EMBO/sd-character-level-ner huggingface dataset:
Snapshots of Rfa1 ChIP-Seq peak at ARS305 from WT and rtt105∆ cells released into HU-medium. The average Rfa1 ChIP-Seq read density from cells released into HU-medium around ACS sites. ACS: ARS consensus sequence.
I Scheme illustrating adult fate-mapping experiment using NestinCreERT2; GFP mice to monitor rNSCs and their generated astrocytic progeny. Two potential modes of adult astrogenesis and their lineage relation are depicted: (1) rNSC-derived astrogenesis, (2) astrocyte-derived astrogenesis.
(C, D) VCaP cells (1x107) infected with lentivirus were injected subcutaneously into NSG mice (n = 8/group). Tumors were measured by caliper twice a week. Tumors at the end point of measurement were isolated and photographed (C), and data are shown as means ± SD (D). Statistical significance was determined by two-tailed Student's t-test for tumors at day 56. *** P < 0.001.
Immunofluorescence showing the Ago3 signals (green) in control and Vret-depleted BmN4 cells (Vret KD). Vret is shown in red. DAPI shows the nuclei (blue). Scale bar: 10 μm. Immunofluorescence showing the Siwi signals (green) in control and Vret-depleted BmN4 cells (Vret KD). Vret is shown in red. DAPI shows the nuclei (blue). Scale bar: 10 μm.
Primary hepatocytes were isolated from 12-week-old male Prom1+/+ (WT) or Prom1-/- (KO) mice and serum-starved. (K) Differentially expressed genes showing more than a 2-fold change with P < 0.05 (118 DEGs) induced (n=55) or repressed (n=63) by Prom1 knockout (n = 2/group). G6pc, glucose-6-phosphatase catalytic subunit; Pck1, phosphoenolpyruvate carboxykinase 1.
Left: cylinder representation of the APC/C-Nek2A complex structure. Apc2 (light blue) and Apc4 (light brown) are highlighted, the rest of the APC/C is shown in transparency. (i) Two different views of cryo-EM density for the Apc2 and Apc4 subunits. Secondary structure elements of the Apc2WHB domain are highlighted. (ii) Cryo-EM density for the second MR tail of Nek2A.   Details of the second MR tail binding site formed by the Apc2 (including the repositioned Apc2WHB) and Apc4 subunits. Nek2AMR2 is shown in orange.
(C). Processing rates were quantified and normalized to ctrl based on hybridization intensities of (B). Significance was assessed using 2‐tailed Student's t‐test, < 0.05*. Data information: All experiments were performed in triplicate. Error bars show SD.
RNA sequencing (RNA-seq) of week 15 COs and transcriptome analysis (WT: n=2, KO: n=4).   Heatmap of 100 upregulated genes (left panel) and 100 downregulated genes (right panel) selected by highest fold change.
(D) Pacs1+/+ and Pacs1ccy/ccy mice were immunized with NP-KLH. Low affinity (anti-NP30) and high affinity (anti-NP2) antibodies were measured 14 days after immunization.
Representative 3D reconstructions of EM tomograms of 250 nm sections from Wt and endophilin DKO mutants. Please note the accumulations of ELVs in IHCs of endophilin 1/2-DKOs. Analysis was performed on 8 tomograms from 2 animals per genotype. Scale bars: 100 nm.
A549 cells with shCtrl or shGUARDIN were treated with 100nM rapamycin or DMSO vehicle in the indicated combinations for 48h. Western blotting was used to measure p21 levels (left) while conducting SA-β-gal staining in parallel (middle) with the percentage of senescent cells calculated from the SA-β-gal staining (right).
G Genomic PCR analysis for a human specific mitochondrial sequence (391 bp) in human-mouse chimeras.
C, hmCD40 mHEVc-LC3-EGFP cells were treated with or without CD154 followed by challenged with WT, MIC1 ko, MIC1 ko+MIC1, MIC3 ko, MIC3 ko+MIC3, MIC1-3 ko, MIC1-3 ko+MIC1-3 tachyzoites. LC3 accumulation around the parasite was examined by fluorescence microscopy 5 h post-challenge. D, hmCD40 mHEVc-LC3-EGFP treated with or without CD154 were challenged with WT, MIC1 ko, MIC1 ko+MIC1, MIC3 ko, MIC3 ko+MIC3, MIC1-3 ko or MIC1-3 ko+MIC1-3 tachyzoites. Parasite load was examined 24 h post-challenge.
(C) Heatmap of the seven transcriptional targets of Slug known to promote proliferation and to be extracellular.
(A) Chi-G4S-DR5 stable 4T1 tumors harboring mice were treated lexatumumab, lexatumumab +ROCK1i, and avelumab + lexatumumab and other controls as indicated. Antibodies were treated i.p at 100μg dose (6 total), ROCK1i (in PBS) was injected directly into tumors at 2mg/kg dose (6 total). Various treatments were started when tumors were ~400mm3 size. Harvested tumors were grouped together and sized matched (3 independent sets: n=2-6 tumors in each set) followed by TIL isolation CD8/CD45 and CD4/CD45 expressing cells were measured by flow cytometry.
(c) Luciferase activity in Jurkat cells transfected as in a, then left uninoculated (−) or inoculated with 10 × 108 E. coli F18 (+), followed by the addition of monoclonal antibody (mAb; amount, under graph) 9D1 to SLAM (α-SLAM) or rat immunoglobulin G2b isotype-matched control antibody (Rat IgG2b).
(F) Defects in synapse elimination in the inner molecular layer revealed by double immunostaining with PSD95 and VGluT2 antibodies (n=5 mice/genotype). GL indicates granule cell layer, IML/OML indicate inner/outer molecular layer, respectively. Density of colocalized PSD95/VGLuT2 puncta was counted. IML: WT 109±21, crmp2-/- 156±15 (p=0.004). OML: WT 281±38, crmp2-/- 297±80 (p=0.7). Scale bars: 10 μm, mean ± SD, *p<0.05, t-test.
µsL (in blue) dimerization likely proceeds via C337 in Cµ2 (top arrow) though C575 intra-subunit bonds (in pink) may favor covalent binding via C337 (in yellow). Compact µs2L2C575OX subunits are then formed which are attacked by ERp44 (depicted in green). Polymerization proceeds by sequential recruitment of mixed ERp44- µs2L2 complexes, until fully oxidized hexamers are formed. A reduced ERp44 is released at each step. It is also possible that oxidized µs2L2 subunits (in red) bind directly to an ERp44- µs2L2 complex. E
Immunoblot analysis of the MG132-induced deposition of FUNDC1, TIM23 and p62 in HeLa cells transfected with Ctrl or DLP1 shRNA.
Distribution of peptides containing sulfhydrated cysteine residues relative to their H/L ratios as determined by the BTA analysis of cell extracts isolated from C1 and P1 patient cells (indicated in A) and C2 and P4 fibroblasts (B). Values of H/L ratios are plotted against the number of identified peptides. The gray line marks the H/L ratio >2, consisting of cysteine-containing peptides in proteins from patient cell lines that exhibited higher reactivity with H2S compared with the respective control. Indicated on the X axes are representative sensitive cysteine peptides, which are common between the ones found in the RedoxDB database, and by the BTA assay.
(a) Number of EC and haemoglobin content in the blood of the indicated mice (10-20 weeks old; mean±s.d., n=6). *P0.05 versus value of WT (Student's t-test).
Low-pass filtered monomer map features of Ca2+/acidic pH (grey) and water structure (green) with differences at lower radius (left). Zoomed inset (right) with maps displayed at a false discovery rate (FDR) threshold of 1% showing significant differences. Detailed map comparison at lower-radius region of Ca2+/acidic pH (grey, left column) with the water condition (green, right column). A total of 3 atomic models (model 1: cyan, model 2: pink, model 3: green) describe the map of TMV in water whereas the Ca2+/acidic pH map could be modelled with a single atomic model (center). Located Ca2+ ion in the Ca2+/acidic pH map with different conformations in the water structure (bottom).
(h) HeLa cells, co-transfected with GFP-IRGMd, and control, BECN1 or ATG7 siRNA, were labelled with MTR 48 h post-transfection, imaged by live-cell microscopy, and percentages of GFP+ cells that were also MTR+ were quantified.
D Amylase, lipase, and ANGPTL4 were assessed in the serum from AP and SAP animal models and ANGPTL4 protein expression were determined in the blood and pancreas (n = 15, each group).
(B) Representative light microscopy images of spinal cord sections of Fus+/+/ChAT-CRE (B1, B4), FusΔNLS/ΔNLS/- (B2, B5) and FusΔNLS/ΔNLS/ChAT-CRE (B3, B6) mice at birth stained with cresyl violet (Nissl, B1-B3) or anti-choline acetyl transferase (ChAT, B4-B6).(C-D) Quantification of Nissl+ (C) and ChAT+ (D) motor neurons per spinal cord ventral horn. N=9 Fus+/+/ChAT-CRE, N=8 FusΔNLS/ΔNLS/- and N=4 FusΔNLS/ΔNLS/ChAT-CRE; for Nissl+ and N=11 Fus+/+/ChAT-CRE, N=7 FusΔNLS/ΔNLS/- and N=8 FusΔNLS/ΔNLS/ChAT-CRE; for ChAT+ (**) p<0.01 vs Fus+/+, (##) p<0.01 vs Fus∆NLS/+ ; (ns) non-significant; One way ANOVA followed by Tukey post hoc test.(E) Total numbers of caspase 3 (Cas3)/ChAT/DAPI triple positive cells in Fus+/+/ChAT-CRE, FusΔNLS/ΔNLS/- and FusΔNLS/ΔNLS/ChAT-CREmice. N=9 Fus+/+/ChAT-CRE, N=7 FusΔNLS/ΔNLS/- and N=8 FusΔNLS/ΔNLS/ChAT-CRE; (**) p<0.01 vs Fus+/+, (#) p<0.05 vs Fus∆NLS/+ ; (ns) non-significant; One way ANOVA followed by Tukey post hoc test.
Transcriptome-wide analysis of the effects of TEFM loss on mtRNA transcripts by TruSeq RNA sequencing. A complete map of mtDNA showing the change in sequence read coverage (log2 fold change [L/L, cre / L/L]) between Tefm knockout (L/L, cre; n= 4) and control (L/L; n= 3) mice on both strands. Increased reads are shown in red and decreased reads in blue. The mtDNA is displayed in the central track, with mt-rRNAs in green, mt-mRNAs in light blue and mt-tRNAs in grey.
Ten-fold serial dilutions WT or rtt105∆ cells in two different backgrounds were assayed on normal growth media (YPD) and on media containing the indicated DNA damaging agents, methyl-methane sulfonate (MMS), camptothecin (CPT), bleomycin (Bleo), and hydroxyurea (HU).
F GO enrichment analysis for the DMRs based on the biological process GO categories. Green dot indicates gene number in each term.
(A) Top: schematic drawing depicts pan-neuronal expression of YFP in head and ventral neurons in the context of the C. elegans body plan. Left: micrographs show the SOD1G85R-YFP proteins expressed in WT or the spr-5(by134);ufd-2(tm1380) mutant background. The double-mutant worms show a marked decrease in protein aggregation in neurons. Enlarged sections of headneurons (red framed) and ventral cord neurons (white framed) are shown. Middle: quantification of locomotion in the spr-5(by134);ufd-2(tm1380) and the WT C. elegans with neuronal expression of SOD1G85R-YFP (n = 30). Right: a decrease in the protein levels of SOD1G85R-YFP in the presence of spr-5(by134);ufd-2(tm1380) is shown by western blots of the supernatant (S) and the pellet (P) fractions. (B and C) Analyses of the spr-5(by134);ufd-2(tm1380) and the WT C. elegans with neuronal expression of TDP-43-c25-YFP (n = 30) or PolyQ-YFP (n = 12) as in (A).
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).
C. Frontal cortices of A53T α-syn heterozygous transgenic mice and control mice at the age of 9 months (old) or 2 months (young) were lysed and Western blot was performed with the indicated antibodies (n=3). *** P < 0.001 compared to WT, unpaired t-test.
(c) Immunoblot analysis of membranous organelles from U937 cells separated by isopycnic sucrose density-gradient centrifugation. Numbers represent fractions from the gradient (1, top; 12, bottom). Uncropped images of blots are shown in Supplementary Information, Fig. S8.
Isothermal titration calorimetry (ITC) binding assay to quantify affinity (KD) of Art22-9 degron for Gid1057-292 substrate-binding domain. The raw ITC results (top) were integrated to calculate the amount of heat released (∆H) during every injection of a peptide and plotted as a function of peptide:protein molar ratio (bottom). Fitting of the obtained data points to the binding model served to determine KD and stoichiometry of the binding reaction (N).
Representative telomere length distributions in parental and AGO2KO HeLaS3. Average telomere length and the standard deviation, as well as the total number of telomeres analyzed, are indicated. Notice the marked shift towards short telomeres in AGO2KO cells compared with the parental HeLa S3 cell line.
Boxplots depict differences in hippocampi of AD and no AD patients regarding SINE Alu RNA processing ratio (left panel) (a p value of 0.05 was considered as threshold for statistical significance with p=0.01 , n=24, unpaired non-directional t-test) and in total Alu RNA levels (right panel) (ns=not significant). In the boxplots, the central band (the line that divides the box into 2 parts) represents the median of the data, the ends of the box shows the upper (Q3) and lower (Q1) quartiles, the extreme line shows Q3+1.5xIQR to Q1-1.5xIQR (the highest and lowest value excluding potential outliers), while dots beyond the extreme line show potential outliers.
(d,e) ULK1 and AMBRA1 constructs are illustrated. Asterisks mark nonspecific bands corresponding to immunoglobulins. (e) HEK293 cells were co-transfected with vectors encoding ULK1-HA together with β-galactosidase-Myc (βgal), AMBRA1 full-length (FL), and F1, F2 or F3 Myc-tagged proteins. Protein extracts were immunoprecipitated using anti-HA antibody. The relative amounts of co-immunoprecipitatedULK1 and F1 or F3, respectively, are the same (see upper and lower left panel).
working model how the HRD1 regulating the circadian behavior, growth and female reproduction through CREBH-FGF21 axis.
(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.
B. Quantitative PCR of Cyp46 of total brain and synaptosomes from wt and NPC1nmf164 mice. 3 biological replicates mean ± SEM is shown.
(E) FLAG-tagged Taf12 and TAP-tagged Pab1 were affinity purified separately from cells grown in rich conditions (upper panels). TAP-tagged Pab1 was cleaved off from beads using the Tobacco Etch Virus (TEV) protease, releasing a shorter form of Pab1 (CBP-Pab1) in the eluate (E). CBP-Pab1 was then mixed with beads containing FLAG-Taf12 IPs and incubated in a phosphatase buffer, with and without 0.5 µM microcystin. Each reaction was then analyzed by IB and simultaneously probed with anti-FLAG or anti-CBP antibodies (lower panel).
axonal transport analysis. Quantification of percentage of moving mitochondria (J), number of moving mitochondria (K) and number of stationary mitochondria (L) normalized to neurite length 100µm.
Strand-specific RT-qPCR detection of the mitochondrial precursor transcripts containing the antisense of mt-tRNAA and antisense of mt-tRNAC in control and Tefm knockout mice (n= 12 mice for each group). The mt-mRNAs are shown in light blue and mt-tRNAs in grey. Arrows show the binding position of RT-qPCR primers. Actin transcript was used as endogenous control.
D, E. HeLa cells were transfected with Ctrl, TOM20, TOM22 or TOM70 shRNA vectors including nuclear localized GFP (N-GFP) expressing elements, then treated with MG132 and immunostained with the indicated antibodies. Scale bar=10 µm. Quantification is show in (E).
F Cumulative probability plot of the total mEPSC amplitudes, small mEPSCs (i) and big mEPSCs (ii) from both WT and Tau-/- mice (black and red traces, respectively) (***p < 0.001; Kolmogorov-Smirnov Z test).
(A-E) Confocal images of representative midguts of the indicated genotypes using kluReDDM for tracing and age- and EB-specific transgene expression at day 7 after temperature shift. ISC mitosis was monitored by using PH3 labelling (white) in all guts. (B-E) Accumulation and loss of klu+ cells by loss (B and E) and gain (C and D) of N and EGFR signalling. In (C), the accumulation of EC-committed EBs (klu+ cells) in midguts with constitutively activated EGFR (kluReDDM> EGFRact) is accompanied with a non-autonomous increase in ISC mitosis. Inset in (C) shows labelling with Dl (blue), revealing symmetric ISC mitoses Data information: Scale bar, 100µm for all images.
Day 0: The TRs Rcan1, Taf1c, Tead4 and Tfap4 are expressed in naïve MEFS. Approximately 50% of naïve cells express all 4 factors. 18 hours: OSKM induce the expression of Cbfa2t3 in ~40% of the cells. Only a fraction of the population expresses all 5 TRs. Day 3: The expression of Gli2, Irf6, and Ovol1 has been induced by direct and indirect OSKM effects. Various interconnections between the TRs are established, thus stabilizing their expression. All eight TRs are expressed in a limited number of cells found exclusively in early-iPSCs colonies. Day 6: Nanog expression is induced in ~40% of the cells within the early-iPSCs colonies. All nine TRs are expressed only in ~6% of the cells found exclusively within these early formations. The nine TRs reconstruct the 9TR GRN, which is required to promote cellular reprogramming. iPSCs: The 9TR GRN GRN is dissolved in iPSCs because Ovol1 and Cbfa2t3 expression is dramatically reduced to undetectable levels.
(B) Alizarin red staining of bone shows spinal curvature but no bony fusions in the skeleton of smyhc1-/- adults, in contrast to the compression and fusion of vertebrae seen in smyhc1R673H/+ adults. Distal tail regions are highlighted and enlarged.
HeLa cells were co-transfected with Myc, F1-Myc or ΔLIR-Myc and Mito-OM-cherry and immunostained with anti-HSC70 and anti-Myc antibodies. Scale bar=10 µm.
Average time of return to baseline obtained by fitting a linear function to the Cm-data following a 20 ms depolarization.
HMDM were stimulated with AdV (50 000 pp/cell) and antibody (h9C12; 20 ug/ml, IVIg: 20 mg/ml) or 10 μg/ml pI:C for 3h and gene expression was measured by qPCR (n = 4 mean ± s.e.m).
(D) HEK293T cells were transfected with GST-tagged NEMO domain constructs together with Strep-tagged MARCH2-TM. Whole cell lysates were subjected to a Strep-PD assay, followed by immunoblotting with an anti-GST antibody.
a, Kaplan-Meier analysis comparing PDAC-free survival in Atg7+/+ (blue) or Atg7−/− (red) KrasG12D/+ p53−/− mice.
I siRNAs against scrambled sequence or human OGT were transfected in 293T cells and STAT1 levels were determined 48 hours later
FP competition binding of C5 and Tat-C5 to PICK1 with 5FAM-Tat-C5 (20 nM) as tracer. Saturation binding curve is shown in EV1B.
Figure 3. Archaellum orientation with respect to the cell envelope. (A-D) show tomographic slices through side views of cones. In the bottom row, white lines show the angle of the archaellum with respect to the surface layer, and red dashed lines show the conserved distance from the archaellum at the membrane to the cone. Scale bar 100 nm (applies to A-D).
D. Schematic presentation of FET family of fusion oncoproteins, targeted DNA sequences and associated tumors. Left: FET N-terminal fusion partners and binding to SWI/SNF. Center: C-terminal transcription factor fusion partners and their DNA target sequences (JASPAR database). Right: Tumor types caused by respective fusion oncogene. Note tumor type specificity for each fusion oncoprotein and that the FET NTDs replace each other as fusion partners in some entities. Only a selection of the FET family fusion-oncoproteins and tumors is shown as more members are continuously discovered.
CD4+T cells from wild-type (WT), CBLOST and CBLBOSTmice were left unstimulated (unstim) or stimulated for 30, 120, 300 or 600 seconds with anti-CD3 and anti-CD4 antibodies. Equal amounts of cell lysates were subjected to affinity purification using Strep-Tactin-Sepharose beads and subjected to MS analysis as described in Material and Methods.C, D List of specific interacting partners of CBLB (C) and CBL (D) ranked according to their maximum mean enrichment across all time points. Heat maps show, for each time point, the fraction of bootstrap iterations for which the corresponding proteins were detected as specific partners (denoted as "P(Detection)"). Red dots indicate the proteins that have been previously reported as CBL (D) interactors in the BioGRID database. Ubiquitin (UB) is highlighted with a black arrow.
(a) Cell death was analysed after the activation of death pathways in the presence and absence of enforced Atg5 expression (18 h cultures). Values are means ± s.e.m. of three independent experiments.
Western blot analysis of ATF4 levels in the hypothalamus of mice 4 h after i.c.v. injection of vehicle (Veh) or 10 pmol AβOs; graph shows densitometric data normalized by β-actin (n = 7 Veh; 8 AβOs). #P = 0.0731; Student's t-test.
(C) Metadata profile showing enrichment of SUV39H1 and H2 over the MERVL consensus sequence including 1kb sequences flanking the start
(F, G) HeLa cells were treated as in E in the presence of 50 μM zVAD‐FMK and analysed by immunofluorescence microscopy for active BAX (6A7 epitope; F) or cyt c (G). Data are expressed as the average of three experiments±s.d. *P0.01.
Significant genomic co-occupancy between AIB1 and TEAD in normal breast and breast cancer cells. Overlap of AIB1 and TEAD4 ChIP-seq peaks in MCF10A and MCF7 cell lines. Select peaks from MCF10A ChIP-seq shown. ChIP-sequencing performed in triplicate.
(J) KLF4 was poly(ADP-ribosyl) ated. KLF4 was immunoprecipitated and detected by anti-PAR and anti-KLF4 antibodies in MDA-MB-231 cells.
(A) Immunolocalization of Arp2 in a wound-healing assay. A549 cells expressing control or WDR63 were serum-starved for 6 h before they were scratched. Cells were then treated with or without 10% FBS for 30 min, followed by immunofluorescence assay. The branched actin networks were shown by immunostaining with anti-Cortactin antibody. Data shown represent three independent experiments. Scale bar: 20 μm. The lamellipodia formation was quantified by measuring the length of the outer margin of lamellipodia in individual cell (n=20 for each condition), and expressed as the proportion of the total length of the cell perimeter. Data shown are mean ± SD; n = 3 independent experiments. ***, P ˂ 0.001; One-way ANOVA.
G Quantification of dendritic length [p=0.1857], branch points [p=0.1331], and Sholl analysis [p=0.1501] showed no difference between β-catex3 iDCX and control cells at 13dpT (control: n= 18 cells from 4 animals, β-catex3 iDCX: n= 20 cells from 4 animals)
Sequence of the engineered strong terminator (arg10-23T) at the SPCTRNAARG.10 gene.
(A) Representative images of COS7 cells transiently transfected with GFP-COP1 WT or GFP-COP1 NESmut (V238A/L242A) (green) and empty vector or 3xFLAG-CRM1 (grayscale). Cells were stained with anti-FLAG (Cell Signaling) and anti-rabbit Alexa Fluor 680. Nuclei were counterstained with DAPI (blue). Scale bar, 10 µm.
(D) Comparison of the probability density of the data (kernel density estimates) with the model (using model M4). To estimate the probability from the model, the data set was simulated 15 times using the posterior mean parameter values combined with the measured cell areas.
Ca2+-current-voltage relationships in response to 10 ms step-depolarizations. (A') The peak of Ca2+-influx was significantly reduced in endophilin 1-SKO (**p = 0.0024) and 1/3-DKO (***p < 0.0001) when compared to Wt. (Wt n = 30/ N = 20; 1-SKO n = 15/ N = 9; 1/3-DKO n = 39/ N = 20; Non-parametric K-W with post-hoc Dunn's correction).
(C) Co-immunofluorescence analysis of α-synuclein with SMI-32 in WT and MPS-IIIA hippocampal neurons (DIV14). α-Synuclein synaptic puncta present in a neurite tract of 10µm is showed in a representative enlarged image. Quantification of α-synuclein synaptic puncta was calculated from 30 different enlarged images c.
(D) Effect of motif context sequence exchange. Heatmap depicting the mean expression fold changes caused by motifs (y-axis) inserting of RpL5, RpL36A, thoc6, CG8157, and cas to different context sequences (x-axis). The heatmap shows the expression changes relative to wild-type expressions of the context-origin promoters CG10915, CG15674, cas, CG8157, thoc6, RpL36A', and RpL5, respectively.
(d) Chronological ageing of wild-type (▪, o) and Δatg7 (▴, ▿) with (open symbols) or without (closed symbols) addition of spermidine (4 mM) at day 1. Data represent means ± s.e.m. (n = 4).