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Levels of HuR and exosomal miRNA isolated from control and 24 hrs of LPS treated RAW 264.7 cells. RNA content was normalized against total exosomal proteins (B). β-Actin as loading control for HuR western blot.
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(C) Total read counts for the ten most abundant 22 nt SARS-CoV-2 small RNAs in A549-ACE2 cells at 48 hpi. The two most abundant small RNAs derived from the ORF7a region marked by the red box in (A) are marked in red. The third abundant small RNA, marked in blue, derived from the ORF1b region marked by the blue box in (A).
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HeLa cell lines were treated with the small-molecule Bcl-2/Bcl-XL-inhibitor ABT-737 for 72 h. Cytokines were measured by ELISA. (B) Concentrations of IL-8 were determined (CTRL, n=7; Bax/Bak, n=4).
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(F) CDC induction by the 24 indicated antibodies. The % of CDC was calculated as the relative percentage of dead cells compared to the "no antibody" condition. n=3 donors of serum. Data information: Error bars indicate SEM. Significance was determined by comparing each antibody to mGO53. Only significant comparisons are depicted; *P<0.05, Mann-Whitney test.
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(A) Heat maps representing the genes significantly downregulated or upregulated in HF feeding and HF fecal transplantation at ZT0 and ZT12 (n=4, Cyber-T test p<0.05).
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RT-PCR (middle panel) and quantification (upper panel) of IPO5 minor intron 21 (U12-type) splicing on RNA extracted from HeLaEGFP-AID-CENATAC cells treated as in Figure 2C (three biological replicates, normalized to siCENATAC + IAA). The bottom panel shows RT-PCR analysis of IPO5 major intron 19 (U2-type).
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(A) Dynamic regulation of fluorescently tagged Beta-catenin/Armadillo (Arm-GFP) during mitosis in the growing fly wing epithelium. Notice down-regulation of Arm-GFP as cells round up for mitosis (arrow). Scale bar ~2µm. n>10 independent biological replicates.
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G. Pairwise scatter plots comparing the global gene expression profile of O6SKM iPSCs1 with OG2 ESCs (left) and O4SK iPSCs (right). Black lines represent a two-fold change in gene expression levels between the paired cell lines. On the right side of the plots, the color bar indicates scattering density. Red and green dots represent up- and downregulated genes, respectively. Positions of selected pluripotency-related genes are highlighted as orange points.
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(J) BAT mRNA levels from 4‐mo‐old RD‐fed Con and KO mice cold‐challenged for 75 min (n=3). Values are mean±s.e. ***P0.001.
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Experimental design. Rag1KO-mice were adoptively transferred with WT B lymphocytes and either Rab27-KO T cells (top) or WT T cells. Thereafter mice were inoculated with sheep red blood cells, and spleens and serum were harvested after 7 days.
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E. Relative mRNA expression in proximal hind limb muscle of AR21Q (n = 5) and AR113Q (n = 3) males backcrossed to C57BL/6J. ** p<0.01, ***p<0.001 by Student's t test. F. Relative mRNA expression in spinal cord of AR21Q (n = 5) and AR113Q (n = 3) males (mean +/− SEM). n. s. = not significant by Student's t test.
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V. cholerae wild-type and ΔrpoE strains carrying an empty vector control (pCtr), pRybB, or the sRNA library after consecutive selection experiments (Sel1, Sel2, Sel3) were grown in LB to OD600 of 0.2. Cells were treated with ethanol (3.5% final conc.) for 6 hours. Serial dilutions were prepared and spotted onto agar plates. R1 and R2 indicate two independent biological replicates.
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MCF10A WT or two independent clones for IRF3 KO cells were pretreated with DMSO or AZD6738 (250 nM) for 2 hours, and then irradiated with 20 Gy, 3 days later, cells were harvested for immunoblotting with indicated antibodies. Data are presented as mean + standard error of the mean of three biological replicates.
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(E) High resolution complexome analysis of SPY complex members SLP2, YME1L and PARL using MEFmitochondria (n=3). Heat maps and migration profiles are shown after separation using a 3-9% BN-PAGE. SLP2, YME1L and PARL migrate in a high molecular weight complex (2 MDa), whereas SLP2 additionally is present in complexes of 1.6 MDa).
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(F) Representative confocal images of the shift in the fluorescence emission of Keima from 458 nm to 543 nm. Scale bar, 10 μm. Cell-based studies were performed independently at least three times with comparable results.
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(C BMDMs (Zdhhc18+/+ or Zdhhc18-/-) were infected with HSV-1 (MOI=2) for 8 h, and viral titers in the supernatants were quantified by plaque assay. Data information: Data are representative of at least two independent experiments.
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USP36 interacts with SUMO in cells. H1299 cells transfected with either control or Flag-USP361-800 were assayed by co-IP using anti-Flag, followed by IB with anti-SUMO2/3 antibodies.
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B) Gene set enrichment analysis of the transcriptome data comparing uninfected vs. 48 h SARS-CoV-2 infected organoids and the "Hallmark interferon gamma response" gene set. p-values were calculated using the fgsea package from https://www.bioconductor.org with 5000 permutations.
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C. Dose response curves for the activation of a LEF/TCF reporter gene in HEK293T cells transfected with FZD4, LRP5 and with either GFP or TSPAN12 by serial dilutions of F4L5.13 or NDP proteins (x-axis). Data are presented as mean ± SEM, n=3.
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a, Samples from animals with salivary gland-specific expression of p35 (fkh-Gal4/+; UAS-p35/+), n = 18 (left), drpr null animals (+/w; +/UAS-p35; drpr∆5/drpr∆5), n = 10 (middle), and drpr null animals with salivary gland-specific expression of p35 (fkh-Gal4/w; UAS-p35/+; drpr∆5/drpr∆5), n = 16 (right), analysed by histology for the presence of salivary gland material 24 h after puparium formation. Red circles, cell fragments; yellow circle, gland fragments. b, Quantification of data from a.
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F: HeLa CRISPR/Cas9 PRMT1 deleted (KO_1) cells were transfected with Flag-tagged mutant RK or RF p14ARF-containing plasmid and subsequently irradiated at 150 J/cm2 UVC. After 4 hours, the apoptotic cell fraction was quantified by flow cytometry using FITC-labeled AnnexinV and propidium iodide (PI) for seven independent experiments (mean ± SD, *: p-value ≤ 0.05 using the paired t-test).
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(E) Quantification of reactive oxygen species. Bars indicate the percentages of cells exhibiting the reactive oxygen species-mediated conversion of dihydroethidine (DHE) into ethidium (Eth; n = 4). Data represent means ± SEM; *, P < 0.001 as compared with untreated cells of the same genotype. GAPDH, glyceraldehyde 3-phosphate dehydrogenase. RFU, relative fluorescence unit.
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Enrichment analyses of nodes in the inferred causal regulatory signaling networks of Foxd1Cre::Pdgfrb+/J mice and human CKD patients using the Biocarta database.
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B. Co-silencing of SDHB and Hsp27 reversed siSDHB-mediated AR protein upregulation in LNCaP cells.
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A. Western analysis of nuclear (N) or cytoplasmic (C) fractions from whole cell lysates (W) from A549 cells (RL WT), RNase L knock out A549 cells (RL KO), or A549 cells with either wild-type RNase L (NLS-RL-WT) or RNase L-R667A (NLS-RL-CM) fused to a nuclear localization signal sequence. Short and long exposure with anti-RL antibody. GAPDH protein used as cytoplasmic marker. Histone H3 protein used as nuclear marker. B. Graph depicting the fraction of RNase L found in the nucleus or cytoplasm. Mean and SEM of two experiments with individual experiment values plotted.
|
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F, G PLA for Parkin and ∆Tau, revealing interactions via the projection domain of tau. Data were analysed with a Mann-Whitney test (U = 185, p = 0.9224, n = 21, 18 cells/group for hTau and ∆Tau, respectively). Data information: Scale bars = 10 μm. Data are given as mean and SEM, ** = p < 0.01, **** = p < 0.0001.
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SAMHD1-flag 1-547 was cotransfected with VR1012 or TRIM21-HA for 24 h, and the cells were then treated with 10 μM MG132 for 12 h before harvest and subjected to HA IP and IB.
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Simulated 3D structures of AMSIN-1 and CBSIN-2. Their presentations are in the same pattern with that of AMSIN CBSIN-2). The interchain disulfide bridge in AMSIN-1 and the Cys1-Cys2 vicinal disulfide ring (VDR) in CBSIN-2 (shown as sticks) are denoted by arrows. The N- and C-termini are labeled. Data information: All structure images are displayed by MOLMOL.
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(g,h) IL-17A promotes biofilm formation in A. fumigatus AF293 strain. SEM images refer to cells untreated (g) or pretreated (h) with 10 ng ml−1 IL-17A for 4 h and subsequently cultured onto plastic discs for 24 h. Scale bars, 20 μm.
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Serum, liver, and lung from the VSV-infected mice were collected. The viral load of serum and tissue homogenate were measured by TCID50 assay (I), and the serum IFN-β protein level were checked by ELISA (J).
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(h) After the same treatment of peritoneal macrophages as in f, cells were stained with MitoTracker Red and MitoTracker Green for FACS analysis to determine mitochondrial potential. The numbers in g,h indicate the percentages of cells in the designated gate.
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d Immunoblot analysis of equal amounts of proteins from total lysates of CD4+ T cells treated with DMSO, U0126 (10 μM) or AKTi VIII (10 μM) and left unstimulated (-) or stimulated for 15, 120, or 300 sec with anti-CD3 and anti-CD4 antibodies, probed with the indicated phospho-specific antibodies. Anti-ERK1/2 immunoblot served as a loading control.
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E) Intersection of Nhp2 and H2AQ105me pulldown. 17 proteins were enriched in both experiments and the majority are members of the small subunit processome (highlighted in red).
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Positive correlation between a gene's median APA Shannon index across tissues and its APA switch score.
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(i) Schematic of setup used to record the movement of 5 worms each under control and 1-undecene odor exposure. (ii) Movement trajectories of N2 worms on E. coli OP50 lawn exposed to 1-undecene odor for 30 min and 60 min, each color represents the trajectory of single worm. Scale bar = 10 mm.
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(F) PAQR3-deficient HeLa cells were infected with lentivirus expressing WT or T32A PAQR3. Then PAQR3 expression levels were examined by IB.
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(H) qRT-PCR of selected genes found to be overlapping between Gata6 iKO and Eda transgenic analyzed in Gata6 WT and iKO keratinocytes (average SD, n=4). *Unpaired t-test P-values: Mcm3=0.001, Mcm6=0.02, Mcm10=0.04, Exo1=0.02, Pold1=0.02. Mann-Whitney U test P-values: Mcm3=0.03, Mcm6=0.03, Mcm10=0.03, Exo1=0.03, Pold1=0.06.
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B. Comparison of OCR vs ECAR clearly shows significant upregulation of glycolytic capacity (2 fold) in SDH-repressed cells compared to ENZA alone..
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(E) Identification of the domains of ENKD1 mediating its interaction with CP110.
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Localization of initially labeled Omp2b (green) on TRSE-labeled (red) bacteria before (0 h) and after 2 h of growth in the absence of both labelings (2 h). Scale bars: 2 μm.
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C. ELISA of IFN-b (upper) and IL-6 (lower) levels in the supernatant of (A), (B), and in vector, HDAC6, or HDAC6-CDM-overexpressing stable RAW264.7 cells treated with poly(I:C) (20 μg/ml) or transfected with 5'ppp-dsRNA (1 µg/ml).
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Quantification of mean number of TAF and % of TAF-positive CMs in 24 months old wild-type mice treated with vehicle or navitoclax (50mg/kg/day). Data are mean± SEM of n=5-8 mice per group. More than 100 CMs were quantified per animal.
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Transwell invasion assay (D) confirmed that only oemiR-370-3p can reverse oecircFNTA induced invasion in J82 cells,
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MCF10A cells were transfected with LIMT-specific siRNAs (or with control siRNA) and their migration (A, left panels) or invasion (B, left panels) were determined. Likewise, cells were stably transfected with plasmids encoding for shRNAs against LIMT (middle panels) or with plasmid encoding for either LIMT or eGFP (Control). Also shown is quantification of cell migration and invasion upon lncRNA knockdown and over-expression (OX). P-values of one-way ANOVA are presented. Each assay was repeated at least 3 times.
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GFP-ATG8a expressing seedlings in Murashige & Skoog (MS) growth medium or 30 min after treatment with MS containing ACC, ABA, ATP, BL, 6-BA, Flg22, NAA or PEP1. (C) GFP-ATG8a cleavage immunoblot for plants exposed to the same treatments as in (A). Numbers below the blots represent ratio for given sample normalized to input and relative to non-treated control. Experiments were repeated minimum 3 times with similar results.
|
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GST pulldown assays of indicated in vitro transcribed/translated 35S-Myc-CALCOCO1 constructs with indicated recombinant GST-tagged ATG8 family proteins. Precipitated GST and GST fusions and co-precipitated Myc-CALCOCO1 constructs were analyzed as in A.
|
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d, Percentage of the total variation in cell cycle duration contributed by individual phases.
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(I) Immunoblot analysis of PBMCs from Donor#1 transfected with control siRNA or NLRP3 siRNA followed by ZIKV infection (MOI=1) for the indicated time points.
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Schematics showing key assembly stages in minor intron splicing and minor tri-snRNP assembly: intron recognition (A-complex) and the catalytic spliceosome (C-complex). For simplicity, several stages of spliceosome assembly are omitted, such as the pre-B-complex, which consists of the intron recognition complex together with the tri-snRNP before architectural changes lead to the exclusion of U11 to give rise to the B complex, after which subsequent architectural changes lead to the exclusion of U4atac to give rise to the BACT complex, which is a precursor stage for the catalytically active C complex depicted in this figure (Turunen et al, 2013b).
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(c) Pan-neuronal expression of the UAS-Odc-1 in a wild-type background suppressed AMI in 30-d-old female flies (n = 7 independent experiments, F = 21.35, one-way-ANOVA with Bonferroni correction).
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Clonogenicity analysis of CLESCs treated with siArl13b and its siControl. Colonies were stained with crystal violet
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D. Bar plot shows the resample model inclusion proportion (RMIP) of qualified circRNAs calculated in the training dataset. The red line presents the threshold used to obtain the final markers.
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Anti-hTAPBPL mAb (clone 54) neutralized the inhibitory activity of hTAPBPL-Ig on CD69 expression by CD4+ and CD8+ T cells in vitro. Significance in was calculated by one‐way ANOVA with Dunnett test and others by two‐tailed Student's t‐test. * P<0.05, anti-hTAPBPL Ab group was compared with isotype Ab group.
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B,B' Generation of transformation matrices for linearization of mitochondria to analyze the directionality of the movement. The number of individual trajectories is shown in brackets.
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(C) Immunoblots for mitochondrial ferritin (FTMT) following FTMT knockdown in the absence or presence of DFP using the mitochondrial fraction of Huh7 cells and those transfected with FTMT siRNA-resistant FTMT (left panel). HSP60 as the loading control. Those cells were subjected to the quantification of mitophagy using mt-mKeima transfection and FACS analysis before and after DFP (1.0 mM) treatment (n=5, biological replicates) (right panel). The central horizontal bar and the error bards indicate mean ± SD. The Tukey's honestly significant test was used for statistical analysis. ***: P<0.001.
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(D) Relative GFP-Buc density at the cleavage furrow of 4-cell stage embryos injected with GFP-Buc mRNA + RFP mRNA (n = 11), GFP-Buc mRNA + RFP mRNA + Control MO (n = 11) and GFP-Buc mRNA + RFP mRNA + kif26ab MO (n = 10). Data shown are mean ± SEM (n = the number of embryos analyzed).
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E. left panel; Superimposed single-cell traces representative of the effect of 100 μM D-Asp on [Ca2+]i detected in MO3.13 cells in presence of siCtl or sincx3 silencing. E, right panel; Quantification of the oscillation index in MO3.13 cells in absence or in presence of sincx3. e, Quantification of the initial [Ca2+]i increase elicited by D-Asp and measured as ∆% of peak versus basal values in absence or in presence of sincx3 Data information: The values represent the mean ± S.E.M from 3 independent experimental sessions. Level of significance was determined by usin E and e, one way-ANOVA P<0.001 followed by Bonferroni post hoc test, *P< 0.05 versus sictl, ˄P< 0.05 versus D-Asp + sictl. Data are reported as mean of 25-30 cells in each group, n=3 biological replicate
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Knockdown of endogenous CSAG2 in HCT116 (H-I) cells increased p53 ac-K382 levels. CSAG2-knockdown stable cells were treated by 1 μM doxorubicin/ 0.4 μM TSA for 6 hr. Cells were then harvested and blotted for the indicated proteins. Quantitation of ac-p53 K382 levels relative to total p53 is shown (I as the mean ± SD, n=3 biological replicates.
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mTORC2 in adipose tissue is not required for cold-induced mitochondrial uncoupling and β-oxidation. (A) mRNA levels of the indicated genes in BAT of AdRiKO and control mice housed at 22°C or at 4°C for 8h (n=6/group).
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(E) NSG mice (n = 5 mice per group) were injected with 5x102 4T1LN or 4T1PT cells collected from control IgG-, anti-CD4, or anti-CD25 antibody-treated 4T1 tumor-bearing mice. Distant organ metastasis was examined by bioluminscent images on day 21. The bioluminescent signal (pseudocolor) was recorded as photons per second per centimeter squared per steradian (p/s/cm2/sr) and the luminescent image was overlaid on the photographic image.
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(D) Length of the 5'UTR of mRNAs that are more actively translated by the CMB cells (as compared to CTRL cells) vs. non-target mRNAs (n=3). The central band corresponds to the median. The lower and upper hinges correspond to the first and third quartiles (the 25th and 75th percentiles). The upper and lower whiskers extend from the hinges to the largest and smallest values no further than 1.5 * inter-quartile range from the hinges, respectively.
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(C) Macrophages from (B) were exposed to mock, infectious, or RNase/DNase I treated AT-2-inactivated purified HIV for 24 h. Cells were harvested and qRT-PCR for UVRAG, ATG9B, MCOLN1 was performed. Data were normalized to the shNS mock infected control for each gene. Bar charts are reported as mean ± s.e.m., n = 4.
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(A) Tumor growth delay was measured in the different groups, as indicated (n=6 mice per group). Anti-PD-L1 was given at days 0 3, 6 and 9 (black arrows). The average time (days) for tumors to reach a volume of 400 mm3 from day 0 is shown (means ± SD, n=1, One-way ANOVA, Bonferroni test). No weight loss was observed in the in vivo experiment
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The Cse4-containing nucleosome is depicted with the extended N-terminus, which carries R37Me and K49Ac. COMA subunits are shown in colour.
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A Overview highlighting the positions of TC, eIF1 and eIF1A in the complete human 43S PIC.
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(A) The C106 mutation (C106S) of HMGB1 impairs its nuclear localization. Hmgb1−/− MEFs were transfected with wild-type and cysteine mutant HMGB1-GFP plasmids as indicated and then were treated with 1 µM rapamycin for 12 h or starved (HBSS) for 3 h. The mean nuclear (Nuc) and cytosolic (Cyt) HMGB1 intensity per cell was analyzed by imaging cytometric analysis. *, P < 0.05 versus HMGB1+/+ group; n = 3. Representative images of HMGB1 location are shown on the left (green, HMGB1; blue, nucleus). The right panel is a schematic diagram of HMGB1 structure illustrating the basic A box and B box as well as the acidic C-terminal domain, with the cysteine mutation locations identified.
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(B) Cumulative amphetamine-induced ipsilateral rotations. Progression of amphetamine-induced ipsilateral rotations over time (right panel). Mean + SD are shown, n=11-12 animals in each group. Tukey post hoc analysis after two-way RM ANOVA, **** P <0.0001 compared to the initial rotation score at week 2. Comparison of the treatment's effect between groups (left panel). Mean + SD are shown, n=11-12 animals in each group. Tukey post hoc analysis after two-way RM ANOVA, *P < 0.05, **P < 0.01 compared to vehicle group.
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B, Immunoblots of PRL1 expressed in HEK293 cells show phosphorylation requires the catalytic cysteine (C104) but not the adjacent cysteine (C49) in the active site.
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(D) Representative images of tumor cell proliferation determined by immunofluorescence Ki67 staining in A375 xenografts treated as indicated. Bar graphs indicate the Ki67+ area/tumor area (n=4 tumors), ***P < 0.001 versus vehicle (PLX4720 P = 2.83E-08; bevacizumab P = 4.25E-13; COMBO P = 6.16E-08).(E) Representative images of tumor cell apoptosis determined by immunofluorescence staining with TUNEL in A375 xenografts treated as indicated. Bar graphs indicate the TUNEL+ area/tumor area (n=3 tumors). ***P < 0.001 versus vehicle (P = 6.2.7E-10).
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GST pull-down analysis of interactions between wild type (WT) or LIR-mutant (L219A/V222A) Stx16 and GST-tagged LC3C or GABARAP. Lower panel shows percentages of WT or LIR-mutant Stx16 bound to GST-LC3C or GST-GABARAP. Data shown as means ± SEM of precipitated Stx16, n = 3.
|
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A FLIP of BaxTBakSS without (○, broken line) or with (●, straight line) overexpressed Bcl-xL. Fluorescence of a neighboring cell is shown as control (, dotted line). Data represent averages ± SEM from 20 (-Bcl-xL) and 16 (+Bcl-xL) ROI measurements.
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NIH3T3 cells stably expressing the WT or mutant forms of vBcl-2 were treated with TNFα and cycloheximide (CHX) for 12 h, then assayed for cell viability by trypan blue exclusion assay (A),
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Mouse GDF15 plasma levels in post-absorptive state of young (10wks) vs. old (95wks) male WT and TG mice (young WT n=10, TG n=13; old WT n=13, TG n=13).
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] |
C-F. HA-tagged poly-GA, poly-GP, poly-GR or poly-PR (red) and EXOSC10 (green) were immunostained with anti-HA and anti-EXOSC10 antibodies. Nuclei were stained with DAPI (blue).
|
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I. ChIP analyses of endogenous β-catenin binding at the TCF-binding site of the Axin2 promoter were performed in FoxM1 siRNA-, ICAT siRNA-, control siRNA- or combination of FoxM1 siRNA and ICAT siRNA-transfected U87 cells as described in (H).
|
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B. GOLPH3-OE HeLa cells were fixed and processed for IF: Endogenous LCS (green), GOLPH3 (red), and TGN46 (blue). Dashed lines indicate cells overexpressing GOLPH3. Scale bar, 20 µm. Quantification of the amount of endogenous LCS (right graph) at the Golgi (data are means ± SEM derived from two biological replicates, n=21 in CTRL, n=11 in GOLPH3 OE; ***p <0.001 [Student's t-test]).
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(H) Quantitative representation of the percentage of DIV14 neurons transfected with PEX-RFP together with either KIF1C, KIF21A or KIF5B and an indicated shRNA. as in (A) in which after addition of rapalog peroxisomes redistributed to axons ("a", blue bars), to both axons and dendrites ("a+d", red bars) or did not redistribute into any neuronal compartment ("nt"-no targeting, gray bars). Per condition 19-44 neurons were analyzed; N = 2.
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The expression of indicated markers was analyzed in 5.2+ vs 5.1+ pDC of each MBMC type. Results were expressed as 5.2/5.1 ratio of Mean Fluorescence Intensity (MFI) values for CD86 or of the percentages of IFN-I-producing cells obtained from CpG-stimulated mice. Black, CTR MBMC; red, Ifnar1-TST MBMC (red) Data shown (mean±SEM) are from 2 pooled independent experiments each with at least 3 mice per group.
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Total sleep for Tβh mutant and control flies in video-based method (From left to right mean±SEM: 688.2±32.71, n=48; 123.2±11.68, n=46).
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(C) Immunoblot analysis as in (A) but in cortex (CTX), hippocampus (HIP) and mid‐brain (MB).
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Following BAK1 depletion, possibly by pathogen effector actions, MAMP-triggered outputs including induction of PROPEPs are weakened. However, effector-dependent PROPEP induction compensates for low amounts of MAMP-induced PROPEPs in the absence of BAK1. Cell death spread following dysfunction of BAK1/BON-mediated control probably facilitates release of cytosolic PROPEPs into the extracellular space. Moreover, in the absence of BAK1/BON1 complexes, PEPR signaling is strengthened by the stabilization of the receptor and by the potentiation of SA-related defenses toward anti-biotrophic resistance.
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Effect of antimonial drug resistant and sensitive forms of the Ld (LdR and LdS) on cellular cytokine level RAW 264.7 cells were infected with Antimony sensitive (LdS-Ag83) and antimony resistant (LdR-BHU569) form of Ld for 24 hours along with uninfected cells kept as control. IL-10 (A) and TNF-α (B) were measured at mRNA level by qRT-PCR after infection (mean+/- s.e.m. and, n=4).
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A. Reconstitution of yeast V-ATPase from Hchim containing V1 (V1Hchim), lipid nanodisc reconstituted Vo (VoND), and recombinant subunit C.
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Distribution of mitotic spindle orientation of dividing cells from wildtype H9 hCOs, #6 and #23 RGCC-KO hCOs. Each plot represents a dividing cell (H9, n=22; #6, n=27; #23, n=39 from 2 independent experiments). Statistic analysis of splitting plane angle in RGCC-KO hCOs. Data were presented as mean ± SEM. Each plot represents a dividing cell (H9, n=22; #6, n=27; #23, n=39 from 2 independent experiments).Statistical significance was tested by one-way ANOVA. **, p<0.01; ***, p<0.001; ****, p<0.0001.
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F. Line scan analysis taken from white dashed lines in (E) showing intensity changes of P4M and TGN38 signal from control (top) and NPC1I1061T (bottom) cells.
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C Shoot phenotypes of Mx under control (Hoagland nutrient solution) and excess Zn (300 μM Zn) conditions for 3 weeks. Scale Bar: 1 cm.
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(H) Quantification of PLA signals from (G). Data in (A) to (H) are representative of at least three experiments with graphs depicting means ± SEM
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Figure 8. Model of p53 binding and local histone modification as a form of genome protection to DNA damage stress.
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(a-c) Native merged images or images with colocalization highlighted in white pixels are shown. Nuclei are blue (DAPI). Scale bar, 10 μm.
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A, NPCs carrying Dnmt3a/b-KO or WT alleles were differentiated into neurons. Neurons were isolated by FACS and their DNA methylation patterns analyzed using RRBS (n = 3 cultures per genotype).
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A Immunoblot analysis of USP33 and HIF2α protein levels in T387 GSCs expressing USP33-targeting shRNAs (shUSP33) or non-targeting shRNA (shNT). Targeting USP33 by two distinct shRNA clones through lentiviral infection reduced USP33 and HIF2α expression in GSCs.
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Representative images of H&E and immunohistochemical staining for lung differentiation markers TTF-1 and Mucin 5B for at least 2 independent regions of n=4 H1299control and n=2 H1299RASSF1A primary tumours at day 17 with quantification (right) of TTF-1 based on nuclear intensity. Scale bars 100µm. Statistical significance was determined by Student's t-test (2-tailed). Error bars represent the mean ± S.E.M
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A In vitro differentiation to mature ookinete of wildtype (WT), Δisp1, Δisp3, and Δisp1/3 parasites. Values are means ± SD (n=4 biological replicates); two-tailed t test, *, P<0.05, **, P<0.01, ***, P<0.001, ns: not significant.
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D. Size of lumen in cells transduced with WT or mutant INVS is shown. Results presented are scatter plots of acini size (n=205 for Vector, n=143 for HA-WT, n=131 for -3D, n=167 for -3A, n=144 for -R899X, n=128 for -Q671X, and n=144 for -R603X INVS stably transfected MDCK cells, respectively). Two independent experiments showed similar results. Statistical significance was determined by Mann-Whitney's non-parametric median test.
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(D) Gene expression of VE-cadherin (CDH5) from sh-Control and sh-PI3KC2β hCMEC/D3 cells in resting condition or after 6 hours of stimulation with TNFα. The mRNA levels are given as fold change to resting control hCMEC/D3 cells normalized to PGK1. Data represent mean ± SEM of n=3 independent experiments in duplicate; for Sh-PI3KC2β+TNFα, n=3 independent experiments with only two experiments in duplicate. No significant changes between conditions were noted (Mann-Whitney test).
|
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(E) Alignment of the RGG box of in ICP27 proteins of the simplexvirus genera of alpha-herpesviruses.
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Balb/C mice were aerosolically challenged with Rv, Rv∆aosR, and Rv∆aosR::aosR strains. Each data point represents log10 CFU obtained from the infected lung of mice and error bar depicts the median with interquartile range for each group. Each data point represents log10 CFU obtained from the infected spleen of a mice and the error bar depicts the mean with SD for each group.
|
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D Comparison of cell size in WAT of WT and FADD-D mice maintained on SD and HFD (n = 5 for each genotype).
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Top panel, left to right: NSP5-∆CTR labelled with Atto-647 (25 μM) incubated with unlabeled NSP2 (10 μΜ); NSP5-∆CTR in the presence of 10% v/v PEG-20K; and with 5 μΜ of poly-arginine (polyArg). Bottom panel: Atto-647-labelled NSP5-∆CTR (5 μΜ) incubated with unlabeled NSP5 (25 μΜ) and Atto-488 labelled NSP2 (10 μΜ). NSP5/NSP2 droplets containing labelled NSP2 (green) also contain NSP5-∆CTR-Atto647 (magenta), shown along with an image of both 488/647 channels overlaid. Scale bar, 10 µm.
|
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Representative images of H&E and cleaved caspase-3 staining from each treatment group (E).
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