EMBO/sd-character-level-ner huggingface dataset:
d, Co-localization of NDP52 with galectin-positive bacteria in HeLa cells stably expressing YFP fused to the indicated galectins, infected with S. Typhimurium and stained with NDP52 antiserum 1 h after infection. Mean and s.d. of duplicate HeLa cultures, n > 100 bacteria per coverslip, representative of two independent experiments. Scale bar, 10 µm.
K Flow cytometry analysis of ATZ-HA polymer levels in MEFs mock treated, exposed to BafA1, and co-expressing FAM134LIR. MFI: mean fluorescence intensity (Mean ± SEM, n=5, unpaired two-tailed t-test, ns P>0.05, ** P<0.01, *** P <0.001).
A Overlapping between SARS-CoV-2 virus-host interaction with virus RNA-host protein interaction results.
D). Sequence alignment of PTP-MEG2 from different species and with other PTP members. Important structural motifs participating in phosphatase catalysis or the recognition of the NSF-pY83 site are shown, and key residues contributing to the substrate specificity are highlighted.
Caco-2 cells incubated with P57-68 or PGAV or with P31-43 in the presence or absence of VX-770 Immunoblotting with specific antibodies in Caco-2 cells challenged for 2 or 4 h in the presence or absence of VX-770. NLRP3 expression (C) Densitometric analysis of protein levels relative to loading control. Mean ± SD of triplicates of independent experiments. **p<0.01 and °°p<0.001 vs 2h or 4h of culture with P31-43 in the presence of VX-770 (ANOVA, Bonferroni post hoc test). Data information: The blots are representative of one experiment for group of treatment.
C. SDS-PAGE gel of a Ni2+-NTA pull-down of full-length IFT25/27/74/81 complex with His-tagged IFT22 (WT and S19N mutant). The nucleotide-binding deficient mutant IFT22S19N interacts with IFT25/27/74/81 in the pull-down experiment.
(K) FRAP recovery curves in insoluble lipid domain or soluble plasma membrane fraction in SKOV3-Empty "E" and SKOV3-OPCML "O" cells treated with Gas6 Data in (A) to (O) are representative of at least three experiments with graphs depicting means ± SEM s; *P < 0.05, **P < 0.01, ***P < 0.001, and ****P < 0.0001 by Student"s t tests
(B) Venn diagram depicting the number of genes upregulated (up, LFC > 1 and P ≤ 0.05) and downregulation (dn, LFC < -1 and P ≤ 0.05) by DEX in normoxia and hypoxia after 6h.
Average number of unique peptides identified for R2-P1 performed on 5 different days (n=5).   Average number of unique phosphopeptides identified for R2-P2 performed on 5 different days (n=5).   Boxplot depicting CVs of peptide MS1 signal intensities for reproducibility analysis of R2-P1 within the same batch (n=5) and between different batches conducted on different days (n=5). For each peptide, one replicate per batch was randomly chosen for inter-batch comparisons.   Boxplot depicting CVs of phosphopeptide MS1 signal intensities for reproducibility analysis of R2-P2 within the same batch (n=5) and between different batches conducted on different days (n=5). For each peptide, one replicate per batch was randomly chosen for inter-batch comparisons.
Fat and lean mass (E) of body composition from male mice after 11 weeks of AKG supplementation (n = 9 per group).
F. Representative flow plot of parenchymal Db-NP tetramer+ CD8+ T cells (CD69+CD8+ T cells protected from i.v. CD45 labeling) derived from host or donor.
(j) Real-time RT-PCR analyses reveal a significant increase in the expression of the atrial natriuretic peptide gene (Nppa), a clinical biomarker for heart hypertrophy, in Hace1−/− sTAC heart; expression levels were normalized to Hprt and Gapdh mRNAs. n=6-9 per group. In all panels, error bars represent s.e.m., one-way analysis of variance were used to calculate P-values.
(B-G) Graphs represent the relative abundance of the indicated proteins in each fraction of the gradient, as measured by densitometry analysis of western blot signals (ImageJ). Note the reduced degree of co-migration of C99MUT with MAM markers (Acsl4), compared to C99WT.
Quantification of the integrated GFP signal intensity for GFP-tagged Rad54 (N = 75), Rdh54NRad54 (N = 46), Rdh54 (N = 50) and Rad54NRdh54 (N = 35; 1, 3, 10 and 30 nM each) bound to Rad51-ssDNA molecules. The data was fit by non-linear regression and error bars represent s.d. for individual DNA molecules.
B) Kaplan-Meier survival analysis of cortical neurons followed for 13 days post-transfection.
(A) Short interfering RNAs (siRNA) knockdown of p19ink4d messenger RNA and protein in SCC25 cells. SiRNAs were directed against p19ink4d, scrambled p19ink4d (Scr.) or cyclophilin (cyc.) controls.
(C) Occurrence of GFP-ATG8 puncta in promastigotes when incubated in the conditions detailed in (B). Means ± SD from four independent experiments. * and **, occurrence of GFP-ATG8 puncta in Δatg5 were significantly different from in WT in nutrient-deprived and nutrient-rich conditions (p<0.05).
(K, L) quantifications of the number of boutons normalized to muscle surface area (x1000) in the indicated genotypes. ****, p<0.0001; ***, p<0.001; **, p<0.01; ns, not significant by unpaired t-test with Welch's correction. n=23 (w; da-GAL4, btz/Df), n=6 (btz/+), n=10 (Df/+, UAS-BtzGFP/+; btz/Df), n=8 (btz/Df), n=22 (da>btz-GFP; btz/Df), n=13 (BG380-GAL4; btz/Df; BG380+24B>Btz-GFP; btz/Df; da-GAL4/+), n=5 (BG380>Btz-GFP; btz/Df), n=11 (24B-GAL4; btz/Df; da>btz RNAi), n=12 (24B>Btz-GFP; btz/Df; btz RNAi/+), n=9 (BG380+24B-GAL4; btz/Df), n=15 (BG380-GAL4/+), n=14 (BG380>btz RNAi; repo>btz RNAi), n=16 (mhc-GAL4/+), n=28 (mhc>btz RNAi), or n=21 (repo-GAL4/+). Error bars show mean ± SEM. NMJ size is reduced in btz mutants and rescued by expressing UAS-btz with da-GAL4 or with the combination of the BG380-GAL4 and 24B-GAL4 drivers, but not with any single driver. Expressing UAS-btz RNAi with da-GAL4 or in motor neurons with BG380-GAL4, muscles with mhc-GAL4 or glia with repo-GAL4 also reduces NMJ size.
Quantification of pADAM17-positive cells/HPF in lungs of the indicated groups (n = 5 per group).
C Heatmap showing pseudotime-dependent gene expression. Bars on the top were colored as in (A). Representative genes were highlighted on both sides.
A-C. Analysis of autophagy flux in stable inducible HeLa cell lines expressing mCherry-fusion proteins of indicated ATG8 sensor upon doxycycline (DOX) induction: Autophagy flux is monitored after autophagy induction by Torin I (C) indirectly via lipidation of LC3B and turnover of the autophagy receptor p62.
(d) Western blot analysis of ORF1p in autophagosome-enriched fractions. LC3-II is a marker of autophagosomes.
F. Comparison of TCR oligomer size using BN-PAGE and anti-CD3ζ immunoblotting in day 10, IL-2-expanded WT and CCR5-/- OT-II lymphoblasts lysed in buffer containing digitonin or Brij-96. The marker protein is ferritin (f1, 440 and f2, 880 kDa forms). The ratio of TCR nanoclusters to monomeric TCR in each lysis condition was quantified by densitometry (right; n = 5).
(d) ITT was performed by insulin injection at 16 weeks of age as described in the Methods. *P0.05, **P0.01, ***P0.001; Student's t-test.
HME control cells were treated with IFNβ for 2 days to induce OAS expression, fixed and stained with anti-OAS1, 2, or 3. Scale bar, 10μm.
A) Heatmap showing the normalized enrichment score (NES) measured by GSEA analysis of the listed pathways for FAPs, MuSCs and Macrophages (MAC) RNAseq in the comparison of OC vs YC (on the left) and for FAPs and MuSCs in the comparison of WO vs WY (on the right). GSEA results were filtered for significance by FDR q-value≤0.25.
C IFA of episomally expressed DHHC2::6HA and three truncation mutants in zygotes and retorts. Scale bar = 5 μm.
8-week-old female C57Bl/6 mice were infected intranasally with 150 pfu of influenza A/Scotland/20/74 (H3N2) virus (IAV) and treated or not simultaneously with 4 mg of succinate (Suc; by the intranasal route). Some mice were euthanized at 4 days post-infection and lungs as well as BAL fluids were collected to determine: (d) the levels of 111 additional mediators using a specific protein-array;
Colitis was induced by oral administration of 3 % DSS for 5 d. Mice were treated daily (s.c.) with either PRN1126 (40 mg/kg), or ONX 0914 (10 mg/kg), or vehicle. Data points represent mean ± SEM of 15 mice pooled from three independent experiments.
(b) Double-labeling immunohistochemistry of huntingtin (EM48; green) and mTOR (red) in brain tissue of mice expressing mutant huntingtin.
Survival of B mice and TNFR1−/− mice injected with LPS, 24 h after miR-511 or miR-CTR hydrodynamic plasmid injection. B mice pretreated with miR-511 (grey, n = 16) were significantly protected against 200 μg LPS compared to miR-CTR-pretreated mice (■, n = 15) or PBS-pretreated mice (●, n = 15) (left panel). No difference in survival was found between TNFR1−/− mice pretreated with miR-511 (grey, n = 11) or with miR-CTR (■, n = 9) against 500 μg LPS (right panel).
A Immunoblotting of serum placensin from patients at second trimester (1-3), term pregnancy (4-6) using specific placensin antibodies.
H. Quantification of SapI regeneration in Mock or SCAI-depleted extracts. Note that plasmids containing a SapI site but no ICL account for ~5-7% of each pICLpt preparation. Primary data are shown in Figure EV2F,G. A representative of two independent experiments is shown.
(C) In MGC80-3 and HGC-27 cells, expression changes of different markers (β-catenin, ZO-1, SNAIL and VIMENTIN) of epithelial-to-mesenchymal transition were examined after overexpression or knockout of lncPSCA.
Mean ± SEM SM levels, expressed as percentage of vehicle values, in cerebellar, hippocampal, cortical and liver extracts from WT and ASM-KO mice 48 hours after one single administration of vehicle or the indicated doses of PF. (*PKOVeh Vs KO 5 = 0.0304, n = 3 mice per group, one - way ANOVA, Bonferroni post hoc)
C Western blot analysis of detergent‐extracted brain lysates using anti‐total Tau, Tau1, AT8 or MC1 antibodies. WT: wild‐type; WT + TFEB: wide‐type mice injected with TFEB; Tau: rTg4510 transgenic mice; Tau + TFEB: rTg4510 transgenic mice injected with TFEB. Two exposures were displayed for total : the short exposure was used for quantification of Tau transgenic samples; the long exposure was used for side‐by‐side comparisons of the total levels in WT and Taumice and for quantification of WT total Tau. γ‐tubulin was used as a loading control.
F) Representative pictures of extracellular vesicles (EVs) heterogeneity purified from conditioned media of HEK293T cells transfected with control (ev) or TMED2 plasmid and analyzed by cryo-electron microscopy. Right upper panel: western blot analysis of CD63 in total medium (left) and in the purified extracellular vesicles fraction purified from media conditioned by control and TMED2 overexpressing cells (middle) and western blot analysis of AGR2 levels (right) in extracellular vesicles enriched from culture media conditioned by control and TMED2 overexpressing cells.
(A) ICP-MS quantification of mitochondrial iron in mouse quadriceps (n=6-8). (B) Gastrocnemius heme content quantified by fluorescent heme assay (n=4-6). Data information: For all data, n represents the number of biological replicates. Statistical significance was calculated by unpaired, two-tailed Student's T-test. Data are mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001.
(A) Representative VE-cadherin staining and graph quantification of fluorescence intensity normalized to total number of cells per field (DAPI labelling) in sh-Control and sh-PI3KC2β hCMEC/D3 in resting condition and after 24 hours activation with 25 ng/ml of TNFα. Control normalized to 100%. Scale bar, 15 µm. Data represent mean ± SEM of cell fields randomly selected (dots n=14-19). Data are collected from 4-5 independent experiments; ***p<0.001, unpaired t-test.
C. Overexpression of LRP6 blocked the increase of YAP phosphorylation under serum starvation conditions. HEK293T cells were transfected with empty vector (-) or LRP6-EGFP as indicated in the figure. One day after transfection, cells were incubated in serum-free medium for 4 h. Cells were lysed and the cell lysates were analyzed by immunoblotting (left panel). The ratio of LRP6/β-actin and p-YAP/YAP of three independent immunoblots was quantified (middle and right panel, respectively). Error bars indicate standard deviation of biological triplicate measurements. *P < 0.05 and ***P < 0.001. Student's t-test was used for statistical analysis.
Gene expression level of indicated pro-inflammatory cytokines of lung infected by PAO1 with WT-mDASCs or LL-37-mDASCs transplantation. n=3. Error bars, S.E.M. *, P<0.05; **, P<0.01; ***, P<0.001; ****, P<0.0001.
A Schematic diagram of constructs used to express patient-derived pure and interrupted SCA8 repeat tracts with predicted protein products and C-terminal epitope tags. * Due to TAG encoded stop codons polyGln proteins do not express an epitope tag. CGG interruptions and the encoded amino acid interruptions are indicated in red.
A Representation of the domain structure from different C‐terminal fragments of GC‐G analyzed for coolness‐induced activity (amino acids of GC‐G encoded in each expression plasmid are indicated).
(E) MDA-MB-231 breast cancer cells were transfected with vector, wild type PPM1G or catalytically inactive PPM1G D496A (D/A) mutant. Levels of phosphorylated α-catenin were detected by using phospho-specific antibodies.
(D) Average expression of Bmal1 (black), Rev-erbα (grey) and Per2 (red) in HIO, kcHIE, and bHIE. (E) Amplitude of Bmal1 (black), Rev-erbα (grey) and Per2 (red). AU stands for arbitrary units.
A Expression of PTPN11 (gene encoding SHP2) in skin lesions in psoriatic patients compared with skin from healthy donors based on microarray data (No. GSE14905). B Expression of ptpn11 in human PBMCs of psoriatic patients (n=14) and normal controls (n=16). Data information: Data are represented mean ± SEM. P values are determined by two-tailed Mann-Whitney U test *P<0.05, **P<0.01.
Lysates from HEK-293T cells expressing Flag-ITSN-s and GFP or GFP-DENND2B were incubated with protein A beads or protein A beads coupled to anti-GFP. Bound proteins were detected by Western blot.
p62 immunohistochemistry (IHC) staining in humanbrain tissue.A, B Normal vascular endothelium of autoptic brain parenchyma samples is lacking the typical autophagic p62 granules as shown by the negative staining for p62. Scale bars: (A) 200 μm; (B) 100 μm.
A,B) Relative gene expression analysis of IGF1R, Fas, and the death receptors TRAILR-1 and TRAILR-2 after bortezomib treatment with the respective IC50 concentrations for 48 h. Untreated control cells served as reference value (ratio = 1).
Mitochondrial respiratory capacity (oxygen consumption rate, OCR) from oxidative soleus (SOL) (J) and glycolytic extensor digitorum longus (EDL) muscle fibers (K), and NetOXPHOS control ratio of 95wks old mice (L) (n=5per genotype).
GSEA analysis comparing a query gene set of modulated genes from (A) with GO biological process signatures associated with epidermis development and keratinocyte differentiation. NES=normalised enrichment score, FDR=false discovery rate. Kolmogorov-Smirnov statistic was used.
H) Total number of hepatocytes per well (+/- s.d.) for NF54, NF135 and NF175 on day 5 p.i., under different parasite to hepatocyte ratios (starting from 8 sporozoites to 1 hepatocyte to 1 sporozoites to 8 hepatocytes). Two biological replicates were performed with two technical replicates in each.
Average daily food intake of conditionally modified mice (n=4-10 animals/genotype, mean±SEM).
(E) Representative images showing stages of meiotic prophase I from culture day 9 (c9) germ cells from XGFP+ and XGFP- PGCLCs. c9 germ cells were spread and immunostained for SYCP3 (red), and γH2AX (grey). Scale bars = 10 µm. (F) Quantification of meiotic progression in culture day (c9) expanded germ cells derived from XGFP+ and XGFP- PGCLCs. The graphs show the percentages of the meiotic stage for SYCP3+ cells. Lepto, leptotene; Zygo, zygotene; Pachy, pachytene; Diplo, diplotene. Numbers indicate detected cells per meiotic stage and original XGFP status.
HT-29 cells were transfected with siRNA for MLKL or scramble non-specific (NS) siRNA for 72 hours. Cells pre-treated with 10 μM QVD-OPh (Q), 5 μM Birinapant (S), 20 μM necrostatin-1 (Nec-1s) were stimulated with 1-10 ng.mL-1 TNFα (T). Cell viability was assessed by CellTiter-Glo (A) after 16 hours. Data are means ± SEM of three independent experiments. *P< 0.1, ****P<0.0001 (ANOVA).
(L) Analysis of the total cell counts upon loss of TH and Ddc in the PSC at 48h AEL (Antp-Gal4; UAS-GFP/+, n=19, Antp-Gal4; UAS-GFP; THRNAi, n=13, Antp-Gal4; UAS-GFP; DdcRNAi, n=17), at 72h AEL (Antp-Gal4; UAS-GFP/+, n=17, Antp-Gal4; UAS-GFP; THRNAi, n=18, Antp-Gal4; UAS-GFP; DdcRNAi, n=22) and 96h AEL (Antp-Gal4; UAS-GFP/+, n=15, Antp-Gal4; UAS-GFP; THRNAi, n=14, Antp-Gal4; UAS-GFP; DdcRNAi, n=15) Data information: The quantification in L represents the median with whiskers indicating maximum and minimum values, box indicates the lower and upper quartiles. The statistical analysis applied in L is Two-way Anova with Tukey's multiple comparisons test. 'n' represents the number of lymph gland lobes analyzed, *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001.
H) Quantification of the proportion of mCherry-positive cells in the VZ plus SVZ that are GFP-positive 48 h after control (Con, white) or gGFP (black) Cas9 protein electroporation. Data are the mean of 4 independent experiments (5 embryos per condition in total, from 4 litters).
A) Differential expression analysis of transposable elements in rpb-9 (mj261) mutants versus wild type (polyA-selected RNA-seq libraries). [p<=0.01, log2(fold change)>=1, DESeq2 analysis]
Representative immunofluorescence images of stomach unit bases at homeostasis, 6 hour, and 24h HDT stained with GIF (red, granules) and LAMP1 (green, lysosomes) Scale bar, 25μm. Stomach unit base outlined by dashed white line.
B-G Cells containing the expression constructs shown in (A) were mated with COI12KO cells in the presence of cadmium ions. The localization of Twi1p was analyzed by immunofluorescence microscopy staining using an anti‐Twi1p antibody at 3 hpm (B-D). In (B-D), the parental MACs are marked with arrowheads. DNA elimination was analyzed by DNAFISH with probes against Tlr1 IESs at 36 hpm (E).
E-H. HEK293Cx43+ or HEK293Cx43- were transiently transfected with hnRNPA2B1-GFP, GFP-hnRNPQ or GFP alone, for 24 h. miR-133b levels were assessed in EVCx43+ and EVCx43- (E; n=4 biological replicates) and EV-producing cells (F; n=3 biological replicates). miR-509-3p levels were assessed in EVCx43+ and EVCx43- (G; n=4 biological replicates) and EV-producing cells (H; n=3 biological replicates). Data information: p-values were derived by Mann-Whitney test. Bars and error bars indicate mean ± SD in all graphs.
(A) Identification of Ams1 and Ape4 as Nbr1 interactors. Nbr1-associated proteins were identified by affinity purification coupled with mass spectrometry (AP-MS) analysis using YFP-FLAG-His6-tagged Nbr1 as bait.
(F) The enrichment of genes related to "accessibility-increased regions at the late phase (Brown dot in Fig 3E)" (left) or "accessibility-decreased regions (Green dot in Fig 3E)" (right) within genes up-regulated in CD150+CD34- HSCs or CD150+CD34+ progenitor cells.
(C, D) Schematic diagram of the luciferase reporter separated by TET1 intron 8 and 9 or GAPDH intron 3 and 4. DSCR1 reduction increases the activity of this luciferase construct, while DSCR1 overexpression decreases its activity. In contrast, altering DSCR1 levels did not affect luciferase activity of the construct containing GAPDH introns. Values are shown as mean ± SEM, and tested for statistical significance by one-way ANOVA followed by Bonferroni post hoc test. N = 3 for each condition, *P< 0.05, **P< 0.01. ***P< 0.001.
B, The protein levels of pAkt (Ser473), total Akt, pERK (Thr202 and Tyr204) and total ERK were observed by western blot in spleen, lung and pancreas tissue lysates after treatment with oral doses of vehicle (0.5% methyl cellulose with 0.2% Tween-80) or of BYL-719 (50mg/kg).
Kaplan-Meier survival curve of tumour bearing mice injected with GBM cells infected with lenti-Ctrl or lenti-CYP46A1 (n = 5 per group). A log-rank test was used to assess statistical significance.
Representative images showing the intraplatelet expression of LC3 and active caspase-3 in CD41 stained platelets from the KO mice using fluorescent labelled antibodies against the respective proteins of interest. Magnification: 100X. Rightmost panel represents zoom in on an individual platelet showing the colocalization and expression of LC3 and active caspase-3.
Both thermopriming/heat acclimation and SA187-induced thermotolerance are mediated by HSFA2 dependent H3K4 trimethylation of chromatin at HS memory gene loci. However, thermopriming is conveyed to HSFA2 via the family of HSFA1A, B, D and E transcription factors whereas SA187 regulates HSFA2 by ethylene signaling via the transcription factor EIN3.
BMDMs were stimulated with TNF (100 ng/ml) in combination with TAK1i (125 nM) for the indicated time points. LDH release
RNA-Seq analysis of PBMCs of macaques infected with SIVmac239 before and after suppression of viremia with ART Expression levels were normalized as Log2 fold change or as enrichment score in ART-treated vs ART-naïve animals (B). (B) data were analyzed by Gene Set Enrichment Analysis (GSEA, number of animals =8). Symbols in the GSEA enrichment plots represent the position of the gene set members in the transcriptome ranked by differential expression between ART-naïve and ART-treated time points. Red color indicates leading edge genes. All analyses were conducted on the genes of the pathway GO cellular response to oxidative stress (184 genes; GO:0034599).
(G) Purkinje cell with numerous single-membrane bound, cytoplasmic vacuoles tethering to each other (arrows, inset). Electronmicrograph, scale bar 2 μm. Inset: scale bar 1 μm.
E Western blot analysis of KDM6A, nephrin, WT-1 and H3K27me3 expressed in kidney glomeruli of normal, diabetic and GSK-J4-treated diabetic mice at 12 weeks after diabetic induction. *P < 0.05 versus normal controls, #P < 0.05 versus untreated diabetic mice (Parametric ANOVA and a Bonferroni post hoc test; n = 3).
C) Representative zygotene-like Stag3 mutant and Smc1β−/− univalents. Nuclear spreads were immunostained for SYCP3, SYCE1 and RAD21. Bars, 1 μm.
(F) Nuclear extracts from MPH pre-treated for 30min with 10µM MG132 or 10µM PP2 followed by addition of 1µM thapsigargin (ERS) for 1h were subjected to Western blot or Simple Western immunoassay with antibodies against HNF4A, NR1H4, FOXA2 or XBP1S. LMNA was used as loading control. Results obtained from 2 independent biological replicates are shown. (G) Densitometric quantification of the protein expression data shown in panel (F) Repression by ERS in MG132 condition (average of 4 biological replicates) is shown relative to repression by ERS in vehicle condition. The bar graph shows means ± SD (standard deviations). One-sample t-test with BH correction for multiple testing was used to determine if the mean relative repression is statistically different from 100%, *P < 0.05.
(F) In situ PLA images using anti-IP3R and anti-VDAC1 antibodies. Scale bar: 20 μm. Data represent fluorescent in MEFs normalized LRRK2+/+ MEFs. Error bars represent ±SD from six independent experiments. Data information: For graph the P values was determined by a Mann-Whitney U test. ns = not significant, *P < 0.05, **P < 0.01
Quantification of FOS expression detected by fluorescent Western blots at different timepoints prior to illumination. Datasets were corrected for background fluorescence and scaled to FOS level at 3 hours. Bars show mean ± SEM (n=3). Quantification of the magnitude of phosphorylated FOS (p-FOSS32) as a fraction of total FOS, detected by fluorescent Western blots at different timepoints prior to illumination. Datasets were scaled relative to phosphorylated FOS level at 3 hours. Bars show mean ± SEM (n=3).
NO production from the co-culture supernatant was quantified by Griess reaction.