EMBO/sd-character-level-ner huggingface dataset:
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.
H) Representative images of 14DIV PTX3 KO neurons (Ctr, +N terminal PTX3, +C terminal PTX3) stained for surface AMPARs (GluA, green), Bassoon (blue) and tubulin (red). Arrowheads point to postsynaptic GluA clusters. Scale bar: 5µm. I) Quantification of the surface synaptic AMPARs normalized to the total number of Bsn shows an increase in PTX3 KO treated with N terminal fragment of PTX3 but not with the C terminal fragment (PTX3 KO=1.000±0.042, PTX3 KO+C-term=1.103±0.070, PTX3 KO+N-term=1.428±0.061. Number of fields examined: 63, 38, 57 respectively; Kruskall-Wallis test, p<0.0001 followed by Dunn"s test; 3 independent experiments, data are presented as normalized mean values
j, Fold change of glycolytic intermediates in +/−KRas cells (n = 4). Ala, alanine; BPG, bisphsphoglycerate; DHAP, dihydroxyacetone phosphate; F6P, fructose-6-phosphate; F(1,6) BP, fructose-1,6-bisphosphate; G6P, glucose-6-phosphate; G1P, glucose-1-phosphate; Ga3P, glyceraldehyde- 3-phosphate; G3P, glycerol-3-phosphate; Lac, lactate; PEP, phosphoenolpyruvate; 3PG, 3-phosphoglycerate; Pyr, pyruvate.
U2OS cells were depleted of endogenous ATM by repeated transfections with shRNA and induced, by doxycycline incubation, to express ATMWT, ATM2RA, or ATMCL mutant. Where indicated, cells were further transfected with a GSNOR-coding vector and then treated for 2 h with 10 μM CCCP. F) fluorescence microscopy analyses upon incubation with chloroquine (CLQ) to enhance differences in mitophagy. Percentage of mitochondria merging with LC3-positive puncta calculated by Fiji analysis software using the open-source plugin ComDet v. 0.3.7. Values are expressed as % of mitochondria (TOM20+ particles) co-localizing with LC3/cell and graphed as boxes (25th-75th interquartile range) and whiskers (minimum to maximum showing all points), with central bands representing the median of n ≥ 9 different cells. **p<0.01; ***p<0.001; n.s., not significant.
Topology diagrams of PTPIP51_TPR and other TPRs: TTC0263_TPR (PDB ID 2PL2), PILF_TPR (PDB ID 2FI7), and CUT9_TPR (PDB ID 2XPI). TPR pairs are presented in different color, which are identical to those in the topology diagrams.
Vegfc/LacZβ-Gal staining reaction with smooth muscle actin (SMA) peroxidase staining.Data information: Arrows indicate the VEGF-C expression in arterialSMC, arrowheads indicate the VEGF-C expression in SMCfibers in the villus, and asterisks highlight the VEGF-C expression in circular smooth muscle cell layer of the intestinal wall. Scale bars: 50 μm, except (C) inset 25 μm.
Overexpression of IRE1α K481R induced apoptosis. MEFs were transfected with indicated vectors. After 24 hours, these cells were stained with Annexin V-FITC
e, Caspase 3 activity in murine macrophages following glucose starvation, n = 3 mice. RLU, relative light units.
(D) Scheme of oxaloacetate biosynthesis. MDH-2 stimulates oxaloacetate biosynthesis, which can be used to support tricarboxylic acid cycle (TCA) and/or cytosolic phosphoenolpyruvate generation by PCK-1. In physiological settings, phosphoenolpyruvate can be used to generate pyruvate, which can be reduced to lactate or oxidized to acetyl-CoA (dashed lines).
Quantification of the kinetics of EC migration. Values of forward and reverse migration for RhojWT/WT are normalized to 1. n = 33 vessel branches per group.
(C) Quantification of anterograde, retrograde, mean velocity, linear flow rate and number of BDNF-mCherry-containing vesicles from the data in (A) (siMecp2+Vehicle: n=801 vesicles/95 axons; siMecp2+FK506: n=1020 vesicles/116 axons; siCtl+Vehicle: n=780 vesicles/83 axons; siCtl+FK506: n=1029 vesicles/102 axons). Data are presented as the mean ± SEM of at least three independent experiments (one-way ANOVA with Tukey's comparison). *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001, ns = not significant.
C Immunofluorescence (IF) staining of PC3-LN4 EDC3 knock out cells following 6 h treatment with DMSO (Control), PIMi (PIM447, 3µM), AKTi (GSK690693, 5μM), and both inhibitors (AKTi + PIMi) and stained with anti-EDC3, and anti-DCP1a antibodies (Abs) as well as DAPI. Data information: IF Images were subsequently merged using FIJI image analysis software. The yellow box shows a zoom of the merged image. Images were captured under 40x magnification; scale bar: 10µm. P-body number was counted by FIJI.
(D) Distribution of differentially methylated tiles over promoter, gene bodies, or intergenic sequences.
C Fold changes in nucleotide, central carbon metabolite and amino acid levels after IMT1 treatment in RKO and IMT1-resistant RKO cells. Metabolites levels are expressed as fold of DMSO-treated RKO cells (mean IMT1-treated/control, n=3 experiments). Dark blue, minimum (0), dark red, maximum (2). G6P, glucose-6-phosphate; F6P, fructose-6-phosphate; FBP, fructose-1,6-bisphosphate; 3PG, 3-phosphoglycerate; PEP, phosphoenolpyruvate.
(F) HOMA values from 6‐h‐fasted 6‐mo‐old (n=7-9) and (G) 12‐mo‐old Con and KO mice (n=6) on RD. (H) Glucose tolerance tests in 6‐h‐fasted 6‐mo‐old mice on RD (n=4) and in (I) 6‐h‐fasted 12‐mo‐old Con and KO mice fed HFD for 10 mo (n=4).
In vitro CDK1/cyclin B1 kinase assay for immunoprecipitation-purified BCL9-Flag or T172A-Flag proteins.
(E) De novo motif discovery using MEME with STAT5 binding sites as input. The most significantly enriched motifs in unstimulated and TPO-treated HPC7 cells are shown.
E. Localization of P. berghei concavin-GFP in liver stages. Nuclei (blue) stained with Hoechst. Scale bar: 5 µm.
C. Schematic depiction of the stopped-flow experiment. 2-AP was substituted at position +18 of the nontarget strand. The 2-AP fluorescence signals as a function of time are shown for four sgRNAs. The solid lines are double-exponential fits of the data
IL6 levels in spleen homogenates (C) of C57BL/6J (B6J) or STING-/- mice following i.v. infection with 4 x 105 PFU parental MCMV or MCMV m152stop were analyzed 6 hpi by ELISA.
Working model of the Uba4-catalyzed reaction cycle of Urm1 thiocarboxylation. After adenylation by the Uba4 AD (ochre), Urm1 (red) forms a thioester intermediate with the catalytic cysteine (C202) located within the crossover loop. The RHD (blue) connected to the AD by a flexible linker reaches Urm1 and replaces the thioester linkage by an acyl-disulfide bond by a nucleophilic attack of the persulfide on the active cysteine (C397). Thiocarboxylated Urm1 is released and serves as sulfur donor for tRNA thiolation.
(A) Metabolomic analysis of CRISPR-generated cystinotic cells (CTNS-/-) treated with cysteamine (100 µM), bicalutamide (35 µM), and a combination of cysteamine and bicalutamide (100 µM and 35 µM, respectively) (n
(E) Import of Mrp17-DHFRmut into purified ∆tom22 mitochondria, control import into WT mitochondria is shown on Appendix Figure S6B
The initiation form of Pol2 with an unphosphorylated carboxy terminal domain (Pol2 null-P CTD) is highly enriched in HMR_-L1s.
(D) Graph reporting the volume of blood loss (µL) in treated mice (n=4-9 per group) observed during 30 minutes post TVT. Dosing was 10 mg/kg for KB-AT-23 and 1 mg/kg for FVIIa. The grey area represents the range of blood loss in FVIII-treated mice (33-245 μL), which is similar to that of wild-type C57BL/6 mice (49-308 μL; Johansen et al. 2016).
(C, D) Loss of Mcp3 has no effect on the phospholipid composition of mitochondria. Highly-pure mitochondria were isolated from the indicated yeast cells. Lipids were extracted and then analysed by mass spectrometry analysis. The level of each phospholipid species in wild-type mitochondria was set to 100% and the ERG/PL ratio to 1. Relative changes in mitochondria from mcp3 cells are presented. The mean with standard deviations of three biological repeats with two technical repeats for each (n=6; SD) is given.
d, Immunoblot for IFT20 and ATG16L in the same fractions isolated from Ctrl, IFT20− and IFT88− MEFs in the presence (top) and absence (bottom) of serum.
Ni-NTA His-ubiquitin pulldown K48 or K63 in control and HA-USP28 overexpressing HEK293 cells, followed by immunoblot against exogenous ΔNp63. The input corresponds to 10% of the total protein amount used for the pulldown. Relative ubiquitination of the representative immunoblot was calculated using VINCULIN for normalization.
K,L Quantification of K, F4/80 and L, CD206 positive cells in KC and oncogenic PI3Kα mice.
(B) HeLa cell lysates treated with control or p97/VCP siRNA were immunoblotted with anti-p97/VCP and anti-tubulin antibodies.
(B) The extracellular β-1,4-endoglucanase activity from bacterial cultures supernatants (OD600 = 1) was determined by a colorimetric assay in solution (n = 2 replicates). Wild-type, XccbphP, pXccBphP and pC13 strains were assayed under normal laboratory conditions. Data derive from 3 independent experiments. (A-B) Values are expressed as mean ± s.e.m. Statistical analysis was performed by a Kruskal-Wallis test and Dunn´s multiple comparison test (*P < 0.05, **P < 0.01, ***P < 0.001).
S-Z Morphological analysis demonstrated the effective ability of the PF and Mabs-PlGF combination to generate a complete and functional artificial TA replacing the ablated TA injury. H&amp;amp;E staining of TA injury in mice by cross section at an early (10 days) (S-V) and late (6 months) (W-Z) time point after ablation (in S, U, W, Y displayed items are obtained from a multi-photo collage). At the early time point, the acellular PF-treated mice revealed few mature muscle fibres that survive the massive ablation (box in S) signs of continued muscle degeneration (arrows in T), whereas PF-embedded Mabs implanted mice showed remarkable muscle regeneration indicated by centre-nucleated myofibres (arrows in V). At later stages, the control mice grafted with acellular PF showed an almost devoid TA (W) with very few muscle fibres (X), in contrast to PF-embedded Mabs, which exhibited a complete muscle replacement generating an artificial TA (Y), enlarged view (Z) proved the complete and mature organization of the newly formed muscle showing capillary and blood vessel around myofibres (arrows). Scale bar: (S, U, W, Y) 500 μm, (T, V, X, Z) 50 μm.
B. Basal respiration, maximal respiration, and spare respiration capacity were calculated from A. n=5 biological repeats; error bars indicate SEM; p values were calculated using student t-test.
Manders' coefficients of colocalization between NPY-pHluorin and ChgB per neuron.
R. The indicated 7SK were in vitro transcribed in the presence of 32p-UTP and subjected to in vitro modification reactions. The nuclease P1-digested products were analyzed by 1D-TLC with pU and pΨ as controls.
C. Lysate of MCF7 and MCF7aTT cells (rendered thermoresistant through the protocol described in Fig. 1A) were separated by sucrose density gradient centrifugation, and P/M ratios were determined by integration of monosomal and polysomal peak areas (bar graph, mean P/M ratios +/- SD, n = 6). Numbers above bars indicate p values calculated with the two-stage linear step-up procedure of Benjamini, Krieger and Yekutieli.
(A) CRISPR/Cas9 gene editing was used to generate peroxisome-null cell lines by knocking out PEX19. In wild-type HCT116 cells, catalase localized to peroxisomes (dot-like structures), whereas in PEX19 -/- cells catalase was diffusely localized throughout the cytosol, indicating loss of peroxisomes. Scale bars, 10 µm.
G) Graph indicating the inter-axis distances measured at terminally and centrally located sites of LSAEs in zygotene-like Stag3 mutant univalents. Each measurement corresponds to 1 distance measured at terminally (n=20) and centrally (n=20) located sites of local separation of axial elements. Horizontal lines indicate median.
(A) Atg8WT-HA, Atg8F77A-HA, Atg8F79A-HA or Atg8F77/79A-HA was transformed into Δatg8 cells. Cell extracts were prepared and subjected to 13.5% SDS-polyacrylamide gel electrophoresis (SDS-PAGE) containing 6 M urea, followed by immunoblot analysis with anti-Atg8 antibodies.
A simple model of growth and lag phases. (i.) Species initially grow exponentially with Aci2 initially consumes only alanine and Pa consuming alanine and glutamate in a fixed 2:3 ratio. (ii.) When a resource is depleted, both species experience a diauxic lag. Aci2's lag time is long and varies with resource supply. Pa's lag is short and constant at 1 hour. Growth rates recover with a quadratic time-dependence. (iii.) Once recovered from its diauxic lag, each species grows on the remaining resource at its initial growth rate.
(A) Sphere formation in MGC-803 cells incubated with fresh medium or conditioned medium from MGC-803 cells for 7 days. The number of spheres was quantified and indicated on the right. Scale bar = 100 µm (n = 3 biological replicates; mean ± standard error of mean (SEM); *P = 0.0146; two-tailed unpaired Student's t-test).
(C) BAG1 knockdown was performed in 293 cells for 48 h. Thereafter, cells were transfected with GFP or GFP‐based UPS reporter genes as indicated. After additional 24 h, levels of GFP‐positive proteins were detected by western‐blot analysis using a GFP antibody.
(C) IFNβ-Luc, pRL-TK, cGAS-GFP (stimulated) or IRES-GFP (unstimulated) and either LacZ or m152 together with the indicated murine STING mutants described in (B) were transiently expressed in 293T cells. Luciferase activity was measured as described in (A). Data information: Data in (C) is normalized to LacZ, combined from three independent experiments and shown as mean ± SD.
(f) Overexpression of the RALB-G23V-K47R mutant leads to accumulation of LC3-lipid conjugates. HEK293T cells overexpressing the RALB-G23V or RALB-G23V-K47R mutants were assayed for the relative accumulation of LC3-I and LC3-II by immunoblotting using anti-LC3 antibody.
serum FITC-Dextran level of colonic section from the WT and Ang-/- mice on day 9 with (n = 9) or without (n = 6) 2.5% DSS treatment. FITC-Dextran: fluorescein isothiocyanate-labeled dextran.
A. Western blot of PGRN in whole-cell lysates of WT and GRN-/- hiMGL. Actin was used as loading control. B. Western blot of TREM2 in whole-cell lysates of WT and GRN-/- hiMGL. Mature (mTREM) and immature TREM2 (imTREM2) are indicated. Actin was used as loading control.
Culture of small intestinal crypts of WT and VilCreER Apcfl/fl (or AhCreER Apcfl/fl) mice with/without R-spo1 shows the dependence of the Wnt agonist in WT organoids but not in Apc-deficient spheres. Representative photos were taken at day 5 in culture. Black scale bar, 50 μm.
(C) Gene expression analysis of Ub-associated Nrf2 targets mapped to mouse orthologues. Probes detecting transcripts exhibiting differential expression (Benjamini-Hochberg-adjusted P < 0.05) in at least one of the four comparisons are shown. Heat map represents Log2 (fold changes) with respect to either wild type (WT) or Atg7 KO (as indicated). Labels show the symbol, RefSeq (accession numbers from the NCBI Nucleotide database), gene probe name, and the gene row and gene column (i.e., array coordinates).
I. Clonogenic survival of U2OS and U2OS/FANCA KO cells subjected to indicated doses of MMC for 24 h (mean±SEM; n=3 independent experiments). J. Clonogenic survival of U2OS, U2OS/SCAI KO, U2OS/FANCA KO, and U2OS/FANCA+SCAI DKO cells subjected to indicated doses of MMC for 24 h (mean±SEM; n=3 independent experiments).
(g) Quantification of 4-HNE-positive cells of the immunohistochemical stainings described in (f). Data are shown as mean ± standard deviation (SD). Statistical significance was calculated using one-way ANOVA. Each data point represents the average of 3 technical replicates of one histological section, the numbers of tumor samples are given in (e).
E) Levels of phosphorylated proteins were quantified by densitometry, normalized to the amount of total protein present in each sample, and expressed relative to the basal level in uninfected cells. Values are means ± SEM, N = 3, *p<0.05. Dashed line drawn at 1 indicates basal levels of activation.
E: Frequencies of chromosome loss were quantified at permissive temperature (25°C).
H. Working model: Pre-miR-181a-1 is transported along RGC axons tethered to CD63-positive late endosomes / lysosomes. Under non-stimulated conditions TUBB3 undergoes basal translation in the axonal compartment. Upon Sema3A exposure, pre-miR-181a-1 is locally processed and the expression level of the concomitant newly generated miRNAs increase locally within the growth cone. miR-181a-5p, the predominant mature miRNA generated from pre-miR-181a-1 targets TUBB3, thereby silencing protein synthesis through LPS inhibition (LPS-I). Abbreviations: ns, not significant; LE/Ly, late endosomes / lysosomes; LPS, local protein synthesis; LPS-I, LPS inhibition; TUBB3, tubulin beta 3 class III.
D, Images from FRAP experiments carried out on protrusion connected and isolated Nrl::GFP cultures pre- and post-photobleaching. Area of photobleaching (white dashed circles). Analysed regions (yellow, orange and red dashed circles). Photoreceptor FRAP results shown from multiple experiments (isolated cells, n=14; connected to recipient, n=21; connected donor, n= 21). All data presented as percentage, mean ± SEM and fitted to the curve in a non-linear regression with two phase association.
The gastric cancer risk-associated rs2978980 T>G genetic variant disrupts RORA binding to the intronic enhancer region of lncPSCA and down-regulates lncPSCA expression in cells. LncPSCA is a tumor suppressive lncRNA that acts by controlling DDX5 degradation through ubiquitination, resulting in released RNA Pol II from the DDX5-Pol II complex and activated transcription and expression of the P53 signaling genes that are important for gastric cancer progression.
B Diagram showing electrophysiological analysis of transmission across the spinal lesion site.
B and C, Deletion of PUF3 upregulates mitochondrial transcripts in WT cells (B), whereas downregulates mitochondrial transcripts in ρ0 cells (C). WT and mutant yeast cells were cultured to log phase. RNAseq was performed with three biological replicates per genotype (Dataset EV4). All the transcripts and the Puf3-associated transcripts encoding mitochondrial proteins are shown. The significantly changed transcripts (P value < 0.05; fold change > 1.5 or < 0.67) are highlighted with dashed lines; numbers of significantly changed transcripts are indicated.
Diploid and tetraploid cells were grown on YPD or PRE-SPO medium at 30°C or 37°C, respectively, for 24 h and stained with CellROX Green. Cell images indicate calcofluor white staining (cell wall; blue), GFP, and a merged image of GFP/DAPI/DIC channels. Scale bar = 10 μm. Diploid and tetraploid cells were grown on YPD or PRE-SPO medium at 30°C or 37°C, respectively, for 24 h, stained with CellROX Green, and signal analyzed via flow cytometry.
(B) Quantitative real-time PCR of FLS2 transcripts from 12-day-old seedlings treated with mock or 1 μM GLV2 for the indicated time, n=3 biological replicates. UBQ was used as a house keeping gene. Students T-test revealed no statistical difference for each of the different timepoints. Data information: Similar results were obtained in 3 independent experiments.
Immunoprecipitation and subsequent western blotting shows that Armi-Flag (Armi-F) but not Flag-Armi (F-Armi) strongly bound with Gasz in Zuc/Armi-depleted OSCs (Zuc KD + Armi KD). Piwi bound with both Armi (F-Armi and Armi-F). Luciferase-Flag (Luc-F) was used as a negative control.
D) Basolateral in vivo imaging of abdominal histoblasts expressing Tsp96F-RFP in the Hh receiving cells shows colocalization with Ptc-GFP at mobile punctae (yellow arrows).
d. Representative example of the protein expression of AKT1, AKT2, AKT3, PTEN and FOXO3 on sorted CD4+CD25highCD127- Tregs stimulated in the presence of IL-2 (grey line) or IL-2+IL-12 (black line) and day 2 for AKT1, AKT2, AKT3 and PTEN and day 3 for FOXO3. Grey histogram represents the isotype. e. Statistical analysis of AKT1, AKT2, AKT3, FOXO3 and PTEN gMFI of n=6 experiments performed. * p<0.05, ** p<0.005, *** p<0.0005.
Endogenous levels of free cholesterol revealed by filipin staining of (B) WT cells under the indicated treatments. Graphs show the filipin fluorescence intensity as a percentage over VEH.
A Lysates of HeLa cells stably expressing GFP alone or GFP-FXR1 were subjected to immunoprecipitation using GFP-Trap beads (GFP-IP), analysed by Western blot and quantified (shown a mean value, *P < 0.05, **P < 0.01; N = 3).
(I) The sketch shows the position of the ARE binding sites in the ADAR2 promoter region.
The activity of the CNFY derivatives was tested by analyzing the deamidation of RhoA in HEp-2 cell lysates by the mobility shift of the modified GTPase detected by immunoblotting.
(F) ZIKV NS1 and FANCC immunostaining 48 h after ZIKV infection of hNSCs. Scale bar = 100 µm.
(I) Top2B levels in mitotic cells are increased in DIA treated B1dd/B2ko cells. The left panel shows immunofluorescence images, for quantification we segmented mitotic DAPI staining, measured the mean intensity of Top2B staining and plotted the ratio between mitotic and interphase nuclei.
(b) Combinatorial analysis of genes differentially expressed between Sorafenib-sensitive and resistant cells and genes with depleted barcodes in the synthetic lethal screen in Huh7-IR and CR cells. 38 common genes were identified, among which was WWTR1 coding for TAZ.
D) PCR products using the primers in C(1) over the ABCB1 and EEF1A1 regions in RPE-1 Parental and the different Taxol resistant clones. E) PCR products using the primers in C(2) over the specific break site in the ABCB1 promoter in RPE-1 Parental and the different Taxol resistant clones.
(A) Frequency of mitotic phenotypes observed in indicated cell lines with or without DIA treatment (3 repeats, n>50 per repeat, error-bars indicate s. d.). DIA was added for four hours in asynchronous cells followed by 12 hours of imaging.
Relative expression of Pank1α, Pank1β, total Pank1 and Pank3 in mouse brain regions. n=8,8,4 for both genotypes (GP, SN, Cerebellum, respectively).
F. Levels of CtBP2 and of synaptic proteins in retina homogenates from littermate RBEWT/WT and RBEKO/KO mice. Levels were determined by quantitative immunoblotting using fluorescently labeled secondary antibodies; results are normalized to loading controls depending on molecular weights (actin, fodrin, VCP, and GDI) and to wild-type controls. Statistical analyses were performed using Student's t-test; data are presented as mean ± SEM (*, p<0.05; n=4 mice per genotype).
(B) The correlation between the percentage of soft primary tumor cells from breast (n = 11) or colon (n = 23) cancer patients and the grade of breast or colon cancer, respectively. Data information: Pearson's correlation test (B The data represent mean ± SD.
Pearson correlation between S1P (A-C) PSI days from admission and NLR in COV (n=111). Scatter plots and fitted regression line are shown in each figure. Exact p values or ****p < 0.0001 are reported.
A) VEGF-A levels only slightly increased from D16 to D30 in the IgG control. At D16 levels of IgG control are significantly higher compared to anti-VEGF-A (++++, P < 0.0001); RG7716, 30 μg (++++, P < 0.0001) and RG7716, 90 μg (++++, P < 0.0001). Anti-ANG-2 levels are comparable to IgG control and therefore significantly different from anti-VEGF-A (++++, P < 0.0001); RG7716, 30 μg (++++, P < 0.0001) and RG7716, 90 μg (++++, P < 0.0001). At D30 the levels of VEGF-A are significantly reduced in the RG7716, 90 μg group are compared to IgG control (*, P = 0.0309). Anti-ANG-2 remains at levels comparable to IgG control and is therefore significantly higher than RG7716, 30 μg (*, P = 0.0107), RG7716, 90 μg (**, P = 0.002) and anti-VEGF-A (*, P = 0.0162).
Groups of five mice were intranasally infected with IAV (1918), and recombinant DDX3 protein was administered intranasally. Survival was monitored daily for 2 weeks.