EMBO/sd-character-level-ner huggingface dataset:
(A) Prioritized compounds proposed to have potential antiviral activities and their involvement in different modules in the viral-host PPI network. 25 compounds/drugs were identified for each of the four modules, resulting in a total of 64 distinct repurposable drugs or investigational compounds, some participating in multiple modules. The entries in the heat map display the ranking, color-coded from red (highest) to blue (lowest). The ranking was based on the proximity of their targets to proteins belonging to the modules.
(F) Cell viability assay of Parental (PAR) and FLIP knockout (CFLAR CRISPR cells) treated with an escalating dose (0-1000ng/mL) of IZ-TRAIL for 72 hours.
D. Schematic representation of pathways involved in the preservation of skeletal muscle mass during prolonged periods of immobilization. SGK1, in addition to Akt, mediates protein degradation via phosphorylation of Foxo3a, with the subsequent inhibition of proteolysis and autophagy and protein synthesis through the activation of mTOR.
A: Cell lysates of the indicated human pancreatic tumor cell lines (S2-007, PaTu8988t, MiaPaCa-2, Panc1) were resolved by SDS-PAGE and analyzed by immunoblotting for p14ARF (α-p14ARF) and PRMT1 (α-PRMT1) protein levels. GAPDH staining served as loading control.
A) SEM analysis of promastigote culture initiated with Δatg5 isolated from a mouse lesion and cultured in nutrient-rich medium. Shown are ovoid and amastigote-like form (left); spindled-shaped form without an external flagellum (centre left panel) and with an external flagellum of varying lengths (centre right and right panels). Scale bar, 10 µm.
(A) IFT54 has three previously undefined and conserved regions. Schematic representation of the primary structure of Chlamydomonas IFT54 is shown on the top. Three conserved regions are shown on the bottom. Abbreviations for the species and protein entries: Cr, Chlamydomonas reinhardtii (Cre11.g467739); Hs, Homo sapiens (NP_056465.2); Mm, Mus musculus (NP_082994.1); Ce, Caenorhabditis (NP_508149.1); Dr, Danio, rerio (ABW96885); Dm, Drosophila melanogaster (NP_650353); Tt, Tetrahymena thermophila (XP_001026831.1).
Growth curves of Trf1Δ/Δ MEFs transduced with eGFP-Trf1 WT or mutant alleles as indicated. Data are representative of n=5 biological replicates
The rate of Hsc70/DnaJB1-mediated dissociation of Hsf1 from HSE-DNA depends on concentration of the nucleotide exchange factor Apg2 (HSPA4) (n = 3, ANOVA, **, p < 0.01; ****, p < 0.0001) (I). Shown are mean ± SD.
A. Correlative plot of changes in protein abundance between control neurons and neurons treated with Centrinone-B (day7/day3). Pearson correlation R=0.5716, p<0.001. Specific, significantly changing growth cone proteins highlighted in red.
(D) The same batch mice as in (B) were given water containing BrdU. The BrdU+ cells of the islets were visualized and quantified (BrdU+ labeling). TUNEL-positive cells in the islets of the mice (B) were visualized and quantified (TUNEL assay). BrdU+ cells per islet area (0.01 mm2) and TUNEL+ cells per islet area (0.05 mm2) are expressed in arbitrary units (AU). The dash circles indicate islet regions and the black arrowheads indicate TUNEL+ cells. Data information: Data from over 3 experiments are presented as the mean ± SD. one-way ANOVA test were used for statistical analysis of differences between groups, and P (*) < 0.05; P (**) < 0.01 and P (***) < 0.001 are considered statistically significant.
A-C. Fluorescent images of human iPSC derived microglia cells, labelled with 493/503 BODIPY (green) and FM-dye (red) to mark lipids and membranes respectively. iPSC derived microglia cells were obtained from 3 different donors, and treated with either DMSO, GW, TAPI-1 or GI. Scale bars: 10μm
K: AS or STLC-synchronised (M) HeLa, A549 and HaCaT cells were subjected to IP with either IgG- or anti-FAM83D-coupled sepharose beads. Input and IP samples were analysed by IB with the indicated antibodies. Data information: All blots are representative of at least 3 independent experiments.
(C) Immunoblot analyses with anti-phospho-S6K and anti-phospho-S6 antibodies show that NO donors activated mTORC1 in Ikkβ+/+ MEFs, but not in Ikkβ−/− MEFs.
(e) qrtPCR of MCUR1 mRNA from HeLa cell clones and of rescued MCUR1 mRNA levels in shHe2 clone cells (n = 3; mean ± s.e.m.). The same lentiviral shRNAs were used to generate shHK4 and shHe1 and shHK5 and shHe2, respectively.
F Input of TDP-43-MBP-His6 variants used in the SDD-AGE assay, detected by Western blot (anti-TDP-43 N-term).
H. WB of cells treated as in (G). Densitometric quantification of the blot is plotted in the top panel (data are means of at least 3 experiments ± SD).
Comparison of the level of 24-h pS6 inhibition for 8 cell lines treated with SB590885 versus PLX4720.
(F) Western blotting of Non-Targeting siRNA (NTrg), or siOPCML (si 6, si 7) transfected FT190 cells stimulated with Gas6 over a 24 hour time course. GAPDH was used as loading control. Data in (A, B, D, F) are representative blots of at least three experiments. RPPA analysis was performed in triplicate
B.) Genotyping PCR confirming the insertion of the PfDPCK-mCherry construct using attP/attB integration. PCR reactions demonstrate integration at the Δ5' and Δ3' integration sites and lack of parental parasites (P) as compared to the parental control (P230p-attB).
F 8-week neurosphere size (diameter) remained unchanged by treatment with either drug (one-way ANOVA, F6,344 = 0.52, P = 0.79; N = 44 Q83X neurospheres and 65 WT83 neurospheres).
(Left) Detection of XBP1 mRNA splicing in shCtrl and shFAM20C HepG2 cells (D) treated with or without 2 μg/ml Tm for 8 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).
Basal respiration of preadipocytes and adipocytes after 4 days of in vitro differentiation was determined by calculating the area under the curve (AUC) during measurements of oxygen consumption rate (OCR). The whole experiment was repeated three times. Data are shown as mean ± SEM of 3-7 cell lines per group.
Design of Bak variants with reduced pore-forming activity. Mutated amino acids are highlighted in red. (a) Bak∆TM_1 (green frame): R156Q stabilizes the interaction between the latch domain (α6-8) and helix 1 (gold). (
(B-E) G1-arrested cell cultures (αf) were released in YEPD supplemented with CPT (50 μM). Sample collected at the indicated time points were subjected to western blot analysis with anti-Rad53 antibodie
C Nfib overexpression in the HR1 parental cells enhances experimental metastases. Kaplan-Meier showing metastatic incidence of animals inoculated i.v. with HR1 gCtrl (n = 11) or HR1 g4Nfib (n = 11) cells, two-tailed log-rank test.
E Pexophagy assay was monitored by the degradation of Pot1‐GFP and analyzed for GFP cleavage by immunoblotting.
(B) High-magnification view of single mitotic cell stained for p-MLC (purple) and E-cadherin (green), with metaphase plate chromosomes stained by DAPI (blue). Scale bar ~1µm. n>10 independent biological replicates. (C) High-magnification view of single UAS.Rok-RNAi expressing mitotic cell stained for p-MLC (purple) and E-cadherin (green), with metaphase plate chromosomes stained by DAPI (blue). Note loss of cortical p-MLC staining (purple). Scale bar ~1µm. n>10 independent biological replicates.
PTPA is an essential factor for PP2A mediated dephosphorylation of Ago2. Effect of PTPA depletion on Ago2 phosphorylation level in RAW 264.7 cells (I). Phosphorylated Ago2 level was measured by western blot in HA-immunoprecipitated materials isolated from either siCon or siPTPA transfected cells expressing FH-Ago2 upon 24 hrs of LPS treatment using a phosphotyrosine specific 4G10 antibody (I, left panel). The PTPA was detected with anti PTPA antibody, β-Actin was used as loading control (I, right panel).
5C) nt and PINK1 knockdown (kd) SH-SY5Y cells were either kept in RPMI medium with 5% FCS for 48 h or starved with HBSS for the indicated time points. For quantification the cleaved PARP 89 kDa product was normalized to the full length 113 kDa PARP and the resulting value normalized to GAPDH. Cells with PINK1 knockdown demonstrated increased PARP cleavage that was significant after 24 h starvation; n = 4; 24 h: p<0.005.
A Cell cycle analysis by flow cytometry (EdU vs. TO-PRO-3) in complete medium (ENRAD) or in the absence of A83-01 (24 hours).
B Representative images and quantification of vacuolar morphology of late meristematic cells of Col-0 and 35S::LRR4-cit. PI (green) and MDY-64 (yellow) staining depict cell wall and vacuolar membrane, respectively. Col-0 (n=36) and 35S::LRR4-cit (n=32-36) seedlings were treated with DMSO or 50 µM EGCG for 22 h on solid medium. Kruskal Wallis test followed by Dunn´s multiple comparison (b: p < 0.05, c: p < 0.001). Data information: 5 µm (B). Boxplots: Boxplots: Box limits represent 25th and 75th percentile, horizontal line represents median. Whiskers display min. to max. values.
typical spontaneous neuron activity recorded in GFP controls (B, top panel) and Kir2.1 neurons (B, bottom); and comparison in resting membrane potentials between the two groups (C, **p<0.0001, unpaired Student's t test).
G Percentage of hepatic glucose output (HGO) suppression during hyperinsulinemic euglycemic clamps in weight-matched WT (n = 4) and NOD2−/− (n = 3) mice fed a HFD for 16 weeks, *P = 0.005.
A-C Co-localization of Nurr1 and Foxa2 proteins in mDA neurons of the adult mousemidbrain. Representative confocal sections of the ventral midbrain (A) stained with antibodies specific for TH, Nurr1, and Foxa2. The midbrains of mice at 10 weeks were cryosectioned, and stained images were taken using a confocal microscope with z-stacks through the section thickness (12 μm). Shown in (B) are individual and merged images of TH, Nurr1, and Foxa2 staining of the boxed area in (A) at higher magnification. Representative images of a single nucleus from a TH+mDA neuron of an adult midbrain section (C) co-stained with Nurr1 (red) and Foxa2 (green). Co-localization of Nurr1 and Foxa2 in the merged images was assessed by Pearson's correlation and overlap coefficient values (n = 4, right/low quadrant in C).
(C) Representative immunoblots of the indicated proteins from whole-cell lysates of MCF7 cells treated with ULK1 or SQSTM1 siRNAs for 54 h before the exposure to fresh medium (0) or amino acid starvation (−AA) for 12 h. Ctr, control.
B LNCaP cells were cultured in RPMI 1640 medium containing 10% CT-FBS and treated with or without 1 nM R1881 for 24 h before being transfected with the indicated siRNAs. The cells were then cultured for the indicated times, and cell growth was measured by Cell Counting Kit-8. n = 3, *P < 0.0001. Error bars indicate SD.
(A) Expression level of LSD1 (KDM1A) in gastric cancer and non-cancerous tissues from UALCAN datasets (STAD, stomach adenocarcinoma; central band, boxes, and whiskers of the boxplot represent the median, first quartile, third quartile, minimum, and maximum values, respectively).
C. Club cell depletion/recovery after naphthalene treatment. Microscopic imaging of epifluorescence in lung sections from control and injured BASC viewer animals isolated 3, 7 and 21 days post naphthalene (dpn). Blue: DAPI. Scale bar: 200 µm.
Bar graph representing quantification of stiffness measured by atomic force microscopy (Young modulus) of ECM area generated by H1299control or H1299RASSAF1A cells in vitro. Data information: All statistical analyses were performed using Student's t-test (2-tailed) of n=3 for in vitro experiments and error bars represent the mean ± S.E.M.
The mRNA expression of SHH effector genes (Gli1/2 and Glis1-3) on laser microdissection captured samples were evaluated by real-time RT-PCR analysis. The results are in arbitrary values after normalization for GapDH. Each sample was isolated from distinct mice (n = 3).
Kymograph of the lamellar activity of WASP-deficient cells that lack actin foci.
ROS measurement in mESCs treated with INK128 or transduced with Rptor shRNAs in 2iL (mean values ± SD). n = 3 biological replicates.
b, Samples from control animals (+/w; +/drpr∆5), n = 12, and drpr null mutants (w; drpr∆5/drpr∆5), n = 47, analysed by histology for the presence of salivary gland material (red circles) 24 h after puparium formation. c, Quantification of data from b and d. d, Samples from control animals (+/w; +/UAS-drprIR), n = 11, and those with salivary gland-specific knockdown of drpr (fkh-Gal4/w; UAS-drprIR/+), n = 19, analysed by histology for the presence of salivary gland material (red circles) 24 h after puparium formation.
(A) Aldh1l1 mRNA expression in various muscles in MCK-KO mice that were transfected with gRNA DNAs against Aldh1l1 or control. (n = 4 for Soleus, n = 3 GA gCont and n = 4 GA gAldh1l1, n = 4 EDL gCont and n = 3 EDL gAldh1l1 , means ± SEM, * p < 0.05, two-tailed student's t-test).
C) Ultrastructural alterations shown by electron microscopy in wild-type and Tubb1-/- thyroid tissues. In Tubb1-/- tissues, note the disorganisation of secretion vesicles (white asterisks) and rods of identical density to secretion vesicles (white arrow). The ER is considerably dilated in Tubb1-/- thyrocytes. Representative views. Scale bars at the bottom left for each view. Co: colloi
C) Expression levels of all M. florum reference proteins quantified by two-dimensional liquid chromatography-tandem mass spectrometry (2D LC-MS/MS). Abundance was estimated according to the normalized spectral abundance factor (NSAF) calculated for each protein. A NSAF value of 0 was assigned to undetected proteins. The corresponding number of protein molecules per cell (derived from the biomass data) are indicated. Proteins were sorted from least to most abundant. The selected genes of importance presented in panel A are also highlighted.
Body weights of mice that had consumed a chow or HFD diet for 22 weeks; n=3. Mean ± SD. Mice are grouped to reflect their randomization to vehicle or SH-BC-893 groups, weight measured prior to treatment.
(G). Intracellular calcium ion [Ca2+] changes in adrenal medulla cell cultured with vehicle + NC, vehicle + siOXGR1, AKG (100 μM) + NC or AKG + siOXGR1 (n = 30 per group).
Effect of Ctcflos KD on brite adipocyte respiratory capacity. Time course of oxygen consumption rates in primary brite adipocytes 72 hours after treatment (day 1 diff), comparing Ctcflos tr1 KD (ASO 1) and its control in UCP1 wildtype (WT) and UCP1 knockout (KO) cells, measured by microplate-based respirometry (Seahorse XF96 Analyzer). Oxygen consumption is recorded under basal conditions and in response to successive injection of oligomycin (5µM), isoproterenol (1.5µM), FCCP (1µM) and antimycin A (5µM) to determine basal leak, UCP1 dependent uncoupled, maximal and non-mitochondrial respiration, respectively. Data are expressed after deduction of non-mitochondrial respiration. Mean value ± SD, n=7 (technical replicates). Quantification of isoproterenol-stimulated UCP1-mediated uncoupled respiration, expressed as fold of basal leak respiration. Mean and single values, (K n=4 (biological replicates), paired t test *p<0.05, (L) n=5 (biological replicates), paired t test *p<0.05, (N, O) n=7 (technical replicates), unpaired t test, n.s. p>0.05, ****p<0.0001.
Quantification of tumor growth relative to initial tumor size. Representative CT images are shown to the right. The white arrowhead indicates a tumor within a highly inflammatory region.
Hypothetical model for the regulation of CMA by PPCA. Under normal nutritional conditions (FED, left), binding of PPCA to the lysosomal membrane might trigger cleavage of lamp2a by an unidentified metalloprotease (at the transmembrane region) (1) and by PPCA (at the intersection between the transmembrane and luminal regions) (see inset). That cleavage releases a truncated lamp2a into the matrix (2), where it is completely degraded by the lysosomal proteases (3). During starvation (right), PPCA dissociates from the lysosomal membrane (1) so that lamp2a is not longer degraded and remains in the membrane, accessible for substrate binding (2) and uptake into the lysosomes (3).
(C) Structural comparison of the N‐terminal tail-LC3 interaction with the p62-LC3 interaction. The structure of LC3 complexed with a p62 peptide is superimposed on that complexed with the N‐terminal tail peptide. As the structure of LC3 is almost identical to each other, only that bound to the N‐terminal tail peptide of Hs is shown.
(C, E and G) WT PEMs expressing GFP-FAK were incubated with either ΔinvG Salmonella (C), LPS-coated beads (E) or E. coli (G) for a total of 5 hours before analysis by immunofluorescence. Cells were co-stained with antibodies recognizing LAMP1 (red). Dapi was used to visualize nuclei and bacteria (blue). Bars represent 10 µm. Arrowheads indicate bacteria or beads in enlarged panel where bars represent 2 µm. (D, F and H) The percent of LAMP1-positive (gray bars) and LAMP1+GFP+ (black bars) ΔinvG Salmonella (D), LPS-coated beads (F) and E. coli (H) was quantified. At least 100 bacteria were counted per condition; N = 3.
(G) Viability of six PTEN-null VS five PTEN-WT TNBC cell lines - not carrying other known mutations in PIK3CA, PIK3CB or PIK3R1 genes - treated with PI3Kβi (AZD8186 90 nM), EGFRi (gefitinib 3 μM) alone or in combination for 6 days. Mean of 3 independent experiments ± SD. Statistical significance of two-tailed unpaired student t-test in PTEN-null PI3Kbi versus PI3Kbi+EGFRi **P=0.0059, PTEN-null EGFRi versus PI3Kbi+EGFRi **P=0.0047, PTEN-null PI3Kbi+EGFRi versus PTEN-WT PI3Kbi+EGFRi *P=0.0459, PTEN-WT PI3Kbi versus PI3Kbi+EGFRi *P=0.0108, PTEN-WT EGFRi versus PI3Kbi+EGFRi n.s. P=0.1926. PTEN-null cell lines used in the experiments were: MDA-MB-468, HCC70, HCC1937, HCC38, HCC1395 and BT-549; PTEN-WT cell lines were: MDA-MB-157, MDA-MB-231, HCC1187, HCC1428 and HCC1806.
A) Immunofluorescent staining of fetal lung bud tip progenitor organoids grown in expansion medium co-expressing stem cell markers Sox2 (green) and Sox9 (red). Phalloidin (white) was used to stain actin. Data information: Nuclei are stained with Hoechst
(A) Control, CITK or ASPM-depleted HeLa cells immunostained for α-tubulin (red) and DNA (blue). Maximum intensity projections of confocal z-stacks are shown.(B) Quantification of astral MT number and maximal length in HeLa cells transfected with CTRL, CITK or ASPM siRNA (n > 130 cells in 3 independent experiments).
(a) Immunoblot analysis of Irgm1 in lysates of flow cytometry-sorted naive wild-type CD4+ lymphocytes activated for 48 h with immobilized agonistic mAb to CD3 (10 μg/ml) alone or with mAb to CD28 (2 μg/ml) in the presence or absence of IFN-γ-neutralizing mAb. Actin, loading control.
(B) A schematic illustration of the polysome profiling analysis workflow: cytoplasmic lysate was layered on top of a linear 10-40% sucrose gradient, ultracentrifuged (36,000 rpm, 2¼ hours, 40C) and fractionated using the Foxy Jr Fraction Collector with constant monitoring of absorbance at 260 (A260) nm by an ISCO UA-6 Absorbance Detector. Fractions (one fraction per minute: 800 µL per tube) corresponding to polysomal mRNAs that were bound by four or more ribosomes were pooled and analyzed by RNA-seq followed by data analysis using anota2seq or limma.
(G) HIV-1-WT-luc infection is increased in CHME3 cells stably expressing Flag-CLIP170, but not control Flag or Flag-CLIP170ΔCAPgly. Molecular weight markers (in kDa) are shown to the right of WBs.
Schematic workflow for the ImageJ plugin for analysis of peripheral mitochondria.
A FERM superposition of autoinhibited FAK (Lietha et al., 2007) (yellow, PDB: 2J0J) with a membrane bound FAK monomer as observed in the cryo-EM structure (green) shown from the membrane proximal view. The KAKTLRK membrane binding site on the FERM domain is colored red and membrane interacting residues K621 and K627 in the kinase domain are in cyan with side chains in space fill representation.
MICU2_WT (A), MICU2_K172A (B) were pulled-down by GST-MICU1 both in the absence and presence of 2 mM Ca2+. MICU2_EF1mut was not pulled-down by GST-MICU1 in the presence of 2 mM Ca2+ (C), while MICU2_EF2mut was pulled-down by GST-MICU1 both in the absence and presence of 2 mM Ca2+ (D). MICU2_R352A was not pulled-down by GST-MICU1 in the absence of 2 mM Ca2+ (E), while MICU2_E329A was pulled-down by GST-MICU1 both in the absence and presence of 2 mM Ca2+ (F). MICU2_D185A was partially pulled-down by GST-MICU1 in the presence of Ca2+, while they showed a strong interaction in the absence of 2 mM Ca2+. MICU2_E196K was not pulled-down by GST-MICU1 in the presence of 2 mM Ca2+, while a strong interaction was observed in the absence of 2 mM Ca2+.
A Expression of the somatostatin receptor subtype 1 (sst1) analysed by RT-qPCR in the human pancreatic endocrine cell line BON and in CAFs isolated from 11 different patients (mean ± SD).
(F) The 100 soft NSP or stiff SP- 4T1, MCF-7, B16 or MP-1 cells were injected into the mammary fat pads (4T1and MCF-7) or subcutaneous tissue (B16 and MP-1) of NSG mice. The tumor formation in the lungs was recorded.
(C) Binding of acetyl‐Histone H3 to the p62 promoter increased under starvation conditions, suggesting p62 gene derepression (data are from one representative experiment of at least three independent experiments performed in triplicate).
FcγR-mediated phagocytosis was monitored using beads conjugated to Alexa Fluor 488 (in green). External beads were differentially labelled with anti-IgG (in red) and distinguished by their dual labelling (in yellow). Cytochalasin D (10 μM, Cyt D) prevented bead internalization.
D) Overall DNA, tRNA, rRNA, mRNA, and protein proportions in terms of intracellular abundances in M. florum.
Schematic showing the OptoCAR replacing the antigen receptor (dotted region) as the primary driver of intracellular T cell signaling. Illumination of the cells leads to the dissociation of the intracellular signaling domain of the OptoCAR complex and the loss of signal transduction. The network nodes investigated in this study are explicitly depicted within the boxes.
retention were determined towards coatings with collagen I (COL), fibronectin (FN) or TNC in the presence of CXCL10 and, upon AMD3100 (AMD, 5 µg/mL) 3 independent experiments in duplicates, Mann-Whitney test, ns > 0.05; * p <0.05; **p < 0.01; ***p < 0.005. Mean ± SEM.
E RIPK3-gyrase were inducibly expressed in Ripk3-/- MDFs by doxycycline (dox) for 5 hrs, and cells were then treated ± combination of TSI, or coumermycin (coum) for 3 hrs.
(A) Immunoblot analysis for lamp2a, all lamp2s, lamp1, transferrin receptor (TFR) or cathepsin D (cath D) of liver homogenates (100 μg of protein) from wild‐type (WT), PPCA(−/−) and β‐galactosidase(−/−) (GM) mice. Right: densitometric quantification of three immunoblots (means + SE) similar to the ones shown here. Differences from the control value were significant to P 0.001 (**) and P 0.05 (*).
(D) The experiment as shown in (C) was repeated three times. Each dot represents the slope of the Cell Index of the first 30 hours of one technical replicate (one-way ANOVA, Bonferroni"s multiple comparison test, vec vs. WT p>0,9999, S90A vs S86A p=0,1276, ****p < 0,0001;; n.s. not significant, p > 0,05)
Overexpression of mouse PD-L1 in Vgll4 knockdown LLC cells restored the tumor growth in C57BL/6 mice. Tumor weights of shVgll4 or shVgll4-lenti-mPD-L1 LLC cells were determined 21 days after tumor cell transplantation into C57BL/6 mice (left panel). Expression of mPD-L1 was shown in the right panel by immunoblot analysis with anti-mPD-L1 antibody. n=10 tumors for each group
(B) A431 and HT29 cells expressing endogenous mutant R273Hp53 were treated with control morpholinos (Ctl-2 or Ctl-1) or antisense morpholino oligo targeting Δ160p53's translation initiation site (MO) before lysis and WB. wtp53-expressing A549 cells were used as reference for endogenous wtp53 expression levels. Δ160 lane was used as a marker lane showing Δ160p53 as transiently expressed in p53-null H1299 cells.
E) Representative TEM images of quadriceps muscle from Mfn2KO young mice, control old mice and Mfn2KO old mice showing the presence of autophagosomes and mitophagosomes (n=3 mice per group) (Scale bar: 500 nm).