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  • 95
    Thermo Fisher anhydrous dmso
    Inhibition of CAMKK2 or AMPK Activity Blocks the Synaptotoxic Effects of <t>Aβ42</t> Oligomers in Hippocampal Neurons In Vitro (A and B) Representative images of dendritic segments (A) and spine density quantification (B) of 21 DIV hippocampal neurons treated at 20 DIV with the CAMKK2 inhibitor STO-609 (2.5 μM) or <t>DMSO</t> (control) 2 hr prior to Aβ42 oligomer or INV42 application (1 μM for 24 hr). Neurons treated with STO-609 were resistant to spine loss induced by Aβ42 oligomers. (C and D) Representative images of dendritic segments (C) and quantification of spine density (D) of hippocampal neurons at 21 DIV expressing a KD version of CAMKK2 (K194A, transfected at 15 DIV), which significantly reduces the synaptotoxic effects of Aβ42 oligomers. (E and F) Representative images of dendritic segments (E) and quantification of spine density (F) of neurons that express a KD version of AMPKα2 (K45A, transfected at 15 DIV), which blocks the synaptotoxic effects of Aβ42 oligomers. Each condition is quantified from at least three independent experiments (19–151 dendritic segments quantified per condition). (G) Representative traces of mEPSCs recorded from 18 to 19 DIV hippocampal neurons expressing CAMKK2 KD or control vector (transfected at 11 DIV) and treated with Aβ42 oligomers or INV42 (1 μM for 24 hr). (H and I) Inter-mEPSC intervals (H) and mEPSC amplitudes (I) were quantified from 16 to 21 cells per condition (obtained from six independent experiments). Expression of CAMKK2 KD prevented the increase in inter-mEPSC interval induced by Aβ42 oligomers. There was no significant difference in mEPSC amplitude among the different conditions. Histograms represent mean with SEM. Box plots in (B), (D), and (F) represent data distribution (box 25 th –75 th percentiles, bars 10 th –90 th percentiles with central bar representing median). Statistical analysis was performed using ANOVA test followed by Dunnett's posttest in (B) and (F) and Kruskal-Wallis test followed by Dunn's posttest in (D), (H), and (I). *p
    Anhydrous Dmso, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 170 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    dmso  (Mylan)
    92
    Mylan dmso
    Inhibition of CAMKK2 or AMPK Activity Blocks the Synaptotoxic Effects of <t>Aβ42</t> Oligomers in Hippocampal Neurons In Vitro (A and B) Representative images of dendritic segments (A) and spine density quantification (B) of 21 DIV hippocampal neurons treated at 20 DIV with the CAMKK2 inhibitor STO-609 (2.5 μM) or <t>DMSO</t> (control) 2 hr prior to Aβ42 oligomer or INV42 application (1 μM for 24 hr). Neurons treated with STO-609 were resistant to spine loss induced by Aβ42 oligomers. (C and D) Representative images of dendritic segments (C) and quantification of spine density (D) of hippocampal neurons at 21 DIV expressing a KD version of CAMKK2 (K194A, transfected at 15 DIV), which significantly reduces the synaptotoxic effects of Aβ42 oligomers. (E and F) Representative images of dendritic segments (E) and quantification of spine density (F) of neurons that express a KD version of AMPKα2 (K45A, transfected at 15 DIV), which blocks the synaptotoxic effects of Aβ42 oligomers. Each condition is quantified from at least three independent experiments (19–151 dendritic segments quantified per condition). (G) Representative traces of mEPSCs recorded from 18 to 19 DIV hippocampal neurons expressing CAMKK2 KD or control vector (transfected at 11 DIV) and treated with Aβ42 oligomers or INV42 (1 μM for 24 hr). (H and I) Inter-mEPSC intervals (H) and mEPSC amplitudes (I) were quantified from 16 to 21 cells per condition (obtained from six independent experiments). Expression of CAMKK2 KD prevented the increase in inter-mEPSC interval induced by Aβ42 oligomers. There was no significant difference in mEPSC amplitude among the different conditions. Histograms represent mean with SEM. Box plots in (B), (D), and (F) represent data distribution (box 25 th –75 th percentiles, bars 10 th –90 th percentiles with central bar representing median). Statistical analysis was performed using ANOVA test followed by Dunnett's posttest in (B) and (F) and Kruskal-Wallis test followed by Dunn's posttest in (D), (H), and (I). *p
    Dmso, supplied by Mylan, used in various techniques. Bioz Stars score: 92/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher dmso
    One-carbon folate metabolism is a core pathway altered with AML targeting compounds. (A) Intersection of genes down-regulated by five compounds that cause AML death and differentiation: Vitamin D, PMA, ATRA, JQ1, and <t>EPZ004777.</t> Reported is the number of significantly down-regulated genes by each agent <t>(DMSO</t> vs. agent: SNR ≥ 1.5; P ≤ 0.05; FDR[BH] ≤ 0.05). The core 198 genes are significantly down-regulated by each of the five agents (DMSO vs. agent: average SNR across all conditions ≥ 1.5 and SNR ≥ 1.5 in four out of five conditions). P-values calculated using the permutation test implemented in the comparative marker selection procedure, Gene Pattern v3.8.1. (B) Pathway enrichment analysis across KEGG canonical pathways showed eight significantly overlapping pathways. P-values calculated using the hypergeometric test for gene set overlapping analysis. (C) Heat maps showing expression for genes of one-carbon folate pathway across five treatments with differentiation agents. (D) Expression of MTHFD2 across the hematopoietic lineage.
    Dmso, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 17140 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    dmso  (Tocris)
    94
    Tocris dmso
    mDia2 functional inhibition does not affect mDia2 protein expression. A. MDA-MB-231 cells were grown to 60% confluency and treated with vehicle <t>(DMSO)</t> or 40μM <t>SMIFH2</t> for 1-16h prior to lysate collection and Western blotting. B. Densitometry from A. where mDia2 was normalized to GAPDH and compared relative to DMEM. C. MDA-MB-231 cells were treated with 40μM SMIFH2 starting at T0 continuously for 16h during a wound closure experiment. Experiments were repeated thrice.
    Dmso, supplied by Tocris, used in various techniques. Bioz Stars score: 94/100, based on 1134 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Accustandard Inc dmso
    mDia2 functional inhibition does not affect mDia2 protein expression. A. MDA-MB-231 cells were grown to 60% confluency and treated with vehicle <t>(DMSO)</t> or 40μM <t>SMIFH2</t> for 1-16h prior to lysate collection and Western blotting. B. Densitometry from A. where mDia2 was normalized to GAPDH and compared relative to DMEM. C. MDA-MB-231 cells were treated with 40μM SMIFH2 starting at T0 continuously for 16h during a wound closure experiment. Experiments were repeated thrice.
    Dmso, supplied by Accustandard Inc, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Agilent technologies dmso
    mDia2 functional inhibition does not affect mDia2 protein expression. A. MDA-MB-231 cells were grown to 60% confluency and treated with vehicle <t>(DMSO)</t> or 40μM <t>SMIFH2</t> for 1-16h prior to lysate collection and Western blotting. B. Densitometry from A. where mDia2 was normalized to GAPDH and compared relative to DMEM. C. MDA-MB-231 cells were treated with 40μM SMIFH2 starting at T0 continuously for 16h during a wound closure experiment. Experiments were repeated thrice.
    Dmso, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 470 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Amresco dmso
    Effects of <t>rapamycin</t> on vegetative growth, autophagic cell death and pathogenicity of M. oryzae . (A) Plate colonies of the Guy11 strain in CM agar medium. The Guy11 strain was grown on CM medium supplemented with rapamycin (rapa.) at the indicated concentration. Solvent <t>DMSO</t> was seperately added into medium as a control. (B) Diameters of plate colonies recorded every 2 days. (C) Autophagic conidial cell death of the Guy11 strain at 24 hpi of appressorium development on hydrophobic coverslip in the presence of rapamycin. Scale bar: 10 μm. (D) Percentage of Guy11 strain spores containing 3 totally-collapsed conidial cells at 24 hpi (n > 100, triple replications, ** P
    Dmso, supplied by Amresco, used in various techniques. Bioz Stars score: 93/100, based on 499 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Applichem dmso
    Block of β1 integrin and JNK signaling enhances radiation induced DSB by chromatin modification ( A ) Western blot analysis of indicated proteins from whole cell lysates of U343MG and GS-8 cells treated with AIIB2/SP600125 (EC10) or control <t>IgG/DMSO</t> without and with X-ray irradiation (6 Gy). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls according to representative blots. ( B ) Immunofluorescence analysis of nuclei with 53BP1-positive foci after indicated treatments. Scale bar, 10 μm. ( C ) Quantification of the number of DSB per cell at the indicated time points after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation. ( D ) Basal surviving fraction of U343MG cells upon treatment with AIIB2/SP600125 (EC10), LBH589 (EC50) or a combination thereof compared to control treatment (IgG/DMSO). ( E ) Clonogenic radiation survival of U343MG cells treated as described in (H). (C–E) Results are mean +/− SEM ( n = 3, t -test).
    Dmso, supplied by Applichem, used in various techniques. Bioz Stars score: 93/100, based on 440 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Avantor dmso
    Rld-derived cells do not belong to Er81 or Lhx5 CR cell populations. Er81 in situ hybridization (ISH) was performed in CFDA-labeled embryos (E11.5 + 24 h in culture) in several conditions. (A) Wild-type (WT) embryo showing Er81 expression in rostrolateral and rostrodorsal areas. (B,b) Migration of CFDA-labeled cells in a caudo-ventral direction. (C,D,d) Control embryo (cultured in 0.1% <t>DMSO)</t> showing similar pattern of Er81 expression and direction of migration of CFDA labeled cells as in (A,B) . (E,F) Treatment with the FGF inhibitor <t>SU5402</t> showing decreased Er81 expression (E) and a reduction in the caudoventral migration of CFDA + migrating cells (F,f) . (G,H,h) Heterozygous Lhx5 mouse embryo showing patterns of both Er81 expression and CFDA-labeled cell migration similar to WT controls (A,B) . (I) Lhx5 knock-out mouse embryo showing an expansion of Er81 expression in dorsocaudal regions. (J,j) Lhx5 mutants showing a slight decrease in the amount of CFDA-labeled cells, and although migration in the caudoventral direction was present, cells appeared to be disorganized. Arrows in (A,I) show the normal limit of Er81 expression; arrowhead in (I) shows expanded Er81 expression in Lhx5 mutants (I) and asterisk shows some dispersed points of Er81 expression. Scale bar: 200 μm.
    Dmso, supplied by Avantor, used in various techniques. Bioz Stars score: 92/100, based on 416 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Beijing Solarbio Science dmso
    Rld-derived cells do not belong to Er81 or Lhx5 CR cell populations. Er81 in situ hybridization (ISH) was performed in CFDA-labeled embryos (E11.5 + 24 h in culture) in several conditions. (A) Wild-type (WT) embryo showing Er81 expression in rostrolateral and rostrodorsal areas. (B,b) Migration of CFDA-labeled cells in a caudo-ventral direction. (C,D,d) Control embryo (cultured in 0.1% <t>DMSO)</t> showing similar pattern of Er81 expression and direction of migration of CFDA labeled cells as in (A,B) . (E,F) Treatment with the FGF inhibitor <t>SU5402</t> showing decreased Er81 expression (E) and a reduction in the caudoventral migration of CFDA + migrating cells (F,f) . (G,H,h) Heterozygous Lhx5 mouse embryo showing patterns of both Er81 expression and CFDA-labeled cell migration similar to WT controls (A,B) . (I) Lhx5 knock-out mouse embryo showing an expansion of Er81 expression in dorsocaudal regions. (J,j) Lhx5 mutants showing a slight decrease in the amount of CFDA-labeled cells, and although migration in the caudoventral direction was present, cells appeared to be disorganized. Arrows in (A,I) show the normal limit of Er81 expression; arrowhead in (I) shows expanded Er81 expression in Lhx5 mutants (I) and asterisk shows some dispersed points of Er81 expression. Scale bar: 200 μm.
    Dmso, supplied by Beijing Solarbio Science, used in various techniques. Bioz Stars score: 92/100, based on 78 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Beyotime dmso
    NaCl promotion of inflammation relies on the p38/MAPK pathway. A: LPMCs were stimulated with 60 mmol/L NaCl in the presence of 100 ng/mL LPS and 20 ng/mL <t>IFN-γ</t> for 1 h, 6 h, 12 h and 24 h, and the p38 and phosphorylated-p38 proteins were detected by western blot; B: LPMCs were stimulated with different NaCl concentrations in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 24 h and phosphorylated p38 protein was detected by western blot; C: LPMCs were stimulated with different NaCl concentrations in the presence of LPS and IFN-γ, and the mRNA expression of SGK1 was measured by RT-PCR; D: LPMCs were pretreated with 10 μmol/L SB or <t>DMSO</t> for 2 h and were subsequently stimulated with 60 mmol/L NaCl along with 100 ng/mL LPS and 20 ng/mL IFN-γ in the presence of DMSO or 10 μmol/L SB for 24 h and the proteins of p38 and phosphorylated-p38 were detected by western blot. In all the panels, data indicate three separate experiments. a P
    Dmso, supplied by Beyotime, used in various techniques. Bioz Stars score: 93/100, based on 423 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Biotium dmso
    NaCl promotion of inflammation relies on the p38/MAPK pathway. A: LPMCs were stimulated with 60 mmol/L NaCl in the presence of 100 ng/mL LPS and 20 ng/mL <t>IFN-γ</t> for 1 h, 6 h, 12 h and 24 h, and the p38 and phosphorylated-p38 proteins were detected by western blot; B: LPMCs were stimulated with different NaCl concentrations in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 24 h and phosphorylated p38 protein was detected by western blot; C: LPMCs were stimulated with different NaCl concentrations in the presence of LPS and IFN-γ, and the mRNA expression of SGK1 was measured by RT-PCR; D: LPMCs were pretreated with 10 μmol/L SB or <t>DMSO</t> for 2 h and were subsequently stimulated with 60 mmol/L NaCl along with 100 ng/mL LPS and 20 ng/mL IFN-γ in the presence of DMSO or 10 μmol/L SB for 24 h and the proteins of p38 and phosphorylated-p38 were detected by western blot. In all the panels, data indicate three separate experiments. a P
    Dmso, supplied by Biotium, used in various techniques. Bioz Stars score: 92/100, based on 203 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Cambridge Isotope Laboratories dmso
    NaCl promotion of inflammation relies on the p38/MAPK pathway. A: LPMCs were stimulated with 60 mmol/L NaCl in the presence of 100 ng/mL LPS and 20 ng/mL <t>IFN-γ</t> for 1 h, 6 h, 12 h and 24 h, and the p38 and phosphorylated-p38 proteins were detected by western blot; B: LPMCs were stimulated with different NaCl concentrations in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 24 h and phosphorylated p38 protein was detected by western blot; C: LPMCs were stimulated with different NaCl concentrations in the presence of LPS and IFN-γ, and the mRNA expression of SGK1 was measured by RT-PCR; D: LPMCs were pretreated with 10 μmol/L SB or <t>DMSO</t> for 2 h and were subsequently stimulated with 60 mmol/L NaCl along with 100 ng/mL LPS and 20 ng/mL IFN-γ in the presence of DMSO or 10 μmol/L SB for 24 h and the proteins of p38 and phosphorylated-p38 were detected by western blot. In all the panels, data indicate three separate experiments. a P
    Dmso, supplied by Cambridge Isotope Laboratories, used in various techniques. Bioz Stars score: 92/100, based on 74 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Carl Roth GmbH dmso
    Immunofluorescence staining with phalloidin of U2OS cells treated with <t>cytochalasans.</t> ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM <t>DMSO</t> (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.
    Dmso, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 93/100, based on 622 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Chembridge dmso
    Immunofluorescence staining with phalloidin of U2OS cells treated with <t>cytochalasans.</t> ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM <t>DMSO</t> (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.
    Dmso, supplied by Chembridge, used in various techniques. Bioz Stars score: 92/100, based on 114 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Daejung Chemicals dmso
    Immunofluorescence staining with phalloidin of U2OS cells treated with <t>cytochalasans.</t> ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM <t>DMSO</t> (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.
    Dmso, supplied by Daejung Chemicals, used in various techniques. Bioz Stars score: 91/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Edwards Lifesciences Inc dmso
    Immunofluorescence staining with phalloidin of U2OS cells treated with <t>cytochalasans.</t> ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM <t>DMSO</t> (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.
    Dmso, supplied by Edwards Lifesciences Inc, used in various techniques. Bioz Stars score: 92/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Fisher Scientific dmso
    Increased NOTCH activation facilitates EHT. a Schematic diagram of experiments. D4 HE cultured in presence of <t>DAPT</t> for 4 days (D4 + 4) or 1 day (D4 + 1), or <t>DMSO</t> (control). CD144 + endothelial and CD43 + blood cells were analyzed following 4 days of culture. b Flow cytometric analysis demonstrates that NOTCH activation facilitates EHT as evidenced by the decrease in hematopoietic activity when DAPT is added only from D4 to D4 + 1. Representative contour plots from three independent experiments are shown. c Frequencies of endothelial and blood cells in HE cultures treated with DAPT or DMSO (control). Results are mean ± s.e.m. for at least three independent experiments; two-way ANOVA Bonferroni post-hoc test, * p
    Dmso, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 93/100, based on 1380 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    FUJIFILM dmso
    TEM observation results of the Pal-GH gel formulations at different magnifications (×2500 and ×10,000). F5 MTZ (A1,A2), F5 IPM-MTZ (B1,B2), F5 PG-MTZ (C1,C2), F5 <t>DMSO-MTZ</t> (D1,D2), F5 <t>EtOH-MTZ</t> (E1,E2), and F5 TRANS-MTZ (F1,F2).
    Dmso, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 93/100, based on 549 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    GENTAUR dmso
    TEM observation results of the Pal-GH gel formulations at different magnifications (×2500 and ×10,000). F5 MTZ (A1,A2), F5 IPM-MTZ (B1,B2), F5 PG-MTZ (C1,C2), F5 <t>DMSO-MTZ</t> (D1,D2), F5 <t>EtOH-MTZ</t> (E1,E2), and F5 TRANS-MTZ (F1,F2).
    Dmso, supplied by GENTAUR, used in various techniques. Bioz Stars score: 92/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck & Co dmso
    Effects of phosphatase and kinase inhibitors on 86 Rb + uptake. Cells were pre-incubated at 37°C in basic medium for 30 min followed by 30 min in basic medium in the absence (control) or presence of: 1% <t>DMSO</t> (vehicle), 0.25 µM <t>calyculin</t> (A), 1 mM orthovanadate for the entire 60 min (B), 50 µM PP1 (C) or 120 µM genistein (D) before measuring 86 Rb + uptake in the presence of the drugs. Bumetanide-sensitive (B-S) 86 Rb + uptakes are shown as mean ± s . e . m . (n = 3–7, values for HEK-293 cells in B and C are means of triplicates in a single experiment). Using paired, normalised comparisons * signifies P
    Dmso, supplied by Merck & Co, used in various techniques. Bioz Stars score: 92/100, based on 970 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Merck KGaA dmso
    Pharmacological inhibition of ABCG2 modulates the potency of SN-38, but not <t>FL118.</t> A and B , Western blot analysis of ABCG2 protein expression in HCT116 colon cancer cells, drug-resistant HCT116 sub-lines (A) , and H460 and EKVX NSCLC cells (B) . C and E , dose-response curves in the presence and absence of 1 μM Ko143, an ABCG2 inhibitor, after 72 hour treatments in HCT116 sub-lines (C) and NSCLC cell lines (E) . D and F , dose-response curves in the presence and absence of 1 μM Ko143 after 72-hour treatments in HCT116 sub-lines (D) and NSCLC cell lines (F) . Viability for each dose was determined using a ViCELL XR cell viability analyzer and normalized to that of <t>DMSO</t> control. Error bars = SEM, n = 3 independent experiments.
    Dmso, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 94/100, based on 1546 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Inhibition of CAMKK2 or AMPK Activity Blocks the Synaptotoxic Effects of Aβ42 Oligomers in Hippocampal Neurons In Vitro (A and B) Representative images of dendritic segments (A) and spine density quantification (B) of 21 DIV hippocampal neurons treated at 20 DIV with the CAMKK2 inhibitor STO-609 (2.5 μM) or DMSO (control) 2 hr prior to Aβ42 oligomer or INV42 application (1 μM for 24 hr). Neurons treated with STO-609 were resistant to spine loss induced by Aβ42 oligomers. (C and D) Representative images of dendritic segments (C) and quantification of spine density (D) of hippocampal neurons at 21 DIV expressing a KD version of CAMKK2 (K194A, transfected at 15 DIV), which significantly reduces the synaptotoxic effects of Aβ42 oligomers. (E and F) Representative images of dendritic segments (E) and quantification of spine density (F) of neurons that express a KD version of AMPKα2 (K45A, transfected at 15 DIV), which blocks the synaptotoxic effects of Aβ42 oligomers. Each condition is quantified from at least three independent experiments (19–151 dendritic segments quantified per condition). (G) Representative traces of mEPSCs recorded from 18 to 19 DIV hippocampal neurons expressing CAMKK2 KD or control vector (transfected at 11 DIV) and treated with Aβ42 oligomers or INV42 (1 μM for 24 hr). (H and I) Inter-mEPSC intervals (H) and mEPSC amplitudes (I) were quantified from 16 to 21 cells per condition (obtained from six independent experiments). Expression of CAMKK2 KD prevented the increase in inter-mEPSC interval induced by Aβ42 oligomers. There was no significant difference in mEPSC amplitude among the different conditions. Histograms represent mean with SEM. Box plots in (B), (D), and (F) represent data distribution (box 25 th –75 th percentiles, bars 10 th –90 th percentiles with central bar representing median). Statistical analysis was performed using ANOVA test followed by Dunnett's posttest in (B) and (F) and Kruskal-Wallis test followed by Dunn's posttest in (D), (H), and (I). *p

    Journal: Neuron

    Article Title: The CAMKK2-AMPK Kinase Pathway Mediates the Synaptotoxic Effects of A? Oligomers through Tau Phosphorylation

    doi: 10.1016/j.neuron.2013.02.003

    Figure Lengend Snippet: Inhibition of CAMKK2 or AMPK Activity Blocks the Synaptotoxic Effects of Aβ42 Oligomers in Hippocampal Neurons In Vitro (A and B) Representative images of dendritic segments (A) and spine density quantification (B) of 21 DIV hippocampal neurons treated at 20 DIV with the CAMKK2 inhibitor STO-609 (2.5 μM) or DMSO (control) 2 hr prior to Aβ42 oligomer or INV42 application (1 μM for 24 hr). Neurons treated with STO-609 were resistant to spine loss induced by Aβ42 oligomers. (C and D) Representative images of dendritic segments (C) and quantification of spine density (D) of hippocampal neurons at 21 DIV expressing a KD version of CAMKK2 (K194A, transfected at 15 DIV), which significantly reduces the synaptotoxic effects of Aβ42 oligomers. (E and F) Representative images of dendritic segments (E) and quantification of spine density (F) of neurons that express a KD version of AMPKα2 (K45A, transfected at 15 DIV), which blocks the synaptotoxic effects of Aβ42 oligomers. Each condition is quantified from at least three independent experiments (19–151 dendritic segments quantified per condition). (G) Representative traces of mEPSCs recorded from 18 to 19 DIV hippocampal neurons expressing CAMKK2 KD or control vector (transfected at 11 DIV) and treated with Aβ42 oligomers or INV42 (1 μM for 24 hr). (H and I) Inter-mEPSC intervals (H) and mEPSC amplitudes (I) were quantified from 16 to 21 cells per condition (obtained from six independent experiments). Expression of CAMKK2 KD prevented the increase in inter-mEPSC interval induced by Aβ42 oligomers. There was no significant difference in mEPSC amplitude among the different conditions. Histograms represent mean with SEM. Box plots in (B), (D), and (F) represent data distribution (box 25 th –75 th percentiles, bars 10 th –90 th percentiles with central bar representing median). Statistical analysis was performed using ANOVA test followed by Dunnett's posttest in (B) and (F) and Kruskal-Wallis test followed by Dunn's posttest in (D), (H), and (I). *p

    Article Snippet: Aβ42 monomers were dissolved in anhydrous DMSO to make a 5 mM solution, then added to cold phenol red-free F12 medium (Invitrogen) to make a 100 μM solution.

    Techniques: Inhibition, Activity Assay, In Vitro, Expressing, Transfection, Plasmid Preparation

    Characterization of a small compound inhibiting GRASP55 interaction with JAMs. (A) 2D structure, PubChem Common Identifier (CID) and given name of the prioritized hit from the structure-based drug design approach. (B) Representative curves were obtained by HTRF using GST-GRASP55 FL or GST-Erbin with the indicated biotinylated peptides and competed with Graspin (IC 50 = 8.4 μM for GRASP55/JAM-B and 12 μM for GRASP55/JAM-C). (C) Fluorescence profiles presenting results obtained by differential scanning fluorimetry (DSF). Shifts in the melting temperatures of His-GRASP55 PDZ12 incubated with a twelve molar equivalent of ligand or DMSO as control are shown. (D) Golgi density of Gorasp2 +/+ and Gorasp2 -/- MEFs treated or not with Graspin at 50 μM during 48 h. Each circle represents one Golgi. Data are the mean ± s.e.m. of pooled results of three independent experiments (analysis of 30–90 Golgi per condition, per experiment). Student’s unpaired t -test; ***: P

    Journal: PLoS Genetics

    Article Title: Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis

    doi: 10.1371/journal.pgen.1006803

    Figure Lengend Snippet: Characterization of a small compound inhibiting GRASP55 interaction with JAMs. (A) 2D structure, PubChem Common Identifier (CID) and given name of the prioritized hit from the structure-based drug design approach. (B) Representative curves were obtained by HTRF using GST-GRASP55 FL or GST-Erbin with the indicated biotinylated peptides and competed with Graspin (IC 50 = 8.4 μM for GRASP55/JAM-B and 12 μM for GRASP55/JAM-C). (C) Fluorescence profiles presenting results obtained by differential scanning fluorimetry (DSF). Shifts in the melting temperatures of His-GRASP55 PDZ12 incubated with a twelve molar equivalent of ligand or DMSO as control are shown. (D) Golgi density of Gorasp2 +/+ and Gorasp2 -/- MEFs treated or not with Graspin at 50 μM during 48 h. Each circle represents one Golgi. Data are the mean ± s.e.m. of pooled results of three independent experiments (analysis of 30–90 Golgi per condition, per experiment). Student’s unpaired t -test; ***: P

    Article Snippet: Graspin stock solution was dissolved at 10mM concentration in anhydrous DMSO (Cat# D12345, Life Technology).

    Techniques: Fluorescence, Incubation

    One-carbon folate metabolism is a core pathway altered with AML targeting compounds. (A) Intersection of genes down-regulated by five compounds that cause AML death and differentiation: Vitamin D, PMA, ATRA, JQ1, and EPZ004777. Reported is the number of significantly down-regulated genes by each agent (DMSO vs. agent: SNR ≥ 1.5; P ≤ 0.05; FDR[BH] ≤ 0.05). The core 198 genes are significantly down-regulated by each of the five agents (DMSO vs. agent: average SNR across all conditions ≥ 1.5 and SNR ≥ 1.5 in four out of five conditions). P-values calculated using the permutation test implemented in the comparative marker selection procedure, Gene Pattern v3.8.1. (B) Pathway enrichment analysis across KEGG canonical pathways showed eight significantly overlapping pathways. P-values calculated using the hypergeometric test for gene set overlapping analysis. (C) Heat maps showing expression for genes of one-carbon folate pathway across five treatments with differentiation agents. (D) Expression of MTHFD2 across the hematopoietic lineage.

    Journal: The Journal of Experimental Medicine

    Article Title: Targeting MTHFD2 in acute myeloid leukemia

    doi: 10.1084/jem.20151574

    Figure Lengend Snippet: One-carbon folate metabolism is a core pathway altered with AML targeting compounds. (A) Intersection of genes down-regulated by five compounds that cause AML death and differentiation: Vitamin D, PMA, ATRA, JQ1, and EPZ004777. Reported is the number of significantly down-regulated genes by each agent (DMSO vs. agent: SNR ≥ 1.5; P ≤ 0.05; FDR[BH] ≤ 0.05). The core 198 genes are significantly down-regulated by each of the five agents (DMSO vs. agent: average SNR across all conditions ≥ 1.5 and SNR ≥ 1.5 in four out of five conditions). P-values calculated using the permutation test implemented in the comparative marker selection procedure, Gene Pattern v3.8.1. (B) Pathway enrichment analysis across KEGG canonical pathways showed eight significantly overlapping pathways. P-values calculated using the hypergeometric test for gene set overlapping analysis. (C) Heat maps showing expression for genes of one-carbon folate pathway across five treatments with differentiation agents. (D) Expression of MTHFD2 across the hematopoietic lineage.

    Article Snippet: Development of a core differentiation signature for AML A core differentiation signature for AML was created by intersecting the lists of genes down-regulated by five prodifferentiation small molecules in studies for which gene expression data are available at the National Center for Biotechnology Information’s Gene Expression Omnibus (GEO) database: HL-60 cell line treated with 1,25-dihydroxy Vitamin D3 (Vitamin D), PMA, and all-trans retinoic acid versus DMSO ( ; GEO accession no. GSE995 ; Affymetrix HG-U133A); THP-1 cell line treated with JQ1 versus DMSO ( ; GEO accession no. GSE29799 ; Affymetrix HuGene-1.0 ST Array), and MV4-11 and MOLM-13 cell lines treated with the DOT1L inhibitor EPZ004777 versus DMSO ( ; GEO accession no. GSE29828 ; Affymetrix HG-U133_Plus_2).

    Techniques: Marker, Selection, Expressing

    Scanning electron micrographs demonstrate the effect of rhodomyrtone on EMRSA-16 cell morphology. The bacteria were grown in MHB containing 0.5 µg/ml rhodomyrtone (0.5MIC) and incubated for 4 h (A). Untreated control cultures were grown in MHB supplemented with DMSO and incubated for 4 h (B). Scale bars = 2 µm.

    Journal: PLoS ONE

    Article Title: Transcriptome Analysis of Responses to Rhodomyrtone in Methicillin-Resistant Staphylococcus aureus

    doi: 10.1371/journal.pone.0045744

    Figure Lengend Snippet: Scanning electron micrographs demonstrate the effect of rhodomyrtone on EMRSA-16 cell morphology. The bacteria were grown in MHB containing 0.5 µg/ml rhodomyrtone (0.5MIC) and incubated for 4 h (A). Untreated control cultures were grown in MHB supplemented with DMSO and incubated for 4 h (B). Scale bars = 2 µm.

    Article Snippet: Rhodomyrtone was dissolved in 100% dimethyl sulphoxide (DMSO) prior to addition to Mueller Hinton broth (MHB, Oxoid).

    Techniques: Incubation

    mDia2 functional inhibition does not affect mDia2 protein expression. A. MDA-MB-231 cells were grown to 60% confluency and treated with vehicle (DMSO) or 40μM SMIFH2 for 1-16h prior to lysate collection and Western blotting. B. Densitometry from A. where mDia2 was normalized to GAPDH and compared relative to DMEM. C. MDA-MB-231 cells were treated with 40μM SMIFH2 starting at T0 continuously for 16h during a wound closure experiment. Experiments were repeated thrice.

    Journal: PLoS ONE

    Article Title: Carcinoma associated fibroblasts (CAFs) promote breast cancer motility by suppressing mammalian Diaphanous-related formin-2 (mDia2)

    doi: 10.1371/journal.pone.0195278

    Figure Lengend Snippet: mDia2 functional inhibition does not affect mDia2 protein expression. A. MDA-MB-231 cells were grown to 60% confluency and treated with vehicle (DMSO) or 40μM SMIFH2 for 1-16h prior to lysate collection and Western blotting. B. Densitometry from A. where mDia2 was normalized to GAPDH and compared relative to DMEM. C. MDA-MB-231 cells were treated with 40μM SMIFH2 starting at T0 continuously for 16h during a wound closure experiment. Experiments were repeated thrice.

    Article Snippet: SMIFH2 in DMSO (EMD Biochemicals; Tocris Bioscience, Avonmouth) was used at 10–40 μM with 16h for wound closure assays and 8-72h for western blot analysis.

    Techniques: Functional Assay, Inhibition, Expressing, Multiple Displacement Amplification, Western Blot

    Effects of rapamycin on vegetative growth, autophagic cell death and pathogenicity of M. oryzae . (A) Plate colonies of the Guy11 strain in CM agar medium. The Guy11 strain was grown on CM medium supplemented with rapamycin (rapa.) at the indicated concentration. Solvent DMSO was seperately added into medium as a control. (B) Diameters of plate colonies recorded every 2 days. (C) Autophagic conidial cell death of the Guy11 strain at 24 hpi of appressorium development on hydrophobic coverslip in the presence of rapamycin. Scale bar: 10 μm. (D) Percentage of Guy11 strain spores containing 3 totally-collapsed conidial cells at 24 hpi (n > 100, triple replications, ** P

    Journal: Autophagy

    Article Title: MoSnt2-dependent deacetylation of histone H3 mediates MoTor-dependent autophagy and plant infection by the rice blast fungus Magnaporthe oryzae

    doi: 10.1080/15548627.2018.1458171

    Figure Lengend Snippet: Effects of rapamycin on vegetative growth, autophagic cell death and pathogenicity of M. oryzae . (A) Plate colonies of the Guy11 strain in CM agar medium. The Guy11 strain was grown on CM medium supplemented with rapamycin (rapa.) at the indicated concentration. Solvent DMSO was seperately added into medium as a control. (B) Diameters of plate colonies recorded every 2 days. (C) Autophagic conidial cell death of the Guy11 strain at 24 hpi of appressorium development on hydrophobic coverslip in the presence of rapamycin. Scale bar: 10 μm. (D) Percentage of Guy11 strain spores containing 3 totally-collapsed conidial cells at 24 hpi (n > 100, triple replications, ** P

    Article Snippet: A rapamycin (Selleckchem, S1039) stock solution was prepared in DMSO (Amresco, 0231) at a concentration of 10 mg/ml.

    Techniques: Concentration Assay

    Block of β1 integrin and JNK signaling enhances radiation induced DSB by chromatin modification ( A ) Western blot analysis of indicated proteins from whole cell lysates of U343MG and GS-8 cells treated with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls according to representative blots. ( B ) Immunofluorescence analysis of nuclei with 53BP1-positive foci after indicated treatments. Scale bar, 10 μm. ( C ) Quantification of the number of DSB per cell at the indicated time points after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation. ( D ) Basal surviving fraction of U343MG cells upon treatment with AIIB2/SP600125 (EC10), LBH589 (EC50) or a combination thereof compared to control treatment (IgG/DMSO). ( E ) Clonogenic radiation survival of U343MG cells treated as described in (H). (C–E) Results are mean +/− SEM ( n = 3, t -test).

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Block of β1 integrin and JNK signaling enhances radiation induced DSB by chromatin modification ( A ) Western blot analysis of indicated proteins from whole cell lysates of U343MG and GS-8 cells treated with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls according to representative blots. ( B ) Immunofluorescence analysis of nuclei with 53BP1-positive foci after indicated treatments. Scale bar, 10 μm. ( C ) Quantification of the number of DSB per cell at the indicated time points after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation. ( D ) Basal surviving fraction of U343MG cells upon treatment with AIIB2/SP600125 (EC10), LBH589 (EC50) or a combination thereof compared to control treatment (IgG/DMSO). ( E ) Clonogenic radiation survival of U343MG cells treated as described in (H). (C–E) Results are mean +/− SEM ( n = 3, t -test).

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Blocking Assay, Modification, Western Blot, Irradiation, Immunofluorescence

    Combined β1 integrin/JNK targeting blocks GBM cell invasion ( A ) Work flow of 3D invasion assays. ( B ) Representative images of indicated GBM cells invading into 3D type I collagen 72 h after treatment with AIIB2/SP600125 (EC50) or control IgG/DMSO. Scale bar, 50 μm. ( C ) Invasion distance of indicated treated GBM cell populations. Results are mean +/− SEM ( n = 3, t -test).

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Combined β1 integrin/JNK targeting blocks GBM cell invasion ( A ) Work flow of 3D invasion assays. ( B ) Representative images of indicated GBM cells invading into 3D type I collagen 72 h after treatment with AIIB2/SP600125 (EC50) or control IgG/DMSO. Scale bar, 50 μm. ( C ) Invasion distance of indicated treated GBM cell populations. Results are mean +/− SEM ( n = 3, t -test).

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Flow Cytometry

    Dual inhibition of β1 integrin and JNK delays tumor growth and prolongs survival in combination with radiochemotherapy ( A ) Treatment scheme of mice bearing tumors of GS-8_GFP/fLuc stem-like cells. ( B ) Left panel shows representative image of a mouse brain with GS-8_GFP/fLuc tumor. Scale bar, 2 mm. Region 1 and 2 corresponding to middle and right panel magnifications show invading tumor cells (IC) and blood vessel (BV) of GS-8_GFP/fLuc tumors, respectively. Scale bar, 100 μm. ( C ) Representative images from GS-8_GFP/fLuc tumors showing β1 integrin (green), phospho-JNK (T183/Y185) (red) or merge with nuclei (DAPI, blue). Scale bar, 100 μm. ( D ) Gadolinium-enhanced (Gd) T1-weighted magnetic resonance images (MRI) from mice bearing GS-8_GFP/fLuc tumors 24 days after transplantation and β1 integrin/JNK inhibition without or in combination with radiochemotherapy (RCT). Dashed lines delineate tumors. Lower images show luminescence analyses of representative GS-8_GFP/fLuc tumors 24 days after transplantation and indicated treatment. ( E ) GS-8_GFP/fLuc tumor growth time to 100 fold radiance after indicated treatment. Data are mean +/− SEM (6 - 8 mice per group, one-way ANOVA). ( F ) Survival of GS-8_GFP/fLuc mice treated as indicated. Kaplan Meier analysis includes 6 mice IgG/DMSO, 8 mice AIIB2/SP600125, 6 mice IgG/DMSO+RCT, 6 mice AIIB2/SP600125+RCT (two-sided log rank test, p

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Dual inhibition of β1 integrin and JNK delays tumor growth and prolongs survival in combination with radiochemotherapy ( A ) Treatment scheme of mice bearing tumors of GS-8_GFP/fLuc stem-like cells. ( B ) Left panel shows representative image of a mouse brain with GS-8_GFP/fLuc tumor. Scale bar, 2 mm. Region 1 and 2 corresponding to middle and right panel magnifications show invading tumor cells (IC) and blood vessel (BV) of GS-8_GFP/fLuc tumors, respectively. Scale bar, 100 μm. ( C ) Representative images from GS-8_GFP/fLuc tumors showing β1 integrin (green), phospho-JNK (T183/Y185) (red) or merge with nuclei (DAPI, blue). Scale bar, 100 μm. ( D ) Gadolinium-enhanced (Gd) T1-weighted magnetic resonance images (MRI) from mice bearing GS-8_GFP/fLuc tumors 24 days after transplantation and β1 integrin/JNK inhibition without or in combination with radiochemotherapy (RCT). Dashed lines delineate tumors. Lower images show luminescence analyses of representative GS-8_GFP/fLuc tumors 24 days after transplantation and indicated treatment. ( E ) GS-8_GFP/fLuc tumor growth time to 100 fold radiance after indicated treatment. Data are mean +/− SEM (6 - 8 mice per group, one-way ANOVA). ( F ) Survival of GS-8_GFP/fLuc mice treated as indicated. Kaplan Meier analysis includes 6 mice IgG/DMSO, 8 mice AIIB2/SP600125, 6 mice IgG/DMSO+RCT, 6 mice AIIB2/SP600125+RCT (two-sided log rank test, p

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Inhibition, Mouse Assay, Magnetic Resonance Imaging, Transplantation Assay

    β1 integrin/JNK co-targeting interferes with cell cycle regulatory networks ( A ) Hierarchical clustering of altered phosphorylation sites (30% decrease, 50% increase, fold change) from phosphoproteome analysis of U343MG cells 1 h after indicated treatment with AIIB2, JNKi or AIIB2/JNKi (EC10) normalized to controls (percentage of phosphorylation site changes is shown on the right). ( B ) Percentage of phospho-sites showing 30% decreased and 50% increased phosphorylation upon indicated treatment among the 606 phosphorylations sited investigated in the phosphoproteome analysis. ( C ) Venn diagram analysis of altered phosphosites from (A). ( D ) Functional classification of altered proteins after treatment with AIIB2/SP600125 (EC10) in comparison to the IgG/DMSO controls. Enrichment of genes in signaling pathway: # p

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: β1 integrin/JNK co-targeting interferes with cell cycle regulatory networks ( A ) Hierarchical clustering of altered phosphorylation sites (30% decrease, 50% increase, fold change) from phosphoproteome analysis of U343MG cells 1 h after indicated treatment with AIIB2, JNKi or AIIB2/JNKi (EC10) normalized to controls (percentage of phosphorylation site changes is shown on the right). ( B ) Percentage of phospho-sites showing 30% decreased and 50% increased phosphorylation upon indicated treatment among the 606 phosphorylations sited investigated in the phosphoproteome analysis. ( C ) Venn diagram analysis of altered phosphosites from (A). ( D ) Functional classification of altered proteins after treatment with AIIB2/SP600125 (EC10) in comparison to the IgG/DMSO controls. Enrichment of genes in signaling pathway: # p

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Functional Assay

    Inhibition of β1 integrin and JNK enhances G2/M cell cycle arrest ( A ) Western blot analysis of indicated proteins and phosphorylation sites from whole cell lysates of U343MG cells treated with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Representative blots are shown. ( B ) Quantification of ATM (S1981) and Cdc25A (S216) phosphorylation and p53 expression shown in (A). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls. Results are mean +/− SEM ( n = 3, t -test). ( C ) Flow cytometric cell cycle analysis (BrdU, propidium iodide) of U343MG cells 24 h after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Representative dot blots are shown. ( D ) Quantification of flow cytometric analysis from (C) showing distribution of treated GBM cells into G1/G0, S and G2/M phase of the cell cycle. Results are mean +/− SEM ( n = 3, t -test).

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Inhibition of β1 integrin and JNK enhances G2/M cell cycle arrest ( A ) Western blot analysis of indicated proteins and phosphorylation sites from whole cell lysates of U343MG cells treated with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Representative blots are shown. ( B ) Quantification of ATM (S1981) and Cdc25A (S216) phosphorylation and p53 expression shown in (A). Fold changes are calculated by normalization to β-actin and IgG/DMSO controls. Results are mean +/− SEM ( n = 3, t -test). ( C ) Flow cytometric cell cycle analysis (BrdU, propidium iodide) of U343MG cells 24 h after treatment with AIIB2/SP600125 (EC10) or control IgG/DMSO without and with X-ray irradiation (6 Gy). Representative dot blots are shown. ( D ) Quantification of flow cytometric analysis from (C) showing distribution of treated GBM cells into G1/G0, S and G2/M phase of the cell cycle. Results are mean +/− SEM ( n = 3, t -test).

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Inhibition, Western Blot, Irradiation, Expressing, Flow Cytometry, Cell Cycle Assay

    Co-targeting of β1 integrin and JNK sensitizes GBM cells to radiotherapy ( A ) Workflow of GBM sphere formation and clonogenic survival assay. ( B ) Relative sphere formation and basal surviving fraction of GBM stem-like cells (GS-8), patient-derived GBM cultures (DK32, DK41) and GBM cell lines (U343MG, DD-T4) upon treatment with AIIB2/SP600125 (EC10, EC50) or controls (IgG, DMSO). ( C ) Relative sphere formation and clonogenic survival upon treatment with AIIB2/SP600125 (EC10, EC50) and X-ray irradiation (2, 4, 6 Gy) (controls are IgG and DMSO). (B, C) Results are mean +/− SEM ( n = 3–4, t -test). ( D ) Western blot analysis of β1 integrin, phospho-cJun (S63), cJun and β-actin of whole cell lysates from indicated GBM cells treated as indicated with AIIB2 (10 μg/ml), SP600125 (EC10), IgG control (10 μg/ml) and DMSO. Fold change is calculated by normalization to β-actin and IgG/DMSO controls according to representative blots.

    Journal: Oncotarget

    Article Title: Adhesion- and stress-related adaptation of glioma radiochemoresistance is circumvented by β1 integrin/JNK co-targeting

    doi: 10.18632/oncotarget.17480

    Figure Lengend Snippet: Co-targeting of β1 integrin and JNK sensitizes GBM cells to radiotherapy ( A ) Workflow of GBM sphere formation and clonogenic survival assay. ( B ) Relative sphere formation and basal surviving fraction of GBM stem-like cells (GS-8), patient-derived GBM cultures (DK32, DK41) and GBM cell lines (U343MG, DD-T4) upon treatment with AIIB2/SP600125 (EC10, EC50) or controls (IgG, DMSO). ( C ) Relative sphere formation and clonogenic survival upon treatment with AIIB2/SP600125 (EC10, EC50) and X-ray irradiation (2, 4, 6 Gy) (controls are IgG and DMSO). (B, C) Results are mean +/− SEM ( n = 3–4, t -test). ( D ) Western blot analysis of β1 integrin, phospho-cJun (S63), cJun and β-actin of whole cell lysates from indicated GBM cells treated as indicated with AIIB2 (10 μg/ml), SP600125 (EC10), IgG control (10 μg/ml) and DMSO. Fold change is calculated by normalization to β-actin and IgG/DMSO controls according to representative blots.

    Article Snippet: Non-specific IgG isotype antibodies (10 μg/ml) or DMSO (equal amount as inhibitors, < 0.1 % v/v) (AppliChem) were used as control.

    Techniques: Clonogenic Cell Survival Assay, Derivative Assay, Irradiation, Western Blot

    Rld-derived cells do not belong to Er81 or Lhx5 CR cell populations. Er81 in situ hybridization (ISH) was performed in CFDA-labeled embryos (E11.5 + 24 h in culture) in several conditions. (A) Wild-type (WT) embryo showing Er81 expression in rostrolateral and rostrodorsal areas. (B,b) Migration of CFDA-labeled cells in a caudo-ventral direction. (C,D,d) Control embryo (cultured in 0.1% DMSO) showing similar pattern of Er81 expression and direction of migration of CFDA labeled cells as in (A,B) . (E,F) Treatment with the FGF inhibitor SU5402 showing decreased Er81 expression (E) and a reduction in the caudoventral migration of CFDA + migrating cells (F,f) . (G,H,h) Heterozygous Lhx5 mouse embryo showing patterns of both Er81 expression and CFDA-labeled cell migration similar to WT controls (A,B) . (I) Lhx5 knock-out mouse embryo showing an expansion of Er81 expression in dorsocaudal regions. (J,j) Lhx5 mutants showing a slight decrease in the amount of CFDA-labeled cells, and although migration in the caudoventral direction was present, cells appeared to be disorganized. Arrows in (A,I) show the normal limit of Er81 expression; arrowhead in (I) shows expanded Er81 expression in Lhx5 mutants (I) and asterisk shows some dispersed points of Er81 expression. Scale bar: 200 μm.

    Journal: Frontiers in Neuroanatomy

    Article Title: Origin and Migration of Olfactory Cajal-Retzius Cells

    doi: 10.3389/fnana.2017.00097

    Figure Lengend Snippet: Rld-derived cells do not belong to Er81 or Lhx5 CR cell populations. Er81 in situ hybridization (ISH) was performed in CFDA-labeled embryos (E11.5 + 24 h in culture) in several conditions. (A) Wild-type (WT) embryo showing Er81 expression in rostrolateral and rostrodorsal areas. (B,b) Migration of CFDA-labeled cells in a caudo-ventral direction. (C,D,d) Control embryo (cultured in 0.1% DMSO) showing similar pattern of Er81 expression and direction of migration of CFDA labeled cells as in (A,B) . (E,F) Treatment with the FGF inhibitor SU5402 showing decreased Er81 expression (E) and a reduction in the caudoventral migration of CFDA + migrating cells (F,f) . (G,H,h) Heterozygous Lhx5 mouse embryo showing patterns of both Er81 expression and CFDA-labeled cell migration similar to WT controls (A,B) . (I) Lhx5 knock-out mouse embryo showing an expansion of Er81 expression in dorsocaudal regions. (J,j) Lhx5 mutants showing a slight decrease in the amount of CFDA-labeled cells, and although migration in the caudoventral direction was present, cells appeared to be disorganized. Arrows in (A,I) show the normal limit of Er81 expression; arrowhead in (I) shows expanded Er81 expression in Lhx5 mutants (I) and asterisk shows some dispersed points of Er81 expression. Scale bar: 200 μm.

    Article Snippet: Serum was replaced every 12 h. For FGF inhibition experiments, serum was supplemented with 10 μM of SU5402 (572630, Calbiochem, Billerica, MA, USA) dissolved in DMSO (9224–01 J.T.Baker Center Valley, PA, USA) with an equivalent volume of DMSO used in control cultures.

    Techniques: Derivative Assay, In Situ Hybridization, Labeling, Expressing, Migration, Cell Culture, Knock-Out

    NaCl promotion of inflammation relies on the p38/MAPK pathway. A: LPMCs were stimulated with 60 mmol/L NaCl in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 1 h, 6 h, 12 h and 24 h, and the p38 and phosphorylated-p38 proteins were detected by western blot; B: LPMCs were stimulated with different NaCl concentrations in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 24 h and phosphorylated p38 protein was detected by western blot; C: LPMCs were stimulated with different NaCl concentrations in the presence of LPS and IFN-γ, and the mRNA expression of SGK1 was measured by RT-PCR; D: LPMCs were pretreated with 10 μmol/L SB or DMSO for 2 h and were subsequently stimulated with 60 mmol/L NaCl along with 100 ng/mL LPS and 20 ng/mL IFN-γ in the presence of DMSO or 10 μmol/L SB for 24 h and the proteins of p38 and phosphorylated-p38 were detected by western blot. In all the panels, data indicate three separate experiments. a P

    Journal: World Journal of Gastroenterology

    Article Title: Sodium chloride exacerbates dextran sulfate sodium-induced colitis by tuning proinflammatory and antiinflammatory lamina propria mononuclear cells through p38/MAPK pathway in mice

    doi: 10.3748/wjg.v24.i16.1779

    Figure Lengend Snippet: NaCl promotion of inflammation relies on the p38/MAPK pathway. A: LPMCs were stimulated with 60 mmol/L NaCl in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 1 h, 6 h, 12 h and 24 h, and the p38 and phosphorylated-p38 proteins were detected by western blot; B: LPMCs were stimulated with different NaCl concentrations in the presence of 100 ng/mL LPS and 20 ng/mL IFN-γ for 24 h and phosphorylated p38 protein was detected by western blot; C: LPMCs were stimulated with different NaCl concentrations in the presence of LPS and IFN-γ, and the mRNA expression of SGK1 was measured by RT-PCR; D: LPMCs were pretreated with 10 μmol/L SB or DMSO for 2 h and were subsequently stimulated with 60 mmol/L NaCl along with 100 ng/mL LPS and 20 ng/mL IFN-γ in the presence of DMSO or 10 μmol/L SB for 24 h and the proteins of p38 and phosphorylated-p38 were detected by western blot. In all the panels, data indicate three separate experiments. a P

    Article Snippet: Isolated LPMCs were cultured at a concentration of 5 × 106 cells/mL for 24 h, after which the culture supernatants were collected and cytokine levels were analyzed by enzyme-linked immunosorbent assay (ELISA) or were stimulated using different NaCl concentrations (5, 10, 20, 40, 60 or 80 mmol/L) in the presence of 100 ng/mL LPS (Sigma, United States) and 20 ng/mL IFN-γ (Sigma) with SB20358 (p38 inhibitor) or DMSO (ST038; Beyotime) for 24 h. The cells were detected by western blot (WB) or real time-PCR (RT-PCR).

    Techniques: Western Blot, Expressing, Reverse Transcription Polymerase Chain Reaction

    Immunofluorescence staining with phalloidin of U2OS cells treated with cytochalasans. ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM DMSO (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.

    Journal: Biomolecules

    Article Title: The Effect of Cytochalasans on the Actin Cytoskeleton of Eukaryotic Cells and Preliminary Structure–Activity Relationships

    doi: 10.3390/biom9020073

    Figure Lengend Snippet: Immunofluorescence staining with phalloidin of U2OS cells treated with cytochalasans. ( A ) Treated with 1 µM cytochalasin H ( 8 ). ( B ) Treated with 5 µM cytochalasin H. ( C ) Treated with 1 µM cytochalasin B ( 4 ). ( D ) Treated with 5 µM cytochalasin B. ( E ) treated with 1 µM chaetoglobosin D ( 25 ). ( F ) Treated with 5 µM chaetoglobosin D. ( G ) Treated with 5 µM DMSO (negative control). ( H ) Washout after treatment with 5 µM cytochalasin H.

    Article Snippet: For treatment of the cells, the cytochalasans were dissolved in DMSO (Carl Roth GmbH, Karlsruhe, Germany).

    Techniques: Immunofluorescence, Staining, Negative Control

    Increased NOTCH activation facilitates EHT. a Schematic diagram of experiments. D4 HE cultured in presence of DAPT for 4 days (D4 + 4) or 1 day (D4 + 1), or DMSO (control). CD144 + endothelial and CD43 + blood cells were analyzed following 4 days of culture. b Flow cytometric analysis demonstrates that NOTCH activation facilitates EHT as evidenced by the decrease in hematopoietic activity when DAPT is added only from D4 to D4 + 1. Representative contour plots from three independent experiments are shown. c Frequencies of endothelial and blood cells in HE cultures treated with DAPT or DMSO (control). Results are mean ± s.e.m. for at least three independent experiments; two-way ANOVA Bonferroni post-hoc test, * p

    Journal: Nature Communications

    Article Title: NOTCH signaling specifies arterial-type definitive hemogenic endothelium from human pluripotent stem cells

    doi: 10.1038/s41467-018-04134-7

    Figure Lengend Snippet: Increased NOTCH activation facilitates EHT. a Schematic diagram of experiments. D4 HE cultured in presence of DAPT for 4 days (D4 + 4) or 1 day (D4 + 1), or DMSO (control). CD144 + endothelial and CD43 + blood cells were analyzed following 4 days of culture. b Flow cytometric analysis demonstrates that NOTCH activation facilitates EHT as evidenced by the decrease in hematopoietic activity when DAPT is added only from D4 to D4 + 1. Representative contour plots from three independent experiments are shown. c Frequencies of endothelial and blood cells in HE cultures treated with DAPT or DMSO (control). Results are mean ± s.e.m. for at least three independent experiments; two-way ANOVA Bonferroni post-hoc test, * p

    Article Snippet: Purified CD31+ HE were then plated at a density of 20,000 to 30,000 cells/cm2 on collagen IV-coated plates (1 μg/cm2 ) that were either co-coated with IgG-Fc fragments or human DLL1-Fc (made in-house), in IF9S media supplemented with FGF2, VEGF, EGF, IGF-I, IGF-II, TPO, IL-6 (50 ng ml−1 ), SCF (20 ng ml−1 ), IL-3, FLT3L (10 ng ml−1 , Peprotech), and ROCK inhibitor (5 μM, Cayman Chemicals), and where specified, DMSO (1:1000, Fisher Scientific) or DAPT (10 μM, Cayman Chemicals), and cultured in normoxia (20% O2 , 5% CO2 ).

    Techniques: Activation Assay, Cell Culture, Flow Cytometry, Activity Assay

    TEM observation results of the Pal-GH gel formulations at different magnifications (×2500 and ×10,000). F5 MTZ (A1,A2), F5 IPM-MTZ (B1,B2), F5 PG-MTZ (C1,C2), F5 DMSO-MTZ (D1,D2), F5 EtOH-MTZ (E1,E2), and F5 TRANS-MTZ (F1,F2).

    Journal: Pharmaceutics

    Article Title: Combined Use of N-Palmitoyl-Glycine-Histidine Gel and Several Penetration Enhancers on the Skin Permeation and Concentration of Metronidazole

    doi: 10.3390/pharmaceutics10040163

    Figure Lengend Snippet: TEM observation results of the Pal-GH gel formulations at different magnifications (×2500 and ×10,000). F5 MTZ (A1,A2), F5 IPM-MTZ (B1,B2), F5 PG-MTZ (C1,C2), F5 DMSO-MTZ (D1,D2), F5 EtOH-MTZ (E1,E2), and F5 TRANS-MTZ (F1,F2).

    Article Snippet: EtOH, Transcutol® , DMSO, and IPM were purchased from Wako Pure Chemicals Industries, Ltd. (Osaka, Japan).

    Techniques: Transmission Electron Microscopy

    Effects of phosphatase and kinase inhibitors on 86 Rb + uptake. Cells were pre-incubated at 37°C in basic medium for 30 min followed by 30 min in basic medium in the absence (control) or presence of: 1% DMSO (vehicle), 0.25 µM calyculin (A), 1 mM orthovanadate for the entire 60 min (B), 50 µM PP1 (C) or 120 µM genistein (D) before measuring 86 Rb + uptake in the presence of the drugs. Bumetanide-sensitive (B-S) 86 Rb + uptakes are shown as mean ± s . e . m . (n = 3–7, values for HEK-293 cells in B and C are means of triplicates in a single experiment). Using paired, normalised comparisons * signifies P

    Journal: PLoS ONE

    Article Title: Phosphorylation and Transport in the Na-K-2Cl Cotransporters, NKCC1 and NKCC2A, Compared in HEK-293 Cells

    doi: 10.1371/journal.pone.0017992

    Figure Lengend Snippet: Effects of phosphatase and kinase inhibitors on 86 Rb + uptake. Cells were pre-incubated at 37°C in basic medium for 30 min followed by 30 min in basic medium in the absence (control) or presence of: 1% DMSO (vehicle), 0.25 µM calyculin (A), 1 mM orthovanadate for the entire 60 min (B), 50 µM PP1 (C) or 120 µM genistein (D) before measuring 86 Rb + uptake in the presence of the drugs. Bumetanide-sensitive (B-S) 86 Rb + uptakes are shown as mean ± s . e . m . (n = 3–7, values for HEK-293 cells in B and C are means of triplicates in a single experiment). Using paired, normalised comparisons * signifies P

    Article Snippet: 4-amino-5-(4-methylphenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP1, Enzo Life Sciences, Farmingdale, NY), genistein (Sigma-Aldrich), calyculin A (Enzo Life Sciences) were dissolved in DMSO (Merck) whereas ouabain (Sigma-Aldrich) and bumetanide (Leo Laboratories, Ballerup, Denmark) were dissolved in water.

    Techniques: Incubation

    Pharmacological inhibition of ABCG2 modulates the potency of SN-38, but not FL118. A and B , Western blot analysis of ABCG2 protein expression in HCT116 colon cancer cells, drug-resistant HCT116 sub-lines (A) , and H460 and EKVX NSCLC cells (B) . C and E , dose-response curves in the presence and absence of 1 μM Ko143, an ABCG2 inhibitor, after 72 hour treatments in HCT116 sub-lines (C) and NSCLC cell lines (E) . D and F , dose-response curves in the presence and absence of 1 μM Ko143 after 72-hour treatments in HCT116 sub-lines (D) and NSCLC cell lines (F) . Viability for each dose was determined using a ViCELL XR cell viability analyzer and normalized to that of DMSO control. Error bars = SEM, n = 3 independent experiments.

    Journal: Molecular Cancer

    Article Title: FL118, a novel camptothecin derivative, is insensitive to ABCG2 expression and shows improved efficacy in comparison with irinotecan in colon and lung cancer models with ABCG2-induced resistance

    doi: 10.1186/s12943-015-0362-9

    Figure Lengend Snippet: Pharmacological inhibition of ABCG2 modulates the potency of SN-38, but not FL118. A and B , Western blot analysis of ABCG2 protein expression in HCT116 colon cancer cells, drug-resistant HCT116 sub-lines (A) , and H460 and EKVX NSCLC cells (B) . C and E , dose-response curves in the presence and absence of 1 μM Ko143, an ABCG2 inhibitor, after 72 hour treatments in HCT116 sub-lines (C) and NSCLC cell lines (E) . D and F , dose-response curves in the presence and absence of 1 μM Ko143 after 72-hour treatments in HCT116 sub-lines (D) and NSCLC cell lines (F) . Viability for each dose was determined using a ViCELL XR cell viability analyzer and normalized to that of DMSO control. Error bars = SEM, n = 3 independent experiments.

    Article Snippet: Drug resource and preparation Topotecan (Selleckchem Chemicals, Houston, TX), FL118 (in house), and FL118 analogues (RTI International) were prepared as stocks at 1 mM in DMSO (Merck KGaA, Darmstadt, Germany).

    Techniques: Inhibition, Western Blot, Expressing