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Similarity plot of the near full-length genome sequence (A) and S gene sequence (B) of Pangolin-CoV to sequences of 2019-nCoV_WIV02, Bat-CoV RaTG13, Bat-CoV ZC45 and Bat-CoV ZXC21. While Pangolin-CoV has a high sequence identity to 2019-nCoV and Bat-CoV-RaTG13 in most regions of the S gene, it is more similar to Bat SARSr-CoV ZXC21 and Bat SARSr-CoV ZC45 at the 5′ end (B). More importantly, Pangolin-CoV is highly similar to 2019-nCoV in the functional RBD region of the S protein, with only one amino difference (insert in B). Because of the presence of genetic recombination, there is a discrepancy in cluster formation among the outcomes of phylogenetic analyses of different regions of the S gene (C). | [
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(E) Venn diagram showing overlapping between DVL3-bound genes and DVL3 transcriptional targets in MCF7 cells. A total of 3% of differentially expressed genes identified by RNA-seq comparing NTC and shB DVL3 were also DVL3 direct targets identified by ChIP-seq. From these, 87.5% were up-regulated and 12.5% down-regulated. A total of 5.6% of differentially expressed genes identified by RNA-seq comparing EV and DVL3-WT were also DVL3 direct targets identified by ChIP-seq. From these, 56.5% were up-regulated and 43.5% down-regulated. | [
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Clustering of metabolome data in patients and controls; PLS-DA plots; VIP score plots of top 15 metabolites; volcano plots of all metabolites in blood of PEO (C) Data information: Colours in VIP score and volcano plots indicate the same most relevant and/or significantly changed metabolites among all patients groups. C3, component 3; CDCA, chenodeoxycholic acid; GABA, γ-aminobutyric acid; OH-Kyn, 3-hydroxy-DL-kynurenine | [
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(f) NRK cells stably expressing LAMP1-Cherry; clathrin-GFP were starved for 4 h and time-lapse images were acquired by spinning-disc microscopy. Scale bar, 500 nm. The white arrows indicate a clathrin punctum moving along a LAMP1-positive structure. | [
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CV protrusions (arrowheads) and vascular loops (asterisks) were observed in zebrafish at 35 hpf. The images within the dotted rectangles are magnified in the right panels. A, anterior; P, posterior; CA, caudal artery; CV, caudal vein. Scale bars, 40 μm. Quantification of the length of the CV protrusions in (G) presented graphically by measuring them in equivalent fields of view (within five somites). | [
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A, Immunoblot analysis of protein lysates from HeLa cells treated with EBSS for 1 h and then incubated with complete medium (refeed) for the indicated times. Samples were run under non-reducing conditions. B, Quantification of immunoblot data shown in (A). Data are presented as mean ± SD using one-way ANOVA (*)p<0.05, and (***)p<0.001 from three independent experiments. C, Quantification of immunoblot data shown in (A). Data are presented as mean ± SD using one-way ANOVA (*)p<0.05, and (***)p<0.001 from three independent experiments. | [
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c, An ML1-/- skin fibroblast cell showed autofluorescence in LAMP1-positive compartments. Autofluorescence (green) was detected within a range of excitation wavelengths (shown with excitation at 480 nm). No significant autofluorescence was observed for a ML1+/+ cell. Lysosomes were stained with a LAMP1 antibody (red). Differential interference contrast (DIC) images are shown for comparison. | [
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(A) Gene expression analysis of WT and Clec12a−/− BMDMs infected with Listeria for the indicated times. Heatmap shows log2 (fold change) relative to uninfected WT BMDMs at indicated time points. Shown are the top ten most-significant upregulated and downregulated genes in Clec12a−/− BMDMs compared to WT BMDMs. | [
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Re-introduction of Cideb rescues SREBP processing in Cideb-/- liver. WT and Cideb-/- mice were injected with AAV-GFP or AAV-Cideb, and sacrificed for IB with the indicated antibodies 20 days after the injection. | [
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(F) Patient-derived and control B cells were cultivated for 24 hours and TNF was determined by ELISA. Data are presented as mean ± SD of 3 individual experiments performed in two technical replicates; *, P = 0.028; unpaired t-test. | [
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A Recombinant Gadd45a protein and its G39A mutant were added to the histones-oligo DNA mixture. The mixtures were separated by 4% non-denaturing PAGE and stained with ethidium bromide (EB). The oligo DNA probes were amplified from the Oct4 promoter. | [
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(E) mRNA relative expression level of Il-6, Il-12 and Il-23 from XBP1fl/flIRE1fl/fl, XBP1ΔDC IRE1truncDC and XBP1ΔDC BMDCs infected with Pru parasites for 16 h compared to non-infected (NI) conditions. Results are normalized to the housekeeping gene Gapdh. Two-way ANOVA Tukey's multiple comparisons, ns: p>0.05; *: p<0.05; **: p<0.01; ***: p<0.001; ****: p<0.0001; mean ± S.E.M (n=3-5 mice pooled from 2 independent experiments). | [
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(a) Quantification of numbers of hyperplastic lesions/per lung (mean values±s.e.m.) in KRas;Atg5fl/+ and KRas;Atg5fl/fl mice2 weeks after AdCre inhalation treated either with an isotype control Ab or a depleting anti-CD25 Ab. n=4 per group. **P0.01 (χ2-test assessing the genotype effect in a generalized linear model with log link). (b) Histological lung sections of KRas;Atg5fl/+ and KRas;Atg5fl/fl littermate mice treated with an isotype control Ab or anti-CD25-immunodepleting Abs. Mice were killed 2 weeks after AdCre inhalation and their lungs were processed for histopathology. Representative lung images (haematoxylin and eosin (HE) staining) are shown for each genotype and treatment. Scale bars, 2 mm. | [
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Western blot analysis of unsynchronized HeLa-H2B/tub cells was carried out to monitor expression of p(S10)-H3, total H3 and TIAR in control and TIAR-depleted cells (mean ± SD; n = 3). Data information: Statistical significance was determined by unpaired Student's t-test; *, p < 0.05; **, p < 0.01; ***, p < 0.001. | [
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Longitudinal 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 effect of time plus the biomarker by time interactions, capturing the longitudinal effects of the biomarkers. For each model, the "average" effect of time is also shown for comparison. Effects were significant (*), meaning that biomarker levels affected the slopes of the outcome, for FDG-PET: T-tau (p=.00038) and Ng (p=.0019) in A-positive. 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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(C, D) Quantification (C) and images (D) of hACE2 protein expression level by Western blot from the lungs of the same mice as in panels A and B, presented in the same order. | [
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(E) Relative expression of in vitro transcribed CGG-nLuc reporter in HEK293T cells pre-treated with DMSO and SRPIN340. Error bars represent mean +/- SD (n=9 biological replicates). Data information: Statistical analysis was performed using Student's t test with Welch's correction. ∗p < 0.05; ∗∗p < 0.01 | [
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(D) Representative confocal micrographs (as maximum intensity projections) of wild-type K562 cells and indicated deletion isolates expressing tf-NBR1. Selected regions (white box) of micrographs are shown as single and merged channels from fluorescence microscopy. Red fluorescent protein (RFP), magenta; Green fluorescent protein (GFP), green; Hoechst, blue. Scale bars: large panels, 5 µm; small panels, 1 µm. All images scaled equally. | [
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G. P493-6 cells were co-transfected with the indicated reporter constructs and Renilla luciferase plasmid. Twenty-four hours after trasfection, cells were treated with doxycycline for 0 hour and 12 hours respectively. Then reporter activity was measured and plotted after normalizing with respect to Renilla luciferase activity. Data shown are mean ± SD (n = 3; **P < 0.01, two-tailed t-test). | [
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B S1 and S3 alleles, by virtue of limited geometries (modified from Chattopadhyay et al, 2005), may have access to distinct subsets of the full range of biological activities of WT PrP, which has access to interchangeable component 1, 2 and 3 geometries. | [
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G Representative images of ALP, ARS and Van Gieson's staining of MSCs obtained from Sp7-Cre;Usp34f/f and littermate control mice | [
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(d) Left panel: Flow cytometry characterization of BOECs for endothelial, leukocyte and progenitor cell markers (grey - isotype control; red/blue/green/purple - cell lineage marker staining). HUVEC and monocytic THP-1 cells were used as positive controls for endothelial and leukocytic markers respectively. Right panel: Percentages of positively expressing cells. Sample sizes are n = 4-6 healthy, n = 2-7 NAFLD. | [
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(B) Mononuclear cells were isolated on day 30 of animals shown in (A) from the CNS of PBS- and DTX-treated CD11c-DTR/GFP→C57BL/6 that had been transferred with 2d2.tdRFP Th17. Flow cytometry was performed on surface stained cell samples. Cells were pre-gated on lymphocyte cells (FSC SSC gate) and PI-negative; pooled data of three animals; representative of two independent experiments. | [
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(B) Chromatin transitions within differential active states between NBCs and CLL. Heatmap representation of the amount of chromatin (log2 Mb+1) transitioning from a particular state in NBC (rows) to CLL (columns). Transitions were considered for all recurrent active chromatin state regions (states 1, 8 ,9 and 11) present in a minimum of 3 samples even if the consensus state was not an active state. Accordingly, the matrix includes transitions between non-active states at low frequencies. | [
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A. In Brachyury (T)-Cre; mTmG embryos, mesoderm-derived cells express membrane eGFP (mG, green) and the other cells membrane tdTomato (mT, grey). | [
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(E) Level of eIF-2a and its phosphorylated form, estimated by western blot using specific antibodies, in siCon or siHuR treated and starved Huh7 cell extracts. Western blot data of HuR confirm reduction of this protein upon siRNA treatment. CAT-1 and Aldolase mRNA levels were estimated by real time quantification and normalized against GAPDH level. Values of siCon treated samples were taken as unit (mean+/- s.e.m., n=3). In the right panel the relative quantity of phosphorylated eIF-2a measured by densitometry were plotted. Levels of p38 and phosphor-p38 levels in siCon and siHuR treated Starved Huh7 cells were detected by western blot. | [
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Immunoblot analysis of phosphorylated ULK1 (Ser 757), total ULK1, and actin in KRIT1 KO+KRIT1, and KRIT1 KO MEFs. Where indicated, cells were treated with 100 nM Torin1 for 4 h. The results are representative of three independent experiments. | [
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Bar plots showing relative occurrence of differential-splicing events in IMR90 undergoing senescence (left), in HMGB1-knockdown IMR90 (middle) or in HMGB1-bound mRNAs (right). The number of bound mRNAs (N) analyzed is indicated below each bar. Venn diagram showing differential-splicing events shared between conditions from panel F. | [
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During cellular stress, Nox4 at the MAM augments the level of Akt activation secondary to redox inhibition of PP2a. Activated Akt in turn phosphorylates InsP3R and leads to an inhibition of calcium flux from ER to mitochondria. Mitochondrial calcium is maintained at a low level, the mitochondrial membrane potential (ΔΨm) is preserved, and cells remain viable. When Nox4 is deficient (bottom panel), high PP2a activity dephosphorylates Akt and leads to a reduced level of InsP3R phosphorylation. This removes the restraint on calcium transfer from ER to mitochondria resulting in increased mitochondrial calcium levels, triggering of the mPT, loss of ΔΨm and eventual cell death. | [
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F. Western blot analyses of cortical and hippocampal lysates from APP/PS1mice for APP and sAPP expressions. | [
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(A-D) Changes in mRNA transcript levels of a series of adhesion molecules (A), chemokines (B, C) and cytokine receptors (D) in injured retinas compared with contralateral noninjured retinas, assessed 1 day after GT intoxication. n = 6 per group. | [
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F Violin plots of selected genes showing the comparison between control and MECP2-KO neurons from the single-cell analyses (log2(expression) values) that overlapped with the results obtained via RT-PCR array. | [
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(C,D) In the SS of adult rhesus monkey, COX6A2 immunoreactivity is present exclusively in PV+ cells (n animals=1, 1-year-old, n sections=6). White arrowheads indicate PV/Cox6a2 double positive cells. | [
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(E) Western blot of whole cells lysates stained with an α-HA antibody. Residues exchanged with BrEtY are indicated in the upper row, mutations at PTH1R are indicated on the left side. The red arrows indicate the two most prominent signals. Red squares indicate signals that vanish upon removal of specific Cys residues in PTH1R. | [
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F. FACS plots illustrate the gating and percentages of common lymphoid progenitors (CLP). Bar graph shows the absolute number of CLPs per 2 femurs and 2 tibias (n=5 mice for each genotype). Data information: All data are presented as mean±SEM. *p<0.05; **p<0.01, and ***p<0.001 by with one-way ANOVAs with two-tailed Student's unpaired t-test analysis for comparison of WT to PKCδ KO mice. | [
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Spata2+/+ (WT) and Spata2-/- (KO) mice were injected intraperitoneally (i.p.) with alum (20 mg/kg bodyweight) and sacrificed 6 h latter to collect peritoneal lavages. Absolute numbers of neutrophils recruited to the peritoneum were counted by FACS (G) | [
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a, Effect of oligomycin (Oli) and DMSO (Ctrl) on spherogenic potential of +/−KRas cells (n = 8); representative calcein staining. | [
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C. Statistical analysis of absolute number of total nucleated cells from bone marrow B-cell subsets. Results represent the data pooled from three independent experiments and numbers represent biological replicates for each group (WT; n = 5, KO; n = 7). Bars and error bars indicate mean ± SD. | [
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(A) Macrophages transduced with non-specific scrambled shRNA (shNS), or BECN1 shRNA (shBECN1) were infected with HIV for 10 days. Cells were lysed and analyzed for BECN1 and ACTB content by Western blotting. Left, a representative blot is shown. Right, densitometric analysis of immunoblots from independent donors presented as means ± s.e.m., n = 4. | [
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(d) Cdk5 mediates the MPP+-induced EndoB1 phosphorylation at Thr 145 and the MPP+-induced increase in the LC3-II level in neurons. | [
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(C,D) Quantification of the nuclear morphologies (C) or γH2AX-positive DNA damage foci (D) from MCF7, MCF7 p53 KO or T47D cells that were treated with palbociclib (1μM) for 0, 1, 4, or 7 days and then analysed 48hr after drug washout. Either 100 cells (nuclear morphology) or 50 cells (γH2AX) were scored per condition per experiment and bar graphs represent mean data + SEM from 3 experiments. | [
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(A) ROS burst in WT and rgi5x after elicitation with 100 nM flg22. Shown is the kinetic of ROS production over 40 min -/+ SE, n=8 biological replicates. RLU = Relative light units. Similar results were obtained in 3 independent experiments. | [
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B. HAT1-catalyzed histone H3K122 succinylation was analyzed by mixing purified HAT1, histone H3 or histone H3 mutant (K122R), and succinyl-CoA in the in vitro succinylation assays. Heat-inactivated HAT1 was used as a negative control. Western blot analysis was performed with indicated antibodies. | [
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Proposed model. CRL2-operated "double-end" inspections safeguard the mitochondrial localization of MIC19. | [
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A. Representative image of CENP-B box FISH and mFISH stained RPE-1 metaphase spread cells. Chromosome 3 homologs are indicated by white arrows with single CENP-B box chromosomes signal magnified in insets. Scale bar represents 5 µm. | [
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(c,d) Multiple proteases are expressed across lung cell types. (c) Distribution of expression (y axis) for ACE2, PCSKs and TMPRSS2 across lung cell types (x axis). White dot: median expression. (d) Proportion of cells (y axis) expressing ACE2, PCSK family or TMPRSS2 across lung cell types (x axis), ordered by compartment. | [
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Mean number of both TAF and non-TAF in neonatal rat cardiomyocytes at days 0, 3, 5, 10 days following treatment for 24h with H2O2. Data are mean ±S.E.M of n=3. >50 cells were quantified per condition. | [
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U2OS-LacO cells transiently expressing EGFP-LacI-Bub1-K together with VSV-Sgo1 or a control vector Cell lysates were immunoblotted (L). * represents non-specific bands. | [
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(F) Scatter dot plots representing normalized total area of the Zwilch and Spindly signals, normalized to the reversine-untreated control, in the indicated number of cells from the experiment shown in panels C-D. Red lines indicate mean and standard deviation. Statistical analysis was performed with a nonparametric t-test comparing two unpaired groups (Mann-Whitney test). Symbols indicate: n.s. = p > 0.05, ∗ = p ≤ 0.05, ∗∗ = p ≤ 0.01, ∗∗∗ = p ≤ 0.001, ∗∗∗∗ = p ≤ 0.000. | [
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(B) qRT-PCR data comparing fold change in eGFP transcript levels relative to ITR2 amplicons from retinal samples infected with all four capsid variants. | [
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A) Partial amino acid sequences of the hMPV F (blue) and hRSV F(red) antigenic site II (Lopez et al., 1998;McLellan et al., 2011b;Toiron et al., 1996). Partial sequences of the F-415 and F-416 chimeras are color coded to indicate the origin of their antigenic site II residues. Amino acids shared by hMPV F and hRSV F are colored purple. The remaining sequences of F-415 and F-416 are derived from hMPV F. | [
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Plot of change in fluorescence from baseline to peak fluorescence for Munc18-1 G544D (H) Data are means ± SEM (*p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001 by one-way one-way ANOVA and Dunnett's multiple comparison test; n = 7-23; exact n and p values are shown in Appendix Table S1). Note, that compound 10 is fluorescent at a similar wavelength than pHluorin, so experiments at concentrations higher than 1 µM were not possible. | [
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O. Purified recombinant His-Erk2 protein incubated with the purified PBK in the presence or absence of ATP (100 μM ) or menin inhibitor (1 μM or 0.1 μM), as indicated. After SDS-PAGE, the phosphorylation of Erk2 was detected with the pERK1/2 antibody. Anti-ERK1/2 antibody showed that equal amount of Erk2 was used for the kinase assay. | [
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Figure 5. SLFN11 inhibits homologous recombination repair. (A-B) SLFN11 suppresses SCE. Representative metaphase spreads showing SCEs from wild type and SLFN11-deficient SF268 cells (red arrows) (A). SCEs were scored for 50 metaphase spreads for each cell line (B). Each point represents the total number of SCEs in a single metaphase spread, and black bars indicate the average value for all spreads. Statistical significance was determined using the Mann-Whitney test (***P < 0.0001). | [
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D-E. Bar graphs showing the number of Jmjd2a peaks displaying at least 1 bp overlap with (D) an H3K4me3 peak. Jmjd2a peaks were classified as TSS-associated ('TSS') if overlapping a region of +/- 1kb of a TSS. | [
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(A) XO8 GSCs and DFCs were differentially labeled with PKH67 (green) and PKH26 (red), respectively, and mixed before plated on laminine-coated plates. The cells were treated with 50 nM MG132 and subjected to fluorescent microscopy. Scale bar, 100 μM. (B) Quantitation of (A). Cell numbers from three independent experiments were normalized to those of control cells treated with DMSO and presented as means +S.D. (*p=0.0035, n=3). Student t-test (two-sided, one type) were used for statistical analysis. | [
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Quantification of the inhibitory effect of BO-110 (BO, 0.8 mg/kg, 2 doses/week I.P. administration, 11 weeks) on the growth of melanoma PDXs. Red arrows mark the initiation of treatment. Shown are mean tumor size in mm3 ± SD in biological triplicates. Statistical significance was determined by Two-Way-ANOVA. P = 0.0009. | [
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C Conformational changes of the alkaline groove between T4L fusion Ca2+-free MICU1-MICU2 and partial Ca2+-bound MICU1-MICU2 heterodimers. Inset, KRKK residues in the alkaline groove rotate upon Ca2+ binding. | [
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(H) Immunoblotting and quantification of total and Afadin S1795 phosphorylation in adipose tissue depots from 12-week old C57BL/6 male mice fed with either chow (CD) or high-fat diet (HFD) for 6-weeks injected with vehicle or insulin (n=6). | [
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C. Top 10 biological process gene ontology terms as determined using DAVID for genes regulated by BAZ2A in ESC+2i and ESC+serum. | [
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(A) lncPSCA predominantly locates in the nuclear fraction of gastric cancer cells. In detail, the cytosolic and nuclear fractions of HGC-27 or MGC80-3 cells were separately isolated. RNA was isolated from either the cytosolic fraction or the nuclear fraction. Expression of lncPSCA in the cytosolc and nuclear RNA was measured. Data show one representative example of three biological replicates. | [
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A Immunofluorescence images showing 53BP1 and γH2AX foci in A549 cells after 2-Gy radiation and A549 cells pre-treated with 6 μM RK-33, 12 h before radiation. Overlap of 53BP1 and γH2AX is seen in the merged picture of the co-immunofluorescence staining. Scale bar is 2 μm. | [
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(C) A heatmap showing the partial correlation between the expression of UPR branch pathway genes with SCNA levels controlling for the effect of the gene copy number change using data from GISTIC2.0. Rows depict genes from the UPR branch pathways from REACTOME and columns depict the 32 tumor types. Cells are colored in red or blue if the gene showed significant correlation with SCNA level in that tumor type (partial correlation test setting copy numbers for genes as control, after Benjamini-Hochberg multiple hypothesis correction, FDR < 0.05). Color intensity corresponds to the partial correlation coefficient between gene expression and SCNA level. The left side bar indicates pathway membership of the genes. The bottom panel shows the variances of SCNA scores for each tumor type and the number of normal tissue samples available for partial correlation analysis. | [
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C) Schematic representation of TSP1 monomer and the TSP1 proteolytic fragments (N-term, C-term) and recombinant domains (P123-1, E123-1, E123CaG-1, Ca-1) used in the study | [
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(C, D) Expression of GGGGCC-nLuc-3xFLAG (C) and +2CGG-nLuc-3xFLAG (D) RAN translation reporters in HEK293T cells treated with 2 μM TG (for stress induction) analyzed by immunoblot (n=3 biological replicates). To evaluate effects of SRPK1 inhibition cells were pre-treated with DMSO or SRPIN340 before reporter transfection. Data information: Error bars represent mean +/- SD. Two-tailed Student's t test with Welch's correction. ∗p < 0.05; ∗∗p < 0.01; ∗∗∗p < 0.001 and ∗∗∗∗p < 0.0001. | [
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Immuno-EM of SipB-transfected COS-2 cells. COS-2 cells were transfected with a plasmid expressing SipB-YFP, and 24 h after transfection, cells were fixed and prepared for immuno-EM using an antibody specific for GFP and a gold-labeled anti-rabbit antibody. SipB was seen localized to structures made up of closely apposed membranes that were often in close proximity to mitochondria (A). Mitochondria were often seen apparently fusing to the SipB-induced membranous structure (B, see arrows in inset on top; C, inset to the right). Mitochondria were often seen contained with the SipB-induced membrane structures (D). Bars, 250 nm. | [
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The expression of the stemness markers SOX2 and NESTIN was evaluated by western-blot and immunofluorescence (SOX2 in red NESTIN in green) in MPZ (+, 20 μM, 16 hours) and vehicle (-, DMSO, 16 hours) treated GSC#9. GAPDH served as a loading control. Scale bar: 10 μm. | [
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(B) Vector copy number (VCN) in peripheral blood eight weeks post-transplantation (mean ± SD, each dot represents an individual mouse). | [
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(C) Schematic representation of the PP2A holoenzyme that is composed of a catalytic subunit (PP2Ac), a scaffold protein (PR65), and a variable regulatory B subunit that interacts with the complex via PR65-α/β HEAT domains (Huntington/elongation/A subunit/TOR). CIP2A interacts with PP2A holoenzyme and modulates its activity toward specific substrates. The gene names for the identified autophagy-regulating candidates and the corresponding proteins (bold) are indicated. | [
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(H) ArfGAP1 WT or ArfGAP1 KO HEK293A cells were starved of amino acids (-AA) for 2 hours, and stimulated with 4mM glutamine (+Gln) or asparagine (+Asn) for 2 hours. Lysates were analyzed for mTORC1 activity as in (B), and phosphorylation of S6 at Serine 235/236 (pS6) was also analyzed. ArfGAP1 and actin were probed for as controls. | [
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(A) Crystal structure of the human AR LBD core dimer based on PDB 5JJM (1 monomer in grey and 1 monomer in pink). W752, located at the interface of the AR LBD dimer, is involved in hydrogen bond formation with T756 of the neighboring LBD and thereby stabilizes the interface. R752 disrupt this stabilization by steric hindrance and charge repulsion. The side chains of both W and R are shown at position 752. A close-up of the LBD-LBD interface is given. The ligand (DHT) is depicted as spheres. | [
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H, I WT and lincRNA-EPS-/- iBMMs were infected with VSV (MOI 0.1) for 6 h or 10 h (H) or transfected with polyI:C (1 μg/mL) for 4 h or 8 h (I), phosphorylation and total protein expression were analyzed by Western blot with α-tubulin and β-Actin as loading controls. | [
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(A) Nuclear (Nuc.) and cytoplasmic (Cyto.) fractions of U2-OS cells were analyzed at times indicated after IR exposure by SDS-PAGE western blotting. PARP1 and LDHA are fractionation controls and phospho-specific p65 signals are indicated. Representative gels from n = 3 biological replicates are shown. Right panel: quantitation of nuclear p65 and phosphorylated p65 species (n = 3). Fold changes compared to untreated samples (ut) and time points post IR are indicated on Y and X axes, respectively. | [
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(D) A visualization of metabolic pathway enrichment results of the differential metabolic fluxes in the virus+remdesivir group vs the control group, using Fisher's exact tests (Methods). Y-axis represents the odds ratio of enrichment, the horizontal dashed line corresponds to odds ratio of 1. The dot color corresponds to the negative log10 adjusted one-sided P value from Fisher's exact tests, and dot size corresponds to the number of enriched target reactions. The datasets are ordered by P values, all pathways displayed have FDR<0.1. | [
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A-D: Surface Plasmon Resonance analysis of the MSP domain of VAP-A binding onto immobilized unphosphorylated (A), monophosphorylated pS209 (B) and pS213 (C), and bi-phosphorylated pS209+pS213 (D) STARD3 FFAT peptides. Representative sensorgrams resulting from the interaction between the MSP domain of VAP-A injected at different concentrations and the different FFAT peptides are shown in (A), (B left), (C), and (D left). Binding curves display the SPR signal (RU) as a function of time. Some samples were measured twice (concentrations printed in bold). Signal obtained for the negative control peptide immobilized on another flowcell is systematically subtracted, as well as the bulk effect recorded with buffer only. Steady-state analysis of the interaction between pS209 (B right) and pS209+pS213 (D right) STARD3 FFAT peptide, and the MSP domain of VAP-A. Equilibrium responses (Req) extracted from the left panel in association phase were plotted as a function of the dimeric MSP domain of VAP-A concentration, and fitted with a Langmuir binding model. | [
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From top to bottom: fluorescence pictures of the SVZ and absolute number of cells in 4D- (white bars) or 4D+ (black or red bars for all or RFP+ cells, respectively) mice scored positive for various markers as indicated. Insets in (C) are magnified (right) with arrowheads pointing label-retaining NSC (white) or astrocytes (empty). | [
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(C-E) RNA-seq analyses were performed in 786-0 cells stably expressing shNT or shGDH1 treated with or without aa starvation for 12 h. Gene ontology cellular components (C) and KEGG enrichment (D) analysis of differentially expressed genes was performed using shNT- and shGDH1-expressing 786-0 cells. The enrichment of differentially expressed ribosomal protein-coding genes was measured by GSEA (E). | [
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A. Validation of Rnaseh2b-/- MEF lines. RER activity (DRD:DNA) is undetectable in a Rnaseh2b-/- line consistent with complete inactivation of the Rnaseh2b gene (Reijns et al, 2012). Mean of three independent experiments; error bars, SEM, **** = p<0.0001, two-tailed t-test. Rnaseh2b-/- and Rnaseh2b+/+ control MEFs on a C57BL/6 p53-/- background. | [
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Representative 1 mm brain coronal slices stained with TTC after 24 h of insult corresponding to animals injected with MTMyc or MTFL457. | [
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(G) The fraction of counts that align to the CHIKV genome is shown for CHIKV-high cells. Only cell types that include >20 cells are shown. | [
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Schematic representation of the β protein (Hedén et al, 1991). The first residue of each domain is indicated. XPZ is a proline-rich repeat region (Areschoug et al, 2002a). Known human ligand binding partners are indicated above each respective domain. IgA binds to a region denoted IgABR. Factor H binds the β75K region, but does not bind via XPZ. | [
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A. Heatmap of 65 DAM-associated gene transcripts analyzed by NanoString in FCRLS- and CD11b-positive Grn-/- (n=6), Trem2-/- (n=5) and Double-/- (n=6) microglia in comparison to WT (n=7) microglia isolated from 6-month-old male mice. The expression corrected and housekeeping gene normalized RNA counts for each gene and sample were normalized to the mean value of WT followed by a log2 transformation. | [
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Model illustrating GemC1 as an early regulator of multiciliogenesis through the control of transcription factors McIdas and FoxJ1.Abbreviations: MCC: multiciliated cells. | [
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B tGnd1‐GFP is stabilized in ubr1Δ san1Δ cells. S. cerevisiae wt and ubr1Δ san1Δ mutant cells expressing tGnd1‐GFP were grown at 30°C. Cycloheximide was added, and protein levels were determined at the indicated time points by Western blot using GFP‐specific antibodies. Zwf1 levels are given as a loading control. | [
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Top: Schematic of the co-culture system used to assess vesicle transfer in transfected cells. Donor cell were transfected with the indicated GFP-fusion proteins and then labeled with DiD. Acceptor cells were transfected with a H2B-mCherry plasmid. After 24 h, the cells were detached, replated in 1:1 ratio and cultured for 4 h. Cells were then fixed and stained with HCS CellMask™ Blue. Bottom: Representative confocal images of co-cultured donor and acceptor CAD cells. Yellow arrows point to DiD-labeled vesicles inside acceptor cells. | [
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D. Western blot of PTEN variants in WT (lane 1) and N-terminal extended PTEN isoforms-/- (lane 2) Hela cells with a PTEN monoclonal antibody | [
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C (left) Immunoblotting of SLC7A5 in MeWo cells transfected with non-targeting (NT) or SLC7A5-specific siRNAs for 48 hr. (right) GC-MS-based quantification of intracellular essential amino acid levels in MeWo cells mock or si-SLC7A5-transfected for 24 hr and then treated with LDHAi for 48 hr. Data information: Statistical analysis was performed by ordinary one-way Anova for the comparison of more than two groups. Data are shown as the mean ± SD, n = 3. ns: not significant, *p ≤ 0.05, **p ≤ 0.01, ***p ≤ 0.001, ****p ≤ 0.0001 | [
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C) The ratio of spliced to unspliced p120-MS2bs RNA was determined by RT-qPCR from cells expressing the indicated MS2 fusion proteins. Average values and standard deviations of seven biological replicates are shown. | [
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E Responsiveness to pilocarpine (PC) of WT (n=6) and Fxr2 KO mice (n=6). (two-tailed Student's t-test). Data are presented as mean ± SEM. | [
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C: Comparative structural analysis of representative 2D class averages of Dam1WTc (upper row) and Dam1WTc-Bim1 (lower row). Densities exclusive to Dam1WTc (arrow) indicate the topology of Bim1 (scale bar; 10 nm). | [
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D Visualization of interaction between PBL27 and MAPKKK5K375M, 6xA by BiFC analysis in Arabidopsis protoplasts. Venus fluorescence indicates interaction between PBL27 and MAPKKK5K375M, 6xA. Scale bar=10µm. | [
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cell type annotations visualized by UMAP. B) The sample specific UMAP visualization of two samples. | [
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B. Binding kinetics of UVR8 pre-monomerized by UV-B versus the COP1 WD40 domain obtained by grating-coupled interferometry (GCI). Sensorgrams of UVR8 injected are shown in red, with their respective 1:1 binding model fits in black. The following amounts were typically used: ligand - COP1 (2000 pg/mm2); analyte - UVR8 +UV-B (highest concentration 2 μM). ka = association rate constant, kd = dissociation rate constant, Kd = dissociation constant. | [
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Left panel: MT-HCT116 cell extracts were fractionated as cytosolic and nuclear portions and subjected to IB analyses, respectively. Right panel: The cytosolic and nuclear fractions were immunoprecipitated with anti-β-catenin antibody and subjected to IB analyses | [
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(a) Immunofluorescence images showing anti-RPA-1-positive foci in response to 5-FU after depleting the indicated genes by RNAi or empty vector control RNAi (L4440; scale bars, 5 μm). | [
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B, C Typical examples (left) and current-voltage relationships (right) of (B) IKur and (C) IK,ACh in VM and AMCMs.Data information: Data are presented as mean ± SEM. In (A), *P < 0.05 by unpaired t-test. In (B, C), *P < 0.05 by two-way repeated measures ANOVA followed by pairwise comparison using the Student-Newman-Keuls test for (B) and Mann-Whitney rank-sum test for (C). In (B), P = 0.778, 0.350, 0.03, 0.02, 0.002, 0.001, < 0.001 and < 0.001, respectively, for comparison between VM and AM within membrane potentials of −20, −10, 0, 10, 20, 30, 40 and 50 mV. In (C), P = 0.01, 0.01, 0.01, 0.01, 0.03, 0.397, 0.397, 0.397, 0.671, 0.207, 0.207, 0.09, 0.01, 0.039 and 0.015, respectively, for comparison between VM and AM within membrane potentials of −120, −110, −100, −90, −80, −70, −60, −50, −40, −30, −20, −10, 0, 10 and 20 mV. CMs = cardiomyocytes; hESC-atrial (AM) and hESC-ventricular (VM) CMs; IK,ACh = acetylcholine-activated potassium current; IKur = potassium ultra-rapid delayed rectifier current. 4-AP = 4-aminopyridine; CCh = carbachol. | [
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