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(F-I) Lineage-tracing evidence supports α- to β-cell transdifferentiation. (G) Quantification of insulin-expressing cells that originate from α-cells. Control larvae, n=13; bactin:igfbp1a larvae, n=16. P=0.0051.
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A Schemes for the genomic loci of the miRNA and E-cadherin genes, showing regions of the CpG islands (yellow), of the qRT-PCR amplicon for chromatin immunoprecipitation (ChIP) analysis (blue) and of the bisulfite sequencing (red).
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(b) (left) Phylogenetic tree produced by the Nextstrain analysis with clade affiliations and nodes corresponding to WCM/NYP in red and other NYC cases in green. (right) occurrence of the six NYC-enriched alleles and the 9 nucleotide deletion across genomes.
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A-C Nurr1 and Foxa2protein levels in mDA neurons decrease in vitro after long-term culture (B and C).Nurr1 and Foxa2protein levels were also quantified in cultured mDA neurons over 6-34 days in vitro immunocytochemical analysis (C). Significantly lower MFI values on day 24 of culture (D24) compared to D12 at *P = 0.027 (Nurr1), *P = 0.012 (Foxa2), n = 60-70 TH+ cells from two cultures in each group, unpaired Student's t-test.
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Immunofluorescence staining of osteocalcin from 8-week-old mice (n=6 mice in Rankl-/- group and 4 mice in Rankl+/+ group). Scale bar=50 μm. TB: trabecular bone. Statistical analyses of Ocn+ cells (n=6 independent microscopic vision fields from random mice samples). Data were compared using an unpaired t‐test (** indicates P < 0.01), error bars are standard deviations.
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Kymograph illustrating the dissociation of GFP-Rdh54 from Rad51-ssDNA; arrowhead highlights the time point at which free GFP-Rdh54 was flushed from the sample chamber. Graph depicting the dissociation rate of GFP-Rdh54 from Rad51-ssDNA. Error bars represent s.d. of individual ssDNA molecules (N=25).
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IL-1β ELISA of Gata6-WT and Gata6-KOmye pMɸ stimulated with 100 ng.ml-1 LPS and either vehicle control (Vh, DMSO) or Ac-YVAD-cmk for 24 h. Data shown are pooled of 5 independent replicates.
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(A) MCF7 cells were incubated with serum-free CM collected from treated BJ fibroblasts (8 dpt) containing EdU for 45 hours and EdU+ cells quantified (n=9 samples from 3 independent experiments). Data information: Data are means ±SD. One-way ANOVA *p<0.05, **p<0.01, ***p<0.001, N.S.=not significant. CM, conditioned media.
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B. Relative quantification of all four histone proteins in each tissue replicate (order of appearance per replicate: H2A, H2B, H3.3 and H4).
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(A, B) AAV-hTau-eGFP (AAV-hTau) or the empty vector AAV-eGFP (1.13×1013 v.g./ml) was stereotaxically injected into hippocampal CA3 of 3-month-old C57 mice. After one month, the increased levels of STAT1 and pY-STAT1 in hippocampal total extracts and the nuclear fraction were detected in hTau group by Western blotting (n=6, Mann-Whitney test). Data information: Data were presented as mean ± SD. *, p<0.05, **, p<0.01, ***, p<0.001 vs eGFP, wt or Ctrl.
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(E) Part of the computed B cell gene regulatory network showing TCF4 and its deregulated target genes as well as some of the adjacent nodes. The GRN was used to calculate the activity of regulators like TCF4 based on their target gene expression. Color code: TFs, red; target genes, grey; chromatin modifier, blue.
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C, AltFUS (arrow) endogenous expression in Human tissues (brain, muscles and kidney - 100 μg), in HEK293 and HeLa cultured cells (100 μg) and using the over-expression of altFUS CDS in HEK293 cells (50 μg) as positive control (representative image from n=3). The asterisk indicates a protein species detected with the anti-altFUS antibody specifically in the brain.
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Western blotting for the indicated pluripotency proteins in mESCs as in (F) (left), and quantification (right) (mean values ± SD). n = 3 biological replicates.
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A. SILAC-based strategy for multidimensional analysis of TNF-α signaling. The "medium" and "heavy" labeled cells were stimulated with TNF-α for 5 and 15 minutes, respectively, and mock-treated "light" labeled cells served as control. For site-specific quantification of phosphorylation and ubiquitylation, equal amounts of proteins from three SILAC populations were mixed and phosphorylated and di-Gly modified peptides were enriched in parallel from the same samples. To investigate the dynamics of TNF-RSC-associated proteins, cells were treated with FLAG-TNF-α, and the ligand-bound TNF-RSCs were affinity-purified using anti-FLAG antibody, proteins were mixed before proteolysis and the relative abundance of proteins was quantified with LC-MS/MS.
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D. Abundance changes of PE-labeled Oct4 and APC-labeled Nanog proteins in Nmnat2 SATS isoform knockdown mESCs by flow cytometry analysis. Knocking down Nmnat2 SATS isoform by two independent siRNAs is included. The siCtrl and siOct4 mESCs are used as negative and positive controls, respectively.
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(D) Human kidney organoids were treated with IL-1β (10ng/ml) for 96 hours. Immunofluorescence reveals significantly increased COUP-TFII (green) and αSMA (red) expression in IL-1β treated organoids, compared to non-treated organoids. Quantification by confocal micrographs in 200x hpf. **p<0.01; ***p<0.001 by t test; mean ± SD.
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A Cellular glucose uptake, lactate production, and oxygen consumption rates were measured in WT and Dgcr8−/−ESCs.
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F SmD1b recognizes in vivo the RNAs of 4 genes regulated by ASCO. In E and F the results were expressed as % INPUT in SmD1b-GFP RIP and IgG RIP used as a negative control.
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G. Ciliary SMO was accumulated above the transition zone (TZ) (yellow line) in RPE1 cells expressing GFP-Rabl2Q80L. Images were acquired through 3D-SIM. CEP290 served as TZ marker. DA, distal appendage.
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D HEK293T cells were transfected with 12XGliBS‐Luc and pRL‐TK Renilla (normalization control) plus control (empty vector) or Gli1 or Gli1K340A mutant and treated with increasing concentrations of GlaB. Treatment time was 24 h, and control cells were treated with DMSO only. Data show the mean ± SD of three independent experiments. *P 0.05 versus DMSO; **P 0.05 K340A versus Gli1 WT.
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(B) RT-qPCR-based analysis of expression changes of DVL3 in stable MDA-MB-468 (EV, HA-DVL3-NESm) cells. (C) RT-qPCR-based analysis of expression changes of KMT2D in stable MDA-MB-468 (EV, HA-DVL3-NESm) cells. (D) RT-qPCR-based analysis of expression changes of ARAP1 , RFX5, GBAT2, WDR74, SNORD3D, HAUS5, TAP1, HLA-A, PDG1, and, MR1 in stable MDA-MB-468 (EV, HA-DVL3-NESm) cells. (E
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[d] Summary histograms of the mean (± SEM) cumulative seizure-like activity at 15 min, from the data in panel c. Statistical significance was assessed by ANOVA with post hoc pairwise comparisons (*p < 0.05).
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Isolated islets from human donors were treated for 3 days with recombinant human IGFBP1 protein, respectively. (E-F) Representative confocal images of control or IGFBP1-treated human islets. A gcg+ins+ cell is indicated by an arrow. For clarity, individual colors for denoting insulin (green), glucagon (red), and DAPI (blue) are also shown separately. Scale bars: 15 μm. (G) Quantification of the percentage of gcg+ins+ bihormonal cells per ins+ cells in human islets from 5 donors. P=0.0036. Co-expression of insulin and glucagon is indicative of transdifferentiation, which could reflect either α cells transdifferentiating to β cells or vice versa.
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(A) Structure of the spindle upon NuMA and Eg5 inhibition. HCT116 TetOsTIR1 NuMA-mAID-mClover-FLAG cells with 2-centrosomes were treated with 1 μg/ml doxycycline (Dox), 500 μM IAA and monastrol. Green, red, and blue represent NuMA (mClover), α-tubulin, and DNA, respectively. Z-projections of 10 sections, every 0.3 μm. Scale bar, 5 μm. (B) Frequency of spindle structure patterns upon NuMA depletion and Eg5 inhibition in (A). Values are mean percentages ± SD. from three independent experiments (N≧22 spindles in each experiment). (
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(C) Immunofluorescence images showing nuclear-enriched Gadd45b in uninfected neurons at 72 hrs post treatment with LY294002. Scale bar, 20 μm. (D) The signal intensity quantification showing the ratio of nuclear/cytoplasmic Gadd45b at 72 hrs post treatment with LY294002 and WAY-150138 neurons. The signal intensity was quantified by ImageJ. 3 biological replicates, 10 EdU positive cells and 10 EdU negative cells were quantified for each replicate. The horizonal line and error bars are mean ± SD. (E) The percentage of Gadd45b nuclear puncta-localized neurons were quantified from latent neurons treated with LY294002 and WAY-150138 for 72 hrs. Each dot represents each biological replicate; 20 cells were quantified for each replicate. The bars and error bars are mean ± SD. Data information: P values equal to or less than 0.05 were considered significant, asterisks denote statistical significance (*, p<0.05; ***, p<0.001; ****, p<0.0001). P values are calculated using two-tailed unpaired Student's t test.
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B - Endocervical epithelial cells were pre-treated or not with 40 μM CP4d for 2 h before addition of the indicated concentration of ionomycin (or an equivalent volume of DMSO) and 0.5 µM BP. Six hours later whole cell lysates were analyzed by western blot. The membrane was first blotted with HRP-conjugated streptavidin to detect TG2 activity, then extensively washed and probed with anti-O-GlcNAcylation antibody followed with HRP-conjugated secondary antibodies. Last the membrane was probed with anti-actin as a loading control.
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Effect of cl-HK2pep on cellular Ca2+ dynamics changes in mitochondrial Ca2+ levels are recorded and quantified using the GCAMP6f sensor (in D, as mean of 475/410 nm ratio; signal±SEM of at least 5 independent experiments and more than 20 cells analized) Data information: Experiments throughout the Figure are carried out on HeLa cells; cl-SCRpep, negative control of cl-HK2pep (2 μM each). Xe-C is Xestospongin C, which selectively inhibits IP3R at the 5 μM concentration used here
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Liver tissue samples obtained from HBV-negative patients undergoing metastasis resection (Control), or patients with acute, self-limiting HBV infection or chronic hepatitis B, or chronic coinfection with HBV and hepatitis D virus (HDV) were stained for ISG20 by immunohistochemistry. For each clinical entity, tissue sections from three different patients are shown; scale bar: 50 µm. ISG20 positive area of each sample (n=3 biological replicates) was determined by Tissue IA image analysis software and is given in % of total tissue area scanned.
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(A and B) ΔΨm (A) and Acly levels (B) in HSCs derived from 5-FU treated mice in the late phase before and after a 1-day culture.
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mRNA expression levels of the indicated genes were assayed by real-time PCR and normalized to Actb (C).
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(H) Tumor growth was detected by BLI. Lines that do not reach day 20 correspond to mice that were sacrificed for ethical reasons. One BoxA treated mouse survived without any BLI signal and was re-challenged with CT26-LUC cells at day 65; at day 79 it was sacrificed and no tumor masses were detected.
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(H) 786-0 or 769-P cells stably expressing shGDH1 were reconstituted with rGDH1 WT or 3KR mutant and then treated with or without aa starvation for the indicated time. Cell viability was determined. Unpaired two-tailed t-test was used. Data information: The data are represented as the mean ± SEM of three independent experiments. The unpaired t-test were used (N.S.: not significant; *p < 0.05; **p < 0.01; ***p < 0.001).
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Transversal section of a recombined VeCadCreER:Confetti AGM from an E10.5 embryo and immunostained with Kit (D) (white in image, black in label). Multistack reconstruction of confocal images. Scale bars 20 μm
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Mean values ± s.e.m. and cumulative histogram of amplitude (top) and frequency/interevent-interval (bottom) of mIPSCs in different mouse-models as indicated . Several cells of 3 mice of each genotype were analyzed. Compared genotypes were siblings. No difference in amplitude or frequency/ interevent-interval distribution of mIPSCs was found in (B) Clcn3-/- and Clcn3+/+ (Clcn3+/+: 16 cells, Clcn3-/-: 15 cells; mean amplitude: p > 0.8, t test; mean frequency: p > 0.4, MW-test), in (C) Clcn3unc/unc and Clcn3+/+ (Clcn3+/+: 21 cells, Clcn3unc/unc: 13 cells; mean amplitude: p > 0.7; mean frequency: p = 0.3, t test), and in (D) Clcn4-/- and Clcn3+/+ (Clcn3+/+: 18 cells, Clcn4-/-: 18 cells; mean amplitude: p > 0.3, t-test; mean frequency: p = 0.6, MW-test).
|
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G Immunoblot analysis demonstrating that the N‐terminus of KSHV‐TK is only auto‐phosphorylated by the kinase domain in cis.
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E. Principle component analysis (PCA) analysis indicating the routes during early reprogramming of CMs and NCs.
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(C) RAW264.7 macrophages were infected with wt MCMV-GFP or ΔM45 at an MOI of 0.1, stimulated 24 h postinfection for 4 hours with TLR agonists Pam3CSK4 (Pam.) or Malp-2 (TLR2), LPS (TLR4), R837 (TLR7), or CpG (TLR9), in the presence of brefeldin A. Cells were fixed, permeabilized, and stained with a TNFα-specific antibody. The percentages of TNFα-positive cells within infected (GFP-positive) cell populations were determined by FACS analysis (mean ± SD).
|
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Pairwise Pearson correlations of in vitro TNG-A and in vivo embryo (Boroviak et al, 2015) RNAseq samples.
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(D-G) ELISA analysis of IL-4, IL-13, IL-1β and IL-18 in lung tissue homogenate samples from wild-type (WT) and EphA2-knockout (KO) mice (n=3 per strain) sensitized with ova. Data information: Each symbol represents an independent experiment; small horizontal lines indicate the average of triplicates. *P<0.05, **P <0.01 and ***P<0.001 (unpaired t test). Data represent three or four independent biological replicates.
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(H) Cell-free plasma was derived from breast cancer patients treated with paclitaxel (n=10) or palbociclib (n=9) and the expression levels of IGFBP3 quantified by ELISA. The values represent the ratio between on-treatment and pre-treatment levels for each patient. Data information: Data are means ±SD. Unpaired student t-test *p<0.05, **p<0.01, ***p<0.001.
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Confocal WM-IF analysis of Kitl-tdTomato expression (red) in a E10.5 (36sp) AGM region. Top panels (3D view) show a maximum intensity 3D projection from a 400μm-thick Z stack. Bottom panels (slice view) show a single 2.5μm-thick Z slice of the dorsal aorta, from the boxed region in the top panels. CD31 (vasculature; green); Kit (hematopoietic progenitors; white). Scale bars: 100μm (top); 25μm (bottom). fl: fetal liver; va: vitelline artery plexus; da: dorsal aorta; fp: floor plate; nt: neural tube. N=6 embryos analyzed.
|
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GO analysis of differentially expressed genes in PAX6 KO cells. Up-regulated genes and down-regulated genes are analyzed separately. The biological processes are ranked by p-value. Only top 15 terms were shown. GO analysis of differentially expressed genes in PAX6D KO cells. Up-regulated genes and down-regulated genes are analyzed separately. The biological processes are ranked by p-value. Only top 15 terms were shown.
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C Interaction between TseL and VgrG-1. Shown are immunoblots of lysates (total) and immunoprecipitates with an anti-FLAG affinity beads (IP:FLAG) of V52 or V52Δtap-1 transformed with empty vector or a plasmid encoding HIS-tagged or FLAG-tagged VgrG-1.
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(B) The total number of yellow vesicles was quantified from three independent experiments (>12 cells each) and presented as the percentage of total mCherry‐GFP‐LC3 dots (red plus yellow) along with the standard deviation.
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(A) DIV 4 cortical neurons expressing p110 isoforms and GFP. Arrow marks the axon tip. (B) Quantification of axon length. n = 3 experiments, 45 neurons per group. (C) Quantification of dendrite length. n = 3 experiments, 45 neurons per group. (D) Quantification of the axon:dendrite length ratio. n = 3 experiments, 45 neurons per group.
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(D) Histological analysis of H&E-stained sections of the kidneys of drug-treated mice or control untreated mice at the termination of the experiment. Pictures are representative of at least 3 mice for each treatment group.
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C. The morphology of EBs at day 10 of differentiation. M15 was the normal EB formation condition and was used as control. Black arrows indicate the cystic structures.
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(j) Immunoblot analysis of LAMP-2A in total lysates of CD4+ T cells obtained from two human donors (A and B) and left resting or activated for 24 or 48 h as in a (above lanes).
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(D, E) Atg5 KO MEFs were either untreated (NT) or starved (ST) with EBSS in the absence or presence of 20 nM wortmannin (Wtm) or 10 mM 3-methyladenine (3-MA) for 30 min. Membranes from each treated cell sample were collected and subjected to a differential centrifugation to separate the 3K ×g, 25K ×g and 100K ×g pellet fractions followed by a lipidation assay as above (E). A diagram is shown in (D).
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(C) Line graph indicating the proportion of correct responses (performance) for bins of 100 trials each during testing with binary mixtures of concentrated octanols. Discontinuous line indicates the similar 95% plateau performance of 4D- (black) and 4D+ (red) mice. (D) Whiskers box plots of performance (left) and lick frequency (right) during a probe of 200 trials with 1:10 diluted octanols after testing as in (C).
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O Confocal fluorescence microscopy image of replication in WT or Sirt5-deficient BMDC cells (Sirt5 +/+ or Sirt5 -/-) after infected with VSV-GFP viruses for 12 h (MOI = 1) (fluorescence, upper; bright-field, bottom). Scale bar = 75 µm.
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Angular displacement and y FMI of control and centrinone-B (500 nM, 7 days) treated hRPEs moving on stiffness gradient gels.
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Schematic model showing the mechanism of EML4-ALK V1 and V3 cytoplasmic foci formation. EML4-ALK V1 foci are formed by dynamic cross-linking interactions between the EML4 trimerization domain (TD), dimerization of ALK domains and additional interactions via the 12N Blade/Blades 1-5 domains. The shorter EML4-ALK V3 variant forms foci via interactions of EML4 TD and ALK kinase dimerization. In both variants, EML4-ALK trimers arises from the stoichiometric mismatch between the trimeric EML4 N-terminus and the dimers formed by ALK in its active conformation which leads to the formation of foci in the cytoplasm that exclude large complexes such as microtubules. The EML4-ALK foci act as signalling platforms by recruiting several proteins and allowing signal transduction. When the ALK kinase domain is monomeric cross-linking does not occur and the inactive EML4-ALK V3 trimers instead localise to microtubules through the EML4 TD and basic region, whereas inactive EML4-ALK V1 trimers are diffusely localised in the cytoplasm.
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BMDMs were costimulated with TNF (100 ng/ml) and SM (250 nM; 6 h) and mixed supernatant and cell extracts were analysed by immunoblot
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, Protein fold changes of the CcpA mutant over wild type. Log2 fold changes were calculated from LFQ values p values were calculated based on 2-sided two sample t-tests with a FDR threshold of 0.05 and S0 equal to 1 (Tusher et al, 2001). Proteins outside the significance lines (FDR = 0.05, S0 = 1) are significantly changed in expression. Example sets of proteins are highlighted and are labeled with their gene names.
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C. Dot plot of the top marker genes for each cell type for (left) colon- and (right) ileum-derived organoids. The dot size represents the percentage of cells expressing the gene; the color represents the average relative expression across the cell type.
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Baseline associations between CSF T-tau, Ng and NFL and other AD traits. Data are estimates (-coefficients) from linear mixed effects models, with 95 % confidence intervals. The estimates are the main effects of the biomarkers, capturing the effects at study baseline. Effects were significant (*) for hippocampal volume: NFL in A-negative (p<.0001). Biomarkers and outcomes were standardized to z-scores. Note also that the range of the y-axes differs for the different outcomes, for visualization purposes. Models were adjusted for age and sex, and education (for cognitive measures), and intracranial volume (for MRI measures). Aβ42 and T-tau were measured using the the INNOBIA AlzBio3 kit (Fujirebio, Ghent, Belgium), Ng was measured using an in-house immunoassay for Ng (Portelius et al, 2015) and NFL was measured using the NF-light® ELISA kit (Uman Diagnostics, Umeå, Sweden).
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f Decreased c-Fos DAB immunosignal in an MK-801 AGS-rescued Grin2aS/S animal (bottom) in the medial amygdala (MeA), the VMH and the PVT when compared to saline-injected Grin2aS/S littermate (top). Scale bars are in mm (for statistics: Supplementary Statistics to Fig. 4).
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Growth curves of the hOSE-shRB1 cells and hOSE-shRB1-LATS2 cells at their 16th passages.
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HEK293T were infected with HIV-Luc for 48h (10ng of p24). Graphs represent fold RLU means ± SD of infected S100A9-expressing cells normalized to infected E2C-expressing cells from duplicates of three independent experiments (n=3).
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G. GST or GST-Rad23 bound to glutathione Sepharose were used to precipitate proteasomes from brain lysates followed by IB with the FBXO7, PI31 or PSMA2 antibody.
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(A) Overall structure of Hs bound to both substrate and non‐substrate LC3. Substrate LC3 is designated as LC3(S) and coloured green, whereas non‐substrate LC3 is designated as LC3(N) and coloured blue.
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(F) The qRT-PCR analysis with cytosolic DNA (minus mitochondria) isolated from Irgm1+/+ and Irgm1-/- mouse BMDMs.
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(a, b) Bax/Bak−/− MEFs were treated with 20 μM etoposide in the absence or presence of 10 mM 3-MA for 24 h, and then were examined by phase-contrast microscopy (a) and electron microscopy (×8,400) (b). Autolysosomes/autophagosomes were hardly observed. (
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(F) Endogenous MITOL is ubiquitylated following valinomycin treatment. After MITOL-3Flag KI HCT116 cells stably expressing HA-Parkin were treated with valinomycin for 3 hours, the collected cell lysates were immunoprecipitated with anti-Flag magnetic beads. The immunoprecipitates were blotted using anti-Flag and anti-ubiquitin antibodies. Red bars indicate ubiquitylation; the black arrowhead indicates MITOL-3Flag.
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(D) Immunohistochemistry showing reduced pERK levels in Purkinje cells of homozygous BrafAVKA mice. Scale bar indicates 10x magnification.
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(D) COUP-TFII+ cells decrease significantly in the UUO kidney in TAM-treated homozygous (F/F;Cre/+) mice (KO group, n=6) compared to wild-type littermates (WT group, n=4). Expression of αSMA (red) and collagen1 (yellow) are also markedly reduced. Masson Trichrome staining shows less kidney fibrosis in KO compared to WT group. Quantification by confocal micrographs in 200x hpf. **p<0.01 by unpaired t test, mean ± SD.
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(E) Flow cytometry time course analysis of cell death at different time points after autophagy shutoff (+dox). The degree of cell death correlated directly with increased htt(Q47)-GFP levels after autophagy shutoff and was significantly enhanced in cells expressing htt(Q47)-GFP compared with htt(Q25)-GFP (***, P ≤ 0.005). Data represent three independent experiments performed on different days.
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H. The bar chart shows the efficiency of ntES derivation. The efficiency was calculated based on the total number of attached blastocysts for ntES derivation. N, total number of embryos analyzed for each condition. Error bars, s.d., n ≥ 3. **P < 0.01 by two-tailed Student"s
t
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(b) Effects of different plasmids on the THPN-induced dissipation of ΔΨm. Top, endogenous TR3 was knocked down by shRNA, and the siRNA-resistant version of TR3, TR3-NLS, TR3-ΔNLS or TAD (Supplementary Fig. 2c) were separately transfected into the cells as indicated. Bottom, similarly, the siRNA-resistant version of Nix or ΔTM were separately transfected into Nix knockdown cells. Transfected cells were treated with THPN (20 μM, 12 h), and their ΔΨm was assessed by flow cytometry. Ctrl, control.
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LDH assay was performed after 24 h of cold stress on ice. Data are presented as mean ± SEM; n = 3, biological replicates. ****p < 0.0001, ***p < 0.001 by one-way ANOVA followed by Dunnett's multiple comparison test.
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(D,E) Cryostat sections of the optic nerve from PLP and control mice were stained with anti-Nav-channel antibody to label the node of Ranvier and with anti-CASPR1 antibody to stain the paranodal region. Length of the node of Ranvier and length of the paranodal region were quantified in G) H). (F) transmission electron micrographs of the optic nerves from PLP/CFA- and CFA-injected animals (F1-F4). Axon numbers and myelin thickness were quantified in I) J)
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Overexpression of Huh7.5 is not sufficient to explain negative memory. Induced expression of USP18 after treatment of Huh7.5-TetON-USP18 and Huh7.5-TetON-control cells with doxycycline for 24 hours in comparison with parental Huh7.5 cells treated with 1400 pM IFNα for 24 hours. Analysis was performed by quantitative immunoblotting. Error bars represent 1σ confidence intervals estimated from biological replicates (N=3 to N=5) (left). Model fits and experimental data of Huh7.5-TetON-USP18 treated with doxycycline for 24 hours and stimulated with 1400 pM IFNα or parental Huh7.5 cells prestimulated with 0 or 1400 pM IFNα and stimulated with 1400 pM IFNα after 24 hours are shown. The dynamics of IFNα-induced phosphorylation of STAT1 and STAT2 and induction of USP18 are depicted. Experimental data was obtained by quantitative immunoblotting using chemiluminescence and CCD camera device (ImageQuant). For modeling purposes data from Huh7.5-TetON empty vector control and untransduced Huh7.5 are combined to one condition. Data is displayed as filled circles with errors representing 1σ confidence-interval estimated from biological replicates (N=3 to N=4) using a combined scaling and error model. Line represents model trajectories.
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A) ChIP-qPCR for Nhp2-myc using anti-myc antibody across the rDNA locus. Samples were normalized to input. n=3, biological replicates, error bars are standard error of the mean. *, p<0.05, **, p<0.001, based on unpaired, 2-tailed t-test
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(C) RPE-1 cells were analyzed as in B. Data are mean ± SEM from 5 biological replicates with 32-37 (siCtrl) and 31-39 (siACTN1+4) analyzed nuclei; ***p < 0.001 by Wilcoxon test and ****p < 0.0001 by Mann Whitney test at 90 min.
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Number of interactions detected per metabolite. Metabolites are grouped according to biological pathways; the height of the bar indicates the total number of interactions. Recovery of interactions reported in EcoCyc database. Metabolites are grouped according to biological pathways, the total height of the bar indicates the number of known interactions that could have been detected, the height of the colored bar indicates the number of actually recovered interactions. Recovery of catalytic (metabolite is substrate or product of the enzyme) and regulatory interactions is shown.
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(E) Experimental scheme of the Mirin aberration analysis is given. The experiment was carried out as in (D) but cells were pre-treated or not with 50 µM Mirin. Dot plot shows the effect of Mirin exposure on the number of chromosome aberrations per cell in shWRNIP1 cells. Horizontal black lines represent the mean SE. Error bars represent standard error (ns, not significant; **, p < 0.01; two-tailed Student's t test). Representative Giemsa-stained metaphases of shWRNIP1 cells treated with Mirin alone or in combination with HU. Arrows indicate chromosomal aberrations.
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H Representative images of the spinal cord myelination of ERp57WT and ERp57Nes-/- mice.
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Alternative NUP58 isoform localizes to the NPC. Representative images of HCT116 cell line showing localization of WT NUP58 protein (top WT isoform, z-stack = 10) and of an isoform lacking exon 4 and ending at exon 13 (bottom mutant isoform, z-stack = 11). Scale bar, 20 μm
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C) Cdk inhibition with flavopiridol prevents M18BP1-1161-580 localization at metaphase centromeres. Representative images showing Myc-M18BP1-1161-580 localization at sperm centromeres in metaphase extract depleted of endogenous M18BP1 following treatment with various mitotic kinase inhibitors. Inhibitor treatment is indicated at left, immunolocalized protein is indicated above. Scale bar, 10 μm. Insets are magnified 3X.
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F) Distribution and the average IdU/CldU ratio in Mybl2+/+ and Mybl2Δ/Δ ESCs with or without MRE11 inhibitor treatment. The length of both incorporated labels for each elongating fork was measured in µm and the positive ratio was calculated. Percentage of highly unstable forks (ratio above 2) are indicated. Dotted line at 1 indicates positive ratio. Y-axis was cut to change scale and display large values. Statistical analysis was carried out using the Mann Whitney U test. At least 260 ratios were calculated per treatment group from 3 separate experiments.( **** p< 0.0001)
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(A) Total AV counting results show that a significant drop occurs in neurons exposed to TNF-α or NMDA for 3 or 24 hr. *** P<0.001, ** P<0.01 for n = 6 experiments. All values are mean±SEM. (B and C) Distribution of AV number in soma and neurites respectively.
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D) Dwell time histograms obtained for N = 4, 5 and 6, with wild type Ago2; histograms were fit with single exponential decay. The first column of the data was not included in the analysis to avoid potential artifacts arising from the limit of the time resolution. The bin size is 0.5 sec for N =4 and 1 sec for N =5 and 6.
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(b) Immunofluorescence showing anti-VPS-34 staining in dissected embryos in the absence or presence of 5-FU (scale bar, 5 μm).
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Western blot analysis performed with lysates of (K-L) Irgm1+/+ and Irgm1-/- mouse brain to determine levels of IRF proteins.
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E. RPE cells were transfected with the indicated siRNAs for 24 hours, and then co-transfected with CMV-renilla and 8X-TBS luciferase. One day after the latter transfection, the cells were re-seeded to either sparse or dense conditions, and reporter activity was measured at 24 hours after re-seeding (n=3). Error bars indicate the S.E.M. (**p < 0.01; paired Student's t-test).
|
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B Telo-PCR analysis of tiTELs using genomic DNA extracted from cells as in (A). Marker (m) molecular weights are on the right in base pairs.
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C Southern blot of genomic DNA double-digested with BsaHI (methyl-sensitive) and BglI (methyl-insensitive) hybridized to a radiolabeled 5' probe. The absence of BsaHI digestion in BL-E5(+) cells confirmed CTCF binding site methylation.
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(F) Transcriptomic effect of Ctcflos tr1 (ASO 1) KD on brown and brite core regulatory gene expression network comparing Ctcflos tr1 (ASO 1) KD with controls. Visualized by Path Visio software. Color code visualizes log2 fold change of genes 24 hours (left part of box) and 72 hours (right part of box) after the KD. Red t-bars represent inhibitory effects, greed arrows represent activating effects.
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(C) GSEA pathway analysis of control vs COCO-treated HUVECs for TGFβ, BMP or ROS pathways.
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B Left, Representative views of H2AX and γ-H2AX immunostaining in TN tumours (N = 22) before and after successive cycles of chemotherapy. Scale bars = 100 μm. Zoom views are focused on the epithelial cells. Scale bars = 25 μm. Right, Scatter plots of H2AX, γ-H2AX histological scores (Hscores) and γ-H2AX/H2AX ratio evaluated from immunostaining in the epithelium, before and after chemotherapy.
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C Representative metaplot of SF cells. 25-32 mer ribosome footprint reads were summed across all annotated reading frames with the AUG staring codon at position zero. In-frame 27-30 mer ribosome footprints showing the correct periodicity.
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G-I. Knockdown of VEAL2 significantly reduced tube formation in Matrigel. (G-H) Magnification-5X, scale bar-50μm. (I) Dot plot representing quantification of number of junctions formed between the vessels in control siRNA and VEAL2 targeting siRNA treated HUVECs. The HUVECs were grown on matrigel. Data from different fields of 4 different technical replicates of 1 biological replicate is represented. Data is shown as individual values; the middle bar represents the mean and the error bar represents ± standard deviation.
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Cartoon showing that sporozoites cannot form in the absence of microtubules, while lower numbers allowed formation of aberrantly shaped parasites. Note that subpellicular microtubules are exclusively polymerized from the apical polar ring.
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(A) Schematic illustration of barasertib treatment protocol. Control and TGFα mice were treated with either vehicle or barasertib (40mg/kg; twice a day) for last 3 wks while they were fed with Dox containing food for total of 6 wks.
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Internalization of EV20/MMAF (10 nM) at indicated times in BT474 and BTRH cells. Scale bar: 20 µm. HER3 staining: red; DAPI: blue.
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H, Representative images of H&E-stained ovaries. Black dotted lines outline the ovaries, blue dotted line indicates a mature follicle. I, Quantification of mature ovary follicles per ovary section (average of three sections/biological sample) (Δ1 n=2-3, Δ2 n=6).
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0,
0,
0,
0,
0,
0,
0,
0,
0,
7,
8,
8,
8,
8,
8,
8,
8,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
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0,
0,
0,
0,
0,
0,
0,
0,
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0,
0,
0,
0,
0,
0,
0,
0,
0,
9,
10,
10,
10,
10,
10,
10,
10,
10,
10,
10,
10,
10,
10,
10,
0,
0,
0,
0,
0,
9,
10,
10,
10,
10,
0,
0,
0,
0,
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0,
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0,
0,
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0,
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0,
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0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0
] |
(D) qRT-PCR analysis of Acta1 and Nppa in NRVMs with or without NCoR1 knockdown. n=4:4.
|
[
0,
0,
0,
0,
13,
14,
14,
14,
14,
14,
14,
0,
0,
0,
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0,
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3,
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4,
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0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0
] |
The trans-well system was performed as in Fig. 1. Schistosome-exposed Th cells or control Th cells were subjected to qRT-PCR with specific schistosomal-Taqman primers to (A) miR-10-5p, (B) Bantam, and (C) miR-125b.
|
[
0,
0,
0,
0,
0,
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11,
12,
12,
12,
12,
12,
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12,
12,
12,
12,
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0,
0,
0,
0,
0,
0,
0,
0,
7,
8,
8,
8,
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8,
8,
8,
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0,
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7,
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8,
8,
8,
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0,
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13,
14,
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14,
14,
14,
14,
0,
0,
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0,
0,
0,
0,
0,
0,
0,
11,
12,
12,
12,
12,
12,
12,
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12,
12,
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12,
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3,
4,
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4,
4,
4,
4,
4,
4,
0,
0,
0,
0,
0,
0,
3,
4,
4,
4,
4,
4,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
3,
4,
4,
4,
4,
4,
4,
4,
0,
0
] |
The N-terminal GTPase domain of Rab8a was essential for BAG6 recognition. A series of Flag-tagged truncated fragments of WT Rab8a were expressed in HeLa cells with S-tagged BAG6 and treated with (+) or without (-) protease inhibitors for 4 h. Flag-Rab8a substrates were immunoprecipitated and probed with an anti-BAG6 antibody.
|
[
0,
0,
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0,
0,
0,
0,
0,
3,
4,
4,
4,
4,
4,
4,
4,
0,
3,
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4,
4,
0,
0,
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0,
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0,
0,
0,
0,
0,
1,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
2,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
3,
4,
4,
4,
0,
3,
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4,
0,
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13,
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14,
14,
14,
14,
14,
14,
14,
14,
14,
14,
14,
14,
14,
14,
0,
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3,
4,
4,
4,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0,
0
] |
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