activated receptor gamma.


OBJECTIVE: << Telmisartan >>, an angiotensin II type 1 receptor (AT1R) antagonist, was found to have a unique property: it is a partial agonist of [[ peroxisome proliferator-activated receptor gamma ]] (PPARgamma).


OBJECTIVE: << Telmisartan >>, an angiotensin II type 1 receptor (AT1R) antagonist, was found to have a unique property: it is a partial agonist of peroxisome proliferator-activated receptor gamma ([[ PPARgamma ]]).


OBJECTIVE: << Telmisartan >>, an [[ angiotensin II type 1 receptor ]] (AT1R) antagonist, was found to have a unique property: it is a partial agonist of peroxisome proliferator-activated receptor gamma (PPARgamma).


OBJECTIVE: << Telmisartan >>, an angiotensin II type 1 receptor ([[ AT1R ]]) antagonist, was found to have a unique property: it is a partial agonist of peroxisome proliferator-activated receptor gamma (PPARgamma).


RESULTS: << Telmisartan >> decreased the expression of [[ AT1R ]] at the mRNA and protein levels in a dose- and time-dependent manner.


Decreased AT1R promoter activity with unchanged mRNA stability suggested that << telmisartan >> suppressed [[ AT1R ]] gene expression at the transcriptional level.


However, the expression of AT1R was not suppressed by other << AT1R >> antagonists such as [[ candesartan ]] or olmesartan.


However, the expression of AT1R was not suppressed by other << AT1R >> antagonists such as candesartan or [[ olmesartan ]].


Since the suppression of << AT1R >> expression was prevented by pretreatment with [[ GW9662 ]], a PPARgamma antagonist, PPARgamma should have participated in the process.


Since the suppression of AT1R expression was prevented by pretreatment with << GW9662 >>, a [[ PPARgamma ]] antagonist, PPARgamma should have participated in the process.


The deletion and mutation analysis of the << AT1R >> gene promoter indicated that a GC box located in the proximal promoter region is responsible for the [[ telmisartan ]]-induced downregulation.


The deletion and mutation analysis of the AT1R gene promoter indicated that a << GC box >> located in the proximal promoter region is responsible for the [[ telmisartan ]]-induced downregulation.


CONCLUSION: Our data provides a novel insight into an effect of telmisartan: << telmisartan >> inhibits AT1R gene expression through [[ PPARgamma ]] activation.


CONCLUSION: Our data provides a novel insight into an effect of telmisartan: << telmisartan >> inhibits [[ AT1R ]] gene expression through PPARgamma activation.


Upon differentiation, osteoclasts express << vesicular glutamate transporter 1 >> (VGLUT1), which is essential for vesicular storage and subsequent exocytosis of [[ glutamate ]] in neurons.


Upon differentiation, osteoclasts express vesicular glutamate transporter 1 (<< VGLUT1 >>), which is essential for vesicular storage and subsequent exocytosis of [[ glutamate ]] in neurons.


<< VGLUT1 >> is localized in transcytotic vesicles and accumulates [[ L-glutamate ]].


Synthesis, << dihydrofolate reductase >> inhibition, antitumor testing, and molecular modeling study of some new [[ 4(3H)-quinazolinone ]] analogs.


In order to produce potent new leads for anticancer drugs, a new series of quinazoline analogs was designed to resemble << methotrexate >> (MTX, 1) structure features and fitted with functional groups believed to enhance inhibition of [[ mammalian DHFR ]] activity.


In order to produce potent new leads for anticancer drugs, a new series of quinazoline analogs was designed to resemble methotrexate (<< MTX >>, 1) structure features and fitted with functional groups believed to enhance inhibition of [[ mammalian DHFR ]] activity.


In order to produce potent new leads for anticancer drugs, a new series of << quinazoline >> analogs was designed to resemble methotrexate (MTX, 1) structure features and fitted with functional groups believed to enhance inhibition of [[ mammalian DHFR ]] activity.


A significant positive correlation was found between dietary intake of total SFAs and total MUFAs and expression of PBMC D6D and D5D genes, but a significant negative correlation between dietary intake of << linoleic acid >> (LA) and alpha-linolenic acid (LNA) and the expression of PBMC [[ D6D ]] and D5D genes.


A significant positive correlation was found between dietary intake of total SFAs and total MUFAs and expression of PBMC D6D and D5D genes, but a significant negative correlation between dietary intake of << linoleic acid >> (LA) and alpha-linolenic acid (LNA) and the expression of PBMC D6D and [[ D5D ]] genes.


A significant positive correlation was found between dietary intake of total SFAs and total MUFAs and expression of PBMC D6D and D5D genes, but a significant negative correlation between dietary intake of linoleic acid (<< LA >>) and alpha-linolenic acid (LNA) and the expression of PBMC [[ D6D ]] and D5D genes.


A significant positive correlation was found between dietary intake of total SFAs and total MUFAs and expression of PBMC D6D and D5D genes, but a significant negative correlation between dietary intake of linoleic acid (<< LA >>) and alpha-linolenic acid (LNA) and the expression of PBMC D6D and [[ D5D ]] genes.


A significant positive correlation was found between dietary intake of total SFAs and total MUFAs and expression of PBMC D6D and D5D genes, but a significant negative correlation between dietary intake of linoleic acid (LA) and << alpha-linolenic acid >> (LNA) and the expression of PBMC [[ D6D ]] and D5D genes.


A significant positive correlation was found between dietary intake of total SFAs and total MUFAs and expression of PBMC D6D and D5D genes, but a significant negative correlation between dietary intake of linoleic acid (LA) and << alpha-linolenic acid >> (LNA) and the expression of PBMC D6D and [[ D5D ]] genes.


A significant positive correlation was found between dietary intake of total SFAs and total MUFAs and expression of PBMC D6D and D5D genes, but a significant negative correlation between dietary intake of linoleic acid (LA) and alpha-linolenic acid (<< LNA >>) and the expression of PBMC [[ D6D ]] and D5D genes.


A significant positive correlation was found between dietary intake of total SFAs and total MUFAs and expression of PBMC D6D and D5D genes, but a significant negative correlation between dietary intake of linoleic acid (LA) and alpha-linolenic acid (<< LNA >>) and the expression of PBMC D6D and [[ D5D ]] genes.


CONCLUSION: Intake of high << SFAs >> and MUFAs appears to increase expression of PBMC [[ D6D ]] and D5D genes, whilst high EFAs intake appears to decrease expression of PBMC D6D and D5D genes.


CONCLUSION: Intake of high << SFAs >> and MUFAs appears to increase expression of PBMC D6D and [[ D5D ]] genes, whilst high EFAs intake appears to decrease expression of PBMC D6D and D5D genes.


CONCLUSION: Intake of high SFAs and << MUFAs >> appears to increase expression of PBMC [[ D6D ]] and D5D genes, whilst high EFAs intake appears to decrease expression of PBMC D6D and D5D genes.


CONCLUSION: Intake of high SFAs and << MUFAs >> appears to increase expression of PBMC D6D and [[ D5D ]] genes, whilst high EFAs intake appears to decrease expression of PBMC D6D and D5D genes.


CONCLUSION: Intake of high SFAs and MUFAs appears to increase expression of PBMC D6D and D5D genes, whilst high << EFAs >> intake appears to decrease expression of PBMC [[ D6D ]] and D5D genes.


CONCLUSION: Intake of high SFAs and MUFAs appears to increase expression of PBMC D6D and D5D genes, whilst high << EFAs >> intake appears to decrease expression of PBMC D6D and [[ D5D ]] genes.


<< Decitabine >> inhibits [[ DNA methyltransferase ]] and has shown therapeutic effects in patients with hematologic malignancies.


Our data suggest that << l-arginine >> is taken up by Sertoli cells and peritubular cells, principally via system y(+)L ([[ SLC3A2 ]]/SLC7A6) and system y(+) (SLC7A1 and SLC7A2), with system B(0+) making a minor contribution.


KIEs were measured on the arsenolysis of << 5'-methylthioadenosine >> (MTA) catalyzed by [[ MTAP ]] and were corrected for the forward commitment to catalysis.


KIEs were measured on the arsenolysis of 5'-methylthioadenosine (<< MTA >>) catalyzed by [[ MTAP ]] and were corrected for the forward commitment to catalysis.


During embryogenesis, lratb is expressed in mostly non-overlapping domains opposite to << retinal dehydrogenase 2 >> (raldh2), the key enzyme for [[ retinoic acid ]] synthesis.


During embryogenesis, lratb is expressed in mostly non-overlapping domains opposite to retinal dehydrogenase 2 (<< raldh2 >>), the key enzyme for [[ retinoic acid ]] synthesis.


Blocking << retinyl ester >> formation by a targeted knock down of [[ Lratb ]] results in significantly increased retinoic acid levels, which lead to severe embryonic patterning defects.


<< ADP >> initiates platelet aggregation by 'simultaneous activation of two [[ G protein-coupled receptors ]], P2Y1 and P2Y12.


<< ADP >> initiates platelet aggregation by 'simultaneous activation of two G protein-coupled receptors, [[ P2Y1 ]] and P2Y12.


<< ADP >> initiates platelet aggregation by 'simultaneous activation of two G protein-coupled receptors, P2Y1 and [[ P2Y12 ]].


Our results imply that << P2Y12 >> has the potential to be inhibited by [[ ADP ]]/ATP analogs, and it suggests that P2Y12 acts as a target of new drugs that inhibit platelet aggregation.


Our results imply that << P2Y12 >> has the potential to be inhibited by ADP/[[ ATP ]] analogs, and it suggests that P2Y12 acts as a target of new drugs that inhibit platelet aggregation.


<< Cd >> decreased [[ ERalpha ]] expression, but not ERbeta.


<< Cd >> also increased ERK1/2, [[ Akt ]] and PDGFRalpha phosphorylation while ICI blocked it.


<< Cd >> also increased ERK1/2, Akt and [[ PDGFRalpha ]] phosphorylation while ICI blocked it.


<< Cd >> rapidly increased [[ c-jun ]], c-fos and PDGFA expression.


<< Cd >> rapidly increased c-jun, [[ c-fos ]] and PDGFA expression.


<< Cd >> rapidly increased c-jun, c-fos and [[ PDGFA ]] expression.


In conclusion, our results indicate that << Cd >> increases BC cell proliferation in vitro by stimulating [[ Akt ]], ERK1/2 and PDGFRalpha kinases activity likely by activating c-fos, c-jun and PDGFA by an ERalpha-dependent mechanism.


In conclusion, our results indicate that << Cd >> increases BC cell proliferation in vitro by stimulating Akt, ERK1/2 and [[ PDGFRalpha ]] kinases activity likely by activating c-fos, c-jun and PDGFA by an ERalpha-dependent mechanism.


In conclusion, our results indicate that << Cd >> increases BC cell proliferation in vitro by stimulating Akt, ERK1/2 and PDGFRalpha [[ kinases ]] activity likely by activating c-fos, c-jun and PDGFA by an ERalpha-dependent mechanism.


In conclusion, our results indicate that << Cd >> increases BC cell proliferation in vitro by stimulating Akt, ERK1/2 and PDGFRalpha kinases activity likely by activating [[ c-fos ]], c-jun and PDGFA by an ERalpha-dependent mechanism.


In conclusion, our results indicate that << Cd >> increases BC cell proliferation in vitro by stimulating Akt, ERK1/2 and PDGFRalpha kinases activity likely by activating c-fos, [[ c-jun ]] and PDGFA by an ERalpha-dependent mechanism.


In conclusion, our results indicate that << Cd >> increases BC cell proliferation in vitro by stimulating Akt, ERK1/2 and PDGFRalpha kinases activity likely by activating c-fos, c-jun and [[ PDGFA ]] by an ERalpha-dependent mechanism.


Gonadotropin-releasing hormone functionally antagonizes << testosterone >> activation of the [[ human androgen receptor ]] in prostate cells through focal adhesion complexes involving Hic-5.


<< Gonadotropin-releasing hormone >> functionally antagonizes testosterone activation of the [[ human androgen receptor ]] in prostate cells through focal adhesion complexes involving Hic-5.


<< GnRH >>-induced [[ Pyk2 ]] activation opposed the association of Hic-5 with androgen receptor as overexpression of a dominant negative Pyk2 enhanced the GnRH-induced nuclear translocation of a green fluorescent protein-tagged human androgen receptor.


<< GnRH >>-induced Pyk2 activation opposed the association of [[ Hic-5 ]] with androgen receptor as overexpression of a dominant negative Pyk2 enhanced the GnRH-induced nuclear translocation of a green fluorescent protein-tagged human androgen receptor.


<< GnRH >>-induced Pyk2 activation opposed the association of Hic-5 with [[ androgen receptor ]] as overexpression of a dominant negative Pyk2 enhanced the GnRH-induced nuclear translocation of a green fluorescent protein-tagged human androgen receptor.


<< GnRH >>-induced [[ c-Src ]] activation resulted in the phosphorylation of expressed Hic-5 and promoted its association with the human androgen receptor.


In contrast to << testosterone >>, GnRH-induced nuclear translocation did not transcriptionally activate the [[ androgen receptor ]].


The discovery that << METH >> and AMPH activate the [[ rTAAR1 ]] motivated us to study the effect of these drugs on the mouse TAAR1 (mTAAR1) and a human-rat chimera (hrChTAAR1).


The discovery that METH and << AMPH >> activate the [[ rTAAR1 ]] motivated us to study the effect of these drugs on the mouse TAAR1 (mTAAR1) and a human-rat chimera (hrChTAAR1).


Furthermore, because S-(+)-isomers of << METH >> and AMPH are reported to be more potent and efficacious in vivo than R-(-), we determined the enantiomeric selectivity of all three species of [[ TAAR1 ]].


Furthermore, because S-(+)-isomers of METH and << AMPH >> are reported to be more potent and efficacious in vivo than R-(-), we determined the enantiomeric selectivity of all three species of [[ TAAR1 ]].


EC50 values for << S-(+)-METH >> were 0.89, 0.92, and 4.44 microM for [[ rTAAR1 ]], mTAAR1, and h-rChTAAR1, respectively.


EC50 values for << S-(+)-METH >> were 0.89, 0.92, and 4.44 microM for rTAAR1, [[ mTAAR1 ]], and h-rChTAAR1, respectively.


EC50 values for << S-(+)-METH >> were 0.89, 0.92, and 4.44 microM for rTAAR1, mTAAR1, and [[ h-rChTAAR1 ]], respectively.


<< PEA >> was a potent and full agonist at each species of [[ TAAR1 ]], whereas TYR was a full agonist for the rodent TAAR1s but was a partial agonist at h-rChTAAR1.


PEA was a potent and full agonist at each species of TAAR1, whereas << TYR >> was a full agonist for the [[ rodent TAAR1s ]] but was a partial agonist at h-rChTAAR1.


PEA was a potent and full agonist at each species of TAAR1, whereas << TYR >> was a full agonist for the rodent TAAR1s but was a partial agonist at [[ h-rChTAAR1 ]].


Interestingly, both isomers of << METH >> were full agonists at [[ mTAAR1 ]] and h-rChTAAR1, whereas both were partial agonists at rTAAR1.


Interestingly, both isomers of << METH >> were full agonists at mTAAR1 and [[ h-rChTAAR1 ]], whereas both were partial agonists at rTAAR1.


Interestingly, both isomers of << METH >> were full agonists at mTAAR1 and h-rChTAAR1, whereas both were partial agonists at [[ rTAAR1 ]].


Finally, we showed that << chlorate >> activated endocrine cell development by inducing [[ neurogenin 3 ]] (Neurog3) expression in early endocrine progenitor cells.


Finally, we showed that << chlorate >> activated endocrine cell development by inducing neurogenin 3 ([[ Neurog3 ]]) expression in early endocrine progenitor cells.


DNA cloning, characterization, and inhibition studies of the << human secretory isoform VI >>, a new target for [[ sulfonamide ]] and sulfamate inhibitors.


DNA cloning, characterization, and inhibition studies of the << human secretory isoform VI >>, a new target for sulfonamide and [[ sulfamate ]] inhibitors.


The kinetic parameters for the << CO2 >> hydration reaction proved [[ hCA VI ]] to possess a kcat of 3.4 x 10(5) s-1 and kcat/KM of 4.9 x 10(7) M-1 s-1 (at pH 7.5 and 20 degrees C). hCA VI has a significant catalytic activity for the physiological reaction on the same order of magnitude as the ubiquitous isoform CA I or the transmembrane, tumor-associated isozyme CA IX.


Some clinically used compounds, such as acetazolamide, methazolamide, ethoxzolamide, << dichlorophenamide >>, dorzolamide, brinzolamide, topiramate, sulpiride, and indisulam, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as << acetazolamide >>, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide, topiramate, sulpiride, and indisulam, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as acetazolamide, << methazolamide >>, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide, topiramate, sulpiride, and indisulam, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as acetazolamide, methazolamide, << ethoxzolamide >>, dichlorophenamide, dorzolamide, brinzolamide, topiramate, sulpiride, and indisulam, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, << dorzolamide >>, brinzolamide, topiramate, sulpiride, and indisulam, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, << brinzolamide >>, topiramate, sulpiride, and indisulam, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide, << topiramate >>, sulpiride, and indisulam, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide, topiramate, << sulpiride >>, and indisulam, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide, topiramate, sulpiride, and << indisulam >>, or the orphan drug benzolamide, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


Some clinically used compounds, such as acetazolamide, methazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, brinzolamide, topiramate, sulpiride, and indisulam, or the orphan drug << benzolamide >>, showed effective [[ hCA VI ]] inhibitory activity, with inhibition constants of 0.8-79 nM.


The best inhibitors were << brinzolamide >> and sulpiride (KI values of 0.8-0.9 nM), the latter compound being also a [[ CA VI ]]-selective inhibitor.


The best inhibitors were brinzolamide and << sulpiride >> (KI values of 0.8-0.9 nM), the latter compound being also a [[ CA VI ]]-selective inhibitor.


The metallic taste reported as a side effect after the treatment with systemic << sulfonamides >> may be due to the inhibition of the [[ salivary CA VI ]].


Some of the compounds investigated in this study might be used as additives in toothpastes for reducing the acidification produced by the relevant << CO2 >> hydrase activity of enamel [[ CA VI ]], which leads to the formation of protons and bicarbonate and may have a role in cariogenesis.


Some of the compounds investigated in this study might be used as additives in toothpastes for reducing the acidification produced by the relevant CO2 hydrase activity of enamel << CA VI >>, which leads to the formation of protons and [[ bicarbonate ]] and may have a role in cariogenesis.


Transmembrane isoforms of << adenylate cyclases >> (AC) integrate a wide variety of extracellular signals from neurotransmitters to morphogens and can also regulate [[ cAMP ]] production in response to calcium entry.


Transmembrane isoforms of adenylate cyclases (<< AC >>) integrate a wide variety of extracellular signals from neurotransmitters to morphogens and can also regulate [[ cAMP ]] production in response to calcium entry.


<< Pirfenidone >> inhibits [[ TGF-beta ]] expression in malignant glioma cells.


Here, we report that the antifibrotic drug << 5-methyl-1-phenyl-2-(1H)-pyridone >> (pirfenidone, PFD) elicits growth-inhibitory effects and reduces [[ TGF-beta2 ]] protein levels in human glioma cell lines.


Here, we report that the antifibrotic drug 5-methyl-1-phenyl-2-(1H)-pyridone (<< pirfenidone >>, PFD) elicits growth-inhibitory effects and reduces [[ TGF-beta2 ]] protein levels in human glioma cell lines.


Here, we report that the antifibrotic drug 5-methyl-1-phenyl-2-(1H)-pyridone (pirfenidone, << PFD >>) elicits growth-inhibitory effects and reduces [[ TGF-beta2 ]] protein levels in human glioma cell lines.


This reduction in << TGF-beta2 >> is biologically relevant since [[ PFD ]] treatment reduces the growth inhibition of TGF-beta-sensitive CCL-64 cells mediated by conditioned media of glioma cells.


This reduction in TGF-beta2 is biologically relevant since << PFD >> treatment reduces the growth inhibition of [[ TGF-beta ]]-sensitive CCL-64 cells mediated by conditioned media of glioma cells.


<< PFD >> leads to a reduction of [[ TGF-beta2 ]] mRNA levels and of the mature TGF-beta2 protein due to decreased expression and direct inhibition of the TGF-beta pro-protein convertase furin.


<< PFD >> leads to a reduction of TGF-beta2 mRNA levels and of the mature [[ TGF-beta2 ]] protein due to decreased expression and direct inhibition of the TGF-beta pro-protein convertase furin.


<< PFD >> leads to a reduction of TGF-beta2 mRNA levels and of the mature TGF-beta2 protein due to decreased expression and direct inhibition of the [[ TGF-beta ]] pro-protein convertase furin.


<< PFD >> leads to a reduction of TGF-beta2 mRNA levels and of the mature TGF-beta2 protein due to decreased expression and direct inhibition of the TGF-beta [[ pro-protein convertase ]] furin.


<< PFD >> leads to a reduction of TGF-beta2 mRNA levels and of the mature TGF-beta2 protein due to decreased expression and direct inhibition of the TGF-beta pro-protein convertase [[ furin ]].


In addition, << PFD >> reduces the protein levels of the [[ matrix metalloproteinase (MMP)-11 ]], a TGF-beta target gene and furin substrate involved in carcinogenesis.


In addition, << PFD >> reduces the protein levels of the matrix metalloproteinase (MMP)-11, a [[ TGF-beta ]] target gene and furin substrate involved in carcinogenesis.


UNLABELLED: << Bile acid-coenzyme A:amino acid N-acyltransferase >> (BAAT) is the sole enzyme responsible for conjugation of primary and secondary bile acids to [[ taurine ]] and glycine.


UNLABELLED: Bile acid-coenzyme A:amino acid N-acyltransferase (<< BAAT >>) is the sole enzyme responsible for conjugation of primary and secondary bile acids to [[ taurine ]] and glycine.


UNLABELLED: << Bile acid-coenzyme A:amino acid N-acyltransferase >> (BAAT) is the sole enzyme responsible for conjugation of primary and secondary bile acids to taurine and [[ glycine ]].


UNLABELLED: Bile acid-coenzyme A:amino acid N-acyltransferase (<< BAAT >>) is the sole enzyme responsible for conjugation of primary and secondary bile acids to taurine and [[ glycine ]].


UNLABELLED: << Bile acid-coenzyme A:amino acid N-acyltransferase >> (BAAT) is the sole enzyme responsible for conjugation of primary and secondary [[ bile acids ]] to taurine and glycine.


UNLABELLED: Bile acid-coenzyme A:amino acid N-acyltransferase (<< BAAT >>) is the sole enzyme responsible for conjugation of primary and secondary [[ bile acids ]] to taurine and glycine.


The absence or presence of a cytosolic pool of << BAAT >> has important implications for the intracellular transport of unconjugated/deconjugated [[ bile salts ]].


The recombinant strains of the flavinogenic yeast Candida famata, which contain the DNA fragment consisting of the FMN1 gene (encoding the << riboflavin kinase >>, enzyme that converts riboflavin to [[ flavinmononucleotide ]]) driven by the strong promoters (the regulated RIB1 or constitutive TEF1 promoter) were isolated.


The recombinant strains of the flavinogenic yeast Candida famata, which contain the DNA fragment consisting of the FMN1 gene (encoding the << riboflavin kinase >>, enzyme that converts [[ riboflavin ]] to flavinmononucleotide) driven by the strong promoters (the regulated RIB1 or constitutive TEF1 promoter) were isolated.


Mechanism of the irreversible inactivation of << mouse ornithine decarboxylase >> by [[ alpha-difluoromethylornithine ]].


<< Mouse ornithine decarboxylase >> (ODC) was expressed in Escherichia coli and the purified recombinant enzyme used for determination of the binding site for pyridoxal 5'-phosphate and of the residues modified in the inactivation of the enzyme by the enzyme-activated irreversible inhibitor, [[ alpha-difluoromethylornithine ]] (DFMO).


Mouse ornithine decarboxylase (<< ODC >>) was expressed in Escherichia coli and the purified recombinant enzyme used for determination of the binding site for pyridoxal 5'-phosphate and of the residues modified in the inactivation of the enzyme by the enzyme-activated irreversible inhibitor, [[ alpha-difluoromethylornithine ]] (DFMO).


<< Mouse ornithine decarboxylase >> (ODC) was expressed in Escherichia coli and the purified recombinant enzyme used for determination of the binding site for pyridoxal 5'-phosphate and of the residues modified in the inactivation of the enzyme by the enzyme-activated irreversible inhibitor, alpha-difluoromethylornithine ([[ DFMO ]]).


Mouse ornithine decarboxylase (<< ODC >>) was expressed in Escherichia coli and the purified recombinant enzyme used for determination of the binding site for pyridoxal 5'-phosphate and of the residues modified in the inactivation of the enzyme by the enzyme-activated irreversible inhibitor, alpha-difluoromethylornithine ([[ DFMO ]]).


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the [[ neutral amino acid transporters ]] of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the [[ solute carrier 1 ]] [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [[[ SLC1 ]], alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, [[ alanine serine cysteine transporter 1 ]] (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 ([[ ASCT1 ]]), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and [[ ASCT2 ]]] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and [[ SLC38 ]] families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [[[ sodium-coupled neutral amino acid transporter 1 ]] (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 ([[ SNAT1 ]]), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), [[ SNAT2 ]], and SNAT4].


Na+-Dependent transmembrane transport of small neutral << amino acids >>, such as glutamine and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and [[ SNAT4 ]]].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the [[ neutral amino acid transporters ]] of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the [[ solute carrier 1 ]] [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [[[ SLC1 ]], alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, [[ alanine serine cysteine transporter 1 ]] (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 ([[ ASCT1 ]]), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and [[ ASCT2 ]]] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and [[ SLC38 ]] families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [[[ sodium-coupled neutral amino acid transporter 1 ]] (SNAT1), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 ([[ SNAT1 ]]), SNAT2, and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), [[ SNAT2 ]], and SNAT4].


Na+-Dependent transmembrane transport of small neutral amino acids, such as << glutamine >> and alanine, is mediated, among others, by the neutral amino acid transporters of the solute carrier 1 [SLC1, alanine serine cysteine transporter 1 (ASCT1), and ASCT2] and SLC38 families [sodium-coupled neutral amino acid transporter 1 (SNAT1), SNAT2, and [[ SNAT4 ]]].