The extent and rate of inhibition are similar to that seen with the known << K(ATP) >> blocker [[ PNU 37883A ]].


Additionally, << phenformin >> inhibited the current elicited through the [[ Kir6.2DeltaC26 ]] (functional without SUR) channel with an IC50 of 1.78 mM.


<< Phenformin >> reduced the open probability of [[ Kir6.1 ]]/SUR2B channels by approximately 90% in inside-out patches.


<< Phenformin >> reduced the open probability of Kir6.1/[[ SUR2B ]] channels by approximately 90% in inside-out patches.


Different VDRAs are known to have differential effects on serum calcium (Ca), which may also affect serum PTH levels since serum << Ca >> regulates [[ PTH ]] secretion mediated by the Ca-sensing receptor (CaSR).


Both drugs at the tested doses (0.042-0.33 mug/kg) suppressed PTH mRNA expression and serum << PTH >> effectively in the 5/6 NX rats, but [[ paricalcitol ]] was less potent in raising serum Ca than doxercalciferol.


Both drugs at the tested doses (0.042-0.33 mug/kg) suppressed PTH mRNA expression and serum << PTH >> effectively in the 5/6 NX rats, but paricalcitol was less potent in raising serum Ca than [[ doxercalciferol ]].


Both drugs at the tested doses (0.042-0.33 mug/kg) suppressed << PTH >> mRNA expression and serum PTH effectively in the 5/6 NX rats, but [[ paricalcitol ]] was less potent in raising serum Ca than doxercalciferol.


Both drugs at the tested doses (0.042-0.33 mug/kg) suppressed << PTH >> mRNA expression and serum PTH effectively in the 5/6 NX rats, but paricalcitol was less potent in raising serum Ca than [[ doxercalciferol ]].


In pig parathyroid cells, paricalcitol and the active form of doxercalciferol induced VDR translocation from the cytoplasm into the nucleus, suppressed PTH mRNA expression and inhibited cell proliferation in a similar manner, although << paricalcitol >> induced the expression of [[ CaSR ]] mRNA more effectively.


In pig parathyroid cells, << paricalcitol >> and the active form of doxercalciferol induced VDR translocation from the cytoplasm into the nucleus, suppressed [[ PTH ]] mRNA expression and inhibited cell proliferation in a similar manner, although paricalcitol induced the expression of CaSR mRNA more effectively.


In pig parathyroid cells, paricalcitol and the active form of << doxercalciferol >> induced VDR translocation from the cytoplasm into the nucleus, suppressed [[ PTH ]] mRNA expression and inhibited cell proliferation in a similar manner, although paricalcitol induced the expression of CaSR mRNA more effectively.


<< Thalidomide >> initiates its teratogenic effects by binding to CRBN and inhibiting the associated [[ ubiquitin ligase ]] activity.


<< Telmisartan >> is an [[ angiotensin II receptor ]] blocker (ARB) displaying unique pharmacologic properties, including a longer half life than any other ARB, that result in large and sustained reductions of blood pressure.


Recent studies indicate that << tamoxifen >> initially acts as an antagonist, but later functions as an [[ ER ]] agonist, promoting tumor growth.


With the pentapeptide linked through the C7alpha position of << estradiol >>, the resulting PROTAC shows the most effective [[ ER ]] degradation and highest affinity for the estrogen receptor.


KEY RESULTS: Several agonists were found to be highly subtype selective because of selective affinity (e.g. << salmeterol >> and formoterol, for the [[ beta(2)-adrenoceptor ]] over the beta(1) or beta(3)), while others (e.g. isoprenaline) had little affinity-selectivity.


KEY RESULTS: Several agonists were found to be highly subtype selective because of selective affinity (e.g. << salmeterol >> and formoterol, for the beta(2)-adrenoceptor over the [[ beta(1) ]] or beta(3)), while others (e.g. isoprenaline) had little affinity-selectivity.


KEY RESULTS: Several agonists were found to be highly subtype selective because of selective affinity (e.g. salmeterol and << formoterol >>, for the [[ beta(2)-adrenoceptor ]] over the beta(1) or beta(3)), while others (e.g. isoprenaline) had little affinity-selectivity.


KEY RESULTS: Several agonists were found to be highly subtype selective because of selective affinity (e.g. salmeterol and << formoterol >>, for the beta(2)-adrenoceptor over the beta(1) or [[ beta(3) ]]), while others (e.g. isoprenaline) had little affinity-selectivity.


KEY RESULTS: Several agonists were found to be highly subtype selective because of selective affinity (e.g. salmeterol and formoterol, for the << beta(2)-adrenoceptor >> over the beta(1) or beta(3)), while others (e.g. [[ isoprenaline ]]) had little affinity-selectivity.


KEY RESULTS: Several agonists were found to be highly subtype selective because of selective affinity (e.g. salmeterol and formoterol, for the beta(2)-adrenoceptor over the << beta(1) >> or beta(3)), while others (e.g. [[ isoprenaline ]]) had little affinity-selectivity.


KEY RESULTS: Several agonists were found to be highly subtype selective because of selective affinity (e.g. salmeterol and formoterol, for the beta(2)-adrenoceptor over the beta(1) or << beta(3) >>), while others (e.g. [[ isoprenaline ]]) had little affinity-selectivity.


<< Rasagiline >>: a novel anti-Parkinsonian [[ monoamine oxidase-B ]] inhibitor with neuroprotective activity.


<< Rasagiline >> (N-propargyl-1-(R)-aminoindan) is a novel, highly potent irreversible [[ monoamine oxidase (MAO)-B ]] inhibitor, anti-Parkinsonian drug.


Rasagiline (<< N-propargyl-1-(R)-aminoindan >>) is a novel, highly potent irreversible [[ monoamine oxidase (MAO)-B ]] inhibitor, anti-Parkinsonian drug.


Its S-isomer, << TVP1022 >> is thousand times less potent as an [[ MAO-B ]] inhibitor.


However, both compounds have similar molecular mechanisms of neuroprotection in neuronal cell cultures and animal neurodegenerative models, indicating that the neuroprotective effect of rasagiline does not depend on inhibition of MAO-B, but rather is associated with the << N-propargyl >> moiety, which promotes mitochondrial viability and stabilizes permeability transition by regulating [[ Bcl-2 ]] family proteins.


However, both compounds have similar molecular mechanisms of neuroprotection in neuronal cell cultures and animal neurodegenerative models, indicating that the neuroprotective effect of << rasagiline >> does not depend on inhibition of [[ MAO-B ]], but rather is associated with the N-propargyl moiety, which promotes mitochondrial viability and stabilizes permeability transition by regulating Bcl-2 family proteins.


Our findings suggest that R316C causes reduced association with and impaired release of NCoR, resulting in RTH predominantly at the pituitary level, and that slightly elevated serum << TSH >> level with high dose of [[ levothyroxine ]] might be optimum for normal growth.


BACKGROUND: Recent epidemiologic and laboratory studies have suggested that non-<< steroidal >> anti-inflammatory drugs (NSAIDs) may reduce the risk of breast cancer through inhibition of [[ cyclooxygenase-2 ]] (COX-2).


BACKGROUND: Recent epidemiologic and laboratory studies have suggested that non-<< steroidal >> anti-inflammatory drugs (NSAIDs) may reduce the risk of breast cancer through inhibition of cyclooxygenase-2 ([[ COX-2 ]]).


METHODS: We conducted a case-control study to measure the association between selective << cox-2 >> inhibitors, particularly [[ celecoxib ]], rofecoxib, valdecoxib and non-specific NSAID subgroups, and breast cancer risk.


METHODS: We conducted a case-control study to measure the association between selective << cox-2 >> inhibitors, particularly celecoxib, [[ rofecoxib ]], valdecoxib and non-specific NSAID subgroups, and breast cancer risk.


METHODS: We conducted a case-control study to measure the association between selective << cox-2 >> inhibitors, particularly celecoxib, rofecoxib, [[ valdecoxib ]] and non-specific NSAID subgroups, and breast cancer risk.


With exposure to << rofecoxib >>, a selective [[ COX-2 ]] inhibitor, breast cancer risk reduction was appreciable (46%), suggesting a possible role for selective COX-2 inhibitors in breast cancer prophylaxis.


With exposure to << rofecoxib >>, a selective COX-2 inhibitor, breast cancer risk reduction was appreciable (46%), suggesting a possible role for selective [[ COX-2 ]] inhibitors in breast cancer prophylaxis.


The suppressive effect of << ceruletide >> on barrel rotation could be partially countered by MK-329, a selective peripheral [[ CCK ]] (CCK-A) receptor antagonist.


The suppressive effect of << ceruletide >> on barrel rotation could be partially countered by MK-329, a selective peripheral CCK [[ (CCK-A) receptor ]] antagonist.


The suppressive effect of ceruletide on barrel rotation could be partially countered by << MK-329 >>, a selective peripheral [[ CCK ]] (CCK-A) receptor antagonist.


The suppressive effect of ceruletide on barrel rotation could be partially countered by << MK-329 >>, a selective peripheral CCK [[ (CCK-A) receptor ]] antagonist.


These findings suggest that << ceruletide >> specifically suppresses the barrel rotation evoked by SMS 201-995 in a long-lasting manner possibly acting through [[ CCK-A receptor ]].


Effects of the << histamine H1 >> antagonist [[ chlorcyclizine ]] on rat fetal palate development.


BACKGROUND: The effects of << histamine H1 >> antagonist [[ chlorcyclizine ]] on rat palate development were characterized following in utero exposure.


Removing medium Ca2+, blocking << Ca2+ channels >> with 50 mumol/l [[ verapamil ]], or inhibiting calmodulin activation with 20 mumol/l trifluoperazine, 10 mumol/l chlorpromazine or 10 mumol/l pimozide almost completely blocked hyposmolarity-induced secretion.


Removing medium Ca2+, blocking Ca2+ channels with 50 mumol/l verapamil, or inhibiting << calmodulin >> activation with 20 mumol/l [[ trifluoperazine ]], 10 mumol/l chlorpromazine or 10 mumol/l pimozide almost completely blocked hyposmolarity-induced secretion.


Removing medium Ca2+, blocking Ca2+ channels with 50 mumol/l verapamil, or inhibiting << calmodulin >> activation with 20 mumol/l trifluoperazine, 10 mumol/l [[ chlorpromazine ]] or 10 mumol/l pimozide almost completely blocked hyposmolarity-induced secretion.


Removing medium Ca2+, blocking Ca2+ channels with 50 mumol/l verapamil, or inhibiting << calmodulin >> activation with 20 mumol/l trifluoperazine, 10 mumol/l chlorpromazine or 10 mumol/l [[ pimozide ]] almost completely blocked hyposmolarity-induced secretion.


The smooth muscle relaxant, << W-7 >>, which is believed relatively specific in inhibiting the Ca2(+)-calmodulin interaction, depressed hyposmolarity-induced [[ PRL ]] secretion in a dose-dependent manner (r = -0.991, p less than 0.01).


An essential control in experiments using Gy mice is to demonstrate that the abnormal phenotypes exhibited by these mice are abolished by providing replacement << spermine >> and this can be accomplished by breeding with CAG-[[ SMS ]] mice that express SpmS from a ubiquitous promoter.


An essential control in experiments using Gy mice is to demonstrate that the abnormal phenotypes exhibited by these mice are abolished by providing replacement << spermine >> and this can be accomplished by breeding with CAG-SMS mice that express [[ SpmS ]] from a ubiquitous promoter.


<< Cabozantinib >> (XL184), a novel [[ MET ]] and VEGFR2 inhibitor, simultaneously suppresses metastasis, angiogenesis, and tumor growth.


<< Cabozantinib >> (XL184), a novel MET and [[ VEGFR2 ]] inhibitor, simultaneously suppresses metastasis, angiogenesis, and tumor growth.


Cabozantinib (<< XL184 >>), a novel [[ MET ]] and VEGFR2 inhibitor, simultaneously suppresses metastasis, angiogenesis, and tumor growth.


Cabozantinib (<< XL184 >>), a novel MET and [[ VEGFR2 ]] inhibitor, simultaneously suppresses metastasis, angiogenesis, and tumor growth.


<< Cabozantinib >> (XL184) is a small-molecule [[ kinase ]] inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


<< Cabozantinib >> (XL184) is a small-molecule kinase inhibitor with potent activity toward [[ MET ]] and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


<< Cabozantinib >> (XL184) is a small-molecule kinase inhibitor with potent activity toward MET and [[ VEGF receptor 2 ]] (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


<< Cabozantinib >> (XL184) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 ([[ VEGFR2 ]]), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


<< Cabozantinib >> (XL184) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other [[ receptor tyrosine kinases ]] that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


<< Cabozantinib >> (XL184) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including [[ RET ]], KIT, AXL, and FLT3.


<< Cabozantinib >> (XL184) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, [[ KIT ]], AXL, and FLT3.


<< Cabozantinib >> (XL184) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, [[ AXL ]], and FLT3.


<< Cabozantinib >> (XL184) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and [[ FLT3 ]].


Cabozantinib (<< XL184 >>) is a small-molecule [[ kinase ]] inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


Cabozantinib (<< XL184 >>) is a small-molecule kinase inhibitor with potent activity toward [[ MET ]] and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


Cabozantinib (<< XL184 >>) is a small-molecule kinase inhibitor with potent activity toward MET and [[ VEGF receptor 2 ]] (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


Cabozantinib (<< XL184 >>) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 ([[ VEGFR2 ]]), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


Cabozantinib (<< XL184 >>) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other [[ receptor tyrosine kinases ]] that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and FLT3.


Cabozantinib (<< XL184 >>) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including [[ RET ]], KIT, AXL, and FLT3.


Cabozantinib (<< XL184 >>) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, [[ KIT ]], AXL, and FLT3.


Cabozantinib (<< XL184 >>) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, [[ AXL ]], and FLT3.


Cabozantinib (<< XL184 >>) is a small-molecule kinase inhibitor with potent activity toward MET and VEGF receptor 2 (VEGFR2), as well as a number of other receptor tyrosine kinases that have also been implicated in tumor pathobiology, including RET, KIT, AXL, and [[ FLT3 ]].


Treatment with << cabozantinib >> inhibited [[ MET ]] and VEGFR2 phosphorylation in vitro and in tumor models in vivo and led to significant reductions in cell invasion in vitro.


Treatment with << cabozantinib >> inhibited MET and [[ VEGFR2 ]] phosphorylation in vitro and in tumor models in vivo and led to significant reductions in cell invasion in vitro.


Importantly, treatment with << cabozantinib >> did not increase lung tumor burden in an experimental model of metastasis, which has been observed with inhibitors of [[ VEGF ]] signaling that do not target MET.


Collectively, these data suggest that << cabozantinib >> is a promising agent for inhibiting tumor angiogenesis and metastasis in cancers with dysregulated [[ MET ]] and VEGFR signaling.


Collectively, these data suggest that << cabozantinib >> is a promising agent for inhibiting tumor angiogenesis and metastasis in cancers with dysregulated MET and [[ VEGFR ]] signaling.


Inhibition of the NF-kappaB pathway was responsible for this effect since the << colchicoside >> inhibited RANKL-induced [[ NF-kappaB ]] activation, activation of IkappaB kinase (IKK) and suppressed inhibitor of NF-kappaBalpha (IkappaBalpha) phosphorylation and degradation, an inhibitor of NF-kappaB.


Inhibition of the NF-kappaB pathway was responsible for this effect since the << colchicoside >> inhibited RANKL-induced NF-kappaB activation, activation of [[ IkappaB kinase ]] (IKK) and suppressed inhibitor of NF-kappaBalpha (IkappaBalpha) phosphorylation and degradation, an inhibitor of NF-kappaB.


Inhibition of the NF-kappaB pathway was responsible for this effect since the << colchicoside >> inhibited RANKL-induced NF-kappaB activation, activation of IkappaB kinase ([[ IKK ]]) and suppressed inhibitor of NF-kappaBalpha (IkappaBalpha) phosphorylation and degradation, an inhibitor of NF-kappaB.


Inhibition of the NF-kappaB pathway was responsible for this effect since the << colchicoside >> inhibited RANKL-induced NF-kappaB activation, activation of IkappaB kinase (IKK) and suppressed inhibitor of [[ NF-kappaBalpha ]] (IkappaBalpha) phosphorylation and degradation, an inhibitor of NF-kappaB.


Inhibition of the NF-kappaB pathway was responsible for this effect since the << colchicoside >> inhibited RANKL-induced NF-kappaB activation, activation of IkappaB kinase (IKK) and suppressed inhibitor of NF-kappaBalpha ([[ IkappaBalpha ]]) phosphorylation and degradation, an inhibitor of NF-kappaB.


Inhibition of the NF-kappaB pathway was responsible for this effect since the << colchicoside >> inhibited RANKL-induced NF-kappaB activation, activation of IkappaB kinase (IKK) and suppressed inhibitor of NF-kappaBalpha (IkappaBalpha) phosphorylation and degradation, an inhibitor of [[ NF-kappaB ]].


Inhibition of the NF-kappaB pathway was responsible for this effect since the << colchicoside >> inhibited [[ RANKL ]]-induced NF-kappaB activation, activation of IkappaB kinase (IKK) and suppressed inhibitor of NF-kappaBalpha (IkappaBalpha) phosphorylation and degradation, an inhibitor of NF-kappaB.


CONCLUSIONS AND IMPLICATIONS: Together, these data suggest that << thiocolchicoside >> significantly suppressed osteoclastogenesis induced by [[ RANKL ]] and tumour cells via the NF-kappaB signalling pathway.


CONCLUSIONS AND IMPLICATIONS: Together, these data suggest that << thiocolchicoside >> significantly suppressed osteoclastogenesis induced by RANKL and tumour cells via the [[ NF-kappaB ]] signalling pathway.


Although genetic polymorphisms in the endothelial nitric oxide synthase (<< eNOS >>) gene may impair endogenous [[ NO ]] formation, there is little information about how eNOS polymorphisms and haplotypes affect the responses to sildenafil.


Although genetic polymorphisms in the << endothelial nitric oxide synthase >> (eNOS) gene may impair endogenous [[ NO ]] formation, there is little information about how eNOS polymorphisms and haplotypes affect the responses to sildenafil.


<< Mercury >> induces the expression of [[ cyclooxygenase-2 ]] and inducible nitric oxide synthase.


<< Mercury >> induces the expression of cyclooxygenase-2 and [[ inducible nitric oxide synthase ]].


Here, we report biochemical evidence that << mercury >> alone induces [[ NF-κB ]] activation, resulting in the induced expression of COX-2 and iNOS.


Here, we report biochemical evidence that << mercury >> alone induces NF-κB activation, resulting in the induced expression of [[ COX-2 ]] and iNOS.


Here, we report biochemical evidence that << mercury >> alone induces NF-κB activation, resulting in the induced expression of COX-2 and [[ iNOS ]].


Unexpectedly, both the << mGluR(5) >>specific agonist, [[ CHPG ]], and the group II mGluR (mGlu(2/3)) agonist, LY379268 (LY), induced a TTX-insensitive outward current/hyperpolarization.


Unexpectedly, both the mGluR(5)specific agonist, CHPG, and the << group II mGluR >> (mGlu(2/3)) agonist, [[ LY379268 ]] (LY), induced a TTX-insensitive outward current/hyperpolarization.


Both outward currents were significantly reduced by the << mGluR >> antagonist [[ MCPG ]] and the CHPG-induced current was blocked by the specific mGluR(5) antagonist MTEP.


Both outward currents were significantly reduced by the mGluR antagonist MCPG and the CHPG-induced current was blocked by the specific << mGluR(5) >> antagonist [[ MTEP ]].


We have examined the effectiveness of two novel << Chk1 >> selective inhibitors, [[ AR323 ]] and AR678, in a panel of melanoma cell lines and normal cell types.


We have examined the effectiveness of two novel << Chk1 >> selective inhibitors, AR323 and [[ AR678 ]], in a panel of melanoma cell lines and normal cell types.


<< Aspirin >> inhibits mTOR signaling, activates [[ AMP-activated protein kinase ]], and induces autophagy in colorectal cancer cells.


<< Aspirin >> inhibits [[ mTOR ]] signaling, activates AMP-activated protein kinase, and induces autophagy in colorectal cancer cells.


RESULTS: << Aspirin >> reduced [[ mTOR ]] signaling in CRC cells by inhibiting the mTOR effectors S6K1 and 4E-BP1.


RESULTS: << Aspirin >> reduced mTOR signaling in CRC cells by inhibiting the [[ mTOR ]] effectors S6K1 and 4E-BP1.


RESULTS: << Aspirin >> reduced mTOR signaling in CRC cells by inhibiting the mTOR effectors [[ S6K1 ]] and 4E-BP1.


RESULTS: << Aspirin >> reduced mTOR signaling in CRC cells by inhibiting the mTOR effectors S6K1 and [[ 4E-BP1 ]].


<< Aspirin >> changed nucleotide ratios and activated [[ AMPK ]] in CRC cells.


<< mTOR >> was still inhibited by [[ aspirin ]] in CRC cells after siRNA knockdown of AMPKalpha, indicating AMPK-dependent and AMPK-independent mechanisms of aspirin-induced inhibition of mTOR.


mTOR was still inhibited by aspirin in CRC cells after siRNA knockdown of AMPKalpha, indicating AMPK-dependent and AMPK-independent mechanisms of << aspirin >>-induced inhibition of [[ mTOR ]].


<< Aspirin >> induced autophagy, a feature of [[ mTOR ]] inhibition.


Aspirin and << metformin >> (an activator of [[ AMPK ]]) increased inhibition of mTOR and Akt, as well as autophagy in CRC cells.


<< Aspirin >> and metformin (an activator of [[ AMPK ]]) increased inhibition of mTOR and Akt, as well as autophagy in CRC cells.


Aspirin and << metformin >> (an activator of AMPK) increased inhibition of [[ mTOR ]] and Akt, as well as autophagy in CRC cells.


Aspirin and << metformin >> (an activator of AMPK) increased inhibition of mTOR and [[ Akt ]], as well as autophagy in CRC cells.


<< Aspirin >> and metformin (an activator of AMPK) increased inhibition of [[ mTOR ]] and Akt, as well as autophagy in CRC cells.


<< Aspirin >> and metformin (an activator of AMPK) increased inhibition of mTOR and [[ Akt ]], as well as autophagy in CRC cells.


Rectal mucosal samples from patients given << aspirin >> had reduced phosphorylation of [[ S6K1 ]] and S6.


Rectal mucosal samples from patients given << aspirin >> had reduced phosphorylation of S6K1 and [[ S6 ]].


CONCLUSIONS: << Aspirin >> is an inhibitor of mTOR and an activator of [[ AMPK ]], targeting regulators of intracellular energy homeostasis and metabolism.


CONCLUSIONS: << Aspirin >> is an inhibitor of [[ mTOR ]] and an activator of AMPK, targeting regulators of intracellular energy homeostasis and metabolism.


Exogenous stimulation of << PKA >> activity, achieved by [[ forskolin ]] treatment, protected K-ras-transformed cells from apoptosis induced by glucose deprivation, enhanced complex I activity, intracellular adenosine triphosphate (ATP) levels, mitochondrial fusion and decreased intracellular reactive oxygen species (ROS) levels.


Exogenous stimulation of PKA activity, achieved by << forskolin >> treatment, protected K-ras-transformed cells from apoptosis induced by glucose deprivation, enhanced [[ complex I ]] activity, intracellular adenosine triphosphate (ATP) levels, mitochondrial fusion and decreased intracellular reactive oxygen species (ROS) levels.


Exogenous stimulation of PKA activity, achieved by forskolin treatment, protected << K-ras >>-transformed cells from apoptosis induced by [[ glucose ]] deprivation, enhanced complex I activity, intracellular adenosine triphosphate (ATP) levels, mitochondrial fusion and decreased intracellular reactive oxygen species (ROS) levels.


In << TGF-β1 >>-induced NPDFs, [[ berberine ]] significantly inhibited the expression of α-SMA and collagen type I mRNA and reduced α-SMA and collagen protein levels.


In TGF-β1-induced NPDFs, << berberine >> significantly inhibited the expression of [[ α-SMA ]] and collagen type I mRNA and reduced α-SMA and collagen protein levels.


In TGF-β1-induced NPDFs, << berberine >> significantly inhibited the expression of α-SMA and [[ collagen type I ]] mRNA and reduced α-SMA and collagen protein levels.


In TGF-β1-induced NPDFs, << berberine >> significantly inhibited the expression of α-SMA and collagen type I mRNA and reduced [[ α-SMA ]] and collagen protein levels.


In TGF-β1-induced NPDFs, << berberine >> significantly inhibited the expression of α-SMA and collagen type I mRNA and reduced α-SMA and [[ collagen ]] protein levels.


<< Berberine >> only suppressed the expression of [[ pp38 ]] among the evaluated signaling molecules.


<< SB203580 >> (a specific inhibitor of p38 kinase) markedly suppressed the increased expression of [[ collagen type I ]] and α-SMA in TGF-β1-induced NPDFs.


<< SB203580 >> (a specific inhibitor of p38 kinase) markedly suppressed the increased expression of collagen type I and [[ α-SMA ]] in TGF-β1-induced NPDFs.


<< SB203580 >> (a specific inhibitor of p38 kinase) markedly suppressed the increased expression of collagen type I and α-SMA in [[ TGF-β1 ]]-induced NPDFs.


<< SB203580 >> (a specific inhibitor of [[ p38 ]] kinase) markedly suppressed the increased expression of collagen type I and α-SMA in TGF-β1-induced NPDFs.


<< SB203580 >> (a specific inhibitor of p38 [[ kinase ]]) markedly suppressed the increased expression of collagen type I and α-SMA in TGF-β1-induced NPDFs.


CRBN mediated antiproliferative activities of lenalidomide and pomalidomide in myeloma cells, as well as << lenalidomide >>- and pomalidomide-induced [[ cytokine ]] production in T cells.


CRBN mediated antiproliferative activities of lenalidomide and pomalidomide in myeloma cells, as well as lenalidomide- and << pomalidomide >>-induced [[ cytokine ]] production in T cells.


<< Lenalidomide >> and pomalidomide inhibited autoubiquitination of [[ CRBN ]] in HEK293T cells expressing thalidomide-binding competent wild-type CRBN, but not thalidomide-binding defective CRBN(YW/AA).


<< Lenalidomide >> and pomalidomide inhibited autoubiquitination of CRBN in HEK293T cells expressing thalidomide-binding competent wild-type [[ CRBN ]], but not thalidomide-binding defective CRBN(YW/AA).


Lenalidomide and << pomalidomide >> inhibited autoubiquitination of [[ CRBN ]] in HEK293T cells expressing thalidomide-binding competent wild-type CRBN, but not thalidomide-binding defective CRBN(YW/AA).


Lenalidomide and << pomalidomide >> inhibited autoubiquitination of CRBN in HEK293T cells expressing thalidomide-binding competent wild-type [[ CRBN ]], but not thalidomide-binding defective CRBN(YW/AA).


Overexpression of CRBN wild-type protein, but not CRBN(YW/AA) mutant protein, in KMS12 myeloma cells, amplified << pomalidomide >>-mediated reductions in c-myc and IRF4 expression and increases in p21([[ WAF-1 ]]) expression.


Overexpression of CRBN wild-type protein, but not CRBN(YW/AA) mutant protein, in KMS12 myeloma cells, amplified << pomalidomide >>-mediated reductions in c-myc and IRF4 expression and increases in [[ p21 ]](WAF-1) expression.


Overexpression of CRBN wild-type protein, but not CRBN(YW/AA) mutant protein, in KMS12 myeloma cells, amplified << pomalidomide >>-mediated reductions in [[ c-myc ]] and IRF4 expression and increases in p21(WAF-1) expression.


Overexpression of CRBN wild-type protein, but not CRBN(YW/AA) mutant protein, in KMS12 myeloma cells, amplified << pomalidomide >>-mediated reductions in c-myc and [[ IRF4 ]] expression and increases in p21(WAF-1) expression.


Long-term selection for << lenalidomide >> resistance in H929 myeloma cell lines was accompanied by a reduction in [[ CRBN ]], while in DF15R myeloma cells resistant to both pomalidomide and lenalidomide, CRBN protein was undetectable.


These << polyphenols >>, but not GvEx, showed a certain level of inhibition of human-cDNA-expressed [[ CYPs ]].


<< Crizotinib >> is an oral tyrosine kinase inhibitor (TKI), which silences the protein product of the [[ ALK ]] fusion gene and has recently been approved for the treatment of NSCLC aberrantly expressing ALK.


<< Crizotinib >> is an oral [[ tyrosine kinase ]] inhibitor (TKI), which silences the protein product of the ALK fusion gene and has recently been approved for the treatment of NSCLC aberrantly expressing ALK.


To clarify if the behavioral interaction between ethanol and adenosine reported previously occur centrally or due to a peripheral hemodynamic change, the effect of i.c.v. << adenosine >> agonists, [[ N6-(R-phenylisopropyl)adenosine ]] (R-PIA), N6-(S-phenylisopropyl)adenosine, 5'-(N-cyclopropyl)-carboxamidoadenosine, antagonists, theophylline and 8-p-(sulfophenyl)theophylline as well as enprofylline on ethanol-(i.p.)-induced motor incoordination was evaluated by rotorod.


To clarify if the behavioral interaction between ethanol and adenosine reported previously occur centrally or due to a peripheral hemodynamic change, the effect of i.c.v. << adenosine >> agonists, N6-(R-phenylisopropyl)adenosine ([[ R-PIA ]]), N6-(S-phenylisopropyl)adenosine, 5'-(N-cyclopropyl)-carboxamidoadenosine, antagonists, theophylline and 8-p-(sulfophenyl)theophylline as well as enprofylline on ethanol-(i.p.)-induced motor incoordination was evaluated by rotorod.


To clarify if the behavioral interaction between ethanol and adenosine reported previously occur centrally or due to a peripheral hemodynamic change, the effect of i.c.v. << adenosine >> agonists, N6-(R-phenylisopropyl)adenosine (R-PIA), [[ N6-(S-phenylisopropyl)adenosine ]], 5'-(N-cyclopropyl)-carboxamidoadenosine, antagonists, theophylline and 8-p-(sulfophenyl)theophylline as well as enprofylline on ethanol-(i.p.)-induced motor incoordination was evaluated by rotorod.


To clarify if the behavioral interaction between ethanol and adenosine reported previously occur centrally or due to a peripheral hemodynamic change, the effect of i.c.v. << adenosine >> agonists, N6-(R-phenylisopropyl)adenosine (R-PIA), N6-(S-phenylisopropyl)adenosine, [[ 5'-(N-cyclopropyl)-carboxamidoadenosine ]], antagonists, theophylline and 8-p-(sulfophenyl)theophylline as well as enprofylline on ethanol-(i.p.)-induced motor incoordination was evaluated by rotorod.


To clarify if the behavioral interaction between ethanol and adenosine reported previously occur centrally or due to a peripheral hemodynamic change, the effect of i.c.v. << adenosine >> agonists, N6-(R-phenylisopropyl)adenosine (R-PIA), N6-(S-phenylisopropyl)adenosine, 5'-(N-cyclopropyl)-carboxamidoadenosine, antagonists, [[ theophylline ]] and 8-p-(sulfophenyl)theophylline as well as enprofylline on ethanol-(i.p.)-induced motor incoordination was evaluated by rotorod.


To clarify if the behavioral interaction between ethanol and adenosine reported previously occur centrally or due to a peripheral hemodynamic change, the effect of i.c.v. << adenosine >> agonists, N6-(R-phenylisopropyl)adenosine (R-PIA), N6-(S-phenylisopropyl)adenosine, 5'-(N-cyclopropyl)-carboxamidoadenosine, antagonists, theophylline and [[ 8-p-(sulfophenyl)theophylline ]] as well as enprofylline on ethanol-(i.p.)-induced motor incoordination was evaluated by rotorod.


To clarify if the behavioral interaction between ethanol and adenosine reported previously occur centrally or due to a peripheral hemodynamic change, the effect of i.c.v. << adenosine >> agonists, N6-(R-phenylisopropyl)adenosine (R-PIA), N6-(S-phenylisopropyl)adenosine, 5'-(N-cyclopropyl)-carboxamidoadenosine, antagonists, theophylline and 8-p-(sulfophenyl)theophylline as well as [[ enprofylline ]] on ethanol-(i.p.)-induced motor incoordination was evaluated by rotorod.


<< Enprofylline >>, a weak adenosine antagonist but potent inhibitor of [[ cyclic AMP phosphodiesterase ]], did not alter ethanol's motor incoordination, further supporting involvement of brain adenosine receptor mechanism(s) in ethanol-adenosine interactions.


<< Enprofylline >>, a weak [[ adenosine ]] antagonist but potent inhibitor of cyclic AMP phosphodiesterase, did not alter ethanol's motor incoordination, further supporting involvement of brain adenosine receptor mechanism(s) in ethanol-adenosine interactions.


<< Celastrol >>, a TAK1 inhibitor and anti-inflammatory compound used in traditional Chinese medicine, also decreased [[ TGF-β1 ]]-induced phosphorylation of TAK1 and RELA, and suppressed basal, TGF-β1- and tumor necrosis factor-alpha (TNF-α)-induced NF-κB reporter gene activity.


<< Celastrol >>, a TAK1 inhibitor and anti-inflammatory compound used in traditional Chinese medicine, also decreased TGF-β1-induced phosphorylation of TAK1 and RELA, and suppressed basal, [[ TGF-β1 ]]- and tumor necrosis factor-alpha (TNF-α)-induced NF-κB reporter gene activity.


<< Celastrol >>, a TAK1 inhibitor and anti-inflammatory compound used in traditional Chinese medicine, also decreased TGF-β1-induced phosphorylation of TAK1 and RELA, and suppressed basal, TGF-β1- and [[ tumor necrosis factor-alpha ]] (TNF-α)-induced NF-κB reporter gene activity.


<< Celastrol >>, a [[ TAK1 ]] inhibitor and anti-inflammatory compound used in traditional Chinese medicine, also decreased TGF-β1-induced phosphorylation of TAK1 and RELA, and suppressed basal, TGF-β1- and tumor necrosis factor-alpha (TNF-α)-induced NF-κB reporter gene activity.


<< Celastrol >>, a TAK1 inhibitor and anti-inflammatory compound used in traditional Chinese medicine, also decreased TGF-β1-induced phosphorylation of [[ TAK1 ]] and RELA, and suppressed basal, TGF-β1- and tumor necrosis factor-alpha (TNF-α)-induced NF-κB reporter gene activity.


<< Celastrol >>, a TAK1 inhibitor and anti-inflammatory compound used in traditional Chinese medicine, also decreased TGF-β1-induced phosphorylation of TAK1 and [[ RELA ]], and suppressed basal, TGF-β1- and tumor necrosis factor-alpha (TNF-α)-induced NF-κB reporter gene activity.


<< Celastrol >>, a TAK1 inhibitor and anti-inflammatory compound used in traditional Chinese medicine, also decreased TGF-β1-induced phosphorylation of TAK1 and RELA, and suppressed basal, TGF-β1- and tumor necrosis factor-alpha (TNF-α)-induced [[ NF-κB ]] reporter gene activity.


<< Celastrol >> also inhibited cell proliferation, while increasing sub-G0 DNA fragmentation and [[ Annexin V ]] markers of apoptosis.


<< Celastrol >> highlights the therapeutic potential of agents targeting [[ TAK1 ]] as a key node in this pro-oncogenic TGF-β-NF-κB signal pathway.


The atypical antidepressant << mianserin >> exhibits agonist activity at [[ kappa-opioid receptors ]].


We previously reported that << tricyclic >> antidepressants act as agonists at distinct [[ opioid receptors ]].


In [(35)S]GTPgammaS assays, << mianserin >> selectively activated [[ kappa-opioid receptors ]].


The agonist activity was antagonized by the selective << kappa-opioid >> blocker [[ nor-binaltorphimine ]] (nor-BNI).


The agonist activity was antagonized by the selective << kappa-opioid >> blocker nor-binaltorphimine ([[ nor-BNI ]]).


The << mianserin >> analogue mirtazapine also displayed [[ kappa-opioid ]] agonist activity.


The mianserin analogue << mirtazapine >> also displayed [[ kappa-opioid ]] agonist activity.


In rat striatum and nucleus accumbens, mianserin stimulated [35S]GTPgammaS binding in a nor-BNI-sensitive manner with maximal effects lower than those of the full << kappa-opioid >> agonists [[ (-)-U50,488 ]] and dynorphin A.


In rat striatum and nucleus accumbens, mianserin stimulated [35S]GTPgammaS binding in a nor-BNI-sensitive manner with maximal effects lower than those of the full << kappa-opioid >> agonists (-)-U50,488 and [[ dynorphin A ]].


When combined, mianserin antagonized the effects of the full kappa-opioid receptor agonists in [(35)S]GTPgammaS assays and reduced the stimulation of << p38 >> MAPK and ERK1/2 phosphorylation by [[ dynorphin A ]].


When combined, mianserin antagonized the effects of the full kappa-opioid receptor agonists in [(35)S]GTPgammaS assays and reduced the stimulation of p38 << MAPK >> and ERK1/2 phosphorylation by [[ dynorphin A ]].


When combined, << mianserin >> antagonized the effects of the full kappa-opioid receptor agonists in [(35)S]GTPgammaS assays and reduced the stimulation of [[ p38 ]] MAPK and ERK1/2 phosphorylation by dynorphin A.


When combined, << mianserin >> antagonized the effects of the full kappa-opioid receptor agonists in [(35)S]GTPgammaS assays and reduced the stimulation of p38 [[ MAPK ]] and ERK1/2 phosphorylation by dynorphin A.


When combined, << mianserin >> antagonized the effects of the full [[ kappa-opioid receptor ]] agonists in [(35)S]GTPgammaS assays and reduced the stimulation of p38 MAPK and ERK1/2 phosphorylation by dynorphin A.


CONCLUSIONS AND IMPLICATIONS: In different cell systems, << mianserin >> directly activates [[ kappa-opioid receptors ]], displaying partial agonist activity at brain receptors.


In the present study we tested whether << propranolol >>, a [[ β-receptor ]] antagonist commonly used as antihypertensive drug, could ameliorate the cognitive impairments and increases in AD-related markers shown by the senescence-accelerated mouse prone-8 (SAMP8).


<< LXRs >> are thought to be activated predominantly by [[ oxysterols ]] generated enzymatically from cholesterol in different cell organelles.


Defects resulting in slowed release of cholesterol from late endosomes and lysosomes or reduction in << sterol-27-hydroxylase >> activity lead to specific blocks in [[ oxysterol ]] production and impaired LXR-dependent gene activation.


The purpose of this review is to summarize current knowledge about << oxysterol >>-dependent activation by [[ LXR ]] of genes involved in reverse cholesterol transport, and what these defects of cell cholesterol homeostasis can teach us about the critical pathways of oxysterol generation for expression of LXR-dependent genes.


<< CBDP >> irreversibly inhibits [[ butyrylcholinesterase ]] (BChE) in human plasma by forming adducts on the active site serine (Ser-198).


<< CBDP >> irreversibly inhibits butyrylcholinesterase ([[ BChE ]]) in human plasma by forming adducts on the active site serine (Ser-198).


Mass spectral analysis of << CBDP >>-inhibited [[ BChE ]] digested with Glu-C showed an o-hydroxybenzyl adduct (+106amu) on lysine 499, a residue far from the active site, but not on His-438.


We previously demonstrated that the somatostatinergic system, implicated in neuronal survival control, can be modulated by << α-tocopherol >> in the rat dentate gyrus, increasing [[ cyclic adenosine monophosphate response element binding protein ]] phosphorylation.


<< Galantamine >> is a reversible, competitive [[ acetylcholinesterase ]] (AChE) inhibitor and allosteric potentiating ligand of nicotinic acetylcholine receptors (nAChR-APL) that shares many common structural elements with morphinan-based opioids.


<< Galantamine >> is a reversible, competitive acetylcholinesterase ([[ AChE ]]) inhibitor and allosteric potentiating ligand of nicotinic acetylcholine receptors (nAChR-APL) that shares many common structural elements with morphinan-based opioids.


Modulation of the << nitric oxide >> producing system (demonstrated via the [[ NADPH-diaphorase ]] histochemical reaction) by oestradiol has been established in several structures of the rat brain.


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective ERα agonist-PPT [4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol], a selective << ERβ >> agonist-[[ DPN ]] [2,3-bis(4-hydroxyphenyl)-propionitrile], a selective ERα antagonist-MPP [1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol]-1H-pyrazole dihydrochloride] or a selective ERβ antagonist-PHTPP (4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol).


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective ERα agonist-PPT [4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol], a selective << ERβ >> agonist-DPN [[[ 2,3-bis(4-hydroxyphenyl)-propionitrile ]]], a selective ERα antagonist-MPP [1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol]-1H-pyrazole dihydrochloride] or a selective ERβ antagonist-PHTPP (4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol).


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective << ERα >> agonist-[[ PPT ]] [4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol], a selective ERβ agonist-DPN [2,3-bis(4-hydroxyphenyl)-propionitrile], a selective ERα antagonist-MPP [1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol]-1H-pyrazole dihydrochloride] or a selective ERβ antagonist-PHTPP (4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol).


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective << ERα >> agonist-PPT [[[ 4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol ]]], a selective ERβ agonist-DPN [2,3-bis(4-hydroxyphenyl)-propionitrile], a selective ERα antagonist-MPP [1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol]-1H-pyrazole dihydrochloride] or a selective ERβ antagonist-PHTPP (4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol).


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective ERα agonist-PPT [4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol], a selective ERβ agonist-DPN [2,3-bis(4-hydroxyphenyl)-propionitrile], a selective << ERα >> antagonist-[[ MPP ]] [1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol]-1H-pyrazole dihydrochloride] or a selective ERβ antagonist-PHTPP (4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol).


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective ERα agonist-PPT [4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol], a selective ERβ agonist-DPN [2,3-bis(4-hydroxyphenyl)-propionitrile], a selective << ERα >> antagonist-MPP [[[ 1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol ]]]-1H-pyrazole dihydrochloride] or a selective ERβ antagonist-PHTPP (4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol).


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective ERα agonist-PPT [4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol], a selective ERβ agonist-DPN [2,3-bis(4-hydroxyphenyl)-propionitrile], a selective << ERα >> antagonist-MPP [1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol]-[[ 1H-pyrazole dihydrochloride ]]] or a selective ERβ antagonist-PHTPP (4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol).


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective ERα agonist-PPT [4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol], a selective ERβ agonist-DPN [2,3-bis(4-hydroxyphenyl)-propionitrile], a selective ERα antagonist-MPP [1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol]-1H-pyrazole dihydrochloride] or a selective << ERβ >> antagonist-[[ PHTPP ]] (4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol).


Adult ovariectomised rats were divided into six groups and injected either with vehicle or a single dose of oestradiol, a selective ERα agonist-PPT [4,4',4″-(4-propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol], a selective ERβ agonist-DPN [2,3-bis(4-hydroxyphenyl)-propionitrile], a selective ERα antagonist-MPP [1,3-bis(4-hydroxyphenyl)-4-methyl-5-[4-(2-piperidinylethoxy)phenol]-1H-pyrazole dihydrochloride] or a selective << ERβ >> antagonist-PHTPP ([[ 4-[2-phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol ]]).


<< Verrucarin A >> sensitizes TRAIL-induced apoptosis via the upregulation of [[ DR5 ]] in an eIF2α/CHOP-dependent manner.


<< Verrucarin A >> sensitizes TRAIL-induced apoptosis via the upregulation of DR5 in an [[ eIF2α ]]/CHOP-dependent manner.


<< Verrucarin A >> sensitizes TRAIL-induced apoptosis via the upregulation of DR5 in an eIF2α/[[ CHOP ]]-dependent manner.


Furthermore, << salubrinal >>, a specific [[ eIF2α ]] phosphorylation-inducing agent, increased CHOP and DR5 expression in the presence of VA.


Furthermore, << salubrinal >>, a specific eIF2α phosphorylation-inducing agent, increased [[ CHOP ]] and DR5 expression in the presence of VA.


Furthermore, << salubrinal >>, a specific eIF2α phosphorylation-inducing agent, increased CHOP and [[ DR5 ]] expression in the presence of VA.


Disruption of microtubule prevented insulin-induced actin remodeling and distal insulin signal transduction, with reduction in surface << glucose transporter isoform 4 >> (GLUT4) and [[ glucose ]] uptake.


Disruption of microtubule prevented insulin-induced actin remodeling and distal insulin signal transduction, with reduction in surface glucose transporter isoform 4 (<< GLUT4 >>) and [[ glucose ]] uptake.


Other groups received either an infusion of the selective << NMDA receptor >> antagonist ([[ AP7 ]]; 10 nmol; intra-mPFC) or vehicle, 10 min prior to PILO preceding LFS600, or prior to a supra-threshold LTD protocol (900 pulses, 1 Hz; LFS900).


Our data also indicate that << NMDA receptor >> pre-activation is essential to the muscarinic enhancement of mPFC synaptic depression, since [[ AP7 ]] microinjection into the mPFC blocked the conversion of transient depression into long-lasting LTD produced by PILO.


Metabolism of << triethylenetetramine >> and 1,12-diamino-3,6,9-triazadodecane by the spermidine/spermine-N(1)-acetyltransferase and [[ thialysine acetyltransferase ]].


Metabolism of << triethylenetetramine >> and 1,12-diamino-3,6,9-triazadodecane by the [[ spermidine/spermine-N(1)-acetyltransferase ]] and thialysine acetyltransferase.


Metabolism of triethylenetetramine and << 1,12-diamino-3,6,9-triazadodecane >> by the spermidine/spermine-N(1)-acetyltransferase and [[ thialysine acetyltransferase ]].


Metabolism of triethylenetetramine and << 1,12-diamino-3,6,9-triazadodecane >> by the [[ spermidine/spermine-N(1)-acetyltransferase ]] and thialysine acetyltransferase.


We recently showed that << TETA >> is metabolized in vitro by polyamine catabolic enzyme [[ spermidine/spermine-N(1)-acetyltransferase ]] (SSAT1) and by thialysine acetyltransferase (SSAT2) to its monoacetylated derivative (MAT).


We recently showed that << TETA >> is metabolized in vitro by polyamine catabolic enzyme spermidine/spermine-N(1)-acetyltransferase ([[ SSAT1 ]]) and by thialysine acetyltransferase (SSAT2) to its monoacetylated derivative (MAT).


We recently showed that << TETA >> is metabolized in vitro by polyamine catabolic enzyme spermidine/spermine-N(1)-acetyltransferase (SSAT1) and by [[ thialysine acetyltransferase ]] (SSAT2) to its monoacetylated derivative (MAT).


We recently showed that << TETA >> is metabolized in vitro by polyamine catabolic enzyme spermidine/spermine-N(1)-acetyltransferase (SSAT1) and by thialysine acetyltransferase ([[ SSAT2 ]]) to its monoacetylated derivative (MAT).


We recently showed that TETA is metabolized in vitro by << polyamine >> catabolic enzyme [[ spermidine/spermine-N(1)-acetyltransferase ]] (SSAT1) and by thialysine acetyltransferase (SSAT2) to its monoacetylated derivative (MAT).


We recently showed that TETA is metabolized in vitro by << polyamine >> catabolic enzyme spermidine/spermine-N(1)-acetyltransferase ([[ SSAT1 ]]) and by thialysine acetyltransferase (SSAT2) to its monoacetylated derivative (MAT).


The acetylation of << TETA >> is increased in [[ SSAT1 ]]-overexpressing mice compared with wild-type mice.


However, SSAT1-deficient mice metabolize << TETA >> at the same rate as the wild-type mice, indicating the existence of another [[ N-acetylase ]] respons 2ible for its metabolism in mice.


Here, we show that siRNA-mediated knockdown of << SSAT2 >> in HEPG2 cells and in primary hepatocytes from the SSAT1-deficient or wild-type mice reduced the metabolism of [[ TETA ]] to MAT.


By contrast, << 1,12-diamino-3,6,9-triazadodecane >>(SpmTrien), a charge-deficient spermine analog, was an extremely poor substrate of human recombinant SSAT2 and was metabolized by [[ SSAT1 ]] in HEPG2 cells and in wild-type primary hepatocytes.


By contrast, << 1,12-diamino-3,6,9-triazadodecane >>(SpmTrien), a charge-deficient spermine analog, was an extremely poor substrate of [[ human recombinant SSAT2 ]] and was metabolized by SSAT1 in HEPG2 cells and in wild-type primary hepatocytes.


By contrast, 1,12-diamino-3,6,9-triazadodecane(<< SpmTrien >>), a charge-deficient spermine analog, was an extremely poor substrate of human recombinant SSAT2 and was metabolized by [[ SSAT1 ]] in HEPG2 cells and in wild-type primary hepatocytes.


By contrast, 1,12-diamino-3,6,9-triazadodecane(<< SpmTrien >>), a charge-deficient spermine analog, was an extremely poor substrate of [[ human recombinant SSAT2 ]] and was metabolized by SSAT1 in HEPG2 cells and in wild-type primary hepatocytes.


By contrast, 1,12-diamino-3,6,9-triazadodecane(SpmTrien), a charge-deficient << spermine >> analog, was an extremely poor substrate of human recombinant SSAT2 and was metabolized by [[ SSAT1 ]] in HEPG2 cells and in wild-type primary hepatocytes.


By contrast, 1,12-diamino-3,6,9-triazadodecane(SpmTrien), a charge-deficient << spermine >> analog, was an extremely poor substrate of [[ human recombinant SSAT2 ]] and was metabolized by SSAT1 in HEPG2 cells and in wild-type primary hepatocytes.


Thus, despite the similar structures of TETA and SpmTrien, << SSAT2 >> is the main acetylator of [[ TETA ]], whereas SpmTrien is primarily acetylated by SSAT1.


Thus, despite the similar structures of TETA and SpmTrien, SSAT2 is the main acetylator of TETA, whereas << SpmTrien >> is primarily acetylated by [[ SSAT1 ]].


In vitro metabolism of the << 5-hydroxytryptamine1B >> receptor antagonist [[ elzasonan ]].


The rCYP data was normalized relative to the levels of each CYP form in native human liver microsomes to better assess the contribution of each << rCYP >> in the metabolism of [[ elzasonan ]].


Cytochrome b5 has shown to be an essential component in << P450 3A4 >> catalyzed [[ 5-hydroxyelzasonan ]] formation and provides insights on the disconnect between human liver microsomes data and that of rCYP.


In utero exposure to << valproic acid >> (VPA), a [[ histone deacetylase ]] (HDAC) inhibitor, causes neural tube, heart, and limb defects.


In utero exposure to << valproic acid >> (VPA), a histone deacetylase ([[ HDAC ]]) inhibitor, causes neural tube, heart, and limb defects.


In utero exposure to valproic acid (<< VPA >>), a [[ histone deacetylase ]] (HDAC) inhibitor, causes neural tube, heart, and limb defects.


In utero exposure to valproic acid (<< VPA >>), a histone deacetylase ([[ HDAC ]]) inhibitor, causes neural tube, heart, and limb defects.


<< VPA >> caused a significant concentration- dependent increase in limb abnormalities, which was correlated with its [[ HDAC ]] inhibitory effect.


The signaling of both << Sox9 >> and Runx2, key regulators of chondrogenesis, was downregulated by [[ VPA ]].


The signaling of both Sox9 and << Runx2 >>, key regulators of chondrogenesis, was downregulated by [[ VPA ]].


<< α-TOCO >> plus a [[ pancaspase ]] inhibitor completely abolished AMD/TNF-induced cytotoxicity.


In summary, activation of << caspases >> and oxidative stress were observed after [[ AMD ]]/TNF cotreatment, and caspase inhibitors and a lipid-soluble free-radical scavenger attenuated AMD/TNF-induced cytotoxicity.


Human serum butyrylcholinesterase (<< HuBChE >>) is currently the most suitable bioscavenger for the prophylaxis of highly toxic [[ organophosphate ]] (OP) nerve agents.


<< Human serum butyrylcholinesterase >> (HuBChE) is currently the most suitable bioscavenger for the prophylaxis of highly toxic [[ organophosphate ]] (OP) nerve agents.


Cu-dependent << tyrosinase >> activity was also markedly reduced in both types of CLDN knockdown cells when incubated with the substrate [[ l-DOPA ]].


Protein expression of << Ugt1a6 >> also decreased and corresponded with reduced in vitro glucuronidation of [[ bisphenol A ]] in S9 fractions from livers of pregnant mice.


<< Dimethylfumarate >> attenuates renal fibrosis via NF-E2-related factor 2-mediated inhibition of transforming growth factor-beta/[[ Smad ]] signaling.


<< Dimethylfumarate >> attenuates renal fibrosis via NF-E2-related factor 2-mediated inhibition of [[ transforming growth factor-beta ]]/Smad signaling.


Results showed that << DMF >> increased nuclear levels of [[ Nrf2 ]], and both DMF and adenovirus-mediated overexpression of Nrf2 (Ad-Nrf2) decreased PAI-1, alpha-smooth muscle actin (alpha-SMA), fibronectin and type 1 collagen expression in TGF-beta-treated rat mesangial cells (RMCs) and renal fibroblast cells (NRK-49F).


Results showed that DMF increased nuclear levels of Nrf2, and both << DMF >> and adenovirus-mediated overexpression of [[ Nrf2 ]] (Ad-Nrf2) decreased PAI-1, alpha-smooth muscle actin (alpha-SMA), fibronectin and type 1 collagen expression in TGF-beta-treated rat mesangial cells (RMCs) and renal fibroblast cells (NRK-49F).


Results showed that DMF increased nuclear levels of Nrf2, and both << DMF >> and adenovirus-mediated overexpression of Nrf2 (Ad-Nrf2) decreased [[ PAI-1 ]], alpha-smooth muscle actin (alpha-SMA), fibronectin and type 1 collagen expression in TGF-beta-treated rat mesangial cells (RMCs) and renal fibroblast cells (NRK-49F).


Results showed that DMF increased nuclear levels of Nrf2, and both << DMF >> and adenovirus-mediated overexpression of Nrf2 (Ad-Nrf2) decreased PAI-1, [[ alpha-smooth muscle actin ]] (alpha-SMA), fibronectin and type 1 collagen expression in TGF-beta-treated rat mesangial cells (RMCs) and renal fibroblast cells (NRK-49F).


Results showed that DMF increased nuclear levels of Nrf2, and both << DMF >> and adenovirus-mediated overexpression of Nrf2 (Ad-Nrf2) decreased PAI-1, alpha-smooth muscle actin ([[ alpha-SMA ]]), fibronectin and type 1 collagen expression in TGF-beta-treated rat mesangial cells (RMCs) and renal fibroblast cells (NRK-49F).


Results showed that DMF increased nuclear levels of Nrf2, and both << DMF >> and adenovirus-mediated overexpression of Nrf2 (Ad-Nrf2) decreased PAI-1, alpha-smooth muscle actin (alpha-SMA), [[ fibronectin ]] and type 1 collagen expression in TGF-beta-treated rat mesangial cells (RMCs) and renal fibroblast cells (NRK-49F).


Results showed that DMF increased nuclear levels of Nrf2, and both << DMF >> and adenovirus-mediated overexpression of Nrf2 (Ad-Nrf2) decreased PAI-1, alpha-smooth muscle actin (alpha-SMA), fibronectin and [[ type 1 collagen ]] expression in TGF-beta-treated rat mesangial cells (RMCs) and renal fibroblast cells (NRK-49F).


Additionally, << DMF >> and Ad-Nrf2 repressed [[ TGF-beta ]]-stimulated Smad3 activity by inhibiting Smad3 phosphorylation, which was restored by siRNA-mediated knockdown of Nrf2 expression.


Additionally, << DMF >> and Ad-Nrf2 repressed TGF-beta-stimulated [[ Smad3 ]] activity by inhibiting Smad3 phosphorylation, which was restored by siRNA-mediated knockdown of Nrf2 expression.


Additionally, << DMF >> and Ad-Nrf2 repressed TGF-beta-stimulated Smad3 activity by inhibiting [[ Smad3 ]] phosphorylation, which was restored by siRNA-mediated knockdown of Nrf2 expression.


However, downregulation of the antioxidant response element (ARE)-driven Nrf2 target genes such as NQO1, HO-1 and glutathione S-transferase (GST) did not reverse the inhibitory effect of << DMF >> on [[ TGF-beta ]]-induced upregulation of profibrotic genes or extracellular matrix proteins, suggesting an ARE-independent anti-fibrotic activity of DMF.


Finally, << DMF >> suppressed unilateral ureteral obstruction (UUO)-induced renal fibrosis and alpha-SMA, fibronectin and type 1 collagen expression in the obstructed kidneys from UUO mice, along with increased and decreased expression of [[ Nrf2 ]] and phospho-Smad3, respectively.


Finally, << DMF >> suppressed unilateral ureteral obstruction (UUO)-induced renal fibrosis and [[ alpha-SMA ]], fibronectin and type 1 collagen expression in the obstructed kidneys from UUO mice, along with increased and decreased expression of Nrf2 and phospho-Smad3, respectively.


Finally, << DMF >> suppressed unilateral ureteral obstruction (UUO)-induced renal fibrosis and alpha-SMA, [[ fibronectin ]] and type 1 collagen expression in the obstructed kidneys from UUO mice, along with increased and decreased expression of Nrf2 and phospho-Smad3, respectively.


Finally, << DMF >> suppressed unilateral ureteral obstruction (UUO)-induced renal fibrosis and alpha-SMA, fibronectin and [[ type 1 collagen ]] expression in the obstructed kidneys from UUO mice, along with increased and decreased expression of Nrf2 and phospho-Smad3, respectively.


Finally, << DMF >> suppressed unilateral ureteral obstruction (UUO)-induced renal fibrosis and alpha-SMA, fibronectin and type 1 collagen expression in the obstructed kidneys from UUO mice, along with increased and decreased expression of Nrf2 and [[ phospho-Smad3 ]], respectively.


In summary, << DMF >> attenuated renal fibrosis via the Nrf2-mediated inhibition of [[ TGF-beta ]]/Smad3 signaling in an ARE-independent manner, suggesting that DMF could be used to treat renal fibrosis.


In summary, << DMF >> attenuated renal fibrosis via the Nrf2-mediated inhibition of TGF-beta/[[ Smad3 ]] signaling in an ARE-independent manner, suggesting that DMF could be used to treat renal fibrosis.


Our results showed that bone remodeling was significantly decreased in CCL3(-/-) and CCR1(-/-) mice and in animals treated with << Met >>-RANTES (an antagonist of [[ CCR5 ]] and CCR1).


Our results showed that bone remodeling was significantly decreased in CCL3(-/-) and CCR1(-/-) mice and in animals treated with << Met >>-RANTES (an antagonist of CCR5 and [[ CCR1 ]]).


mRNA levels of << receptor activator of nuclear factor kappa-B >> (RANK), its ligand RANKL, tumor necrosis factor alpha (TNF-α) and RANKL/osteoprotegerin (OPG) ratio were diminished in the periodontium of CCL3(-/-) mice and in the group treated with [[ Met ]]-RANTES.


mRNA levels of receptor activator of nuclear factor kappa-B (<< RANK >>), its ligand RANKL, tumor necrosis factor alpha (TNF-α) and RANKL/osteoprotegerin (OPG) ratio were diminished in the periodontium of CCL3(-/-) mice and in the group treated with [[ Met ]]-RANTES.


mRNA levels of receptor activator of nuclear factor kappa-B (RANK), its ligand << RANKL >>, tumor necrosis factor alpha (TNF-α) and RANKL/osteoprotegerin (OPG) ratio were diminished in the periodontium of CCL3(-/-) mice and in the group treated with [[ Met ]]-RANTES.


mRNA levels of receptor activator of nuclear factor kappa-B (RANK), its ligand RANKL, << tumor necrosis factor alpha >> (TNF-α) and RANKL/osteoprotegerin (OPG) ratio were diminished in the periodontium of CCL3(-/-) mice and in the group treated with [[ Met ]]-RANTES.


mRNA levels of receptor activator of nuclear factor kappa-B (RANK), its ligand RANKL, tumor necrosis factor alpha (<< TNF-α >>) and RANKL/osteoprotegerin (OPG) ratio were diminished in the periodontium of CCL3(-/-) mice and in the group treated with [[ Met ]]-RANTES.


mRNA levels of receptor activator of nuclear factor kappa-B (RANK), its ligand RANKL, tumor necrosis factor alpha (TNF-α) and << RANKL >>/osteoprotegerin (OPG) ratio were diminished in the periodontium of CCL3(-/-) mice and in the group treated with [[ Met ]]-RANTES.


mRNA levels of receptor activator of nuclear factor kappa-B (RANK), its ligand RANKL, tumor necrosis factor alpha (TNF-α) and RANKL/<< osteoprotegerin >> (OPG) ratio were diminished in the periodontium of CCL3(-/-) mice and in the group treated with [[ Met ]]-RANTES.


mRNA levels of receptor activator of nuclear factor kappa-B (RANK), its ligand RANKL, tumor necrosis factor alpha (TNF-α) and RANKL/osteoprotegerin (<< OPG >>) ratio were diminished in the periodontium of CCL3(-/-) mice and in the group treated with [[ Met ]]-RANTES.


<< Met >>-RANTES treatment also reduced the levels of [[ cathepsin K ]] and metalloproteinase 13 (MMP13).


<< Met >>-RANTES treatment also reduced the levels of cathepsin K and [[ metalloproteinase 13 ]] (MMP13).


<< Met >>-RANTES treatment also reduced the levels of cathepsin K and metalloproteinase 13 ([[ MMP13 ]]).


The expression of the osteoblast markers runt-related transcription factor 2 (RUNX2) and periostin was decreased, while << osteocalcin >> (OCN) was augmented in CCL3(-/-) and [[ Met ]]-RANTES-treated mice.


The expression of the osteoblast markers runt-related transcription factor 2 (RUNX2) and periostin was decreased, while osteocalcin (<< OCN >>) was augmented in CCL3(-/-) and [[ Met ]]-RANTES-treated mice.


The expression of the osteoblast markers runt-related transcription factor 2 (<< RUNX2 >>) and periostin was decreased, while osteocalcin (OCN) was augmented in CCL3(-/-) and [[ Met ]]-RANTES-treated mice.


The expression of the osteoblast markers runt-related transcription factor 2 (RUNX2) and << periostin >> was decreased, while osteocalcin (OCN) was augmented in CCL3(-/-) and [[ Met ]]-RANTES-treated mice.


The expression of the osteoblast markers << runt-related transcription factor 2 >> (RUNX2) and periostin was decreased, while osteocalcin (OCN) was augmented in CCL3(-/-) and [[ Met ]]-RANTES-treated mice.


The quinolizidine alkaloids (natural products) such as oxymatrine, sophoridine, sophocarpine and << matrine >> carry the common molecular structure of O=C=N-C-C-C-N that possessed positive ionotropic effect and [[ hERG ]] blocking activity.


The quinolizidine alkaloids (natural products) such as oxymatrine, sophoridine, sophocarpine and matrine carry the common molecular structure of << O=C=N-C-C-C-N >> that possessed positive ionotropic effect and [[ hERG ]] blocking activity.


The << quinolizidine alkaloids >> (natural products) such as oxymatrine, sophoridine, sophocarpine and matrine carry the common molecular structure of O=C=N-C-C-C-N that possessed positive ionotropic effect and [[ hERG ]] blocking activity.


The quinolizidine alkaloids (natural products) such as << oxymatrine >>, sophoridine, sophocarpine and matrine carry the common molecular structure of O=C=N-C-C-C-N that possessed positive ionotropic effect and [[ hERG ]] blocking activity.


The quinolizidine alkaloids (natural products) such as oxymatrine, << sophoridine >>, sophocarpine and matrine carry the common molecular structure of O=C=N-C-C-C-N that possessed positive ionotropic effect and [[ hERG ]] blocking activity.


The quinolizidine alkaloids (natural products) such as oxymatrine, sophoridine, << sophocarpine >> and matrine carry the common molecular structure of O=C=N-C-C-C-N that possessed positive ionotropic effect and [[ hERG ]] blocking activity.


Several effects of << polyphenols >> are useful in this scenario, including a reduction in the activities of cytokines and modulation of cellular metabolism through histone deacetylase inhibitors, [[ AMPK ]] activators, calorie-restriction mimetics or epigenetic regulators.


Several effects of << polyphenols >> are useful in this scenario, including a reduction in the activities of [[ cytokines ]] and modulation of cellular metabolism through histone deacetylase inhibitors, AMPK activators, calorie-restriction mimetics or epigenetic regulators.


Several effects of << polyphenols >> are useful in this scenario, including a reduction in the activities of cytokines and modulation of cellular metabolism through [[ histone deacetylase ]] inhibitors, AMPK activators, calorie-restriction mimetics or epigenetic regulators.


Inhibition of << EGF >>/EGFR activation with [[ naphtho[1,2-b]furan-4,5-dione ]] blocks migration and invasion of MDA-MB-231 cells.


Inhibition of EGF/<< EGFR >> activation with [[ naphtho[1,2-b]furan-4,5-dione ]] blocks migration and invasion of MDA-MB-231 cells.


<< NFD >> suppressed [[ EGF ]]-mediated protein levels of c-Jun and c-Fos, and reduced MMP-9 expression and activity, concomitantly with a marked inhibition on cell migration and invasion without obvious cellular cytotoxicity.


<< NFD >> suppressed EGF-mediated protein levels of [[ c-Jun ]] and c-Fos, and reduced MMP-9 expression and activity, concomitantly with a marked inhibition on cell migration and invasion without obvious cellular cytotoxicity.


<< NFD >> suppressed EGF-mediated protein levels of c-Jun and [[ c-Fos ]], and reduced MMP-9 expression and activity, concomitantly with a marked inhibition on cell migration and invasion without obvious cellular cytotoxicity.


<< NFD >> suppressed EGF-mediated protein levels of c-Jun and c-Fos, and reduced [[ MMP-9 ]] expression and activity, concomitantly with a marked inhibition on cell migration and invasion without obvious cellular cytotoxicity.


<< NFD >> abrogated [[ EGF ]]-induced phosphorylation of EGF receptor (EGFR) and phosphatidylinositol 3-kinase (PI3K)/Akt.


<< NFD >> abrogated EGF-induced phosphorylation of [[ EGF receptor ]] (EGFR) and phosphatidylinositol 3-kinase (PI3K)/Akt.


<< NFD >> abrogated EGF-induced phosphorylation of EGF receptor ([[ EGFR ]]) and phosphatidylinositol 3-kinase (PI3K)/Akt.


<< NFD >> abrogated EGF-induced phosphorylation of EGF receptor (EGFR) and [[ phosphatidylinositol 3-kinase ]] (PI3K)/Akt.


<< NFD >> abrogated EGF-induced phosphorylation of EGF receptor (EGFR) and phosphatidylinositol 3-kinase ([[ PI3K ]])/Akt.


<< NFD >> abrogated EGF-induced phosphorylation of EGF receptor (EGFR) and phosphatidylinositol 3-kinase (PI3K)/[[ Akt ]].


The specific << PI3K >> inhibitor, [[ wortmannin ]], blocked significantly EGF-induced cell migration and invasion.


The specific PI3K inhibitor, << wortmannin >>, blocked significantly [[ EGF ]]-induced cell migration and invasion.


Furthermore, the EGFR inhibitor << AG1478 >> inhibited EGF-induced [[ MMP-9 ]] expression, cell migration and invasion, as well as the activation of PI3K/Akt, suggesting that PI3K/Akt activation occur downstream of EGFR activation.


Furthermore, the EGFR inhibitor << AG1478 >> inhibited EGF-induced MMP-9 expression, cell migration and invasion, as well as the activation of PI3K/Akt, suggesting that [[ PI3K ]]/Akt activation occur downstream of EGFR activation.


Furthermore, the EGFR inhibitor << AG1478 >> inhibited EGF-induced MMP-9 expression, cell migration and invasion, as well as the activation of PI3K/Akt, suggesting that PI3K/[[ Akt ]] activation occur downstream of EGFR activation.


Furthermore, the EGFR inhibitor << AG1478 >> inhibited EGF-induced MMP-9 expression, cell migration and invasion, as well as the activation of PI3K/Akt, suggesting that PI3K/Akt activation occur downstream of [[ EGFR ]] activation.


Furthermore, the << EGFR >> inhibitor [[ AG1478 ]] inhibited EGF-induced MMP-9 expression, cell migration and invasion, as well as the activation of PI3K/Akt, suggesting that PI3K/Akt activation occur downstream of EGFR activation.


Furthermore, the EGFR inhibitor << AG1478 >> inhibited [[ EGF ]]-induced MMP-9 expression, cell migration and invasion, as well as the activation of PI3K/Akt, suggesting that PI3K/Akt activation occur downstream of EGFR activation.


Furthermore, the EGFR inhibitor << AG1478 >> inhibited EGF-induced MMP-9 expression, cell migration and invasion, as well as the activation of [[ PI3K ]]/Akt, suggesting that PI3K/Akt activation occur downstream of EGFR activation.


Furthermore, the EGFR inhibitor << AG1478 >> inhibited EGF-induced MMP-9 expression, cell migration and invasion, as well as the activation of PI3K/[[ Akt ]], suggesting that PI3K/Akt activation occur downstream of EGFR activation.


These findings suggest that << NFD >> inhibited the EGF-induced invasion and migration of MDA-MB-231 cells via EGFR-dependent [[ PI3K ]]/Akt signaling, leading to the down-regulation of MMP-9 expression.


These findings suggest that << NFD >> inhibited the EGF-induced invasion and migration of MDA-MB-231 cells via EGFR-dependent PI3K/[[ Akt ]] signaling, leading to the down-regulation of MMP-9 expression.


These findings suggest that << NFD >> inhibited the EGF-induced invasion and migration of MDA-MB-231 cells via EGFR-dependent PI3K/Akt signaling, leading to the down-regulation of [[ MMP-9 ]] expression.


These findings suggest that << NFD >> inhibited the [[ EGF ]]-induced invasion and migration of MDA-MB-231 cells via EGFR-dependent PI3K/Akt signaling, leading to the down-regulation of MMP-9 expression.


These findings suggest that << NFD >> inhibited the EGF-induced invasion and migration of MDA-MB-231 cells via [[ EGFR ]]-dependent PI3K/Akt signaling, leading to the down-regulation of MMP-9 expression.


Herein, we report the identification and characterization of << 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile >> (ESI-09), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated [[ insulin ]] secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (<< ESI-09 >>), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated [[ insulin ]] secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (ESI-09), a novel noncyclic << nucleotide >> EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated [[ insulin ]] secretion in pancreatic β cells.


Herein, we report the identification and characterization of << 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile >> (ESI-09), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular [[ EPAC ]]-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of << 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile >> (ESI-09), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated [[ Rap1 ]] activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of << 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile >> (ESI-09), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and [[ Akt ]] phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of << 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile >> (ESI-09), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as [[ EPAC ]]-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (<< ESI-09 >>), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular [[ EPAC ]]-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (<< ESI-09 >>), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated [[ Rap1 ]] activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (<< ESI-09 >>), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and [[ Akt ]] phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (<< ESI-09 >>), a novel noncyclic nucleotide EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as [[ EPAC ]]-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (ESI-09), a novel noncyclic << nucleotide >> EPAC antagonist that is capable of specifically blocking intracellular [[ EPAC ]]-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (ESI-09), a novel noncyclic << nucleotide >> EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated [[ Rap1 ]] activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (ESI-09), a novel noncyclic << nucleotide >> EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and [[ Akt ]] phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (ESI-09), a novel noncyclic << nucleotide >> EPAC antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as [[ EPAC ]]-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of << 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile >> (ESI-09), a novel noncyclic nucleotide [[ EPAC ]] antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (<< ESI-09 >>), a novel noncyclic nucleotide [[ EPAC ]] antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


Herein, we report the identification and characterization of 3-(5-tert-butyl-isoxazol-3-yl)-2-[(3-chloro-phenyl)-hydrazono]-3-oxo-propionitrile (ESI-09), a novel noncyclic << nucleotide >> [[ EPAC ]] antagonist that is capable of specifically blocking intracellular EPAC-mediated Rap1 activation and Akt phosphorylation, as well as EPAC-mediated insulin secretion in pancreatic β cells.


<< Metformin >> directly inhibits [[ ghrelin ]] secretion through AMP-activated protein kinase in rat primary gastric cells.


<< Metformin >> treatment is also associated with lower circulating levels of the [[ orexigenic hormone ]] ghrelin.


<< Metformin >> treatment is also associated with lower circulating levels of the orexigenic hormone [[ ghrelin ]].


Metformin significantly reduced << ghrelin >> secretion and proghrelin mRNA production and both these effects were blocked by co-incubation with the AMPK inhibitor [[ compound C ]].


Metformin significantly reduced ghrelin secretion and << proghrelin >> mRNA production and both these effects were blocked by co-incubation with the AMPK inhibitor [[ compound C ]].


<< Metformin >> significantly reduced [[ ghrelin ]] secretion and proghrelin mRNA production and both these effects were blocked by co-incubation with the AMPK inhibitor compound C.


<< Metformin >> significantly reduced ghrelin secretion and [[ proghrelin ]] mRNA production and both these effects were blocked by co-incubation with the AMPK inhibitor compound C.


Metformin significantly reduced ghrelin secretion and proghrelin mRNA production and both these effects were blocked by co-incubation with the << AMPK >> inhibitor [[ compound C ]].


Furthermore, the << AMPK >> activator [[ 5-amino-1-β-D-ribofuranosyl-imidazole-4-carboxamide ]] (AICAR) significantly inhibited ghrelin secretion.


Furthermore, the << AMPK >> activator 5-amino-1-β-D-ribofuranosyl-imidazole-4-carboxamide ([[ AICAR ]]) significantly inhibited ghrelin secretion.


Furthermore, the AMPK activator 5-amino-1-β-D-ribofuranosyl-imidazole-4-carboxamide (<< AICAR >>) significantly inhibited [[ ghrelin ]] secretion.


Finally, << Metformin >> treatment caused a significant increase in the level of [[ phosphorylated (active) AMPK ]].


Our results show that << Metformin >> directly inhibits stomach [[ ghrelin ]] production and secretion through AMPK.


Fungicide << prochloraz >> and environmental pollutant dioxin induce the [[ ABCG2 ]] transporter in bovine mammary epithelial cells by the arylhydrocarbon receptor signaling pathway.


Fungicide prochloraz and environmental pollutant << dioxin >> induce the [[ ABCG2 ]] transporter in bovine mammary epithelial cells by the arylhydrocarbon receptor signaling pathway.


As these regulatory motifs mediate regulation of target genes by << AhR >> agonists including [[ TCDD ]] and prochloraz, we have systematically investigated the effect of both contaminants on functional ABCG2 transport activity in primary bovine mammary epithelial cells.


As these regulatory motifs mediate regulation of target genes by << AhR >> agonists including TCDD and [[ prochloraz ]], we have systematically investigated the effect of both contaminants on functional ABCG2 transport activity in primary bovine mammary epithelial cells.


TCDD or prochloraz doubled << ABCG2 >>-mediated [[ Hoechst H33342 ]] secretion.


This effect was almost completely reversed by specific << ABCG2 >> inhibitor [[ Ko143 ]].


Receptor binding was significantly reduced by specific << AhR >> antagonist [[ salicyl amide ]].


Induction of AhR by << TCDD >> and prochloraz resulted in a time- and dose-dependent increase of [[ ABCG2 ]] gene expression and transporter protein levels.


Induction of AhR by TCDD and << prochloraz >> resulted in a time- and dose-dependent increase of [[ ABCG2 ]] gene expression and transporter protein levels.


Induction of << AhR >> by [[ TCDD ]] and prochloraz resulted in a time- and dose-dependent increase of ABCG2 gene expression and transporter protein levels.


Induction of << AhR >> by TCDD and [[ prochloraz ]] resulted in a time- and dose-dependent increase of ABCG2 gene expression and transporter protein levels.


We found that << Ag >> NPs were highly cytotoxic to hepatocytes (LC(50) lactate dehydrogenase: 2.5 μg/cm(2)) and affected hepatocyte homeostasis by reducing [[ albumin ]] release.


We observed similar effects of << Ag >> NPs on inflammatory mediator expression in vitro and in vivo with increase of [[ interleukin-8 ]] (IL-8)/macrophage inflammatory protein 2, IL-1RI, and tumor necrosis factor-α expression in both models and increased IL-8 protein release in vitro.


We observed similar effects of << Ag >> NPs on inflammatory mediator expression in vitro and in vivo with increase of interleukin-8 ([[ IL-8 ]])/macrophage inflammatory protein 2, IL-1RI, and tumor necrosis factor-α expression in both models and increased IL-8 protein release in vitro.


We observed similar effects of << Ag >> NPs on inflammatory mediator expression in vitro and in vivo with increase of interleukin-8 (IL-8)/[[ macrophage inflammatory protein 2 ]], IL-1RI, and tumor necrosis factor-α expression in both models and increased IL-8 protein release in vitro.


We observed similar effects of << Ag >> NPs on inflammatory mediator expression in vitro and in vivo with increase of interleukin-8 (IL-8)/macrophage inflammatory protein 2, [[ IL-1RI ]], and tumor necrosis factor-α expression in both models and increased IL-8 protein release in vitro.


We observed similar effects of << Ag >> NPs on inflammatory mediator expression in vitro and in vivo with increase of interleukin-8 (IL-8)/macrophage inflammatory protein 2, IL-1RI, and [[ tumor necrosis factor-α ]] expression in both models and increased IL-8 protein release in vitro.


We observed similar effects of << Ag >> NPs on inflammatory mediator expression in vitro and in vivo with increase of interleukin-8 (IL-8)/macrophage inflammatory protein 2, IL-1RI, and tumor necrosis factor-α expression in both models and increased [[ IL-8 ]] protein release in vitro.


Blood pressure was increased in rats exposed to IH, and treatment with the << PDK-1 >> inhibitor [[ OSU-03012 ]] [2-amino-N-{4-[5-(2-phenanthrenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]-phenyl}-acetamide] (33 mg/day) lowered blood pressure in IH but not sham group rats.


Blood pressure was increased in rats exposed to IH, and treatment with the << PDK-1 >> inhibitor OSU-03012 [[[ 2-amino-N-{4-[5-(2-phenanthrenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]-phenyl}-acetamide ]]] (33 mg/day) lowered blood pressure in IH but not sham group rats.


Following << CdCl₂ >> treatment, [[ ICAM2 ]] was found to be upregulated during restructuring of the seminiferous epithelium, with round spermatids becoming increasingly immunoreactive for ICAM2 by 6-16 h.


Interestingly, there was a loss in the binding of ICAM2 to << actin >> during [[ CdCl₂ ]]-induced germ cell loss, suggesting that a loss of ICAM2-actin interactions might have facilitated junction restructuring.


The catalytic competence of << cytochrome P450 >> in the synthesis of [[ serotonin ]] from 5-methoxytryptamine in the brain: an in vitro study.


The catalytic competence of << cytochrome P450 >> in the synthesis of serotonin from [[ 5-methoxytryptamine ]] in the brain: an in vitro study.


Of the rat CYP isoforms studied, << CYP2D >> isoforms were the most efficient in catalyzing the O-demethylation of 5-methoxytryptamine to [[ serotonin ]], but they were less effective than the human isoform CYP2D6.


Of the rat CYP isoforms studied, CYP2D isoforms were the most efficient in catalyzing the O-demethylation of 5-methoxytryptamine to << serotonin >>, but they were less effective than the [[ human isoform CYP2D6 ]].


Of the rat CYP isoforms studied, << CYP2D >> isoforms were the most efficient in catalyzing the [[ O ]]-demethylation of 5-methoxytryptamine to serotonin, but they were less effective than the human isoform CYP2D6.


Of the rat CYP isoforms studied, CYP2D isoforms were the most efficient in catalyzing the << O >>-demethylation of 5-methoxytryptamine to serotonin, but they were less effective than the [[ human isoform CYP2D6 ]].


Of the rat CYP isoforms studied, << CYP2D >> isoforms were the most efficient in catalyzing the O-demethylation of [[ 5-methoxytryptamine ]] to serotonin, but they were less effective than the human isoform CYP2D6.


Of the rat CYP isoforms studied, CYP2D isoforms were the most efficient in catalyzing the O-demethylation of << 5-methoxytryptamine >> to serotonin, but they were less effective than the [[ human isoform CYP2D6 ]].


The reaction was inhibited by the specific << CYP2D >> inhibitors [[ quinine ]] and fluoxetine.


The reaction was inhibited by the specific << CYP2D >> inhibitors quinine and [[ fluoxetine ]].


Human liver microsomes of the wild-type << CYP2D6 >> metabolized 5-methoxytryptamine to [[ serotonin ]] more effectively than did the defective CYP2D6*4*4 ones.


Human liver microsomes of the wild-type CYP2D6 metabolized 5-methoxytryptamine to << serotonin >> more effectively than did the defective [[ CYP2D6 ]]*4*4 ones.


Human liver microsomes of the wild-type << CYP2D6 >> metabolized [[ 5-methoxytryptamine ]] to serotonin more effectively than did the defective CYP2D6*4*4 ones.


Human liver microsomes of the wild-type CYP2D6 metabolized << 5-methoxytryptamine >> to serotonin more effectively than did the defective [[ CYP2D6 ]]*4*4 ones.


The obtained results indicate that << rat brain CYP2D >> isoforms catalyze the formation of [[ serotonin ]] from 5-methoxytryptamine, and that the deficit or genetic defect of CYP2D may affect serotonin metabolism in the brain.


The obtained results indicate that rat brain CYP2D isoforms catalyze the formation of serotonin from 5-methoxytryptamine, and that the deficit or genetic defect of << CYP2D >> may affect [[ serotonin ]] metabolism in the brain.


The obtained results indicate that << rat brain CYP2D >> isoforms catalyze the formation of serotonin from [[ 5-methoxytryptamine ]], and that the deficit or genetic defect of CYP2D may affect serotonin metabolism in the brain.


<< Toosendanin >> induces apoptosis through suppression of [[ JNK ]] signaling pathway in HL-60 cells.


Western blot analysis indicated that << TSN >> inhibits the [[ CDC42 ]]/MEKK1/JNK pathway.


Western blot analysis indicated that << TSN >> inhibits the CDC42/[[ MEKK1 ]]/JNK pathway.


Western blot analysis indicated that << TSN >> inhibits the CDC42/MEKK1/[[ JNK ]] pathway.


Administration of low, but not high, doses of oral << nicotine >> in DSS-treated mice resulted in a significant decrease in disease severity, histologic damage scores, as well as colonic level of [[ tumor necrosis factor-α ]].


Small interfering RNA directed BDNF, orexin-A, and << SB334867 >> [N-(2-methyl-6-benzoxazolyl)-N'-1,5-naphthyridin-4-yl urea; a specific [[ orexin-1 receptor ]] antagonist] were administered directly into the hypothalamus.


Small interfering RNA directed BDNF, orexin-A, and SB334867 [<< N-(2-methyl-6-benzoxazolyl)-N'-1,5-naphthyridin-4-yl urea >>; a specific [[ orexin-1 receptor ]] antagonist] were administered directly into the hypothalamus.


The MCAO-induced decrease in insulin receptor levels in the liver and skeletal muscle on day 1 was recovered to control levels by orexin-A, and this effect of << orexin-A >> was reversed by the administration of [[ SB334867 ]] as well as by hypothalamic BDNF knockdown.


The MCAO-induced decrease in << insulin receptor >> levels in the liver and skeletal muscle on day 1 was recovered to control levels by orexin-A, and this effect of orexin-A was reversed by the administration of [[ SB334867 ]] as well as by hypothalamic BDNF knockdown.


<< Mesalamine >> modulates intercellular adhesion through inhibition of [[ p-21 activated kinase-1 ]].


Moreover, << 5-ASA >> treatment restored membranous expression of adhesion molecules [[ E-cadherin ]] and β-catenin.


Moreover, << 5-ASA >> treatment restored membranous expression of adhesion molecules E-cadherin and [[ β-catenin ]].


<< PAK1 >> expression was elevated in APC(min) polyps and [[ 5-ASA ]] treatment reduced its expression.


We propose that inhibition of << PAK1 >> expression by [[ 5-ASA ]] can impede with neoplastic progression in colorectal carcinogenesis.


The mechanism of << PAK1 >> inhibition and induction of membranous translocation of adhesion proteins by [[ 5-ASA ]] might be independent of its known anti-inflammatory action.


In contrast, << EGCG >> markedly downregulated major [[ bile acid transporters ]] (Asbt and Ostα) and regulatory molecules (Shp and Fgf15) in the ileum.


In contrast, << EGCG >> markedly downregulated major bile acid transporters ([[ Asbt ]] and Ostα) and regulatory molecules (Shp and Fgf15) in the ileum.


In contrast, << EGCG >> markedly downregulated major bile acid transporters (Asbt and [[ Ostα ]]) and regulatory molecules (Shp and Fgf15) in the ileum.


In contrast, << EGCG >> markedly downregulated major bile acid transporters (Asbt and Ostα) and regulatory molecules ([[ Shp ]] and Fgf15) in the ileum.


In contrast, << EGCG >> markedly downregulated major bile acid transporters (Asbt and Ostα) and regulatory molecules (Shp and [[ Fgf15 ]]) in the ileum.


This study shows ability of << EGCG >> to raise plasma bile acid concentrations, mainly through [[ Cyp7a1 ]] upregulation, and to decrease bile production through reduction in Mrp2-mediated bile acid-independent bile flow.


<< Catalpol >> inhibits LPS plus [[ IFN-γ ]]-induced inflammatory response in astrocytes primary cultures.


Biochemical analyses showed that NO and ROS production and << iNOS >> activity were significantly reduced by [[ catalpol ]].


Data at transcriptional level also demonstrated that << catalpol >> potently attenuated gene expressions involved in inflammation, such as [[ iNOS ]], COX-2 and TLR4.


Data at transcriptional level also demonstrated that << catalpol >> potently attenuated gene expressions involved in inflammation, such as iNOS, [[ COX-2 ]] and TLR4.


Data at transcriptional level also demonstrated that << catalpol >> potently attenuated gene expressions involved in inflammation, such as iNOS, COX-2 and [[ TLR4 ]].


In addition, our exploration further revealed that the suppressive action of << catalpol >> on inflammation was mediated via inhibiting nuclear factor-κB ([[ NF-κB ]]) activation.


In addition, our exploration further revealed that the suppressive action of << catalpol >> on inflammation was mediated via inhibiting [[ nuclear factor-κB ]] (NF-κB) activation.


Collectively, these results suggest that << catalpol >> can exert inhibitory effects on the inflammatory reaction in astrocytes and that inactivation of [[ NF-κB ]] could be the major determinant for its anti-inflammatory mechanism.


<< Protein tyrosine phosphatase 1B >> inhibitory effect by dammarane-type triterpenes from hydrolyzate of total Gynostemma pentaphyllum [[ saponins ]].


<< Protein tyrosine phosphatase 1B >> inhibitory effect by [[ dammarane ]]-type triterpenes from hydrolyzate of total Gynostemma pentaphyllum saponins.


<< Protein tyrosine phosphatase 1B >> inhibitory effect by dammarane-type [[ triterpenes ]] from hydrolyzate of total Gynostemma pentaphyllum saponins.


Also, reactive astrogliosis takes part of the early responses to the insult with << (PhTe)(2) >>, evidenced by upregulated [[ GFAP ]] in Western blot, PCR and immunofluorescence analysis.


Six days after (PhTe)(2) injection we found persistent astrogliosis, increased propidium iodide (PI) positive cells in NeuN positive population evidenced by flow cytometry and reduced immunofluorescence for << NeuN >>, suggesting that the in vivo exposure to [[ (PhTe)(2) ]] progressed to neuronal death.


Neurodegeneration was related with decreased [(3)H]glutamate uptake and decreased << Akt >> immunoreactivity, however phospho-GSK-3-β (Ser9) was not altered in [[ (PhTe)(2) ]] injected rat.


Therefore, the present results show that the earlier cerebellar responses to << (PhTe)(2) >> include disruption of cytoskeletal homeostasis that could be related with [[ MAPK ]] and PKA activation and reactive astrogliosis.


Therefore, the present results show that the earlier cerebellar responses to << (PhTe)(2) >> include disruption of cytoskeletal homeostasis that could be related with MAPK and [[ PKA ]] activation and reactive astrogliosis.


Fluorescence of the reporter dye is turned on by rapid removal of the quinone quencher, an event that immediately occurs only after highly selective, two-electron reduction of the sterically and conformationally restricted << quinone >> substrate by the cancer-associated [[ human NAD(P)H:quinone oxidoreductase isozyme 1 ]] (hNQO1).


Fluorescence of the reporter dye is turned on by rapid removal of the quinone quencher, an event that immediately occurs only after highly selective, two-electron reduction of the sterically and conformationally restricted << quinone >> substrate by the cancer-associated human NAD(P)H:quinone oxidoreductase isozyme 1 ([[ hNQO1 ]]).


Synthesis, biological evaluation, and molecular modeling of << glycyrrhizin >> derivatives as potent [[ high-mobility group box-1 ]] inhibitors with anti-heart-failure activity in vivo.


Within the << TPBP >> scaffold, either electronic or steric perturbations to the central piperidine ring led to a loss of selective M(1) allosteric agonism and afforded pan-[[ mAChR ]] antagonism, which was demonstrated to be mediated via the orthosteric site.


Within the TPBP scaffold, either electronic or steric perturbations to the central << piperidine >> ring led to a loss of selective M(1) allosteric agonism and afforded pan-[[ mAChR ]] antagonism, which was demonstrated to be mediated via the orthosteric site.


Additional SAR around a related M(1) allosteric agonist family (<< VU0357017 >>) identified similar, subtle 'molecular switches' that modulated modes of pharmacology from allosteric agonism to pan-[[ mAChR ]] orthosteric antagonism.


2. The objective of this article is to examine the effects of single and repeated administrations of silymarin on pharmacokinetics of a << P-gp >> substrate, [[ risperidone ]], and its major metabolite, 9-hydroxyrisperidone, in rats.


2. The objective of this article is to examine the effects of single and repeated administrations of silymarin on pharmacokinetics of a << P-gp >> substrate, risperidone, and its major metabolite, [[ 9-hydroxyrisperidone ]], in rats.


On the other hand, peptides modified with << (2S,4R)-4-(naphthalene-2-ylmethyl)pyrrolidine-2-carboxylic acid >>, apart from their moderate antioxytocic activity, turned out to be weak antagonists of the pressor response to [[ arginine vasopressin ]].


<< Liver X Receptor (LXR) α >> and LXR β are nuclear receptors activated by [[ oxysterols ]], oxidized derivatives of cholesterol.


Liver X Receptor (LXR) α and << LXR β >> are nuclear receptors activated by [[ oxysterols ]], oxidized derivatives of cholesterol.


β-catenin regulates << GnRH >>-induced [[ FSHβ ]] gene expression.


<< GnRH >> caused a sustained increase in nuclear [[ β-catenin ]] levels, which was significantly reduced by c-Jun N-terminal kinase (JNK) inhibition.


Small interfering RNA-mediated knockdown of β-catenin mRNA demonstrated that induction of << FSHβ >> mRNA by [[ GnRH ]] depended on β-catenin and that regulation of FSHβ by β-catenin occurred independently of the JNK-c-jun pathway.


Furthermore, knockdown of Brms1L significantly attenuated << GnRH >>-induced [[ FSHβ ]] expression.


Thus, our findings indicate that the expression of Brms1L depends on β-catenin activity and contributes to << FSHβ >> induction by [[ GnRH ]].


The herbicide << paraquat >> (PQ) is a [[ P-gp ]] substrate responsible for thousands of fatal intoxications worldwide that still lacks an effective antidote.


The aim of the present work was to evaluate the effectiveness of such an antidote by testing whether << doxorubicin >> (DOX), a known [[ P-gp ]] inducer, could efficiently protect Caco-2 cells against PQ cytotoxicity, 6 h after the incubation with the herbicide, reflecting a real-life intoxication scenario.


The aim of the present work was to evaluate the effectiveness of such an antidote by testing whether doxorubicin (<< DOX >>), a known [[ P-gp ]] inducer, could efficiently protect Caco-2 cells against PQ cytotoxicity, 6 h after the incubation with the herbicide, reflecting a real-life intoxication scenario.


In conclusion, in this cellular model, << DOX >> effectively protects against PQ toxicity by inducing [[ P-gp ]] and through the interaction with the choline transporter, suggesting that compounds presenting this double feature of promoting the efflux and limiting the uptake of PQ could be used as effective antidotes to treat intoxications.


The selective << SYK >> inhibitor [[ P505-15 ]] (PRT062607) inhibits B cell signaling and function in vitro and in vivo and augments the activity of fludarabine in chronic lymphocytic leukemia.


The selective << SYK >> inhibitor P505-15 ([[ PRT062607 ]]) inhibits B cell signaling and function in vitro and in vivo and augments the activity of fludarabine in chronic lymphocytic leukemia.