EMBO/sd-character-level-ner huggingface dataset:
Figure 1a, Schematic highlighting the application of our single-cell RNA sequencing experimental and analytical workflow for primary patient tissue. b, UMAP visualisation of 4,986 epithelial cells aligned using canonical correlation analysis in Seurat. Cells are coloured by their cell type annotation (left) and patient of origin (right). c, Log normalised expression of markers for epithelial (EPCAM), mature luminal epithelial (ESR1), myoepithelial (KRT5, KRT14 and ACTA2) and proliferating cancer cells (MKI67). d, UMAP visualisation of 19,285 stromal and immune cells aligned and visualised as represented in b. e, Log normalised expression of markers for fibroblasts (PDGFRB, THY1, COL1A1, ITGB1 and S100A4), endothelial cells (PECAM1), T-cells (CD3D), CD8 T cells (CD8A), T-regulatory cells (FOXP3), B-cells (MS4A1), myeloid cells (CD68) and plasma cells (JCHAIN). f, Proportion of cell types across each patient.
DOR localizes to autophagosomes when autophagy is activated.Figure 2DOR localizes to autophagosomes when autophagy is activated. (A) Confocal images of HeLa cells transiently transfected with DOR and GFP‐LC3, and incubated for 1h with DMEM, HBSS (starvation), 2 μM rapamycin or HBSS containing 50 μM chloroquine. Nuclei were labelled with DAPI. Scale bars, 10 μm. (B,C) Confocal images of HeLa cells transiently transfected with DOR or GFP‐LC3 and incubated with 50 nM Lysotracker in DMEM or HBSS. Scale bars, 10 μm. (D) Confocal images of HeLa cells transiently transfected with DOR and LAMP1‐GFP, or with YFP‐LC3 and LAMP1‐GFP. Scale bars, 10 μm. Contrast‐corrected merge RGB pictures and the Z‐projection of Product of the differences from the mean (PDM) images are shown in all panels. Colour scales of PDM images have different maximal values, so the different conditions are not comparable from these projections. Product of the differences from the mean (PDM) values closer to 1 show reliable colocalized pixels. DAPI, 4′,6‐diamidino‐2‐phenylindole; DMEM, Dulbecco's modified Eagle medium; DOR, diabetes‐ and obesity‐regulated gene; GFP, green fluorescent protein; HBSS, Hank's balanced salt solution; LAMP1, lysosomal‐associated membrane protein 1; LC3, microtubule‐associated protein 1A/1B‐light chain 3.
Ub-associated Nrf2 targets are enriched in the autophagy network.Figure 5.(A) A second-order network centered on the core autophagy components (orange nodes) identified via PPIs showed an enrichment (hypergeometric P = 0.01) of Ub-associated Nrf2 targets (red nodes) in the network. (B) Venn diagram showing the various counts and overlaps between the microarray and network analysis. Also shown are the Ub-associated Nrf2 targets featured in the autophagy network mapped to mouse orthologues. Probes detecting transcripts exhibiting differential expression (Benjamini-Hochberg [BH]-adjusted P < 0.05) in at least one of the four comparisons are shown. Heat map represents Log2 (fold changes) with respect to either wild type (WT) or Atg7 KO (as indicated). Labels show the symbol, RefSeq (accession numbers from the NCBI Nucleotide database), gene probe name, and the gene row and gene column (i.e., array coordinates).
Figure 2(A) The response of a mitochondrial matrix-localized roGFP2-Tsa2ΔCR probe, expressed in wild-type and Δprx1, to the addition of exogenous H2O2 at the indicated concentrations. Cells were grown in SGal (-Leu) medium and harvested at early exponential phase. Lighter colored curves are controls showing the probe response to the addition of water. (B,C) The response of a cytosolic roGFP2-Tsa2ΔCR probe, expressed in wild-type, Δtrx3 and Δprx1 cells, to the addition of 0.1 mM (B) or 1 mM (C) exogenous H2O2. Cells were grown in SGal (-Leu) medium and harvested at early exponential phase. (D) The response of a cytosolic roGFP2-Tsa2ΔCR probe, in Δtrx3 cells transformed with a Trx3 plasmid and Δprx1 cells transformed with a Prx1 plasmid, to the addition of 0.1 mM exogenous H2O2. Cells were grown in SGal medium lacking the appropriate amino acids for plasmid selection and harvested at early exponential phase. The light grey curve in both panels represents the wild-type control, treated with the same concentration of exogenous H2O2. (E) The profile of mRNA expression of the yeast redox or redox-related enzymes in Δprx1+empty vector cells, compared to Δprx1+Prx1-WT cells, both grown to an early exponential phase in SGal (-Ura) medium (n = 3 biological replicates, with cells obtained from 3 independent cultures). (F) The response of a cytosolic roGFP2-Tsa2ΔCR probe, in Δprx1 cells or Δctt1Δprx1 cells transformed with either an empty plasmid or a Prx1-WT plasmid to the addition of 0.1 mM exogenous H2O2. Cells were grown in SGal medium lacking the appropriate amino acids for selection and harvested in early exponential phase (G) Model. Levels of the cytosolic catalase Ctt1 increase when activity of mitochondrial redox enzymes is impaired, leading to an increased cytosolic capacity for H2O2 removal.
Figure 6A-D S2 cells were transfected with polyadenylated F-Luc-nerfin-1 or F-Luc-par6 reporters containing an 8-nt or 109-nt 5'-UTR and the corresponding miRNAs. A plasmid expressing Renilla luciferase (R-Luc) served as transfection control. Panels (A) and (C) show normalized firefly luciferase activities and mRNA levels. Northern blot analyses of representative RNA samples are shown in (B) and (D). E,F HeLa cells were transfected with plasmids expressing the indicated R-Luc-let-7 reporters or the corresponding reporters carrying mutations in the let-7 binding sites and a plasmid expressing F-Luc as a transfection control. Renilla luciferase activities were normalized to those of the F-Luc and set to 100% in cells transfected with the reporter lacking the let-7 binding sites and analyzed as described in (A-D). G Interaction of GFP-NOT1 (wild-type or a mutant that does not bind DDX6, Mut) with HA-DDX6 and endogenous CNOT2 and CNOT3 in HEK293T cells. H-K Tethering assay using the R-Luc-HhR reporters containing the MALAT1 3'-UTR (H,I) or a poly(A) tail (J,K) and λN-HA-NOT1 (wild-type or Mut). R-Luc activity and mRNA levels were normalized to those of the F-Luc transfection control and analyzed as described in Fig 2C and D. L Expression levels of wild-type and mutant NOT1.
Figure 7(A) Representative double immunofluorescent stainings for Iba-1 and cGAS, and for GFAP and cGAS. Scale bars, 10 μm. (B) Gene strategy for preparing cGAS-conditional knockout (cKO) mice. (C) Breeding scheme for CX3CR1CreER mice crossed with cGAS-cKO mice, in which cGAS was deleted in microglia. (D) Representative genotyping analysis for WT, cGAS-KD, and cGAS-KO mice. (E) Flow chart illustrates A151 administration and experimental design. Mice received daily i.p. injections of A151 (300μg) or an equal volume of PBS vehicle for 3 consecutive days. (F) Representative images of TTC staining of brain sections from vehicle-treated WT MCAO mice, vehicle-treated cGAS-KO mice, and A151-treated cGAS-KO mice on day 3 after tMCAO. Three representative rostrocaudal levels of TTC staining are shown. (G) Bar graph shows percentages of infarct volume of indicated group. n = 6 mice per group. (H) Bar graph shows modified Neurological Severity Score (mNSS) in vehicle-treated WT MCAO mice, vehicle-treated cGAS-KO mice, and A151-treated cGAS-KO mice n = 10 mice per group.
Figure 5A-B Canonical pathways (A, DRG, and B, spinal cord) identified by IPA are ranked by P (-log10P). Positive and negative z-scores (in the spinal cord) indicate up-regulation or down-regulation, respectively, according to the color scale. Bar colors correspond to significant activation (orange), deactivation (blue), or no change (gray) in pathway regulation.
Figure 5(A) Schematic representation for the intracerebroventricular (ICV) injection of Slc6a20a antisense oligonucleotide (ASO) into the lateral ventricle (LV) for the reduction of Slc6a20a expression in the whole mouse brain. (B) Slc6a20a-ASO decreases the levels of Slc6a20a mRNAs in the brain of WT and PtenΔC/ΔC mice (P20-32), as shown by qRT-PCR analysis performed 1-2 weeks after injection. (n = 5 mice for WT-Sal/saline, 4 for WT-ASO, 3 for ΔC-Sal, and 3 for ΔC-ASO, *P < 0.05, **P < 0.01, ***P < 0.001, Student's t-test for each comparison). The error bars represent SEM. (C) Slc6a20a-ASO decreases the levels of SLC6A20 proteins in the brain of WT mice (2-4 months), as shown by immunoblot analysis of whole-brain lysates six days after injection. (n = 4 mice, **P < 0.01, Student's t-test). The error bars represent SEM. (D) PtenΔC/ΔC mice (2-4 months) treated with Slc6a20a-ASO display partially normalized levels of whole-brain glycine, as shown by the lack of difference between saline-treated WT and ASO-treated PtenΔC/ΔC mice. Note that the glycine levels observed here are ~4 times lower than those measured in Fig. 3A, which could be attributable to different mouse ages (P21 in Fig. 3A vs. 2-4 months in Fig. 5D), absence and presence of ASO injection, or lot-to-lot variation of the ELISA kits. (n = 8 mice for WT-saline, 5 for WT-ASO, 7 for ΔC-saline, and 8 for ΔC-ASO, **P < 0.01, ns, not significant, two-way ANOVA with Tukey's test). The error bars represent SEM. (E) PtenΔC/ΔC mice (P20-37) treated with Slc6a20a-ASO display an NMDA/AMPA ratio at hippocampal SC-CA1 synapses that is comparable to that in ASO-treated WT mice. (n = 11 neurons from 5 mice for WT-ASO, 10 (4) for ΔC-ASO, ns, not significant, Mann-Whitney's U test). The error bars represent SEM. (F) PtenΔC/ΔC mice (P19-37) treated with Slc6a20a-ASO display unaltered mEPSC frequency and amplitude in CA1 pyramidal neurons, as compared with ASO-untreated PtenΔC/ΔC mice. Note that mEPSCs in WT mice are not affected by Slc6a20a-ASO treatment. (n = 13 neurons from 3 mice for WT-saline, 14 (2) for WT-ASO, 14 (3) for ΔC-saline, and 12 (3) for ΔC-ASO, ***P < 0.001, ns, not significant, two-way ANOVA with Bonferroni's test). The error bars represent SEM. (G) PtenΔC/ΔC mice (2-4 months) treated with Slc6a20a-ASO display normal levels of climbing in the Laboras test. n = 6 mice for WT-saline, 7 for WT-ASO, 7 for ΔC-saline, and 8 for ΔC-ASO, *P < 0.05, **P <0.01, ns, not significant, two-way ANOVA with Bonferroni's test. The error bars represent SEM. (H) Slc6a20a-ASO treatment has no effect on the self-grooming of PtenΔC/ΔC mice (2-4 months) in the Laboras test. (n = 6 mice for WT-saline, 7 for WT-ASO, 7 for ΔC-saline, and 8 for ΔC-ASO, ns, not significant, two-way ANOVA with Bonferroni's test). The error bars represent SEM.
Figure 6Expression levels of EGOT (A) were evaluated in two cohorts of HCV-negative (n=13/ n= 10) and HCV-positive (n=15/ n= 19) patients by qRT-PCR. Measurements obtained with patients with HCC are indicated with white squares. Statistical significance was calculated using a two-tailed non-parametric Mann-Whitney U-test. Expression levels of genome equivalents of HCV (GE)/μg of total RNA and TNFα mRNA (B) were evaluated in two cohorts of HCV-negative (n=13/ n= 10) and HCV-positive (n=15/ n= 19) patients by qRT-PCR. Measurements obtained with patients with HCC are indicated with white squares. Statistical significance was calculated using a two-tailed non-parametric Mann-Whitney U-test. Correlation between EGOT and HCV RNA or TNFα mRNA was calculated with Spearman's correlation coefficient. Asterisks mark significant differences (ns, non-significant; * denotes p<0.05, ** p<0.01).
Figure 5(A) Ribbon representation of the complex between the ARM domain of Smc5 (yellow and orange) and Nse2 (red) (PDB 3HTK) (Duan et al, 2009), showing positions of mutated lysine residues covered with black asterisks (3KE: K743E/K745E/K764E; 4KE: K337E/K344E/K354E/K355E; and 7KE: K337E/K344E/K354E/K355E/K743E/K745E/K764E)  (B) Growth test analysis of wild-type, nse2-CH and the indicated smc5-KE mutants; 10-fold serial dilutions of the liquid cultures were spotted in YPD and pictures taken after 48 hours  (C) Same as in (B) but using the nse2-CH, smc5-3KE, smc5-K743,745E, smc5-K743,745R, smc5-7KE and smc5-7KR mutants
Pol II transcription is essential for nucleolar structure and functionConfocal laser scanning fluorescence microscopy (CLSM) images showing DNA staining (blue in the merged images), rDNA FISH (green) and NCL immunofluorescence (red) in untreated HeLa cells or in cells treated with α‐amanitin (50 μg/ml), AMD (50 ng/ml) or the Pol III inhibitor ML‐60218 (200 μM) for 5 h.Figure 1Confocal laser scanning fluorescence microscopy (CLSM) images showing DNA staining (blue in the merged images), rDNA FISH (green) and NCL immunofluorescence (red) in untreated HeLa cells or in cells treated with α‐amanitin (50 μg/ml), AMD (50 ng/ml) or the Pol III inhibitor ML‐60218 (200 μM) for 5 h. CLSM images of propidium iodide‐stained RNA after microinjection of buffer or nucleolar RNA into α‐amanitin‐treated HeLa cells. Nucleoli were visualized by immunofluorescence of nucleophosmin (NPM). The graph represents the average number of nucleolar domains (± 95% CI) based on the analysis of 90, 87, 80 and 86 cells, respectively. **P‐value 0.01, t‐test.
a) EGF enhances nuclear LC3-II content in hepatocytes.f3(a) EGF enhances nuclear LC3-II content in hepatocytes. Immunofluorescence (IF) depicting nuclear LC3-II in RALA hepatocytes in presence or absence of EGF (10 min). Native/inverted images are shown. Scale bar, 5 μm. Bars represent mean±s.e.m. ***P0.001 compared with control (Con); Student's t-test, 50 cells from two experiments. (b) EGF enhances nuclear P-ERK/LC3-II colocalization. IF depicting P-ERK (green)/LC3-II (red) colocalization in untreated (Con) or EGF-treated NIH/3T3 cells. Native images (top)/images with colocalization in white pixels (bottom) are shown. Scale bar, 5 μm. Bars represent mean±s.e.m. ***P0.001 compared with Con; Student's t-test, 50 cells from two experiments. (c) Adipogenic differentiation increases nuclear LC3-II. Images depict nuclear LC3-II in 3T3-L1 preadipocytes in maintenance or differentiation medium (2 h). Scale bar, 5 μm. Bars represent mean±s.e.m. **P0.01 compared with Con; Student's t-test, 50 cells from two experiments. (d) Nuclear P-ERK/LC3-II colocalization in serum-fed cells. IF showing P-ERK (green)/LC3 (red) colocalization in 2 h serum-fed NIH/3T3 cells. Native images (top)/images with colocalization in white pixels (bottom) are shown. Scale bar, 5 μm. (e) LC3 interacts with ERK in vivo. Immunoblots showing co-immunoprecipitation of LC3 with ERK, MEK and bRAF in homogenate (Hom) (e, top), and of LC3 with P- and total ERK in nuclear fractions from mouse livers (e, bottom). (f) Blocking nuclear transport decreases EGF-induced increase in nuclear LC3-II. LC3 IF (red) in EGF-treated NIH/3T3 cells pre-exposed (30 min) or not to WGA. Bars represent mean±s.e.m. ***P0.001 compared to with; Student's t-test, 60 cells from n=3. Scale bar, 10 μm. (g) Blocking nuclear transport decreases nuclear ERK content. ERK IF (green) in EGF-treated NIH/3T3 cells pre-exposed (30 min) or not to WGA. Bars represent mean±s.e.m. ***P0.001 compared with Con; Student's t-test. (h) Blocking nuclear transport does not modify P-ERK/LC3-II colocalization. IF depicting nuclear P-ERK (green)/LC3 (red) colocalization in EGF-treated NIH/3T3 cells pre-exposed or not to WGA. For (g) and (h): Scale bar, 10 μm, bars are mean±s.e.m. 50 cells from n=2. Nuclei are blue (DAPI). Arrows indicate LC3 puncta, ERK or colocalization.
Figure 2A, B Immunohistochemistry analysis of CD8a, CD4 (A), PCNA, and Foxp3 (B) in tumors from WT and Tet2-/- (KO) mice subcutaneously injected with Hepa1-6 hepatoma cells. Corresponding bar charts display positive staining, quantified using Image Pro Plus 6.0 software (n=3). Pictures were captured at 400X magnification. Scale bar = 50 μm. C Schematic illustration of the syngeneic tumor model in which Hepa1-6 cells were injected subcutaneously with or without anti-PD-1 treatment. D Tumor growth curves in WT and KO mice treated with PBS or with anti-PD-1 Ab (n =3). E Representatives images of day-19 tumors from WT and KO from panel D. F Tumor weights from WT and KO mice at day 19. G Flow cytometry analysis of splenic CD8+ T cells in WT and KO mice with or without anti-PD-1 treatment after tumor challenge. H-K GSEA analysis showing the significant down-regulation of genes in GO biological processes: chemokine signaling pathway (H), T cell receptor signaling pathway (I), innate immune response (J) and cytokine receptor interaction (K). The x-axis represents that the mouse genes are ranked from the most up-regulated (left end) to the most down-regulated (right end) in comparison of syngeneic tumor from Hepa1-6 tumor-bearing KO to WT mice (n=4). The y-axis is an enrichment score (ES), which goes up (>0) and down (<0) representing the enrichment of up-regulated genes and down-regulated genes, respectively. NES is the normalized enrichment score. p-value was calculated by permutation.
Figure 2Mice (n = 4/group, data are representative of 2 experiments) underwent a sham (with or without starvation) or CLP operation and liver was isolated on several timepoints post-surgery for RNA preparation and qPCR. Ppara mRNA expression is shown as relative expression, normalized to housekeeping genes Hprt and Rpl. P-values were calculated using 1-way ANOVA analysis. PPARA protein levels were analyzed in livers 24h after CLP by Western Blot using actin as a loading control. Quantification of PPARA western blot. P-value was calculated via 2-way Student's t-test (n = 4/group). Pearson correlation between log fold change (LFC) Ppara expression levels and body temperature 24h post-sepsis (n= 38, r = 0.6875, combined data of 4 independent experiments). Liver Hmgcs2 mRNA expression at different timepoints post-sepsis, expression is shown as relative expression, normalized to housekeeping genes Hprt and Rpl. P-values were calculated using 1-way ANOVA analysis (n = 4/group, data are representative of 2 experiments). Oxygen consumption rates (OCR) of liver tissue explants 24h post sham or CLP. Liver tissue was isolated 24h post-surgery and OCR was measured via Seahorse with BSA or palmitic acid (PA) as a substrate for 42 min. n = 4/group. Visualization of T42(min) OCR, p-values were calculated using 2-way ANOVA analysis.
Figure 2A. Representative FACS profiles of HSPC cell cycle analysis using combinatorial staining for Ki67 and Hoechst 33342. Bar charts depict the average percentage of cells in each phase of the cell cycle for each LSK subset from WT (n=6) and PKCδ KO (n=7) mice. Data compiled from two independent experiments. Data information: All data are presented as mean±SEM, *p<0.05 and **p<0.001, with significance determined by two-tailed Student's unpaired t-test analysis. B. FACS profiles of indicated BM subsets from WT and PKCδ KO mice 20hr after BrdU injection. Data information: All data are presented as mean±SEM, *p<0.05 and **p<0.001, with significance determined by two-tailed Student's unpaired t-test analysis. C. Average percentages of cells in each phase of the cell cycle phases for each of the indicated HSPC subsets from WT and PKCδ KO mice. Data are pooled from two independent experiments (totaling n=6-7 mice per genotype). Data information: All data are presented as mean±SEM, *p<0.05 and **p<0.001, with significance determined by two-tailed Student's unpaired t-test analysis. D. Representative FACS plots and summary of FACS data analyzing the frequency of apoptotic HSPC cells using co-staining for AnnexinV and 7-AAD (WT and PKCδ−/− (n=7 per genotype). Data information: All data are presented as mean±SEM, *p<0.05 and **p<0.001, with significance determined by two-tailed Student's unpaired t-test analysis.
Figure 4(A) Analysis of replicated DNA tracks length by single-molecule DNA combing in WT, rad52∆, rad51∆, mus81∆ and pol32∆ cells exposed to CPT. Exponentially growing cells were treated with DMSO or 50 µM CPT for 2h and then pulse-labeled with 50 µM EdU for 20min. DNA fibers were combed on silanized coverslips and EdU-labeled DNA was detected by Click chemistry. Graph depicts the distribution of EdU tracks length in kb. Box and whiskers indicate 25-75 and 10-90 percentiles, respectively. Median EdU tracks length is indicated in kb (values from two biological replicates were pooled). Asterisks indicate the P-value of the Mann-Whitney unpaired t test, **: p=0.0015. The percentage of EdU track length decrease between the DMSO and CPT conditions is indicated between parentheses for each strain. Representative images of DNA fibers are shown. Red and white: EdU, green: DNA. Schematic representation of replication intermediates visualized by 2D gels. (C) Analysis of replication intermediates by 2D gel electrophoresis. Replication intermediates were monitored at early origin ARS305 and region C in WT, rad3-102, mus81∆ and rad3-102 mus81∆ cells. Cells were synchronized in G1 with α-factor and collected at the indicated time points after release into S phase. A scheme of the studied chromosomal region is shown (drawn to scale). Relevant probes are indicated by gray bars, and coordinates of ARS and restriction sites are indicated in bp. Two biological replicates have been performed.
Tfcp2l1 deletion and FAO defect are associated with the upregulation of glycolysis, the TCA cycle, and glutamine catabolism.Figure 5A. Clustering of a total of 572 metabolites in WT and Tfcp2l1_KO 2i-ESCs. Data were from 9 biological repeats for each genotype. B. A schematic diagram of glycolysis and the TCA cycle. Most metabolites within these two pathways were detected by metabolomics and had significant changes between naïve WT and Tfcp2l1_KO ESCs. Metabolites in red, significantly upregulated in KO versus WT in 2i-ESCs; metabolites in green, significantly down-regulated; metabolites in black, not significantly changed. C. Relative levels of metabolites in glycolysis and the TCA cycle.n=9 biological repeats; upper whiskers, maximum-the third quartile; lower whiskers, the first quartile-minimum; boxes, the third quartile-the first quartile; the central line indicates the median; p-values were calculated using two-sample t-test. D. Live-cell propidium iodide staining to measure cell death in WT, Tfcp2l1_KO, and Tfcp2l1_KO with Cpt1a overexpression (OE) 2i-ESCs after 5 mM 2-DG treatment for 24 hours. n=3 biological repeats; error bars indicate SEM; p-value were calculated using two-sample t-test. E. A schematic diagram of glutamine metabolism. Most metabolites within this pathway were detected by metabolomics and had significant changes between WT and Tfcp2l1_KO 2i-ESCs. Metabolites in red, significantly upregulated in KO versus WT in 2i-ESCs; metabolites in green, significantly down-regulated; metabolites in black, not significantly changed. F. Relative levels of metabolites in glutamine metabolism. n=9 biological repeats; upper whiskers, maximum-the third quartile; lower whiskers, the first quartile-minimum; boxes, the third quartile-the first quartile; the central line indicates the median; p-values were calculated using two-sample t-test. G. Percentage of cell death of WT, Tfcp2l1_KO, and Tfcp2l1_KO with Cpt1a overexpression (OE) 2i-ESCs under glutamine deprivation. Error bars indicate SEM; n=3 biological repeats; p-values were calculated using two-tail t-test.
Figure 4MitoTracker green staining in iNKT cell subsets ex vivo; Quantification of mean fluorescence intensity (MFI) of MitoTracker green staining in iNKT cell subsets; Confocal images of Tim 23 (Alexa Fluor 488, green) and MitoTracker deep red (Alexa Fluor 647, red) in freshly isolated thymic NKT1 (c1, 2) and NKT2 (c5, 6) cells using Airyscan technology. 3D images reconstructed by Imaris software in NKT1 (c3, 4) and NKT2 cells(c7, 8). Dotted line in panel (5-8) indicates juxtaposition of two NKT2 cell images taken with the same resolution and magnification as NKT1 cells. Mitochondrial volume estimated by Tim 23 staining as in (c), and presented as % of total cell volume; Representative images of electron microscopy in NKT1 and NKT2 cells; (f) individual mitochondria size and (g) cristae perimeters normalized to mitochondria perimeter based on EM in (e).