EMBO/sd-character-level-ner huggingface dataset:
Figure 5A, B Immunoblot analyses to detect the protein expression of critical adaptors in the IFN-I and Jak-STAT signaling pathway in A549 cells after transfection with Ctrl or WTAP-specific siRNAs for 48 hrs. C ELISA quantification of m6A levels in mRNA extracted from shCtrl and shWTAP A549 cells. D, E Schematic representation of the position of m6A motifs within the IRF3 (D) and IFNAR1 (E) transcripts. The sites of the m6A RNA modification element 'DRACH' in IRF3 mRNA 5'-UTRs or IFNAR1 mRNA 3'-UTRs were predicted using RMBase v2.0 F1/R1 represents the detection site-1 containing three (IRF3) or four (IFNAR1) 'DRACH' elements and F2/R2 represents the detection site-2 containing two (IRF3) or three (IFNAR1) 'DRACH' elements. F, G Abundance of IRF3 (F) and IFNAR1 (G) transcripts (detection site-1 and -2) among mRNA immunoprecipitated with anti-m6A antibody from shCtrl and shWTAP A549 cells. n = 3 independent biological replicates, and error bars represent standard deviations. H Abundance of IRF3 and IFNAR1 transcripts (detection site-1) among mRNAs immunoprecipitated with anti-m6A antibody from A549 cells that were transfected with empty vector (EV) or HA-tagged WTAP plasmid for 24 hrs. I qRT-PCR analyses of the mRNA expression of IRF3 and IFNAR1 in shNC and shWTAP A549 cells. J Semi-qRT-PCR analyses of IRF3 and IFNAR1 mRNA and RNU6 and GAPDH mRNA (loading controls throughout) in the nucleus (Nu) and cytoplasm (Cyto) of A549 cells transfected with Ctrl or WTAP-specific siRNA for 48 hrs. K qRT-PCR analyses of IFNAR1 mRNA expression in shCtrl and shWTAP A549 cells, followed by treatment with Act D (5 μg/mL) for the indicated times. L Immunoblot analyses of IFNAR1 in shCtrl and shWTAP A549 cells, followed by treatment with Act D (5 μg/mL) for the indicated times. M qRT-PCR analyses of the proportion of IRF3 mRNA in polysome fractions from A549 cells transfected with Ctrl or WTAP-specific siRNAs. N, O Wild-type or mutated m6A consensus sequences (A-to-T mutation) of IFNAR1-3' UTR (N) and IRF3-5' UTR (O) were fused with Renilla luciferase reporter in psiCHECKTM-2 vector. P Relative luciferase activities in 293T cells after transfection with reporter vectors bearing IFNAR1-3' UTR or IRF3-5' UTR with wild-type (WT) or mutated (Mut) m6A sites. Renilla luciferase activity was measured and normalized to firefly luciferase activity. Q Relative luciferase activities of reporter vectors bearing IFNAR1-3' UTR or IRF3-5' UTR with wild-type (WT) m6A sites after cotransfection with empty vector (EV) or HA-tagged WTAP into shWTAP A549 cells. Renilla luciferase activity was measured and normalized to firefly luciferase activity.
Characterization of strains lacking respiratory supercomplexes (A) Blue-native gel electrophoresis and immunoblots of cells expressing the wild type form of Cor1 (Cor1WT), as well as the mutants Cor1N63A, N187A, D192A (Cor1*) and Cor1N63A, N187A, D192A, V189A, Y65A, L238A, K240A (Cor1**) in wild type (WT) background as well as in cells lacking CRD1 (crd1Δ).Figure 2(A) Blue-native gel electrophoresis and immunoblots of cells expressing the wild type form of Cor1 (Cor1WT), as well as the mutants Cor1N63A, N187A, D192A (Cor1*) and Cor1N63A, N187A, D192A, V189A, Y65A, L238A, K240A (Cor1**) in wild type (WT) background as well as in cells lacking CRD1 (crd1Δ). Blots were probed with antibodies against Cor1 to visualize Complex III (CIII), as well as Cox1, to monitor Complex IV (CIV). CV: Complex V; Cor1Cor2: multimer consisting of Cor1 and Cor2 (B) Reduced-minus-oxidized difference spectra of strains described in (A). Heme peaks are indicated for Cor1WT in WT background. Steady-state protein levels of strains as described in (A) cultivated on YP media containing glycerol Steady-state protein levels of strains as described in (A) cultivated on YP media containing CM media with galactose as carbon source (D, E).
Figure 6Figure 6. 4D reorganization of the yeast genome.(A) Dynamics of centromere contacts (top panel), short/long ratio (middle panel) and intra/inter contact ratio (bottom panel) for each of the 20 time-points (blue dots, see bottom x-axis) during the cell cycle. The three folding states (I, II, III; Fig EV4) identified in the analysis is indicated under the panels, as well as interpretation with respect to individualizatio status. Figure 6. 4D reorganization of the yeast genome.. (B) Illustration of the three chromatin folding states characteristic of each of the cell cycle phase. Establishment of sister-chromatid (SC) cohesion during S phase increases intra-SC long-range contacts and leads to the individualization of the replicated chromosomes. Then during M phase, the two sisters are segregated and each chromatid (C) individualized thanks to the action combination of cohesin cleavage, condensin loading and spindle elongation. The chromosomes display a stretched internal structure, which relaxed upon destabilization of the spindle with nocodazole. Figure 6. 4D reorganization of the yeast genome. (C) Model of loop-extrusion generating the condensin-dependent loop formation between the centromere and the rDNA cluster, two regions enriched in condensin deposition. A loop formed in-between the centromere and the rDNA cluster may extend until it reaches these two discrete position, and stall because of mechanic impediment blocking further extrusion.
Figure 1Schematic domain overview of endophilins-A1-3, highlighting the BAR and SH3-domains. Schematic overview of the sample collection procedure for single-cell PCR (scPCR). Single IHC cytoplasms from acutely dissected organs of Corti of C57BL/6J (Wt) mice after hearing onset were aspirated and processed for scPCR as depicted. (B') Expression analysis of endophilins-A1-3 from individually isolated IHC cytoplasms using RT-PCR from a representative experimental run. Please note that for these experiments, negative bath control samples from before and after the isolation procedure were an essential requirement to ensure lack of contamination from cellular debris in bath solution. HPRT was used as a housekeeping gene. Immunoblotting of tissue lysates from p15 Wt (C57BL/6J), 1-SKO, 1/2-DKO and 1/3-DKO revealed protein expression of endophilins-A1 and -A2 in the murine cochlea and ensured antibody specificity. Unfortunately, none of the commercially available endophilin-A3 antibodies we tested in these experiments gave a specific signal for A3 in cochlear extracts, but rather appeared to (also) detect A1. γ-adaptin was used as loading control. All antibody epitopes localize to the distinct C-terminal regions of the different endophilin-A family members. Hi, hippocampus; Ce, cerebellum; Co, pooled cochleae from a single individual of the indicated genotype; Md, modioli (micro-dissected and pooled from 10 Wt animals); OC, organs of Corti (micro-dissected and pooled from 10 Wt animals).
Activation of miR-21-3p by PPAR/ requires TGFβ-1.Figure 2(A) RT-qPCR quantification of relative pri-miR-21 level in HaCaT human keratinocytes treated with the PPAR/ agonist GW0742 (+) or vehicle (-), with (+) or without (-) cycloheximide (Cyclo) as indicated. Pri-miR-21: Veh vs GW0742 P = 0.009. N=3 biological replicates, one representative experiment is shown out of two independent replicates. (B) RT-qPCR quantification of relative pri-miR-21, pre-miR-21, miR-21-5p and miR-21-3p levels in HaCaT cells treated for 24h with 2 or 5ng/ml of recombinant human TGFβ-1 (+) or vehicle (-) as indicated. Pri-miR-21: Veh vs TGF-1 5ng/ml P = 0.029; Pre-miR-21: Veh vs TGF-1 5ng/ml P = 0.001; miR-21-5p: Veh vs TGF-1 5ng/ml P = 0.002; miR-21-3p: Veh vs TGF-1 5ng/ml P = 1.7E-05. N=3 biological replicates, one representative experiment is shown out of two independent replicates . (C) RT-qPCR quantification of pri-miR-21, pre-miR-21, miR-21-5p and miR-21-3p levels in HaCat cells treated for 24h with the PPAR/ agonist GW0742 (+), TGFβ receptor inhibitor SB431542 (+), or vehicle (-) as indicated. Pri-miR-21: GW0742 vs SB431542 P = 0.004, GW0742 vs GW0742/SB431542 P = 0.015; Pre-miR-21: Veh vs GW0742 P = 0.022, GW0742 vs SB431542 P = 0.036, GW0742 vs GW0742/SB431542 P = 0.024; miR-21-5p: GW0742 vs SB431542 P = 0.034, GW0742 vs GW0742/SB431542 P = 0.024; miR-21-3p: Veh vs GW0742 P = 0.036, GW0742 vs SB431542 P = 0.011, GW0742 vs GW0742/SB431542 P = 0.008. N=3 biological replicates, one representative experiment is shown out of two independent replicates. (D) RT-qPCR quantification of relative Tgfb1 level in the epidermis of acutely irradiated (Ac-UV) and non-irradiated Ppard +/+ and -/- mice. Tgfb1: Ppard +/+ no UV vs Ac-UV P= 0.034, Ppard +/+ Ac-UV vs Ppard Ac-UV P= 0.030. N=2-3 animals per group, one representative experiment is shown out of three independent replicates. (E) RT-qPCR quantification of relative miR-21-5p and miR-21-3p levels in the skin of Ppard +/+ mice treated with the TGFβ receptor inhibitor SB431542 (+) or vehicle (-), with (+) or without (-) acute UV exposure (Ac-UV). miR-21-5p: no UV vs Ac-UV P = 0.038, Ac UV vs Ac UV/SB431542 P = 0.028; miR-21-3p: no UV vs Ac-UV P = 0.017; Ac-UV vs Ac-UV/SB431542 P = 0.035. N=3 animals per group, one representative experiment is shown out of three independent replicates.
Figure 1A NF-κB can recruit a variety of binding partners to target promoters, including the chromatin modifying enzyme p300, the elongation complex P-TEFb, and components of transcriptional machinery. NF-κB target genes with a variety of functions were chosen for this study. B Induction of NF-κB targets in Jurkat T cells in response to 20 ng/ml TNF treatment for 1, 2, and 4 hours as measured by RT-qPCR. Target values were normalized to GAPDH and are reported as fold change relative to basal expression. Data are presented as mean ± standard deviation (SD) of 3 biological replicates. C Enrichment of RelA before and 30 and 60 minutes after treatment with 20 ng/mL TNF as measured by ChIP-qPCR and shown as % input (non-IP control). Data are presented as mean ± SD of three biological replicates. D Maximum intensity projections of smFISH fluorescence microscopy z-stacks of basal Jurkat T cells stained for the indicated genes. Nfkbia, Tnfaip3, Tnf, and Il6 were labeled with Quasar 670, and Il8 and Csf2 were labeled with fluorescein. All images were filtered as described in Materials and Methods. Brightness and contrast were enhanced for visualization. Scale bars: 10 μm. E Histograms of transcripts per cell for target genes (blue) overlaid with probability density plots (red) generated from smFISH data. Cells were combined from three replicates (Nfkbia, Tnfaip3, Tnf, and Il6) or one replicate (Il8, Csf2). F-G Bar graphs of mean (F) and CV (G) of smFISH distributions for the indicated genes. Error bars indicate bootstrapped 95% confidence intervals (CIs) for the samples in (E). Significant differences indicated by non-overlapping CIs. H Ratio of enrichment of total histone H3 to acetylated H3 (AcH3) in Jurkat T cells at the indicated target promoters quantified by ChIP-qPCR. Data are presented as mean of % input (non-IP control) ± SD of three biological replicates. I Graph of log10(mean) versus log10(CV2) of basal mRNA distributions measured in Jurkat T cells (black), HeLa cells (red) or murine bone marrow derived macrophages (green) for endogenous genes and four latent HIV LTR integrations. Gray shading indicates 95% CI of the linear regression for the basal trendline. Poisson trendline indicated by dashed line. HeLa data from Lee et al. (2014) and HIV LTR data from Wong et al. (2018).
Localization of α 1S subunit.Figure 7Localization of α 1S subunit. Whole skeletal muscle fibres enzymatically isolated from Ctrl (A-D) or ΔDHPR (E-H) FDB muscles 6 months post injection were processed for immuno‐fluorescent labelling for α1 S subunit (red) and laminin (green). Scale bars, 10 μm; Arrows indicate α1 S subunit expression on sarcolemma; antibody labelling was visualized by serial confocal microscopy and represented as movies of the optical sections (Supplementary Movies S5A and S5B). (D, H) Present projections of confocal Z‐series (step between each frame is 1 μm) along XZ and YZ planes as indicated.
Figure 2(A) Huh7.5 cells were exposed to SARS-CoV-2 pseudovirus directly or after pre-treatment with different concentrations (0.0001, 0.001, 0.1, 0.5, 1, 5, 50, 100, 250 IU/mL) of UF heparin or LMWH enoxaparin for 30 min at 37°C. Infection was determined by luciferase reporter activity after 5 days. Data information: Data show the mean values and error bars are the SEM. Statistical analysis was performed using (A) ordinary one-way ANOVA with Dunnett's multiple-comparison test. *P≤0.05, **P≤0.01, ***P≤0.001, ****P≤0.0001 (n=3 donors measured in triplicate). (B) SARS-CoV-2 pseudovirus was pre-incubated for 30 min at 37°C with UF heparin (250 IU/mL) or LMWHs tinzaparin (250 IU/mL) or dalteparin (250 IU/mL) or LMWH enoxaparin (250 IU/mL) or nadroparin (250 IU/mL). Huh7.5 were exposed to the SARS-CoV-2 pseudovirus, alone or treated with different LMWHs for 4 hours at 4°C, washed, lysed and binding was determined by ELISA. (C) SARS-CoV-2 pseudovirus was pre-incubated for 30 min at 37°C with UF heparin (250 IU/mL) or LMWHs tinzaparin (250 IU/mL) or dalteparin (250 IU/mL) or LMWH enoxaparin (250 IU/mL) or nadroparin (250 IU/mL). Huh7.5 cells were infected with SARS-CoV-2 pseudovirus in presence or absence of different LMWHsSARS-CoV-2 and infection was determined after 5 days by luciferase reporter activity. Data information: Data show the mean values and error bars are the SEM. Statistical analysis was performed using (B) ordinary one-way ANOVA with Tukey's multiple-comparison test (n=3 donors measured in monoplo), (C) ordinary one-way ANOVA with Dunnett's multiple-comparison test. *P≤0.05, **P≤0.01, ***P≤0.001, ****P≤0.0001 (n=3 donors measured in triplicate) (D) 293T cells expressing ACE2 were infected with SARS-CoV-2 in presence or absence of antibodies against ACE2, UF heparin (250 IU/mL) or LMWH enoxaparin (250 IU/mL) and infection was determined after 3 days by luciferase reporter activity. Data information: Data show the mean values and error bars are the SEM. Statistical analysis was performed using ordinary one-way ANOVA with Dunnett's multiple-comparison test. *P≤0.05,**P≤0.01 (n=3 measured in triplicates). RLU: relative light units. (E) VeroE6 cells were infected with SARS-CoV-2 isolate (hCoV-19/Italy; 100 TCID/mL) previously treated with serial dilutions of LMWH enoxaparin. Cell viability was determined by using an MTT assay (n=3 donors measured in triplicate).
Figure 4Schematic representation of Notch reporter E(spl) mδ0.5 expression during photoreceptor differentiation. Expression is initiated in R3 and R4 of the 5-cell pre-cluster and becomes restricted to R4 as Notch activity resolves. Light orange indicates photoreceptors with R3 in light green and R4 in dark green. MF marks the morphogenetic furrow, boxed region indicates the region shown in B. Equatorial region of eye imaginal discs where E(spl) mδ0.5 expression (green) becomes restricted to a single photoreceptor in each cluster (magenta), as detected in control and Dl∆β1-2/+ discs (top panels). In Df(3R)DlFx3 /+ and Dl∆β1-2/Df(3R)DlFx3 discs (bottom panels) E(spl) mδ0.5 expression is reduced (Df(3R)DlFx3 /+) or absent from several clusters (Dl∆β1-2/Df(3R)DlFx3) indicative of reduced Notch signalling. Scale bars correspond to 10 μm. Proportion of photoreceptors clusters that fail to express the E(spl) mδ0.5 reporter in the indicated genotypes. ns, no significant difference, *** P<0.0001 (one-way ANOVA). On the violin plot, dashed line represents the median and the dotted lines show the quartiles.
Figure 1(A) Design of the let-7 sensor reporter and sequence of let-7a. Sensor (+) vector has the antisense sequence of let-7a inserted into the 3'UTR of the luciferase gene. (B) Relative luciferase activity of the let-7 sensor reporter (sensor (+)) or the negative control sensor (-) reporter contransfected with pLX-Lin28A in HEK293FT cells with or without pcDNA-pri-let-7a transfection. Error bars show SD; n=3. Significance was assessed using 2‐tailed Student's t‐test, < 0.05*. (C). The screening model. A screening in 384-well plates with a library of 1469 genes was performed. (D). Screening results: relative luciferase activity of each gene in the library. Only genes that did not affect the luciferase activity of the sensor (-) reporter (0.5 <, > 2.0) were analyzed. (E). Relative luciferase activity of the sensor (+) reporter or sensor (-) reporter induced by expression vectors of the top 5 genes identified in the screen or the GFP vector in HEK293-FT cells. Error bars show SD; n=3. Significance was assessed using 2‐tailed Student's t‐test, < 0.05*. (F). Heat map of relative miRNA expression of various miRNAs in HEK-293FT cells transfected with expression vectors of the top 5 genes from the screen, or the ctrl (GFP) vector. Red color represents suppressed expression compared with ctrl (GFP). n=3.
Summary of functional effects of MICA-129 variants depending on expression intensity.Figure 8For target cells expressing the MICA-129Val variant, the degree of NK-cell cytotoxicity and IFNγ production increased steadily with the MICA expression intensity. Augmented expression of the high-avidity MICA-129Met isoform, in contrast, had no or even a negative effect on these NK-cell functions due to a rapid down-regulation of NKG2D on NK cells. Antigen-dependent co-stimulation of CD8+ T cells with the MICA-129Met variant allowed for an earlier antigen-dependent activation than co-stimulation with the MICA-129Val variant. However, the down-regulation of NKG2D in response to MICA-129Met ligands impaired any subsequent NKG2D-dependent co-stimulation and T-cell activation. The down-regulation of NKG2D on CD8+ T cells was augmented with MICA-129Met expression intensity.
Figure 5A Representative images of co-cultures of control and PKAN NPCs infected with GFP-LV and tdT-LV expressing vectors, respectively, at the beginning (Day 1), after 120 (Day 120) and 150 days of differentiation (Day 150). Scale bar 20 μm. Plots show the number of green and red humanneurons counted at different time points. All data are presented as means + SEM of at least three independent experiments (One-way ANOVA). B Example of electrophysiological properties of cultured PKAN humanneurons with or without CoA incubation for 30 days. Repetitive firing activity (left) and relatively large Na+ and K+ currents (right), were restored by CoA. The histogram on the right shows fractions of repetitively firing cells recorded in untreated vs. CoA-treated neurons from control and PKAN patients (z-test). C An example of neurons stained with the ROS sensible fluorescent probe DCF and the nuclei dye Hoechst. Anti-NCAM antibody was used to detect neurons. Scale bar 20 μm. Plots of the DCF fluorescence signal from NCAM+ controls- and PKAN humanneurons differentiated or not in the presence of CoA (25 μM) in the medium for 3 weeks. All data are presented as means + SEM of at least three independent experiments (One-way ANOVA). D Oxygen consumption rate (OCR) with and without CoA on controls and PKAN patients. Basal and uncoupled (FCCP) respiration increased after CoA supplementation. Data presented as means + SEM of 24 independent replicates for each condition (Two-way ANOVA). E Heme quantification by absorbance at 400 nm of the soluble NPC cell lysates. All data are presented as means + SEM of at least three independent experiments (One-way ANOVA).
Figure 6(A−D) EM analysis demonstrated the induction of GOMED. Primary Atg7 KO β-cells were subjected to glucose deprivation for 1 hr. A representative AP-like structure containing insulingranule is shown in (A). An AL-like structure containing insulingranules is shown in (B). Scale bars = 0.2 µm. (A−D) EM analysis demonstrated the induction of GOMED. Primary Atg7 KO β-cells were subjected to glucose deprivation for 1 hr. (C, D) GOMED structures containing Golgi vesicles. An AP-like structure containing multiple Golgi vesicles (arrows) (C) and an AL-like structure fusing with a lysosome (arrowhead) (D) are shown. Scale bar = 0.5 µm. A magnified image of the dashed rectangle is shown in the inset. Scale bar = 0.2 µm. AP-like structure contained double-membrane. (E) The total number of AL-like structure was calculated from the EM images of WT and Atg7 KO β-cells after glucose deprivation. Error bars indicate s.e.m. (n = 46−163). *p < 0.01 and #p < 0.05 vs the value of 0 min. (F) The total number of GOMED structure was calculated from the EM images of Atg7 KO β-cells after glucose deprivation in the absence or presence of bafilomycin A1 (10 nM). Error bars indicate s.e.m. (n = 109−116). *p < 0.01 vs the value of 60 min. (G−J) EM analysis showed the induction of mitophagy. WT and Atg7 KO β-cells were subjected to glucose deprivation for 1 hr. Representative images showing mitophagy in Atg7 KO β-cells are shown in (G). Arrowhead (G) indicates mitophagy. Scale bars = 0.5 µm. (H, J) The number of structures representative of mitophagy (H) per cell was calculated from the EM images of β-cells after glucose depletion. Error bars indicate s.e.m. (n = 46−163). *p < 0.01 and #p < 0.05 vs the value of 0 min. (G−J) EM analysis showed the induction of crinophagy/SINGD. WT and Atg7 KO β-cells were subjected to glucose deprivation for 1 hr. Representative images showing crinophagy/SINGD in WT β-cells are shown in (I). White arrow (I) indicates crinophagy/SINGD. Arrows indicate insulingranules (I). Scale bars = 0.5 µm. (H, J) The number of structures representative of crinophagy/SINGD (J) per cell was calculated from the EM images of β-cells after glucose depletion. Error bars indicate s.e.m. (n = 46−163). *p < 0.01 and #p < 0.05 vs the value of 0 min. (K) The number of (pro) insulingranule-containing AL-like structure was calculated from the EM images of wild-type (WT) and Atg7 KO β-cells after glucose deprivation. Error bars indicate s.e.m. (n = 46−163). *p < 0.01 and #p < 0.05 vs the value of 0 min.
a) The number of somatic mutations discovered from each paired NPC case subjected to WES and key clinical parameters (Supplementary Table 2a) clustered according to the clinical stage.figf1a) The number of somatic mutations discovered from each paired NPC case subjected to WES and key clinical parameters (Supplementary Table 2a) clustered according to the clinical stage. Indel, insertion or deletion. (b) Trinucleotide contexts of somatic mutations occurring at cytosine nucleotides in NPC. The font size of the nucleotides at the 3′ and 5′ positions is proportional to their frequencies (Supplementary Fig. 3b). (c) Rates of arm-level and focal SCNVs (Online Methods) across different types of malignancies. Data regarding SCNVs of the following types were summarized from Zack et al.: RCC, renal cell carcinoma; GBM, glioblastoma multiforme; UCEC, uterine cervix; COAD, colorectal adenocarcinoma; BRCA, breast; HNSC, head and neck squamous cell; OV, ovary; LUAD, lung adenocarcinoma; BLCA, bladder; LUSC, lung squamous cell.
Analysis of HEK293 mutant MRPS5 V336Y and HEK293 MRPS5 wild-type cells.Figure 3A Generation time (n=8 clones, ± SD). B Whole cell in-vivo mitochondrial translation as determined by 35S-Met incorporation (n=4 clones, ± SEM). C Autoradiography of in-organello translation using 35S-Met labelling. D Top five GO terms (cellular component) associated with genes upregulated in HEK293 mutant MRPS5 V336Y compared to HEK293 wild-type MRPS5. Corresponding GO terms associated with genes upregulated in mutant MT-RNR1 A1555G lymphocytes (Hollis et al, 2015) were plotted. The bars represent the percentage of genes that map to a GO term and which are upregulated. Fisher exact t-test, +p<10-6, ++p<10-7, +++p<10-8 (MRPS5 V336Y n=4, MRPS5 wild-type n=6); *p<10-30, **p<10-40, ***p<10-50 (A1555G n=28, wild-type n=15).
Figure 6(A) Representative western blots showing SQR, TST, ETHE1 and SUOX of two control fibroblasts treated with DMSO (-) or with DMSO+ 4-NB (+). (B) Quantification of proteins levels in fibroblasts treated with 4-NB relative to control. (C) Representative western blots showing ADCK3, SQR, TST, ETHE1 and SUOX in two control (EV) and six ADCK3-depleted clones (ADCK3 RNAi). (D) Quantification of proteins levels in ADCK3-depleted clones (ADCK3 RNAi) relative to controls (EV).