dimethylsulfoxide dmso Search Results


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  • dmso  (ATCC)
    99
    ATCC dmso
    Caspase activity is not required for T3D-induced cell death. (A) <t>ATCC</t> L929 cells were adsorbed with PBS (mock) or T3D at an MOI of 10 PFU/cell. After incubation at 37°C for 48 h in the presence of <t>DMSO</t> or 25 µM caspase-8 (Z-IETD-FMK), caspase-9 (Z-LEHD-FMK), or pan-caspase [Z-VAD(OMe)-FMK] inhibitor, cells were stained with AOEB. The results are expressed as the mean percentages of cells undergoing cell death for three independent experiments. Error bars indicate SD. (B) ATCC L929 cells were adsorbed with PBS (mock) or T3D at the MOI of 10 PFU/cell. After incubation at 37°C for 24 h in the presence of DMSO or 25 µM concentrations of each caspase inhibitor, caspase-3/7 activity in cell lysates was determined. Results are expressed as the mean ratios of caspase-3/7 activity from infected cell lysates to that from equivalently treated mock-infected cells for triplicate samples. We note that the DMSO-treated cells are the same as those used in Fig. 2 . Error bars indicate SD. *, P value of
    Dmso, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 619 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher pluronic f 127
    Intracellular Ca 2+  in  Leishmania  increases in response to allicin stress. Leishmania  promastigotes were treated with allicin (15–120 μM) for 20 min. Calcium levels were determined by Fluo 4AM preloading of cells (60 min) in loading buffer with 0.02% Pluronic F-127. Maximal fluorescence was obtained with cells treated with 0.5% Triton X-100 and minimal after chelation with 8 mM EGTA. Data presented corresponds to the average increase of normalized fluorescence intensity of two independent experiments in triplicate (mean ± S.D.). Asterisks represent significant differences compared to untreated control promastigotes (*:  p
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    Millipore dimethyl sulfoxide dmso
    Suppressing Smad7 protein expression with Notch inhibitor N-(N-[3,5-difluorophenacetyl]-l-alanyl)-S-phenylglycine t-butyl ester facilitates epithelial–mesenchymal transition and growth arrest induced by transforming growth factor-beta. A : Western blot analysis of Smad 2/3 phosphorylation. Left planes: Transforming growth factor-beta (TGFβ1) time-dependently induces Smad2/3 phosphorylation in P1 cells. Right planes: P1 cells were treated with 10 ng/ml TGFβ1 for 30 and 40 min as positive control. P0 and P1 cells were pretreated with 10 µM N-(N-[3,5-difluorophenacetyl]-l-alanyl)-S-phenylglycine t-butyl ester <t>(DAPT)</t> or dimethyl sulfoxide <t>(DMSO)</t> vehicle for 48 h and then stimulated with TGFβ1 for 30 and 40 min, respectively. Cells were harvested and subjected to western blot analysis with phosphospecific antibodies of Smad2 and Smad3. The total protein levels of Smad2 and Smad3 were estimated by reprobing the membranes with total Smad2 and Smad3 antibody shown in the panels below. B : P0 LSCs pretreated with DAPT facilitates mesenchymal marker expression induced by TGFβ1. Representative blots (left panels) and densitometric analysis with standard deviation (SD; right columns) of three independent experiments are shown. *p
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    99
    Millipore dmso
    Artificial diet assays with Myzus persicae to establish the specificity of aphid responses to NAM. Aphid feeding behavior, survival, and fecundity were observed at: ( a ) 6 hours, ( b ) 12 hours, ( c ) 24 hours, and ( d ) 48 hours in response to feeding on artificial diets without supplementation (Control) or supplemented with 10 mM NAM, 10 mM nicotinic acid (NA), 1.38 mM <t>pymetrozine</t> insecticide solubilized in 0.7% <t>DMSO,</t> or 0.7% DMSO alone. The average number of aphids in each behavioral response group were analyzed by one-way ANOVA. Means for each behavioral response that do not share a letter are significantly different at the 95% confidence level.
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    Millipore dimethyl sulphoxide dmso
    Inhibitory effect of <t>17β-estradiol</t> ( E ), genistein ( G ) and daidzein ( D ) on post-injury neointima development in concentrations of 20/30/40 μM, compared to endothelium balloon denuded ( BD ) controls ( C ) (mean ± SD). The medium of all groups contained 1 % isopropanol ( 1 % iso ) and 1 % <t>DMSO</t> . Compared with controls 17β-estradiol, genistein, and daidzein (*) reduced neointima formation significantly (p = 0.05) in a concentration dependent manner. Data from Finking et al., 2000 [ 25 ].
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    93
    Thermo Fisher dmso
    <t>TGF-β</t> signaling impairs demethylation of H3K27me3 and recruitment of GATA4 to target genes A) Global ChIP-seq density heatmap of H3K27me3 in Day 7 GHMT2m-reprogrammed cells with indicated TGF-β pathway manipulation and undifferentiated MEFs at ± 2kb from annotated transcription start sites (TSS). B and C) Representative IGV tracks depicting H3K27me3 intensity at Gata4 (B) and Tbx20 (C) promoters from Day 7 GHMT2m-reprogrammed cells with indicated TGF-β pathway manipulation and undifferentiated MEFs. D and E) Logarithmic transformation of H3K27me3 levels in relation to undifferentiated MEFs at ± 2kb from the annotated TSS of genes within the Muscle System Process Gene Ontology pathway (GO:0003012) that were also upregulated > 2 fold in GHMT2m + A-83-01 reprogrammed cells compared to undifferentiated MEFs as identified by RNA-seq (D) and at candidate cardiac genes selected from GO:0003012 (E). F) H3K27me3 levels at cardiac gene promoters Gata4, Tbx20, Actn2, Des, and Myh6 from Day 7 GHMT2m-reprogrammed cells co-infected with GFP, SMAD2, or SMAD7 or treated with <t>DMSO,</t> 5 ng/mL TGF-β1, or 0.5 µM A-83-01 analyzed by ChIP-qPCR. Undifferentiated MEFs served as a positive control for H3K27me3 levels. Data are presented as percentage of input. N=4 for MEFs, N=6 for GHMT2m + GFP + DMSO, N=6 for GHMT2m + GFP + TGF-β1, N=5 for GHMT2m + GFP + A-83-01, N=4 for GHMT2m + SMAD2, and N=5 for GHMT2m + SMAD7. G) GATA4 levels at cardiac gene promoters Nppa, Tbx20, and Myh6 from Day 5 GHMT2m-reprogrammed cells treated with DMSO, 5 ng/mL TGF-β1, or 0.5 µM A-83-01 analyzed by ChIP-qPCR. Data are presented as enrichment to IgG control. N=5 for GHMT2m + DMSO, N=4 for GHMT2m + TGF-β1, N=5 for GHMT2m + A-83-01. All data shown as mean ± SEM. *, # p
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    99
    Thermo Fisher to pro 3 iodide 642 661 1 mm solution in dmso
    Proliferation is dispensable for OCM. ( A-C ) Confocal sections (live, 24-hpf) showing EGFP-CAAX (membranes, green) and H2A.F/Z-mCherry (nuclei, magenta). (A) Untreated, (B) <t>DMSO</t> and (C) HUA embryos treated from 10.5-24 hpf. Insets show large HUA-treated cells versus DMSO control. ( D-F ) Confocal sections at 24 hpf showing phospho-histone H3 (green) and <t>TO-PRO-3</t> (magenta) in (D) untreated, (E) DMSO-treated and (F) HUA-treated embryos. Dorsal view. ( G-K ) Quantitative analyses of (G) mitoses, (H) cell number, (I) OV volume, (J) cell density and (K) retinal pigmented epithelium (RPE) volume as a fraction of OC [neural retina (NR) plus RPE] at 24 hpf in untreated (U), DMSO-treated (D) and HUA-treated embryos. Numbers of embryos scored (one eye each) are indicated within each bar. *, P
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    99
    Thermo Fisher sybr gold nucleic acid gel stain
    18S and 25S rRNAs protected from Terminator digestion as organisms shift to stationary phase and analysis of 5′-end for possible role in protection. a C. albicans growth curve at 30 °C in YPD medium. b <t>SYBR</t> gold stained gel of total <t>RNA</t> isolated at different time points either digested with Terminator (d) or undigested (u). c Northern blot of gel seen in a using 25S and 5S specific probes (Table 1 ). d RNA digested with Terminator alone or following TAP or AP digestion. As can be seen both 25S and 18S remain protected after AP digestion but get eliminated after TAP digestion. CFUS colony forming units
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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
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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.
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    92
    Thermo Fisher dimethyl sulfoxide dmso
    Inhibition of <t>TMZ-induced</t> G2 arrest by Rsv leads to mitotic catastrophe. U87 cells were treated with Rsv 30 μM, TMZ 100 μM or RT for 24, 38 and 48 h, followed by fixation and DAPI staining. (A) representative images of nuclei from cells treated with <t>DMSO</t> (control), Rsv for 38 h or RT for 48 h. Double arrows point to fragmented/irregular nuclei; single arrow points to micronuclei; double arrowheads point to enlarged nuclei; Scale bar: 6 μm; (B) representative visible and fluorescent images of nuclei from untreated cells showing a normal mitosis (i and ii) ; an abnormal chromosome condensation and mitosis, with cellular enlargement, in a cell treated with RT for 48 h (iii and iv) ; and a triple mitosis in a cell treated with Rsv for 48 h (v and vi) and. Scale bar: 10 μm; (C) direct counting of the percentage of nuclei presenting normal (top), irregular (mid) or large phenotype (bottom); *p
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    Merck KGaA dimethyl sulfoxide dmso
    SEM image of PVA nanofiber (a) before and after solvent vapor treatment with (b) <t>DMF,</t> (c) methanol, and (d) <t>DMSO</t> at a temperature of 40 °C for 8 h, and (e) Young's modulus and tensile strength of PVA nanofiber mats with various solvent types at a temperature of 40 °C for 4 h.
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    Fisher Scientific dimethyl sulfoxide dmso
    Comparison of <t>CFZ</t> and CFZ analog 568: structures, precipitation assay, and absorbance profiles ( a ) The structural difference between CFZ and analog 568 at the tertiary amine is a specific substitution of the isopropyl group with a 2-hydroxyethyl. ( b ) The absorbance profiles (270-550nm) show the similarity of CFZ and analog 568 free base and hydrochloride salt forms, respectively. ( c ) The ability of both CFZ and analog 568 to precipitate as hydrochloride salt in simulated lysosomal conditions (pH 4.5). This was determined by measuring the absorbance (285nm) in different conditions: Soln A (no chloride), Soln B (100mM chloride), and <t>DMSO</t> (red = CFZ, blue = 568). ( d ) Hydrochloride salt precipitation in the presence of chloride (Soln B) was verified by brightfield (BF) and fluorescence microscopy (F cy5 ). Scale bar = 50μm.
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    Thermo Fisher sytox green nucleic acid stain 5 mm solution in dmso
    Viability assay of cysticerci treated with 50 and 500 μM FCF . Viability was analyzed by <t>SYTOX</t> green. (a) Quantification of RFUs of cells treated with <t>DMSO</t> control or FCF (50 or 500 μ M) compared with that of the dead control cells. (b) Microscopic analysis of parasites incubated with SYTOX green after FCF exposure. Scale bars represent 500 μ m. Bright-field images are shown in Supplementary Figure S4 .
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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
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    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.
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    Millipore dimethyl sulfoxide
    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.
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    Millipore hek293 cells
    Disease-associated mutations increase temperature activation of TRPM3. <t>HEK293</t> cells were transfected with the human TRPM3α2, or its mutants; fura-2 Ca 2+ imaging experiments were performed as described in the Materials and methods section. ( A-C ) Averaged fluorescence ratio traces (340 nm/380 nm) for all PregS-responsive cells from one coverslip in cells expressing TRPM3 ( A ), V992M ( B ) and P1092Q ( C ). The cells were first stimulated by increasing the temperature to 37°C, followed by 10 μM primidone at room temperature to facilitate return of Ca 2+ to baseline, finally 25 μM PregS was applied. ( D ) The change in 340/380 ratio induced by 37°C expressed as a fraction of the response to 25 μM PregS. ( E ) 340/380 ratios at baseline, in response to 37°C and in response to 25 μM PregS. Each symbol represents the average value from all PregS-responsive cells from one coverslip, lines connect data points from the same coverslip. Each coverslips had around 70–80 PregS-responsive cells in the WT group; 35–45 for P1092Q, and 15–25 for V992M. Data were collected from three independent transfections.
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    FUJIFILM dimethyl sulfoxide dmso
    Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, <t>DEX,</t> and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and <t>DMSO</t> were assigned a value of 1.
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    Merck & Co dimethyl sulfoxide dmso
    The combination of <t>LCRF‐0006</t> and bortezomib synergistically increases MM tumor response in vivo. A, Schematic representation of treatment regimen. C57BL/KaLwRij mice with established MM (day 14 post‐5TGM1 cell injection) were treated with LCRF‐0006 (100 mg/kg) and bortezomib (0.5 mg/kg) (LCRF‐0006 + bortezomib), LCRF‐0006 and <t>DMSO</t> vehicle (LCRF‐0006), 2‐HP‐b‐CD vehicle and bortezomib (bortezomib) or 2‐HP‐b‐CD and DMSO vehicles (vehicles) i.p., as per treatment regimen. B, Tumor burden was assessed at day 14, 21 and 28 by BLI. Graph depicts mean ± SEM. n = 5‐6 mice/treatment group. *** P
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    Thermo Fisher sypro orange protein gel stain
    Effect of E3330-amide on APE1’s melting temperature as measured by DSF. APE1 was titrated with increasing concentrations of E3330-amide dissolved in <t>DMSO</t> (16 μM – 4 mM) in the presence and absence of 1 mM Mg 2+ . <t>SYPRO</t> Orange dye was then added, and T m measurements were obtained by DSF. The resulting T m of APE1 was plotted versus the concentration of E3330-amide in either the presence or absence of 1 mM Mg 2+ . Increasing concentrations of E3330-amide did not produce a change in the T m of APE1.
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    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
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    Image Search Results


    Caspase activity is not required for T3D-induced cell death. (A) ATCC L929 cells were adsorbed with PBS (mock) or T3D at an MOI of 10 PFU/cell. After incubation at 37°C for 48 h in the presence of DMSO or 25 µM caspase-8 (Z-IETD-FMK), caspase-9 (Z-LEHD-FMK), or pan-caspase [Z-VAD(OMe)-FMK] inhibitor, cells were stained with AOEB. The results are expressed as the mean percentages of cells undergoing cell death for three independent experiments. Error bars indicate SD. (B) ATCC L929 cells were adsorbed with PBS (mock) or T3D at the MOI of 10 PFU/cell. After incubation at 37°C for 24 h in the presence of DMSO or 25 µM concentrations of each caspase inhibitor, caspase-3/7 activity in cell lysates was determined. Results are expressed as the mean ratios of caspase-3/7 activity from infected cell lysates to that from equivalently treated mock-infected cells for triplicate samples. We note that the DMSO-treated cells are the same as those used in Fig. 2 . Error bars indicate SD. *, P value of

    Journal: mBio

    Article Title: Reovirus Activates a Caspase-Independent Cell Death Pathway

    doi: 10.1128/mBio.00178-13

    Figure Lengend Snippet: Caspase activity is not required for T3D-induced cell death. (A) ATCC L929 cells were adsorbed with PBS (mock) or T3D at an MOI of 10 PFU/cell. After incubation at 37°C for 48 h in the presence of DMSO or 25 µM caspase-8 (Z-IETD-FMK), caspase-9 (Z-LEHD-FMK), or pan-caspase [Z-VAD(OMe)-FMK] inhibitor, cells were stained with AOEB. The results are expressed as the mean percentages of cells undergoing cell death for three independent experiments. Error bars indicate SD. (B) ATCC L929 cells were adsorbed with PBS (mock) or T3D at the MOI of 10 PFU/cell. After incubation at 37°C for 24 h in the presence of DMSO or 25 µM concentrations of each caspase inhibitor, caspase-3/7 activity in cell lysates was determined. Results are expressed as the mean ratios of caspase-3/7 activity from infected cell lysates to that from equivalently treated mock-infected cells for triplicate samples. We note that the DMSO-treated cells are the same as those used in Fig. 2 . Error bars indicate SD. *, P value of

    Article Snippet: *, P value of < 0.05 as determined by Student’s t test in comparison to T1L-infected cells treated with DMSO at equivalent times postinfection. (B) ATCC L929 cells were adsorbed with PBS (mock) or 10 PFU/cell of T1L.

    Techniques: Activity Assay, Incubation, Staining, Infection

    NF-κB is activated but dispensable for induction of cell death. (A) ATCC L929 cells were adsorbed with PBS (mock) or 100 PFU/cell of T3D or T1L. Following incubation at 37°C for 7.5 h, cytoplasmic extracts were immunoblotted using an antiserum specific for IκBα or tubulin. (B) ATCC L929 cells were adsorbed with PBS (mock) or 100 PFU/cell of T3D or T1L. Following incubation at 37°C for 7.5 h, nuclear extracts were immunoblotted using an antiserum specific for RelA or PSTAIR. (C) ATCC L929 cells were adsorbed with PBS (mock) or T3D at an MOI of 10 PFU/cell or treated with 10 ng/ml TNF-α. After incubation at 37°C for 48 h (24 h for TNF-α), in the presence of DMSO or a 5 µM concentration of the IKK inhibitor BAY-65-1942, the cells were stained with AOEB. The results are expressed as the mean percentages of cells undergoing cell death for three independent experiments. Error bars indicate SD. *, P value of

    Journal: mBio

    Article Title: Reovirus Activates a Caspase-Independent Cell Death Pathway

    doi: 10.1128/mBio.00178-13

    Figure Lengend Snippet: NF-κB is activated but dispensable for induction of cell death. (A) ATCC L929 cells were adsorbed with PBS (mock) or 100 PFU/cell of T3D or T1L. Following incubation at 37°C for 7.5 h, cytoplasmic extracts were immunoblotted using an antiserum specific for IκBα or tubulin. (B) ATCC L929 cells were adsorbed with PBS (mock) or 100 PFU/cell of T3D or T1L. Following incubation at 37°C for 7.5 h, nuclear extracts were immunoblotted using an antiserum specific for RelA or PSTAIR. (C) ATCC L929 cells were adsorbed with PBS (mock) or T3D at an MOI of 10 PFU/cell or treated with 10 ng/ml TNF-α. After incubation at 37°C for 48 h (24 h for TNF-α), in the presence of DMSO or a 5 µM concentration of the IKK inhibitor BAY-65-1942, the cells were stained with AOEB. The results are expressed as the mean percentages of cells undergoing cell death for three independent experiments. Error bars indicate SD. *, P value of

    Article Snippet: *, P value of < 0.05 as determined by Student’s t test in comparison to T1L-infected cells treated with DMSO at equivalent times postinfection. (B) ATCC L929 cells were adsorbed with PBS (mock) or 10 PFU/cell of T1L.

    Techniques: Incubation, Concentration Assay, Staining

    T3D-induced cell death exhibits characteristics of necroptosis. (A) ATCC L929 cells were adsorbed with T3D at an MOI of 10 PFU/cell. After incubation at 37°C for 48 h in the presence of DMSO, 50 µM RIP1 inhibitor (Nec-1), or a combination of 50 µM RIP1 inhibitor (Nec-1) and 25 µM pan-caspase inhibitor [Z-VAD(OMe)-FMK], cells were harvested and stained with AOEB. The results are expressed as the mean percentages of cells undergoing cell death for three independent experiments. Error bars indicate SD. *, P value of

    Journal: mBio

    Article Title: Reovirus Activates a Caspase-Independent Cell Death Pathway

    doi: 10.1128/mBio.00178-13

    Figure Lengend Snippet: T3D-induced cell death exhibits characteristics of necroptosis. (A) ATCC L929 cells were adsorbed with T3D at an MOI of 10 PFU/cell. After incubation at 37°C for 48 h in the presence of DMSO, 50 µM RIP1 inhibitor (Nec-1), or a combination of 50 µM RIP1 inhibitor (Nec-1) and 25 µM pan-caspase inhibitor [Z-VAD(OMe)-FMK], cells were harvested and stained with AOEB. The results are expressed as the mean percentages of cells undergoing cell death for three independent experiments. Error bars indicate SD. *, P value of

    Article Snippet: *, P value of < 0.05 as determined by Student’s t test in comparison to T1L-infected cells treated with DMSO at equivalent times postinfection. (B) ATCC L929 cells were adsorbed with PBS (mock) or 10 PFU/cell of T1L.

    Techniques: Incubation, Staining

    Intracellular Ca 2+  in  Leishmania  increases in response to allicin stress. Leishmania  promastigotes were treated with allicin (15–120 μM) for 20 min. Calcium levels were determined by Fluo 4AM preloading of cells (60 min) in loading buffer with 0.02% Pluronic F-127. Maximal fluorescence was obtained with cells treated with 0.5% Triton X-100 and minimal after chelation with 8 mM EGTA. Data presented corresponds to the average increase of normalized fluorescence intensity of two independent experiments in triplicate (mean ± S.D.). Asterisks represent significant differences compared to untreated control promastigotes (*:  p

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Allicin Induces Calcium and Mitochondrial Dysregulation Causing Necrotic Death in Leishmania

    doi: 10.1371/journal.pntd.0004525

    Figure Lengend Snippet: Intracellular Ca 2+ in Leishmania increases in response to allicin stress. Leishmania promastigotes were treated with allicin (15–120 μM) for 20 min. Calcium levels were determined by Fluo 4AM preloading of cells (60 min) in loading buffer with 0.02% Pluronic F-127. Maximal fluorescence was obtained with cells treated with 0.5% Triton X-100 and minimal after chelation with 8 mM EGTA. Data presented corresponds to the average increase of normalized fluorescence intensity of two independent experiments in triplicate (mean ± S.D.). Asterisks represent significant differences compared to untreated control promastigotes (*: p

    Article Snippet: Pluronic F-127 (0.02%, Molecular Probes) was added to facilitate the dispersion of the nonpolar AM ester.

    Techniques: Fluorescence

    Top (A) and side (B) views of the stretching device. Single cells were confined in specific geometries on the elastic membranes (white dashed rectangle) by microcontact printing using agarose stamp (C). Fibronectin (FN, green) was used to promote cell adhesion and Pluronic F127 was used as the blocking molecule. Single C2C12 cells of 2000 μm 2 (40 × 50, 20 × 100 and 10 × 200) were successfully confined in different shapes (blue, nuclear stained by DAPI; red, F-actin stained by Rhodamine Phalloidin) (D). The entire list of the geometries of C2C12 cells can be found as Supplementary Figure S2 online.

    Journal: Scientific Reports

    Article Title: Tissue-specific mechanical and geometrical control of cell viability and actin cytoskeleton alignment

    doi: 10.1038/srep06160

    Figure Lengend Snippet: Top (A) and side (B) views of the stretching device. Single cells were confined in specific geometries on the elastic membranes (white dashed rectangle) by microcontact printing using agarose stamp (C). Fibronectin (FN, green) was used to promote cell adhesion and Pluronic F127 was used as the blocking molecule. Single C2C12 cells of 2000 μm 2 (40 × 50, 20 × 100 and 10 × 200) were successfully confined in different shapes (blue, nuclear stained by DAPI; red, F-actin stained by Rhodamine Phalloidin) (D). The entire list of the geometries of C2C12 cells can be found as Supplementary Figure S2 online.

    Article Snippet: After about 5 min of conformal contact, we peeled off the agarose stamp and blocked the substrate with 0.2% Pluronic F127 (Invitrogen) solution in PBS for at least 1 h, before seeding cells ( ).

    Techniques: Blocking Assay, Staining

    Suppressing Smad7 protein expression with Notch inhibitor N-(N-[3,5-difluorophenacetyl]-l-alanyl)-S-phenylglycine t-butyl ester facilitates epithelial–mesenchymal transition and growth arrest induced by transforming growth factor-beta. A : Western blot analysis of Smad 2/3 phosphorylation. Left planes: Transforming growth factor-beta (TGFβ1) time-dependently induces Smad2/3 phosphorylation in P1 cells. Right planes: P1 cells were treated with 10 ng/ml TGFβ1 for 30 and 40 min as positive control. P0 and P1 cells were pretreated with 10 µM N-(N-[3,5-difluorophenacetyl]-l-alanyl)-S-phenylglycine t-butyl ester (DAPT) or dimethyl sulfoxide (DMSO) vehicle for 48 h and then stimulated with TGFβ1 for 30 and 40 min, respectively. Cells were harvested and subjected to western blot analysis with phosphospecific antibodies of Smad2 and Smad3. The total protein levels of Smad2 and Smad3 were estimated by reprobing the membranes with total Smad2 and Smad3 antibody shown in the panels below. B : P0 LSCs pretreated with DAPT facilitates mesenchymal marker expression induced by TGFβ1. Representative blots (left panels) and densitometric analysis with standard deviation (SD; right columns) of three independent experiments are shown. *p

    Journal: Molecular Vision

    Article Title: Notch prevents transforming growth factor-beta-assisted epithelial-mesenchymal transition in cultured limbal progenitor cells through the induction of Smad7

    doi:

    Figure Lengend Snippet: Suppressing Smad7 protein expression with Notch inhibitor N-(N-[3,5-difluorophenacetyl]-l-alanyl)-S-phenylglycine t-butyl ester facilitates epithelial–mesenchymal transition and growth arrest induced by transforming growth factor-beta. A : Western blot analysis of Smad 2/3 phosphorylation. Left planes: Transforming growth factor-beta (TGFβ1) time-dependently induces Smad2/3 phosphorylation in P1 cells. Right planes: P1 cells were treated with 10 ng/ml TGFβ1 for 30 and 40 min as positive control. P0 and P1 cells were pretreated with 10 µM N-(N-[3,5-difluorophenacetyl]-l-alanyl)-S-phenylglycine t-butyl ester (DAPT) or dimethyl sulfoxide (DMSO) vehicle for 48 h and then stimulated with TGFβ1 for 30 and 40 min, respectively. Cells were harvested and subjected to western blot analysis with phosphospecific antibodies of Smad2 and Smad3. The total protein levels of Smad2 and Smad3 were estimated by reprobing the membranes with total Smad2 and Smad3 antibody shown in the panels below. B : P0 LSCs pretreated with DAPT facilitates mesenchymal marker expression induced by TGFβ1. Representative blots (left panels) and densitometric analysis with standard deviation (SD; right columns) of three independent experiments are shown. *p

    Article Snippet: DAPT, IWR-1, cyclopamine, hydrocortisone, dimethyl sulfoxide (DMSO), insulin-transferrin-sodium selenite (ITSE) media supplement, mitomycin C (MMC), bovine serum albumin (BSA), 5-bromo-2'-deoxyuridine (BrdU), Triton X-100, Hoechst 33,258 dye, and formalin were all from Sigma-Aldrich (St. Louis, MO).

    Techniques: Expressing, Western Blot, Positive Control, Marker, Standard Deviation

    Artificial diet assays with Myzus persicae to establish the specificity of aphid responses to NAM. Aphid feeding behavior, survival, and fecundity were observed at: ( a ) 6 hours, ( b ) 12 hours, ( c ) 24 hours, and ( d ) 48 hours in response to feeding on artificial diets without supplementation (Control) or supplemented with 10 mM NAM, 10 mM nicotinic acid (NA), 1.38 mM pymetrozine insecticide solubilized in 0.7% DMSO, or 0.7% DMSO alone. The average number of aphids in each behavioral response group were analyzed by one-way ANOVA. Means for each behavioral response that do not share a letter are significantly different at the 95% confidence level.

    Journal: Scientific Reports

    Article Title: Nicotinamide Inhibits Aphid Fecundity and Impacts Survival

    doi: 10.1038/s41598-019-55931-z

    Figure Lengend Snippet: Artificial diet assays with Myzus persicae to establish the specificity of aphid responses to NAM. Aphid feeding behavior, survival, and fecundity were observed at: ( a ) 6 hours, ( b ) 12 hours, ( c ) 24 hours, and ( d ) 48 hours in response to feeding on artificial diets without supplementation (Control) or supplemented with 10 mM NAM, 10 mM nicotinic acid (NA), 1.38 mM pymetrozine insecticide solubilized in 0.7% DMSO, or 0.7% DMSO alone. The average number of aphids in each behavioral response group were analyzed by one-way ANOVA. Means for each behavioral response that do not share a letter are significantly different at the 95% confidence level.

    Article Snippet: To establish the specificity of the M. persicae response to NAM, diets were supplemented with 10 mM NAM, 10 mM nicotinic acid (NA, negative control), 1.38 µM pymetrozine solubilized in 0.7% DMSO (Millipore-Sigma, positive control), 0.7% DMSO (solvent control) or with diet alone (buffer control).

    Techniques:

    Inhibitory effect of 17β-estradiol ( E ), genistein ( G ) and daidzein ( D ) on post-injury neointima development in concentrations of 20/30/40 μM, compared to endothelium balloon denuded ( BD ) controls ( C ) (mean ± SD). The medium of all groups contained 1 % isopropanol ( 1 % iso ) and 1 % DMSO . Compared with controls 17β-estradiol, genistein, and daidzein (*) reduced neointima formation significantly (p = 0.05) in a concentration dependent manner. Data from Finking et al., 2000 [ 25 ].

    Journal: BMC Cardiovascular Disorders

    Article Title: Reduction of post injury neointima formation due to 17?-estradiol and phytoestrogen treatment is not influenced by the pure synthetic estrogen receptor antagonist ICI 182,780 in vitro

    doi:

    Figure Lengend Snippet: Inhibitory effect of 17β-estradiol ( E ), genistein ( G ) and daidzein ( D ) on post-injury neointima development in concentrations of 20/30/40 μM, compared to endothelium balloon denuded ( BD ) controls ( C ) (mean ± SD). The medium of all groups contained 1 % isopropanol ( 1 % iso ) and 1 % DMSO . Compared with controls 17β-estradiol, genistein, and daidzein (*) reduced neointima formation significantly (p = 0.05) in a concentration dependent manner. Data from Finking et al., 2000 [ 25 ].

    Article Snippet: Control groups were held in medium containing 1 % isopropanol (Roth, Karlsruhe, Germany) and 1% dimethyl sulphoxide (DMSO) (Sigma, Deisenhofen, Germany) because 17β-estradiol, Genistein and Daidzein were dissolved in isopropanol and DMSO of the same concentration.

    Techniques: Concentration Assay

    TGF-β signaling impairs demethylation of H3K27me3 and recruitment of GATA4 to target genes A) Global ChIP-seq density heatmap of H3K27me3 in Day 7 GHMT2m-reprogrammed cells with indicated TGF-β pathway manipulation and undifferentiated MEFs at ± 2kb from annotated transcription start sites (TSS). B and C) Representative IGV tracks depicting H3K27me3 intensity at Gata4 (B) and Tbx20 (C) promoters from Day 7 GHMT2m-reprogrammed cells with indicated TGF-β pathway manipulation and undifferentiated MEFs. D and E) Logarithmic transformation of H3K27me3 levels in relation to undifferentiated MEFs at ± 2kb from the annotated TSS of genes within the Muscle System Process Gene Ontology pathway (GO:0003012) that were also upregulated > 2 fold in GHMT2m + A-83-01 reprogrammed cells compared to undifferentiated MEFs as identified by RNA-seq (D) and at candidate cardiac genes selected from GO:0003012 (E). F) H3K27me3 levels at cardiac gene promoters Gata4, Tbx20, Actn2, Des, and Myh6 from Day 7 GHMT2m-reprogrammed cells co-infected with GFP, SMAD2, or SMAD7 or treated with DMSO, 5 ng/mL TGF-β1, or 0.5 µM A-83-01 analyzed by ChIP-qPCR. Undifferentiated MEFs served as a positive control for H3K27me3 levels. Data are presented as percentage of input. N=4 for MEFs, N=6 for GHMT2m + GFP + DMSO, N=6 for GHMT2m + GFP + TGF-β1, N=5 for GHMT2m + GFP + A-83-01, N=4 for GHMT2m + SMAD2, and N=5 for GHMT2m + SMAD7. G) GATA4 levels at cardiac gene promoters Nppa, Tbx20, and Myh6 from Day 5 GHMT2m-reprogrammed cells treated with DMSO, 5 ng/mL TGF-β1, or 0.5 µM A-83-01 analyzed by ChIP-qPCR. Data are presented as enrichment to IgG control. N=5 for GHMT2m + DMSO, N=4 for GHMT2m + TGF-β1, N=5 for GHMT2m + A-83-01. All data shown as mean ± SEM. *, # p

    Journal: bioRxiv

    Article Title: Suppression of canonical TGF-β signaling enables GATA4 to interact with H3K27me3 demethylase JMJD3 to promote cardiomyogenesis

    doi: 10.1101/2020.02.12.945790

    Figure Lengend Snippet: TGF-β signaling impairs demethylation of H3K27me3 and recruitment of GATA4 to target genes A) Global ChIP-seq density heatmap of H3K27me3 in Day 7 GHMT2m-reprogrammed cells with indicated TGF-β pathway manipulation and undifferentiated MEFs at ± 2kb from annotated transcription start sites (TSS). B and C) Representative IGV tracks depicting H3K27me3 intensity at Gata4 (B) and Tbx20 (C) promoters from Day 7 GHMT2m-reprogrammed cells with indicated TGF-β pathway manipulation and undifferentiated MEFs. D and E) Logarithmic transformation of H3K27me3 levels in relation to undifferentiated MEFs at ± 2kb from the annotated TSS of genes within the Muscle System Process Gene Ontology pathway (GO:0003012) that were also upregulated > 2 fold in GHMT2m + A-83-01 reprogrammed cells compared to undifferentiated MEFs as identified by RNA-seq (D) and at candidate cardiac genes selected from GO:0003012 (E). F) H3K27me3 levels at cardiac gene promoters Gata4, Tbx20, Actn2, Des, and Myh6 from Day 7 GHMT2m-reprogrammed cells co-infected with GFP, SMAD2, or SMAD7 or treated with DMSO, 5 ng/mL TGF-β1, or 0.5 µM A-83-01 analyzed by ChIP-qPCR. Undifferentiated MEFs served as a positive control for H3K27me3 levels. Data are presented as percentage of input. N=4 for MEFs, N=6 for GHMT2m + GFP + DMSO, N=6 for GHMT2m + GFP + TGF-β1, N=5 for GHMT2m + GFP + A-83-01, N=4 for GHMT2m + SMAD2, and N=5 for GHMT2m + SMAD7. G) GATA4 levels at cardiac gene promoters Nppa, Tbx20, and Myh6 from Day 5 GHMT2m-reprogrammed cells treated with DMSO, 5 ng/mL TGF-β1, or 0.5 µM A-83-01 analyzed by ChIP-qPCR. Data are presented as enrichment to IgG control. N=5 for GHMT2m + DMSO, N=4 for GHMT2m + TGF-β1, N=5 for GHMT2m + A-83-01. All data shown as mean ± SEM. *, # p

    Article Snippet: DMSO (Thermo Scientific), 5 ng/mL TGF-β1 (Novoprotein CA59), 0.5 μM A-83-01 (Tocris 2939), or 0.5 μM or 1 μM GSK-J4 (Tocris 4594) were administered starting at 72 hours post-infection.

    Techniques: Chromatin Immunoprecipitation, Transformation Assay, RNA Sequencing Assay, Infection, Real-time Polymerase Chain Reaction, Positive Control

    Proliferation is dispensable for OCM. ( A-C ) Confocal sections (live, 24-hpf) showing EGFP-CAAX (membranes, green) and H2A.F/Z-mCherry (nuclei, magenta). (A) Untreated, (B) DMSO and (C) HUA embryos treated from 10.5-24 hpf. Insets show large HUA-treated cells versus DMSO control. ( D-F ) Confocal sections at 24 hpf showing phospho-histone H3 (green) and TO-PRO-3 (magenta) in (D) untreated, (E) DMSO-treated and (F) HUA-treated embryos. Dorsal view. ( G-K ) Quantitative analyses of (G) mitoses, (H) cell number, (I) OV volume, (J) cell density and (K) retinal pigmented epithelium (RPE) volume as a fraction of OC [neural retina (NR) plus RPE] at 24 hpf in untreated (U), DMSO-treated (D) and HUA-treated embryos. Numbers of embryos scored (one eye each) are indicated within each bar. *, P

    Journal: Development (Cambridge, England)

    Article Title: A complex choreography of cell movements shapes the vertebrate eye

    doi: 10.1242/dev.071407

    Figure Lengend Snippet: Proliferation is dispensable for OCM. ( A-C ) Confocal sections (live, 24-hpf) showing EGFP-CAAX (membranes, green) and H2A.F/Z-mCherry (nuclei, magenta). (A) Untreated, (B) DMSO and (C) HUA embryos treated from 10.5-24 hpf. Insets show large HUA-treated cells versus DMSO control. ( D-F ) Confocal sections at 24 hpf showing phospho-histone H3 (green) and TO-PRO-3 (magenta) in (D) untreated, (E) DMSO-treated and (F) HUA-treated embryos. Dorsal view. ( G-K ) Quantitative analyses of (G) mitoses, (H) cell number, (I) OV volume, (J) cell density and (K) retinal pigmented epithelium (RPE) volume as a fraction of OC [neural retina (NR) plus RPE] at 24 hpf in untreated (U), DMSO-treated (D) and HUA-treated embryos. Numbers of embryos scored (one eye each) are indicated within each bar. *, P

    Article Snippet: Embryos (24 hpf) were fixed in 4% paraformaldehyde (PFA), permeabilized in TBST (TBS containing 0.1% Triton X-100), blocked in TBST containing 2% BSA and incubated with anti-phospho-histone H3 antibody (1:250; Millipore, 06-570), then goat anti-rabbit secondary antibody (Invitrogen, A-11008) co-incubated with 1 μM TO-PRO-3 iodide (Invitrogen, T3605).

    Techniques:

    18S and 25S rRNAs protected from Terminator digestion as organisms shift to stationary phase and analysis of 5′-end for possible role in protection. a C. albicans growth curve at 30 °C in YPD medium. b SYBR gold stained gel of total RNA isolated at different time points either digested with Terminator (d) or undigested (u). c Northern blot of gel seen in a using 25S and 5S specific probes (Table 1 ). d RNA digested with Terminator alone or following TAP or AP digestion. As can be seen both 25S and 18S remain protected after AP digestion but get eliminated after TAP digestion. CFUS colony forming units

    Journal: BMC Molecular Biology

    Article Title: Nutrient depletion and TOR inhibition induce 18S and 25S ribosomal RNAs resistant to a 5′-phosphate-dependent exonuclease in Candida albicans and other yeasts

    doi: 10.1186/s12867-018-0102-y

    Figure Lengend Snippet: 18S and 25S rRNAs protected from Terminator digestion as organisms shift to stationary phase and analysis of 5′-end for possible role in protection. a C. albicans growth curve at 30 °C in YPD medium. b SYBR gold stained gel of total RNA isolated at different time points either digested with Terminator (d) or undigested (u). c Northern blot of gel seen in a using 25S and 5S specific probes (Table 1 ). d RNA digested with Terminator alone or following TAP or AP digestion. As can be seen both 25S and 18S remain protected after AP digestion but get eliminated after TAP digestion. CFUS colony forming units

    Article Snippet: RNA was separated on pre-fabricated formaldehyde agarose gels (Lonza) and stained with SYBR Gold Nucleic Acid Gel Stain (Life Technologies) for 30 min. Gel images were captured with a digital camera (Canon Vixia HFS30).

    Techniques: Staining, Isolation, Northern Blot

    Incorporation of Terminator resistant 18S and 25S transcripts into ribosomes, and analysis of other yeasts for similar resistant rRNAs. a Agarose gel of RNA precipitated from isolated ribosomes from stationary phase cells. Numbers indicate fractions collected sequentially. Different elution fractions were combined prior to precipitation of RNA from isolated ribosomes from mid-log phase cells. Amount of Terminator digested RNA was the same as their undigested RNA pair. b SYBR gold stained gel containing RNA digested with Terminator (D) and undigested (U) isolated from mid log and stationary Candida albican s, Candida krusei , Schizosaccharomyces pombe and Saccharomyces cerevisiae

    Journal: BMC Molecular Biology

    Article Title: Nutrient depletion and TOR inhibition induce 18S and 25S ribosomal RNAs resistant to a 5′-phosphate-dependent exonuclease in Candida albicans and other yeasts

    doi: 10.1186/s12867-018-0102-y

    Figure Lengend Snippet: Incorporation of Terminator resistant 18S and 25S transcripts into ribosomes, and analysis of other yeasts for similar resistant rRNAs. a Agarose gel of RNA precipitated from isolated ribosomes from stationary phase cells. Numbers indicate fractions collected sequentially. Different elution fractions were combined prior to precipitation of RNA from isolated ribosomes from mid-log phase cells. Amount of Terminator digested RNA was the same as their undigested RNA pair. b SYBR gold stained gel containing RNA digested with Terminator (D) and undigested (U) isolated from mid log and stationary Candida albican s, Candida krusei , Schizosaccharomyces pombe and Saccharomyces cerevisiae

    Article Snippet: RNA was separated on pre-fabricated formaldehyde agarose gels (Lonza) and stained with SYBR Gold Nucleic Acid Gel Stain (Life Technologies) for 30 min. Gel images were captured with a digital camera (Canon Vixia HFS30).

    Techniques: Agarose Gel Electrophoresis, Isolation, Staining

    TOR inhibition also leads to Terminator resistance. a SYBR gold stained gel showing RNA from cells grown in fresh YPD with rapamycin at 1 µg/ml for 6 h at 30 °C. Controls (Rap-) were cells in fresh YPD without rapamycin for 6 h at 30 °C. RNA was either undigested (u) or digested by Terminator (d). b Northern blot from a . c Western blot performed on protein isolated and probed with S6 kinase and actin specific antibodies from cells grown as in a with and without rapamycin treatment. d Northern blot performed with ITS2 specific probe using RNA from cells grown under the same conditions as in a (see Table 1 for probe sequences). All blots started with the same amount of total RNA or protein loaded for all conditions

    Journal: BMC Molecular Biology

    Article Title: Nutrient depletion and TOR inhibition induce 18S and 25S ribosomal RNAs resistant to a 5′-phosphate-dependent exonuclease in Candida albicans and other yeasts

    doi: 10.1186/s12867-018-0102-y

    Figure Lengend Snippet: TOR inhibition also leads to Terminator resistance. a SYBR gold stained gel showing RNA from cells grown in fresh YPD with rapamycin at 1 µg/ml for 6 h at 30 °C. Controls (Rap-) were cells in fresh YPD without rapamycin for 6 h at 30 °C. RNA was either undigested (u) or digested by Terminator (d). b Northern blot from a . c Western blot performed on protein isolated and probed with S6 kinase and actin specific antibodies from cells grown as in a with and without rapamycin treatment. d Northern blot performed with ITS2 specific probe using RNA from cells grown under the same conditions as in a (see Table 1 for probe sequences). All blots started with the same amount of total RNA or protein loaded for all conditions

    Article Snippet: RNA was separated on pre-fabricated formaldehyde agarose gels (Lonza) and stained with SYBR Gold Nucleic Acid Gel Stain (Life Technologies) for 30 min. Gel images were captured with a digital camera (Canon Vixia HFS30).

    Techniques: Inhibition, Staining, Northern Blot, Western Blot, Isolation

    Total RNA from yeast in stationary and mid log growth phase treated or untreated with Terminator. a SYBR-Gold stained gel showing RNA treated with Terminator along with untreated RNA. Significant portions of 25S and 18S rRNA are protected from digestion. All conditions started out with the same amount of RNA. b Northern blot, using probes specific for either 5′ or 3′ ends of 25S and 18S ribosomal subunits confirming them to be the large and small subunits of rRNA protected from Terminator digestion. c SYBR-Gold stained gel displaying RNA isolated at mid log and stationary phases and treated with or without Terminator. d Northern Blot using 25S, 18S and 5S probes. Ribosomal 5S was used as loading control

    Journal: BMC Molecular Biology

    Article Title: Nutrient depletion and TOR inhibition induce 18S and 25S ribosomal RNAs resistant to a 5′-phosphate-dependent exonuclease in Candida albicans and other yeasts

    doi: 10.1186/s12867-018-0102-y

    Figure Lengend Snippet: Total RNA from yeast in stationary and mid log growth phase treated or untreated with Terminator. a SYBR-Gold stained gel showing RNA treated with Terminator along with untreated RNA. Significant portions of 25S and 18S rRNA are protected from digestion. All conditions started out with the same amount of RNA. b Northern blot, using probes specific for either 5′ or 3′ ends of 25S and 18S ribosomal subunits confirming them to be the large and small subunits of rRNA protected from Terminator digestion. c SYBR-Gold stained gel displaying RNA isolated at mid log and stationary phases and treated with or without Terminator. d Northern Blot using 25S, 18S and 5S probes. Ribosomal 5S was used as loading control

    Article Snippet: RNA was separated on pre-fabricated formaldehyde agarose gels (Lonza) and stained with SYBR Gold Nucleic Acid Gel Stain (Life Technologies) for 30 min. Gel images were captured with a digital camera (Canon Vixia HFS30).

    Techniques: Staining, Northern Blot, Isolation

    Nucleosomes are excluded from a > 1-kb region surrounding a mismatch. ( A ) The DNA substrate used in this study. The 3011-base-pair (bp) DNA carries an A:T base pair (pMM1 homo ) or an A:C mispair (pMM1 AC ) at position 1. Positions of restriction enzyme sites used in this study, the site of biotin modification, and amplicons for quantitative PCR (qPCR) (P1: 2950–61, P2: 253–383, P3: 476–602, P4: 728–860, P5: 1498–1628, P6: 2266–2397, and P7: 2413–2537) are indicated. ( B ) Supercoiling assay in NPE. Covalently closed pMM1 homo (lanes 2 – 8 ) or pMM1 AC (lanes 9 – 15 ) was incubated in NPE and sampled at the indicated times. (Lane 1 ) Supercoiled pMM1 homo purified from Escherichia coli was used as a size standard. (oc/r) Open circular or relaxed DNA; (sc) supercoiled DNA. ( C ) pMM1 homo (lanes 1 – 4 ) or pMM1 AC (lanes 5 – 8 ) was incubated in NPE for 60 min and digested by micrococcal nuclease (MNase). DNA samples stained with SYBR Gold ( top ) and Southern blotting with the PvuII–PvuII probe ( middle ) and the DraI–DraI probe ( bottom ) are shown. ( D – F ) The MNase assay described in C was repeated in the presence of a control plasmid (pControl), and undigested DNA was quantified by qPCR. The amount of DNA relative to the input ( D ) and normalized to pControl ( E ) and pMM1 homo ( F ) is presented. Mean ± one standard deviation (SD) is shown. n = 3.

    Journal: Genes & Development

    Article Title: Nucleosomes around a mismatched base pair are excluded via an Msh2-dependent reaction with the aid of SNF2 family ATPase Smarcad1

    doi: 10.1101/gad.310995.117

    Figure Lengend Snippet: Nucleosomes are excluded from a > 1-kb region surrounding a mismatch. ( A ) The DNA substrate used in this study. The 3011-base-pair (bp) DNA carries an A:T base pair (pMM1 homo ) or an A:C mispair (pMM1 AC ) at position 1. Positions of restriction enzyme sites used in this study, the site of biotin modification, and amplicons for quantitative PCR (qPCR) (P1: 2950–61, P2: 253–383, P3: 476–602, P4: 728–860, P5: 1498–1628, P6: 2266–2397, and P7: 2413–2537) are indicated. ( B ) Supercoiling assay in NPE. Covalently closed pMM1 homo (lanes 2 – 8 ) or pMM1 AC (lanes 9 – 15 ) was incubated in NPE and sampled at the indicated times. (Lane 1 ) Supercoiled pMM1 homo purified from Escherichia coli was used as a size standard. (oc/r) Open circular or relaxed DNA; (sc) supercoiled DNA. ( C ) pMM1 homo (lanes 1 – 4 ) or pMM1 AC (lanes 5 – 8 ) was incubated in NPE for 60 min and digested by micrococcal nuclease (MNase). DNA samples stained with SYBR Gold ( top ) and Southern blotting with the PvuII–PvuII probe ( middle ) and the DraI–DraI probe ( bottom ) are shown. ( D – F ) The MNase assay described in C was repeated in the presence of a control plasmid (pControl), and undigested DNA was quantified by qPCR. The amount of DNA relative to the input ( D ) and normalized to pControl ( E ) and pMM1 homo ( F ) is presented. Mean ± one standard deviation (SD) is shown. n = 3.

    Article Snippet: After agarose gel electrophoresis, DNA was stained with SYBR Gold nucleic acid stain (Life Technologies) and scanned with a Typhoon FLA9000 (GE Healthcare) or ChemiDoc Touch (Bio-Rad).

    Techniques: Modification, Real-time Polymerase Chain Reaction, Incubation, Purification, Staining, Southern Blot, Plasmid Preparation, Standard Deviation

    Smarcad1 is recruited onto mismatch-carrying DNA in a Msh2-dependent manner. ( A ) The immunodepletion efficiencies of Msh2 or Mlh1. NPE was depleted using preimmune antibodies (lane 1 , mock), a mixture of Msh2 and Msh6 antibodies (lane 2 , ΔMsh2), or Mlh1 antibodies (lane 3 , ΔMlh1). NPE (0.25 µL) was separated by SDS-PAGE and probed with the indicated antibodies. The depletion efficiencies for Msh2 and Mlh1 were estimated as 99% and 98%, respectively. ( B ) Immobilized pMM1 homo (lanes 1 , 3 , 5 ) or pMM1 AC (lanes 2 , 4 , 6 ) was incubated in NPE as described in A and recovered. Immunoblotting of the indicated antibodies and uncut DNA stained with SYBR Gold is presented. ( C ) Quantification of chromatin-binding factors. Band intensities were normalized to the amount of DNA quantified by qPCR. For Smarcad1, Msh2, Mlh1, Spt16, and Ssrp1, the number of molecules on a plasmid was estimated by using recombinant proteins as standards. Histones were normalized to the amount on no mismatch DNA in the mock sample. Mean ± one SD is shown. n = 4. P -values were calculated by the paired t -test (two-tailed). ( D ) Coimmunoprecipitation of Smarcad1 and MutSα. Immunoblotting of supernatant (IP-sup) and bead (IP-ppt) samples is presented. Green numbers represent band intensities relative to the target protein of immunoprecipitation. ( E ) Quantification of immunoprecipitated proteins. Mean ± one SD is shown. n = 3. P -values were calculated by the paired t -test (two-tailed).

    Journal: Genes & Development

    Article Title: Nucleosomes around a mismatched base pair are excluded via an Msh2-dependent reaction with the aid of SNF2 family ATPase Smarcad1

    doi: 10.1101/gad.310995.117

    Figure Lengend Snippet: Smarcad1 is recruited onto mismatch-carrying DNA in a Msh2-dependent manner. ( A ) The immunodepletion efficiencies of Msh2 or Mlh1. NPE was depleted using preimmune antibodies (lane 1 , mock), a mixture of Msh2 and Msh6 antibodies (lane 2 , ΔMsh2), or Mlh1 antibodies (lane 3 , ΔMlh1). NPE (0.25 µL) was separated by SDS-PAGE and probed with the indicated antibodies. The depletion efficiencies for Msh2 and Mlh1 were estimated as 99% and 98%, respectively. ( B ) Immobilized pMM1 homo (lanes 1 , 3 , 5 ) or pMM1 AC (lanes 2 , 4 , 6 ) was incubated in NPE as described in A and recovered. Immunoblotting of the indicated antibodies and uncut DNA stained with SYBR Gold is presented. ( C ) Quantification of chromatin-binding factors. Band intensities were normalized to the amount of DNA quantified by qPCR. For Smarcad1, Msh2, Mlh1, Spt16, and Ssrp1, the number of molecules on a plasmid was estimated by using recombinant proteins as standards. Histones were normalized to the amount on no mismatch DNA in the mock sample. Mean ± one SD is shown. n = 4. P -values were calculated by the paired t -test (two-tailed). ( D ) Coimmunoprecipitation of Smarcad1 and MutSα. Immunoblotting of supernatant (IP-sup) and bead (IP-ppt) samples is presented. Green numbers represent band intensities relative to the target protein of immunoprecipitation. ( E ) Quantification of immunoprecipitated proteins. Mean ± one SD is shown. n = 3. P -values were calculated by the paired t -test (two-tailed).

    Article Snippet: After agarose gel electrophoresis, DNA was stained with SYBR Gold nucleic acid stain (Life Technologies) and scanned with a Typhoon FLA9000 (GE Healthcare) or ChemiDoc Touch (Bio-Rad).

    Techniques: SDS Page, Incubation, Staining, Binding Assay, Real-time Polymerase Chain Reaction, Plasmid Preparation, Recombinant, Two Tailed Test, Immunoprecipitation

    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

    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

    Inhibition of TMZ-induced G2 arrest by Rsv leads to mitotic catastrophe. U87 cells were treated with Rsv 30 μM, TMZ 100 μM or RT for 24, 38 and 48 h, followed by fixation and DAPI staining. (A) representative images of nuclei from cells treated with DMSO (control), Rsv for 38 h or RT for 48 h. Double arrows point to fragmented/irregular nuclei; single arrow points to micronuclei; double arrowheads point to enlarged nuclei; Scale bar: 6 μm; (B) representative visible and fluorescent images of nuclei from untreated cells showing a normal mitosis (i and ii) ; an abnormal chromosome condensation and mitosis, with cellular enlargement, in a cell treated with RT for 48 h (iii and iv) ; and a triple mitosis in a cell treated with Rsv for 48 h (v and vi) and. Scale bar: 10 μm; (C) direct counting of the percentage of nuclei presenting normal (top), irregular (mid) or large phenotype (bottom); *p

    Journal: BMC Cancer

    Article Title: Resveratrol abrogates the Temozolomide-induced G2 arrest leading to mitotic catastrophe and reinforces the Temozolomide-induced senescence in glioma cells

    doi: 10.1186/1471-2407-13-147

    Figure Lengend Snippet: Inhibition of TMZ-induced G2 arrest by Rsv leads to mitotic catastrophe. U87 cells were treated with Rsv 30 μM, TMZ 100 μM or RT for 24, 38 and 48 h, followed by fixation and DAPI staining. (A) representative images of nuclei from cells treated with DMSO (control), Rsv for 38 h or RT for 48 h. Double arrows point to fragmented/irregular nuclei; single arrow points to micronuclei; double arrowheads point to enlarged nuclei; Scale bar: 6 μm; (B) representative visible and fluorescent images of nuclei from untreated cells showing a normal mitosis (i and ii) ; an abnormal chromosome condensation and mitosis, with cellular enlargement, in a cell treated with RT for 48 h (iii and iv) ; and a triple mitosis in a cell treated with Rsv for 48 h (v and vi) and. Scale bar: 10 μm; (C) direct counting of the percentage of nuclei presenting normal (top), irregular (mid) or large phenotype (bottom); *p

    Article Snippet: TMZ and Rsv were dissolved in dimethyl sulfoxide (DMSO) (Acros Organics, NJ, USA).

    Techniques: Inhibition, Staining

    SEM image of PVA nanofiber (a) before and after solvent vapor treatment with (b) DMF, (c) methanol, and (d) DMSO at a temperature of 40 °C for 8 h, and (e) Young's modulus and tensile strength of PVA nanofiber mats with various solvent types at a temperature of 40 °C for 4 h.

    Journal: Heliyon

    Article Title: Solvent vapor treatment improves mechanical strength of electrospun polyvinyl alcohol nanofibers

    doi: 10.1016/j.heliyon.2018.e00592

    Figure Lengend Snippet: SEM image of PVA nanofiber (a) before and after solvent vapor treatment with (b) DMF, (c) methanol, and (d) DMSO at a temperature of 40 °C for 8 h, and (e) Young's modulus and tensile strength of PVA nanofiber mats with various solvent types at a temperature of 40 °C for 4 h.

    Article Snippet: Solvents used for vapor treatment include dimethyl sulfoxide (DMSO), N, N-dimethyl formamide (DMF), and methanol, which were purchased from Merck, Germany.

    Techniques:

    DSC curve of (a) PVA-NF-untreated, (b) PVA-NF-DMF-treated, (c) PVA-NF-methanol treated, and (d) PVA-NF-DMSO treated PVA nanofiber mats at a heating rate of 10 °C/minutes.

    Journal: Heliyon

    Article Title: Solvent vapor treatment improves mechanical strength of electrospun polyvinyl alcohol nanofibers

    doi: 10.1016/j.heliyon.2018.e00592

    Figure Lengend Snippet: DSC curve of (a) PVA-NF-untreated, (b) PVA-NF-DMF-treated, (c) PVA-NF-methanol treated, and (d) PVA-NF-DMSO treated PVA nanofiber mats at a heating rate of 10 °C/minutes.

    Article Snippet: Solvents used for vapor treatment include dimethyl sulfoxide (DMSO), N, N-dimethyl formamide (DMF), and methanol, which were purchased from Merck, Germany.

    Techniques:

    Comparison of CFZ and CFZ analog 568: structures, precipitation assay, and absorbance profiles ( a ) The structural difference between CFZ and analog 568 at the tertiary amine is a specific substitution of the isopropyl group with a 2-hydroxyethyl. ( b ) The absorbance profiles (270-550nm) show the similarity of CFZ and analog 568 free base and hydrochloride salt forms, respectively. ( c ) The ability of both CFZ and analog 568 to precipitate as hydrochloride salt in simulated lysosomal conditions (pH 4.5). This was determined by measuring the absorbance (285nm) in different conditions: Soln A (no chloride), Soln B (100mM chloride), and DMSO (red = CFZ, blue = 568). ( d ) Hydrochloride salt precipitation in the presence of chloride (Soln B) was verified by brightfield (BF) and fluorescence microscopy (F cy5 ). Scale bar = 50μm.

    Journal: The Journal of investigative dermatology

    Article Title: The Physicochemical Basis of Clofazimine-Induced Skin Pigmentation

    doi: 10.1016/j.jid.2017.09.031

    Figure Lengend Snippet: Comparison of CFZ and CFZ analog 568: structures, precipitation assay, and absorbance profiles ( a ) The structural difference between CFZ and analog 568 at the tertiary amine is a specific substitution of the isopropyl group with a 2-hydroxyethyl. ( b ) The absorbance profiles (270-550nm) show the similarity of CFZ and analog 568 free base and hydrochloride salt forms, respectively. ( c ) The ability of both CFZ and analog 568 to precipitate as hydrochloride salt in simulated lysosomal conditions (pH 4.5). This was determined by measuring the absorbance (285nm) in different conditions: Soln A (no chloride), Soln B (100mM chloride), and DMSO (red = CFZ, blue = 568). ( d ) Hydrochloride salt precipitation in the presence of chloride (Soln B) was verified by brightfield (BF) and fluorescence microscopy (F cy5 ). Scale bar = 50μm.

    Article Snippet: To synthesize the hydrochloride salt crystals for CFZ and 568, 7mM drug solution in dimethyl sulfoxide (DMSO) (67-68-5, Fisher Scientific, Fair Lawn, NJ) was added to 1M NH4 Cl in 1:1 (v/v) ratio and left for 24-48 hours at room temperature in the dark.

    Techniques: Fluorescence, Microscopy

    Viability assay of cysticerci treated with 50 and 500 μM FCF . Viability was analyzed by SYTOX green. (a) Quantification of RFUs of cells treated with DMSO control or FCF (50 or 500 μ M) compared with that of the dead control cells. (b) Microscopic analysis of parasites incubated with SYTOX green after FCF exposure. Scale bars represent 500 μ m. Bright-field images are shown in Supplementary Figure S4 .

    Journal: Journal of Parasitology Research

    Article Title: In Vitro Analyses Reveal the Effect of Synthetic Cytokinin Forchlorfenuron (FCF) on a Septin-Like Protein of Taeniid Cysticerci

    doi: 10.1155/2019/8578936

    Figure Lengend Snippet: Viability assay of cysticerci treated with 50 and 500 μM FCF . Viability was analyzed by SYTOX green. (a) Quantification of RFUs of cells treated with DMSO control or FCF (50 or 500 μ M) compared with that of the dead control cells. (b) Microscopic analysis of parasites incubated with SYTOX green after FCF exposure. Scale bars represent 500 μ m. Bright-field images are shown in Supplementary Figure S4 .

    Article Snippet: For establishing the visual and quantitative effects of FCF on the viability of the cysticerci, we used 5 μ M of a commercial fluorescent dead cell stain, SYTOX Green Nucleic Acid Stain (S7020; Thermo-Fisher Scientific, Waltham, MA, USA), according to the recommendations of the manufacturer.

    Techniques: Viability Assay, Incubation

    NFATc1 controls Nod1 mRNA expression in macrophages. (A) Representative reverse transcription-PCR of the inhibition of NFATc1 in BMMs transfected with a multiple set (n = 4) of NFATc1 a–d siRNAs compared to non-transfected BMMS or with cells transfected with a negative control (Control) siRNA. GAPDH mRNA expression was used as internal control. (B and C) Fold variation of Nod1 and Nod2 mRNAs measured by quantitative real time PCR in BMMs transfected with the set of NFATc1 a–d siRNAs, or with a negative control (Control) siRNA and compared to non-transfected BMMs (B), and in BMMs incubated with or without 1 µM 11R-VIVIT for 48 h (C) (n = 3 independent experiments in each condition tested). (D) Nucleo-cytoplasmic distribution of the NFATc1 immunostaining (shown in red) (left panel) and percentage of NFATc1 immunostaining co-localized with Sytox green nuclear acid staining ( n = 7–13 nuclei analyzed for each condition from two separate experiments) (right panel) in WT BMMs sequentially incubated without or with 11R-VIVIT or 10 −7 M CsA for 48 h, then without or with 2 µM ionomycin for additional 60 min. Bar = 10 µm. (E) Fold variation of Nod1 and Nod2 mRNAs expression over corresponding β-actin mRNA measured by quantitative real-time PCR in WT BMMs incubated or not with 11R-VIVIT or CsA for 48 h, then with or without 2 µM ionomycin. ( n = 3 independent experiments). *, p

    Journal: PLoS Pathogens

    Article Title: Cyclosporine A Impairs Nucleotide Binding Oligomerization Domain (Nod1)-Mediated Innate Antibacterial Renal Defenses in Mice and Human Transplant Recipients

    doi: 10.1371/journal.ppat.1003152

    Figure Lengend Snippet: NFATc1 controls Nod1 mRNA expression in macrophages. (A) Representative reverse transcription-PCR of the inhibition of NFATc1 in BMMs transfected with a multiple set (n = 4) of NFATc1 a–d siRNAs compared to non-transfected BMMS or with cells transfected with a negative control (Control) siRNA. GAPDH mRNA expression was used as internal control. (B and C) Fold variation of Nod1 and Nod2 mRNAs measured by quantitative real time PCR in BMMs transfected with the set of NFATc1 a–d siRNAs, or with a negative control (Control) siRNA and compared to non-transfected BMMs (B), and in BMMs incubated with or without 1 µM 11R-VIVIT for 48 h (C) (n = 3 independent experiments in each condition tested). (D) Nucleo-cytoplasmic distribution of the NFATc1 immunostaining (shown in red) (left panel) and percentage of NFATc1 immunostaining co-localized with Sytox green nuclear acid staining ( n = 7–13 nuclei analyzed for each condition from two separate experiments) (right panel) in WT BMMs sequentially incubated without or with 11R-VIVIT or 10 −7 M CsA for 48 h, then without or with 2 µM ionomycin for additional 60 min. Bar = 10 µm. (E) Fold variation of Nod1 and Nod2 mRNAs expression over corresponding β-actin mRNA measured by quantitative real-time PCR in WT BMMs incubated or not with 11R-VIVIT or CsA for 48 h, then with or without 2 µM ionomycin. ( n = 3 independent experiments). *, p

    Article Snippet: Indirect immunofluorescence studies were performed on WT BMMs using a mouse anti-NFATc1 monoclonal antibody (Thermo Scientific Pierce Antibodies) and Sytox green nucleic acid stain (Invitrogen).

    Techniques: Expressing, Polymerase Chain Reaction, Inhibition, Transfection, Negative Control, Real-time Polymerase Chain Reaction, Incubation, Immunostaining, Staining

    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

    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

    Disease-associated mutations increase temperature activation of TRPM3. HEK293 cells were transfected with the human TRPM3α2, or its mutants; fura-2 Ca 2+ imaging experiments were performed as described in the Materials and methods section. ( A-C ) Averaged fluorescence ratio traces (340 nm/380 nm) for all PregS-responsive cells from one coverslip in cells expressing TRPM3 ( A ), V992M ( B ) and P1092Q ( C ). The cells were first stimulated by increasing the temperature to 37°C, followed by 10 μM primidone at room temperature to facilitate return of Ca 2+ to baseline, finally 25 μM PregS was applied. ( D ) The change in 340/380 ratio induced by 37°C expressed as a fraction of the response to 25 μM PregS. ( E ) 340/380 ratios at baseline, in response to 37°C and in response to 25 μM PregS. Each symbol represents the average value from all PregS-responsive cells from one coverslip, lines connect data points from the same coverslip. Each coverslips had around 70–80 PregS-responsive cells in the WT group; 35–45 for P1092Q, and 15–25 for V992M. Data were collected from three independent transfections.

    Journal: eLife

    Article Title: Disease-associated mutations in the human TRPM3 render the channel overactive via two distinct mechanisms

    doi: 10.7554/eLife.55634

    Figure Lengend Snippet: Disease-associated mutations increase temperature activation of TRPM3. HEK293 cells were transfected with the human TRPM3α2, or its mutants; fura-2 Ca 2+ imaging experiments were performed as described in the Materials and methods section. ( A-C ) Averaged fluorescence ratio traces (340 nm/380 nm) for all PregS-responsive cells from one coverslip in cells expressing TRPM3 ( A ), V992M ( B ) and P1092Q ( C ). The cells were first stimulated by increasing the temperature to 37°C, followed by 10 μM primidone at room temperature to facilitate return of Ca 2+ to baseline, finally 25 μM PregS was applied. ( D ) The change in 340/380 ratio induced by 37°C expressed as a fraction of the response to 25 μM PregS. ( E ) 340/380 ratios at baseline, in response to 37°C and in response to 25 μM PregS. Each symbol represents the average value from all PregS-responsive cells from one coverslip, lines connect data points from the same coverslip. Each coverslips had around 70–80 PregS-responsive cells in the WT group; 35–45 for P1092Q, and 15–25 for V992M. Data were collected from three independent transfections.

    Article Snippet: HEK293 cells were cultured in MEM supplemented with 10% FBS and 100 IU/ml penicillin plus 100 µg/ml streptomycin in 5% CO2 at 37°C.

    Techniques: Activation Assay, Transfection, Imaging, Fluorescence, Expressing

    PregS responses of wild type and mutant TRPM3 at 37°C. HEK293 cells were transfected with the Ca 2+ indicator GCaMP6f and the hTRPM3α2 or its mutants, and fluorescence was measured in a 96-well plate reader (Flexstation-3) as described in the Materials and method section. ( A ) Average traces from one plate (four wells for each condition) for stimulation with different concentrations of PregS for cells expressing wild type TRPM3; at the end of the experiment, 2 μM ionomycin was applied as a normalizing stimulus. ( B ) Hill fit of the PregS concentration response relationship, symbols show values obtained in individual wells n = 8 from two independent transfections. The dashed line shows the fit for the concentration response curve obtained at 21°C from Figure 1D . ( C-D ) Identical experiments to those shown in panel A, on cells expressing the V992M (C) and the P1092Q (D) mutants.

    Journal: eLife

    Article Title: Disease-associated mutations in the human TRPM3 render the channel overactive via two distinct mechanisms

    doi: 10.7554/eLife.55634

    Figure Lengend Snippet: PregS responses of wild type and mutant TRPM3 at 37°C. HEK293 cells were transfected with the Ca 2+ indicator GCaMP6f and the hTRPM3α2 or its mutants, and fluorescence was measured in a 96-well plate reader (Flexstation-3) as described in the Materials and method section. ( A ) Average traces from one plate (four wells for each condition) for stimulation with different concentrations of PregS for cells expressing wild type TRPM3; at the end of the experiment, 2 μM ionomycin was applied as a normalizing stimulus. ( B ) Hill fit of the PregS concentration response relationship, symbols show values obtained in individual wells n = 8 from two independent transfections. The dashed line shows the fit for the concentration response curve obtained at 21°C from Figure 1D . ( C-D ) Identical experiments to those shown in panel A, on cells expressing the V992M (C) and the P1092Q (D) mutants.

    Article Snippet: HEK293 cells were cultured in MEM supplemented with 10% FBS and 100 IU/ml penicillin plus 100 µg/ml streptomycin in 5% CO2 at 37°C.

    Techniques: Mutagenesis, Transfection, Fluorescence, Expressing, Concentration Assay

    Disease-associate mutations increase temperature sensitivity of TRPM3. HEK293 cells were transfected with the human TRPM3α2, or its mutants; whole-cell patch clamp electrophysiology was performed as descried in the Materials and methods section using a ramp protocol from −100 to 100 mV. ( A-C ) Representative measurements, top panels show temperature recordings, bottom panels show currents at 100 mV and −100 mV. The applications of 100 μM PregS are indicated by the horizontal lines. ( D-F ) The heat-induced current amplitudes at 100 mV were normalized to the currents induced by PregS and plotted as a function of the temperature from the same data presented in panels A-C. ( G ) Summary of the slopes of the current increases between 23°C and 33°C determined from linear fits from panels D-F. ( H ) Summary of current amplitudes at 100 and −100 mV induced by increasing the temperature to 25°C, 30°C and 35°C as well as in response to PregS.

    Journal: eLife

    Article Title: Disease-associated mutations in the human TRPM3 render the channel overactive via two distinct mechanisms

    doi: 10.7554/eLife.55634

    Figure Lengend Snippet: Disease-associate mutations increase temperature sensitivity of TRPM3. HEK293 cells were transfected with the human TRPM3α2, or its mutants; whole-cell patch clamp electrophysiology was performed as descried in the Materials and methods section using a ramp protocol from −100 to 100 mV. ( A-C ) Representative measurements, top panels show temperature recordings, bottom panels show currents at 100 mV and −100 mV. The applications of 100 μM PregS are indicated by the horizontal lines. ( D-F ) The heat-induced current amplitudes at 100 mV were normalized to the currents induced by PregS and plotted as a function of the temperature from the same data presented in panels A-C. ( G ) Summary of the slopes of the current increases between 23°C and 33°C determined from linear fits from panels D-F. ( H ) Summary of current amplitudes at 100 and −100 mV induced by increasing the temperature to 25°C, 30°C and 35°C as well as in response to PregS.

    Article Snippet: HEK293 cells were cultured in MEM supplemented with 10% FBS and 100 IU/ml penicillin plus 100 µg/ml streptomycin in 5% CO2 at 37°C.

    Techniques: Transfection, Patch Clamp

    Primidone inhibits Ca 2+ responses induced by EC 50 concentrations of PregS. HEK293 cells were transfected with the Ca 2+ indicator GCaMP6f and the hTRPM3α2 or its mutants, and fluorescence was measured in a 96-well plate reader (Flexstation-3) at room temperature (~21°C) as described in the Materials and method section. ( A-C ) Cells were stimulated by PregS at its EC 50 concentration for each construct, as indicated by the first arrow, then various concentrations of primidone were applied (second arrow). ( D ) Hill1 fits of the concentration dependence of primidone; symbols show mean ± SEM from five or six wells, from two independent transfections. The IC 50 values were 2.37 ± 0.39 μM for wild-type channels, 8.62 ± 1.42 μM for V992M and 3.52 ± 1.13 μM for P1092Q.

    Journal: eLife

    Article Title: Disease-associated mutations in the human TRPM3 render the channel overactive via two distinct mechanisms

    doi: 10.7554/eLife.55634

    Figure Lengend Snippet: Primidone inhibits Ca 2+ responses induced by EC 50 concentrations of PregS. HEK293 cells were transfected with the Ca 2+ indicator GCaMP6f and the hTRPM3α2 or its mutants, and fluorescence was measured in a 96-well plate reader (Flexstation-3) at room temperature (~21°C) as described in the Materials and method section. ( A-C ) Cells were stimulated by PregS at its EC 50 concentration for each construct, as indicated by the first arrow, then various concentrations of primidone were applied (second arrow). ( D ) Hill1 fits of the concentration dependence of primidone; symbols show mean ± SEM from five or six wells, from two independent transfections. The IC 50 values were 2.37 ± 0.39 μM for wild-type channels, 8.62 ± 1.42 μM for V992M and 3.52 ± 1.13 μM for P1092Q.

    Article Snippet: HEK293 cells were cultured in MEM supplemented with 10% FBS and 100 IU/ml penicillin plus 100 µg/ml streptomycin in 5% CO2 at 37°C.

    Techniques: Transfection, Fluorescence, Concentration Assay, Construct

    Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, DEX, and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and DMSO were assigned a value of 1.

    Journal: Drug metabolism and pharmacokinetics

    Article Title: An Efficient Method for Differentiation of Human Induced Pluripotent Stem Cells into Hepatocyte-like Cells Retaining Drug Metabolizing Activity

    doi:

    Figure Lengend Snippet: Effects of drugs on testosterone 6 β -hydroxylase activity in hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, DEX, and RIF for 72 h and then cultured with the medium containing testosterone for 6h. 6 β -Hydroxytestosterone was analyzed using liquid chromatography coupled with tandem mass spectrometry as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. The graphs represent the relative activity ratios when the value in the hepatocyte-like cells using collagen I and DMSO were assigned a value of 1.

    Article Snippet: Oncostatin M (OSM), dexa-methasone (DEX), omeprazole (OME), rifampicin (RIF), dimethyl sulfoxide (DMSO), and human normal adult liver total RNA, derived from a 64-year-old male donor, were obtained from Wako Pure Chemicals (Osaka, Japan).

    Techniques: Activity Assay, Cell Culture, Liquid Chromatography, Mass Spectrometry

    Effects of drugs on expression of CYP3A enzymes and UGT1A1 mRNAs in the hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, DEX, and RIF for 72 h. The total mRNA was extracted from the cells. The expression of CYP3A and UGT1A1 mRNAs were analyzed by microarray analysis as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. Values were normalized to the levels of GAPDH mRNA. The graphs represent the relative gene expression level when the levels in the hepatocyte-like cells using collagen I and DMSO were assigned a value of 1.

    Journal: Drug metabolism and pharmacokinetics

    Article Title: An Efficient Method for Differentiation of Human Induced Pluripotent Stem Cells into Hepatocyte-like Cells Retaining Drug Metabolizing Activity

    doi:

    Figure Lengend Snippet: Effects of drugs on expression of CYP3A enzymes and UGT1A1 mRNAs in the hepatocyte-like cells The cells differentiated from human iPS cells (Fetch) were treated with OME, DEX, and RIF for 72 h. The total mRNA was extracted from the cells. The expression of CYP3A and UGT1A1 mRNAs were analyzed by microarray analysis as described in Materials and Methods. Each bar represents the mean ± SD from triplicate experiments. Values were normalized to the levels of GAPDH mRNA. The graphs represent the relative gene expression level when the levels in the hepatocyte-like cells using collagen I and DMSO were assigned a value of 1.

    Article Snippet: Oncostatin M (OSM), dexa-methasone (DEX), omeprazole (OME), rifampicin (RIF), dimethyl sulfoxide (DMSO), and human normal adult liver total RNA, derived from a 64-year-old male donor, were obtained from Wako Pure Chemicals (Osaka, Japan).

    Techniques: Expressing, Microarray

    The combination of LCRF‐0006 and bortezomib synergistically increases MM tumor response in vivo. A, Schematic representation of treatment regimen. C57BL/KaLwRij mice with established MM (day 14 post‐5TGM1 cell injection) were treated with LCRF‐0006 (100 mg/kg) and bortezomib (0.5 mg/kg) (LCRF‐0006 + bortezomib), LCRF‐0006 and DMSO vehicle (LCRF‐0006), 2‐HP‐b‐CD vehicle and bortezomib (bortezomib) or 2‐HP‐b‐CD and DMSO vehicles (vehicles) i.p., as per treatment regimen. B, Tumor burden was assessed at day 14, 21 and 28 by BLI. Graph depicts mean ± SEM. n = 5‐6 mice/treatment group. *** P

    Journal: FASEB BioAdvances

    Article Title: LCRF‐0006, a small molecule mimetic of the N‐cadherin antagonist peptide ADH‐1, synergistically increases multiple myeloma response to bortezomib, et al. LCRF‐0006, a small molecule mimetic of the N‐cadherin antagonist peptide ADH‐1, synergistically increases multiple myeloma response to bortezomib

    doi: 10.1096/fba.2019-00073

    Figure Lengend Snippet: The combination of LCRF‐0006 and bortezomib synergistically increases MM tumor response in vivo. A, Schematic representation of treatment regimen. C57BL/KaLwRij mice with established MM (day 14 post‐5TGM1 cell injection) were treated with LCRF‐0006 (100 mg/kg) and bortezomib (0.5 mg/kg) (LCRF‐0006 + bortezomib), LCRF‐0006 and DMSO vehicle (LCRF‐0006), 2‐HP‐b‐CD vehicle and bortezomib (bortezomib) or 2‐HP‐b‐CD and DMSO vehicles (vehicles) i.p., as per treatment regimen. B, Tumor burden was assessed at day 14, 21 and 28 by BLI. Graph depicts mean ± SEM. n = 5‐6 mice/treatment group. *** P

    Article Snippet: 2.2 Drugs For in vitro experiments, LCRF‐0006 (kindly provided by Crocus Laboratories) was solubilized in dimethyl sulfoxide (DMSO) (Merck).

    Techniques: In Vivo, Mouse Assay, Injection

    Effect of E3330-amide on APE1’s melting temperature as measured by DSF. APE1 was titrated with increasing concentrations of E3330-amide dissolved in DMSO (16 μM – 4 mM) in the presence and absence of 1 mM Mg 2+ . SYPRO Orange dye was then added, and T m measurements were obtained by DSF. The resulting T m of APE1 was plotted versus the concentration of E3330-amide in either the presence or absence of 1 mM Mg 2+ . Increasing concentrations of E3330-amide did not produce a change in the T m of APE1.

    Journal: Biochemistry

    Article Title: Inhibition of Apurinic/apyrimidinic endonuclease I's redox activity revisited

    doi: 10.1021/bi400179m

    Figure Lengend Snippet: Effect of E3330-amide on APE1’s melting temperature as measured by DSF. APE1 was titrated with increasing concentrations of E3330-amide dissolved in DMSO (16 μM – 4 mM) in the presence and absence of 1 mM Mg 2+ . SYPRO Orange dye was then added, and T m measurements were obtained by DSF. The resulting T m of APE1 was plotted versus the concentration of E3330-amide in either the presence or absence of 1 mM Mg 2+ . Increasing concentrations of E3330-amide did not produce a change in the T m of APE1.

    Article Snippet: Reactions were carried out in 100 mM HEPES pH 7.0, 150 mM NaCl, and 4x SYPRO orange (Invitrogen Cat # S6651)/0.08% DMSO.

    Techniques: Concentration Assay

    Effect of E3330 on APE1’s melting temperature in the presence and absence of Mg 2+ as measured by DSF. APE1 was titrated with increasing concentrations of E3330 dissolved in DMSO (10 μM-1 mM) in the presence and absence of 1 mM Mg 2+ . SYPRO Orange dye was then added and T m measurements were obtained by DSF. The resulting T m of APE1 was plotted versus the concentration of E3330 in either the presence or absence of 1 mM Mg 2+ . Increasing concentrations of E3330 resulted in decreased APE1 melting temperatures in both the presence and absence of Mg 2+ .

    Journal: Biochemistry

    Article Title: Inhibition of Apurinic/apyrimidinic endonuclease I's redox activity revisited

    doi: 10.1021/bi400179m

    Figure Lengend Snippet: Effect of E3330 on APE1’s melting temperature in the presence and absence of Mg 2+ as measured by DSF. APE1 was titrated with increasing concentrations of E3330 dissolved in DMSO (10 μM-1 mM) in the presence and absence of 1 mM Mg 2+ . SYPRO Orange dye was then added and T m measurements were obtained by DSF. The resulting T m of APE1 was plotted versus the concentration of E3330 in either the presence or absence of 1 mM Mg 2+ . Increasing concentrations of E3330 resulted in decreased APE1 melting temperatures in both the presence and absence of Mg 2+ .

    Article Snippet: Reactions were carried out in 100 mM HEPES pH 7.0, 150 mM NaCl, and 4x SYPRO orange (Invitrogen Cat # S6651)/0.08% DMSO.

    Techniques: Concentration Assay

    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