EMBO/sd-character-level-ner huggingface dataset:
Flow cytometry analysis of tumours collected on Day 10 following treatment (n = 3 animals per group). ILP-TNF/Mel/SM significantly upregulated Granzyme B in CD3+CD8+CD161- cytoxtoxic T cells
(D) Chitin production is reduced upon Bch1 overexpression. Fluorescence images of chitin stained with calcofluor in Chs3-GFP WT, chs5 and GPD-BCH1 strains.
Western blot analysis of caspase-1 cleavage in the supernatant of Prdx4 WT and KO BMDMs in response to Nigericin (10 µg/ml) stimulation for 1 h after priming with LPS (100 ng/ml), LPS-priming alone or without stimulation. Whole cell lysates were analyzed for pro-caspase-1 and Gapdh levels.
(D) Chromatin recruitment of PPARγ at PPAR binding site contained in Cidecand Pcxpromoters (n=3-5, per group, per ZT, Two-way ANOVA, post hoc Holm-Sidak comparisons *p<0.05). H3K4me3 abundance at Cidecand Pcxpromoters (n=4-7, per group, per ZT, unpaired, two-tailed Student t-test *p<0.05).
D HEK-293T cells expressing Flag-DENND2B were treated with 250 nM OA alone or with 50 µm PKD inhibitor CID755673 and cell lysates were incubated with GST-14-3-3. Total proteins and bound proteins were detected by Ponceau S staining and Western blot, respectively.
B. The rates of of LCVs positively stained for MavQ 2 h post-infection. At least 100 LCVs (n≥100) were scored for each sample.
F Diagrams and co-IP results showing BTG4 binding to PABPN1L. Lysates from HeLa cells expressing HA-BTG4 and FLAG-PABPN1L (full length and C-terminal deleted) were immunoprecipitated with an anti-FLAG antibody. The immunoprecipitated proteins are detected by western blot with the indicated antibodies.
Depletion of Prkrir, Pcbp4 and Tsc22d1 rescues TGF-β-induced reduction in the rate of cell division. (A) Lineage trees tracked by live imaging under control, Non treated control (NTC) and siRNA-mediated depletion of factors (X= cell death/cells could not be tracked till the end).
(B) Quantification of the percentage of ciliated cells Data represent mean ± SD (n=3 experiments), 200 GFP-positive cells were scored per condition per experiment, *P < 0.05, Student's t-test.
]. (C) Quantification of mean (±SEM) mEPSP amplitudes, in which 75 consecutive spontaneous events were averaged per cell, and then cell amplitudes were averaged per genotype. [UAS-RFP n = 15 cells, UAS-dNmnat n = 14 cells, UAS-Wnd n= 10 cells. 1-way ANOVA w/Tukey's multiple comparisons, DF=38, F=11.66, p = 0.0001. UAS-RFP vs UAS-dNmnat p=0.994 (NS), UAS-RFP vs UAS-Wnd p = 0.0003 (***)].
B (Left) Detection of spliced XBP1 (S) and unspliced XBP1 (U) mRNA in shCtrl and shFAM20C HepG2 cells treated with or without 5 μM Tg for 1 h. (Right) Quantification of XBP1 mRNA splicing levels. Data information: data were shown as mean ± SEM of three independent experiments. *p < 0.05, **p < 0.01 (two-tailed Student's t-test).
B Median fluorescence intensity of the distribution plots in A plotted against the indicated time after HPG addition. Linear regression line fitted from 5 minutes onwards.
Kaplan Meier survival curve on the full lawn of P. aeruginosa for N2 (naive) worms and N2 worms pre exposed to 1-undecene odor. Survival assay was performed at 20°C.
C. IP on Hela cells co-expressing VPS41WT-APEX2-V5, VPS41S285P-APEX2-V5 or VPS41R662*-APEX2-V5 and FLAG-RAB7 or GFP-Arl8b. The IP was performed on FLAG or GFP respectively. All VPS41 variants interact with Rab7 and Arl8b (n=3).
Changes in the concentration of plasma metabolites are associated with COVID-19 severity. The discharge group consist of all patients (mild and severe) that were recovered and discharged. L1, low-density lipoprotein subclass-1 (LDL1); VL, very low- density lipoprotein (VLDL); L5, LDL5; L6, LDL6; H2: high-density lipoprotein subclass-2 (HDL2); H3: HDL3; H4: HDL4.
Epidermal cells transfected with control siRNA (siCtrl) or S100A9-targetting siRNA (siS100A9) were challenged for 72h with 200 ng P24 of HIV-1-R5 (left dot-plots) or HIV-1 primary isolate (right dot-plots). Cells were fixed, permeabilised and stained with langerin (Y-axis) and HIV Gag P24 (X-axis) fluorescently coupled antibodies. Samples were acquired on a Flow cytometer. The experiment shown is representative of four donors for HIV-1-R5 (n=4) and five donors for HIV-1 primary isolates (n=5). The same as above was done but on MoLC gated by size (FSC).
D. As for C, but comparing genotypes in wild type or HEI10-OE backgrounds. Values for replicate individuals are plotted, in addition to the mean (red).
Sexing of established ESCs (gDNA-qPCR, Zfy/Gapdh), performed as described in Figure 1B.
Amounts of Aβ40 or Aβ42 in the TBS-soluble or Gu-HCl-extractable fraction from (A) 3-month-old or (B) 12-month-old hAPP/Mgat3+/+, hAPP/Mgat3+/−, or hAPP/Mgat3−/− brains (n = 5). P = 0.015 for TBS Aβ40, P = 0.034 for TBS Aβ42, P = 0.001 and 0.012 for Gn-HCl Aβ40, P = 0.024 for Gn-HCl Aβ42 in (A), P = 0.040 for Gn-HCl Aβ40, P = 0.047 for Gn-HCl Aβ42 in (B).
AP staining of H8-Bptf or H8-Tbx3 exon-KO ES cells after LIF withdrawal. hnRNPLL-H8, hnRNPLL-KO ES cells; H8-Bptf KO, alternative Bptf exon was deleted in hnRNPLL-KO H8 cells; H8-Tbx3 KO, alternative Tbx3 exon was deleted in hnRNPLL-KO H8 cells; H8-Bptf/Tbx3 KO, alternative Bptf or Tbx3 exons were simultaneously deleted in hnRNPLL-KO H8 cells. Scale bar, 200 μm.
(J) Quantitative Real-Time PCR analysis of eEF1A1 and eEF1A2 mRNA abundance in hearts from neonatal mice, adult wild-type mice (Adult) and adult wild-type mice 2 weeks after TAC surgery (Adult TAC, N=3 to 4 mice/group). *P<0.05, ***P<0.001. One-way ANOVA with Sidak´s multiple comparisons test.
A: oxidative growth. W303-1Bcym1Δ strains harbouring the wild-type CYM1 allele (CYM1wt), the cym1R163Q mutant allele or the empty vector were serially diluted from 107 to 104 cells/ml. Five microliters of each dilution were spotted on SC agar plates without uracil, supplemented with 2% glucose, 2% glycerol or 2% ethanol. Plates were incubated at 37°C for 3-7 days.
After NEBD, Cyclin B2 localizes to unattached kinetochores, mediated by Mad2 bound to Mad1 or by Mad2 bound to a yet unidentified kinetochore receptor (protein-X). Multiple SAC factors, including kinases, localize at the outer kinetochores. Mad2-mediated Cyclin B2-Cdk1 contributes to SAC signalling, in complement with Mad1-mediated Cyclin B1-Cdk1. As a scaffold recruiting multiple SAC factors to the vicinity, the outer kinetochore catalyses the assembly of MCC. As a consequence, MCC inhibits the activity of APC/C to preclude the anaphase as long as improperly attached kinetochores are present. The error-correction machinery promotes the establishment of correct bipolar microtubule kinetochore attachment. When all kinetochores achieve bipolar attachment, SAC signalling is silenced, and the cell enters anaphase. C: C-Mad2, O: O-Mad2, X: protein X, B1: Cyclin B1, B2: Cyclin B2
E. Spatially restricted AC and DMZ cell clusters embedded in UMAP of whole embryo scRNA-seq data
MQ can bind both high molecular weight (HMW) targets such as mutant p53 and low molecular weight (LMW) targets e.g. GSH and Cysteine. MQ conjugation to GSH (GS-MQ) is reversible, indicating that MQ can transfer between multiple HMW and LMW cellular targets. Thus, GS-MQ serves as an intracellular drug reservoir. MRP1 regulates GSH and oxidized GSH (GSSG) content and exports GS-MQ. Therefore, MRP1 inhibition potentiates the effect of APR-246/MQ through a dual mechanism: 1) inhibition of GS-MQ efflux and 2) disruption of the intracellular thiol balance sensitizing cells to oxidative stress. We postulate that a MQ reservoir is similarly formed by conjugation to other thiols (R-SH) targets, e.g. Cys. Furthermore, xCT and MRP1 collectively regulate LMW target availability and thus the intracellular reservoir of MQ, thereby governing sensitivity to APR-246.
D) Representative images of NMJs in the soleus muscle at 130 days. Muscles were immunostained for neurofilament H (NF-H, in red) and stained with α-bungarotoxin (α-BTX, in green). Scale bar, 20 µm.
E. Maximum frequency (kHz) of each syllable in YFO and AFO. Data information: Data are presented in the box plot or pie chart format. The central band in each box represents the median; boxes indicate the middle quartiles, and whiskers extend to the minimum and maximum values. *p<0.05, determined using Student's or Welch t-test.
(D) Plot showing the time course of T. thermophila cell growth in the presence of CA4 (20µM) or parabulin (50µM; error bars corresponding to the standard deviation of triplicate biological measurements). Control experiments are done with DMSO alone.
(G) Representative picrosirius red staining of cross sections of left ventricles. Scale bar: 50μm.
H Luciferase activity in 293T cells transfected with scramble or USP19-specific siRNA and ISRE luciferase reporter after SeV infection for indicated time points with or without Beclin-1.
Oct4-eGFP reporter MEFs or WT MEFs were infected with combinations of shRNAs. (D) Representative FACS profiles of mouse-specific pluripotency cell surface marker SSEA1+ iPSCs on day 14 of reprogramming and (E) quantification of the percentage of SSEA1+ iPSCs in MEF cultures that were infected with the indicated shRNAs targeting Vim and/or Tnfaip2 [n=5 biological replicates; data were normally distributed (P>0.05 as per Shapiro-Wilk test) but showed unequal variance; data were analyzed by Brown-Forsythe and Welch ANOVA and Dunnett's multiple comparisons test].
Venn diagram showing 1055 genes uniquely downregulated in the "main LPS" cluster (red) and 29 genes exclusively decreased in the "subset LPS" (yellow) compared to their corresponding controls (blue) (FDR<0.05). A total of 87 genes were shared between the two LPS populations.
Densities (cells/mm2) of GFAP+Ki67+ cells in V-SVZ whole-mounts 24h after TMZ treatment. Arrowheads point to dividing NSCs under regenerative condition. n=6, *p= 0.0173. Scale bar: 10 μm.
Deubiquitinating activity of UBP13 against K48- and K63-linked ubiquitination. Diubiquitins linked through K48 or K63 (K48 Di-Ub or K63 Di-Ub) were incubated alone or with GST-UBP13 or GST-UBP13C207S for 18 h. Deubiquitination of the diubiquitins was analyzed by western blot with the α-ubiquitin (α-Ub, P4D1) antibody. The presence of GST-UBP13/UBP13C207S recombinant proteins was confirmed by the α-GST antibody.
C Experimental workflow for validation experiment using a different promoter (EF1α), reporter gene (luciferase) and quantification method (qPCR).
(B) At 48h post-transfection of wtSPINK6 plasmid in 293T cells, cell lysate and concentrated supernatant (50×) were applied to the detection of SPINK6 protein and β-actin by WB.
(C) Immunoblotting of cell lysates prepared as (B) with antibodies to respiratory chain subunits NDUFB8 and COXII, and GAPDH as loading control. Means ± SEM of n=3 experiments
Representative images showing colony formation in hOSE-MXIV, hOSE-YAP and hOSE-YAPS127A cells with or without pRB knockdown or LATS2 knockout. hOSEs at the 7th passage were incubated in the growth medium in a soft agar culture system for 9 days before imaging.
Primary astrocytes from OTUB1fl/fl and GFAP-Cre OTUB1fl/fl mice were transfected with SOCS1-MYC plasmids. Twenty-four hours after transfection, cells were treated with cycloheximide (CHX, 100 μg/ml) for indicated times. SOCS1 protein levels were analyzed by WB (upper panel). The lower panel shows the relative protein levels of SOCS1 normalized to Tubulin (n = 3 for both groups).
(C) Relative changes in fluorescence for WT, D312N and D405N GltPh upon a temperature jump in MST experiments as a function of [K+]. Solid lines represent non-parametric fits, and shaded area show bootstrapped 99% confidence intervals for those fits. Non-overlapping confidence intervals indicate significant difference between WT and mutant binding curves. Values are given as mean ± SD (n≥3).
(G, H) Co-immunoprecipitation of ectopically expressed Myc-CDC20 171-499 with ectopically expressed Flag-p65 1-310 fragment in HEK293T cells.
D) Proteasome activity measured using the ProteasomeGlo Assay (Promega), normalised to WT means. Mean±SD, 2-way ANOVA with Holm-Sidak's multiple comparisons. N=6 experiments, representative experiment shown (n=4 technical replicates), ****p≤0.0001.
(B and C) The tumor load (B) or tumor number (C) in the whole colon was measured (n = 12 biological replicates, mean ± s.e.m., *P = 0.0431, **P = 0.003, two-tailed unpaired Student's t-test).
B Sequence logos corresponding to enriched elements identified by de novo motif analysis of two clusters of H3K9cr peaks located in promoter regions in the E13.5 forebrain.
(C) and (D) represents nucleotide and amino acid abundances after 4 hours of growth in amino acid supplemented M9 medium at 40/42°C (condition of filamentation). Concentration of all metabolites were normalized to WT levels at 4 hours when grown under similar conditions. Methionine levels are extremely low, which recover largely in panel (D). Levels of purines (IMP, AMP) are also largely rescued with amino acid supplementation, however dTMP, dTDP and dTTP levels remain extremely low. Error bars represent SEM of at least three biological replicates (see Methods). The dashed line in each plot represents value of 1 for WT.
The expression levels of the endogenous LAMP2A and LAMP1 proteins were analyzed in wild-type (WT) and Ctns−/−mousefibroblasts (A), kidney (B) and liverlysosomes (C) by Western blot. Quantitative densitometry analysis of immunoblots obtained from different experiments was performed by calculating the ratio between LAMP2A and actin signals in each lane. Results are mean ± SEM of four independent experiments with mousefibroblasts, 5 WT and 6 Ctns−/−mousekidneys, 3 WT and 3 Ctns−/−mouselivers (lysosomal extracts).
Immune cell contexture in healthy colon and colon tumors of Apcfl/fl-Cdx2CreERT2 mice. Relative TCRβ+ T cell content in colon (n=10) and tumor (n=22). relative content of individual cell types was determined in tissue-derived single cell suspension using cell type specific antibodies and FACS analysis.
Phospho-site clusters in the carboxyl-terminus of V2R and AT1aR are underlined and color-coded to reflect the PXPXXP and PXXPXXP patterns as proposed in a previous study (Zhou et al., 2017).
(E) Example of interaction screening as in B, but using sNASP-dNLS against EGFP (EGFP-OMP25), tethered H3.1 (H3.1-EGFP-OMP25) and tethered H4 (H4-EGFP-OMP25). Scale bar represents 10 μm
Frequency distribution of ChIP-seq signals at 48 hours compared to 6 hours hypoxia. The ratio of total HIF-α signal had a unimodal distribution (purple line). However, upper tertile HIF-α sites (solid red line) had a comparable ratio of HIF-1β signal (dotted red line) to the ratio of HIF-1β signal in the lower tertile HIF-α sites (blue lines) suggesting that differences in HIF-α signal resulted from random variation rather than a true biological difference
(G) Survival curves of GRfl/fl and GRVillKO mice treated for 7 days with 25 mM ZnSO4 in the drinking water and challenged, i.p., with 35 µg TNF, solved in sterile PBS, per 20 g bodyweight. No deaths occurred later than 150 h after TNF injection. Results represent combined data of 6 experiments.
B PCA plot showing global gene expression profiles of EpCAM+ cells isolated from ethanol-, P4- and R5020-treated human breast tissue microstructures, n=3.
B. Uridylated tRNA reads overlap mainly with 3' trailers, T-loop and anticodon loop regions. Heat map showing the coverage of uridylated reads on pre-tRNAs. The pre-tRNA sub-regions (as indicated in (A)) are in small letters on the x-axis.
(D-E) Quantification of nuclear morphologies (D) and γH2AX-positive DNA damage foci (E) following palbociclib (1.25μM) treatment in p53 WT and KO RPE1 cells. Cells were treated for 1, 4 or 7 days and then analysed before or after drug washout for 48 hours. 100 cells (nuclear morphology) or 50 cells (γH2AX foci) were scored per condition per experiment, and bar graphs represent mean data +SEM from 6 experiments.
| Representative analysis of B220 and IgM surface expression in bone marrow (left) and spleen cells (right) of mice from the indicated genotypes.
(B) Serum levels of A-dione in WT males, ARLmon/Y and AR-/Y mice at the age of 13 weeks.
A) Diagram showing the genomic background and the approximation used to measure DSB-SPB interaction. Cnm67-RFP and Ddc2-GFP were used as SPB and DSB markers respectively. D1: inter-SPB distance; D2: DSB distance to proximal SPB; D3: DSB distance to distal SPB. Graph represents the mean ± SD of D1, D2 and D3 distances from three independent experiments. At least 100 cells per experiment were scored using the maximum projection of three z-planes. P values were calculated using a 2-tailed unpaired Student t test. A representative picture of a wild-type strain depicting DSB-SPB interaction is shown. Scale bar: 3μm.
(B-D) Representative images of WT or ANKRD26-/- PLK4Dox cells immunostained with the indicated antibodies. Scale bar = 5 µm.
A-D. CMTs visualized with MAP4-GFP in root epidermal cells of the cre1-12 mutant at the transition (TZ) and the elongation (EZ) zones at time point 0 and 60 min after mock (DMSO) (A), cytokinin (CK) (B), auxin (C) and CK plus auxin (D) treatments. As CK and auxin sources 10 µM BAP and 0.1 µM NAA were used, respectively. For the double CK plus auxin treatment roots were pretreated for 60 min with CK, whereafter they were transferred to medium supplemented with both compounds. Scale bar 10 µm.
(C, D) Spine morphology of P21 Thy1-Yfp (C) and Tlr3-/-; Thy1-Yfp mice (D) after poly(I:C) stimulation at P4 and P5. One secondary dendrite of an apical dendrite of each somatosensory layer 5 cortical neuron was selected to examine the spine morphology. Three mice were analyzed for each group. Saline-treated Thy1-Yfp, 44 neurons; poly(I:C)-treated Thy1-Yfp, 43 neurons; saline-treated Tlr3-/-;Thy1-Yfp, 46 neurons; poly(I:C)-treated Tlr3-/-;Thy1-Yfp, 50 neurons. Mean values SEM are shown. Data were analyzed by unpaired t-test. Scale bar, 5 μm. *** P < 0.0001.
G. Co-immunoprecipitation performed on HeLa cells expressing LacZ control, HA-PNRC1WT, HA-PNRC1W300A or HA-PNRC1ΔNLS constructs with a specific anti-DCP1α antibody and probed with anti-PNRC1 and anti-NPM1 antibodies.
Top: same as the top part of Figure 2B. Middle/Bottom: Nuc/Cyto (middle) and IP/Input (bottom) ratios for variants of Jpx#9 in which the indicated sequence was introduced at the indicated position (aligned to the sequence on top) in either the WT or the mutated Jpx#9 context. Yellow, turquoise, and white arrows indicate the tiles mentioned in the text. The histograms on the right indicate the distributions of the values in each heatmap. Asterisks indicate positions where the Nuc/Cyto ratios of the mutated tiles are significantly different than those of the WT tile (Wilcoxon two-sided rank-sum test P<0.05).
The graph shows the averages over 60 neurons from WT adult mice (n=3) and 60 neurons from KO+A-mWwox adult mice (n=3). There was no significant change observed between the average firing rate of the WT and the KO+A-mWwox adult mice.
(d) The measured concentration of CTP in synchronized cells shown in red (mean and s.d. of n=5; ) in Equation 7; the deconvoluted concentration dynamics, in case of no synchronization loss (green; in Equation 7); and the expected concentration dynamics based on the deconvoluted concentrations and considering the loss in synchronization, matching the measured concentrations (black; Equation 7). The measured concentrations converge towards the steady-state concentrations measured in non-synchronized cells (horizontal blue line).
(D) qRT-PCR analysis of IL6 expression in HDFs upon indicated stimulations for 4 h in absence or presence of the inhibitor of sphingosine kinases-SKI II (SPHKi, 50 µM).
(C) Quantification of the phenotypes in (B); 100 small budded and 100 large budded cells were quantified per experiment. Average and SD of three independent biological experiments is shown.
C. Binding assay using MBP fused Apc1-loop500 fragments and B56γ. Apc1-loop500 WT or its derivatives (∆11 or 3A) were incubated with the 35S-labelled Flag-B56γ in interphase extract (Inter) or anaphase extract (Ana) supplemented with CycB∆167 at 23˚C for 1 hr. The bound proteins were recovered by amylose beads, separated by SDS-PAGE and detected by autoradiography or coomassie brilliant blue (CBB) staining. The bar graph is quantification of bound B56γ. The intensities of MBP control were arbitrarily set to 1.0. Error bars, s.e.m. from three independent experiments.
Temporal regulation of MYBL2 in HPAF-II orthotopic xenografts treated with ETC-159. Each data point represents an individual tumor. The horizontal lines represent median of 4-6 replicates with the upper and the lower edges of the boxes representing the 75th and the 25th percentile of the data respectively and the whiskers representing 1.5x interquartile range.
A) Map of the region upstream of IL3 gene spanning the -34 kb pDHS and -37 kb inducible enhancer, together with the locations of the guide RNAs used to delete the -34 kb pDHS and the PCR primers used to detect the deletion. On the right is a PCR analysis confirming deletion of the -34 kb pDHS on both alleles in 2 out of 4 clones selected for the analyses shown below.
(G) Immunohistochemistry for YAP and TAZ in well-differentiated and mesenchymal SCC from Lgr5CREER/KRASG12D/TP53KO mouse model
I, SynGO enrichment for synaptic localization and function of commonly affected transcripts between Ctrl/S vs Ctrl/SD and Ctrl/SD vs Fxr1over/SD comparisons.
A, B (A) Schematic of the spatially-restricted activation of ROS production at the plasma membrane after CIF stimulation (B) Comparison of the components of the cytoplasmic/nuclear signaling cascades induced by the flg22 bacterial pattern peptide (left) and the CIF peptides (right). Note that all of the signaling components in the two pathways belong to the same gene families, with the exception of the transcription factors. Components for which there is currently no direct experimental evidence are marked in gray, as are arrows indicating activation events that have not yet been experimentally established.
(C) Graph shows the normalized cell contraction measured by Xcelligence Real time cell analyzer in wt (red) and FLNAΔECS (green) primary vascular smooth muscle cells (vSMC) indicating hypercontraction in FLNAΔECS cells in response to 10μM U46619. Data shown as mean ± SD from three independent experiments.
E. Mean tumour volume at 21 days after sub-cutaneous injection of TF-1 TpoR CALRdel61 cells following treatment with 4D7 or IgG. Cells were pre-treated with 4D7 or IgG control for 1 hour prior to injection and treatment continued twice weekly at 12.5 mg/kg until euthanasia (n=3 mice per treatment) Data information: a student's unpaired t-test was used to determine statistical significance.
Quantification of IL-1β and IL-1Ra levels in plasma from human healthy control and MPSIII patients (n=6 control participants and n=21 MPSIII patients). Data are expressed as mean ± STDEV and were tested by unpaired t-test. C. IL-1β, control vs. MPSIII P=0.0407; D. IL-1Ra, control vs. MPSIII P=0.0001. Quantification of IL-1β and IL-1Ra levels in cerebrospinal fluid (CSF) from control and MPSIII patients (n=3 control participants and n=21 MPSIII patients). Data are expressed as mean ± STDEV and were tested by unpaired t-test; *P<0.05. F. IL-1Ra, control vs. MPSIII P=0.0167.
(A) Schematic depicting the identification of EI24 and BiP as IRE1 interaction proteins. HeLa cells transfected with HA-IRE1 were subjected to anti-HA immunoprecipitation followed by mass spectrometry assay.
Cytokine secretion of macrophages incubated with the indicated stimuli for 24 h. XO added to macrophages for 24 h. Febuxostat (Feb) was pre-incubated for 30 minutes with XO before addition to macrophages. Each symbol represents the value obtained for cells from an independent donor in an independent experiment. Insets show paired samples by donor in two different conditions. Grey asterisks mark comparison with Control n=3. One-way ANOVA with Tukey test for multiple comparisons was performed to determine statistical significance (*p<0.05, **p<0.01 and ***p<0.001).