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    Nikon niselements software
    CLR 01 inhibits R120G‐induced protein aggregation in a dose‐dependent manner. Neonatal rat ventricular cardiomyocytes were infected with Ad GFP ‐Cry AB R 120G and treated with different doses of CLR 01 or CLR 03. A and B, NRVM s were fixed and immunostained with troponin I (TnI; red) and 4',6‐diamidino‐2‐phenylindole ( DAPI , nuclear staining; blue). C and D, Aggregates (green) in the neonatal rat ventricular cardiomyocytes were <t>quantitated</t> using <t>NIS</t> ‐elements (Nikon) software. E, Dose‐response curve for CLR 01 inhibition of R120G‐induced protein aggregation. At least 100 cells were quantitated in each group for each experiment, and each group was replicated n=6. The IC 50 value is indicated. R120G indicates Ad GFP ‐Cry AB R 120G . * P
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    CLR 01 inhibits R120G‐induced protein aggregation in a dose‐dependent manner. Neonatal rat ventricular cardiomyocytes were infected with Ad GFP ‐Cry AB R 120G and treated with different doses of CLR 01 or CLR 03. A and B, NRVM s were fixed and immunostained with troponin I (TnI; red) and 4',6‐diamidino‐2‐phenylindole ( DAPI , nuclear staining; blue). C and D, Aggregates (green) in the neonatal rat ventricular cardiomyocytes were quantitated using NIS ‐elements (Nikon) software. E, Dose‐response curve for CLR 01 inhibition of R120G‐induced protein aggregation. At least 100 cells were quantitated in each group for each experiment, and each group was replicated n=6. The IC 50 value is indicated. R120G indicates Ad GFP ‐Cry AB R 120G . * P

    Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

    Article Title: Inhibition of Mutant αB Crystallin‐Induced Protein Aggregation by a Molecular Tweezer

    doi: 10.1161/JAHA.117.006182

    Figure Lengend Snippet: CLR 01 inhibits R120G‐induced protein aggregation in a dose‐dependent manner. Neonatal rat ventricular cardiomyocytes were infected with Ad GFP ‐Cry AB R 120G and treated with different doses of CLR 01 or CLR 03. A and B, NRVM s were fixed and immunostained with troponin I (TnI; red) and 4',6‐diamidino‐2‐phenylindole ( DAPI , nuclear staining; blue). C and D, Aggregates (green) in the neonatal rat ventricular cardiomyocytes were quantitated using NIS ‐elements (Nikon) software. E, Dose‐response curve for CLR 01 inhibition of R120G‐induced protein aggregation. At least 100 cells were quantitated in each group for each experiment, and each group was replicated n=6. The IC 50 value is indicated. R120G indicates Ad GFP ‐Cry AB R 120G . * P

    Article Snippet: Relative aggregate areas per cell were quantitated using NIS‐elements software (Nikon) with the observer blinded as to sample identity.

    Techniques: Infection, Staining, Software, Inhibition

    CLR 01 blocks R120G‐induced aggregate formation. A, Neonatal rat ventricular cardiomyocytes were fixed and immunostained with TnI and DAPI at different days after Ad GFP ‐Cry AB R 120G infection. Column 1 contains cells that were untreated with CLR 01. CLR 01 was added at either 1 day (column 2) or 3 days postinfection (column 3) in order to explore its effects on formation vs clearance of aggregates. B, Aggregates were quantitated using NIS ‐elements software. R120G indicates Ad GFP ‐Cry AB R 120G . At least 100 cells were quantitated in each group for each experiment, and each group was replicated with n=6. * P

    Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

    Article Title: Inhibition of Mutant αB Crystallin‐Induced Protein Aggregation by a Molecular Tweezer

    doi: 10.1161/JAHA.117.006182

    Figure Lengend Snippet: CLR 01 blocks R120G‐induced aggregate formation. A, Neonatal rat ventricular cardiomyocytes were fixed and immunostained with TnI and DAPI at different days after Ad GFP ‐Cry AB R 120G infection. Column 1 contains cells that were untreated with CLR 01. CLR 01 was added at either 1 day (column 2) or 3 days postinfection (column 3) in order to explore its effects on formation vs clearance of aggregates. B, Aggregates were quantitated using NIS ‐elements software. R120G indicates Ad GFP ‐Cry AB R 120G . At least 100 cells were quantitated in each group for each experiment, and each group was replicated with n=6. * P

    Article Snippet: Relative aggregate areas per cell were quantitated using NIS‐elements software (Nikon) with the observer blinded as to sample identity.

    Techniques: Infection, Software

    Atypical PKCζ regulates HDAC6 deacetylase activity. Parental MEF cells were transfected to overexpress either HA-HDAC6 or myc-PKCζ or were treated with HDAC6 inhibitor tubacin (10μM for 4 hours) or aPKC inhibitor (myristoylated pseudosubstrate—20μM for 16 hours). Cells were subsequently fixed with 4% paraformaldehyde prior to immunofluorescence staining using α-tubulin antibodies (1:100) detected with Cy5 secondary antibody (1:400) and acetyl-tubulin antibody (1:100) detected with Texas Red secondary antibody (1:400). Texas Red labeled acetyl tubulin was pseudocolored to 400nm using Nikon NIS Elements AR software to visually separate it from Cy5. Inset panels for HA-HDAC6 and myc-PKCζ (HA and myc antibodies used at 1:100) overexpression were detected with Oregon Green secondary antibody (1:400). Images from a minimum of 25 cells each were used for statistical analysis. Scale bar is 10μm.

    Journal: PLoS ONE

    Article Title: aPKC Phosphorylation of HDAC6 Results in Increased Deacetylation Activity

    doi: 10.1371/journal.pone.0123191

    Figure Lengend Snippet: Atypical PKCζ regulates HDAC6 deacetylase activity. Parental MEF cells were transfected to overexpress either HA-HDAC6 or myc-PKCζ or were treated with HDAC6 inhibitor tubacin (10μM for 4 hours) or aPKC inhibitor (myristoylated pseudosubstrate—20μM for 16 hours). Cells were subsequently fixed with 4% paraformaldehyde prior to immunofluorescence staining using α-tubulin antibodies (1:100) detected with Cy5 secondary antibody (1:400) and acetyl-tubulin antibody (1:100) detected with Texas Red secondary antibody (1:400). Texas Red labeled acetyl tubulin was pseudocolored to 400nm using Nikon NIS Elements AR software to visually separate it from Cy5. Inset panels for HA-HDAC6 and myc-PKCζ (HA and myc antibodies used at 1:100) overexpression were detected with Oregon Green secondary antibody (1:400). Images from a minimum of 25 cells each were used for statistical analysis. Scale bar is 10μm.

    Article Snippet: The intensity of the fluorescence from the α-tubulin and acetylated tubulin images were measured using NIS-Elements AR software (Nikon).

    Techniques: Histone Deacetylase Assay, Activity Assay, Transfection, Immunofluorescence, Staining, Labeling, Software, Over Expression

    Clathrin/Caveolin-dependent entry of AAV2. (A, B) HeLa cells were incubated with QD-labeled AAV2 for 30 min at 4°C to synchronize infection. The cells were then shifted to 37°C for 5 or 15 min, fixed, permeabilized, and immunostained with anti-clathrin (A) or anti-caveolin-1 antibody (B). The boxed regions are enlarged in the right panels. Scale bar represents 5 µm. (C) Quantification of QD-AAV2 colocalized with clathrin or caveolin-1 signals after 5 or 15 min of incubation. Colocalization coefficients were calculated using the Manders' overlap coefficient by viewing more than 10 cells at each time point using the Nikon NIS-Elements software. Error bars represent the standard deviation of the mean from analysis of multiple images. (D to F) Real-time monitoring of QD-AAV2 internalization through the clathrin-coated pit. HeLa cells seeded on a glass bottom dish were transiently transfected with mRFP-clathrin (red). At 24 h post-transfection, the cells were incubated with QD-labeled AAV2 (green) for 30 min at 4°C, and were then warmed to 37°C to initiate virus internalization. Confocal time-lapse images were then recorded. A representative trajectory of QD-AAV2 in HeLa cells expressing mRFP-clathrin (D) and the selected frames of the real-time imaging (E) are presented. (F) Kinetics of the fluorescence intensity of mRFP-clathrin (red) and diffusion coefficients (blue) of AAV2 particle indicated by the white circle is shown. Scale bar represents 2 µm. (G) Inhibition of low pH-dependent endosomal processing by bafilomycin A1 (BAF, 50 nM), clathrin-dependent internalization by chlorpromazine (CPZ, 25 µg/ml), caveolin-dependent internalization by filipin (5 µg/ml), or depletion of cholesterol by methyl-beta-cyclodextrin (MβCD, 15 mM). HeLa cells were preincubated with the indicated drugs at 37°C for 30 min except for MβCD (15 min). The cells (1 × 10 5 ) were spin-infected with unlabeled or QD-labeled AAV2 in the presence of drugs (BAF, CPZ, and filipin) or in the absence of drug (MβCD). After an additional 3 h of incubation with drugs (BAF, CPZ, and filipin) at 37°C, the cells were washed with PBS and replenished with fresh media. The percentage of GFP-positive cells was analyzed by flow cytometry. Error bars represent the standard deviation of the mean from triplicate experiments. Asterisk indicates comparison to the no drug treatment group (* p

    Journal: ACS nano

    Article Title: Enhanced Real-Time Monitoring of Adeno-Associated Virus Trafficking by Virus-Quantum Dot Conjugates

    doi: 10.1021/nn102651p

    Figure Lengend Snippet: Clathrin/Caveolin-dependent entry of AAV2. (A, B) HeLa cells were incubated with QD-labeled AAV2 for 30 min at 4°C to synchronize infection. The cells were then shifted to 37°C for 5 or 15 min, fixed, permeabilized, and immunostained with anti-clathrin (A) or anti-caveolin-1 antibody (B). The boxed regions are enlarged in the right panels. Scale bar represents 5 µm. (C) Quantification of QD-AAV2 colocalized with clathrin or caveolin-1 signals after 5 or 15 min of incubation. Colocalization coefficients were calculated using the Manders' overlap coefficient by viewing more than 10 cells at each time point using the Nikon NIS-Elements software. Error bars represent the standard deviation of the mean from analysis of multiple images. (D to F) Real-time monitoring of QD-AAV2 internalization through the clathrin-coated pit. HeLa cells seeded on a glass bottom dish were transiently transfected with mRFP-clathrin (red). At 24 h post-transfection, the cells were incubated with QD-labeled AAV2 (green) for 30 min at 4°C, and were then warmed to 37°C to initiate virus internalization. Confocal time-lapse images were then recorded. A representative trajectory of QD-AAV2 in HeLa cells expressing mRFP-clathrin (D) and the selected frames of the real-time imaging (E) are presented. (F) Kinetics of the fluorescence intensity of mRFP-clathrin (red) and diffusion coefficients (blue) of AAV2 particle indicated by the white circle is shown. Scale bar represents 2 µm. (G) Inhibition of low pH-dependent endosomal processing by bafilomycin A1 (BAF, 50 nM), clathrin-dependent internalization by chlorpromazine (CPZ, 25 µg/ml), caveolin-dependent internalization by filipin (5 µg/ml), or depletion of cholesterol by methyl-beta-cyclodextrin (MβCD, 15 mM). HeLa cells were preincubated with the indicated drugs at 37°C for 30 min except for MβCD (15 min). The cells (1 × 10 5 ) were spin-infected with unlabeled or QD-labeled AAV2 in the presence of drugs (BAF, CPZ, and filipin) or in the absence of drug (MβCD). After an additional 3 h of incubation with drugs (BAF, CPZ, and filipin) at 37°C, the cells were washed with PBS and replenished with fresh media. The percentage of GFP-positive cells was analyzed by flow cytometry. Error bars represent the standard deviation of the mean from triplicate experiments. Asterisk indicates comparison to the no drug treatment group (* p

    Article Snippet: The Manders overlap coefficient was generated by the Nikon NIS-Elements software.

    Techniques: Incubation, Labeling, Infection, Software, Standard Deviation, Transfection, Expressing, Imaging, Fluorescence, Diffusion-based Assay, Inhibition, Flow Cytometry, Cytometry

    ROCK1/2 is required for IKK ε and IRF5 activation. a Confocal microscopy analysis of primary human ARPE-19 cells 24 h after transfection with plasmids encoding GFP-tagged IRF5 and RFP-tagged GEF-H1 in presence of IKK ε or IKKε (K38A) variant expressing constructs. Nuclear DNA was labeled using Hoechst 33342. Image acquisition was carried out with NIS-Elements imaging software (Nikon) followed by analysis by Volocity (PerkinElmer) to quantify the percentage of nuclei with GFP signal above cytoplasm in either IKKε or IKKε (K38A) transfected cells. Error bars indicate mean±SEM. Statistical significance was calculated using Student’s t -test *** P

    Journal: Nature Communications

    Article Title: Microbial recognition by GEF-H1 controls IKKε mediated activation of IRF5

    doi: 10.1038/s41467-019-09283-x

    Figure Lengend Snippet: ROCK1/2 is required for IKK ε and IRF5 activation. a Confocal microscopy analysis of primary human ARPE-19 cells 24 h after transfection with plasmids encoding GFP-tagged IRF5 and RFP-tagged GEF-H1 in presence of IKK ε or IKKε (K38A) variant expressing constructs. Nuclear DNA was labeled using Hoechst 33342. Image acquisition was carried out with NIS-Elements imaging software (Nikon) followed by analysis by Volocity (PerkinElmer) to quantify the percentage of nuclei with GFP signal above cytoplasm in either IKKε or IKKε (K38A) transfected cells. Error bars indicate mean±SEM. Statistical significance was calculated using Student’s t -test *** P

    Article Snippet: Image acquisition was carried out with NIS-Elements imaging software (Nikon) followed by analysis with Volocity (PerkinElmer)

    Techniques: Activation Assay, Confocal Microscopy, Transfection, Variant Assay, Expressing, Construct, Labeling, Imaging, Software

    Rg1 promotes Akt-dependent myotube hypertrophy. (A) C2C12 myoblasts were induced to differentiate in DM for 2 d and then treated with Rg1 for additional 2 d. The myotube formation was analyzed by MHC immunostaining. DAPI was used to visualize nuclei. (B) Average myotube diameter shown in panel (A) was measured by NIS-Elements F software (Nikon, Tokyo, Japan). Data are presented as means determination of six fields ± 1 SD. ** p

    Journal: Journal of Ginseng Research

    Article Title: Ginsenoside Rg1 from Panax ginseng enhances myoblast differentiation and myotube growth

    doi: 10.1016/j.jgr.2017.05.006

    Figure Lengend Snippet: Rg1 promotes Akt-dependent myotube hypertrophy. (A) C2C12 myoblasts were induced to differentiate in DM for 2 d and then treated with Rg1 for additional 2 d. The myotube formation was analyzed by MHC immunostaining. DAPI was used to visualize nuclei. (B) Average myotube diameter shown in panel (A) was measured by NIS-Elements F software (Nikon, Tokyo, Japan). Data are presented as means determination of six fields ± 1 SD. ** p

    Article Snippet: Images were captured and processed with a Nikon ECLIPSE TE-2000U microscope and NIS-Elements F software (Nikon, Tokyo, Japan).

    Techniques: Immunostaining, Software

    Effects of matriptase knockdown on ErbB-2-promoted cell migration of prostate cancer cells. Cells were seeded at a density of 1.2 × 10 6 per well in 6-cm dishes. Cells were infected by lentiviral particles with shRNAs specific to matriptase for 24 hours, selected by 1 μg/ml puromycin for 72 hours and then harvested for Western blot analysis. A: Cell lysates were collected with 0.5% NP-40 in HEPES buffer. The p-Tyr and protein levels of ErbB-2 were detected by anti-pTyr (PY100) and anti-ErbB-2 (C18) Abs. Nonreduced and nonboiled cell lysates were used for immunoblotting to detect the activation status and total matriptase with anti-total matriptase (M32) and anti-activated matriptase (M69) mAbs. Loading was analyzed with an anti-β-actin mAb (AC-15). B: Effects of matriptase knockdown on ErbB-2-promoting cell motility by wound-healing assays. Wounds with widths of approximately 250 μm were made by scraping by using 10-μl pipette tips. Cells were incubated for 24 hours for wound-healing assay. Images were captured by a light microscopy with a magnification of 100×. The dotted lines define the edges of the wounds. Migratory distances (widths at 0 hours to widths at 24 hours) were analyzed by a NIS-Elements D software (Nikon) and are represented as means ± SE calculated from triplicates; a statistically significant difference (* P

    Journal: The American Journal of Pathology

    Article Title: Matriptase Is Involved in ErbB-2-Induced Prostate Cancer Cell Invasion

    doi: 10.2353/ajpath.2010.100228

    Figure Lengend Snippet: Effects of matriptase knockdown on ErbB-2-promoted cell migration of prostate cancer cells. Cells were seeded at a density of 1.2 × 10 6 per well in 6-cm dishes. Cells were infected by lentiviral particles with shRNAs specific to matriptase for 24 hours, selected by 1 μg/ml puromycin for 72 hours and then harvested for Western blot analysis. A: Cell lysates were collected with 0.5% NP-40 in HEPES buffer. The p-Tyr and protein levels of ErbB-2 were detected by anti-pTyr (PY100) and anti-ErbB-2 (C18) Abs. Nonreduced and nonboiled cell lysates were used for immunoblotting to detect the activation status and total matriptase with anti-total matriptase (M32) and anti-activated matriptase (M69) mAbs. Loading was analyzed with an anti-β-actin mAb (AC-15). B: Effects of matriptase knockdown on ErbB-2-promoting cell motility by wound-healing assays. Wounds with widths of approximately 250 μm were made by scraping by using 10-μl pipette tips. Cells were incubated for 24 hours for wound-healing assay. Images were captured by a light microscopy with a magnification of 100×. The dotted lines define the edges of the wounds. Migratory distances (widths at 0 hours to widths at 24 hours) were analyzed by a NIS-Elements D software (Nikon) and are represented as means ± SE calculated from triplicates; a statistically significant difference (* P

    Article Snippet: Widths of the wound and migratory distances were measured and calculated by using NIS-Elements D software (Nikon).

    Techniques: Migration, Infection, Western Blot, Activation Assay, Transferring, Incubation, Wound Healing Assay, Light Microscopy, Software

    Detection of LGR5 in cultured cells. ( A ) Photomicrographs of LGR5-positive cells detected by Alexa488-LSAB, the Qdot, and the tyramide methods in LGR5+CSC, LOVO, and HCT116. Bar=25 μm. ( B ) Positive rate of LGR5 by Alexa488-LSAB, the Qdot, and the tyramide methods in LGR5+CSC, LOVO, and HCT116. ( C ) Subcellular distribution of LGR5-positive reaction by Alexa488-LSAB, the Qdot, and the tyramide methods in LGR5+CSC. Bar=10 μm. ( D ) Bar chart of individual values for intensity profile in ascending order. Intensity profile of a hundred LGR5+CSCs with the Qdot and the tyramide methods measured by Imaging Software NIS-Elements.

    Journal: Acta Histochemica et Cytochemica

    Article Title: Intensive Immunofluorescence Staining Methods for Low Expression Protein: Detection of Intestinal Stem Cell Marker LGR5

    doi: 10.1267/ahc.15019

    Figure Lengend Snippet: Detection of LGR5 in cultured cells. ( A ) Photomicrographs of LGR5-positive cells detected by Alexa488-LSAB, the Qdot, and the tyramide methods in LGR5+CSC, LOVO, and HCT116. Bar=25 μm. ( B ) Positive rate of LGR5 by Alexa488-LSAB, the Qdot, and the tyramide methods in LGR5+CSC, LOVO, and HCT116. ( C ) Subcellular distribution of LGR5-positive reaction by Alexa488-LSAB, the Qdot, and the tyramide methods in LGR5+CSC. Bar=10 μm. ( D ) Bar chart of individual values for intensity profile in ascending order. Intensity profile of a hundred LGR5+CSCs with the Qdot and the tyramide methods measured by Imaging Software NIS-Elements.

    Article Snippet: The intensity profile of a hundred cells for the Qdot and the tyramide were measured by Imaging Software NIS-Elements (Nikon, Tokyo, Japan).

    Techniques: Cell Culture, Imaging, Software