u 73122 Search Results


96
Tocris u73122 tocris
Figure 6. CCL2 Promotes Excitatory Synaptic Transmission through CCR2 and PLC Signaling (A and B) The effect of CCL2 application on mEPSC frequency and amplitude in CA1 pyramidal neurons of Ccr2 KO mice, representative traces (A) and summary data (B) (13 cells from 3 mice; Wilcoxon matched-pairs signed rank test). (C and D) The effect of CCL2 application on firing responses to stepwise current injections in CA1 pyramidal neurons of Ccr2 KO mice, representative traces (C) and summary data (D) (12–13 cells from 2 mice; two-way ANOVA, Bonferroni post hoc test). (E–H) mEPSC recordings from Lenti-Ccr2 RNAi infected CA1 pyramidal neurons (E and F), or neighboring uninfected neurons (G and H) before and after CCL2 application, representative traces (E, G) and summary data (F, H) (8–10 cells from 5 mice per condition; Wilcoxon matched-pairs signed rank test). (I–L) mEPSC recordings before and after CCL2 application with 10 mM <t>U73122</t> in aCSF (I and J) or with 5 mM BAPTA tetracesium in the internal cellular solution (K and L), representative traces (I, K) and summary data (J, L) (9–11 cells from 3 mice; Wilcoxon matched-pairs signed rank test). See also Figure S7.
U73122 Tocris, supplied by Tocris, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MedChemExpress u73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U73122, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Tocris 663684b u 73122 1 6 17b 3 methoxyestra 1 3 5 10 trien 17 yl amino hexyl 1h pyrrole 2 5 dione tocris
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
663684b U 73122 1 6 17b 3 Methoxyestra 1 3 5 10 Trien 17 Yl Amino Hexyl 1h Pyrrole 2 5 Dione Tocris, supplied by Tocris, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Santa Cruz Biotechnology u73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U73122, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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TargetMol u73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U73122, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Funakoshi ltd 1-[6-[amino]hexyl]-1h-pyrrole-2,5-dione (u-73122)
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
1 [6 [Amino]Hexyl] 1h Pyrrole 2,5 Dione (U 73122), supplied by Funakoshi ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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VASCO DRUG LABORATORIES u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
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FUJIFILM u73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
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Gartner Inc u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U 73122, supplied by Gartner Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ICN Pharmaceuticals 1-6-17ß-3-methoxgestra-1,3,5 (10)-trien-17yl-aminohexyl-1-h-pirrole-2,5-dione (u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
1 6 17ß 3 Methoxgestra 1,3,5 (10) Trien 17yl Aminohexyl 1 H Pirrole 2,5 Dione (U 73122, supplied by ICN Pharmaceuticals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Chemie GmbH u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
U 73122, supplied by Chemie GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Pfizer Inc u-73122
( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor <t>U73122</t> (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .
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Figure 6. CCL2 Promotes Excitatory Synaptic Transmission through CCR2 and PLC Signaling (A and B) The effect of CCL2 application on mEPSC frequency and amplitude in CA1 pyramidal neurons of Ccr2 KO mice, representative traces (A) and summary data (B) (13 cells from 3 mice; Wilcoxon matched-pairs signed rank test). (C and D) The effect of CCL2 application on firing responses to stepwise current injections in CA1 pyramidal neurons of Ccr2 KO mice, representative traces (C) and summary data (D) (12–13 cells from 2 mice; two-way ANOVA, Bonferroni post hoc test). (E–H) mEPSC recordings from Lenti-Ccr2 RNAi infected CA1 pyramidal neurons (E and F), or neighboring uninfected neurons (G and H) before and after CCL2 application, representative traces (E, G) and summary data (F, H) (8–10 cells from 5 mice per condition; Wilcoxon matched-pairs signed rank test). (I–L) mEPSC recordings before and after CCL2 application with 10 mM U73122 in aCSF (I and J) or with 5 mM BAPTA tetracesium in the internal cellular solution (K and L), representative traces (I, K) and summary data (J, L) (9–11 cells from 3 mice; Wilcoxon matched-pairs signed rank test). See also Figure S7.

Journal: Neuron

Article Title: PDGFRβ Cells Rapidly Relay Inflammatory Signal from the Circulatory System to Neurons via Chemokine CCL2.

doi: 10.1016/j.neuron.2018.08.030

Figure Lengend Snippet: Figure 6. CCL2 Promotes Excitatory Synaptic Transmission through CCR2 and PLC Signaling (A and B) The effect of CCL2 application on mEPSC frequency and amplitude in CA1 pyramidal neurons of Ccr2 KO mice, representative traces (A) and summary data (B) (13 cells from 3 mice; Wilcoxon matched-pairs signed rank test). (C and D) The effect of CCL2 application on firing responses to stepwise current injections in CA1 pyramidal neurons of Ccr2 KO mice, representative traces (C) and summary data (D) (12–13 cells from 2 mice; two-way ANOVA, Bonferroni post hoc test). (E–H) mEPSC recordings from Lenti-Ccr2 RNAi infected CA1 pyramidal neurons (E and F), or neighboring uninfected neurons (G and H) before and after CCL2 application, representative traces (E, G) and summary data (F, H) (8–10 cells from 5 mice per condition; Wilcoxon matched-pairs signed rank test). (I–L) mEPSC recordings before and after CCL2 application with 10 mM U73122 in aCSF (I and J) or with 5 mM BAPTA tetracesium in the internal cellular solution (K and L), representative traces (I, K) and summary data (J, L) (9–11 cells from 3 mice; Wilcoxon matched-pairs signed rank test). See also Figure S7.

Article Snippet: DH5a TIANGEN Biotech Cat# CB101 Lentiviruses Genechem, Shanghai, China N/A Chemicals, Peptides, and Recombinant Proteins Lipopolysaccharides (Escherichia coli, serotype O111:B4) Sigma Cat# L2630-25MG Poly(I:C) Tocris Cat# 4287 ODN-1668 InvivoGen Cat# tlrl-1668-5 DAPI Thermo Fisher Scientific Cat# D1306; RRID:AB_2629482 Recombinant Mouse CCL2/JE/MCP-1 R&D Systems Cat# 479-JE-050 BAPTA tetracesium salt Thermo Fisher Scientific Cat# B-1212 NBQX Tocris Cat# 1044 D-APV Tocris Cat# 0106 Gabazine Tocris Cat# 1262 U73122 Tocris Cat# 1268 Fast red Roche Cat# 11496549001 (Continued on next page) Neuron 100, 1–18.e1–e8, October 10, 2018 e1

Techniques: Transmission Assay, Infection

( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor U73122 (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .

Journal: The EMBO Journal

Article Title: Dual interference with host neuropeptide signaling allows parasitoid wasp to hijack host sugar metabolism

doi: 10.1038/s44318-025-00636-5

Figure Lengend Snippet: ( A ) RNAi efficiency of ds PxsNPFR in host larvae (whole body) at 3 L instar ( n = 5–6). ds PxGFP was used as the control. ( B , C ) Relative mRNA levels of PxHK ( B ) and PxGP ( C ) in non-parasitised host larvae (whole body) at 3 L instar upon synthetic sNPF (0.5 ng) or ds PxsNPFR treatment ( n = 6–7). ( D ) Dose-dependent inhibition of forskolin-induced cAMP accumulation in PxsNPFR–expressing HEK293 cells in response to sPxsNPF-1 or sCvsNPF. Cells were treated with 10 μM forskolin and various concentrations of the indicated peptide for 15 min at 37 °C ( n = 3). ( E , F ) Intracellular Ca 2+ mobilisation mediated by sPxsNPF-1 ( E ) and sCvsNPF ( F ) in PxsNPFR–expressing HEK293 cells. ( G , H ) Relative mRNA levels of PxHK in the midgut ( G , n = 5) and PxGP in the fat body ( H , n = 6) of host larvae incubated with the indicated sNPF peptide (20 µM) mixed with G i inhibitor PTX (0.4 µM), PLCβ inhibitor U73122 (10 µM), or DMSO. ( I ) Structural alignment between CvsNPF (red)- PxsNPFR (pink) and PxsNPF-1 (green)-PxsNPFR (light blue) complex. Views from the extracellular (right-upper panel) and cytoplasmic (right-lower panel) sides are shown on the right. The red arrow represents the movement of the TM helix, extracellular loop (ECL) or intracellular loop (ICL) in the CvsNPF-PxsNPFR complex compared to the PxsNPF-1-bound PxsNPFR. ( J ) Structure of the hydrophobic region at the bottom of the binding pocket upon CvsNPF and PxsNPF-1 binding. The PxsNPFR residues (pink and light blue), C-terminal tail of CvsNPF (red) and PxsNPF1 (green) that participate in sNPF binding are presented as sticks. Data are represented as mean ± SEM. * P <0.05, ** P < 0.01, *** P < 0.005, not shown P > 0.05. The exact P values are provided in Appendix Table . ( A ) Two-tailed unpaired Student’s t test; ( B – H ) one-way ANOVA and Tukey’s multiple comparison tests. .

Article Snippet: U73122 , MedChemExpress , HY-13419.

Techniques: Control, Inhibition, Expressing, Incubation, Binding Assay, Two Tailed Test, Comparison