EMBO/sd-character-level-ner huggingface dataset:
Baseline associations between CSF T-tau, Ng and NFL and other AD traits. Data are estimates (-coefficients) from linear mixed effects models, with 95 % confidence intervals. The estimates are the main effects of the biomarkers, capturing the effects at study baseline. Effects were significant (*) for MMSE: T-tau (p=.034) and NFL (p<.0001) in A-negative. 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).
Under normal conditions, a fraction of agonist‐activated FXR is modified by SUMO2 at K277 by the E3 SUMO ligase PIASy and regulates an anti‐inflammatory transcriptional pathway in response to inflammatory signaling. SUMO2‐FXR increases its interaction with NF‐κB and SMRT and blocks its interaction with RXRα, which results in selective trans‐repression of inflammatory genes without entering transcriptional pathway regulating FXR/RXRα target genes (left). In contrast, in diet‐induced obese mice, FXR is highly and constitutively acetylated at K217, which inhibits SUMO2 modification at K277, at least in part, by blocking its interaction with PIASy and results in diminished SUMO2‐dependent anti‐inflammatory action (right).
B) Location of TUBB1 mutations in the cDNA and of the corresponding changes in the protein. Exons are represented by boxes numbered from 1 to 4. The dark grey box represents the protein domain responsible for encoding guanosine triphosphate (GTP) and the light grey box the domain for microtubule-associated protein (MAP) binding. The arrows show the consequences of the three TUBB1 mutations in our patients, all of which are in the GTP domain. Mutations of this study are in bold, published mutations associated with congenital macrothrombocytopenia are in italic
(A,B) NIH3T3 cells transfected with DsRed (A) or DsRed-CA7 (B) were incubated in growth medium with 5 µM Latrunculin B for 0, 2, 5, 10, or 30 minutes, or in an equal amount of DMSO for 60 minutes. Analyses of experiments show that in cells transfected with DsRed-CA7 F-actin structures collapse more slowly (0 min: 83% "normal"; 2 min: 80%, p = 0.44; 5 min: 74%, p = 0.39; 10 min: 27%, p = 0.08; 30 min: 16%, p = 0.02; DMSO: 82%, p = 0.99; tested against 0 min with two-way ANOVA, Dunnett's multiple comparison test) than in the DsRed-transfected ones (0 min: 89% "normal"; 2 min: 48%, p = 0.14; 5 min: 31%, p = 0.04; 10 min: 2%, p = 0.001; 30 min: 0.7%, p = 0.001; DMSO: 88%, p = 0.8; tested against 0 min with two-way ANOVA, Dunnett's multiple comparison test) . For the analysis, cells were categorized to three groups as "normal", "some shape/F-actin left" and "round". The upper panel shows example images of the cells in all three categories for (A) DsRed- or (B) DsRed-CA7 transfected cells (actin visualized with Phalloidin-488).
Quantification of normalized MA Piezo2 currents in HEK293 cells transiently transfected with Piezo2+ GABAB1+ GABAB2 + GFP (A, n=12), treated with the MAPK inhibitor U0126 10 µM (C, n=7). Cells were treated with U0126 for 30 min before the experiments, and were present throughout the measurements.
(F) Epistatic analysis of the effects of TAB2 and TAB3 depletion on autophagy. HeLa cells stably expressing GFP-LC3 were transfected with siRNAs specific for TAB2 or TAB3 and/or with cDNAs coding for full‐length HA‐tagged TAB2 (HA-TAB2) or TAB3 (HA-TAB3). Twenty‐four hours later, the frequency of cells exhibiting >5 GFP-LC3+cytosolic puncta (GFP-LC3VAC cells) was determined. Results are mean values±s.d. (n=3; *P0.01 versus siUNR‐transfected cells).
B Violin plots of Z scores from the three metrics for ER size determined for each of the 4800 mutant strains. The untreated WT is shown for reference.
C) Inferred stress differences (brown) and mean recoil velocities (blue) as measured by PIV and in the LECs (cyan - n = 18)), 10 µm (red - n = 16) and 40 µm within the nest (green - n = 20). Error bars represent Standard Deviations.
Screen data plot of the cholesterol content of LBPA-endosomes. Automated unbiased quantification of the filipin integrated fluorescence signal (cholesterol content) in LBPA-containing endosomes, after treatment with each compound of the Prestwick library. As in Fig 1D, each dot is the average of replicates in the duplicate plates, and ≥600 cells were analysed per compound - only compounds that showed less than 20% toxicity are plotted. The fluorescence signal of LBPA-endosomes was used to segment the imaged and generate a mask, which was then applied on the micrographs to quantify the integrated intensity of filipin staining. The samples treated with thioperamide (pink), trimeprazine (light blue), DMSO (red) and U18666A (green) are indicated.
LTβR‐Fc‐treated wild‐type or IL17R−/− mice; percentage of mice with at least one ANA. E denotes gestational day. ANA were determined with LIA at the age of 3 months
A, B, C. Double knockdown of EXOSC10 and DIS3 significantly increased poly-GA and repeat RNA expression compared with single knockdown of EXOSC10 in cells expressing (G4C2) 80 repeats.
(F) 2-deoxyglucose (2-DG) treatment inhibits TGFβ1-induced glycolysis (left) and fibrosis (right) in COUP-TFII-OE cells by qRT-PCR (n=6). **p<0.01; ****p<0.0001 by one-way ANOVA, mean ± SD.
E) Larval brains at 0 h ALH from Jupiter-GFP (G147) were labeled with GFP, Msps, and Dpn. F) Larval brains at 24 h ALH from Jupiter-GFP were raised on normal food (fed) and food depleted of amino acids (nutritional restriction/NR) and labelled with GFP and Dpn.
G Quantification of TDP-43-NLS mutants in SGs versus band around SGs of two independent replicates ± SD. ***p < 0.0002 by Kruskal-Wallis test with Dunn´s multiple comparison test to Wt (≥ 56 cells; ≥ 315 SGs per condition).
(D) Correlation between changes in chromatin accessibility on day 2 of neuronal differentiation in the indicated perturbations and H3K4me3 or Fam60a ChIP coverage from mouse ES cells (H3K4me3 is from ENCODE project and Fam60a from (Streubel et al., 2017)). Coefficient and P-value computed using Spearman's correlation. n=49,722 peaks.
A, cGAMP-HA-VLPs and Empty-HA-VLPs + AddaVax protect against IAV challenge. One month after immunisation, animals were infected with 104 TCID50 of IAV PR8 virus. Weight loss was monitored over the following eleven days and is shown as a percentage of starting weight (A, upper graph shows mean and lower graphs show individual mice for each condition).
Microarray analysis following introduction of let‐7 and miR‐125 in Dgcr8Δ/Δ GPCs. Upregulated transcripts are shown in red, downregulated transcripts in blue (adjusted P‐value 0.05). Data shown is for average of 3 replicates.
Detection of endogenous Rabl2 in purified multicilia. Multicilia purified from cultured mEPCs were analyzed by immunoblotting (E). Ac-tub, Ift25, and Ift81 served as positive controls for cilia, whereas Lamin B1, GM130, Cep162, and Gapdh served as quality controls for the ciliary preparation to exclude major contaminations from the nucleus, Golgi, basal body, and cytosolic proteins, respectively. 1/400 of the mEPC lysate and 1/20 of the cilia lysate were loaded per lane.
plaNET-seq signal of RNAPII in the promoter proximal region of AT1G70600 in NRPB2WT +/+ nrpb2-2 -/- (NRPB2WT, blue) and NRPB2Y732F +/+ nrpb2-2 -/- (NRPB2Y732F ,red). Arrows indicate the RNAPII signal at the region of promoter-proximal stalling.
Pair-wise crosslinking between BrEtY-βarr1-3xHA and wt PTH1R. (D) Ribbon representation of active PTH1R as seen from the intracellular side (PDB 6NBF) (Zhao et al, 2019). Cys residues are shown in red. ECL3 (not resolved in the structure) is represent as a yellow dashed line. The approximate position of the Cys residue in this loop is marked with a fuzzy red circle.
b, (left) P8 Nrl.Cre+/- photoreceptors transplanted into subretinal space of TdTomatofloxed reporter mice (N = 5 eyes), compared to (middle) subretinal injection of AAV-Nrl.Cre subretinal injection (10^12 vp/ml), (N = 10 eyes) and (right) contralateral uninjected control (N = 10 eyes). Arrows indicate recombined host photoreceptors (white arrows) or RPE (green arrows). Note clearly recombined RPE cells upon AAV transduction.
(E) Flp-In T-REx 293 cells induced to express MIA40FLAG were transfected with a plasmid that encoded COA7HIS or an empty vector. The affinity purification of MIA40FLAG was performed, and eluate fractions were analyzed by SDS-PAGE and Western blot.
1x106 primary DLBCL cells obtained by passaging through a MISTRG6 mouse were intravenously injected into MISTRG or MISTRG6 recipients. the lymphoma burden at the study endpoint eight weeks p.i., as quantified in the spleen and bone marrow in D Representative flow cytometry plots are shown in D for bone marrow and spleen (MISTRG, MISTRG6).
Chromogenic WM-ISH showing neuroD4 expression intensity in: uninjected (UI) 51/56 embryos (91%), CTRL 50/54 embryos (93%) and mutant (MBSm); 36/65 embryos (55 %); longitudinal view, scale bar 100μm.
Heat map plots of the mRNA level changes of chaperones, ubiquitin-proteasome pathway, and autophagy genes (gene list in Table EV1F) in the indicated strains (data from Dataset EV1 and Dataset EV10). Selected genes for growth analysis in B are highlighted in red.
(c) Confocal microscopy analysis of the colocalization of endogenous UVRAG and Vps16 or Vps18 in HeLa cells. Insets highlight colocalization.
(D) Quantification of the fraction of cells with PIDD1 localized to the mature mother centriole in PLK4Dox cells expressing an sgRNA targeting the indicated genes. A dot displays measurements from each experiment. Experiments were performed in PLK4Dox polyclonal knockout cells. Data acquired across n = 3 biological replicates. Mean ± s.e.m.
H, Experimental scheme of the FRET experiment. The attractant serine lowers the phosphorylation level of CheY. As a result, CheY dissociates from the switch and the energy transfer from YPet (conjugated to FliM) to mCherry (conjugated to CheY) is reduced.
C) Evaluation of HP1β mutants for ensuring protein stability of Jmjd1a/b. Protein levels of Jmjd1a/b in HP1-cTKO lines expressing 3xFlag-hHP1β mutants were compared before and after 4OHT treatment. The intensities were quantified with ImageJ software and are summarized on the right. Data represented as mean ± SD (n > 3, biological replicates). *p < 0.05, **p < 0.01 (Welch's test).
(J) The levels of YAP target gene expression was analyzed using RT-qPCR in control (WT) and TRIP6-KO HEK293A cells. (Mean ± SD; n=3; ***P≤0.001, T-test)
DC(p38-KO) and DC(p38+NLRC3-KO) mice were immunized with MOG(35-55) peptide in CFA adjuvant and pertussis toxin to induce EAE. Mean clinical scores of EAE in immunized DC(WT) (n= 5) and DC(NLRC3-KO) mice (n= 5).
WT (CD45.1) and DKO (CD45.2) AMs were sorted, mixed in a 1:1 ratio, labeled with CellTrace Violet and cultured in the presence of GM-CSF. The ratio of CD45.1 and CD45.2 cells and CellTrace Violet dilution was analyzed prior to culture (day 0) and after 7 days of culture as described in Materials and Methods.
(A-C) KNL1 localization analysis in control, SNAP29 KD and SNAP29 KD expressing full length human SNAP29, CFP tagged, full length Drosophila Snap29 (CFP-Snap29), or the mutant forms schematized above the panels. Max projections of single cells in prophase are shown. (D) Quantification of 3 independent experiments evaluating the localization of KNL1 relative to CREST. 200 KTs from 10 control cells and 200 KTs from 10 SNAP29 KD cells per sample were identified by CREST staining. P values are obtained by 2-way ANOVA with Dunnett's multiple comparison analysis relative to localization of KNL1 in SNAP29KD cells.
Vero cells infected with BTV-8 were fixed at 16hpi, and stained with anti-BTV-VP7 antibody.
C) Representative images of haploid S. cerevisiae with mad1Δ, Okp1_fl mad1Δ, or Okp1_cmΔ mad1Δ; native: S. cerevisiae S288C type (identifier DDY904 in Table EV6). Dilution is as we describe for A. We show two unique clones for Okp1_fl mad1Δ.
(A-D) Exemplar STCs in response to SGN illumination with a single μLED (A), a block of four neighboring μLEDs (B) and all μLEDs of an oCI inserted via the round window in a CatCh-transduced gerbil (C) and with all µLEDs in a wildtype gerbil (WT; D). μLEDs were spaced by 250 μm.
(C) Immunofluorescence analysis of staining for TSC2 and LAMP2 in HCT116 cells The degree of colocalization of TSC2 and LAMP2 is graphed as the mean ± SEM. ***p<0.001.
Tumor immunostaining for apoptosis using an anti- caspase-3 antibody. Scale bar, 100 μm.
(f) eIF4A mutant larvae have impaired TORC1 inactivation upon shifting to food lacking amino acids. Control (w1118) or eIF4A1006/1013 1st instar larvae were transferred from standard food to plates containing either standard fly food or PBS/1% agarose+2%sucrose for 1h prior to lysis and immunoblot analysis. Two biological replicates are shown. Representative of 3 biological replicates.
(C) Mitochondrial morphology in mock treated cells or HeLa cells depleted of Sept2 and then transfected with empty vector, siRNA-resistant HA-tagged Sept2 (Sept2-rescue) or Sept7 (Sept7-rescue). Mitochondria were labeled with mitotracker (shown in green), asterisks mark transfected cells. Scale bar: 10 µm, insets are twofold enlargements. (D) Quantification of mean mitochondrial length in mock treated cells, in cells depleted of Sept2 or in cells depleted of Sept2 and transfected with siRNA-resistant Sept2 (Sept2-rescue) or Sept7 (Sept7-rescue). n>200 individual mitochondria from two independent experiments.
(C) FRET efficiency was measured with HEK cells transfected with STIM1-CFP, ANO8-YFP, and with (red) and without (black) Orai1-HA before and after store depletion. Here and all other FRET measurements, representative images of the FRET signal under each condition are shown next to the traces. Data information: The first number in parenthesis indicates the number of similar experiments performed and the second number is the number of cells analyzed. All results are given as mean±s.e.m of the indicated number of experiments or cells analyzed.
Confocal microscopy images of proximity ligation assay (PLA) in HeLa cells showing interaction of GW182 with Ago1, but not with Ago1x. Rabbit anti-GW182 and Mouse anti-FLAG antibodies were used to achieve proximity ligation. Interaction is indicated by red dots that results from proximity ligation. Quantification of dots per cell is shown (right). Each black circle represents a microscopic field. Mean ± S.E. are shown as horizontal lines (n=10 fields for vector control; n=12 fields for Ago1; n=11 fields for Ago1x). At least 100 cells were counted for dots in each category. ***, P < 0.0001 (Mann-Whitney test).
C ChIP‐seq tracks with Scl binding in Flk1+MES, HPC7, FL erythroblasts and MEL (mouse erythroleukemia cells) around cardiac (Gata4, Myocd, Nkx2.5) and hematopoietic (Gata1, Gata2 and Lyl1) genes show that binding to cardiac genes occurs only in mesoderm, while binding to hematopoietic genes is maintained throughout hematopoietic development.
(F) Representative stereoscopic images of IκBα KO organoids treated with dexamethasone as IFN inhibitor and DAPT as Notch inhibitor. Data information Scale bars in F, 50 μm.
(E) Target engagement dose response demonstrated saturated bound sTREM2 at 50 and 10mg/kg with >50% bound sTREM2 at 1mg/kg of antibody. 4D9-bound sTREM2 was undetectable at 0.1mg/kg and lower. 4D9 was IV-dosed at 50, 10, 1, 0.1, 0.01, 0.001, 0.0001 mg/kg, and isotype dosed at 50mg/kg. CSF bound: total sTREM2 in wildtype mice was measured at 24hrs. Data represent the mean ± SEM (n=5).
Spearman correlation between the expression level of a gene and its first, middle and last PAS usage for genes with exactly 3 PASs in 3' UTR and major PAS in 3' UTR(M). P values are from binomial tests, **P < 0.01; ***P < 0.001. The boxplot shows the Q1 to Q3 quartile values (the box limits), the median (the horizontal green line) and values within the 1.5 * IQR (the whiskers).
Co-IP from 293T cells 48 h after transfection. RhoJ-PlexinD1 binding was disrupted by deleting the RBD or ECD of PlexinD1 and by 30-min stimulation with Sema3E. Arrows indicate PD1 Full (upper, 250 kDa) and PD1△RBD (lower, 1.7 kDa smaller than PD1 Full).
D. The control INS-1cells and JunD KD INS-1 cells were subjected to ChIP assay to detect for the binding of menin, HDAC3, JunD, and histone3 acetylation level at the Pbk locus. 1% input denotes the signal level normalized by the equivalent total input DNA (i.e. 1% of sonicated genome DNA) for ChIP assay. Three independent experimets (n=3). *P = 0.0430 (JunD), *P = 0.0480 (Menin), ***P = 0.0008 (HDAC3), *P = 0.0480 (Ac-H3) (two-tailed unpaired student's t-test). ns, not statistically significant difference.
Cell extracts from RPE cells stably expressing EGFP or EGFP-FAM110A arrested in mitosis by nocodazole were incubated with GFP Trap. Bound proteins were analyzed by mass spectrometry. Shown are top ten proteins that that were significantly enriched in EGFP-FAM110A complex compared to EGFP in three independent experiments. Proteins TUBB8 and TUB1AC were also significantly enriched in complex with EGFP-FAM110A. Number indicates the fold change interaction compared to the control.
Serum-starved HaCaT cells were infected with HSV-1 (MOI=0.5) in the presence or absence of FGF7 (10 ng/ml) or IFN-α (1000 U/ml). Viral load was determined 24 h post infection (hpi) by qPCR for the HSV-1 Glyc-B gene relative to the human β-actin gene (ACTB) (A)
H. Analysis of the CMT plus-end growth with the EB1b-GFP reporter. Z-stack maximum image projections of EB1b-GFP tracked over 30 sec in epidermal cells without (mock, DMSO) and with CK, auxin or CK and auxin treatment (60 min). Scale bars 10 µm.
C. MA and Volcano plots, and Top50 DEGs (FDR<0.05, Log2FC>±0.585, Means>5) for visualization of pairwise differential gene expression analysis of BASCs and Club cells. D. MA and Volcano plots, and Top50 DEGs (FDR<0.05, Log2FC>±0.585, Means>5) for visualization of pairwise differential gene expression analysis of BASCs and AT2 cells.
h) ATG4B deficiency increases nuclear P-ERK levels. Native (top)/inverted images (bottom) showing nuclear P-ERK content. P-ERK fluorescence in untreated (Con)/EGF-treated scr or siATG4B NIH/3T3 cells is shown. Scale bars, 5 μm. Bars represent mean±s.e.m. **P0.01, ***P0.001 compared with scr; Student's t-test, 60 cells from n=2. Nuclei are blue (DAPI).
A, B Infected brain homogenates were PK-digested and analysed by Western blot using (A) Sha31 antibody and (B) after PK and PNGaseF digestion using Sha31.
G Echocardiography measurement of ejection fraction (EF), end-systolic-volume (ESV) and end-diastolic-volume (EDV) before and after ZT13 MI. Two-way ANOVA; n = 6 mice for no MI in both groups, n = 9 for isotype and n = 5 for Ly6G at 72h post MI, n = 8 for isotype and n = 4 for Ly6G at 7d post MI. Isotype vs. Ly6G: *P = 0.0001 (EF, 3d), *P = 0.0227 (EF, 7d); MI *P = 0.0133 (ESV, 3d), *P = 0.0004 (ESV, 7d); *P = 0.0017 (EDV, 7d).
Bar plots with dot density plots showing that PP1c mean intensities within CRs are similar between WT and LUZP1 KO cells [28.68 ± 9.60 arbitrary units (a.u.) (WT) vs. 25.04 ± 9.47 a.u. (LUZP1 KO)]. p = 0.09 (Mann-Whitney U test). n = 3. Bars and error bars represent the mean ± standard deviation (SD).
Wildtype SIRT7 or its RF mutant was re-expressed in Sirt7-knockdown MEF cells (A)
(g) SK-N-SH cells, transfected with EGFP-HDQ74 along with empty vector (pcDNA3.1) or constitutive active m-calpain (1:3 ratio) for 4 h, were subsequently treated with DMSO (control), 1 μM verapamil or 1 μM clonidine for 48 h. The proportions of EGFP-positive cells with aggregates were assessed as in Figure 1c. Error bars show 95% confidence interval. ***P 0.001; **P 0.01; *P 0.05.
D Volcano plot showing proteomic changes of RKO cells treated with 1 μM IMT1 for 96 hours. Data are plotted as average log2-fold change versus log10 of adjusted p-value of DMSO-treated controls; mitochondrial protein are highlighted in red.
The diagram depicts the cascade of inhibition of autophagy and mitochondrial fragmentation triggered by re-stimulation of the T cell receptor during AICD. Early after AICD induction PKA activation induces inhibition of AMPK/ULK1-dependent autophagy as well as a direct block of LC3. Subsequently, mitochondria fragment in a Calcineurin/DRP1-dependent manner. The lack of the removal of mitochondria results in accumulation of dysfunctional and damaged organelles releasing cytochrome c, thus amplifying cell death signals.
i, Effect of forced expression and knockdown of ISX on cell invasion (transwell) activity measured in A549 cells. Data are presented as mean ± SD in bar graph (***, p < 0.001 , Student's t‐test) of 3 independent experiments, each performed in triplicate. Scale bar, 100μm.
a, Images show the localisation of endogeneous SEPT2 and SEPT7 in RPE1 ARLB13B-mRuby2 cells with basal body staining. The insets to the right show enlargements of the cilium. Scale bar: 4µm (large) and 2µm (small). b, STED microscopy images showing ciliated RPE1 cells expressing EGFP-SEPT2 or SEPT7-EGFP and stained for ARL13B. Scale bar: 1µm.
(C) Quantification of the experiment described in (B). Shown is the percentage of phage infected PY79 (WT) and ET29 (Pveg-mCherry, PIPTG-sigX) cells at the indicated time points, scored by the Lysin-SPP1-YFP signal, with average values and SD (n ≥ 200 cells for each time point). Of note, the majority of WT cells were lysed at t=75 min post infection.
Quantification of non-esterified cholesterol content by means of filipin staining in hearts of 25-week old male CD1 Flt1+/lacz (n=20) mice, normalized to wildtype CD1 (Flt1+/+) mice (n=16). Data presented as box-and-whisker plots. Boxes represents lower/upper quartiles with the median values indicated with a horizontal line. Whiskers represent min-max values. Statistical evaluation using t-test, p-value: ** <0.01.
The engraftment of MOLM-13 after FST knockdown was detected by flow cytometry of human CD45 and mouse CD45.1 positive cells in recipient mouse BM aspiration at week 2 post transplantation.
CD8+ T cells were activated for 16h and then co-transduced with miR-AB retroviruses at 1:1 ratio, which carries a SplashRNA-designed shRNAmir, targeting surface protein CD127, CD90, CD44 or CD8, with Azurite, GFP, Ametrine or mCherry2 as fluorescent reporters respectively for 4h. miR-AB retroviruses expressing CD19-specific shRNAmirs with same fluorescent reporters were used as controls. Surface staining was performed 72h after transduction. FACS data were shown as overlaid histograms of control shRNAmirs (shCD19s) and target shRNAmirs (shCD127, shCD90, shCD44 or shCD8). Cells were categorized as sixteen populations expressing single, double, triple or quadruple fluorescent proteins or not (none) and fluorescent reporter-positive plots were highlighted with thick frames and white background. Each population's surface staining profile was shown on the right. The data was representative of two biologically independent experiments.
(A) Heatmap indicating the normalized forward versus inverted reverse experiment enrichments on a log2 scale of quantitative proteomics upon pulldown of Flag-tagged Ythdf in S2R+ cells. The threshold was set to a 1-fold enrichment. Fmr1 is co-purified with Ythdf. Known Fmr1 interacting proteins are highlighted in bold with asterisk.
(D) Levels of miR-483-3p were inversely correlated with serum levels of ET-1 (IPAH, n = 118; HC, n = 95) and IL-6 (IPAH, n = 112; HC, n = 93). Data information: Values are expressed as median ± interquartile range.
(A-B) qPCR gene expression analysis of miRNA target genes Mapk3, Notch1, Dicer, Tab2, Sox2, Calm2, Smad2, Smad5, Dnmt3 and Irak1 in mixed cortical cultures incubated with EVs isolated from CSF from untreated (black) or LPS treated (grey) mice (A) and in brain tissue (B) before (black) and 8 h after LPS injection (grey) (n=3).