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 ]]].


Here, we describe a new photolabile << alanine >> derivative based on protection of alanine with the 4-methoxy-7-nitroindolinyl (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by [[ ASCT2 ]], SNAT1, and SNAT2.


Here, we describe a new photolabile << alanine >> derivative based on protection of alanine with the 4-methoxy-7-nitroindolinyl (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by ASCT2, [[ SNAT1 ]], and SNAT2.


Here, we describe a new photolabile << alanine >> derivative based on protection of alanine with the 4-methoxy-7-nitroindolinyl (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by ASCT2, SNAT1, and [[ SNAT2 ]].


Here, we describe a new photolabile alanine derivative based on protection of << alanine >> with the 4-methoxy-7-nitroindolinyl (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by [[ ASCT2 ]], SNAT1, and SNAT2.


Here, we describe a new photolabile alanine derivative based on protection of << alanine >> with the 4-methoxy-7-nitroindolinyl (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by ASCT2, [[ SNAT1 ]], and SNAT2.


Here, we describe a new photolabile alanine derivative based on protection of << alanine >> with the 4-methoxy-7-nitroindolinyl (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by ASCT2, SNAT1, and [[ SNAT2 ]].


Here, we describe a new photolabile alanine derivative based on protection of alanine with the << 4-methoxy-7-nitroindolinyl >> (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by [[ ASCT2 ]], SNAT1, and SNAT2.


Here, we describe a new photolabile alanine derivative based on protection of alanine with the << 4-methoxy-7-nitroindolinyl >> (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by ASCT2, [[ SNAT1 ]], and SNAT2.


Here, we describe a new photolabile alanine derivative based on protection of alanine with the << 4-methoxy-7-nitroindolinyl >> (MNI) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by ASCT2, SNAT1, and [[ SNAT2 ]].


Here, we describe a new photolabile alanine derivative based on protection of alanine with the 4-methoxy-7-nitroindolinyl (<< MNI >>) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by [[ ASCT2 ]], SNAT1, and SNAT2.


Here, we describe a new photolabile alanine derivative based on protection of alanine with the 4-methoxy-7-nitroindolinyl (<< MNI >>) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by ASCT2, [[ SNAT1 ]], and SNAT2.


Here, we describe a new photolabile alanine derivative based on protection of alanine with the 4-methoxy-7-nitroindolinyl (<< MNI >>) caging group, which we use for pre-steady-state kinetic analysis of alanine transport by ASCT2, SNAT1, and [[ SNAT2 ]].


Stimulated << P-selectin >> and integrin alpha(IIb)beta(3) expression were also higher in the upper tertile both before and after [[ aspirin ]].


Stimulated P-selectin and << integrin alpha(IIb)beta(3) >> expression were also higher in the upper tertile both before and after [[ aspirin ]].


At least 4 h of estrogen pre-treatment was required to elicit protection, an effect that was blocked by the << ER >> antagonist, [[ ICI 182,780 ]].


Moreover, ERalpha mediated the protection afforded by estrogen since only the ERalpha agonist, HPTE, but not the << ERbeta >> agonist, [[ DPN ]], protected against dopamine cell loss.


Differential activation of << cAMP response element binding protein >> in discrete nucleus accumbens subregions during early and late [[ cocaine ]] sensitization.


The present study examined the differential << cocaine >>-induced activation of the cyclic adenosine monophosphate (cAMP) response element binding protein ([[ CREB ]]) throughout discrete zones of analysis of the nucleus accumbens (NAc) in rats.


The present study examined the differential << cocaine >>-induced activation of the [[ cyclic adenosine monophosphate (cAMP) response element binding protein ]] (CREB) throughout discrete zones of analysis of the nucleus accumbens (NAc) in rats.


Using immunohistochemistry, the authors analyzed changes in << CREB >> phosphorylation in the NAc after 5 days of [[ cocaine ]], a short or long drug-free period, and a subsequent challenge injection.


Repeated << cocaine >> resulted in [[ CREB ]] phosphorylation in all analyzed subregions of the NAc excluding the most ventrolateral region of the shell 2 weeks after cessation of repeated cocaine, but rats challenged after 2 drug-free days yielded a more localized activation of CREB in the 3 most dorsomedial zones of the shell.


Repeated cocaine resulted in CREB phosphorylation in all analyzed subregions of the NAc excluding the most ventrolateral region of the shell 2 weeks after cessation of repeated << cocaine >>, but rats challenged after 2 drug-free days yielded a more localized activation of [[ CREB ]] in the 3 most dorsomedial zones of the shell.


The temporal and anatomical determinants of << cocaine >>-induced [[ CREB ]] activity may indicate functional differences among NAc shell subregions and suggest the involvement of CREB in early and late cocaine effects.


The carboxylation of glutamic acid residues to << gamma-carboxyglutamic acid >> (Gla) by the [[ vitamin K-dependent gamma-glutamyl carboxylase ]] (gamma-carboxylase) is an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation.


The carboxylation of glutamic acid residues to << gamma-carboxyglutamic acid >> (Gla) by the vitamin K-dependent gamma-glutamyl carboxylase ([[ gamma-carboxylase ]]) is an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation.


The carboxylation of glutamic acid residues to gamma-carboxyglutamic acid (<< Gla >>) by the [[ vitamin K-dependent gamma-glutamyl carboxylase ]] (gamma-carboxylase) is an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation.


The carboxylation of glutamic acid residues to gamma-carboxyglutamic acid (<< Gla >>) by the vitamin K-dependent gamma-glutamyl carboxylase ([[ gamma-carboxylase ]]) is an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation.


The carboxylation of << glutamic acid >> residues to gamma-carboxyglutamic acid (Gla) by the [[ vitamin K-dependent gamma-glutamyl carboxylase ]] (gamma-carboxylase) is an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation.


The carboxylation of << glutamic acid >> residues to gamma-carboxyglutamic acid (Gla) by the vitamin K-dependent gamma-glutamyl carboxylase ([[ gamma-carboxylase ]]) is an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation.


We posed the following questions: (1) Do cholangiocytes express H3R? (2) Does in vivo administration of << (R)-(alpha)-(-)-methylhistamine dihydrobromide >> (RAMH) ([[ H3R ]] agonist), thioperamide maleate (H3R antagonist) or histamine, in the absence/presence of thioperamide maleate, to bile duct ligated (BDL) rats regulate cholangiocyte proliferation? and (3) Does RAMH inhibit cholangiocyte proliferation by downregulation of cAMP-dependent phosphorylation of protein kinase A (PKA)/extracellular signal-regulated kinase 1/2 (ERK1/2)/ets-like gene-1 (Elk-1)? The expression of H3R was evaluated in liver sections by immunohistochemistry and immunofluorescence, and by real-time PCR in cholangiocyte RNA from normal and BDL rats.


We posed the following questions: (1) Do cholangiocytes express H3R? (2) Does in vivo administration of (R)-(alpha)-(-)-methylhistamine dihydrobromide (<< RAMH >>) ([[ H3R ]] agonist), thioperamide maleate (H3R antagonist) or histamine, in the absence/presence of thioperamide maleate, to bile duct ligated (BDL) rats regulate cholangiocyte proliferation? and (3) Does RAMH inhibit cholangiocyte proliferation by downregulation of cAMP-dependent phosphorylation of protein kinase A (PKA)/extracellular signal-regulated kinase 1/2 (ERK1/2)/ets-like gene-1 (Elk-1)? The expression of H3R was evaluated in liver sections by immunohistochemistry and immunofluorescence, and by real-time PCR in cholangiocyte RNA from normal and BDL rats.


We posed the following questions: (1) Do cholangiocytes express H3R? (2) Does in vivo administration of (R)-(alpha)-(-)-methylhistamine dihydrobromide (RAMH) (H3R agonist), << thioperamide maleate >> ([[ H3R ]] antagonist) or histamine, in the absence/presence of thioperamide maleate, to bile duct ligated (BDL) rats regulate cholangiocyte proliferation? and (3) Does RAMH inhibit cholangiocyte proliferation by downregulation of cAMP-dependent phosphorylation of protein kinase A (PKA)/extracellular signal-regulated kinase 1/2 (ERK1/2)/ets-like gene-1 (Elk-1)? The expression of H3R was evaluated in liver sections by immunohistochemistry and immunofluorescence, and by real-time PCR in cholangiocyte RNA from normal and BDL rats.


<< RAMH >> inhibition of cholangiocyte growth was associated with decreased cAMP levels and [[ PKA ]]/ERK1/2/Elk-1 phosphorylation.


<< RAMH >> inhibition of cholangiocyte growth was associated with decreased cAMP levels and PKA/[[ ERK1/2 ]]/Elk-1 phosphorylation.


<< RAMH >> inhibition of cholangiocyte growth was associated with decreased cAMP levels and PKA/ERK1/2/[[ Elk-1 ]] phosphorylation.


<< Proline dehydrogenase >> (PRODH) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) catalyze the two-step oxidation of proline to [[ glutamate ]].


Proline dehydrogenase (<< PRODH >>) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) catalyze the two-step oxidation of proline to [[ glutamate ]].


Proline dehydrogenase (PRODH) and << Delta(1)-pyrroline-5-carboxylate dehydrogenase >> (P5CDH) catalyze the two-step oxidation of proline to [[ glutamate ]].


Proline dehydrogenase (PRODH) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (<< P5CDH >>) catalyze the two-step oxidation of proline to [[ glutamate ]].


<< Proline dehydrogenase >> (PRODH) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) catalyze the two-step oxidation of [[ proline ]] to glutamate.


Proline dehydrogenase (<< PRODH >>) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) catalyze the two-step oxidation of [[ proline ]] to glutamate.


Proline dehydrogenase (PRODH) and << Delta(1)-pyrroline-5-carboxylate dehydrogenase >> (P5CDH) catalyze the two-step oxidation of [[ proline ]] to glutamate.


Proline dehydrogenase (PRODH) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (<< P5CDH >>) catalyze the two-step oxidation of [[ proline ]] to glutamate.


Finally, we demonstrate that << T. thermophilus PRODH >> reacts with O(2) producing [[ superoxide ]].


Finally, we demonstrate that << T. thermophilus PRODH >> reacts with [[ O(2) ]] producing superoxide.


This is significant because << superoxide >> production underlies the role of [[ human PRODH ]] in p53-mediated apoptosis, implying commonalities between eukaryotic and bacterial monofunctional PRODHs.


The << phosphodiesterase (PDE) 4 >> is the predominant [[ cyclic AMP ]] degrading enzyme in a variety of inflammatory cells including eosinophils, neutrophils, macrophages, T cells and monocytes.


Consequently, << PDE4 >> inhibitors including [[ cilomilast ]] and AWD 12-281 have been tested in several models of allergic and irritant skin inflammation.


Consequently, << PDE4 >> inhibitors including cilomilast and [[ AWD 12-281 ]] have been tested in several models of allergic and irritant skin inflammation.


Results of early clinical trials with both topically (<< cipamfylline >>, CP80,633) and systemically (CC-10004) active [[ PDE4 ]] inhibitors demonstrated efficacy in atopic dermatitis and in the case of CC-10004, also in psoriasis.


Results of early clinical trials with both topically (cipamfylline, << CP80,633 >>) and systemically (CC-10004) active [[ PDE4 ]] inhibitors demonstrated efficacy in atopic dermatitis and in the case of CC-10004, also in psoriasis.


Although considerable functional diversity exists, most << C2 domains >> are activated by [[ Ca2+ ]] binding and then dock to a specific cellular membrane.


<< Bile acid coenzyme A:amino acid N-acyltransferase >> (BAT) is responsible for the amidation of [[ bile acids ]] with the amino acids glycine and taurine.


Bile acid coenzyme A:amino acid N-acyltransferase (<< BAT >>) is responsible for the amidation of [[ bile acids ]] with the amino acids glycine and taurine.


Because of their low asparagine synthetase (<< ASNS >>) expression and [[ asparagine ]] biosynthesis, acute lymphoblastic leukemia (ALL) cells are exquisitely sensitive to asparagine depletion.


Because of their low << asparagine synthetase >> (ASNS) expression and [[ asparagine ]] biosynthesis, acute lymphoblastic leukemia (ALL) cells are exquisitely sensitive to asparagine depletion.


<< Asparagine >> secretion by MSCs was directly related to their [[ ASNS ]] expression levels, suggesting a mechanism - increased concentrations of asparagine in the leukemic cell microenvironment - for the protective effects we observed.


<< MK-801 >> ((+)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine maleate), a noncompetitive [[ NMDA receptor ]] antagonist, partially prevented the decrease in cell viability and the energy impairment.


MK-801 (<< (+)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine maleate >>), a noncompetitive [[ NMDA receptor ]] antagonist, partially prevented the decrease in cell viability and the energy impairment.


The use of << Delta 6 desaturase >> (D6D) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of [[ DHA ]] from ALA.


The use of Delta 6 desaturase (<< D6D >>) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from [[ ALA ]].


The use of << Delta 6 desaturase >> (D6D) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to [[ docosahexaenoic acid ]] (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA.


The use of Delta 6 desaturase (<< D6D >>) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to [[ docosahexaenoic acid ]] (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA.


The use of << Delta 6 desaturase >> (D6D) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to docosahexaenoic acid ([[ DHA ]]; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA.


The use of Delta 6 desaturase (<< D6D >>) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to docosahexaenoic acid ([[ DHA ]]; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA.


The use of Delta 6 desaturase (<< D6D >>) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of [[ DHA ]] from ALA.


The use of << Delta 6 desaturase >> (D6D) twice in the conversion of alpha-linolenic acid (ALA; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from [[ ALA ]].


The use of << Delta 6 desaturase >> (D6D) twice in the conversion of [[ alpha-linolenic acid ]] (ALA; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA.


The use of Delta 6 desaturase (<< D6D >>) twice in the conversion of [[ alpha-linolenic acid ]] (ALA; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA.


The use of << Delta 6 desaturase >> (D6D) twice in the conversion of alpha-linolenic acid ([[ ALA ]]; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA.


The use of Delta 6 desaturase (<< D6D >>) twice in the conversion of alpha-linolenic acid ([[ ALA ]]; 18:3n-3) to docosahexaenoic acid (DHA; 22:6n-3) suggests that this enzyme may play a key regulatory role in the synthesis and accumulation of DHA from ALA.


The accumulation of the post-<< D6D >> products of 22:5n-3, 24:6n-3 and [[ DHA ]], in cell phospholipids was saturated at concentrations of >18 microM ALA.


The parallel pattern of accumulation of 24:6n-3 and DHA in response to increasing concentrations of ALA suggests that the competition between 24:5n-3 and ALA for << D6D >> may contribute to the limited accumulation of [[ DHA ]] in cell membranes.


The parallel pattern of accumulation of 24:6n-3 and DHA in response to increasing concentrations of ALA suggests that the competition between 24:5n-3 and << ALA >> for [[ D6D ]] may contribute to the limited accumulation of DHA in cell membranes.


<< Dopamine D1 receptor >> agonist and D2 receptor antagonist effects of the natural product [[ (-)-stepholidine ]]: molecular modeling and dynamics simulations.


Dopamine D1 receptor agonist and << D2 receptor >> antagonist effects of the natural product [[ (-)-stepholidine ]]: molecular modeling and dynamics simulations.


<< (-)-Stepholidine >> (SPD), an active ingredient of the Chinese herb Stephania, is the first compound found to have dual function as a [[ dopamine receptor D1 ]] agonist and D2 antagonist.


(-)-Stepholidine (<< SPD >>), an active ingredient of the Chinese herb Stephania, is the first compound found to have dual function as a [[ dopamine receptor D1 ]] agonist and D2 antagonist.


<< (-)-Stepholidine >> (SPD), an active ingredient of the Chinese herb Stephania, is the first compound found to have dual function as a dopamine receptor D1 agonist and [[ D2 ]] antagonist.


(-)-Stepholidine (<< SPD >>), an active ingredient of the Chinese herb Stephania, is the first compound found to have dual function as a dopamine receptor D1 agonist and [[ D2 ]] antagonist.


The Ki for << mycophenolic acid >> inhibition of the [[ L263F ]] variant was comparable with the wild-type, and the variant Km for inosine 5'-monophosphate and nicotinamide adenine dinucleotide did not change significantly.


<< L-BOAA >> causes loss of GSH and inhibition of [[ mitochondrial complex I ]] in lumbosacral cord of male mice through oxidation of thiol groups, while female mice are resistant.


Female mice express higher levels of glutaredoxin in certain CNS regions and downregulation of glutaredoxin using antisense oligonucleotides sensitizes them to << L-BOAA >> toxicity seen as [[ mitochondrial complex I ]] loss.


Ovariectomy downregulates glutaredoxin and renders female mice vulnerable to << L-BOAA >> toxicity as evidenced by activation of [[ AP1 ]], loss of GSH and complex I activity indicating the important role of glutaredoxin in neuroprotection.


Ovariectomy downregulates glutaredoxin and renders female mice vulnerable to << L-BOAA >> toxicity as evidenced by activation of AP1, loss of GSH and [[ complex I ]] activity indicating the important role of glutaredoxin in neuroprotection.


<< Estrogen >> protects against mitochondrial dysfunction caused by excitotoxicity by maintaining cellular redox status through higher constitutive expression of [[ glutaredoxin ]] in the CNS.


The mechanisms that specify the vesicular phenotype of inhibitory interneurons in vertebrates are poorly understood because the two main inhibitory transmitters, << glycine >> and GABA, share the same [[ vesicular inhibitory amino acid transporter ]] (VIAAT) and are both present in neurons during postnatal development.


The mechanisms that specify the vesicular phenotype of inhibitory interneurons in vertebrates are poorly understood because the two main inhibitory transmitters, << glycine >> and GABA, share the same vesicular inhibitory amino acid transporter ([[ VIAAT ]]) and are both present in neurons during postnatal development.


The mechanisms that specify the vesicular phenotype of inhibitory interneurons in vertebrates are poorly understood because the two main inhibitory transmitters, glycine and << GABA >>, share the same [[ vesicular inhibitory amino acid transporter ]] (VIAAT) and are both present in neurons during postnatal development.


The mechanisms that specify the vesicular phenotype of inhibitory interneurons in vertebrates are poorly understood because the two main inhibitory transmitters, glycine and << GABA >>, share the same vesicular inhibitory amino acid transporter ([[ VIAAT ]]) and are both present in neurons during postnatal development.


We have expressed << VIAAT >> and the plasmalemmal transporters for glycine and [[ GABA ]] in a neuroendocrine cell line and measured the quantal release of glycine and GABA using a novel double-sniffer patch-clamp technique.


We have expressed VIAAT and the << plasmalemmal transporters >> for glycine and [[ GABA ]] in a neuroendocrine cell line and measured the quantal release of glycine and GABA using a novel double-sniffer patch-clamp technique.


We have expressed << VIAAT >> and the plasmalemmal transporters for [[ glycine ]] and GABA in a neuroendocrine cell line and measured the quantal release of glycine and GABA using a novel double-sniffer patch-clamp technique.


We have expressed VIAAT and the << plasmalemmal transporters >> for [[ glycine ]] and GABA in a neuroendocrine cell line and measured the quantal release of glycine and GABA using a novel double-sniffer patch-clamp technique.


We found that << glycine >> is released from vesicles when [[ VIAAT ]] is coexpressed with either the neuronal transporter GlyT2 or the glial transporter GlyT1.


However, GlyT2 was more effective than GlyT1, probably because GlyT2 is unable to operate in the reverse mode, which gives it an advantage in maintaining the high cytosolic << glycine >> concentration required for efficient vesicular loading by [[ VIAAT ]].


The vesicular inhibitory phenotype was gradually altered from glycinergic to GABAergic through mixed events when << GABA >> is introduced into the secretory cell and competes for uptake by [[ VIAAT ]].


Interestingly, the VIAAT ortholog from Caenorhabditis elegans (UNC-47), a species lacking glycine transmission, also supports << glycine >> exocytosis in the presence of [[ GlyT2 ]], and a point mutation of UNC-47 that abolishes GABA transmission in the worm confers glycine specificity.


Together, these results suggest that an increased cytosolic availability of << glycine >> in [[ VIAAT ]]-containing terminals was crucial for the emergence of glycinergic transmission in vertebrates.


<< Na+ >>/Cl- dipole couples agonist binding to [[ kainate receptor ]] activation.


Na+/<< Cl- >> dipole couples agonist binding to [[ kainate receptor ]] activation.


<< Kainate-selective ionotropic glutamate receptors >> (GluRs) require external Na+ and Cl- as well as the neurotransmitter [[ L-glutamate ]] for activation.


Kainate-selective ionotropic glutamate receptors (<< GluRs >>) require external Na+ and Cl- as well as the neurotransmitter [[ L-glutamate ]] for activation.


<< Kainate-selective ionotropic glutamate receptors >> (GluRs) require external [[ Na+ ]] and Cl- as well as the neurotransmitter L-glutamate for activation.


Kainate-selective ionotropic glutamate receptors (<< GluRs >>) require external [[ Na+ ]] and Cl- as well as the neurotransmitter L-glutamate for activation.


<< Kainate-selective ionotropic glutamate receptors >> (GluRs) require external Na+ and [[ Cl- ]] as well as the neurotransmitter L-glutamate for activation.


Kainate-selective ionotropic glutamate receptors (<< GluRs >>) require external Na+ and [[ Cl- ]] as well as the neurotransmitter L-glutamate for activation.


Additionally, << Na+ >> and Cl- ions coactivate [[ GluR6 ]] receptors by establishing a dipole, accounting for their common effect on KARs.


Additionally, Na+ and << Cl- >> ions coactivate [[ GluR6 ]] receptors by establishing a dipole, accounting for their common effect on KARs.


Phenserine. << Phenserine >>, a derivative of physostigmine, was first described as an inhibitor of acetylcholinesterase ([[ AChE ]]) and was shown to improve cognition in various experimental paradigms in rodents and dogs.


Phenserine. << Phenserine >>, a derivative of physostigmine, was first described as an inhibitor of [[ acetylcholinesterase ]] (AChE) and was shown to improve cognition in various experimental paradigms in rodents and dogs.


Phenserine. Phenserine, a derivative of << physostigmine >>, was first described as an inhibitor of acetylcholinesterase ([[ AChE ]]) and was shown to improve cognition in various experimental paradigms in rodents and dogs.


Phenserine. Phenserine, a derivative of << physostigmine >>, was first described as an inhibitor of [[ acetylcholinesterase ]] (AChE) and was shown to improve cognition in various experimental paradigms in rodents and dogs.


<< Phenserine >> deserves attention for an additional quality of action: in addition to inhibiting AChE, it modulates the amount of beta-amyloid precursor protein (APP) in neuronal cell culture by reducing [[ APP ]] translation.


<< Phenserine >> deserves attention for an additional quality of action: in addition to inhibiting [[ AChE ]], it modulates the amount of beta-amyloid precursor protein (APP) in neuronal cell culture by reducing APP translation.


<< Phenserine >> apparently reduces translational efficiency of [[ APP ]] mRNA into protein, a process that may involve an interaction with iron and/or an iron-responsive element.


As a consequence, << phenserine >> reduces [[ beta-amyloid ]] peptide (Abeta) formation in vitro and in vivo.


As a consequence, << phenserine >> reduces beta-amyloid peptide ([[ Abeta ]]) formation in vitro and in vivo.


Phenserine is also unique because of differing actions of its enantiomers: << (-)-phenserine >> is the active enantiomer for inhibition of [[ AChE ]], whereas (+)-phenserine ('posiphen') has weak activity as an AChE inhibitor and can be dosed much higher.


Phenserine is also unique because of differing actions of its enantiomers: (-)-phenserine is the active enantiomer for inhibition of AChE, whereas << (+)-phenserine >> ('posiphen') has weak activity as an [[ AChE ]] inhibitor and can be dosed much higher.


Phenserine is also unique because of differing actions of its enantiomers: (-)-phenserine is the active enantiomer for inhibition of AChE, whereas (+)-phenserine ('<< posiphen >>') has weak activity as an [[ AChE ]] inhibitor and can be dosed much higher.


BACKGROUND AND PURPOSE: << AMP-activated protein kinase >> (AMPK) is activated by metformin, phenformin, and the AMP mimetic, 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside ([[ AICAR ]]).


BACKGROUND AND PURPOSE: AMP-activated protein kinase (<< AMPK >>) is activated by metformin, phenformin, and the AMP mimetic, 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside ([[ AICAR ]]).


BACKGROUND AND PURPOSE: << AMP-activated protein kinase >> (AMPK) is activated by [[ metformin ]], phenformin, and the AMP mimetic, 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR).


BACKGROUND AND PURPOSE: AMP-activated protein kinase (<< AMPK >>) is activated by [[ metformin ]], phenformin, and the AMP mimetic, 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR).


BACKGROUND AND PURPOSE: << AMP-activated protein kinase >> (AMPK) is activated by metformin, [[ phenformin ]], and the AMP mimetic, 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR).


BACKGROUND AND PURPOSE: AMP-activated protein kinase (<< AMPK >>) is activated by metformin, [[ phenformin ]], and the AMP mimetic, 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR).


BACKGROUND AND PURPOSE: << AMP-activated protein kinase >> (AMPK) is activated by metformin, phenformin, and the AMP mimetic, [[ 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside ]] (AICAR).


BACKGROUND AND PURPOSE: AMP-activated protein kinase (<< AMPK >>) is activated by metformin, phenformin, and the AMP mimetic, [[ 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside ]] (AICAR).


KEY RESULTS: << Phenformin >>, AICAR and metformin increased [[ AMPK (alpha1) ]] activity and decreased I(amiloride).


KEY RESULTS: Phenformin, << AICAR >> and metformin increased [[ AMPK (alpha1) ]] activity and decreased I(amiloride).


KEY RESULTS: Phenformin, AICAR and << metformin >> increased [[ AMPK (alpha1) ]] activity and decreased I(amiloride).


The << AMPK >> inhibitor Compound C prevented the action of metformin and AICAR but not [[ phenformin ]].


Additional pharmacological effects evoked by << AICAR >> and phenformin on I(ouabain), with potential secondary effects on apical Na+ conductance, ENaC activity and monolayer resistance, have important consequences for their use as pharmacological activators of [[ AMPK ]] in cell systems where Na+K+ATPase is an important component.


Additional pharmacological effects evoked by AICAR and << phenformin >> on I(ouabain), with potential secondary effects on apical Na+ conductance, ENaC activity and monolayer resistance, have important consequences for their use as pharmacological activators of [[ AMPK ]] in cell systems where Na+K+ATPase is an important component.


Additional pharmacological effects evoked by AICAR and phenformin on I(<< ouabain >>), with potential secondary effects on apical Na+ conductance, ENaC activity and monolayer resistance, have important consequences for their use as pharmacological activators of [[ AMPK ]] in cell systems where Na+K+ATPase is an important component.


Neuroprotective effect of << nimesulide >>, a preferential [[ COX-2 ]] inhibitor, against pentylenetetrazol (PTZ)-induced chemical kindling and associated biochemical parameters in mice.


Brain cyclooxygenases (<< COX >>), the rate-limiting enzyme in [[ prostaglandin ]] synthesis, is rapidly and transiently induced by convulsions in hippocampal and cortical neurons.


Brain << cyclooxygenases >> (COX), the rate-limiting enzyme in [[ prostaglandin ]] synthesis, is rapidly and transiently induced by convulsions in hippocampal and cortical neurons.


Previous studies have explored the protective effect of naproxen (non-selective COX-inhibitor) or << rofecoxib >> (selective [[ COX-2 ]] inhibitor) against chemical kindling in mice.


Previous studies have explored the protective effect of << naproxen >> (non-selective [[ COX ]]-inhibitor) or rofecoxib (selective COX-2 inhibitor) against chemical kindling in mice.


With this background, the present study was designed to explore the possible effect of << nimesulide >> (a preferential [[ COX-2 ]] inhibitor) against pentylenetetrazol (PTZ)-induced kindling epilepsy in mice.


Compared with normal control group, << PTZ >>-kindled mice had significantly higher levels of malondialdehyde, nitrite, [[ myeloperoxidase ]] but had lower levels of reduced glutathione in the whole brain homogenate.


These results suggested that << nimesulide >>, a preferential [[ COX-2 ]] inhibitor offered neuroprotection against PTZ-induced kindling in mice.


While vitamin C is essential for PHD activity in vitro, N-acetyl-L-cysteine had no effect, and << gallic acid >> or n-propyl gallate efficiently inhibited the activity of all three [[ PHDs ]], demonstrating different functions of these antioxidants.


While vitamin C is essential for PHD activity in vitro, N-acetyl-L-cysteine had no effect, and gallic acid or << n-propyl gallate >> efficiently inhibited the activity of all three [[ PHDs ]], demonstrating different functions of these antioxidants.


<< LTC4 synthase >> (LTC4S), the pivotal enzyme for the biosynthesis of [[ LTC4 ]] (ref. 10), is an 18-kDa integral nuclear membrane protein that belongs to a superfamily of membrane-associated proteins in eicosanoid and glutathione metabolism that includes 5-lipoxygenase-activating protein, microsomal glutathione S-transferases (MGSTs), and microsomal prostaglandin E synthase 1 (ref. 13).


LTC4 synthase (<< LTC4S >>), the pivotal enzyme for the biosynthesis of [[ LTC4 ]] (ref. 10), is an 18-kDa integral nuclear membrane protein that belongs to a superfamily of membrane-associated proteins in eicosanoid and glutathione metabolism that includes 5-lipoxygenase-activating protein, microsomal glutathione S-transferases (MGSTs), and microsomal prostaglandin E synthase 1 (ref. 13).


LTC4 synthase (LTC4S), the pivotal enzyme for the biosynthesis of LTC4 (ref. 10), is an 18-kDa integral nuclear membrane protein that belongs to a superfamily of membrane-associated proteins in << eicosanoid >> and glutathione metabolism that includes 5-lipoxygenase-activating protein, [[ microsomal glutathione S-transferases ]] (MGSTs), and microsomal prostaglandin E synthase 1 (ref. 13).


LTC4 synthase (LTC4S), the pivotal enzyme for the biosynthesis of LTC4 (ref. 10), is an 18-kDa integral nuclear membrane protein that belongs to a superfamily of membrane-associated proteins in << eicosanoid >> and glutathione metabolism that includes 5-lipoxygenase-activating protein, microsomal glutathione S-transferases ([[ MGSTs ]]), and microsomal prostaglandin E synthase 1 (ref. 13).


LTC4 synthase (LTC4S), the pivotal enzyme for the biosynthesis of LTC4 (ref. 10), is an 18-kDa integral nuclear membrane protein that belongs to a superfamily of membrane-associated proteins in << eicosanoid >> and glutathione metabolism that includes 5-lipoxygenase-activating protein, microsomal glutathione S-transferases (MGSTs), and [[ microsomal prostaglandin E synthase 1 ]] (ref. 13).


LTC4 synthase (LTC4S), the pivotal enzyme for the biosynthesis of LTC4 (ref. 10), is an 18-kDa integral nuclear membrane protein that belongs to a superfamily of membrane-associated proteins in eicosanoid and << glutathione >> metabolism that includes 5-lipoxygenase-activating protein, [[ microsomal glutathione S-transferases ]] (MGSTs), and microsomal prostaglandin E synthase 1 (ref. 13).


LTC4 synthase (LTC4S), the pivotal enzyme for the biosynthesis of LTC4 (ref. 10), is an 18-kDa integral nuclear membrane protein that belongs to a superfamily of membrane-associated proteins in eicosanoid and << glutathione >> metabolism that includes 5-lipoxygenase-activating protein, microsomal glutathione S-transferases ([[ MGSTs ]]), and microsomal prostaglandin E synthase 1 (ref. 13).


LTC4 synthase (LTC4S), the pivotal enzyme for the biosynthesis of LTC4 (ref. 10), is an 18-kDa integral nuclear membrane protein that belongs to a superfamily of membrane-associated proteins in eicosanoid and << glutathione >> metabolism that includes 5-lipoxygenase-activating protein, microsomal glutathione S-transferases (MGSTs), and [[ microsomal prostaglandin E synthase 1 ]] (ref. 13).


<< Phenelzine >> causes an increase in brain ornithine that is prevented by prior [[ monoamine oxidase ]] inhibition.


<< Phenelzine >> (PLZ), a nonselective irreversible inhibitor of monoamine oxidase (MAO), also inhibits GABA-transaminase ([[ GABA-T ]]), markedly increasing brain GABA levels.


<< Phenelzine >> (PLZ), a nonselective irreversible inhibitor of [[ monoamine oxidase ]] (MAO), also inhibits GABA-transaminase (GABA-T), markedly increasing brain GABA levels.


<< Phenelzine >> (PLZ), a nonselective irreversible inhibitor of monoamine oxidase ([[ MAO ]]), also inhibits GABA-transaminase (GABA-T), markedly increasing brain GABA levels.


<< Phenelzine >> (PLZ), a nonselective irreversible inhibitor of monoamine oxidase (MAO), also inhibits [[ GABA-transaminase ]] (GABA-T), markedly increasing brain GABA levels.


Phenelzine (<< PLZ >>), a nonselective irreversible inhibitor of monoamine oxidase (MAO), also inhibits GABA-transaminase ([[ GABA-T ]]), markedly increasing brain GABA levels.


Phenelzine (<< PLZ >>), a nonselective irreversible inhibitor of [[ monoamine oxidase ]] (MAO), also inhibits GABA-transaminase (GABA-T), markedly increasing brain GABA levels.


Phenelzine (<< PLZ >>), a nonselective irreversible inhibitor of monoamine oxidase ([[ MAO ]]), also inhibits GABA-transaminase (GABA-T), markedly increasing brain GABA levels.


Phenelzine (<< PLZ >>), a nonselective irreversible inhibitor of monoamine oxidase (MAO), also inhibits [[ GABA-transaminase ]] (GABA-T), markedly increasing brain GABA levels.


<< PLZ >> is also a substrate for [[ MAO ]], and studies suggest that a metabolite formed by the action of this enzyme on PLZ may be responsible for the increase in GABA observed.


To determine whether a metabolite formed by the action of MAO on PLZ may be responsible for the elevation in brain ORN observed, animals were pretreated with vehicle or the << MAO >> inhibitor [[ tranylcypromine ]] (TCP) before vehicle or PLZ (15 mg/kg), and brains collected 3 h later.


To determine whether a metabolite formed by the action of MAO on PLZ may be responsible for the elevation in brain ORN observed, animals were pretreated with vehicle or the << MAO >> inhibitor tranylcypromine ([[ TCP ]]) before vehicle or PLZ (15 mg/kg), and brains collected 3 h later.


Pretreatment with TCP completely abolished the PLZ-induced increase in brain ORN, suggesting, as with GABA, that a metabolite of << PLZ >> formed by the action of [[ MAO ]] is responsible for the elevation of brain ORN observed.


Nitric oxide (<< NO >>) is an important vasorelaxant produced along with L-citrulline from L-arginine in a reaction catalyzed by [[ endothelial nitric oxide synthase ]] (eNOS).


Nitric oxide (<< NO >>) is an important vasorelaxant produced along with L-citrulline from L-arginine in a reaction catalyzed by endothelial nitric oxide synthase ([[ eNOS ]]).


<< Nitric oxide >> (NO) is an important vasorelaxant produced along with L-citrulline from L-arginine in a reaction catalyzed by [[ endothelial nitric oxide synthase ]] (eNOS).


<< Nitric oxide >> (NO) is an important vasorelaxant produced along with L-citrulline from L-arginine in a reaction catalyzed by endothelial nitric oxide synthase ([[ eNOS ]]).


Nitric oxide (NO) is an important vasorelaxant produced along with << L-citrulline >> from L-arginine in a reaction catalyzed by [[ endothelial nitric oxide synthase ]] (eNOS).


Nitric oxide (NO) is an important vasorelaxant produced along with << L-citrulline >> from L-arginine in a reaction catalyzed by endothelial nitric oxide synthase ([[ eNOS ]]).


Nitric oxide (NO) is an important vasorelaxant produced along with L-citrulline from << L-arginine >> in a reaction catalyzed by [[ endothelial nitric oxide synthase ]] (eNOS).


Nitric oxide (NO) is an important vasorelaxant produced along with L-citrulline from << L-arginine >> in a reaction catalyzed by endothelial nitric oxide synthase ([[ eNOS ]]).


As further support, << alpha-methyl-DL-aspartate >>, an inhibitor of [[ argininosuccinate synthase ]] (AS), a component of the citrulline-NO cycle, inhibited NO production in a dose-dependent manner.


As further support, << alpha-methyl-DL-aspartate >>, an inhibitor of argininosuccinate synthase ([[ AS ]]), a component of the citrulline-NO cycle, inhibited NO production in a dose-dependent manner.


Caution is necessary only when it is coadministered with drugs metabolised by << CYP2D6 >>, such as [[ metoprolol ]], or administered to the elderly or patients with severe hepatic or renal impairment.


Inhibition of platelet aggregation by AZD6140, a reversible oral << P2Y12 >> receptor antagonist, compared with [[ clopidogrel ]] in patients with acute coronary syndromes.


Inhibition of platelet aggregation by << AZD6140 >>, a reversible oral [[ P2Y12 ]] receptor antagonist, compared with clopidogrel in patients with acute coronary syndromes.


<< AZD6140 >> is a reversible oral [[ P2Y(12) ]] receptor antagonist that has been studied in ACS patients in comparison with clopidogrel (DISPERSE-2 study).


AZD6140 is a reversible oral << P2Y(12) >> receptor antagonist that has been studied in ACS patients in comparison with [[ clopidogrel ]] (DISPERSE-2 study).


<< Oxybutynin >> (1) is a non-selective [[ muscarinic receptor ]] antagonist that is used clinically for the treatment of urinary incontinence.


Degradation of submandibular gland << AQP5 >> by parasympathetic denervation of chorda tympani and its recovery by [[ cevimeline ]], an M3 muscarinic receptor agonist.


Degradation of submandibular gland AQP5 by parasympathetic denervation of chorda tympani and its recovery by << cevimeline >>, an [[ M3 muscarinic receptor ]] agonist.


Administration of << cevimeline hydrochloride >>, an M3 muscarinic receptor agonist (10 mg/kg for 7 days po), but not pilocarpine (0.3 mg/kg for 7 days po), recovered the [[ AQP5 ]] protein level reduced by CTD and increased the AQP1 protein level above the control one.


Administration of << cevimeline hydrochloride >>, an M3 muscarinic receptor agonist (10 mg/kg for 7 days po), but not pilocarpine (0.3 mg/kg for 7 days po), recovered the AQP5 protein level reduced by CTD and increased the [[ AQP1 ]] protein level above the control one.


Administration of << cevimeline hydrochloride >>, an [[ M3 muscarinic receptor ]] agonist (10 mg/kg for 7 days po), but not pilocarpine (0.3 mg/kg for 7 days po), recovered the AQP5 protein level reduced by CTD and increased the AQP1 protein level above the control one.


Administration of << chloroquine >> (50 mg/kg for 7 days po), a denaturant of lysosomes, increased the [[ AQP5 ]] protein level reduced by CTD.


Differential pharmacokinetics and pharmacodynamics of methylphenidate enantiomers: does chirality matter? d,l-threo-methylphenidate (MPH) is an effective first-line treatment for the symptoms associated with attention-deficit/hyperactivity disorder. << threo-methylphenidate >> inhibits the [[ dopamine transporter ]] and the norepinephrine transporter, resulting in elevations of these monoamines after impulse release.


Differential pharmacokinetics and pharmacodynamics of methylphenidate enantiomers: does chirality matter? d,l-threo-methylphenidate (MPH) is an effective first-line treatment for the symptoms associated with attention-deficit/hyperactivity disorder. << threo-methylphenidate >> inhibits the dopamine transporter and the [[ norepinephrine transporter ]], resulting in elevations of these monoamines after impulse release.


Differential pharmacokinetics and pharmacodynamics of methylphenidate enantiomers: does chirality matter? d,l-threo-methylphenidate (MPH) is an effective first-line treatment for the symptoms associated with attention-deficit/hyperactivity disorder. threo-methylphenidate inhibits the << dopamine transporter >> and the norepinephrine transporter, resulting in elevations of these [[ monoamines ]] after impulse release.


Differential pharmacokinetics and pharmacodynamics of methylphenidate enantiomers: does chirality matter? d,l-threo-methylphenidate (MPH) is an effective first-line treatment for the symptoms associated with attention-deficit/hyperactivity disorder. threo-methylphenidate inhibits the dopamine transporter and the << norepinephrine transporter >>, resulting in elevations of these [[ monoamines ]] after impulse release.


The direct inhibition of << stathmin >> by [[ CCNU ]] is likely a contributing factor.


The principal aim of the study was to find << amiodarone >> analogues that retained [[ human ether-a-go-go-related protein (hERG) channel ]] inhibition but with reduced cytotoxicity.


CONCLUSIONS AND IMPLICATIONS: << Amiodarone >> analogues with better [[ hERG ]] channel inhibition and cytotoxicity profiles than the parent compound have been identified, demonstrating that cytotoxicity and hERG channel interaction are mechanistically distinct and separable properties of the compounds.


In addition to OT and to a lesser extent AVP (pitressin), a number of OT and AVP analogues; such as << carbetocin >> ([[ OT ]] agonist) dDAVP (desmopressin, V(2) agonist), terlipressin (V(1a) agonist), felypressin (V(1a) agonist) and atosiban (Tractocile OT antagonist) are also in clinical use.


In addition to OT and to a lesser extent AVP (pitressin), a number of OT and AVP analogues; such as carbetocin (OT agonist) dDAVP (<< desmopressin >>, [[ V(2) ]] agonist), terlipressin (V(1a) agonist), felypressin (V(1a) agonist) and atosiban (Tractocile OT antagonist) are also in clinical use.


In addition to OT and to a lesser extent AVP (pitressin), a number of OT and AVP analogues; such as carbetocin (OT agonist) dDAVP (desmopressin, V(2) agonist), << terlipressin >> ([[ V(1a) ]] agonist), felypressin (V(1a) agonist) and atosiban (Tractocile OT antagonist) are also in clinical use.


In addition to OT and to a lesser extent AVP (pitressin), a number of OT and AVP analogues; such as carbetocin (OT agonist) dDAVP (desmopressin, V(2) agonist), terlipressin (V(1a) agonist), << felypressin >> ([[ V(1a) ]] agonist) and atosiban (Tractocile OT antagonist) are also in clinical use.


In addition to OT and to a lesser extent AVP (pitressin), a number of OT and AVP analogues; such as carbetocin (OT agonist) dDAVP (desmopressin, V(2) agonist), terlipressin (V(1a) agonist), felypressin (V(1a) agonist) and << atosiban >> (Tractocile [[ OT ]] antagonist) are also in clinical use.


In addition to OT and to a lesser extent AVP (pitressin), a number of OT and AVP analogues; such as carbetocin (OT agonist) dDAVP (desmopressin, V(2) agonist), terlipressin (V(1a) agonist), felypressin (V(1a) agonist) and atosiban (<< Tractocile >> [[ OT ]] antagonist) are also in clinical use.


While a number of orally active non-peptide << V(2) >> antagonists (Vaptans); notably, [[ Tolvaptan ]], Lixivaptan and Satavaptan, are currently in Phase III clinical trials; to date, only the mixed V(2)/V(1a), antagonist Conivaptan (Vaprisol), has been approved by the US FDA for clinical use (by i.v. administration), for the treatment of euvolemic and hypervolemic hyponatremia in hospitalized patients.


While a number of orally active non-peptide << V(2) >> antagonists (Vaptans); notably, Tolvaptan, [[ Lixivaptan ]] and Satavaptan, are currently in Phase III clinical trials; to date, only the mixed V(2)/V(1a), antagonist Conivaptan (Vaprisol), has been approved by the US FDA for clinical use (by i.v. administration), for the treatment of euvolemic and hypervolemic hyponatremia in hospitalized patients.


While a number of orally active non-peptide << V(2) >> antagonists (Vaptans); notably, Tolvaptan, Lixivaptan and [[ Satavaptan ]], are currently in Phase III clinical trials; to date, only the mixed V(2)/V(1a), antagonist Conivaptan (Vaprisol), has been approved by the US FDA for clinical use (by i.v. administration), for the treatment of euvolemic and hypervolemic hyponatremia in hospitalized patients.


While a number of orally active non-peptide V(2) antagonists (Vaptans); notably, Tolvaptan, Lixivaptan and Satavaptan, are currently in Phase III clinical trials; to date, only the mixed << V(2) >>/V(1a), antagonist [[ Conivaptan ]] (Vaprisol), has been approved by the US FDA for clinical use (by i.v. administration), for the treatment of euvolemic and hypervolemic hyponatremia in hospitalized patients.


While a number of orally active non-peptide V(2) antagonists (Vaptans); notably, Tolvaptan, Lixivaptan and Satavaptan, are currently in Phase III clinical trials; to date, only the mixed V(2)/<< V(1a) >>, antagonist [[ Conivaptan ]] (Vaprisol), has been approved by the US FDA for clinical use (by i.v. administration), for the treatment of euvolemic and hypervolemic hyponatremia in hospitalized patients.


While a number of orally active non-peptide V(2) antagonists (Vaptans); notably, Tolvaptan, Lixivaptan and Satavaptan, are currently in Phase III clinical trials; to date, only the mixed << V(2) >>/V(1a), antagonist Conivaptan ([[ Vaprisol ]]), has been approved by the US FDA for clinical use (by i.v. administration), for the treatment of euvolemic and hypervolemic hyponatremia in hospitalized patients.


While a number of orally active non-peptide V(2) antagonists (Vaptans); notably, Tolvaptan, Lixivaptan and Satavaptan, are currently in Phase III clinical trials; to date, only the mixed V(2)/<< V(1a) >>, antagonist Conivaptan ([[ Vaprisol ]]), has been approved by the US FDA for clinical use (by i.v. administration), for the treatment of euvolemic and hypervolemic hyponatremia in hospitalized patients.


Absorbable drugs (<< fibric acids >>, nicotinic acid, probucol, HMG-CoA reductase inhibitors) reduce [[ plasma very-low-density lipoproteins ]] (VLDL) and/or low-density lipoproteins (LDL) by a variety of mechanisms.


Absorbable drugs (<< fibric acids >>, nicotinic acid, probucol, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins ([[ VLDL ]]) and/or low-density lipoproteins (LDL) by a variety of mechanisms.


Absorbable drugs (<< fibric acids >>, nicotinic acid, probucol, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins (VLDL) and/or [[ low-density lipoproteins ]] (LDL) by a variety of mechanisms.


Absorbable drugs (<< fibric acids >>, nicotinic acid, probucol, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins (VLDL) and/or low-density lipoproteins ([[ LDL ]]) by a variety of mechanisms.


Absorbable drugs (fibric acids, << nicotinic acid >>, probucol, HMG-CoA reductase inhibitors) reduce [[ plasma very-low-density lipoproteins ]] (VLDL) and/or low-density lipoproteins (LDL) by a variety of mechanisms.


Absorbable drugs (fibric acids, << nicotinic acid >>, probucol, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins ([[ VLDL ]]) and/or low-density lipoproteins (LDL) by a variety of mechanisms.


Absorbable drugs (fibric acids, << nicotinic acid >>, probucol, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins (VLDL) and/or [[ low-density lipoproteins ]] (LDL) by a variety of mechanisms.


Absorbable drugs (fibric acids, << nicotinic acid >>, probucol, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins (VLDL) and/or low-density lipoproteins ([[ LDL ]]) by a variety of mechanisms.


Absorbable drugs (fibric acids, nicotinic acid, << probucol >>, HMG-CoA reductase inhibitors) reduce [[ plasma very-low-density lipoproteins ]] (VLDL) and/or low-density lipoproteins (LDL) by a variety of mechanisms.


Absorbable drugs (fibric acids, nicotinic acid, << probucol >>, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins ([[ VLDL ]]) and/or low-density lipoproteins (LDL) by a variety of mechanisms.


Absorbable drugs (fibric acids, nicotinic acid, << probucol >>, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins (VLDL) and/or [[ low-density lipoproteins ]] (LDL) by a variety of mechanisms.


Absorbable drugs (fibric acids, nicotinic acid, << probucol >>, HMG-CoA reductase inhibitors) reduce plasma very-low-density lipoproteins (VLDL) and/or low-density lipoproteins ([[ LDL ]]) by a variety of mechanisms.


<< Fibric acids >>, in particular, act by stimulating the catabolism of [[ VLDL ]] and also, as a consequence, improving LDL delipidation, thus favoring receptor uptake.


Probucol acts by a newly described mechanism, i.e. accelerating reverse transport of << cholesteryl esters >> from [[ high-density lipoproteins ]] to lower-density lipoproteins.


Probucol acts by a newly described mechanism, i.e. accelerating reverse transport of << cholesteryl esters >> from high-density lipoproteins to [[ lower-density lipoproteins ]].


<< Lapatinib >>: a dual inhibitor of [[ human epidermal growth factor receptor ]] tyrosine kinases.


<< Lapatinib >>: a dual inhibitor of human epidermal growth factor receptor [[ tyrosine kinases ]].


BACKGROUND: << Lapatinib >>, the first dual inhibitor of epidermal growth factor receptor (EGFR) and human epidermal growth factor receptor 2 ([[ HER2 ]]) tyrosine kinases, was approved by the US Food and Drug Administration (FDA) in 2007.


BACKGROUND: << Lapatinib >>, the first dual inhibitor of epidermal growth factor receptor (EGFR) and human epidermal growth factor receptor 2 (HER2) [[ tyrosine kinases ]], was approved by the US Food and Drug Administration (FDA) in 2007.


BACKGROUND: << Lapatinib >>, the first dual inhibitor of [[ epidermal growth factor receptor ]] (EGFR) and human epidermal growth factor receptor 2 (HER2) tyrosine kinases, was approved by the US Food and Drug Administration (FDA) in 2007.


BACKGROUND: << Lapatinib >>, the first dual inhibitor of epidermal growth factor receptor ([[ EGFR ]]) and human epidermal growth factor receptor 2 (HER2) tyrosine kinases, was approved by the US Food and Drug Administration (FDA) in 2007.


BACKGROUND: << Lapatinib >>, the first dual inhibitor of epidermal growth factor receptor (EGFR) and [[ human epidermal growth factor receptor 2 ]] (HER2) tyrosine kinases, was approved by the US Food and Drug Administration (FDA) in 2007.


<< Lapatinib >> is metabolized primarily by the [[ cytochrome P450 3A4 ]] isozyme, with 1 metabolite remaining active against EGFR but not HER2.


CONCLUSIONS: << Lapatinib >> is a dual inhibitor of the [[ EGFR ]] and HER2 tyrosine kinases.


CONCLUSIONS: << Lapatinib >> is a dual inhibitor of the EGFR and [[ HER2 ]] tyrosine kinases.


CONCLUSIONS: << Lapatinib >> is a dual inhibitor of the EGFR and HER2 [[ tyrosine kinases ]].


Phenelzine is a more potent << monoamine oxidase >> inhibitor than is [[ N2-acetylphenelzine ]].


<< Phenelzine >> is a more potent [[ monoamine oxidase ]] inhibitor than is N2-acetylphenelzine.


Acetylation of << phenelzine >> at the N2 position presumably interferes with the inhibition of the [[ transaminase ]] enzymes for gamma-aminobutyric acid and alanine.


Acetylation of phenelzine at the << N2 >> position presumably interferes with the inhibition of the [[ transaminase ]] enzymes for gamma-aminobutyric acid and alanine.


Acetylation of phenelzine at the N2 position presumably interferes with the inhibition of the << transaminase >> enzymes for [[ gamma-aminobutyric acid ]] and alanine.


Acetylation of phenelzine at the N2 position presumably interferes with the inhibition of the << transaminase >> enzymes for gamma-aminobutyric acid and [[ alanine ]].


All neurotrophic effects were blocked by the unselective D2/D3 receptor antagonist sulpiride (5 microm) and by the selective << D3 receptor >> antagonist [[ SB-277011-A ]] at a low dose (50 nm).


<< Quinpirole >> and 7-OH-DPAT also increased the phosphorylation of [[ extracellular signal-regulated kinase ]] (ERK) within minutes, an effect blocked by pretreatment with SB-277011-A.


<< Quinpirole >> and 7-OH-DPAT also increased the phosphorylation of extracellular signal-regulated kinase ([[ ERK ]]) within minutes, an effect blocked by pretreatment with SB-277011-A.


Quinpirole and << 7-OH-DPAT >> also increased the phosphorylation of [[ extracellular signal-regulated kinase ]] (ERK) within minutes, an effect blocked by pretreatment with SB-277011-A.


Quinpirole and << 7-OH-DPAT >> also increased the phosphorylation of extracellular signal-regulated kinase ([[ ERK ]]) within minutes, an effect blocked by pretreatment with SB-277011-A.


Quinpirole and 7-OH-DPAT also increased the phosphorylation of << extracellular signal-regulated kinase >> (ERK) within minutes, an effect blocked by pretreatment with [[ SB-277011-A ]].


Quinpirole and 7-OH-DPAT also increased the phosphorylation of extracellular signal-regulated kinase (<< ERK >>) within minutes, an effect blocked by pretreatment with [[ SB-277011-A ]].


This study identified four clinically approved antihypertensive drugs (<< efonidipine >>, felodipine, isradipine, and nitrendipine) as potent [[ T-channel ]] blockers (IC(50) < 3 microM).


This study identified four clinically approved antihypertensive drugs (efonidipine, << felodipine >>, isradipine, and nitrendipine) as potent [[ T-channel ]] blockers (IC(50) < 3 microM).


This study identified four clinically approved antihypertensive drugs (efonidipine, felodipine, << isradipine >>, and nitrendipine) as potent [[ T-channel ]] blockers (IC(50) < 3 microM).


This study identified four clinically approved antihypertensive drugs (efonidipine, felodipine, isradipine, and << nitrendipine >>) as potent [[ T-channel ]] blockers (IC(50) < 3 microM).


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: [[ carbenoxolone ]] > disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS) approximately disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate approximately 5-nitro-2-(3-phenylpropylamino)benzoic acid > indanyloxyacetic acid 94 >> probenecid >> flufenamic acid = niflumic acid.


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: carbenoxolone > [[ disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate ]] (DIDS) approximately disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate approximately 5-nitro-2-(3-phenylpropylamino)benzoic acid > indanyloxyacetic acid 94 >> probenecid >> flufenamic acid = niflumic acid.


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: carbenoxolone > disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate ([[ DIDS ]]) approximately disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate approximately 5-nitro-2-(3-phenylpropylamino)benzoic acid > indanyloxyacetic acid 94 >> probenecid >> flufenamic acid = niflumic acid.


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: carbenoxolone > disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS) approximately [[ disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate ]] approximately 5-nitro-2-(3-phenylpropylamino)benzoic acid > indanyloxyacetic acid 94 >> probenecid >> flufenamic acid = niflumic acid.


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: carbenoxolone > disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS) approximately disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate approximately [[ 5-nitro-2-(3-phenylpropylamino)benzoic acid ]] > indanyloxyacetic acid 94 >> probenecid >> flufenamic acid = niflumic acid.


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: carbenoxolone > disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS) approximately disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate approximately 5-nitro-2-(3-phenylpropylamino)benzoic acid > [[ indanyloxyacetic acid 94 ]] >> probenecid >> flufenamic acid = niflumic acid.


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: carbenoxolone > disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS) approximately disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate approximately 5-nitro-2-(3-phenylpropylamino)benzoic acid > indanyloxyacetic acid 94 >> [[ probenecid ]] >> flufenamic acid = niflumic acid.


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: carbenoxolone > disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS) approximately disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate approximately 5-nitro-2-(3-phenylpropylamino)benzoic acid > indanyloxyacetic acid 94 >> probenecid >> [[ flufenamic acid ]] = niflumic acid.


We found compounds that inhibited << Panx1 >> currents with a rank order of potency: carbenoxolone > disodium 4,4'-diisothiocyanatostilbene-2,2'-disulfonate (DIDS) approximately disodium 4-acetamido-4'-isothiocyanato-stilben-2,2'-disulfonate approximately 5-nitro-2-(3-phenylpropylamino)benzoic acid > indanyloxyacetic acid 94 >> probenecid >> flufenamic acid = [[ niflumic acid ]].


Triphosphate nucleotides (ATP, GTP, and << UTP >>) rapidly and reversibly inhibited [[ Panx1 ]] currents via mechanism(s) independent of purine receptors.


<< Triphosphate nucleotides >> (ATP, GTP, and UTP) rapidly and reversibly inhibited [[ Panx1 ]] currents via mechanism(s) independent of purine receptors.


Triphosphate nucleotides (<< ATP >>, GTP, and UTP) rapidly and reversibly inhibited [[ Panx1 ]] currents via mechanism(s) independent of purine receptors.


Triphosphate nucleotides (ATP, << GTP >>, and UTP) rapidly and reversibly inhibited [[ Panx1 ]] currents via mechanism(s) independent of purine receptors.


When Panx1 was coexpressed with purinergic P2X(7) receptor (P2X(7)R), << DIDS >> was found to act as a [[ P2X(7)R ]] antagonist to inhibit ATP-evoked currents, but none of the other compounds inhibited P2X(7)R currents.


We investigated the effect of << captopril >>, an [[ ACE ]] inhibitor, on MMP-2 and MMP-9 in monocrotaline-induced right ventricular hypertrophy.


<< MMP-2 >> and MMP-9 expressions and activities in right ventricles increased significantly in [[ monocrotaline ]]-injected rats and captopril inhibited them.


MMP-2 and << MMP-9 >> expressions and activities in right ventricles increased significantly in [[ monocrotaline ]]-injected rats and captopril inhibited them.


<< MMP-2 >> and MMP-9 expressions and activities in right ventricles increased significantly in monocrotaline-injected rats and [[ captopril ]] inhibited them.


MMP-2 and << MMP-9 >> expressions and activities in right ventricles increased significantly in monocrotaline-injected rats and [[ captopril ]] inhibited them.


These findings indicate that captopril attenuates the development of << monocrotaline >>-induced right ventricular hypertrophy in association with inhibition of [[ MMP-2 ]] and MMP-9 in rats.


These findings indicate that captopril attenuates the development of << monocrotaline >>-induced right ventricular hypertrophy in association with inhibition of MMP-2 and [[ MMP-9 ]] in rats.


These findings indicate that << captopril >> attenuates the development of monocrotaline-induced right ventricular hypertrophy in association with inhibition of [[ MMP-2 ]] and MMP-9 in rats.


These findings indicate that << captopril >> attenuates the development of monocrotaline-induced right ventricular hypertrophy in association with inhibition of MMP-2 and [[ MMP-9 ]] in rats.


<< Thiazide >> and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of carbonic anhydrase ([[ CA ]], EC 4.2.1.1) with a very different profile as compared to classical inhibitors, such as acetazolamide, methazolamide, and ethoxzolamide.


<< Thiazide >> and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of carbonic anhydrase (CA, [[ EC 4.2.1.1 ]]) with a very different profile as compared to classical inhibitors, such as acetazolamide, methazolamide, and ethoxzolamide.


<< Thiazide >> and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of [[ carbonic anhydrase ]] (CA, EC 4.2.1.1) with a very different profile as compared to classical inhibitors, such as acetazolamide, methazolamide, and ethoxzolamide.


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of carbonic anhydrase (<< CA >>, EC 4.2.1.1) with a very different profile as compared to classical inhibitors, such as [[ acetazolamide ]], methazolamide, and ethoxzolamide.


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of carbonic anhydrase (CA, << EC 4.2.1.1 >>) with a very different profile as compared to classical inhibitors, such as [[ acetazolamide ]], methazolamide, and ethoxzolamide.


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of << carbonic anhydrase >> (CA, EC 4.2.1.1) with a very different profile as compared to classical inhibitors, such as [[ acetazolamide ]], methazolamide, and ethoxzolamide.


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of carbonic anhydrase (<< CA >>, EC 4.2.1.1) with a very different profile as compared to classical inhibitors, such as acetazolamide, [[ methazolamide ]], and ethoxzolamide.


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of carbonic anhydrase (CA, << EC 4.2.1.1 >>) with a very different profile as compared to classical inhibitors, such as acetazolamide, [[ methazolamide ]], and ethoxzolamide.


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of << carbonic anhydrase >> (CA, EC 4.2.1.1) with a very different profile as compared to classical inhibitors, such as acetazolamide, [[ methazolamide ]], and ethoxzolamide.


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of carbonic anhydrase (<< CA >>, EC 4.2.1.1) with a very different profile as compared to classical inhibitors, such as acetazolamide, methazolamide, and [[ ethoxzolamide ]].


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of carbonic anhydrase (CA, << EC 4.2.1.1 >>) with a very different profile as compared to classical inhibitors, such as acetazolamide, methazolamide, and [[ ethoxzolamide ]].


Thiazide and high ceiling diuretics were recently shown to inhibit all mammalian isoforms of << carbonic anhydrase >> (CA, EC 4.2.1.1) with a very different profile as compared to classical inhibitors, such as acetazolamide, methazolamide, and [[ ethoxzolamide ]].


Some of these structurally related compounds have a very different behavior against the widespread isozyme CA II, with << chlorthalidone >>, trichloromethiazide, and furosemide being efficient inhibitors against [[ CA II ]] (K(I)s of 65-138 nM), whereas indapamide is a much weaker one (K(I) of 2520 nM).


Some of these structurally related compounds have a very different behavior against the widespread isozyme CA II, with chlorthalidone, << trichloromethiazide >>, and furosemide being efficient inhibitors against [[ CA II ]] (K(I)s of 65-138 nM), whereas indapamide is a much weaker one (K(I) of 2520 nM).


Some of these structurally related compounds have a very different behavior against the widespread isozyme CA II, with chlorthalidone, trichloromethiazide, and << furosemide >> being efficient inhibitors against [[ CA II ]] (K(I)s of 65-138 nM), whereas indapamide is a much weaker one (K(I) of 2520 nM).


Some of these structurally related compounds have a very different behavior against the widespread isozyme CA II, with chlorthalidone, trichloromethiazide, and furosemide being efficient inhibitors against << CA II >> (K(I)s of 65-138 nM), whereas [[ indapamide ]] is a much weaker one (K(I) of 2520 nM).


<< Sergliflozin etabonate >>, a selective [[ SGLT2 ]] inhibitor, improves glycemic control in streptozotocin-induced diabetic rats and Zucker fatty rats.


The low-affinity << sodium glucose cotransporter >> (SGLT2) is responsible for most of the [[ glucose ]] reabsorption in the kidney and has been highlighted as a novel therapeutic target for the treatment of diabetes.


The low-affinity sodium glucose cotransporter (<< SGLT2 >>) is responsible for most of the [[ glucose ]] reabsorption in the kidney and has been highlighted as a novel therapeutic target for the treatment of diabetes.


We discovered << sergliflozin etabonate >>, a novel selective [[ SGLT2 ]] inhibitor, and found that selective inhibition of SGLT2 increased urinary glucose excretion and consequently decreased plasma glucose levels.


We discovered << sergliflozin etabonate >>, a novel selective SGLT2 inhibitor, and found that selective inhibition of [[ SGLT2 ]] increased urinary glucose excretion and consequently decreased plasma glucose levels.


In this report, we examined the antihyperglycemic effects of sergliflozin etabonate in normal and diabetic rats in comparison with those of a sulfonylurea (gliclazide) and an << alpha-glucosidase >> inhibitor ([[ voglibose ]]).


Chronic treatment with << sergliflozin etabonate >> reduced the levels of [[ glycated hemoglobin ]] and fasting plasma glucose, and improved the glycemic response after glucose loading in Zucker fatty rats.


Although the D1-like receptor, by itself, had no effect on VSMC proliferation, stimulation with << fenoldopam >>, a D1-like receptor agonist, inhibited the stimulatory effect of [[ insulin ]].


Although the D1-like receptor, by itself, had no effect on VSMC proliferation, stimulation with << fenoldopam >>, a [[ D1-like receptor ]] agonist, inhibited the stimulatory effect of insulin.


The inhibitory effect of << fenoldopam >> on [[ insulin ]]-mediated VSMC proliferation was receptor specific, because its effect could be blocked by SCH23390, a D1-like receptor antagonist.


The inhibitory effect of fenoldopam on insulin-mediated VSMC proliferation was receptor specific, because its effect could be blocked by << SCH23390 >>, a [[ D1-like receptor ]] antagonist.


<< Fenoldopam >> also inhibited [[ insulin receptor ]] mRNA and protein expression, which was time dependent and concentration dependent.


A PKC or MAP kinase inhibitor blocked the inhibitory effect of << fenoldopam >> on [[ insulin receptor ]] expression, indicating that PKC and MAP kinase were involved in the signaling pathway.


The progress of the enzymatic reaction of the hydrolysis of << acetylthiocholine >> at pH 8 in the presence of [[ AChE ]] and the inhibitor studied is determined by measuring at 230 nm the peak area of the reaction product thiocholine (TCh).


The mechanism of << OP >> poisoning involves inhibition of [[ acetylcholinesterase ]] (AChE) leading to inactivation of the enzyme which has an important role in neurotransmission.


The mechanism of << OP >> poisoning involves inhibition of acetylcholinesterase ([[ AChE ]]) leading to inactivation of the enzyme which has an important role in neurotransmission.


They act by reactivation of << AChE >> inhibited by [[ OP ]].


Presently, a combination of an antimuscarinic agent, e.g. atropine, << AChE >> reactivator such as one of the recommended pyridinium oximes (pralidoxime, [[ trimedoxime ]], obidoxime and HI-6) and diazepam are used for the treatment of OP poisoning in humans.


Presently, a combination of an antimuscarinic agent, e.g. atropine, << AChE >> reactivator such as one of the recommended pyridinium oximes (pralidoxime, trimedoxime, [[ obidoxime ]] and HI-6) and diazepam are used for the treatment of OP poisoning in humans.


Presently, a combination of an antimuscarinic agent, e.g. atropine, << AChE >> reactivator such as one of the recommended pyridinium oximes (pralidoxime, trimedoxime, obidoxime and [[ HI-6 ]]) and diazepam are used for the treatment of OP poisoning in humans.


Presently, a combination of an antimuscarinic agent, e.g. atropine, << AChE >> reactivator such as one of the recommended pyridinium oximes (pralidoxime, trimedoxime, obidoxime and HI-6) and [[ diazepam ]] are used for the treatment of OP poisoning in humans.


Presently, a combination of an antimuscarinic agent, e.g. << atropine >>, [[ AChE ]] reactivator such as one of the recommended pyridinium oximes (pralidoxime, trimedoxime, obidoxime and HI-6) and diazepam are used for the treatment of OP poisoning in humans.


Presently, a combination of an antimuscarinic agent, e.g. atropine, << AChE >> reactivator such as one of the recommended [[ pyridinium oximes ]] (pralidoxime, trimedoxime, obidoxime and HI-6) and diazepam are used for the treatment of OP poisoning in humans.


Presently, a combination of an antimuscarinic agent, e.g. atropine, << AChE >> reactivator such as one of the recommended pyridinium oximes ([[ pralidoxime ]], trimedoxime, obidoxime and HI-6) and diazepam are used for the treatment of OP poisoning in humans.


Presently, a combination of an antimuscarinic agent, e.g. atropine, << AChE >> reactivator such as one of the recommended pyridinium oximes (pralidoxime, trimedoxime, obidoxime and HI-6) and diazepam are used for the treatment of [[ OP ]] poisoning in humans.


<< Palonosetron >> is a second-generation serotonin 5-HT3 receptor antagonist, with a distinct pharmacological profile that differs from first-generation [[ 5-HT3 receptor ]] antagonists.


<< Palonosetron >> is a second-generation [[ serotonin 5-HT3 receptor ]] antagonist, with a distinct pharmacological profile that differs from first-generation 5-HT3 receptor antagonists.


Oral << palonosetron >> is likely to be a useful addition to oral formulations of other [[ 5-HT3 recepto ]]r antagonists in preventing CINV in patients receiving MEC.


Luteinizing hormone-releasing hormone (LHRH) agonists, such as << buserelin >>, goserelin, leuprorelin and triptorelin, stimulate the pituitary's [[ gonadotrophin-releasing hormone (GnRH) receptor ]], ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Luteinizing hormone-releasing hormone (LHRH) agonists, such as buserelin, << goserelin >>, leuprorelin and triptorelin, stimulate the pituitary's [[ gonadotrophin-releasing hormone (GnRH) receptor ]], ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Luteinizing hormone-releasing hormone (LHRH) agonists, such as buserelin, goserelin, << leuprorelin >> and triptorelin, stimulate the pituitary's [[ gonadotrophin-releasing hormone (GnRH) receptor ]], ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Luteinizing hormone-releasing hormone (LHRH) agonists, such as buserelin, goserelin, leuprorelin and << triptorelin >>, stimulate the pituitary's [[ gonadotrophin-releasing hormone (GnRH) receptor ]], ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Luteinizing hormone-releasing hormone (LHRH) agonists, such as << buserelin >>, goserelin, leuprorelin and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of [[ LH ]] and testosterone levels.


Luteinizing hormone-releasing hormone (LHRH) agonists, such as buserelin, << goserelin >>, leuprorelin and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of [[ LH ]] and testosterone levels.


Luteinizing hormone-releasing hormone (LHRH) agonists, such as buserelin, goserelin, << leuprorelin >> and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of [[ LH ]] and testosterone levels.


Luteinizing hormone-releasing hormone (LHRH) agonists, such as buserelin, goserelin, leuprorelin and << triptorelin >>, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of [[ LH ]] and testosterone levels.


<< Luteinizing hormone-releasing hormone >> (LHRH) agonists, such as [[ buserelin ]], goserelin, leuprorelin and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Luteinizing hormone-releasing hormone (<< LHRH >>) agonists, such as [[ buserelin ]], goserelin, leuprorelin and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


<< Luteinizing hormone-releasing hormone >> (LHRH) agonists, such as buserelin, [[ goserelin ]], leuprorelin and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Luteinizing hormone-releasing hormone (<< LHRH >>) agonists, such as buserelin, [[ goserelin ]], leuprorelin and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


<< Luteinizing hormone-releasing hormone >> (LHRH) agonists, such as buserelin, goserelin, [[ leuprorelin ]] and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Luteinizing hormone-releasing hormone (<< LHRH >>) agonists, such as buserelin, goserelin, [[ leuprorelin ]] and triptorelin, stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


<< Luteinizing hormone-releasing hormone >> (LHRH) agonists, such as buserelin, goserelin, leuprorelin and [[ triptorelin ]], stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Luteinizing hormone-releasing hormone (<< LHRH >>) agonists, such as buserelin, goserelin, leuprorelin and [[ triptorelin ]], stimulate the pituitary's gonadotrophin-releasing hormone (GnRH) receptor, ultimately leading to its de-sensitization and subsequent reduction of LH and testosterone levels.


Two pure << GnRH >> antagonists have been developed, [[ abarelix ]] and degarelix, that are devoid of any agonist effect on the GnRH receptor and consequently do not result in testosterone flare.


Two pure << GnRH >> antagonists have been developed, abarelix and [[ degarelix ]], that are devoid of any agonist effect on the GnRH receptor and consequently do not result in testosterone flare.


<< Abarelix >> was the first [[ GnRH ]] antagonist to be developed and was approved by the USA Food and Drug Administration in 2004 for the initiation of hormonal castration in advanced or metastasizing hormone-dependent prostate carcinoma, when rapid androgen suppression is necessary.


<< Fulvestrant >>, a pure [[ estrogen receptor ]] downregulator, is a new addition to the antiestrogen therapeutic armamentarium since its FDA approval in 2002.


The concentration of << estramustine phosphate >> required to inhibit the assembly or to induce the disassembly of [[ chick brain MAP2 ]]:tubulin microtubules is markedly dependent upon the microtubule protein concentration.


The concentration of << estramustine phosphate >> required to inhibit the assembly or to induce the disassembly of chick brain MAP2:[[ tubulin ]] microtubules is markedly dependent upon the microtubule protein concentration.


It is proposed that two molecules of << estramustine phosphate >> interact with each of the three tubulin-binding sites of MAP2 and inhibit the [[ MAP2 ]]:tubulin interaction by neutralising two highly conserved basic residues.


It is proposed that two molecules of << estramustine phosphate >> interact with each of the three tubulin-binding sites of MAP2 and inhibit the MAP2:[[ tubulin ]] interaction by neutralising two highly conserved basic residues.


Activity of << XL184 >> (Cabozantinib), an oral [[ tyrosine kinase ]] inhibitor, in patients with medullary thyroid cancer.


Activity of XL184 (<< Cabozantinib >>), an oral [[ tyrosine kinase ]] inhibitor, in patients with medullary thyroid cancer.


PURPOSE: XL184 (<< cabozantinib >>) is a potent inhibitor of MET, vascular endothelial growth factor receptor 2 ([[ VEGFR2 ]]), and RET, with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models.


PURPOSE: XL184 (<< cabozantinib >>) is a potent inhibitor of MET, vascular endothelial growth factor receptor 2 (VEGFR2), and [[ RET ]], with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models.


PURPOSE: XL184 (<< cabozantinib >>) is a potent inhibitor of [[ MET ]], vascular endothelial growth factor receptor 2 (VEGFR2), and RET, with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models.


PURPOSE: XL184 (<< cabozantinib >>) is a potent inhibitor of MET, [[ vascular endothelial growth factor receptor 2 ]] (VEGFR2), and RET, with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models.


PURPOSE: << XL184 >> (cabozantinib) is a potent inhibitor of MET, vascular endothelial growth factor receptor 2 ([[ VEGFR2 ]]), and RET, with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models.


PURPOSE: << XL184 >> (cabozantinib) is a potent inhibitor of MET, vascular endothelial growth factor receptor 2 (VEGFR2), and [[ RET ]], with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models.


PURPOSE: << XL184 >> (cabozantinib) is a potent inhibitor of [[ MET ]], vascular endothelial growth factor receptor 2 (VEGFR2), and RET, with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models.


PURPOSE: << XL184 >> (cabozantinib) is a potent inhibitor of MET, [[ vascular endothelial growth factor receptor 2 ]] (VEGFR2), and RET, with robust antiangiogenic, antitumor, and anti-invasive effects in preclinical models.


Further, we used this model to test the efficacy of << GDC-0941 >>, a [[ PI3K ]] inhibitor, in clinical development, and showed that the tumors respond to PI3K inhibition.


Further, we used this model to test the efficacy of << GDC-0941 >>, a PI3K inhibitor, in clinical development, and showed that the tumors respond to [[ PI3K ]] inhibition.


Inhibitory effect of synthetic << progestins >>, 4-MA and cyanoketone on [[ human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene-isomerase ]] activity.


Inhibitory effect of synthetic progestins, << 4-MA >> and cyanoketone on [[ human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene-isomerase ]] activity.


Inhibitory effect of synthetic progestins, 4-MA and << cyanoketone >> on [[ human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene-isomerase ]] activity.


<< Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase >> (3 beta-HSD) purified from human placenta transforms C-21 (pregnenolone and 17 alpha-hydroxy pregnenolone) as well as C-19 (dehydroepiandrosterone and androst-5-ene-3 beta, 17 beta-diol) steroids into the corresponding [[ 3-keto-4-ene-steroids ]] and is thus involved in the biosynthesis of all classes of hormonal steroids.


Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase (<< 3 beta-HSD >>) purified from human placenta transforms C-21 (pregnenolone and 17 alpha-hydroxy pregnenolone) as well as C-19 (dehydroepiandrosterone and androst-5-ene-3 beta, 17 beta-diol) steroids into the corresponding [[ 3-keto-4-ene-steroids ]] and is thus involved in the biosynthesis of all classes of hormonal steroids.


<< Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase >> (3 beta-HSD) purified from human placenta transforms C-21 ([[ pregnenolone ]] and 17 alpha-hydroxy pregnenolone) as well as C-19 (dehydroepiandrosterone and androst-5-ene-3 beta, 17 beta-diol) steroids into the corresponding 3-keto-4-ene-steroids and is thus involved in the biosynthesis of all classes of hormonal steroids.


Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase (<< 3 beta-HSD >>) purified from human placenta transforms C-21 ([[ pregnenolone ]] and 17 alpha-hydroxy pregnenolone) as well as C-19 (dehydroepiandrosterone and androst-5-ene-3 beta, 17 beta-diol) steroids into the corresponding 3-keto-4-ene-steroids and is thus involved in the biosynthesis of all classes of hormonal steroids.


<< Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase >> (3 beta-HSD) purified from human placenta transforms C-21 (pregnenolone and [[ 17 alpha-hydroxy pregnenolone ]]) as well as C-19 (dehydroepiandrosterone and androst-5-ene-3 beta, 17 beta-diol) steroids into the corresponding 3-keto-4-ene-steroids and is thus involved in the biosynthesis of all classes of hormonal steroids.


Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase (<< 3 beta-HSD >>) purified from human placenta transforms C-21 (pregnenolone and [[ 17 alpha-hydroxy pregnenolone ]]) as well as C-19 (dehydroepiandrosterone and androst-5-ene-3 beta, 17 beta-diol) steroids into the corresponding 3-keto-4-ene-steroids and is thus involved in the biosynthesis of all classes of hormonal steroids.


<< Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase >> (3 beta-HSD) purified from human placenta transforms C-21 (pregnenolone and 17 alpha-hydroxy pregnenolone) as well as C-19 ([[ dehydroepiandrosterone ]] and androst-5-ene-3 beta, 17 beta-diol) steroids into the corresponding 3-keto-4-ene-steroids and is thus involved in the biosynthesis of all classes of hormonal steroids.


Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase (<< 3 beta-HSD >>) purified from human placenta transforms C-21 (pregnenolone and 17 alpha-hydroxy pregnenolone) as well as C-19 ([[ dehydroepiandrosterone ]] and androst-5-ene-3 beta, 17 beta-diol) steroids into the corresponding 3-keto-4-ene-steroids and is thus involved in the biosynthesis of all classes of hormonal steroids.


<< Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase >> (3 beta-HSD) purified from human placenta transforms C-21 (pregnenolone and 17 alpha-hydroxy pregnenolone) as well as C-19 (dehydroepiandrosterone and [[ androst-5-ene-3 beta, 17 beta-diol ]]) steroids into the corresponding 3-keto-4-ene-steroids and is thus involved in the biosynthesis of all classes of hormonal steroids.


Human placental 3 beta-hydroxysteroid dehydrogenase/5----4-ene isomerase (<< 3 beta-HSD >>) purified from human placenta transforms C-21 (pregnenolone and 17 alpha-hydroxy pregnenolone) as well as C-19 (dehydroepiandrosterone and [[ androst-5-ene-3 beta, 17 beta-diol ]]) steroids into the corresponding 3-keto-4-ene-steroids and is thus involved in the biosynthesis of all classes of hormonal steroids.


<< Trilostane >>, epostane and cyanoketone are potent inhibitors of [[ 3 beta-HSD ]] with Ki values of approximately 50 nM.


Trilostane, << epostane >> and cyanoketone are potent inhibitors of [[ 3 beta-HSD ]] with Ki values of approximately 50 nM.


Trilostane, epostane and << cyanoketone >> are potent inhibitors of [[ 3 beta-HSD ]] with Ki values of approximately 50 nM.


<< 4-MA >>, a well known [[ 5 alpha-reductase ]] inhibitor, is also a potent inhibitor of 3 beta-HSD with a Ki value of 56 nM.


<< 4-MA >>, a well known 5 alpha-reductase inhibitor, is also a potent inhibitor of [[ 3 beta-HSD ]] with a Ki value of 56 nM.


<< Cyproterone acetate >>, a progestin used in the treatment of hirsutism, acne and prostate cancer as well as norgestrel and norethindrone that are widely used as oral contraceptives also inhibit [[ 3 beta-HSD ]] activity at Ki values of 1.5, 1.7 and 2.5 microM, respectively.


Cyproterone acetate, a << progestin >> used in the treatment of hirsutism, acne and prostate cancer as well as norgestrel and norethindrone that are widely used as oral contraceptives also inhibit [[ 3 beta-HSD ]] activity at Ki values of 1.5, 1.7 and 2.5 microM, respectively.


Cyproterone acetate, a progestin used in the treatment of hirsutism, acne and prostate cancer as well as << norgestrel >> and norethindrone that are widely used as oral contraceptives also inhibit [[ 3 beta-HSD ]] activity at Ki values of 1.5, 1.7 and 2.5 microM, respectively.


Cyproterone acetate, a progestin used in the treatment of hirsutism, acne and prostate cancer as well as norgestrel and << norethindrone >> that are widely used as oral contraceptives also inhibit [[ 3 beta-HSD ]] activity at Ki values of 1.5, 1.7 and 2.5 microM, respectively.


However, chronic treatment of cLH rats with << MPEP >> did not reverse learned helplessness, indicating that the enhanced [[ mGlu5 receptor ]] function is not the only player in the behavioral phenotype of this genetic model of depression.


Rescue of this impaired extinction consolidation/retrieval was achieved with d-cycloserine (N-methly-d-aspartate partial agonist) or << MS-275 >> ([[ histone deacetylase ]] (HDAC) inhibitor), applied after extinction training.


Rescue of this impaired extinction consolidation/retrieval was achieved with d-cycloserine (N-methly-d-aspartate partial agonist) or << MS-275 >> (histone deacetylase ([[ HDAC ]]) inhibitor), applied after extinction training.


Rescue of both impaired extinction acquisition and deficient extinction consolidation/retrieval was achieved with prior extinction training administration of valproic acid (a GABAergic enhancer and HDAC inhibitor) or AMN082 [metabotropic glutamate receptor 7 (mGlu7) agonist], while << MS-275 >> or PEPA ([[ AMPA receptor ]] potentiator) failed to affect extinction acquisition in S1 mice.


Rescue of both impaired extinction acquisition and deficient extinction consolidation/retrieval was achieved with prior extinction training administration of valproic acid (a GABAergic enhancer and HDAC inhibitor) or AMN082 [metabotropic glutamate receptor 7 (mGlu7) agonist], while MS-275 or << PEPA >> ([[ AMPA receptor ]] potentiator) failed to affect extinction acquisition in S1 mice.


Rescue of both impaired extinction acquisition and deficient extinction consolidation/retrieval was achieved with prior extinction training administration of << valproic acid >> (a GABAergic enhancer and [[ HDAC ]] inhibitor) or AMN082 [metabotropic glutamate receptor 7 (mGlu7) agonist], while MS-275 or PEPA (AMPA receptor potentiator) failed to affect extinction acquisition in S1 mice.


Rescue of both impaired extinction acquisition and deficient extinction consolidation/retrieval was achieved with prior extinction training administration of valproic acid (a GABAergic enhancer and HDAC inhibitor) or << AMN082 >> [[[ metabotropic glutamate receptor 7 ]] (mGlu7) agonist], while MS-275 or PEPA (AMPA receptor potentiator) failed to affect extinction acquisition in S1 mice.


Rescue of both impaired extinction acquisition and deficient extinction consolidation/retrieval was achieved with prior extinction training administration of valproic acid (a GABAergic enhancer and HDAC inhibitor) or << AMN082 >> [metabotropic glutamate receptor 7 ([[ mGlu7 ]]) agonist], while MS-275 or PEPA (AMPA receptor potentiator) failed to affect extinction acquisition in S1 mice.


Electroencephalographic recordings during substance consumption showed reduced alpha activity and << P300 >> latencies in the [[ nicotine ]] group compared to the control group.


These findings suggest that oral consumption of << nicotine >> enhances the efficacy of [[ nicotinic acetylcholine receptors ]].


Toxicity profile of small-molecule << IAP >> antagonist [[ GDC-0152 ]] is linked to TNF-α pharmacology.


<< GDC-0152 >> is a small-molecule drug that triggers tumor cell apoptosis by selectively antagonizing [[ IAPs ]].


<< GDC-0152 >> induces [[ NF-κB ]] transcriptional activity leading to expression of several chemokines and cytokines, of which tumor necrosis factor alpha (TNF-α) is the most important for single-agent tumor activity.


The << PARP >> inhibitor [[ PJ34 ]] modifies proliferation, NIS expression and epigenetic marks in thyroid cancer cell lines.


Since PARP-1 is supposed to be part of a multimeric repressor of sodium iodide symporter (NIS) expression, in this study the effect of the << PARP >> inhibitor [[ PJ34 ]] on several properties of thyroid cancer cell lines was investigated.


In TPC1, BCPAP, FRO, WRO cell lines << PJ34 >> induced a strong increase in [[ NIS ]] mRNA levels.


Accordingly, in transfection experiments performed in TPC1 cells, treatment with << PJ34 >> increased [[ NIS promoter ]] activity without affecting PARP-1 binding to the promoter sequence.


We also investigated the epigenetic status of NIS promoter after << PJ34 >> treatment in TPC1 cell line: in addition to an increase of [[ histone modification activation marks ]] (H3K9K14ac, H3K4me3), surprisingly we observed also an increase of H3K27me3, a classical repressive mark.


We also investigated the epigenetic status of NIS promoter after << PJ34 >> treatment in TPC1 cell line: in addition to an increase of histone modification activation marks ([[ H3K9K14ac ]], H3K4me3), surprisingly we observed also an increase of H3K27me3, a classical repressive mark.


We also investigated the epigenetic status of NIS promoter after << PJ34 >> treatment in TPC1 cell line: in addition to an increase of histone modification activation marks (H3K9K14ac, [[ H3K4me3 ]]), surprisingly we observed also an increase of H3K27me3, a classical repressive mark.


Both << apo-lycopenoic acids >> also decreased CSE-induced ROS production, 8-OHdG formation and reduced the increase in [[ NOX-4 ]] and COX-2 expressions caused by CSE.


Both << apo-lycopenoic acids >> also decreased CSE-induced ROS production, 8-OHdG formation and reduced the increase in NOX-4 and [[ COX-2 ]] expressions caused by CSE.


Recent studies, however, have demonstrated a promising potential treatment option with the help of the serum enzyme << butyrylcholinesterase >> (BChE), which is capable of breaking down naturally occurring [[ (-)-cocaine ]] before the drug can influence the reward centers of the brain or affect other areas of the body.


Recent studies, however, have demonstrated a promising potential treatment option with the help of the serum enzyme butyrylcholinesterase (<< BChE >>), which is capable of breaking down naturally occurring [[ (-)-cocaine ]] before the drug can influence the reward centers of the brain or affect other areas of the body.


This prompted the design of variants of << BChE >> which exhibit significantly improved catalytic activity against [[ (-)-cocaine ]].


Here, in expressing << cocaine >>-hydrolyzing mutants of [[ BChE ]] in Nicotiana benthamiana using the MagnICON virus-assisted transient expression system, and in reporting their initial biochemical analysis, we provide proof-of-principle that plants can express engineered BChE proteins with desired properties.


We examined in cats the 1) ulcerogenic effects of selective << COX-1 >> ([[ SC-560 ]], ketorolac) and COX-2 (celecoxib, meloxicam) inhibitors on the gastrointestinal mucosa, 2) effect of feeding and cimetidine on the expression of COX isoforms and prostaglandin E(2) (PGE(2)) level in the duodenum, and 3) localization of COX isoforms in the duodenum.


We examined in cats the 1) ulcerogenic effects of selective << COX-1 >> (SC-560, [[ ketorolac ]]) and COX-2 (celecoxib, meloxicam) inhibitors on the gastrointestinal mucosa, 2) effect of feeding and cimetidine on the expression of COX isoforms and prostaglandin E(2) (PGE(2)) level in the duodenum, and 3) localization of COX isoforms in the duodenum.