EMBO/sd-character-level-ner huggingface dataset:
Figure 1A) Ten-fold serial dilutions from overnight cultures of wild-type and cdc14-1 cells dropped and grown on solid rich media or media containing MMS at 25, 28, 30 or 33ºC. Note that cdc14-1 cells exhibit growth sensitivity to MMS at 28ºC and 30ºC compared to wild-type cells. B) Ten-fold serial dilution from mid-log phase cultures of wild-type and cdc14-1 cells grown on solid rich media or media containing mock DMSO (as non-treated control), 4NQO, HU, phleomycin and benomyl at 30ºC. Note that cdc14-1 cells present a market sensitivity to all DNA damaged agents tested. C) Left panel: Schematic representation showing relevant genomic structure of the strain used to assess intra-chromosomal repair. The location of a MAT specific probe and the restriction endonuclease cleavage sites used for Southern blot analysis to detect repair product formation are indicated. Arrow depicts the localization of the double-strand break. Right panel: Physical analysis of intra-chromosomal repair in wild-type and cdc14-1 cultures at the semipermisive temperature. After DSB formation by the expression of the HO, glucose was added to repress it, thus allowing repair with HM donor sequences. Genomic DNA was digested with StyI, separated on agarose gel and blotted. Blots were hybridized with a probe corresponding to the MATa-distal sequence. A second probe for the actin gene was used to control the amount of genomic DNA loaded at each time-point. Immunoblot analysis of Rad53 during mating type switching experiments is shown. Coomassie blue staining is depicted as loading control. Graphs show quantification of gene conversion (GC) leading to the re-establishment of MATa or switching to MAT and DSB formation. The data was normalized with the actin loading control. Graphs show the mean ± S.D. from three independent experiments. Replicates were averaged and statistical significance of differences assessed by a 2-tailed unpaired Student t test.
Effect of mistargeting Vps41 on the AP-3 pathway.Figure 4(A) GNS was localized by fluorescence microscopy in the indicated strains grown in medium containing glucose or galactose Images were inverted to visualize possible defects. First column shows DIC image of cells. Scale bar, 5 µm. (B) Quantification of the AP-3 defect from (A). Linear intensity plots were laid over cells grown in medium containing glucose (D) or galactose (G), the AP-3 defect was calculated by dividing GFP-intensities on the vacuolar membrane by the sum of the intensity of vacuolar, and plasma membrane signal (n ≥ 15 cells). Bars show the mean vacuolar signal over total signal ± standard deviation. (C) Effect of different truncations and deletions on AP-3 targeting to mitochondria. Indicated strains were grown at 30°C in YPG and kept in logarithmic phase. Localization of Apl5 or Apl6 and Vps41 was analysed by fluorescence microscopy. First column shows DIC image of cells. Scale bar, 5 µm. Scale bar in inset, 2 µm. (D) Quantification of (C). (-) Control corresponds to Vps41(ΔPEST)-GFP-Fis1 Apl6-mCherry (CUY12558) and (+) corresponds to Vps41(S-D)-GFP-Fis1 Apl6-mCherry (CUY12560). Apl5- /Apl6-dots co-localizing with GFP signal were counted and plotted in percent of the total number of Apl5- /Apl6-dots (n ≥ 63). Bars show the mean percentage of co-localization ± standard deviation.
Figure 4A BM-derived eosinophil from Dusp5+/+ mice were treated with IL-33 (50 ng/ml). Left panel: Total RNA was harvested and Dusp5 gene expression was assayed by Taqman Realtime PCR. Data are represented as relative gene expression using the 2-delta Ct method normalized to Gapdh. Right panel: 250 µg cell lysate was loaded per lane for immunoblotting with anti-DUSP5 mAb (top) and anti-ACTIN antibody (bottom). B Decreased apoptosis of Dusp5-/- BM-derived eosinophils stimulated with IL-33. Representative FACS plots of Dusp5+/+ and Dusp5-/- BM-derived eosinophils treated with low dose (0.5 ng/ml) IL-33 for 16 hours (left). Apoptosis was assessed by staining for AnnexinV and 7AAD. Percentage of live (AnnexinV- 7AAD-), apoptotic (AnnexinV+ 7AAD-) and necrotic (AnnexinV+ 7AAD+) cells are quantitated on the right. C Decreased mitochondrial membrane depolarization of Dusp5-/- BM-derived eosinophils when stimulated with IL-33. Dusp5+/+ and Dusp5-/ -BM-derived eosinophils were labeled with the mitochondria-permeant dye JC-1 according to manufacturer's recommendations and treated with IL-33 (0.15 ng/ml) for 16 hours. Mitochondria depolarization was assessed by a decrease in the red (~590 nm) to green (529 nm) fluorescence ratio (left). Mitochondria depolarization of Dusp5+/+ and Dusp5-/ -BM-derived eosinophils was quantitated using a range of IL-33 concentrations (right). D Dusp5+/+ (open circles) and Dusp5-/- (grey squares) BM-derived eosinophils were incubated with IL-5 (10 ng) or IL-33 (10 ng) for 7 days, and remaining live eosinophils quantitated. E Dusp5+/+Rag2-/- (open circles) or Dusp5-/-Rag2-/- (grey squares) mice were injected intraperitoneally daily with IL-33 (500 ng) for 6 days and eosinophils quantitated on day 7 following IL-33 administration.
Egg monoubiquitination occurs in the nucleus Ubc2-dependently.Figure 2Immunofluorescence analysis of OSCs using anti-Egg antibodies. Endogenous Egg is shown in red. DAPI (blue) shows the nuclei. Scale bar: 10 μm. Western blotting of fractionated OSC materials. Anti-Egg, anti-β-Tubulin (Tub), and anti-histone H3 antibodies were used. H3 and Tub were detected as markers for nuclear (Nuc) and cytoplasmic (Cyto) fractions, respectively. Whole: the whole OSC lysates. Western blotting of Myc-Egg expressed in OSCs before (siEGFP) and after (siUbc2) Ubc2 depletion. Anti-Myc-antibody was used for western blotting. The ratios of mUb-Egg over non-mUb-Egg band signals were 1.43 (siEGFP) and 0.78 (siUbc2). Immunofluorescence analysis using anti-Flag antibody to identify Flag-Ubc2 (green) expressed in OSCs. DAPI (blue) shows the nuclei. Scale bar: 10 μm. Immunofluorescence analysis of Myc-Egg WT, Myc-SV40-NLS-Egg, and Myc-PKI-NES-Egg expressed in OSCs using anti-Myc antibody. DAPI (blue) shows the nuclei. Scale bar: 10 μm. Western blotting of Myc-Egg WT, Myc-SV40-NLS-Egg, and Myc-PKI-NES-Egg expressed in OSCs. Anti-Myc antibody was used. The ratios of mUb-Egg over non-mUb-Egg band signals were 1.50 (WT), 2.29 (SV40-NLS), and 0.95 (PKI-NES). Rescue assays. Myc-Egg WT, Myc-SV40-NLS-Egg, and Myc-PKI-NES-Egg were expressed in OSCs upon endogenous Egg depletion (siEgg). Western blotting was performed using anti-Egg (left) and anti-Myc (right) antibodies. Stalker2 transposon expression was quantified using RT-qPCR. The act5c gene was used for normalization. siEGFP: siRNA for EGFP was used as a negative control. Error bars represent SD from three independent experiments. *p < 0.05 (unpaired Student's t-test). In vitro HMT assays. Top: silver staining of purified Myc-Egg WT, Myc-Egg K1085R, Myc-SV40-NLS-Egg WT, and Myc-SV40-NLS-Egg K1085R. Middle: CBB staining of histone H3.1. Bottom: 14C autoradiogram. Myc-EGFP was used as a negative control (EGFP: not shown). Rescue assays. Myc-Egg WT, Myc-Egg K1085R, and Myc-SV40-NLS-K1085R were expressed in OSCs upon endogenous Egg depletion (siEgg). Western blotting was performed using anti-Egg (left) and anti-Myc (right) antibodies. RT-qPCR quantified the expression level of the Stalker2 transposon. The act5c gene was used for normalization. siEGFP: siRNA for EGFP was used as a negative control. Error bars represent SD from three independent experiments. *p < 0.05 (unpaired Student's t-test).
Figure 7A. Co-immunoprecipitation of endogenous HNF1A and KDM6A followed by western blot demonstrated that HNF1A is in the same complex as KDM6A. B. Western blot showing loss of HNF1A and unchanged KDM6A in Hnf1a-/- pancreas. C. Differential binding analysis of KDM6A in Hnf1a-/- vs. wild type pancreas. Pink dots below zero (1873 sites) show regions with reduced KDM6A binding and pink dots above zero (118 sites) are regions with increased binding at FDR<0.05. Regions that show reduced KDM6A binding in Hnf1a-/- chromatin are strongly bound by HNF1A and are highly enriched in HNF1 motifs. P-values in (D) were calculated with two-tailed Mann-Whitney U test Regions that show reduced KDM6A binding in Hnf1a-/- chromatin are strongly bound by HNF1A and are highly enriched in HNF1 motifs. P-values in (E) with Fisher's exact test. F. KDM6A binding is markedly reduced in HNF1A and KDM6A co-bound regions in Hnf1a-/- pancreas, but not in other KDM6A bound regions. G. Genes that loose KDM6A binding in Hnf1a-mutant pancreas are predominantly downregulated in Hnf1aaKO pancreas and are direct HNF1A target genes (red dots). H. Summary model depicting that HNF1A recruits KDM6A to genomic binding sites, activating an acinar differentiation program that indirectly suppresses core oncogenic pathways. Defective HNF1A or KDM6A function results in failure of this shared program, with increased activity of pathways that, in the presence of KRAS mutations, promote high-grade non-classical PDAC with sarcomatoid features.
Figure 5(A) The mutant chm allele we used removes the catalytic, histone acetyltransferase MYST domain. The chm mutants consistently display 50% mRNA reduction in young (7 days) and midlife (22 days) when compared to wild-type flies. N=5 young wt, 6 young chm mutants, 4 midlife wt and 6 midlife chm mutants. (B) MS-based quantification of histone H4 and H3 acetylation reveals a specific reduction of H4K12ac in male chm heterozygous mutants at 22 days of age (midlife). N=7 per group. (C) RNA-seq analysis reveals 1,758 significantly altered genes during wild-type aging and 1,319 altered genes during chm aging process. 920 genes are common to both aging processes. N=5 young wt, 6 young chm mutants, 4 midlife wt and 6 midlife chm mutants. (D) Shared age-associated down regulated genes display similar fold-change response in wild-type and chm aging. In contrast, the up regulated genes display higher fold change in wild-type aging compared with +/chm aging. (E) Chm male flies show increased mean lifespan and slower mortality rates in midlife. Survival 90% control = 20 days, chm = 22 days. Median survival for control = 34 days, chm = 42 days, N = 180 (control) and 175 (chm). Log Rank Test, χ2 =37.15, p<0.0001. (F) Midlife chm mutants display increase activity compared to midlife control. (G) Double chm/atpcl mutant display similar lifespan to +/atpcl mutant. Survival 90% +/atpcl = 39 days, chm/atpcl = 35 days. Median survival for +/atpcl = 57 days, chm/atpcl = 54 days, N = 256 (+/atpcl) and 301 (chm/atpcl). Log Rank Test, χ2 =3.19. (*P<0.05, **P<0.01, ***P<0.001). Error bars indicate the S.E.M. in all the graphs. Unpaired two tailed t-tests were used for calculating the p-values in A, B and F. All male flies were collected from a mixed male/female population.
Figure 5PRKRIR, PCBP4 and TSC22D1 are crucial for maintenance of the mesenchymal fate. (A) Scratch assay in MDA-MB-231 cells treated for four days with DMSO or JNKi. Scale bar, 200 μm; 20 X magnification. Mean and SEM is plotted from three independent biological replicates. (B) mRNA levels for key EMT marker genes in MDA-MB-231 treated with DMSO or JNKi for 4 days were measured by qRT-PCR relative to Ctcf and plotted on the y-axis. Mean and SEM is plotted from three independent biological replicates (C) mRNA levels for transcription factors in isogenic epithelial (MDA-MB-361) and mesenchymal (MDA-MB-231) breast cancer cells were measured by qRT-PCR relative to Ctcf and plotted on the y-axis. Mean and SEM is plotted from three independent biological replicates. (D) Scratch assay in MDA-MB-231 cells transfected with NTC or siRNA against PRKRIR, NFIL3, PCBP4 and TSC22D1 for 4 days as in A. Mean and SEM is plotted from three independent biological replicates as bar plot on right . (E) Invasion assay in MDA-MB-231 cells treated as in (D). Mean and SEM is plotted from three independent biological replicates. (F) mRNA levels of key EMT marker genes in MDA-MB-231 and MDA-MB-231 transfected with either empty vector or vector overexpressing PCBP4 or TSC22D1 for 48 hours and then treated with the JNK inhibitor (SP600125) for 24 hours were measured by qRT-PCRs relative to Ctcf and plotted on the y-axis. Mean and SEM is plotted from three independent biological replicates. Plotted Mean ± SEM of three biological replicates. * p<0.05, ** p<0.01, *** p< 0.001, Student's t-test.
Agreement between spatial proximity and gene coexpression in highly granular cell subtypes in the hippocampus.Figure 5a-b. Relationship between the frequency of a (sub) type's neighbors and it's transcriptional pearson correlation between CA1 subtypes (a) and between CA3 subtypes (b). c. Cell type map in the hippocampus shows specific colocalization patterns between a subset of Sst subtypes (purple) and CA1 neurons (green); these Sst subtypes do not colocalize with CA3 neurons (cyan). Scale bar is 500 microns. d. Colocalization patterns of Sst subtypes with CA1 and CA3 subtypes. Sst subtypes that colocalize with the CA1 subtypes have high transcriptional similarity. Colocalization was defined as the percent of neighbors that are of that subtype (Materials and Methods) e Transcriptional correlation patterns between Sst subtypes and CA1 and CA3 neurons. Green, purple and cyan sidebars highlight the subset of Sst co-localized with CA1 (purple), CA1 (green) and CA3 (cyan).
Molecular model for PNRC1-dependent nucleolar RNA decapping Schematic model of the molecular events triggered by PNRC1 inside nucleoli.Figure 7Schematic model of the molecular events triggered by PNRC1 inside nucleoli. PNRC1 functionally interacts with DCP1α/DCP2 decapping complex acting as a scaffold to tether the decapping machinery inside nucleoli and promoting the m3G-cap hydrolysis from U3 and U8 snoRNAs, ultimately leading to rRNA processing block.
a) Confocal analysis of the subcellular localization of HA–PLD1 (green) and endogenous LC3 (red) in HeLa cells in normal medium and under nutrient deprivation conditions.f1(a) Confocal analysis of the subcellular localization of HA-PLD1 (green) and endogenous LC3 (red) in HeLa cells in normal medium and under nutrient deprivation conditions. Left panels: normal medium condition (Nm); middle panels: 1 h with nutrient-deprived medium (1 h St); right panels: 2 h with nutrient-deprived medium (2 h St). Insets denote high magnification of the selected area. Scale bar, 5 μm. (b) Immuno-gold EM micrographs of HeLa cells transfected with GFP-PLD1 and subjected to 1 h of nutrient deprivation in the presence (St+B) or absence (St) of bafilomycin (50 nM). Insets denote high magnification of the selected area. Scale bar, 500 nm. Right panel: Histogram showing morphometric analysis of the relative distribution of GFP-PLD1-positive gold particles on the outer (arrows) and inner (arrowheads) membranes of the autophagosomal-like structures. Values denote means±s.e.m. (n=14). **P0.01.
Figure 1 Immunoblot of media and lysate collected from HEK293T cells overexpressing ERdj3WT or ERdj3KDEL. Fresh media was conditioned on cells for 24 h prior to harvest.  qPCR analysis of ERdj3 mRNA in HEK293T cells treated with or without thapsigargin (Tg; 6 h, 100 nM). Error bars represent the mean ± 95% confidence interval as calculated in DataAssist 2.0 (n = 3).   Representative immunoblot of lysates and media collected from HEK293T-Rex cells stably expressing non-silencing (NS) or ERdj3 shRNA. Cells were treated with the indicated concentration of Tg in fresh media for 16 h. Quantification of the fold increase of ERdj3 in lysates and media collected from HEK293T-Rex cells treated with the indicated concentration of Tg in fresh media for 16 h as in Figure 1C. *indicates a pvalue < 0.05; (n = 3).    Representative autoradiogram of [35S]-labeled ERdj3 in lysates and media collected from Huh7 cells incubated in the presence or absence of Tg (1 µM). The experimental paradigm for labeling is shown above. Quantification of fraction intracellular (dark grey) and extracellular (light grey) [35S]-labeled ERdj3 following a 4 h chase relative to total [35S]-labeled ERdj3 at 4 h (as shown in Figure 1E). Error bars represent standard error from biological replicates (n = 3). Quantification of total [35S]-labeled ERdj3 in media collected from cells pretreated with vehicle or Tg, as shown in Figure 1E. The media [35S]-labeled ERdj3 was measured by densitometry and is normalized to the amount of media [35S]-labeled ERdj3 at 4 h from vehicle-treated cells. Error bars represent standard error from biological replicates. *indicates a pvalue < 0.05; (n = 3).  Representative immunoblot and quantification of sera collected at the indicated times from DBA/2J mice fed a high fat (60% fat) diet after a 18 h fast. A schematic of the fasting/refeeding experimental setup is shown above. The quantification was normalized for each mouse to the amount of ERdj3 in the serum draw immediately prior the fast. *indicates a p-value < 0.05; (n = 6).
Sequence alignment of SARS-CoV-2 Nsp15 coronaviral homologs with structures available in the PDB:SARS-CoV-2 (6VWW), SARS-CoV (2H85), MERS-CoV (5YVD), H-CoV-29E (4RS4) MHV (2GTH).Figure 3.Sequence alignment of SARS-CoV-2 Nsp15 coronaviral homologs with structures available in the PDB:SARS-CoV-2 (6VWW), SARS-CoV (2H85), MERS-CoV (5YVD), H-CoV-29E (4RS4) MHV (2GTH). The secondary structure elements labeled for SARS-CoV-2 Nsp15.
Figure 5Tumor infiltrating immune cells were isolated from the either CT26 or MCA205 tumor bearing model and analyzed for the expression of BODIPY in CD206+ (black) and CD206- (grey) cells. Balb/c mice were inoculated with 5×105 CT26 tumor cells subcutaneously. Since day 6, vehicle or DGAT inhibitors (iDGAT) were administrated via intra-tumoral injection once daily. At day 13, tumor infiltrated immune cells were isolated and stained for CD206 and CD11b. 5×105 MCA205 were injected subcutaneously into C57BL/6 mice. PBS, liposome control or iDGAT-liposome was injected into the peritoneum every other day starting at day 7. Tumor size and body weight were measured every 7 days and the mice were sacrificed on day 31 for analysis. Immune cells from spleen, tumor-draining lymph nodes (TDLN) or tumor were isolated and stained for CD11b and with BODIPY for lipid droplets quantification in myeloid cells. Tumor infiltrating CD8+ T cells (red) were stained together with nuclei (DAPI/blue) after sacrificing the tumor bearing mice.
Arginine-rich DPR modulates intracellular distribution of endogenous EXOSC10 A, B.Figure 6A, B. HeLa cells were transfected with one of the G4C2 repeat plasmids (A), antisense C4G2 repeat plasmid (B) or control mock plasmid. "mock" indicates a control vector which lacks the repeat but still contains the 5' flanking region and 3xTAG. C-F. HA-tagged poly-GA, poly-GP, poly-GR or poly-PR (red) and EXOSC10 (green) were immunostained with anti-HA and anti-EXOSC10 antibodies. Nuclei were stained with DAPI (blue). G. EXOSC10 (green) were immunostained with anti-EXOSC10 antibody in cells transfected with control mock plasmid. Nuclei were stained with DAPI (blue). H, I. Quantification of the frequency of cells with mislocalized EXOSC10. Only DPR-positive cells were quantified (except mock transfected cells expressing no DPR. (Total cell counts: (figure H) mock 300 cells, GA 112 cells, GP 69 cells, GR 53 cells, (figure I) mock 445 cells, PR 159 cells).
WIPI2b and FIP200 Bind in Adjacent, but Distinct, Regions of Atg16L1.Figure 3(A) Alignment of Atg16L1 and Atg16L2 in the WIPI2b binding region. The acidic residues in Atg16L1 (highlighted in red) that are not conserved in Atg16L2 were individually mutated to arginine (basic residues in blue, noncharged in green). (B) Lysates from HEK293A cells transfected with GFP-WIPI2b were mixed with lysates from HEK293A cells transfected with FLAG-Atg16L2, FLAG-Atg16L1, or Flag-Atg16L1 mutants, immunoprecipitated, and analyzed by immunoblotting.(C) Statistical analysis of FLAG-Atg16L1 binding in (B) was performed by Student's t test. SEM for n = 4. ∗p < 0.05. (D) Cell lysates from HEK293A cells transiently expressing FLAG-Atg16L2, FLAG-Atg16L1, or FLAG-Atg16L1 mutants were subjected to immunoprecipitation using FLAG M2 agarose beads. Protein complexes were analyzed using immunoblotting.(E) Statistical analysis of FIP200 binding in (D) was performed by Student's t test. SEM for n = 3. ∗p < 0.05. (F) WIPI2 was immunoprecipitated from lysates from WT or FIP200−/− MEFS after treatment with 0.5 mM DSP. Bound Atg16 and Atg12-5 were detected by immunoblotting. (G) HEK293 cells stably expressing GFP-WIPI2b were and transiently transfected either FLAG-Atg16L1 WT, E226R E230R (ERER), or D237R D239R (DRDR). Bound and input (bottom) were analyzed by immunoblotting. (H) Structural model of the region of Atg16L1 207-246 that interacts with WIPI2b and FIP200. See also Figure S3 and Table S1.
Figure 1(A) Time-lapse 3D-SIM of T6SS assembly, contraction and disassembly by visualizing TssB-sfGFP in A. baylyi. Yellow arrows indicate examples of contact-dependent T6SS assembly pairs. (B) Scheme representing that contact-dependent and -independent T6SS assemblies occur within the cells in close contact with each other. (C) Examples of two T6SS modes in A. baylyi revealed by 3D-SIM live-cell imaging. Upper panel: an example of contact-dependent T6SS dynamics indicated by a green arrow; lower panel: an example of contact-independent T6SS dynamics indicated by an orange arrow. (D) Violin plots showing the distribution of sheath polymerization speed for both modes of T6SS assemblies. 300 assemblies (100 from each biological replicate; 3 biological replicates) were analyzed over at least 3 min at 5 s intervals. The central dash line indicates the median while the upper and lower dash lines indicate the quartiles. Unpaired t-test was performed (ns: not significant). (E) Time-lapse 3D-SIM imaging of sheath dynamics (TssB-sfGFP) in the absence of membrane complex protein TssM. (F) Time-lapse 3D-SIM imaging of sheath dynamics (TssB-sfGFP) in the absence of TagX. Yellow arrows indicate examples of contact-dependent T6SS sheath foci pairs. (G) Time-lapse 2D-SIM imaging of TssA and sheath dynamics. Imaging was performed on cells of the double-tagged strain (tssB-mCherry2 mNeonGreen-tssA) by 2D-SIM. White arrow indicates an example of paired T6SS assembly.
Figure 4Immunoblo of mGPD in GA muscles from obese patient IH of mGPD in GA muscles from obese patient Immunoblo of mGPDH and myogenin in GA muscles fro indicated mic qRT-PCR of mGPDH in GA muscle of indicated mice at days 0 and 3 post CTX intramuscular injection Experimental setup (upper of E), qRT-PCR of mGPDH, myogenin and myh3 (bottom of E in GA muscle from AAV-mGPDH-treated HFD-fed mice at days 7 post CTX intramuscular injection ), H&E staining (arrowhead, necrotic myofibers; asterisks, regenerating fibers) (F), distribution of the fiber CSA (G) in GA muscle from AAV-mGPDH-treated HFD-fed mice at days 7 post CTX intramuscular injection percentage of myofibers with central nuclei (H) in GA muscle from AAV-mGPDH-treated HFD-fed mice at days 7 post CTX intramuscular injection Experimental setup (upper of I qRT-PCR of mGPDH, myogenin and myh3 (bottom of I) in GA muscle from AAV-mGPDH-treated STZ-treated mice at day post CTX intramuscular injection H&E staining (arrowhead, necrotic myofibers; asterisks, regenerating fibers) (J) in GA muscle from AAV-mGPDH-treated STZ-treated mice at day post CTX intramuscular injection distribution of the fibers CSA (K), percentage of myofibers with central nuclei (L in GA muscle from AAV-mGPDH-treated STZ-treated mice at day post CTX intramuscular injection Experimental setup (uppe and muscle weight (bottom of M) in GA muscle from AAV-mGPDH-treated STZ-treated mice at da 14 (M) post CTX intramuscular injection Immunoblots of mGPDH, p-AMPK, p-ACC, PGC1α and myogenin for the experiment described in E.