Aqueous << ethanol >> (80%) extract of lentil hulls exhibited high antioxidant and anti-inflammatory activities preferentially inhibiting 15-LOX (IC(50), 55 μg/ml), with moderate COX-1 (IC(50), 66 μg/ml) and [[ COX-2 ]] (IC(50), 119 μg/ml) inhibitory effects on the COX pathway, whereas faba bean hull extracts exerted relatively mild LOX inhibitory activity.


Aqueous << ethanol >> (80%) extract of lentil hulls exhibited high antioxidant and anti-inflammatory activities preferentially inhibiting 15-LOX (IC(50), 55 μg/ml), with moderate COX-1 (IC(50), 66 μg/ml) and COX-2 (IC(50), 119 μg/ml) inhibitory effects on the [[ COX ]] pathway, whereas faba bean hull extracts exerted relatively mild LOX inhibitory activity.


Aqueous << ethanol >> (80%) extract of lentil hulls exhibited high antioxidant and anti-inflammatory activities preferentially inhibiting 15-LOX (IC(50), 55 μg/ml), with moderate COX-1 (IC(50), 66 μg/ml) and COX-2 (IC(50), 119 μg/ml) inhibitory effects on the COX pathway, whereas faba bean hull extracts exerted relatively mild [[ LOX ]] inhibitory activity.


<< Histidine decarboxylase >> (HDC) catalyses the formation of histamine, a bioactive [[ amine ]].


Histidine decarboxylase (<< HDC >>) catalyses the formation of histamine, a bioactive [[ amine ]].


<< Histidine decarboxylase >> (HDC) catalyses the formation of [[ histamine ]], a bioactive amine.


Histidine decarboxylase (<< HDC >>) catalyses the formation of [[ histamine ]], a bioactive amine.


We searched for inhibitors of << HDC >> from the [[ ethyl acetate ]] extract of the petal of Filipendula ulmaria, also called meadowsweet.


Discovery of a novel series of << quinolone >> [[ α7 nicotinic acetylcholine receptor ]] agonists.


High throughput screening led to the identification of a novel series of << quinolone >> α7 nicotinic acetylcholine receptor ([[ nAChR ]]) agonists.


High throughput screening led to the identification of a novel series of << quinolone >> [[ α7 nicotinic acetylcholine receptor ]] (nAChR) agonists.


<< Amino acid >> derived quinazolines as [[ Rock ]]/PKA inhibitors.


<< Amino acid >> derived quinazolines as Rock/[[ PKA ]] inhibitors.


Amino acid derived << quinazolines >> as [[ Rock ]]/PKA inhibitors.


Amino acid derived << quinazolines >> as Rock/[[ PKA ]] inhibitors.


SAR and lead optimization studies for << Rock >> inhibitors based on [[ amino acid ]]-derived quinazolines are described.


SAR and lead optimization studies for << Rock >> inhibitors based on amino acid-derived [[ quinazolines ]] are described.


This is distinct from << Rock >> inhibitors based on non-[[ amino acid ]] derived quinazolinones, where high selectivity against PKA could be obtained.(22) The inhibitors presented here in some cases possessed sub-nanomolar inhibition of Rock, nanomolar potency in ppMLC cell based assays, low to fair cytochrome P-450 inhibition, and good human microsomal stability.


This is distinct from Rock inhibitors based on non-<< amino acid >> derived quinazolinones, where high selectivity against [[ PKA ]] could be obtained.(22) The inhibitors presented here in some cases possessed sub-nanomolar inhibition of Rock, nanomolar potency in ppMLC cell based assays, low to fair cytochrome P-450 inhibition, and good human microsomal stability.


This is distinct from << Rock >> inhibitors based on non-amino acid derived [[ quinazolinones ]], where high selectivity against PKA could be obtained.(22) The inhibitors presented here in some cases possessed sub-nanomolar inhibition of Rock, nanomolar potency in ppMLC cell based assays, low to fair cytochrome P-450 inhibition, and good human microsomal stability.


This is distinct from Rock inhibitors based on non-amino acid derived << quinazolinones >>, where high selectivity against [[ PKA ]] could be obtained.(22) The inhibitors presented here in some cases possessed sub-nanomolar inhibition of Rock, nanomolar potency in ppMLC cell based assays, low to fair cytochrome P-450 inhibition, and good human microsomal stability.


The << cyclooxygenase-2 >> inhibitor, [[ diflunisal ]], is used in the clinic for its anti-inflammatory activity.


Although there was no change in the levels of insulin receptor (IR), Akt (protein kinase B) and glucose transporter-4 (GLUT4) messenger RNA, << BPA >> significantly decreased the IR, [[ Akt ]] and GLUT4 protein levels (both plasma membrane and cytosolic fraction) of the gastrocnemius muscle.


Although there was no change in the levels of insulin receptor (IR), Akt (protein kinase B) and glucose transporter-4 (GLUT4) messenger RNA, << BPA >> significantly decreased the IR, Akt and [[ GLUT4 ]] protein levels (both plasma membrane and cytosolic fraction) of the gastrocnemius muscle.


Although there was no change in the levels of insulin receptor (IR), Akt (protein kinase B) and glucose transporter-4 (GLUT4) messenger RNA, << BPA >> significantly decreased the [[ IR ]], Akt and GLUT4 protein levels (both plasma membrane and cytosolic fraction) of the gastrocnemius muscle.


In conclusion, << BPA >> has adverse effects on phosphorylation of Akt, [[ GLUT4 ]] translocation and (14)C-glucose oxidation.


In conclusion, << BPA >> has adverse effects on phosphorylation of [[ Akt ]], GLUT4 translocation and (14)C-glucose oxidation.


The obtained results showed that << Cd >> increased lipid peroxidation and abnormal sperm count and decreased plasma testosterone, [[ lactate dehydrogenase ]], acid phosphatase, alkaline phosphatase and testicular steroidogenic enzymes: 3β-hydroxysteroid dehydrogenase (HSD), 17β-HSD activities as well as epididymal sperm counts and motility, while RUT and Se treatment reversed this change to control values.


The obtained results showed that << Cd >> increased lipid peroxidation and abnormal sperm count and decreased plasma testosterone, lactate dehydrogenase, [[ acid phosphatase ]], alkaline phosphatase and testicular steroidogenic enzymes: 3β-hydroxysteroid dehydrogenase (HSD), 17β-HSD activities as well as epididymal sperm counts and motility, while RUT and Se treatment reversed this change to control values.


The obtained results showed that << Cd >> increased lipid peroxidation and abnormal sperm count and decreased plasma testosterone, lactate dehydrogenase, acid phosphatase, [[ alkaline phosphatase ]] and testicular steroidogenic enzymes: 3β-hydroxysteroid dehydrogenase (HSD), 17β-HSD activities as well as epididymal sperm counts and motility, while RUT and Se treatment reversed this change to control values.


The obtained results showed that << Cd >> increased lipid peroxidation and abnormal sperm count and decreased plasma testosterone, lactate dehydrogenase, acid phosphatase, alkaline phosphatase and [[ testicular steroidogenic enzymes ]]: 3β-hydroxysteroid dehydrogenase (HSD), 17β-HSD activities as well as epididymal sperm counts and motility, while RUT and Se treatment reversed this change to control values.


The obtained results showed that << Cd >> increased lipid peroxidation and abnormal sperm count and decreased plasma testosterone, lactate dehydrogenase, acid phosphatase, alkaline phosphatase and testicular steroidogenic enzymes: [[ 3β-hydroxysteroid dehydrogenase ]] (HSD), 17β-HSD activities as well as epididymal sperm counts and motility, while RUT and Se treatment reversed this change to control values.


The obtained results showed that << Cd >> increased lipid peroxidation and abnormal sperm count and decreased plasma testosterone, lactate dehydrogenase, acid phosphatase, alkaline phosphatase and testicular steroidogenic enzymes: 3β-hydroxysteroid dehydrogenase ([[ HSD ]]), 17β-HSD activities as well as epididymal sperm counts and motility, while RUT and Se treatment reversed this change to control values.


The obtained results showed that << Cd >> increased lipid peroxidation and abnormal sperm count and decreased plasma testosterone, lactate dehydrogenase, acid phosphatase, alkaline phosphatase and testicular steroidogenic enzymes: 3β-hydroxysteroid dehydrogenase (HSD), [[ 17β-HSD ]] activities as well as epididymal sperm counts and motility, while RUT and Se treatment reversed this change to control values.


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GR), glutathione (GSH), and glutathione-S-transferase ([[ GST ]])).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system ([[ superoxide dismutase ]] (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GR), glutathione (GSH), and glutathione-S-transferase (GST)).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase ([[ SOD ]]), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GR), glutathione (GSH), and glutathione-S-transferase (GST)).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase (SOD), [[ catalase ]] (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GR), glutathione (GSH), and glutathione-S-transferase (GST)).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase (SOD), catalase ([[ CAT ]]), glutathione peroxidase (GSH-Px), glutathione reductase (GR), glutathione (GSH), and glutathione-S-transferase (GST)).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase (SOD), catalase (CAT), [[ glutathione peroxidase ]] (GSH-Px), glutathione reductase (GR), glutathione (GSH), and glutathione-S-transferase (GST)).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase ([[ GSH-Px ]]), glutathione reductase (GR), glutathione (GSH), and glutathione-S-transferase (GST)).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), [[ glutathione reductase ]] (GR), glutathione (GSH), and glutathione-S-transferase (GST)).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase ([[ GR ]]), glutathione (GSH), and glutathione-S-transferase (GST)).


Acute intoxication with << Cd >> was also followed by significantly decreased activity of the antioxidant defence system (superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GSH-Px), glutathione reductase (GR), glutathione (GSH), and [[ glutathione-S-transferase ]] (GST)).


The << tyrosine hydroxylase >> inhibitor [[ α-methyltyrosine ]] (300µM, 24h) completely abolished MeHg-induced DA release.


MeHg significantly increased DA precursor accumulation in cells treated with 3-hydroxybenzylhydrazine (10µM), revealing that << MeHg >> increases [[ tyrosine hydroxylase ]] activity.


The solubility-driven structural modification of (pyridin-3-yl) benzoxazinyl-oxazolidinones is described, which resulted in the development of a new series of << benzoxazinyl-oxazolidinone >> analogues with high antibacterial activity against Gram-positive pathogens, including that against linezolid-resistant strains and low [[ hERG ]] inhibition.


Secondary point mutations in the Fms-like tyrosine kinase 3 (FLT3) tyrosine kinase domain (KD) are common causes of acquired clinical resistance to the << FLT3 >> inhibitors [[ AC220 ]] (quizartinib) and sorafenib.


Secondary point mutations in the Fms-like tyrosine kinase 3 (FLT3) tyrosine kinase domain (KD) are common causes of acquired clinical resistance to the << FLT3 >> inhibitors AC220 ([[ quizartinib ]]) and sorafenib.


Secondary point mutations in the Fms-like tyrosine kinase 3 (FLT3) tyrosine kinase domain (KD) are common causes of acquired clinical resistance to the << FLT3 >> inhibitors AC220 (quizartinib) and [[ sorafenib ]].


<< Ponatinib >> (AP24534) is a [[ multikinase ]] inhibitor with in vitro and clinical activity in tyrosine kinase inhibitor (TKI)-resistant chronic myeloid leukemia, irrespective of BCR-ABL KD mutation.


Ponatinib (<< AP24534 >>) is a [[ multikinase ]] inhibitor with in vitro and clinical activity in tyrosine kinase inhibitor (TKI)-resistant chronic myeloid leukemia, irrespective of BCR-ABL KD mutation.


However, the involvement of the caspase-dependent pathway in the process of cell death induced by either BSC 3g or 3n is discarded since cell death could not be prevented by pretreatment with the pan<< caspase >> inhibitor [[ z-VAD-fmk ]].


Moreover, since reduced levels of << p21CIP1 >> and Chk2 proteins but no change in p53 levels could be detected in MCF-7 cells after [[ BSC ]] 3g or 3n treatment our results suggest that BSC treated cells die from lethal mitosis.


Moreover, since reduced levels of p21CIP1 and << Chk2 >> proteins but no change in p53 levels could be detected in MCF-7 cells after [[ BSC ]] 3g or 3n treatment our results suggest that BSC treated cells die from lethal mitosis.


A one-pot domino synthesis and discovery of highly functionalized << dihydrobenzo[b]thiophenes >> as [[ AChE ]] inhibitors.


These compounds were evaluated for their acetylcholinesterase (AChE) inhibitory activity and << 5-amino-2,7-bis(4-methoxyphenyl)-2,3-dihydrobenzo[b]thiophene-4,6-dicarbonitrile >> was found to be the most potent against [[ AChE ]] with IC50 4.16 μmol/L.


Furthermore, knockdown of OPN enhanced cell death caused by other drugs, including << paclitaxel >>, doxorubicin, actinomycin-D, and rapamycin, which are also [[ P-gp ]] substrates.


Furthermore, knockdown of OPN enhanced cell death caused by other drugs, including paclitaxel, << doxorubicin >>, actinomycin-D, and rapamycin, which are also [[ P-gp ]] substrates.


Furthermore, knockdown of OPN enhanced cell death caused by other drugs, including paclitaxel, doxorubicin, << actinomycin-D >>, and rapamycin, which are also [[ P-gp ]] substrates.


Furthermore, knockdown of OPN enhanced cell death caused by other drugs, including paclitaxel, doxorubicin, actinomycin-D, and << rapamycin >>, which are also [[ P-gp ]] substrates.


Compared with normally-fed counterparts, PM-CP rats exhibited higher glutathione S-transferase, aminopeptidase N and cysteine S-conjugate beta-lyase (CCBL) and lower gamma-glutamyltransferase activities, PM-FU rats exhibited decreased dihydropyrimidine dehydrogenase and cytochrome P450 1A1/2 activities and PM-<< MMC >> rats showed higher [[ quinone reductase ]] and depleted xanthine oxidase activities.


Compared with normally-fed counterparts, PM-CP rats exhibited higher glutathione S-transferase, aminopeptidase N and cysteine S-conjugate beta-lyase (CCBL) and lower gamma-glutamyltransferase activities, PM-FU rats exhibited decreased dihydropyrimidine dehydrogenase and cytochrome P450 1A1/2 activities and PM-<< MMC >> rats showed higher quinone reductase and depleted [[ xanthine oxidase ]] activities.


Conclusively, protein malnutrition alters CP, FU and << MMC >> metabolism in rat stomach by enhancing [[ CCBL ]] pathway for CP activation, delaying FU elimination and activating two-electron reduction of MMC, potentiating their gastrotoxicity.


N-acetylcysteine (NAC, 33 mM) and the c-jun N-terminal kinase (<< JNK >>) inhibitor ([[ SP600125 ]], 33 μM) further decreased the viability in the presence of DEP (200 μg/ml) and 3.3% FCS.


N-acetylcysteine (NAC, 33 mM) and the << c-jun N-terminal kinase >> (JNK) inhibitor ([[ SP600125 ]], 33 μM) further decreased the viability in the presence of DEP (200 μg/ml) and 3.3% FCS.


<< HENA >> activated the [[ BK (cbv1 + β1) channels ]] cloned from rat cerebral artery myocytes with a potency (EC50 = 53 μM) similar to and an efficacy (×2.5 potentiation) significantly greater than that of LCA.


HENA activated the << BK (cbv1 + β1) channels >> cloned from rat cerebral artery myocytes with a potency (EC50 = 53 μM) similar to and an efficacy (×2.5 potentiation) significantly greater than that of [[ LCA ]].


<< HENA >> failed to activate the channels made of cbv1 + β2, β3, β4, or β1T169A, indicating that this drug selectively targets [[ β1-containing BK channels ]] via the BK β1 steroid-sensing site.


Assessment of the abuse liability of << ABT-288 >>, a novel [[ histamine H3 receptor ]] antagonist.


RATIONALE: << Histamine H3 receptor >> antagonists, such as [[ ABT-288 ]], have been shown to possess cognitive-enhancing and wakefulness-promoting effects.


CONCLUSIONS: The sum of these preclinical data, the first of their kind applied to H3 antagonists, indicates that << ABT-288 >> is unlikely to possess a high potential for abuse in the human population and suggests that [[ H3 ]] antagonists, as a class, are similar in this regard.


Uptake of << estrone-3-sulfate >> (5 nM) by [[ OATP1B1 ]] was reduced by 82%-95%.


This methodology was subsequently used to assess the relative contribution of << OATP1B1 >> uptake in human hepatocytes for olmesartan (42%-62%), valsartan (28%-81%), rosuvastatin (64%-72%), [[ pitavastatin ]] (84%-98%) and lopinavir (64%-89%).


This methodology was subsequently used to assess the relative contribution of << OATP1B1 >> uptake in human hepatocytes for olmesartan (42%-62%), valsartan (28%-81%), rosuvastatin (64%-72%), pitavastatin (84%-98%) and [[ lopinavir ]] (64%-89%).


This methodology was subsequently used to assess the relative contribution of << OATP1B1 >> uptake in human hepatocytes for [[ olmesartan ]] (42%-62%), valsartan (28%-81%), rosuvastatin (64%-72%), pitavastatin (84%-98%) and lopinavir (64%-89%).


This methodology was subsequently used to assess the relative contribution of << OATP1B1 >> uptake in human hepatocytes for olmesartan (42%-62%), [[ valsartan ]] (28%-81%), rosuvastatin (64%-72%), pitavastatin (84%-98%) and lopinavir (64%-89%).


This methodology was subsequently used to assess the relative contribution of << OATP1B1 >> uptake in human hepatocytes for olmesartan (42%-62%), valsartan (28%-81%), [[ rosuvastatin ]] (64%-72%), pitavastatin (84%-98%) and lopinavir (64%-89%).


Oral << l-glutamine >> increases active [[ GLP-1 ]] (7-36) amide secretion and improves glycemic control in stretpozotocin-nicotinamide induced diabetic rats.


The objective of the present investigation was to evaluate << l-glutamine >> increases [[ glucagon like peptide-1 ]] (GLP-1) (7-36) amide secretion in streptozotocin-nicotinamide (STZ-NTM) induced diabetic Sprague Dawley rats.


The objective of the present investigation was to evaluate << l-glutamine >> increases glucagon like peptide-1 ([[ GLP-1 ]]) (7-36) amide secretion in streptozotocin-nicotinamide (STZ-NTM) induced diabetic Sprague Dawley rats.


<< l-glutamine >> decreased plasma glucose, increased plasma and pancreatic [[ insulin ]], increased plasma and colonic active GLP-1 (7-36) amide secretion as well as decreased oxidative stress in streptozotocin-nicotinamide induced diabetic rats.


<< l-glutamine >> decreased plasma glucose, increased plasma and pancreatic insulin, increased plasma and colonic active [[ GLP-1 ]] (7-36) amide secretion as well as decreased oxidative stress in streptozotocin-nicotinamide induced diabetic rats.


In the present study, << hinokitiol >> (1 and 2μM) inhibited the [[ collagen ]]-induced aggregation of human platelets, but did not inhibit the activation of platelets by other agonists, including thrombin, arachidonic acid, and ADP.


<< Hinokitiol >> inhibited the phosphorylation of [[ phospholipase C (PLC)γ2 ]], protein kinase C (PKC), mitogen-activated protein kinases (MAPKs), and Akt in collagen-activated human platelets, and significantly reduced intracellular calcium mobilization and hydroxyl radical (OH) formation.


<< Hinokitiol >> inhibited the phosphorylation of phospholipase C (PLC)γ2, [[ protein kinase C ]] (PKC), mitogen-activated protein kinases (MAPKs), and Akt in collagen-activated human platelets, and significantly reduced intracellular calcium mobilization and hydroxyl radical (OH) formation.


<< Hinokitiol >> inhibited the phosphorylation of phospholipase C (PLC)γ2, protein kinase C ([[ PKC ]]), mitogen-activated protein kinases (MAPKs), and Akt in collagen-activated human platelets, and significantly reduced intracellular calcium mobilization and hydroxyl radical (OH) formation.


<< Hinokitiol >> inhibited the phosphorylation of phospholipase C (PLC)γ2, protein kinase C (PKC), [[ mitogen-activated protein kinases ]] (MAPKs), and Akt in collagen-activated human platelets, and significantly reduced intracellular calcium mobilization and hydroxyl radical (OH) formation.


<< Hinokitiol >> inhibited the phosphorylation of phospholipase C (PLC)γ2, protein kinase C (PKC), mitogen-activated protein kinases ([[ MAPKs ]]), and Akt in collagen-activated human platelets, and significantly reduced intracellular calcium mobilization and hydroxyl radical (OH) formation.


<< Hinokitiol >> inhibited the phosphorylation of phospholipase C (PLC)γ2, protein kinase C (PKC), mitogen-activated protein kinases (MAPKs), and [[ Akt ]] in collagen-activated human platelets, and significantly reduced intracellular calcium mobilization and hydroxyl radical (OH) formation.


<< Hinokitiol >> inhibited the phosphorylation of phospholipase C (PLC)γ2, protein kinase C (PKC), mitogen-activated protein kinases (MAPKs), and Akt in [[ collagen ]]-activated human platelets, and significantly reduced intracellular calcium mobilization and hydroxyl radical (OH) formation.


<< Hinokitiol >> also reduced the [[ PKC ]] activation and platelet aggregation stimulated by PDBu.


In conclusion, << hinokitiol >> may inhibit platelet activation by inhibiting the [[ PLCγ2 ]]-PKC cascade and hydroxyl radical formation, followed by suppressing the activation of MAPKs and Akt.


In conclusion, << hinokitiol >> may inhibit platelet activation by inhibiting the PLCγ2-[[ PKC ]] cascade and hydroxyl radical formation, followed by suppressing the activation of MAPKs and Akt.


In conclusion, << hinokitiol >> may inhibit platelet activation by inhibiting the PLCγ2-PKC cascade and hydroxyl radical formation, followed by suppressing the activation of [[ MAPKs ]] and Akt.


In conclusion, << hinokitiol >> may inhibit platelet activation by inhibiting the PLCγ2-PKC cascade and hydroxyl radical formation, followed by suppressing the activation of MAPKs and [[ Akt ]].


Novel << 5-(benzyloxy)pyridin-2(1H)-one >> derivatives as potent [[ c-Met ]] inhibitors.


Design, Synthesis, and Pharmacological Characterization of Novel << Endomorphin-1 >> Analogues as Extremely Potent [[ μ-Opioid ]] Agonists.


Furthermore, no impact on cytokine release (i.e., on IL-10, IL-6, IL-12/23p40 and TNFα levels) was seen in LPS-stimulated human PBMCs, except with << JWH-210 >> and JWH-122 which caused a decrease of [[ TNFα ]] and IL-12/23p40.


Furthermore, no impact on cytokine release (i.e., on IL-10, IL-6, IL-12/23p40 and TNFα levels) was seen in LPS-stimulated human PBMCs, except with << JWH-210 >> and JWH-122 which caused a decrease of TNFα and [[ IL-12 ]]/23p40.


Furthermore, no impact on cytokine release (i.e., on IL-10, IL-6, IL-12/23p40 and TNFα levels) was seen in LPS-stimulated human PBMCs, except with << JWH-210 >> and JWH-122 which caused a decrease of TNFα and IL-12/[[ 23p40 ]].


Furthermore, no impact on cytokine release (i.e., on IL-10, IL-6, IL-12/23p40 and TNFα levels) was seen in LPS-stimulated human PBMCs, except with JWH-210 and << JWH-122 >> which caused a decrease of [[ TNFα ]] and IL-12/23p40.


Furthermore, no impact on cytokine release (i.e., on IL-10, IL-6, IL-12/23p40 and TNFα levels) was seen in LPS-stimulated human PBMCs, except with JWH-210 and << JWH-122 >> which caused a decrease of TNFα and [[ IL-12 ]]/23p40.


Furthermore, no impact on cytokine release (i.e., on IL-10, IL-6, IL-12/23p40 and TNFα levels) was seen in LPS-stimulated human PBMCs, except with JWH-210 and << JWH-122 >> which caused a decrease of TNFα and IL-12/[[ 23p40 ]].


<< AlCl3 >> markedly reduced AA performance and activities of [[ cytochrome c oxidase ]] (COX) and acetylcholinesterase (AChE) in all regions.


<< AlCl3 >> markedly reduced AA performance and activities of cytochrome c oxidase ([[ COX ]]) and acetylcholinesterase (AChE) in all regions.


<< AlCl3 >> markedly reduced AA performance and activities of cytochrome c oxidase (COX) and [[ acetylcholinesterase ]] (AChE) in all regions.


<< AlCl3 >> markedly reduced AA performance and activities of cytochrome c oxidase (COX) and acetylcholinesterase ([[ AChE ]]) in all regions.


GTLE pretreatment completely reversed the damaging effects of << AlCl3 >> on AA and [[ superoxide dismutase ]] activity, markedly corrected COX and AChE activities, and moderately improved TGC.


GTLE pretreatment completely reversed the damaging effects of << AlCl3 >> on AA and superoxide dismutase activity, markedly corrected [[ COX ]] and AChE activities, and moderately improved TGC.


GTLE pretreatment completely reversed the damaging effects of << AlCl3 >> on AA and superoxide dismutase activity, markedly corrected COX and [[ AChE ]] activities, and moderately improved TGC.


Our study demonstrated that << curcumin >> inhibited OVA-induced increases in eosinophil count; interleukin (IL)-17A level were recovered in bronchoalveolar lavage fluid increased [[ IL-10 ]] level in bronchoalveolar lavage fluid.


Our study demonstrated that << curcumin >> inhibited [[ OVA ]]-induced increases in eosinophil count; interleukin (IL)-17A level were recovered in bronchoalveolar lavage fluid increased IL-10 level in bronchoalveolar lavage fluid.


Our study demonstrated that << curcumin >> inhibited OVA-induced increases in eosinophil count; [[ interleukin (IL)-17A ]] level were recovered in bronchoalveolar lavage fluid increased IL-10 level in bronchoalveolar lavage fluid.


Histological studies demonstrated that << curcumin >> substantially inhibited [[ OVA ]]-induced eosinophilia in lung tissue.


The results in vivo show << ovalbumin >>-induced significantly broke Treg/Th17 balance; [[ curcumin ]] treatments markedly attenuated the inflammatory in asthma model by regulating Treg/Th17 balance.


Synthesis of a << DOTA >> (Gd(3+))-conjugate of [[ proton-pump ]] inhibitor pantoprazole for gastric wall imaging studies.


Synthesis of a DOTA (<< Gd(3+) >>)-conjugate of [[ proton-pump ]] inhibitor pantoprazole for gastric wall imaging studies.


Synthesis of a DOTA (Gd(3+))-conjugate of << proton-pump >> inhibitor [[ pantoprazole ]] for gastric wall imaging studies.


To overcome this limitation, we de novo synthesized a conjugate that covalently combines a << Gd >>-based MRI contrast agent, encaged with a chelating agent (DOTA), with pantoprazole, which is a widely used [[ proton pump ]] inhibitor that binds to proton pumps in the stomach and colon.


To overcome this limitation, we de novo synthesized a conjugate that covalently combines a Gd-based MRI contrast agent, encaged with a chelating agent (<< DOTA >>), with pantoprazole, which is a widely used [[ proton pump ]] inhibitor that binds to proton pumps in the stomach and colon.


To overcome this limitation, we de novo synthesized a conjugate that covalently combines a Gd-based MRI contrast agent, encaged with a chelating agent (DOTA), with << pantoprazole >>, which is a widely used [[ proton pump ]] inhibitor that binds to proton pumps in the stomach and colon.


Second, EPSCs were recorded from rat hippocampal slices before and after their superfusion with the reversible << AChE >> inhibitor [[ donepezil ]] (100nM).


A Nanogram Dose of the << CYP3A >> Probe Substrate [[ Midazolam ]] to Evaluate Drug Interactions.


We then evaluated the interactions with the << CYP3A >> inhibitor [[ ketoconazole ]] (400 mg q.d.) after nanogram and regular doses of midazolam.


<< CYP3A5 >> carrier status had no influence on midazolam oral clearance or its inhibition by [[ ketoconazole ]].


<< CYP3A5 >> carrier status had no influence on [[ midazolam ]] oral clearance or its inhibition by ketoconazole.


Metabolism of << Beclomethasone Dipropionate >> by [[ Cytochrome P450 3A ]] Enzymes.


It is possible that variations in << cytochrome P450 3A >> enzyme-mediated metabolism of [[ BDP ]] may contribute to this phenomenon.


This hypothesis was explored by evaluating the contributions of CYP3A4, 3A5, 3A7, and << esterase >> enzymes in the metabolism of [[ BDP ]] in vitro and relating metabolism to changes in CYP3A enzyme mRNA expression via the glucocorticoid receptor in lung and liver cells.


<< CYP3A4 >> and CYP3A5 metabolized [[ BDP ]] via hydroxylation ([M4] and [M6]) and dehydrogenation ([M5]) at similar rates; CYP3A7 did not metabolize BDP.


CYP3A4 and << CYP3A5 >> metabolized [[ BDP ]] via hydroxylation ([M4] and [M6]) and dehydrogenation ([M5]) at similar rates; CYP3A7 did not metabolize BDP.


These studies show that << CYP3A4 >> and CYP3A5 metabolize [[ BDP ]] to inactive metabolites and suggest that differences in the expression or function of these enzymes in the lung and/or liver could influence BDP disposition in humans.


These studies show that CYP3A4 and << CYP3A5 >> metabolize [[ BDP ]] to inactive metabolites and suggest that differences in the expression or function of these enzymes in the lung and/or liver could influence BDP disposition in humans.


In macrophages, levels of << TNF-α >>, IFN-γ, NO, IL-6 and IL-10 were increased by [[ CDM ]] used alone or in combination with HSV-2.


In macrophages, levels of TNF-α, << IFN-γ >>, NO, IL-6 and IL-10 were increased by [[ CDM ]] used alone or in combination with HSV-2.


In macrophages, levels of TNF-α, IFN-γ, NO, << IL-6 >> and IL-10 were increased by [[ CDM ]] used alone or in combination with HSV-2.


In macrophages, levels of TNF-α, IFN-γ, NO, IL-6 and << IL-10 >> were increased by [[ CDM ]] used alone or in combination with HSV-2.


Besides, << CDM >> not only synergized [[ TNF-α ]] production combined with IFN-γ, but also prolonged its expression in time.


Besides, << CDM >> not only synergized TNF-α production combined with [[ IFN-γ ]], but also prolonged its expression in time.


Results indicate that << CDM >> inhibits HSV-2 multiplication in epithelial cells and also increases [[ cytokine ]] production in macrophages, both important actions to the clearance of infecting virus in the mouse vagina.


Intestinal and hepatic first-pass extraction of the << 11β-HSD1 >> inhibitor [[ AMG 221 ]] in rats with chronic vascular catheters.


A catheterized rat model was used to define the intestinal and hepatic components of oral bioavailability for an << 11β-HSD1 >> inhibitor, [[ AMG 221 ]].


In DU-PM cells with acquired resistance to << elisidepsin >>, ErbB3 expression was decreased, while [[ Bcl2 ]] was increased.


In DU-PM cells with acquired resistance to << elisidepsin >>, [[ ErbB3 ]] expression was decreased, while Bcl2 was increased.


Administration of << bicuculline >>, a [[ GABAA ]] inhibitor, isolated a single response to ω-agatoxin, which was characterized by a reduction in network activity.


Administration of << bicuculline >>, a GABAA inhibitor, isolated a single response to [[ ω-agatoxin ]], which was characterized by a reduction in network activity.


<< tert-Butylcarbamate >>-Containing [[ Histone Deacetylase ]] Inhibitors: Apoptosis Induction, Cytodifferentiation, and Antiproliferative Activities in Cancer Cells.


Herein we report novel pyrrole- and benzene-based hydroxamates (8, 10) and 2'-aminoanilides (9, 11) bearing the << tert-butylcarbamate >> group at the CAP moiety as [[ histone deacetylase ]] (HDAC) inhibitors.


Herein we report novel pyrrole- and benzene-based hydroxamates (8, 10) and 2'-aminoanilides (9, 11) bearing the << tert-butylcarbamate >> group at the CAP moiety as histone deacetylase ([[ HDAC ]]) inhibitors.


Herein we report novel << pyrrole >>- and benzene-based hydroxamates (8, 10) and 2'-aminoanilides (9, 11) bearing the tert-butylcarbamate group at the CAP moiety as [[ histone deacetylase ]] (HDAC) inhibitors.


Herein we report novel << pyrrole >>- and benzene-based hydroxamates (8, 10) and 2'-aminoanilides (9, 11) bearing the tert-butylcarbamate group at the CAP moiety as histone deacetylase ([[ HDAC ]]) inhibitors.


Herein we report novel pyrrole- and << benzene >>-based hydroxamates (8, 10) and 2'-aminoanilides (9, 11) bearing the tert-butylcarbamate group at the CAP moiety as [[ histone deacetylase ]] (HDAC) inhibitors.


Herein we report novel pyrrole- and << benzene >>-based hydroxamates (8, 10) and 2'-aminoanilides (9, 11) bearing the tert-butylcarbamate group at the CAP moiety as histone deacetylase ([[ HDAC ]]) inhibitors.


Herein we report novel pyrrole- and benzene-based << hydroxamates >> (8, 10) and 2'-aminoanilides (9, 11) bearing the tert-butylcarbamate group at the CAP moiety as [[ histone deacetylase ]] (HDAC) inhibitors.


Herein we report novel pyrrole- and benzene-based << hydroxamates >> (8, 10) and 2'-aminoanilides (9, 11) bearing the tert-butylcarbamate group at the CAP moiety as histone deacetylase ([[ HDAC ]]) inhibitors.


Herein we report novel pyrrole- and benzene-based hydroxamates (8, 10) and << 2'-aminoanilides >> (9, 11) bearing the tert-butylcarbamate group at the CAP moiety as [[ histone deacetylase ]] (HDAC) inhibitors.


Herein we report novel pyrrole- and benzene-based hydroxamates (8, 10) and << 2'-aminoanilides >> (9, 11) bearing the tert-butylcarbamate group at the CAP moiety as histone deacetylase ([[ HDAC ]]) inhibitors.


Compounds 8 b and 10 c selectively inhibited HDAC6 at the nanomolar level, whereas the other << hydroxamates >> effected an increase in [[ acetyl-α-tubulin ]] levels in human acute myeloid leukemia U937 cells.


Discovery of a synthetic << Aminopeptidase N >> inhibitor [[ LB-4b ]] as a potential anticancer agent.


<< LB-4b >> is the first synthetic [[ APN ]] inhibitor to be evaluated for both of its anti-invasion and anti-angiogenesis effects.


As a potent synthetic << APN >> inhibitor (IC50=850nM, versus [[ bestatin ]] of 8.1μM), LB-4b was determined to have more significant block effects to cancer cell invasion and angiogenesis than bestatin.


As a potent synthetic << APN >> inhibitor (IC50=850nM, versus bestatin of 8.1μM), [[ LB-4b ]] was determined to have more significant block effects to cancer cell invasion and angiogenesis than bestatin.


As a potent synthetic << APN >> inhibitor (IC50=850nM, versus bestatin of 8.1μM), LB-4b was determined to have more significant block effects to cancer cell invasion and angiogenesis than [[ bestatin ]].


Both types of granules contain << catechol oxidase >> that catalyzes oxidative cross-linking of [[ L-DOPA ]].


Under << NaCl >> and sorbitol stresses, [[ catalase ]] (CAT) activity in wnk8 mutant was 1.92- and 3.7-times of that in Col-0, respectively.


Under << NaCl >> and sorbitol stresses, catalase ([[ CAT ]]) activity in wnk8 mutant was 1.92- and 3.7-times of that in Col-0, respectively.


Under NaCl and << sorbitol >> stresses, [[ catalase ]] (CAT) activity in wnk8 mutant was 1.92- and 3.7-times of that in Col-0, respectively.


Under NaCl and << sorbitol >> stresses, catalase ([[ CAT ]]) activity in wnk8 mutant was 1.92- and 3.7-times of that in Col-0, respectively.


Immunofluorescence staining and western blotting demonstrated that << cilostazol >> treatment reduced GFAP and [[ VEGF ]] expression in the retinas of OLETF rats.


Immunofluorescence staining and western blotting demonstrated that << cilostazol >> treatment reduced [[ GFAP ]] and VEGF expression in the retinas of OLETF rats.


Other dams received 1.8ng/kg/day of a mixture of << aryl hydrocarbon receptor >> (AhR) agonists (non-ortho PCBs, PC-dibenzodioxins and [[ PC-dibenzofurans ]]) without or with 0.5M (0.5MAhR).


Other dams received 1.8ng/kg/day of a mixture of << aryl hydrocarbon receptor >> (AhR) agonists ([[ non-ortho PCB ]]s, PC-dibenzodioxins and PC-dibenzofurans) without or with 0.5M (0.5MAhR).


Other dams received 1.8ng/kg/day of a mixture of << aryl hydrocarbon receptor >> (AhR) agonists (non-ortho PCBs, [[ PC-dibenzodioxins ]] and PC-dibenzofurans) without or with 0.5M (0.5MAhR).


Discovery of a series of novel << 5H-pyrrolo[2,3-b]pyrazine-2-phenyl ethers >>, as potent [[ JAK3 ]] kinase inhibitors.


Discovery of a series of novel << 5H-pyrrolo[2,3-b]pyrazine-2-phenyl ethers >>, as potent JAK3 [[ kinase ]] inhibitors.


We report the discovery of a novel series of ATP-competitive << Janus kinase 3 >> (JAK3) inhibitors based on the [[ 5H-pyrrolo[2,3-b]pyrazine ]] scaffold.


We report the discovery of a novel series of ATP-competitive Janus kinase 3 (<< JAK3 >>) inhibitors based on the [[ 5H-pyrrolo[2,3-b]pyrazine ]] scaffold.


<< Arsenic trioxide >> depletes cancer stem-like cells and inhibits repopulation of neurosphere derived from glioblastoma by downregulation of [[ Notch ]] pathway.


<< ATO >> inhibited the phosphorylation and activation of AKT and STAT3 through [[ Notch ]] signaling blockade.


<< ATO >> inhibited the phosphorylation and activation of AKT and [[ STAT3 ]] through Notch signaling blockade.


<< ATO >> inhibited the phosphorylation and activation of [[ AKT ]] and STAT3 through Notch signaling blockade.


These data show that the << ATO >> is a promising new approach to decrease glioblastoma proliferation and recurrence by downregulation of [[ Notch ]] pathway.


The high fat diet significantly increased hepatic mRNA expressions of << PPARγ >>, SREBP1C and SCD-1 genes in comparison to the control diet, which was subsequently reversed by supplementation with [[ fisetin ]].


The high fat diet significantly increased hepatic mRNA expressions of PPARγ, << SREBP1C >> and SCD-1 genes in comparison to the control diet, which was subsequently reversed by supplementation with [[ fisetin ]].


The high fat diet significantly increased hepatic mRNA expressions of PPARγ, SREBP1C and << SCD-1 >> genes in comparison to the control diet, which was subsequently reversed by supplementation with [[ fisetin ]].


In addition, << fisetin >> supplementation significantly reduced hepatic mRNA abundance of [[ FAS ]], ATPCL and G6Pase compared to the control group.


In addition, << fisetin >> supplementation significantly reduced hepatic mRNA abundance of FAS, [[ ATPCL ]] and G6Pase compared to the control group.


In addition, << fisetin >> supplementation significantly reduced hepatic mRNA abundance of FAS, ATPCL and [[ G6Pase ]] compared to the control group.


Finally, epididymal mRNA abundance of << GLUT4 >> was significantly increased by [[ fisetin ]] supplementation, compared to levels in the control and HF groups.


Enhancement of << GLUT4 >> expression by [[ fisetin ]] was further confirmed in differentiated 3T3-L1 adipocytes.


Western blot assay demonstrated that << DICO >> decreased Bcl-2 level and induced [[ Bax ]] translocation to cause cytochrome c release.


Western blot assay demonstrated that << DICO >> decreased Bcl-2 level and induced Bax translocation to cause [[ cytochrome c ]] release.


Western blot assay demonstrated that << DICO >> decreased [[ Bcl-2 ]] level and induced Bax translocation to cause cytochrome c release.


<< Quercetin >> and rutin also increased [[ alkaline phosphatase ]] activity by about 150 and 240% and demonstrated mineralization up to 110 and 200% respectively as compared to control (which was considered as 100%).


Quercetin and << rutin >> also increased [[ alkaline phosphatase ]] activity by about 150 and 240% and demonstrated mineralization up to 110 and 200% respectively as compared to control (which was considered as 100%).


Further, both the << flavonoids >> were also found to increase the expression of some of the prominent markers for differentiation of osteoblast like [[ osteopontin ]], osterix, RunX2, osteoprotegerin and osteocalcin.


Further, both the << flavonoids >> were also found to increase the expression of some of the prominent markers for differentiation of osteoblast like osteopontin, [[ osterix ]], RunX2, osteoprotegerin and osteocalcin.


Further, both the << flavonoids >> were also found to increase the expression of some of the prominent markers for differentiation of osteoblast like osteopontin, osterix, [[ RunX2 ]], osteoprotegerin and osteocalcin.


Further, both the << flavonoids >> were also found to increase the expression of some of the prominent markers for differentiation of osteoblast like osteopontin, osterix, RunX2, [[ osteoprotegerin ]] and osteocalcin.


Further, both the << flavonoids >> were also found to increase the expression of some of the prominent markers for differentiation of osteoblast like osteopontin, osterix, RunX2, osteoprotegerin and [[ osteocalcin ]].


<< Cytochrome P450 2E1 >> (CYP 450 2E1), activity was determined as hydroxylation of [[ aniline ]] in liver microsomes.


Cytochrome P450 2E1 (<< CYP 450 2E1 >>), activity was determined as hydroxylation of [[ aniline ]] in liver microsomes.


Serum markers of liver damage (<< AST >>, ALT, ALP and Bilirubin) were increased by [[ CCl4 ]] and TAA intoxication (p<0.001), whereas co-treatment with NAC reversed such changes (p<0.001).


Serum markers of liver damage (AST, << ALT >>, ALP and Bilirubin) were increased by [[ CCl4 ]] and TAA intoxication (p<0.001), whereas co-treatment with NAC reversed such changes (p<0.001).


Serum markers of liver damage (AST, ALT, << ALP >> and Bilirubin) were increased by [[ CCl4 ]] and TAA intoxication (p<0.001), whereas co-treatment with NAC reversed such changes (p<0.001).


Serum markers of liver damage (<< AST >>, ALT, ALP and Bilirubin) were increased by CCl4 and [[ TAA ]] intoxication (p<0.001), whereas co-treatment with NAC reversed such changes (p<0.001).


Serum markers of liver damage (AST, << ALT >>, ALP and Bilirubin) were increased by CCl4 and [[ TAA ]] intoxication (p<0.001), whereas co-treatment with NAC reversed such changes (p<0.001).


Serum markers of liver damage (AST, ALT, << ALP >> and Bilirubin) were increased by CCl4 and [[ TAA ]] intoxication (p<0.001), whereas co-treatment with NAC reversed such changes (p<0.001).


Serum markers of liver damage (<< AST >>, ALT, ALP and Bilirubin) were increased by CCl4 and TAA intoxication (p<0.001), whereas co-treatment with [[ NAC ]] reversed such changes (p<0.001).


Serum markers of liver damage (AST, << ALT >>, ALP and Bilirubin) were increased by CCl4 and TAA intoxication (p<0.001), whereas co-treatment with [[ NAC ]] reversed such changes (p<0.001).


Serum markers of liver damage (AST, ALT, << ALP >> and Bilirubin) were increased by CCl4 and TAA intoxication (p<0.001), whereas co-treatment with [[ NAC ]] reversed such changes (p<0.001).


LPO was increased while as GSH, << CAT >> and GPx decreased by the administration of CCl4 and TAA (p<0.001); co-administration of [[ NAC ]] restored these liver markers to normal levels (p<0.001).


LPO was increased while as GSH, CAT and << GPx >> decreased by the administration of CCl4 and TAA (p<0.001); co-administration of [[ NAC ]] restored these liver markers to normal levels (p<0.001).


This report concerns the marked up-regulation in differentiated CaCo-2 colonic epithelial cells of two key inflammatory << interleukins >>, IL-6 and IL-8, caused by a mixture of [[ oxysterols ]] representative of a high cholesterol diet.


This report concerns the marked up-regulation in differentiated CaCo-2 colonic epithelial cells of two key inflammatory interleukins, << IL-6 >> and IL-8, caused by a mixture of [[ oxysterols ]] representative of a high cholesterol diet.


This report concerns the marked up-regulation in differentiated CaCo-2 colonic epithelial cells of two key inflammatory interleukins, IL-6 and << IL-8 >>, caused by a mixture of [[ oxysterols ]] representative of a high cholesterol diet.


This report concerns the marked up-regulation in differentiated CaCo-2 colonic epithelial cells of two key inflammatory << interleukins >>, IL-6 and IL-8, caused by a mixture of oxysterols representative of a high [[ cholesterol ]] diet.


This report concerns the marked up-regulation in differentiated CaCo-2 colonic epithelial cells of two key inflammatory interleukins, << IL-6 >> and IL-8, caused by a mixture of oxysterols representative of a high [[ cholesterol ]] diet.


This report concerns the marked up-regulation in differentiated CaCo-2 colonic epithelial cells of two key inflammatory interleukins, IL-6 and << IL-8 >>, caused by a mixture of oxysterols representative of a high [[ cholesterol ]] diet.


<< Oxysterol >>-dependent [[ NOX1 ]] activation, as well as interleukin synthesis, were completely prevented by Cannonau red wine extract that contains an abundant phenolic fraction, in particular phenolic acids and flavonoids.


<< Oxysterol >>-dependent NOX1 activation, as well as [[ interleukin ]] synthesis, were completely prevented by Cannonau red wine extract that contains an abundant phenolic fraction, in particular phenolic acids and flavonoids.


Oxysterol-dependent NOX1 activation, as well as << interleukin >> synthesis, were completely prevented by Cannonau red wine extract that contains an abundant phenolic fraction, in particular [[ phenolic acids ]] and flavonoids.


Oxysterol-dependent NOX1 activation, as well as << interleukin >> synthesis, were completely prevented by Cannonau red wine extract that contains an abundant phenolic fraction, in particular phenolic acids and [[ flavonoids ]].


Oxysterol-dependent << NOX1 >> activation, as well as interleukin synthesis, were completely prevented by Cannonau red wine extract that contains an abundant phenolic fraction, in particular [[ phenolic acids ]] and flavonoids.


Oxysterol-dependent << NOX1 >> activation, as well as interleukin synthesis, were completely prevented by Cannonau red wine extract that contains an abundant phenolic fraction, in particular phenolic acids and [[ flavonoids ]].


Conversely, cell pre-treatment with Vermentino white wine extract with smaller phenolic fraction showed only a partial NOX1 down-regulation and was ineffective in << interleukin >> synthesis induced by dietary [[ oxysterols ]].


Conversely, cell pre-treatment with Vermentino white wine extract with smaller phenolic fraction showed only a partial << NOX1 >> down-regulation and was ineffective in interleukin synthesis induced by dietary [[ oxysterols ]].


Besides this direct activity, an excess of phenolic compounds detectable in red wine, may exert an additional indirect action by blocking << oxysterol >>-related [[ NOX1 ]] induction, thus totally preventing the pro-oxidant and pro-inflammatory events triggered by dietary oxysterols.


Besides this direct activity, an excess of << phenolic >> compounds detectable in red wine, may exert an additional indirect action by blocking oxysterol-related [[ NOX1 ]] induction, thus totally preventing the pro-oxidant and pro-inflammatory events triggered by dietary oxysterols.


<< Arsenic >> inhibits autophagic flux activating the [[ Nrf2 ]]-Keap1 pathway in a p62-dependent manner.


<< Arsenic >> inhibits autophagic flux activating the Nrf2-[[ Keap1 ]] pathway in a p62-dependent manner.


<< Arsenic >> deregulates the autophagic pathway through blockage of autophagic flux, resulting in accumulation of autophagosomes and sequestration of [[ p62 ]], Keap1, and LC3.


<< Arsenic >> deregulates the autophagic pathway through blockage of autophagic flux, resulting in accumulation of autophagosomes and sequestration of p62, [[ Keap1 ]], and LC3.


<< Arsenic >> deregulates the autophagic pathway through blockage of autophagic flux, resulting in accumulation of autophagosomes and sequestration of p62, Keap1, and [[ LC3 ]].


Thus, << arsenic >> activates [[ Nrf2 ]] through a non-canonical mechanism (p62-dependent), leading to a chronic, sustained activation of Nrf2.


Thus, << arsenic >> activates Nrf2 through a non-canonical mechanism (p62-dependent), leading to a chronic, sustained activation of [[ Nrf2 ]].


In contrast, activation of << Nrf2 >> by [[ sulforaphane ]] and tert-butylhydroquinone depend upon Keap1-C151 and not p62 (the canonical mechanism).


In contrast, activation of << Nrf2 >> by sulforaphane and [[ tert-butylhydroquinone ]] depend upon Keap1-C151 and not p62 (the canonical mechanism).


Collectively, these findings provide evidence that << arsenic >> causes prolonged activation of [[ Nrf2 ]] through autophagy dysfunction, possibly providing a similar scenario to constitutive activation of Nrf2 found in certain human cancers.


Collectively, these findings provide evidence that << arsenic >> causes prolonged activation of Nrf2 through autophagy dysfunction, possibly providing a similar scenario to constitutive activation of [[ Nrf2 ]] found in certain human cancers.


Ovarian AR was not influenced by either treatment, and oviduct << AR >> was reduced after [[ ethanol ]]-melatonin combination.


Ovarian AR was not influenced by either treatment, and oviduct << AR >> was reduced after ethanol-[[ melatonin ]] combination.


Oviduct << ER-α >>, ER-β and uterine ER-β were down-regulated by either [[ ethanol ]] or melatonin.


Oviduct ER-α, << ER-β >> and uterine ER-β were down-regulated by either [[ ethanol ]] or melatonin.


Oviduct ER-α, ER-β and uterine << ER-β >> were down-regulated by either [[ ethanol ]] or melatonin.


Oviduct << ER-α >>, ER-β and uterine ER-β were down-regulated by either ethanol or [[ melatonin ]].


Oviduct ER-α, << ER-β >> and uterine ER-β were down-regulated by either ethanol or [[ melatonin ]].


Oviduct ER-α, ER-β and uterine << ER-β >> were down-regulated by either ethanol or [[ melatonin ]].


Conversely, ovarian PRA and PRB were positively regulated by ethanol and ethanol-melatonin combination, whereas << PRA >> was down-regulated in the uterus and oviduct after [[ ethanol ]] consumption.


<< MT1R >> was increased in ovaries and uteri of [[ melatonin ]]-treated rats.


Intraplantar or intrathecal administered Phα1β reduced both nocifensive behavior and mechanical hypersensitivity induced by capsaicin similarly to that observed with << SB366791 >>, a specific [[ TRPV1 ]] antagonist.


Recently, the << c-Abl >> kinase inhibitor [[ imatinib mesylate ]] (imatinib) has become the focus of research as a fertoprotective drug against cisplatin.


Recently, the c-Abl << kinase >> inhibitor [[ imatinib mesylate ]] (imatinib) has become the focus of research as a fertoprotective drug against cisplatin.


Recently, the << c-Abl >> kinase inhibitor imatinib mesylate ([[ imatinib ]]) has become the focus of research as a fertoprotective drug against cisplatin.


Recently, the c-Abl << kinase >> inhibitor imatinib mesylate ([[ imatinib ]]) has become the focus of research as a fertoprotective drug against cisplatin.


We found that, before apoptosis, << cisplatin >> induces [[ c-Abl ]] and TAp73 expression in the oocyte.


We found that, before apoptosis, << cisplatin >> induces c-Abl and [[ TAp73 ]] expression in the oocyte.


While imatinib was unable to block << cisplatin >>-induced DNA damage and damage response, such as the upregulation of [[ p53 ]], imatinib inhibited the cisplatin-induced nuclear accumulation of c-Abl/TAp73 and the subsequent downregulation of TAp63 and upregulation of Bax, thereby abrogating oocyte cell death.


While imatinib was unable to block cisplatin-induced DNA damage and damage response, such as the upregulation of p53, << imatinib >> inhibited the cisplatin-induced nuclear accumulation of c-Abl/TAp73 and the subsequent downregulation of [[ TAp63 ]] and upregulation of Bax, thereby abrogating oocyte cell death.


While imatinib was unable to block cisplatin-induced DNA damage and damage response, such as the upregulation of p53, imatinib inhibited the << cisplatin >>-induced nuclear accumulation of [[ c-Abl ]]/TAp73 and the subsequent downregulation of TAp63 and upregulation of Bax, thereby abrogating oocyte cell death.


While imatinib was unable to block cisplatin-induced DNA damage and damage response, such as the upregulation of p53, imatinib inhibited the << cisplatin >>-induced nuclear accumulation of c-Abl/[[ TAp73 ]] and the subsequent downregulation of TAp63 and upregulation of Bax, thereby abrogating oocyte cell death.


While imatinib was unable to block cisplatin-induced DNA damage and damage response, such as the upregulation of p53, imatinib inhibited the << cisplatin >>-induced nuclear accumulation of c-Abl/TAp73 and the subsequent downregulation of TAp63 and upregulation of [[ Bax ]], thereby abrogating oocyte cell death.


While imatinib was unable to block cisplatin-induced DNA damage and damage response, such as the upregulation of p53, << imatinib >> inhibited the cisplatin-induced nuclear accumulation of [[ c-Abl ]]/TAp73 and the subsequent downregulation of TAp63 and upregulation of Bax, thereby abrogating oocyte cell death.


While imatinib was unable to block cisplatin-induced DNA damage and damage response, such as the upregulation of p53, << imatinib >> inhibited the cisplatin-induced nuclear accumulation of c-Abl/[[ TAp73 ]] and the subsequent downregulation of TAp63 and upregulation of Bax, thereby abrogating oocyte cell death.


While imatinib was unable to block cisplatin-induced DNA damage and damage response, such as the upregulation of p53, << imatinib >> inhibited the cisplatin-induced nuclear accumulation of c-Abl/TAp73 and the subsequent downregulation of TAp63 and upregulation of [[ Bax ]], thereby abrogating oocyte cell death.


While imatinib was unable to block cisplatin-induced DNA damage and damage response, such as the upregulation of p53, imatinib inhibited the << cisplatin >>-induced nuclear accumulation of c-Abl/TAp73 and the subsequent downregulation of [[ TAp63 ]] and upregulation of Bax, thereby abrogating oocyte cell death.


Surprisingly, the conditional deletion of Trp63, but not ΔNp63, in oocytes inhibited apoptosis, as well as the accumulation of << c-Abl >> and TAp73 caused by [[ cisplatin ]].


Surprisingly, the conditional deletion of Trp63, but not ΔNp63, in oocytes inhibited apoptosis, as well as the accumulation of c-Abl and << TAp73 >> caused by [[ cisplatin ]].


The expression kinetics of TAp63, c-Abl and TAp73 suggest that << cisplatin >> activates [[ TAp63 ]]-dependent expression of c-Abl and TAp73 and, in turn, the activation of TAp73 by c-Abl-induced BAX expression.


The expression kinetics of TAp63, c-Abl and TAp73 suggest that << cisplatin >> activates TAp63-dependent expression of c-Abl and TAp73 and, in turn, the activation of [[ TAp73 ]] by c-Abl-induced BAX expression.


The expression kinetics of TAp63, c-Abl and TAp73 suggest that << cisplatin >> activates TAp63-dependent expression of c-Abl and TAp73 and, in turn, the activation of TAp73 by [[ c-Abl ]]-induced BAX expression.


The expression kinetics of TAp63, c-Abl and TAp73 suggest that << cisplatin >> activates TAp63-dependent expression of [[ c-Abl ]] and TAp73 and, in turn, the activation of TAp73 by c-Abl-induced BAX expression.


The expression kinetics of TAp63, c-Abl and TAp73 suggest that << cisplatin >> activates TAp63-dependent expression of c-Abl and [[ TAp73 ]] and, in turn, the activation of TAp73 by c-Abl-induced BAX expression.


The expression kinetics of TAp63, c-Abl and TAp73 suggest that << cisplatin >> activates TAp63-dependent expression of c-Abl and TAp73 and, in turn, the activation of TAp73 by c-Abl-induced [[ BAX ]] expression.


Our findings indicate that << imatinib >> protects oocytes from cisplatin-induced cell death by inhibiting c-Abl [[ kinase ]], which would otherwise activate TAp73-BAX-mediated apoptosis.


Our findings indicate that imatinib protects oocytes from << cisplatin >>-induced cell death by inhibiting [[ c-Abl ]] kinase, which would otherwise activate TAp73-BAX-mediated apoptosis.


Our findings indicate that imatinib protects oocytes from << cisplatin >>-induced cell death by inhibiting c-Abl [[ kinase ]], which would otherwise activate TAp73-BAX-mediated apoptosis.


Our findings indicate that imatinib protects oocytes from << cisplatin >>-induced cell death by inhibiting c-Abl kinase, which would otherwise activate [[ TAp73 ]]-BAX-mediated apoptosis.


Our findings indicate that imatinib protects oocytes from << cisplatin >>-induced cell death by inhibiting c-Abl kinase, which would otherwise activate TAp73-[[ BAX ]]-mediated apoptosis.


Our findings indicate that << imatinib >> protects oocytes from cisplatin-induced cell death by inhibiting [[ c-Abl ]] kinase, which would otherwise activate TAp73-BAX-mediated apoptosis.


Our findings indicate that << imatinib >> protects oocytes from cisplatin-induced cell death by inhibiting c-Abl kinase, which would otherwise activate [[ TAp73 ]]-BAX-mediated apoptosis.


Our findings indicate that << imatinib >> protects oocytes from cisplatin-induced cell death by inhibiting c-Abl kinase, which would otherwise activate TAp73-[[ BAX ]]-mediated apoptosis.


Thus, << imatinib >> and other [[ c-Abl ]] kinase inhibitors provide an intriguing new way to halt cisplatin-induced oocyte death in early follicles and perhaps conserve the endocrine function of the ovary against chemotherapy.Cell Death and Differentiation advance online publication, 19 April 2013; doi:10.1038/cdd.2013.31.


Thus, << imatinib >> and other c-Abl [[ kinase ]] inhibitors provide an intriguing new way to halt cisplatin-induced oocyte death in early follicles and perhaps conserve the endocrine function of the ovary against chemotherapy.Cell Death and Differentiation advance online publication, 19 April 2013; doi:10.1038/cdd.2013.31.


Among the possible transporters involved in the uptake of << Cd(2+) >> and Mn(2+), the expression of ZIP8 (Zrt-, Irt-related protein 8), encoded by [[ Slc39a8 ]], showed a marked suppression in both RBL-Cdr and RBL-Mnr cells.


Among the possible transporters involved in the uptake of << Cd(2+) >> and Mn(2+), the expression of [[ ZIP8 ]] (Zrt-, Irt-related protein 8), encoded by Slc39a8, showed a marked suppression in both RBL-Cdr and RBL-Mnr cells.


Among the possible transporters involved in the uptake of << Cd(2+) >> and Mn(2+), the expression of ZIP8 ([[ Zrt-, Irt-related protein 8 ]]), encoded by Slc39a8, showed a marked suppression in both RBL-Cdr and RBL-Mnr cells.


Among the possible transporters involved in the uptake of Cd(2+) and << Mn(2+) >>, the expression of ZIP8 (Zrt-, Irt-related protein 8), encoded by [[ Slc39a8 ]], showed a marked suppression in both RBL-Cdr and RBL-Mnr cells.


Among the possible transporters involved in the uptake of Cd(2+) and << Mn(2+) >>, the expression of [[ ZIP8 ]] (Zrt-, Irt-related protein 8), encoded by Slc39a8, showed a marked suppression in both RBL-Cdr and RBL-Mnr cells.


Among the possible transporters involved in the uptake of Cd(2+) and << Mn(2+) >>, the expression of ZIP8 ([[ Zrt-, Irt-related protein 8 ]]), encoded by Slc39a8, showed a marked suppression in both RBL-Cdr and RBL-Mnr cells.


These results suggest that << ZIP8 >> plays a pivotal role in the transport and toxicity of [[ Cd(2+) ]] and Mn(2+) in RBL-2H3 cells.


These results suggest that << ZIP8 >> plays a pivotal role in the transport and toxicity of Cd(2+) and [[ Mn(2+) ]] in RBL-2H3 cells.


Optimization of a 1,5-dihydrobenzo[b][1,4]diazepine-2,4-dione series of << HIV capsid >> assembly inhibitors 2: Structure-activity relationships (SAR) of the C3-[[ phenyl ]] moiety.


Optimization of a << 1,5-dihydrobenzo[b][1,4]diazepine-2,4-dione >> series of [[ HIV capsid ]] assembly inhibitors 2: Structure-activity relationships (SAR) of the C3-phenyl moiety.


Detailed structure-activity relationships of the C3-phenyl moiety that allow for the optimization of antiviral potency of a series of << 1,5-dihydrobenzo[b][1,4]diazepine-2,4-dione >> inhibitors of [[ HIV capsid ]] (CA) assembly are described.


Detailed structure-activity relationships of the C3-phenyl moiety that allow for the optimization of antiviral potency of a series of << 1,5-dihydrobenzo[b][1,4]diazepine-2,4-dione >> inhibitors of HIV capsid ([[ CA ]]) assembly are described.


<< Arsenic >> upregulates the expression of [[ angiotensin II Type I receptor ]] in mouse aortic endothelial cells.


Quantitative real-time PCR analysis revealed significant increases in the mRNA levels of 2 << AT1R >> subtypes, AT1AR and AT1BR following [[ sodium arsenite ]] (SA) treatment.


Quantitative real-time PCR analysis revealed significant increases in the mRNA levels of 2 AT1R subtypes, << AT1AR >> and AT1BR following [[ sodium arsenite ]] (SA) treatment.


Quantitative real-time PCR analysis revealed significant increases in the mRNA levels of 2 AT1R subtypes, AT1AR and << AT1BR >> following [[ sodium arsenite ]] (SA) treatment.


Finally, SA-induced << AT1R >> expression was found to be prevented both by NAC and specific JNK inhibitor, [[ SP6001325 ]], strongly indicating that AT1R upregulation is a result of the ROS-mediated activation of the JNK signaling pathway.


Finally, SA-induced AT1R expression was found to be prevented both by NAC and specific << JNK >> inhibitor, [[ SP6001325 ]], strongly indicating that AT1R upregulation is a result of the ROS-mediated activation of the JNK signaling pathway.


Taken together, our results indicate that << arsenic >> indeed upregulates the [[ AT1R ]] expression, thus highlighting a role of arsenic-induced aberrant AT1R signaling in the pathogenesis of hypertension.


Taken together, our results indicate that arsenic indeed upregulates the AT1R expression, thus highlighting a role of << arsenic >>-induced aberrant [[ AT1R ]] signaling in the pathogenesis of hypertension.


The mRNA levels of << SOD1 >>, CAT, GPx and Txnrd1 were increased significantly (P<0.05) in the combined [[ Na2SeO3 ]]+NaAsO2 treatment group.


The mRNA levels of SOD1, << CAT >>, GPx and Txnrd1 were increased significantly (P<0.05) in the combined [[ Na2SeO3 ]]+NaAsO2 treatment group.


The mRNA levels of SOD1, CAT, << GPx >> and Txnrd1 were increased significantly (P<0.05) in the combined [[ Na2SeO3 ]]+NaAsO2 treatment group.


The mRNA levels of << SOD1 >>, CAT, GPx and Txnrd1 were increased significantly (P<0.05) in the combined Na2SeO3+[[ NaAsO2 ]] treatment group.


The mRNA levels of SOD1, << CAT >>, GPx and Txnrd1 were increased significantly (P<0.05) in the combined Na2SeO3+[[ NaAsO2 ]] treatment group.


The mRNA levels of SOD1, CAT, << GPx >> and Txnrd1 were increased significantly (P<0.05) in the combined Na2SeO3+[[ NaAsO2 ]] treatment group.


The mRNA levels of SOD1, CAT, GPx and << Txnrd1 >> were increased significantly (P<0.05) in the combined Na2SeO3+[[ NaAsO2 ]] treatment group.


The mRNA levels of SOD1, CAT, GPx and << Txnrd1 >> were increased significantly (P<0.05) in the combined [[ Na2SeO3 ]]+NaAsO2 treatment group.


The expressions of << HSP70 >> and HO-1 were significantly (P<0.05) increased in the [[ NaAsO2 ]] group and reduced in the combined treatment group.


The expressions of HSP70 and << HO-1 >> were significantly (P<0.05) increased in the [[ NaAsO2 ]] group and reduced in the combined treatment group.


From the 10 isolated compounds, << methyl-3,5-di-O-caffeoylquinate >> showed the most potent inhibition, with IC50 values of 0.30 and 0.67 μM for [[ rAR ]] and rhAR, respectively.


From the 10 isolated compounds, << methyl-3,5-di-O-caffeoylquinate >> showed the most potent inhibition, with IC50 values of 0.30 and 0.67 μM for rAR and [[ rhAR ]], respectively.


In the kinetic analyses using Lineweaver-Burk plots of 1/velocity and 1/substrate, << methyl-3,5-di-O-caffeoylquinate >> showed competitive inhibition of [[ rhAR ]].


Recent observations revealed that << human UDP-glucuronosyltransferase (UGT) 2B10 >> catalyzes N-glucuronidation of [[ amine ]]-containing compounds.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of [[ amitriptyline ]], imipramine, ketotifen, pizotifen, olanzapine, diphenhydramine, tamoxifen, ketoconazole and midazolam.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of amitriptyline, [[ imipramine ]], ketotifen, pizotifen, olanzapine, diphenhydramine, tamoxifen, ketoconazole and midazolam.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of amitriptyline, imipramine, [[ ketotifen ]], pizotifen, olanzapine, diphenhydramine, tamoxifen, ketoconazole and midazolam.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of amitriptyline, imipramine, ketotifen, [[ pizotifen ]], olanzapine, diphenhydramine, tamoxifen, ketoconazole and midazolam.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of amitriptyline, imipramine, ketotifen, pizotifen, [[ olanzapine ]], diphenhydramine, tamoxifen, ketoconazole and midazolam.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of amitriptyline, imipramine, ketotifen, pizotifen, olanzapine, [[ diphenhydramine ]], tamoxifen, ketoconazole and midazolam.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of amitriptyline, imipramine, ketotifen, pizotifen, olanzapine, diphenhydramine, [[ tamoxifen ]], ketoconazole and midazolam.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of amitriptyline, imipramine, ketotifen, pizotifen, olanzapine, diphenhydramine, tamoxifen, [[ ketoconazole ]] and midazolam.


Using recombinant << UGT2B10 >>, we found that it catalyzes the N-glucuronidation of amitriptyline, imipramine, ketotifen, pizotifen, olanzapine, diphenhydramine, tamoxifen, ketoconazole and [[ midazolam ]].


This group of drugs contains secondary or primary amines, and these results suggest that << UGT2B10 >> preferably conjugates [[ tertiary amines ]].


Kinetic analyses revealed that the affinity and clearance of << UGT2B10 >> for [[ amitriptyline ]], imipramine, and diphenhydramine are significantly higher than the corresponding values of UGT1A4 and UGT1A3, although the Vmax values of UGT1A4 toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of UGT2B10 for << amitriptyline >>, imipramine, and diphenhydramine are significantly higher than the corresponding values of [[ UGT1A4 ]] and UGT1A3, although the Vmax values of UGT1A4 toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of UGT2B10 for << amitriptyline >>, imipramine, and diphenhydramine are significantly higher than the corresponding values of UGT1A4 and UGT1A3, although the Vmax values of [[ UGT1A4 ]] toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of << UGT2B10 >> for amitriptyline, [[ imipramine ]], and diphenhydramine are significantly higher than the corresponding values of UGT1A4 and UGT1A3, although the Vmax values of UGT1A4 toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of UGT2B10 for amitriptyline, << imipramine >>, and diphenhydramine are significantly higher than the corresponding values of [[ UGT1A4 ]] and UGT1A3, although the Vmax values of UGT1A4 toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of UGT2B10 for amitriptyline, << imipramine >>, and diphenhydramine are significantly higher than the corresponding values of UGT1A4 and [[ UGT1A3 ]], although the Vmax values of UGT1A4 toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of UGT2B10 for amitriptyline, << imipramine >>, and diphenhydramine are significantly higher than the corresponding values of UGT1A4 and UGT1A3, although the Vmax values of [[ UGT1A4 ]] toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of << UGT2B10 >> for amitriptyline, imipramine, and [[ diphenhydramine ]] are significantly higher than the corresponding values of UGT1A4 and UGT1A3, although the Vmax values of UGT1A4 toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of UGT2B10 for amitriptyline, imipramine, and << diphenhydramine >> are significantly higher than the corresponding values of [[ UGT1A4 ]] and UGT1A3, although the Vmax values of UGT1A4 toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of UGT2B10 for amitriptyline, imipramine, and << diphenhydramine >> are significantly higher than the corresponding values of UGT1A4 and [[ UGT1A3 ]], although the Vmax values of UGT1A4 toward these drugs are considerably higher.


Kinetic analyses revealed that the affinity and clearance of UGT2B10 for amitriptyline, imipramine, and << diphenhydramine >> are significantly higher than the corresponding values of UGT1A4 and UGT1A3, although the Vmax values of [[ UGT1A4 ]] toward these drugs are considerably higher.


In conclusion, this study expands the understanding of the substrate specificity of << UGT2B10 >>, highlighting its preference for [[ tertiary amines ]] with higher affinities and clearance values than those of UGT1A4 and UGT1A3.


In conclusion, this study expands the understanding of the substrate specificity of UGT2B10, highlighting its preference for << tertiary amines >> with higher affinities and clearance values than those of [[ UGT1A4 ]] and UGT1A3.


In conclusion, this study expands the understanding of the substrate specificity of UGT2B10, highlighting its preference for << tertiary amines >> with higher affinities and clearance values than those of UGT1A4 and [[ UGT1A3 ]].


<< SB225002 >> (SB) is an IL-8 receptor B (IL-8RB) antagonist that has previously been shown to inhibit [[ IL-8 ]]-based cancer cell invasion, and to possess in vivo anti-inflammatory and anti-nociceptive effects.


<< SB225002 >> (SB) is an [[ IL-8 receptor B ]] (IL-8RB) antagonist that has previously been shown to inhibit IL-8-based cancer cell invasion, and to possess in vivo anti-inflammatory and anti-nociceptive effects.


<< SB225002 >> (SB) is an IL-8 receptor B ([[ IL-8RB ]]) antagonist that has previously been shown to inhibit IL-8-based cancer cell invasion, and to possess in vivo anti-inflammatory and anti-nociceptive effects.


Of note, << SB265610 >> which is a close structural analogue of SB225002 with a potent [[ IL-8RB ]] antagonistic activity did not exhibit a similar antimitotic activity.


Of note, SB265610 which is a close structural analogue of << SB225002 >> with a potent [[ IL-8RB ]] antagonistic activity did not exhibit a similar antimitotic activity.


In support of this observation, elongation can be reversed by the << tyrosine kinase >> inhibitor [[ SU5402 ]], mRNA for the FGFR antagonist sprouty4, or FGF8 morpholino.


<< Caffeic Acid Phenethyl Ester >> Suppresses Proliferation and Survival of TW2.6 Human Oral Cancer Cells via Inhibition of [[ Akt ]] Signaling.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor [[ p27Kip ]].


Treatment with << CAPE >> decreased protein abundance of [[ Akt ]], Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, [[ Akt1 ]], Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, [[ Akt2 ]], Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, [[ Akt3 ]], phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, [[ phospho-Akt ]] Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, [[ phospho-Akt ]] Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, [[ GSK3β ]], FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, [[ FOXO1 ]], FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, [[ FOXO3a ]], phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, [[ phospho-FOXO1 ]] Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, [[ phospho-FoxO3a ]] Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, [[ NF-κB ]], phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, [[ phospho-NF-κB ]] Ser536, Rb, phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, [[ Rb ]], phospho-Rb Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, [[ phospho-Rb ]] Ser807/811, Skp2, and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, [[ Skp2 ]], and cyclin D1, but increased cell cycle inhibitor p27Kip.


Treatment with << CAPE >> decreased protein abundance of Akt, Akt1, Akt2, Akt3, phospho-Akt Ser473, phospho-Akt Thr 308, GSK3β, FOXO1, FOXO3a, phospho-FOXO1 Thr24, phospho-FoxO3a Thr32, NF-κB, phospho-NF-κB Ser536, Rb, phospho-Rb Ser807/811, Skp2, and [[ cyclin D1 ]], but increased cell cycle inhibitor p27Kip.


Here we show that << fisetin >> rapidly increases the levels of both [[ Nrf2 ]] and ATF4 as well as Nrf2- and ATF4-dependent gene transcription via distinct mechanisms.


Here we show that << fisetin >> rapidly increases the levels of both Nrf2 and [[ ATF4 ]] as well as Nrf2- and ATF4-dependent gene transcription via distinct mechanisms.


Here we show that << fisetin >> rapidly increases the levels of both Nrf2 and ATF4 as well as [[ Nrf2 ]]- and ATF4-dependent gene transcription via distinct mechanisms.


Here we show that << fisetin >> rapidly increases the levels of both Nrf2 and ATF4 as well as Nrf2- and [[ ATF4 ]]-dependent gene transcription via distinct mechanisms.


Although << fisetin >> greatly increases the stability of both [[ Nrf2 ]] and ATF4, only the effect on ATF4 is dependent on protein kinase activity.


Although << fisetin >> greatly increases the stability of both Nrf2 and [[ ATF4 ]], only the effect on ATF4 is dependent on protein kinase activity.


<< Cynomolgus FMO1 >>, FMO2, FMO3, and FMO5 metabolized [[ benzydamine ]], and FMO1/FMO3 and FMO3 also metabolized methimazole and trimethylamine, respectively.


Cynomolgus FMO1, << FMO2 >>, FMO3, and FMO5 metabolized [[ benzydamine ]], and FMO1/FMO3 and FMO3 also metabolized methimazole and trimethylamine, respectively.


Cynomolgus FMO1, FMO2, << FMO3 >>, and FMO5 metabolized [[ benzydamine ]], and FMO1/FMO3 and FMO3 also metabolized methimazole and trimethylamine, respectively.


Cynomolgus FMO1, FMO2, FMO3, and << FMO5 >> metabolized [[ benzydamine ]], and FMO1/FMO3 and FMO3 also metabolized methimazole and trimethylamine, respectively.


Cynomolgus FMO1, FMO2, FMO3, and FMO5 metabolized benzydamine, and << FMO1 >>/FMO3 and FMO3 also metabolized [[ methimazole ]] and trimethylamine, respectively.


Cynomolgus FMO1, FMO2, FMO3, and FMO5 metabolized benzydamine, and FMO1/<< FMO3 >> and FMO3 also metabolized [[ methimazole ]] and trimethylamine, respectively.


Cynomolgus FMO1, FMO2, FMO3, and FMO5 metabolized benzydamine, and FMO1/FMO3 and << FMO3 >> also metabolized [[ methimazole ]] and trimethylamine, respectively.


Cynomolgus FMO1, FMO2, FMO3, and FMO5 metabolized benzydamine, and << FMO1 >>/FMO3 and FMO3 also metabolized methimazole and [[ trimethylamine ]], respectively.


Cynomolgus FMO1, FMO2, FMO3, and FMO5 metabolized benzydamine, and FMO1/<< FMO3 >> and FMO3 also metabolized methimazole and [[ trimethylamine ]], respectively.


Cynomolgus FMO1, FMO2, FMO3, and FMO5 metabolized benzydamine, and FMO1/FMO3 and << FMO3 >> also metabolized methimazole and [[ trimethylamine ]], respectively.


Rates of << benzydamine >> N-oxygenation (catalyzed by [[ FMO3 ]]) varied (approximately 20-fold) among the 28 cynomolgus livers and were significantly correlated with FMO3 protein expression, indicating that the inter-animal variations in benzydamine N-oxygenation might be partly accounted for by the variable FMO3 expression.


Rates of benzydamine << N >>-oxygenation (catalyzed by [[ FMO3 ]]) varied (approximately 20-fold) among the 28 cynomolgus livers and were significantly correlated with FMO3 protein expression, indicating that the inter-animal variations in benzydamine N-oxygenation might be partly accounted for by the variable FMO3 expression.


Rates of benzydamine N-oxygenation (catalyzed by FMO3) varied (approximately 20-fold) among the 28 cynomolgus livers and were significantly correlated with FMO3 protein expression, indicating that the inter-animal variations in << benzydamine >> N-oxygenation might be partly accounted for by the variable [[ FMO3 ]] expression.


Rates of benzydamine N-oxygenation (catalyzed by FMO3) varied (approximately 20-fold) among the 28 cynomolgus livers and were significantly correlated with FMO3 protein expression, indicating that the inter-animal variations in benzydamine << N >>-oxygenation might be partly accounted for by the variable [[ FMO3 ]] expression.


<< Cynomolgus FMO6 >> metabolized [[ benzydamine ]] only slightly, but minimal expression of FMO6 in all tissue precludes the importance of FMO6 in drug metabolism, unlike cynomolgus FMO1, FMO2, FMO3, and FMO5 which were all functional.


Cynomolgus FMO6 metabolized << benzydamine >> only slightly, but minimal expression of FMO6 in all tissue precludes the importance of FMO6 in drug metabolism, unlike cynomolgus [[ FMO1 ]], FMO2, FMO3, and FMO5 which were all functional.


Cynomolgus FMO6 metabolized << benzydamine >> only slightly, but minimal expression of FMO6 in all tissue precludes the importance of FMO6 in drug metabolism, unlike cynomolgus FMO1, [[ FMO2 ]], FMO3, and FMO5 which were all functional.


Cynomolgus FMO6 metabolized << benzydamine >> only slightly, but minimal expression of FMO6 in all tissue precludes the importance of FMO6 in drug metabolism, unlike cynomolgus FMO1, FMO2, [[ FMO3 ]], and FMO5 which were all functional.


Cynomolgus FMO6 metabolized << benzydamine >> only slightly, but minimal expression of FMO6 in all tissue precludes the importance of FMO6 in drug metabolism, unlike cynomolgus FMO1, FMO2, FMO3, and [[ FMO5 ]] which were all functional.


Activation of << AMPK >> using [[ AICAR ]] resulted in STIM1 phosphorylation on serine residues and prevented PAR-1-induced Ca2+ entry.


Activation of AMPK using << AICAR >> resulted in [[ STIM1 ]] phosphorylation on serine residues and prevented PAR-1-induced Ca2+ entry.


Activation of AMPK using << AICAR >> resulted in STIM1 phosphorylation on serine residues and prevented [[ PAR-1 ]]-induced Ca2+ entry.


Further, << AICAR >> pretreatment blocked [[ PAR-1 ]]-induced increase in permeability of mouse-lung microvessels.


Interestingly, << SB203580 >>, a selective inhibitor of [[ p38 ]] MAPK, blocked STIM1 phosphorylation and led to sustained STIM1-puncta formation and Ca2+ entry.


Interestingly, << SB203580 >>, a selective inhibitor of p38 [[ MAPK ]], blocked STIM1 phosphorylation and led to sustained STIM1-puncta formation and Ca2+ entry.


Interestingly, << SB203580 >>, a selective inhibitor of p38 MAPK, blocked [[ STIM1 ]] phosphorylation and led to sustained STIM1-puncta formation and Ca2+ entry.


Mitochondria in the steroidogenic cells of the adrenal, gonad, placenta and brain contain the << cholesterol >> side-chain cleavage enzyme, [[ P450scc ]], and its two electron-transfer partners, ferredoxin reductase and ferredoxin.


The precise fashion in which these proteins interact and move << cholesterol >> from the OMM to [[ P450scc ]], and the means by which cholesterol is loaded into the OMM, remain unclear.


<< Matrix Metalloproteinase >> Inhibitors Based on the [[ 3-Mercaptopyrrolidine ]] Core.


New series of << pyrrolidine mercaptosulfide >>, 2-mercaptocyclopentane arylsulfonamide, and 3-mercapto-4-arylsulfonamido pyrrolidine [[ matrix metalloproteinase ]] inhibitors (MMPIs) were designed, synthesized, and evaluated.


New series of pyrrolidine mercaptosulfide, << 2-mercaptocyclopentane arylsulfonamide >>, and 3-mercapto-4-arylsulfonamido pyrrolidine [[ matrix metalloproteinase ]] inhibitors (MMPIs) were designed, synthesized, and evaluated.


New series of pyrrolidine mercaptosulfide, 2-mercaptocyclopentane arylsulfonamide, and << 3-mercapto-4-arylsulfonamido pyrrolidine >> [[ matrix metalloproteinase ]] inhibitors (MMPIs) were designed, synthesized, and evaluated.


Exhibiting unique properties over other MMPIs (e.g., << hydroxamates >>), these newly reported compounds are capable of modulating activities of several [[ MMPs ]] in the low nanomolar range, including MMP-2 (~2 to 50 nM), MMP-13 (~2 to 50 nM), and MMP-14 (~4 to 60 nM).


Exhibiting unique properties over other MMPIs (e.g., << hydroxamates >>), these newly reported compounds are capable of modulating activities of several MMPs in the low nanomolar range, including [[ MMP-2 ]] (~2 to 50 nM), MMP-13 (~2 to 50 nM), and MMP-14 (~4 to 60 nM).


Exhibiting unique properties over other MMPIs (e.g., << hydroxamates >>), these newly reported compounds are capable of modulating activities of several MMPs in the low nanomolar range, including MMP-2 (~2 to 50 nM), [[ MMP-13 ]] (~2 to 50 nM), and MMP-14 (~4 to 60 nM).


Exhibiting unique properties over other MMPIs (e.g., << hydroxamates >>), these newly reported compounds are capable of modulating activities of several MMPs in the low nanomolar range, including MMP-2 (~2 to 50 nM), MMP-13 (~2 to 50 nM), and [[ MMP-14 ]] (~4 to 60 nM).


Recent literature shows that Brassica vegetables (Cruciferae) possess therapeutic effects particularly ascribed due to their content in glucosinolates, which upon << myrosinase >> hydrolysis release the corresponding [[ isothiocyanates ]].


Recent literature shows that Brassica vegetables (Cruciferae) possess therapeutic effects particularly ascribed due to their content in << glucosinolates >>, which upon [[ myrosinase ]] hydrolysis release the corresponding isothiocyanates.


RESULTS: By Western blot analysis of spinal cord tissues, we have demonstrated that treatment with bioactive << RS -GRA >> significantly decreased nuclear factor (NF)-kB translocation, pro-inflammatory cytokine production such as [[ interleukin-1β ]] (IL-1β), and apoptosis (Bax and caspase 3 expression).


RESULTS: By Western blot analysis of spinal cord tissues, we have demonstrated that treatment with bioactive << RS -GRA >> significantly decreased nuclear factor (NF)-kB translocation, pro-inflammatory cytokine production such as interleukin-1β ([[ IL-1β ]]), and apoptosis (Bax and caspase 3 expression).


RESULTS: By Western blot analysis of spinal cord tissues, we have demonstrated that treatment with bioactive << RS -GRA >> significantly decreased nuclear factor (NF)-kB translocation, pro-inflammatory cytokine production such as interleukin-1β (IL-1β), and apoptosis ([[ Bax ]] and caspase 3 expression).


RESULTS: By Western blot analysis of spinal cord tissues, we have demonstrated that treatment with bioactive << RS -GRA >> significantly decreased nuclear factor (NF)-kB translocation, pro-inflammatory cytokine production such as interleukin-1β (IL-1β), and apoptosis (Bax and [[ caspase 3 ]] expression).


RESULTS: By Western blot analysis of spinal cord tissues, we have demonstrated that treatment with bioactive << RS -GRA >> significantly decreased [[ nuclear factor (NF)-kB ]] translocation, pro-inflammatory cytokine production such as interleukin-1β (IL-1β), and apoptosis (Bax and caspase 3 expression).


RESULTS: By Western blot analysis of spinal cord tissues, we have demonstrated that treatment with bioactive << RS -GRA >> significantly decreased nuclear factor (NF)-kB translocation, pro-inflammatory [[ cytokine ]] production such as interleukin-1β (IL-1β), and apoptosis (Bax and caspase 3 expression).


Herein, we investigated the effect of a natural neuroprotective flavonoid, calycopterin, on << H2O2 >>-induced disruption of [[ phase II detoxifying enzyme ]] system and cAMP response element binding protein (CREB) phosphorylation.


Herein, we investigated the effect of a natural neuroprotective flavonoid, calycopterin, on << H2O2 >>-induced disruption of phase II detoxifying enzyme system and [[ cAMP response element binding protein ]] (CREB) phosphorylation.


Herein, we investigated the effect of a natural neuroprotective flavonoid, calycopterin, on << H2O2 >>-induced disruption of phase II detoxifying enzyme system and cAMP response element binding protein ([[ CREB ]]) phosphorylation.


In H2O2-treated cells, << calycopterin >> also suppressed [[ cytochrome C ]] release to cytosol that is necessary for maintaining mitochondrial homeostasis in survived cells.


Moreover, << calycopterin >>, in presence of H2O2 inhibited the decrease caused by oxidative stress in stress-sensing transcription factors, [[ CREB ]] and Nrf2, which play an important role in antioxidant capacity of the cell.


Moreover, << calycopterin >>, in presence of H2O2 inhibited the decrease caused by oxidative stress in stress-sensing transcription factors, CREB and [[ Nrf2 ]], which play an important role in antioxidant capacity of the cell.


There was also an increase in << γ-GCS >> and HO-1 levels in [[ calycopterin ]] pretreated cells.


There was also an increase in γ-GCS and << HO-1 >> levels in [[ calycopterin ]] pretreated cells.


In the presence of H2O2, << calycopterin >> inhibited decrease in GSH level and [[ SOD ]] activity.


<< Indoxyl 3-sulfate >> stimulates Th17 differentiation enhancing phosphorylation of [[ c-Src ]] and STAT3 to worsen experimental autoimmune encephalomyelitis.


<< Indoxyl 3-sulfate >> stimulates Th17 differentiation enhancing phosphorylation of c-Src and [[ STAT3 ]] to worsen experimental autoimmune encephalomyelitis.


In the present study, using in vitro Th17 differentiation model, we examined effects of << AhR >> activation by [[ indoxyl 3-sulfate ]] (I3S), a uremic toxin, on Th17 differentiation and investigated underlying mechanisms.


In the present study, using in vitro Th17 differentiation model, we examined effects of << AhR >> activation by indoxyl 3-sulfate ([[ I3S ]]), a uremic toxin, on Th17 differentiation and investigated underlying mechanisms.


<< I3S >> increased expression of [[ RORγt ]], the master transcription factor for Th17 differentiation, and stimulated Th17 differentiation, in a comparative manner as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), a prototypical AhR ligand.


Activation of << STAT3 >>, which is phosphorylated by the IL-6 signaling pathways and thus is necessary for Th17 differentiation, was strongly stimulated by I3S and [[ TCDD ]].


Activation of STAT3, which is phosphorylated by the << IL-6 >> signaling pathways and thus is necessary for Th17 differentiation, was strongly stimulated by I3S and [[ TCDD ]].


Activation of << STAT3 >>, which is phosphorylated by the IL-6 signaling pathways and thus is necessary for Th17 differentiation, was strongly stimulated by [[ I3S ]] and TCDD.


Activation of STAT3, which is phosphorylated by the << IL-6 >> signaling pathways and thus is necessary for Th17 differentiation, was strongly stimulated by [[ I3S ]] and TCDD.


Phosphorylation of << c-Src >>, which was shown to be activated by AhR ligands, was also increased by [[ I3S ]] and TCDD, and blocking of c-Src activity by 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine (PP2) inhibited phosphorylation of both c-Src and STAT3, raising a possibility that stimulatory activities of I3S and TCDD on Th17 differentiation could be exerted via increased phosphorylation of c-Src, which in turn stimulates STAT3 activation.


Phosphorylation of << c-Src >>, which was shown to be activated by AhR ligands, was also increased by I3S and [[ TCDD ]], and blocking of c-Src activity by 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine (PP2) inhibited phosphorylation of both c-Src and STAT3, raising a possibility that stimulatory activities of I3S and TCDD on Th17 differentiation could be exerted via increased phosphorylation of c-Src, which in turn stimulates STAT3 activation.


Phosphorylation of c-Src, which was shown to be activated by AhR ligands, was also increased by I3S and TCDD, and blocking of c-Src activity by 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine (PP2) inhibited phosphorylation of both c-Src and STAT3, raising a possibility that stimulatory activities of << I3S >> and TCDD on Th17 differentiation could be exerted via increased phosphorylation of [[ c-Src ]], which in turn stimulates STAT3 activation.


Phosphorylation of c-Src, which was shown to be activated by AhR ligands, was also increased by I3S and TCDD, and blocking of c-Src activity by 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine (PP2) inhibited phosphorylation of both c-Src and STAT3, raising a possibility that stimulatory activities of << I3S >> and TCDD on Th17 differentiation could be exerted via increased phosphorylation of c-Src, which in turn stimulates [[ STAT3 ]] activation.


Phosphorylation of c-Src, which was shown to be activated by AhR ligands, was also increased by I3S and TCDD, and blocking of c-Src activity by 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine (PP2) inhibited phosphorylation of both c-Src and STAT3, raising a possibility that stimulatory activities of I3S and << TCDD >> on Th17 differentiation could be exerted via increased phosphorylation of [[ c-Src ]], which in turn stimulates STAT3 activation.


Phosphorylation of c-Src, which was shown to be activated by AhR ligands, was also increased by I3S and TCDD, and blocking of c-Src activity by 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine (PP2) inhibited phosphorylation of both c-Src and STAT3, raising a possibility that stimulatory activities of I3S and << TCDD >> on Th17 differentiation could be exerted via increased phosphorylation of c-Src, which in turn stimulates [[ STAT3 ]] activation.


Phosphorylation of c-Src, which was shown to be activated by AhR ligands, was also increased by I3S and TCDD, and blocking of << c-Src >> activity by [[ 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine ]] (PP2) inhibited phosphorylation of both c-Src and STAT3, raising a possibility that stimulatory activities of I3S and TCDD on Th17 differentiation could be exerted via increased phosphorylation of c-Src, which in turn stimulates STAT3 activation.


Phosphorylation of c-Src, which was shown to be activated by AhR ligands, was also increased by I3S and TCDD, and blocking of c-Src activity by << 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine >> (PP2) inhibited phosphorylation of both [[ c-Src ]] and STAT3, raising a possibility that stimulatory activities of I3S and TCDD on Th17 differentiation could be exerted via increased phosphorylation of c-Src, which in turn stimulates STAT3 activation.


Phosphorylation of c-Src, which was shown to be activated by AhR ligands, was also increased by I3S and TCDD, and blocking of c-Src activity by << 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo[3,4-d]pyrimidine >> (PP2) inhibited phosphorylation of both c-Src and [[ STAT3 ]], raising a possibility that stimulatory activities of I3S and TCDD on Th17 differentiation could be exerted via increased phosphorylation of c-Src, which in turn stimulates STAT3 activation.


Finally, we found that << I3S >> worsened experimental autoimmune encephalomyelitis (EAE), which is primarily mediated by Th17 cells, enhancing the frequency of [[ IL-17 ]]-producing cells in draining lymph nodes.


<< TCDD >> induces the expression of [[ insulin-like growth factor binding protein 4 ]] in 5L rat hepatoma cells: a cautionary tale of the use of this cell line in studies on dioxin toxicity.


By "working upwards" from mTOR, we observed that << TCDD >> inhibited endogenous and IGF-I-induced [[ AKT ]] and ERK activation by interfering with tyrosine phosphorylation of insulin receptor substrate 1.


By "working upwards" from mTOR, we observed that << TCDD >> inhibited endogenous and IGF-I-induced AKT and [[ ERK ]] activation by interfering with tyrosine phosphorylation of insulin receptor substrate 1.


By "working upwards" from mTOR, we observed that << TCDD >> inhibited endogenous and [[ IGF-I ]]-induced AKT and ERK activation by interfering with tyrosine phosphorylation of insulin receptor substrate 1.


This inhibition was mediated by a << TCDD >>-induced secreted factor which was identified as [[ insulin-like growth factor binding protein 4 ]] (IGFBP-4).


This inhibition was mediated by a << TCDD >>-induced secreted factor which was identified as insulin-like growth factor binding protein 4 ([[ IGFBP-4 ]]).


The induction of IGFBP-4 protein was dependent on a functional aryl hydrocarbon receptor and was preceded by a rapid increase in the level of << IGFBP-4 >> mRNA indicating that IGFBP-4 is a previously unknown transcriptional target of [[ TCDD ]] in 5L cells.


The observations suggest that in 5L cells the Igfbp-4 gene may have got under the control of a promoter containing dioxin responsive element(s) leading to the induction of << IGFBP-4 >> by [[ TCDD ]].


Although numerous mechanisms of action of << pimozide >> and thioridazine have been identified, both drugs are [[ calmodulin ]] antagonists at drug concentrations that inhibit breast cancer cell growth in vitro.


Although numerous mechanisms of action of pimozide and << thioridazine >> have been identified, both drugs are [[ calmodulin ]] antagonists at drug concentrations that inhibit breast cancer cell growth in vitro.


Inhibition of MCF-7 cell growth by the selective calmodulin antagonists W-13 and W-12 is consistent with a role for << calmodulin >> antagonism in the broad growth-inhibitory properties of [[ pimozide ]].


Inhibition of MCF-7 cell growth by the selective << calmodulin >> antagonists [[ W-13 ]] and W-12 is consistent with a role for calmodulin antagonism in the broad growth-inhibitory properties of pimozide.


Inhibition of MCF-7 cell growth by the selective << calmodulin >> antagonists W-13 and [[ W-12 ]] is consistent with a role for calmodulin antagonism in the broad growth-inhibitory properties of pimozide.


Levels of homovanillic acid (HVA), dihydroxyphenylacetic acid (DOPAC) and dihydroxyphenylglycol (DHPG) in plasma and the striatium were measured after inhibition of monoamine oxidase type A (MAO-A) by clorgyline (4 mg/kg i.p.), << MAO-B >> by [[ (-)deprenyl ]] (1 mg/kg i.p.), both MAO-A and MAO-B by nialamide (75 mg/kg i.p.) or peripheral neuronal MAO by debrisoquin (40 mg/kg i.p.).


Levels of homovanillic acid (HVA), dihydroxyphenylacetic acid (DOPAC) and dihydroxyphenylglycol (DHPG) in plasma and the striatium were measured after inhibition of monoamine oxidase type A (MAO-A) by clorgyline (4 mg/kg i.p.), MAO-B by (-)deprenyl (1 mg/kg i.p.), both << MAO-A >> and MAO-B by [[ nialamide ]] (75 mg/kg i.p.) or peripheral neuronal MAO by debrisoquin (40 mg/kg i.p.).


Levels of homovanillic acid (HVA), dihydroxyphenylacetic acid (DOPAC) and dihydroxyphenylglycol (DHPG) in plasma and the striatium were measured after inhibition of monoamine oxidase type A (MAO-A) by clorgyline (4 mg/kg i.p.), MAO-B by (-)deprenyl (1 mg/kg i.p.), both MAO-A and << MAO-B >> by [[ nialamide ]] (75 mg/kg i.p.) or peripheral neuronal MAO by debrisoquin (40 mg/kg i.p.).