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  • siha  (ATCC)
    99
    ATCC siha
    USP13 and Mcl-1 expression correlate in cervical cancer. A) Representative western blot of Mcl-1 expression in normal human keratinocytes (NHKs), HPV-C33A cells, HPV16+ <t>SiHa</t> and CaSKi cells and <t>HPV18+</t> SW756 and HeLa cells. GAPDH served as a loading control. Quantification of the protein band intensities are shown on the right. B) Representative immunohistochemical (IHC) staining of Mcl-1 expression in cervical cancer tissues and normal cervical epithelium from a tissue microarray (TMA). Scale bars, 10025FBμm. C) Scatter dot plot analysis of Mcl-1 expression from a larger cohort of cervical cancer cases (n=41) and normal cervical epithelium (n=9) is shown on the right. D) Representative immunohistochemical (IHC) staining of USP13 and Mcl-1 expression in cervical cancer tissue from two patients. Staining was performed from separate cores from the same patient samples. Scale bars, 10025FBμm. Correlation was determined using Spearman’s analysis and is shown on the right. * p
    Siha, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1073 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore xylenol orange
    USP13 and Mcl-1 expression correlate in cervical cancer. A) Representative western blot of Mcl-1 expression in normal human keratinocytes (NHKs), HPV-C33A cells, HPV16+ <t>SiHa</t> and CaSKi cells and <t>HPV18+</t> SW756 and HeLa cells. GAPDH served as a loading control. Quantification of the protein band intensities are shown on the right. B) Representative immunohistochemical (IHC) staining of Mcl-1 expression in cervical cancer tissues and normal cervical epithelium from a tissue microarray (TMA). Scale bars, 10025FBμm. C) Scatter dot plot analysis of Mcl-1 expression from a larger cohort of cervical cancer cases (n=41) and normal cervical epithelium (n=9) is shown on the right. D) Representative immunohistochemical (IHC) staining of USP13 and Mcl-1 expression in cervical cancer tissue from two patients. Staining was performed from separate cores from the same patient samples. Scale bars, 10025FBμm. Correlation was determined using Spearman’s analysis and is shown on the right. * p
    Xylenol Orange, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 420 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    MatTek 35 mm glass bottom dishes
    Distribution of extracellular PS in cells expressing EBOV proteins. Vero-E6 cells grown on <t>35-mm</t> glass bottom dishes were transfected with the expression plasmids of mCherry-VP40 and wtVP40 at a ratio of 1:5 (a), GP alone (b), mCherry-VP40 and wtVP40 with GP (c), or wtVP40 and GP (d). At 48 h.p.t., the cells were harvested followed by AF-ANX V staining. For detection of GP, the cells were incubated in the medium containing the anti-GP antibody, followed by incubation with Alexa Fluor 647-conjugated secondary antibody. After being washed with medium and ANX V binging buffer, the cells were treated with AF-ANX V. After washing again, the AF-ANX V signal (green) and EBOV proteins were observed by using a confocal microscope. Individual viral proteins are shown in magenta (a, b, and d). In panel (c), mCherry-VP40 and GP are shown in magenta and cyan, respectively. As a control, a backbone plasmid was transfected (e). Panel (f) represents Vero-E6 cells treated with 1 μM STS for 6 h. The nuclei (blue) were counterstained with Hoechst 33342. Insets show the boxed areas. The plots indicate the individual fluorescence intensity along each of the corresponding lines. A.U.; arbitrary unit. Scale bars in the large panels: 10 μm.
    35 Mm Glass Bottom Dishes, supplied by MatTek, used in various techniques. Bioz Stars score: 94/100, based on 2049 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Carl Zeiss axiovert 35 microscope
    Distribution of extracellular PS in cells expressing EBOV proteins. Vero-E6 cells grown on <t>35-mm</t> glass bottom dishes were transfected with the expression plasmids of mCherry-VP40 and wtVP40 at a ratio of 1:5 (a), GP alone (b), mCherry-VP40 and wtVP40 with GP (c), or wtVP40 and GP (d). At 48 h.p.t., the cells were harvested followed by AF-ANX V staining. For detection of GP, the cells were incubated in the medium containing the anti-GP antibody, followed by incubation with Alexa Fluor 647-conjugated secondary antibody. After being washed with medium and ANX V binging buffer, the cells were treated with AF-ANX V. After washing again, the AF-ANX V signal (green) and EBOV proteins were observed by using a confocal microscope. Individual viral proteins are shown in magenta (a, b, and d). In panel (c), mCherry-VP40 and GP are shown in magenta and cyan, respectively. As a control, a backbone plasmid was transfected (e). Panel (f) represents Vero-E6 cells treated with 1 μM STS for 6 h. The nuclei (blue) were counterstained with Hoechst 33342. Insets show the boxed areas. The plots indicate the individual fluorescence intensity along each of the corresponding lines. A.U.; arbitrary unit. Scale bars in the large panels: 10 μm.
    Axiovert 35 Microscope, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 93/100, based on 1446 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare α 35 s datp
    Distribution of extracellular PS in cells expressing EBOV proteins. Vero-E6 cells grown on <t>35-mm</t> glass bottom dishes were transfected with the expression plasmids of mCherry-VP40 and wtVP40 at a ratio of 1:5 (a), GP alone (b), mCherry-VP40 and wtVP40 with GP (c), or wtVP40 and GP (d). At 48 h.p.t., the cells were harvested followed by AF-ANX V staining. For detection of GP, the cells were incubated in the medium containing the anti-GP antibody, followed by incubation with Alexa Fluor 647-conjugated secondary antibody. After being washed with medium and ANX V binging buffer, the cells were treated with AF-ANX V. After washing again, the AF-ANX V signal (green) and EBOV proteins were observed by using a confocal microscope. Individual viral proteins are shown in magenta (a, b, and d). In panel (c), mCherry-VP40 and GP are shown in magenta and cyan, respectively. As a control, a backbone plasmid was transfected (e). Panel (f) represents Vero-E6 cells treated with 1 μM STS for 6 h. The nuclei (blue) were counterstained with Hoechst 33342. Insets show the boxed areas. The plots indicate the individual fluorescence intensity along each of the corresponding lines. A.U.; arbitrary unit. Scale bars in the large panels: 10 μm.
    α 35 S Datp, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 494 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Millipore aβ25 35
    NGF defends against <t>Aβ25–35‐triggered</t> neuronal toxicity in SKNSH cells. (A) Twenty‐four‐hour incubation was conducted using various Aβ25–35 concentrations. Scale bars: 100 nm. (B) Cells received supplementation with Aβ25–35 (25 μ m ) for the indicated time. (C) Cells received supplementation with NGF at the particular concentrations for 24 h. (D, E) Cells received preliminary NGF supplementation (0, 25, 50, or 100 ng·mL −1 ) for 24 h before the addition of 25 μ m Aβ25–35. Survival was evaluated using a CCK‐8 assay in SKNSH cells (D) and primary neurons (E). Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, * P
    Aβ25 35, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 429 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    ADInstruments powerlab 8 35
    NGF defends against <t>Aβ25–35‐triggered</t> neuronal toxicity in SKNSH cells. (A) Twenty‐four‐hour incubation was conducted using various Aβ25–35 concentrations. Scale bars: 100 nm. (B) Cells received supplementation with Aβ25–35 (25 μ m ) for the indicated time. (C) Cells received supplementation with NGF at the particular concentrations for 24 h. (D, E) Cells received preliminary NGF supplementation (0, 25, 50, or 100 ng·mL −1 ) for 24 h before the addition of 25 μ m Aβ25–35. Survival was evaluated using a CCK‐8 assay in SKNSH cells (D) and primary neurons (E). Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, * P
    Powerlab 8 35, supplied by ADInstruments, used in various techniques. Bioz Stars score: 91/100, based on 189 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher 35 mm petri dishes
    NGF defends against <t>Aβ25–35‐triggered</t> neuronal toxicity in SKNSH cells. (A) Twenty‐four‐hour incubation was conducted using various Aβ25–35 concentrations. Scale bars: 100 nm. (B) Cells received supplementation with Aβ25–35 (25 μ m ) for the indicated time. (C) Cells received supplementation with NGF at the particular concentrations for 24 h. (D, E) Cells received preliminary NGF supplementation (0, 25, 50, or 100 ng·mL −1 ) for 24 h before the addition of 25 μ m Aβ25–35. Survival was evaluated using a CCK‐8 assay in SKNSH cells (D) and primary neurons (E). Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, * P
    35 Mm Petri Dishes, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 270 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Anatrace amphipol a8 35
    Reconstitution of full-length VanS A with the <t>amphipol</t> <t>A8-35.</t> (A) Size-exclusion chromatogram of amphipol-reconstituted VanS A , demonstrating the presence of a single soluble and homogeneous species. (B) Comparison of autophosphorylation activity for VanS A in detergent solution vs. amphipols. The amphipol-reconstituted species exhibits substantially higher enzymatic activity. This is demonstrated in the anti-6xHis loading control, which shows that small amounts of the protein-plus-amphipol solution give essentially equivalent activity to much larger amounts of the detergent-solubilized protein. (C) 50 μM vancomycin has no effect on the autophosphorylation activity of amphipol-reconstituted VanS A . (D) (E) 50 μM vancomycin has no effect on the phosphatase activity of amphipol-reconstituted VanS A . Panel (D) shows a representative Phos-tag gel, with panel (E) showing the quantification of assays involving three independent sets of measurements.
    Amphipol A8 35, supplied by Anatrace, used in various techniques. Bioz Stars score: 89/100, based on 157 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Carl Zeiss axiovert 35 inverted microscope
    Reconstitution of full-length VanS A with the <t>amphipol</t> <t>A8-35.</t> (A) Size-exclusion chromatogram of amphipol-reconstituted VanS A , demonstrating the presence of a single soluble and homogeneous species. (B) Comparison of autophosphorylation activity for VanS A in detergent solution vs. amphipols. The amphipol-reconstituted species exhibits substantially higher enzymatic activity. This is demonstrated in the anti-6xHis loading control, which shows that small amounts of the protein-plus-amphipol solution give essentially equivalent activity to much larger amounts of the detergent-solubilized protein. (C) 50 μM vancomycin has no effect on the autophosphorylation activity of amphipol-reconstituted VanS A . (D) (E) 50 μM vancomycin has no effect on the phosphatase activity of amphipol-reconstituted VanS A . Panel (D) shows a representative Phos-tag gel, with panel (E) showing the quantification of assays involving three independent sets of measurements.
    Axiovert 35 Inverted Microscope, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 90/100, based on 365 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore monoclonal anti splicing factor sc 35 antibody
    SRRM4 promotes the inclusion of the alternative microexon 34ʹ in TAF1 mRNA. Immunoblot (A) and immunofluorescence (B) analysis of Flp-In T-REx derivatives of HeLa cells expressing GFP-SRRM4. Transgene expression is verified after DOX induction for 24 h. GFP-SRRM4 is enriched in the nuclear fraction (NXT). Histone H3 was used as nuclear marker while cytoplasmic extract (CXT) was verified using α-tubulin (C). GFP-SRRM4 resides within the nuclear speckles as revealed by <t>SRSF2</t> co-staining (D). Scale bars in panels B and D are 10 µm. RT-PCR analysis demonstrated the progressive incorporation of microexon 34ʹ in TAF1 mRNA during SRRM4 induction time curve. Plasmids containing cTAF1 and TAF1-34ʹ were used as size-specific controls. The quantified PSI is depicted below each time lane (E). SRRM4 protein expression correlates with microexon 34ʹ incorporation (F). RNA-seq data from N2a knockdown (KD) experiments and from the Srrm4 knockout model (Srrm4 Δ7−8/Δ7−8 ) are depicted in panel G and H, respectively. cRPKM indicates corrected reads per kilo base per million mapped reads.
    Monoclonal Anti Splicing Factor Sc 35 Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 265 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Prospec il 35
    SRRM4 promotes the inclusion of the alternative microexon 34ʹ in TAF1 mRNA. Immunoblot (A) and immunofluorescence (B) analysis of Flp-In T-REx derivatives of HeLa cells expressing GFP-SRRM4. Transgene expression is verified after DOX induction for 24 h. GFP-SRRM4 is enriched in the nuclear fraction (NXT). Histone H3 was used as nuclear marker while cytoplasmic extract (CXT) was verified using α-tubulin (C). GFP-SRRM4 resides within the nuclear speckles as revealed by <t>SRSF2</t> co-staining (D). Scale bars in panels B and D are 10 µm. RT-PCR analysis demonstrated the progressive incorporation of microexon 34ʹ in TAF1 mRNA during SRRM4 induction time curve. Plasmids containing cTAF1 and TAF1-34ʹ were used as size-specific controls. The quantified PSI is depicted below each time lane (E). SRRM4 protein expression correlates with microexon 34ʹ incorporation (F). RNA-seq data from N2a knockdown (KD) experiments and from the Srrm4 knockout model (Srrm4 Δ7−8/Δ7−8 ) are depicted in panel G and H, respectively. cRPKM indicates corrected reads per kilo base per million mapped reads.
    Il 35, supplied by Prospec, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore cremophor el
    Influence of Taxol® and its constituents paclitaxel and <t>cremophor-EL</t> on the RBC morphology. Increasing concentrations of Taxol® (A), paclitaxel (B), and cremophor-EL (C) were incubated with whole blood (haematocrit 45%) for 60 min at 37°C, and RBC morphology, expressed as morphological index, was assessed by light microscopy. n =6. * P
    Cremophor El, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 102 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    ADInstruments powerlab 4 35
    Influence of Taxol® and its constituents paclitaxel and <t>cremophor-EL</t> on the RBC morphology. Increasing concentrations of Taxol® (A), paclitaxel (B), and cremophor-EL (C) were incubated with whole blood (haematocrit 45%) for 60 min at 37°C, and RBC morphology, expressed as morphological index, was assessed by light microscopy. n =6. * P
    Powerlab 4 35, supplied by ADInstruments, used in various techniques. Bioz Stars score: 89/100, based on 101 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    MatTek 35 mm mattek dishes
    Influence of Taxol® and its constituents paclitaxel and <t>cremophor-EL</t> on the RBC morphology. Increasing concentrations of Taxol® (A), paclitaxel (B), and cremophor-EL (C) were incubated with whole blood (haematocrit 45%) for 60 min at 37°C, and RBC morphology, expressed as morphological index, was assessed by light microscopy. n =6. * P
    35 Mm Mattek Dishes, supplied by MatTek, used in various techniques. Bioz Stars score: 89/100, based on 241 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher brij 35
    Inhibitory zone diameter of nano-formulations of Nano-1-Amp+Brij 35 and Nano-2-Amp+Brij 35. All data were analyzed by Duncan’s multiple range tests using SAS software package. Different letters represented significantly differences at the level of 0.05 (p  ≤  0.05).
    Brij 35, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 201 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Becton Dickinson cd21 35
    BAFF-mediated cellular responses of PKCβ-deficient B cells are altered in vitro and in vivo. (A) B cells from PKCβ +/+ (squares) and PKCβ-deficient (triangles) B cells were cultured in medium alone (open symbols) or in the presence of 25 ng/ml (light gray symbols), 100 ng/ml (dark gray symbols), or 250 ng/ml (closed symbols) of BAFF, and the frequencies of viable B cells were measured by FACS analysis. (B) The cell size of live BAFF-treated PKCβ +/+ (squares) and PKCβ-deficient (triangles) B cells was measured by FACS analysis of the forward scatter (FSC). Symbol shadings represent the same BAFF concentrations as in A. (C) BAFF-R expression on splenic B220-positive cells from PKCβ +/+ (continuous black line) and PKCβ-deficient (dashed black line) was measured by FACS. Gray lines (continuous and dashed) represent staining with an isotype control antibody. (D) Maturity of splenic B cells from PKCβ +/+ (left) and PKCβ-deficient (right) mice was assessed by expression of the surface markers IgD versus IgM (top) and <t>CD21/35</t> versus IgM (bottom). Only live lymphocytes are shown, and the bottom panel is gated on B220-positve cells. Numbers in the top panels represent frequencies of cells in the respective quadrants. Gates in the bottom panels denote B cell developmental stages T1 (IgM hi CD21 lo ), T2 (IgM hi CD21 hi ), and mature (IgM int CD21 int ).
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    99
    Carl Zeiss axio zoom v16
    The effect of NO on tumor growth. CM-Dil labeled glioma cells were injected into the yolk of zebrafish embryos at 2 dpf and incubated with CPTIO (200μM). Images were taken at 1 dpi and 4 dpi. Images (A-A”‘) and (B-B”‘) show the tumors at 1 dpi and 4 dpi for control and CPTIO treated embryo. At 4 dpi, tumors have increased in size in untreated embryos (A”-A”‘) in comparison to CPTIO treated embryos (B”-B”‘). (C) Percentage of fluorescence intensity of the tumor surfaces was determined by ZEN software (n = 10). Images were taken with an <t>Axio</t> zoom <t>V16</t> (Zeiss) macroscope, with the same exposure time for all embryos. Error bars represent SEM, *** p
    Axio Zoom V16, supplied by Carl Zeiss, used in various techniques. Bioz Stars score: 99/100, based on 299 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Thermo Fisher taqman gmo soy 35s detection kit
    The effect of NO on tumor growth. CM-Dil labeled glioma cells were injected into the yolk of zebrafish embryos at 2 dpf and incubated with CPTIO (200μM). Images were taken at 1 dpi and 4 dpi. Images (A-A”‘) and (B-B”‘) show the tumors at 1 dpi and 4 dpi for control and CPTIO treated embryo. At 4 dpi, tumors have increased in size in untreated embryos (A”-A”‘) in comparison to CPTIO treated embryos (B”-B”‘). (C) Percentage of fluorescence intensity of the tumor surfaces was determined by ZEN software (n = 10). Images were taken with an <t>Axio</t> zoom <t>V16</t> (Zeiss) macroscope, with the same exposure time for all embryos. Error bars represent SEM, *** p
    Taqman Gmo Soy 35s Detection Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    ADInstruments powerlab 16 35
    The effect of NO on tumor growth. CM-Dil labeled glioma cells were injected into the yolk of zebrafish embryos at 2 dpf and incubated with CPTIO (200μM). Images were taken at 1 dpi and 4 dpi. Images (A-A”‘) and (B-B”‘) show the tumors at 1 dpi and 4 dpi for control and CPTIO treated embryo. At 4 dpi, tumors have increased in size in untreated embryos (A”-A”‘) in comparison to CPTIO treated embryos (B”-B”‘). (C) Percentage of fluorescence intensity of the tumor surfaces was determined by ZEN software (n = 10). Images were taken with an <t>Axio</t> zoom <t>V16</t> (Zeiss) macroscope, with the same exposure time for all embryos. Error bars represent SEM, *** p
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    Image Search Results


    USP13 and Mcl-1 expression correlate in cervical cancer. A) Representative western blot of Mcl-1 expression in normal human keratinocytes (NHKs), HPV-C33A cells, HPV16+ SiHa and CaSKi cells and HPV18+ SW756 and HeLa cells. GAPDH served as a loading control. Quantification of the protein band intensities are shown on the right. B) Representative immunohistochemical (IHC) staining of Mcl-1 expression in cervical cancer tissues and normal cervical epithelium from a tissue microarray (TMA). Scale bars, 10025FBμm. C) Scatter dot plot analysis of Mcl-1 expression from a larger cohort of cervical cancer cases (n=41) and normal cervical epithelium (n=9) is shown on the right. D) Representative immunohistochemical (IHC) staining of USP13 and Mcl-1 expression in cervical cancer tissue from two patients. Staining was performed from separate cores from the same patient samples. Scale bars, 10025FBμm. Correlation was determined using Spearman’s analysis and is shown on the right. * p

    Journal: bioRxiv

    Article Title: The deubiquitinase (DUB) USP13 promotes Mcl-1 stabilisation in cervical cancer. H( HO(

    doi: 10.1101/2020.07.25.220996

    Figure Lengend Snippet: USP13 and Mcl-1 expression correlate in cervical cancer. A) Representative western blot of Mcl-1 expression in normal human keratinocytes (NHKs), HPV-C33A cells, HPV16+ SiHa and CaSKi cells and HPV18+ SW756 and HeLa cells. GAPDH served as a loading control. Quantification of the protein band intensities are shown on the right. B) Representative immunohistochemical (IHC) staining of Mcl-1 expression in cervical cancer tissues and normal cervical epithelium from a tissue microarray (TMA). Scale bars, 10025FBμm. C) Scatter dot plot analysis of Mcl-1 expression from a larger cohort of cervical cancer cases (n=41) and normal cervical epithelium (n=9) is shown on the right. D) Representative immunohistochemical (IHC) staining of USP13 and Mcl-1 expression in cervical cancer tissue from two patients. Staining was performed from separate cores from the same patient samples. Scale bars, 10025FBμm. Correlation was determined using Spearman’s analysis and is shown on the right. * p

    Article Snippet: Cell cultureHeLa (HPV18+ cervical adenocarcinoma cells), SW756 (HPV18+ cervical squamous carcinoma cells), SiHa (HPV16+ cervical squamous carcinoma cells), CaSKi (HPV16+ cervical squamous carcinoma cells) and C33A (HPV-cervical squamous carcinoma) cells obtained from the ATCC and grown in DMEM supplemented with 10% FBS (ThermoFischer Scientific, USA) and 50 U/mL penicillin.

    Techniques: Expressing, Western Blot, Immunohistochemistry, Staining, Microarray

    USP13 expression is upregulated in pre-malignant cervical disease and cervical cancer. A) Genomic alterations of USP13 across human cancers determined by cBioportal analysis of TCGA data. B) Scatter dot plot analysis of USP13 mRNA expression against USP13 copy number alterations in cervical cancer determined by cBioportal analysis of TCGA data. Correlation was determined using Spearman’s analysis. C) RT-qPCR analysis of USP13 mRNA expression in normal human keratinocytes (NHKs), HPV-C33A cells, HPV16+ SiHa and CaSKi cells and HPV18+ SW756 and HeLa cells. mRNA expression was normalized against U6 mRNA levels. D) Representative western blot of USP13 expression in normal human keratinocytes (NHKs), HPV-C33A cells, HPV16+ SiHa and CaSKi cells and HPV18+ SW756 and HeLa cells. GAPDH served as a loading control. Quantification of the protein band intensities from four biological, independent repeats are shown on the right. E) Representative immunohistochemical (IHC) staining of USP13 expression in cervical cancer tissues and normal cervical epithelium from a tissue microarray (TMA). Scale bars, 10025FBμm. Scatter dot plot analysis of USP13 expression from a larger cohort of cervical cancer cases (n=41) and normal cervical epithelium (n=9) is shown on the right. F) Scatter dot plot of RT-qPCR analysis of USP13 mRNA expression from a panel of cervical cytology samples representing CIN lesions of increasing grade. Five samples from each clinical grade (negative (Neg) and CIN I-III) were analysed and mRNA levels were normalized to the negative samples. Samples were normalized against U6 mRNA levels. G) Representative western blot of cervical cytology samples of CIN lesions of increasing grade analysed for USP13 protein expression. GAPDH served as a loading control. Scatter dot and box plot analysis of a larger cohort of samples (n=15 for each grade) is shown on the right. Bars represent the mean ± standard deviation from at least three biological repeats unless otherwise stated. * p

    Journal: bioRxiv

    Article Title: The deubiquitinase (DUB) USP13 promotes Mcl-1 stabilisation in cervical cancer. H( HO(

    doi: 10.1101/2020.07.25.220996

    Figure Lengend Snippet: USP13 expression is upregulated in pre-malignant cervical disease and cervical cancer. A) Genomic alterations of USP13 across human cancers determined by cBioportal analysis of TCGA data. B) Scatter dot plot analysis of USP13 mRNA expression against USP13 copy number alterations in cervical cancer determined by cBioportal analysis of TCGA data. Correlation was determined using Spearman’s analysis. C) RT-qPCR analysis of USP13 mRNA expression in normal human keratinocytes (NHKs), HPV-C33A cells, HPV16+ SiHa and CaSKi cells and HPV18+ SW756 and HeLa cells. mRNA expression was normalized against U6 mRNA levels. D) Representative western blot of USP13 expression in normal human keratinocytes (NHKs), HPV-C33A cells, HPV16+ SiHa and CaSKi cells and HPV18+ SW756 and HeLa cells. GAPDH served as a loading control. Quantification of the protein band intensities from four biological, independent repeats are shown on the right. E) Representative immunohistochemical (IHC) staining of USP13 expression in cervical cancer tissues and normal cervical epithelium from a tissue microarray (TMA). Scale bars, 10025FBμm. Scatter dot plot analysis of USP13 expression from a larger cohort of cervical cancer cases (n=41) and normal cervical epithelium (n=9) is shown on the right. F) Scatter dot plot of RT-qPCR analysis of USP13 mRNA expression from a panel of cervical cytology samples representing CIN lesions of increasing grade. Five samples from each clinical grade (negative (Neg) and CIN I-III) were analysed and mRNA levels were normalized to the negative samples. Samples were normalized against U6 mRNA levels. G) Representative western blot of cervical cytology samples of CIN lesions of increasing grade analysed for USP13 protein expression. GAPDH served as a loading control. Scatter dot and box plot analysis of a larger cohort of samples (n=15 for each grade) is shown on the right. Bars represent the mean ± standard deviation from at least three biological repeats unless otherwise stated. * p

    Article Snippet: Cell cultureHeLa (HPV18+ cervical adenocarcinoma cells), SW756 (HPV18+ cervical squamous carcinoma cells), SiHa (HPV16+ cervical squamous carcinoma cells), CaSKi (HPV16+ cervical squamous carcinoma cells) and C33A (HPV-cervical squamous carcinoma) cells obtained from the ATCC and grown in DMEM supplemented with 10% FBS (ThermoFischer Scientific, USA) and 50 U/mL penicillin.

    Techniques: Expressing, Quantitative RT-PCR, Western Blot, Immunohistochemistry, Staining, Microarray, Standard Deviation

    Expression study of MDR mRNA and proteins. Expression of LRP and MRP-1 mRNA (a) and proteins (b) was determined by semiquantitative PCR and western blotting respectively. RNA was extracted and PCR was performed with gene specific primers. The PCR products were run in 2% agarose gel. β-actin serves as control for equal loading. The expression of MDR proteins was further confirmed by western blot analysis (b). Cells were lysed and expression of MDR proteins was analysed by respective primary antibodies. A549 cells act as positive control for LRP and MRP-1 expression, while HEK and SIHA serve as negative control for MRP-1 and LRP expression respectively. The results are representative of three independent experiments.

    Journal: PLoS ONE

    Article Title: Folate Decorated Dual Drug Loaded Nanoparticle: Role of Curcumin in Enhancing Therapeutic Potential of Nutlin-3a by Reversing Multidrug Resistance

    doi: 10.1371/journal.pone.0032920

    Figure Lengend Snippet: Expression study of MDR mRNA and proteins. Expression of LRP and MRP-1 mRNA (a) and proteins (b) was determined by semiquantitative PCR and western blotting respectively. RNA was extracted and PCR was performed with gene specific primers. The PCR products were run in 2% agarose gel. β-actin serves as control for equal loading. The expression of MDR proteins was further confirmed by western blot analysis (b). Cells were lysed and expression of MDR proteins was analysed by respective primary antibodies. A549 cells act as positive control for LRP and MRP-1 expression, while HEK and SIHA serve as negative control for MRP-1 and LRP expression respectively. The results are representative of three independent experiments.

    Article Snippet: Y79, A549, HEK293 and SIHA cells were purchased from American Type Culture Collection (ATCC, Manassas, VA) and were grown in RPMI 1640 (Invitrogen, CA, U. S.

    Techniques: Expressing, Polymerase Chain Reaction, Western Blot, Agarose Gel Electrophoresis, Activated Clotting Time Assay, Positive Control, Negative Control

    Distribution of extracellular PS in cells expressing EBOV proteins. Vero-E6 cells grown on 35-mm glass bottom dishes were transfected with the expression plasmids of mCherry-VP40 and wtVP40 at a ratio of 1:5 (a), GP alone (b), mCherry-VP40 and wtVP40 with GP (c), or wtVP40 and GP (d). At 48 h.p.t., the cells were harvested followed by AF-ANX V staining. For detection of GP, the cells were incubated in the medium containing the anti-GP antibody, followed by incubation with Alexa Fluor 647-conjugated secondary antibody. After being washed with medium and ANX V binging buffer, the cells were treated with AF-ANX V. After washing again, the AF-ANX V signal (green) and EBOV proteins were observed by using a confocal microscope. Individual viral proteins are shown in magenta (a, b, and d). In panel (c), mCherry-VP40 and GP are shown in magenta and cyan, respectively. As a control, a backbone plasmid was transfected (e). Panel (f) represents Vero-E6 cells treated with 1 μM STS for 6 h. The nuclei (blue) were counterstained with Hoechst 33342. Insets show the boxed areas. The plots indicate the individual fluorescence intensity along each of the corresponding lines. A.U.; arbitrary unit. Scale bars in the large panels: 10 μm.

    Journal: PLoS Pathogens

    Article Title: Ebola virus requires a host scramblase for externalization of phosphatidylserine on the surface of viral particles

    doi: 10.1371/journal.ppat.1006848

    Figure Lengend Snippet: Distribution of extracellular PS in cells expressing EBOV proteins. Vero-E6 cells grown on 35-mm glass bottom dishes were transfected with the expression plasmids of mCherry-VP40 and wtVP40 at a ratio of 1:5 (a), GP alone (b), mCherry-VP40 and wtVP40 with GP (c), or wtVP40 and GP (d). At 48 h.p.t., the cells were harvested followed by AF-ANX V staining. For detection of GP, the cells were incubated in the medium containing the anti-GP antibody, followed by incubation with Alexa Fluor 647-conjugated secondary antibody. After being washed with medium and ANX V binging buffer, the cells were treated with AF-ANX V. After washing again, the AF-ANX V signal (green) and EBOV proteins were observed by using a confocal microscope. Individual viral proteins are shown in magenta (a, b, and d). In panel (c), mCherry-VP40 and GP are shown in magenta and cyan, respectively. As a control, a backbone plasmid was transfected (e). Panel (f) represents Vero-E6 cells treated with 1 μM STS for 6 h. The nuclei (blue) were counterstained with Hoechst 33342. Insets show the boxed areas. The plots indicate the individual fluorescence intensity along each of the corresponding lines. A.U.; arbitrary unit. Scale bars in the large panels: 10 μm.

    Article Snippet: Vero-E6 cells grown on 35-mm glass bottom dishes were transfected with the expression plasmids of mCherry-VP40 and wtVP40 at a ratio of 1:5 (a), GP alone (b).

    Techniques: Expressing, Transfection, Staining, Incubation, Microscopy, Plasmid Preparation, Fluorescence

    Experimental schema for the OSU rotavirus adsorption assay to leafy vegetables and tomato fruits. Each piece of vegetable leaf or tomato fruit skin was transferred carefully and gently onto the top of a droplet of 300 μl OSU rotavirus solution in PBS on a 35-mm-glass-bottom-dish. The edge effects (viruses might diffuse into the piece through its edge) were avoided by cutting the piece into a smaller disk for later RNA extraction.

    Journal: PLoS ONE

    Article Title: Influence of Epicuticular Physicochemical Properties on Porcine Rotavirus Adsorption to 24 Leafy Green Vegetables and Tomatoes

    doi: 10.1371/journal.pone.0132841

    Figure Lengend Snippet: Experimental schema for the OSU rotavirus adsorption assay to leafy vegetables and tomato fruits. Each piece of vegetable leaf or tomato fruit skin was transferred carefully and gently onto the top of a droplet of 300 μl OSU rotavirus solution in PBS on a 35-mm-glass-bottom-dish. The edge effects (viruses might diffuse into the piece through its edge) were avoided by cutting the piece into a smaller disk for later RNA extraction.

    Article Snippet: Each piece was gently transferred, with a tweezer, onto the top of a droplet of 300 μl diluted porcine rotavirus solution in PBS on a 35-mm-glass-bottom-dish (MatTek Corporation, Ashland, MA).

    Techniques: Adsorption, RNA Extraction

    Effect of Ras on IL-1-induced focal adhesion formation. A , B ) NIH 3T3 cells were plated in 35-mm collagen-coated glass-bottom microwell dishes (MatTek) and treated with transfection reagent and empty vector (Ras +/+ ) or transiently transfected with DN

    Journal: The FASEB Journal

    Article Title: Focal adhesions and Ras are functionally and spatially integrated to mediate IL-1 activation of ERK

    doi: 10.1096/fj.11-183459

    Figure Lengend Snippet: Effect of Ras on IL-1-induced focal adhesion formation. A , B ) NIH 3T3 cells were plated in 35-mm collagen-coated glass-bottom microwell dishes (MatTek) and treated with transfection reagent and empty vector (Ras +/+ ) or transiently transfected with DN

    Article Snippet: NIH 3T3 cells were plated in 35-mm glass-bottom microwell dishes (MatTek Corp., Ashland, MA, USA) and transiently transfected with GFP-H-Ras, K-Ras or N-Ras, respectively.

    Techniques: Transfection, Plasmid Preparation

    NGF defends against Aβ25–35‐triggered neuronal toxicity in SKNSH cells. (A) Twenty‐four‐hour incubation was conducted using various Aβ25–35 concentrations. Scale bars: 100 nm. (B) Cells received supplementation with Aβ25–35 (25 μ m ) for the indicated time. (C) Cells received supplementation with NGF at the particular concentrations for 24 h. (D, E) Cells received preliminary NGF supplementation (0, 25, 50, or 100 ng·mL −1 ) for 24 h before the addition of 25 μ m Aβ25–35. Survival was evaluated using a CCK‐8 assay in SKNSH cells (D) and primary neurons (E). Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, * P

    Journal: FEBS Open Bio

    Article Title: NGF protects neuroblastoma cells against β‐amyloid‐induced apoptosis via the Nrf2/HO‐1 pathway

    doi: 10.1002/2211-5463.12742

    Figure Lengend Snippet: NGF defends against Aβ25–35‐triggered neuronal toxicity in SKNSH cells. (A) Twenty‐four‐hour incubation was conducted using various Aβ25–35 concentrations. Scale bars: 100 nm. (B) Cells received supplementation with Aβ25–35 (25 μ m ) for the indicated time. (C) Cells received supplementation with NGF at the particular concentrations for 24 h. (D, E) Cells received preliminary NGF supplementation (0, 25, 50, or 100 ng·mL −1 ) for 24 h before the addition of 25 μ m Aβ25–35. Survival was evaluated using a CCK‐8 assay in SKNSH cells (D) and primary neurons (E). Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, * P

    Article Snippet: Double‐distilled water was used to dissolve the Aβ25–35 (Sigma, St Louis, MO, USA).

    Techniques: Incubation, CCK-8 Assay

    NGF reduced Aβ25–35‐triggered cell apoptosis in SKNSH cells. SKNSH cells received preliminary supplementation with NGF (100 ng·mL −1 ) for 24 h prior to a 24‐h treatment with Aβ25–35 (25 μ m ). (A) Representative apoptosis depicted by FC. (B, C) Quantification of cell apoptosis in SKNSH cells (B) and primary neurons (C). Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, ** P

    Journal: FEBS Open Bio

    Article Title: NGF protects neuroblastoma cells against β‐amyloid‐induced apoptosis via the Nrf2/HO‐1 pathway

    doi: 10.1002/2211-5463.12742

    Figure Lengend Snippet: NGF reduced Aβ25–35‐triggered cell apoptosis in SKNSH cells. SKNSH cells received preliminary supplementation with NGF (100 ng·mL −1 ) for 24 h prior to a 24‐h treatment with Aβ25–35 (25 μ m ). (A) Representative apoptosis depicted by FC. (B, C) Quantification of cell apoptosis in SKNSH cells (B) and primary neurons (C). Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, ** P

    Article Snippet: Double‐distilled water was used to dissolve the Aβ25–35 (Sigma, St Louis, MO, USA).

    Techniques:

    NGF suppressed Aβ25–35‐triggered JNK/c‐Jun activation in SKNSH cells. SKNSH cells received preliminary supplementation with NGF (100 ng·mL −1 ) for 24 h prior to 24‐h stimulation with Aβ25–35 (25 μ m ). (A–D) Representative immunoblots (A) and quantitative evaluation of p‐JNK (B), p‐c‐Jun (C), and PUMA (D) in SKNSH cells. Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, ** P

    Journal: FEBS Open Bio

    Article Title: NGF protects neuroblastoma cells against β‐amyloid‐induced apoptosis via the Nrf2/HO‐1 pathway

    doi: 10.1002/2211-5463.12742

    Figure Lengend Snippet: NGF suppressed Aβ25–35‐triggered JNK/c‐Jun activation in SKNSH cells. SKNSH cells received preliminary supplementation with NGF (100 ng·mL −1 ) for 24 h prior to 24‐h stimulation with Aβ25–35 (25 μ m ). (A–D) Representative immunoblots (A) and quantitative evaluation of p‐JNK (B), p‐c‐Jun (C), and PUMA (D) in SKNSH cells. Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, ** P

    Article Snippet: Double‐distilled water was used to dissolve the Aβ25–35 (Sigma, St Louis, MO, USA).

    Techniques: Activation Assay, Western Blot

    NGF ameliorated ROS production triggered by Aβ25–35 in SKNSH cells. SKNSH cells received preliminary NGF supplement (100 ng·mL −1 ) for 24 h prior to 24‐h treatment with Aβ25–35 (25 μ m ). A. Intracellular ROS was measured via oxidation of H2DCFDA to DCF in SKNSH cells. B. Superoxide dismutase activity was measured using a colorimetric assay kit. C. A catalase‐specific activity assay kit was used to measure CAT function. D. A. Intracellular ROS was measured via oxidation of H2DCFDA to DCF in primary neurons. Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, * P

    Journal: FEBS Open Bio

    Article Title: NGF protects neuroblastoma cells against β‐amyloid‐induced apoptosis via the Nrf2/HO‐1 pathway

    doi: 10.1002/2211-5463.12742

    Figure Lengend Snippet: NGF ameliorated ROS production triggered by Aβ25–35 in SKNSH cells. SKNSH cells received preliminary NGF supplement (100 ng·mL −1 ) for 24 h prior to 24‐h treatment with Aβ25–35 (25 μ m ). A. Intracellular ROS was measured via oxidation of H2DCFDA to DCF in SKNSH cells. B. Superoxide dismutase activity was measured using a colorimetric assay kit. C. A catalase‐specific activity assay kit was used to measure CAT function. D. A. Intracellular ROS was measured via oxidation of H2DCFDA to DCF in primary neurons. Results are expressed as mean ± SEM for three independent experiments. One‐way ANOVA, * P

    Article Snippet: Double‐distilled water was used to dissolve the Aβ25–35 (Sigma, St Louis, MO, USA).

    Techniques: Activity Assay, Colorimetric Assay

    Nrf2/HO‐1 mediated defensive influence of NGF against apoptosis triggered by Aβ25–35 in SKNSH cells. Twenty‐four‐hour transfection of SKNSH cells was carried out with Nrf2 siRNA and subsequently supplemented with Aβ25–35 or Aβ25–35 + NGF for 24 h. (A, B) Representative immunoblots (A) and quantitative evaluation of Nrf2 (B) in SKNSH cells. (C) FC was used for the assessment of cell death. (D) Intracellular ROS was evaluated via the oxidation of H2DCFDA to DCF. (E–H) Representative immunoblots (E) and quantitative evaluation of p‐JNK (F), p‐c‐Jun (G), and PUMA (H) in SKNSH cells. Results are expressed as mean ± SEM for three independent experiments. Two‐way ANOVA, ** P

    Journal: FEBS Open Bio

    Article Title: NGF protects neuroblastoma cells against β‐amyloid‐induced apoptosis via the Nrf2/HO‐1 pathway

    doi: 10.1002/2211-5463.12742

    Figure Lengend Snippet: Nrf2/HO‐1 mediated defensive influence of NGF against apoptosis triggered by Aβ25–35 in SKNSH cells. Twenty‐four‐hour transfection of SKNSH cells was carried out with Nrf2 siRNA and subsequently supplemented with Aβ25–35 or Aβ25–35 + NGF for 24 h. (A, B) Representative immunoblots (A) and quantitative evaluation of Nrf2 (B) in SKNSH cells. (C) FC was used for the assessment of cell death. (D) Intracellular ROS was evaluated via the oxidation of H2DCFDA to DCF. (E–H) Representative immunoblots (E) and quantitative evaluation of p‐JNK (F), p‐c‐Jun (G), and PUMA (H) in SKNSH cells. Results are expressed as mean ± SEM for three independent experiments. Two‐way ANOVA, ** P

    Article Snippet: Double‐distilled water was used to dissolve the Aβ25–35 (Sigma, St Louis, MO, USA).

    Techniques: Transfection, Western Blot

    Schematic layout depicting that NGF defends neuroblastoma against cell death triggered by Aβ25–35 via suppression of ROS–JNK/c‐Jun pathway activation through the Nrf2/HO‐1 pathway. NGF increases Nrf2 nuclear translocation and promotes expression of HO‐1. NGF decreases ROS concentration, which impairs the stimulation of the JNK/c‐Jun signaling pathway and results in a decrease in apoptosis.

    Journal: FEBS Open Bio

    Article Title: NGF protects neuroblastoma cells against β‐amyloid‐induced apoptosis via the Nrf2/HO‐1 pathway

    doi: 10.1002/2211-5463.12742

    Figure Lengend Snippet: Schematic layout depicting that NGF defends neuroblastoma against cell death triggered by Aβ25–35 via suppression of ROS–JNK/c‐Jun pathway activation through the Nrf2/HO‐1 pathway. NGF increases Nrf2 nuclear translocation and promotes expression of HO‐1. NGF decreases ROS concentration, which impairs the stimulation of the JNK/c‐Jun signaling pathway and results in a decrease in apoptosis.

    Article Snippet: Double‐distilled water was used to dissolve the Aβ25–35 (Sigma, St Louis, MO, USA).

    Techniques: Activation Assay, Translocation Assay, Expressing, Concentration Assay

    Reconstitution of full-length VanS A with the amphipol A8-35. (A) Size-exclusion chromatogram of amphipol-reconstituted VanS A , demonstrating the presence of a single soluble and homogeneous species. (B) Comparison of autophosphorylation activity for VanS A in detergent solution vs. amphipols. The amphipol-reconstituted species exhibits substantially higher enzymatic activity. This is demonstrated in the anti-6xHis loading control, which shows that small amounts of the protein-plus-amphipol solution give essentially equivalent activity to much larger amounts of the detergent-solubilized protein. (C) 50 μM vancomycin has no effect on the autophosphorylation activity of amphipol-reconstituted VanS A . (D) (E) 50 μM vancomycin has no effect on the phosphatase activity of amphipol-reconstituted VanS A . Panel (D) shows a representative Phos-tag gel, with panel (E) showing the quantification of assays involving three independent sets of measurements.

    Journal: PLoS ONE

    Article Title: Vancomycin does not affect the enzymatic activities of purified VanSA

    doi: 10.1371/journal.pone.0210627

    Figure Lengend Snippet: Reconstitution of full-length VanS A with the amphipol A8-35. (A) Size-exclusion chromatogram of amphipol-reconstituted VanS A , demonstrating the presence of a single soluble and homogeneous species. (B) Comparison of autophosphorylation activity for VanS A in detergent solution vs. amphipols. The amphipol-reconstituted species exhibits substantially higher enzymatic activity. This is demonstrated in the anti-6xHis loading control, which shows that small amounts of the protein-plus-amphipol solution give essentially equivalent activity to much larger amounts of the detergent-solubilized protein. (C) 50 μM vancomycin has no effect on the autophosphorylation activity of amphipol-reconstituted VanS A . (D) (E) 50 μM vancomycin has no effect on the phosphatase activity of amphipol-reconstituted VanS A . Panel (D) shows a representative Phos-tag gel, with panel (E) showing the quantification of assays involving three independent sets of measurements.

    Article Snippet: To determine whether the lower activity observed with full-length VanSA in detergent reflects a regulatory effect contributed by the protein’s transmembrane region, or a nonspecific detergent effect, we used amphipol A8-35 [ ] as an alternative means of solubilizing the protein.

    Techniques: Activity Assay

    SRRM4 promotes the inclusion of the alternative microexon 34ʹ in TAF1 mRNA. Immunoblot (A) and immunofluorescence (B) analysis of Flp-In T-REx derivatives of HeLa cells expressing GFP-SRRM4. Transgene expression is verified after DOX induction for 24 h. GFP-SRRM4 is enriched in the nuclear fraction (NXT). Histone H3 was used as nuclear marker while cytoplasmic extract (CXT) was verified using α-tubulin (C). GFP-SRRM4 resides within the nuclear speckles as revealed by SRSF2 co-staining (D). Scale bars in panels B and D are 10 µm. RT-PCR analysis demonstrated the progressive incorporation of microexon 34ʹ in TAF1 mRNA during SRRM4 induction time curve. Plasmids containing cTAF1 and TAF1-34ʹ were used as size-specific controls. The quantified PSI is depicted below each time lane (E). SRRM4 protein expression correlates with microexon 34ʹ incorporation (F). RNA-seq data from N2a knockdown (KD) experiments and from the Srrm4 knockout model (Srrm4 Δ7−8/Δ7−8 ) are depicted in panel G and H, respectively. cRPKM indicates corrected reads per kilo base per million mapped reads.

    Journal: RNA Biology

    Article Title: Neuronal-specific microexon splicing of TAF1 mRNA is directly regulated by SRRM4/nSR100

    doi: 10.1080/15476286.2019.1667214

    Figure Lengend Snippet: SRRM4 promotes the inclusion of the alternative microexon 34ʹ in TAF1 mRNA. Immunoblot (A) and immunofluorescence (B) analysis of Flp-In T-REx derivatives of HeLa cells expressing GFP-SRRM4. Transgene expression is verified after DOX induction for 24 h. GFP-SRRM4 is enriched in the nuclear fraction (NXT). Histone H3 was used as nuclear marker while cytoplasmic extract (CXT) was verified using α-tubulin (C). GFP-SRRM4 resides within the nuclear speckles as revealed by SRSF2 co-staining (D). Scale bars in panels B and D are 10 µm. RT-PCR analysis demonstrated the progressive incorporation of microexon 34ʹ in TAF1 mRNA during SRRM4 induction time curve. Plasmids containing cTAF1 and TAF1-34ʹ were used as size-specific controls. The quantified PSI is depicted below each time lane (E). SRRM4 protein expression correlates with microexon 34ʹ incorporation (F). RNA-seq data from N2a knockdown (KD) experiments and from the Srrm4 knockout model (Srrm4 Δ7−8/Δ7−8 ) are depicted in panel G and H, respectively. cRPKM indicates corrected reads per kilo base per million mapped reads.

    Article Snippet: For immunoblot and immunofluorescence, the following primary antibodies were used: GFP (JL-8, Clontech, Mountain View, CA), SRRM4 [ ], α-tubulin (DM1A, CP06, Calbiochem, San Diego, CA), SRSF2 (SC-35, S4045, Sigma), histone H3 (ab1791, Abcam, Cambridge, UK) and vinculin (7F9, sc-7 3,614, Santa Cruz).

    Techniques: Immunofluorescence, Expressing, Marker, Staining, Reverse Transcription Polymerase Chain Reaction, RNA Sequencing Assay, Knock-Out

    SRRM4 promotes the alternative splicing of TAF1-34ʹ in different non-neuronal cell lines. RPE1 and U-2 OS derivative cell lines express GFP-SRRM4 as validated by immunoblot (A and C) and immunofluorescence (B and D). The expression of the transgene is verified after 24 h DOX induction. GFP-SRRM4 resides in the nucleus where it co-localizes with the nuclear speckle marker SRSF2 (B and D, lower panels). In both RPE1 and U-2 OS, the induction of SRRM4 results in microexon 34ʹ incorporation into TAF1 mRNA. Plasmids containing cTAF1 and TAF1-34ʹ cDNAs were used as controls. The different PSI quantifications are depicted below each lane (E).

    Journal: RNA Biology

    Article Title: Neuronal-specific microexon splicing of TAF1 mRNA is directly regulated by SRRM4/nSR100

    doi: 10.1080/15476286.2019.1667214

    Figure Lengend Snippet: SRRM4 promotes the alternative splicing of TAF1-34ʹ in different non-neuronal cell lines. RPE1 and U-2 OS derivative cell lines express GFP-SRRM4 as validated by immunoblot (A and C) and immunofluorescence (B and D). The expression of the transgene is verified after 24 h DOX induction. GFP-SRRM4 resides in the nucleus where it co-localizes with the nuclear speckle marker SRSF2 (B and D, lower panels). In both RPE1 and U-2 OS, the induction of SRRM4 results in microexon 34ʹ incorporation into TAF1 mRNA. Plasmids containing cTAF1 and TAF1-34ʹ cDNAs were used as controls. The different PSI quantifications are depicted below each lane (E).

    Article Snippet: For immunoblot and immunofluorescence, the following primary antibodies were used: GFP (JL-8, Clontech, Mountain View, CA), SRRM4 [ ], α-tubulin (DM1A, CP06, Calbiochem, San Diego, CA), SRSF2 (SC-35, S4045, Sigma), histone H3 (ab1791, Abcam, Cambridge, UK) and vinculin (7F9, sc-7 3,614, Santa Cruz).

    Techniques: Immunofluorescence, Expressing, Marker

    Influence of Taxol® and its constituents paclitaxel and cremophor-EL on the RBC morphology. Increasing concentrations of Taxol® (A), paclitaxel (B), and cremophor-EL (C) were incubated with whole blood (haematocrit 45%) for 60 min at 37°C, and RBC morphology, expressed as morphological index, was assessed by light microscopy. n =6. * P

    Journal: British Journal of Pharmacology

    Article Title: Commercial taxane formulations induce stomatocytosis and increase blood viscosity

    doi: 10.1038/sj.bjp.0704387

    Figure Lengend Snippet: Influence of Taxol® and its constituents paclitaxel and cremophor-EL on the RBC morphology. Increasing concentrations of Taxol® (A), paclitaxel (B), and cremophor-EL (C) were incubated with whole blood (haematocrit 45%) for 60 min at 37°C, and RBC morphology, expressed as morphological index, was assessed by light microscopy. n =6. * P

    Article Snippet: Cremophor-EL and paclitaxel (from Taxus brevifolia) were purchased from Sigma (Buchs, Switzerland).

    Techniques: Incubation, Light Microscopy

    Effect of cremophor-EL on viscosity of whole blood and plasma. Increasing concentrations of cremophor-EL were incubated with whole blood (haematocrit 45%) or plasma for 60 min at 37°C prior to determination of viscosity. (A) High shear viscosity of whole blood; (B) Low shear viscosity of whole blood; (C) Plasma viscosity. n =5. * P

    Journal: British Journal of Pharmacology

    Article Title: Commercial taxane formulations induce stomatocytosis and increase blood viscosity

    doi: 10.1038/sj.bjp.0704387

    Figure Lengend Snippet: Effect of cremophor-EL on viscosity of whole blood and plasma. Increasing concentrations of cremophor-EL were incubated with whole blood (haematocrit 45%) or plasma for 60 min at 37°C prior to determination of viscosity. (A) High shear viscosity of whole blood; (B) Low shear viscosity of whole blood; (C) Plasma viscosity. n =5. * P

    Article Snippet: Cremophor-EL and paclitaxel (from Taxus brevifolia) were purchased from Sigma (Buchs, Switzerland).

    Techniques: Incubation

    Inhibitory zone diameter of nano-formulations of Nano-1-Amp+Brij 35 and Nano-2-Amp+Brij 35. All data were analyzed by Duncan’s multiple range tests using SAS software package. Different letters represented significantly differences at the level of 0.05 (p  ≤  0.05).

    Journal: PLoS ONE

    Article Title: Antimicrobial Nanoemulsion Formulation with Improved Penetration of Foliar Spray through Citrus Leaf Cuticles to Control Citrus Huanglongbing

    doi: 10.1371/journal.pone.0133826

    Figure Lengend Snippet: Inhibitory zone diameter of nano-formulations of Nano-1-Amp+Brij 35 and Nano-2-Amp+Brij 35. All data were analyzed by Duncan’s multiple range tests using SAS software package. Different letters represented significantly differences at the level of 0.05 (p ≤ 0.05).

    Article Snippet: Screening and evaluation of the candidate adjuvants for enhancing penetration Eight adjuvants were evaluated by cuticular permeability, of which Brij 35 (CAS 9002-92-0), Brij 58 (CAS 9004-95-9), Brij 98 (CAS 9004-98-2), and Urea (CAS 57-13-6) were purchased from ACROS Organic (Thermo Fisher Scientific, NJ), dimethyl sulfoxide (DMSO, CAS 67-68-5) and 2-methyl-2-pyrrolidinone (NMP, CAS 872-50-4) from Sigma-Aldrich (St. Louis, MO), Laurocapram (CAS 59227-89-3) from NetQem LLC (Research Triangle Park, NC), and Oleic acid (CAS 112-80-1) from MP Biomedicals LLC (Santa Ana, CA).

    Techniques: Software

    HLB-affected citrus treated by nano-formulations. ( A ): Amp (left) vs. tap water (CK) (right); ( B ): Nano-1-Amp+Brij 35 (left) vs. tap water (CK) (right); ( C ): Nano-2-Amp+Brij 35 (left) vs. tap water (CK) (right).

    Journal: PLoS ONE

    Article Title: Antimicrobial Nanoemulsion Formulation with Improved Penetration of Foliar Spray through Citrus Leaf Cuticles to Control Citrus Huanglongbing

    doi: 10.1371/journal.pone.0133826

    Figure Lengend Snippet: HLB-affected citrus treated by nano-formulations. ( A ): Amp (left) vs. tap water (CK) (right); ( B ): Nano-1-Amp+Brij 35 (left) vs. tap water (CK) (right); ( C ): Nano-2-Amp+Brij 35 (left) vs. tap water (CK) (right).

    Article Snippet: Screening and evaluation of the candidate adjuvants for enhancing penetration Eight adjuvants were evaluated by cuticular permeability, of which Brij 35 (CAS 9002-92-0), Brij 58 (CAS 9004-95-9), Brij 98 (CAS 9004-98-2), and Urea (CAS 57-13-6) were purchased from ACROS Organic (Thermo Fisher Scientific, NJ), dimethyl sulfoxide (DMSO, CAS 67-68-5) and 2-methyl-2-pyrrolidinone (NMP, CAS 872-50-4) from Sigma-Aldrich (St. Louis, MO), Laurocapram (CAS 59227-89-3) from NetQem LLC (Research Triangle Park, NC), and Oleic acid (CAS 112-80-1) from MP Biomedicals LLC (Santa Ana, CA).

    Techniques:

    BAFF-mediated cellular responses of PKCβ-deficient B cells are altered in vitro and in vivo. (A) B cells from PKCβ +/+ (squares) and PKCβ-deficient (triangles) B cells were cultured in medium alone (open symbols) or in the presence of 25 ng/ml (light gray symbols), 100 ng/ml (dark gray symbols), or 250 ng/ml (closed symbols) of BAFF, and the frequencies of viable B cells were measured by FACS analysis. (B) The cell size of live BAFF-treated PKCβ +/+ (squares) and PKCβ-deficient (triangles) B cells was measured by FACS analysis of the forward scatter (FSC). Symbol shadings represent the same BAFF concentrations as in A. (C) BAFF-R expression on splenic B220-positive cells from PKCβ +/+ (continuous black line) and PKCβ-deficient (dashed black line) was measured by FACS. Gray lines (continuous and dashed) represent staining with an isotype control antibody. (D) Maturity of splenic B cells from PKCβ +/+ (left) and PKCβ-deficient (right) mice was assessed by expression of the surface markers IgD versus IgM (top) and CD21/35 versus IgM (bottom). Only live lymphocytes are shown, and the bottom panel is gated on B220-positve cells. Numbers in the top panels represent frequencies of cells in the respective quadrants. Gates in the bottom panels denote B cell developmental stages T1 (IgM hi CD21 lo ), T2 (IgM hi CD21 hi ), and mature (IgM int CD21 int ).

    Journal: The Journal of Experimental Medicine

    Article Title: BAFF controls B cell metabolic fitness through a PKC?- and Akt-dependent mechanism

    doi: 10.1084/jem.20060990

    Figure Lengend Snippet: BAFF-mediated cellular responses of PKCβ-deficient B cells are altered in vitro and in vivo. (A) B cells from PKCβ +/+ (squares) and PKCβ-deficient (triangles) B cells were cultured in medium alone (open symbols) or in the presence of 25 ng/ml (light gray symbols), 100 ng/ml (dark gray symbols), or 250 ng/ml (closed symbols) of BAFF, and the frequencies of viable B cells were measured by FACS analysis. (B) The cell size of live BAFF-treated PKCβ +/+ (squares) and PKCβ-deficient (triangles) B cells was measured by FACS analysis of the forward scatter (FSC). Symbol shadings represent the same BAFF concentrations as in A. (C) BAFF-R expression on splenic B220-positive cells from PKCβ +/+ (continuous black line) and PKCβ-deficient (dashed black line) was measured by FACS. Gray lines (continuous and dashed) represent staining with an isotype control antibody. (D) Maturity of splenic B cells from PKCβ +/+ (left) and PKCβ-deficient (right) mice was assessed by expression of the surface markers IgD versus IgM (top) and CD21/35 versus IgM (bottom). Only live lymphocytes are shown, and the bottom panel is gated on B220-positve cells. Numbers in the top panels represent frequencies of cells in the respective quadrants. Gates in the bottom panels denote B cell developmental stages T1 (IgM hi CD21 lo ), T2 (IgM hi CD21 hi ), and mature (IgM int CD21 int ).

    Article Snippet: B cell surface marker expression was analyzed using antibodies against IgD, CD21/35, B220 (BD Biosciences), BAFF-R (R & D Systems), or a F(ab′)2 fragment of goat anti–mouse IgM (Jackson ImmunoResearch Laboratories), as previously described ( ).

    Techniques: In Vitro, In Vivo, Cell Culture, FACS, Expressing, Staining, Mouse Assay

    The effect of NO on tumor growth. CM-Dil labeled glioma cells were injected into the yolk of zebrafish embryos at 2 dpf and incubated with CPTIO (200μM). Images were taken at 1 dpi and 4 dpi. Images (A-A”‘) and (B-B”‘) show the tumors at 1 dpi and 4 dpi for control and CPTIO treated embryo. At 4 dpi, tumors have increased in size in untreated embryos (A”-A”‘) in comparison to CPTIO treated embryos (B”-B”‘). (C) Percentage of fluorescence intensity of the tumor surfaces was determined by ZEN software (n = 10). Images were taken with an Axio zoom V16 (Zeiss) macroscope, with the same exposure time for all embryos. Error bars represent SEM, *** p

    Journal: PLoS ONE

    Article Title: The Impact of Tumor Nitric Oxide Production on VEGFA Expression and Tumor Growth in a Zebrafish Rat Glioma Xenograft Model

    doi: 10.1371/journal.pone.0120435

    Figure Lengend Snippet: The effect of NO on tumor growth. CM-Dil labeled glioma cells were injected into the yolk of zebrafish embryos at 2 dpf and incubated with CPTIO (200μM). Images were taken at 1 dpi and 4 dpi. Images (A-A”‘) and (B-B”‘) show the tumors at 1 dpi and 4 dpi for control and CPTIO treated embryo. At 4 dpi, tumors have increased in size in untreated embryos (A”-A”‘) in comparison to CPTIO treated embryos (B”-B”‘). (C) Percentage of fluorescence intensity of the tumor surfaces was determined by ZEN software (n = 10). Images were taken with an Axio zoom V16 (Zeiss) macroscope, with the same exposure time for all embryos. Error bars represent SEM, *** p

    Article Snippet: For tumor growth observation we used an Axio zoom V16 (Zeiss) macroscope, composed of motorized stereo zoom microscope, a fluorescence light HPX 200 C, coupled to a Zeiss HRm CCD camera and a computer.

    Techniques: Labeling, Injection, Incubation, Fluorescence, Software