EMBO/sd-character-level-ner huggingface dataset:
Effect of antimonial drug resistant and sensitive forms of the Ld (LdR and LdS) on cellular cytokine level RAW 264.7 cells were infected with Antimony sensitive (LdS-Ag83) and antimony resistant (LdR-BHU569) form of Ld for 24 hours along with uninfected cells kept as control. IL-10 (A) and TNF-α (B) were measured at mRNA level by qRT-PCR after infection (mean+/- s.e.m. and, n=4).
A. Reconstitution of yeast V-ATPase from Hchim containing V1 (V1Hchim), lipid nanodisc reconstituted Vo (VoND), and recombinant subunit C.
Distribution of mitotic spindle orientation of dividing cells from wildtype H9 hCOs, #6 and #23 RGCC-KO hCOs. Each plot represents a dividing cell (H9, n=22; #6, n=27; #23, n=39 from 2 independent experiments). Statistic analysis of splitting plane angle in RGCC-KO hCOs. Data were presented as mean ± SEM. Each plot represents a dividing cell (H9, n=22; #6, n=27; #23, n=39 from 2 independent experiments).Statistical significance was tested by one-way ANOVA. **, p<0.01; ***, p<0.001; ****, p<0.0001.
F. Line scan analysis taken from white dashed lines in (E) showing intensity changes of P4M and TGN38 signal from control (top) and NPC1I1061T (bottom) cells.
C Shoot phenotypes of Mx under control (Hoagland nutrient solution) and excess Zn (300 μM Zn) conditions for 3 weeks. Scale Bar: 1 cm.
(H) Quantification of PLA signals from (G). Data in (A) to (H) are representative of at least three experiments with graphs depicting means ± SEM
Figure 8. Model of p53 binding and local histone modification as a form of genome protection to DNA damage stress.
(a-c) Native merged images or images with colocalization highlighted in white pixels are shown. Nuclei are blue (DAPI). Scale bar, 10 μm.
A, NPCs carrying Dnmt3a/b-KO or WT alleles were differentiated into neurons. Neurons were isolated by FACS and their DNA methylation patterns analyzed using RRBS (n = 3 cultures per genotype).
A Immunoblot analysis of USP33 and HIF2α protein levels in T387 GSCs expressing USP33-targeting shRNAs (shUSP33) or non-targeting shRNA (shNT). Targeting USP33 by two distinct shRNA clones through lentiviral infection reduced USP33 and HIF2α expression in GSCs.
Representative images of H&E and immunohistochemical staining for lung differentiation markers TTF-1 and Mucin 5B for at least 2 independent regions of n=4 H1299control and n=2 H1299RASSF1A primary tumours at day 17 with quantification (right) of TTF-1 based on nuclear intensity. Scale bars 100µm. Statistical significance was determined by Student's t-test (2-tailed). Error bars represent the mean ± S.E.M
A In vitro differentiation to mature ookinete of wildtype (WT), Δisp1, Δisp3, and Δisp1/3 parasites. Values are means ± SD (n=4 biological replicates); two-tailed t test, *, P<0.05, **, P<0.01, ***, P<0.001, ns: not significant.
D. Size of lumen in cells transduced with WT or mutant INVS is shown. Results presented are scatter plots of acini size (n=205 for Vector, n=143 for HA-WT, n=131 for -3D, n=167 for -3A, n=144 for -R899X, n=128 for -Q671X, and n=144 for -R603X INVS stably transfected MDCK cells, respectively). Two independent experiments showed similar results. Statistical significance was determined by Mann-Whitney's non-parametric median test.
(D) Gene expression of VE-cadherin (CDH5) from sh-Control and sh-PI3KC2β hCMEC/D3 cells in resting condition or after 6 hours of stimulation with TNFα. The mRNA levels are given as fold change to resting control hCMEC/D3 cells normalized to PGK1. Data represent mean ± SEM of n=3 independent experiments in duplicate; for Sh-PI3KC2β+TNFα, n=3 independent experiments with only two experiments in duplicate. No significant changes between conditions were noted (Mann-Whitney test).
(E) Alignment of the RGG box of in ICP27 proteins of the simplexvirus genera of alpha-herpesviruses.
Balb/C mice were aerosolically challenged with Rv, Rv∆aosR, and Rv∆aosR::aosR strains. Each data point represents log10 CFU obtained from the infected lung of mice and e­rror bar depicts the median with interquartile range for each group. Each data point represents log10 CFU obtained from the infected spleen of a mice and the error bar depicts the mean with SD for each group.
D Comparison of cell size in WAT of WT and FADD-D mice maintained on SD and HFD (n = 5 for each genotype).
Top panel, left to right: NSP5-∆CTR labelled with Atto-647 (25 μM) incubated with unlabeled NSP2 (10 μΜ); NSP5-∆CTR in the presence of 10% v/v PEG-20K; and with 5 μΜ of poly-arginine (polyArg). Bottom panel: Atto-647-labelled NSP5-∆CTR (5 μΜ) incubated with unlabeled NSP5 (25 μΜ) and Atto-488 labelled NSP2 (10 μΜ). NSP5/NSP2 droplets containing labelled NSP2 (green) also contain NSP5-∆CTR-Atto647 (magenta), shown along with an image of both 488/647 channels overlaid. Scale bar, 10 µm.
Representative images of H&E and cleaved caspase-3 staining from each treatment group (E).
Representative confocal images of immunostaining against muHTT (red) and DARPP32 (D) showing muHTT aggregates positive for EM48 antibody in the infused striatum in neurons or astrocytes and relative quantification (E Hoechst (Ho, blue) was used to counterstain nuclei. All values are expressed as % above the mean of aggregates in the contralateral striatum of R6/2 chol-high. The data are shown as scatterplots with means±standard error. Each dot corresponds to aggregates counted in all the images from 3 animals. Scale bars: 5 µm Statistics: one‐way ANOVA followed by Newman-Keuls multiple comparison tests (*p<0.05; **p<0.01; ****p<0.0001).
(D) MKH2/MK ratios were measured in cells grown aerobically for 20 h in MHB-ca medium. Data are expressed as average ± SD of three independent experiments. * Denotes p < 0.05 compared to WT via one-way ANOVA with Dunnett's posttest.
J, Quantification of mean PI(4,5) P2 immunoreactivity in cells. Mean ± SD, n = 16-26 cells pooled from 2 independent experiments. Student's t-test.
Expression levels of MIR9-3 and Ai854517 correlate in mouse cerebellar development. Time points: E18, postnatal day 0, 3, 6, 9; three mice per time point.. Expression calculated as cap analysis of gene expression (CAGE) hits in the transcription start site (CTSS).
Diagram for ablation of CX3CR1+ macrophages using CX3CR1-DTR (DTR) mice. DT, diphtheria toxin.
A. Accumulation of the HY5 protein in WT and phyB1B2 (phyB) plants grown under 20 μM Fe-EDTA in nutrient solution in a growth room. Rubisco and β-Actin were used as loading controls for leaves and roots in the western blot analysis, respectively. The values shown above each lane indicate the relative abundance of the HY5 protein.
G The CEN activity stacked in time showing how the waves become diffuse after the perturbation is introduced.
E IF at E10.5 for OCT4+PGCs and H3K9me2. White arrows mark OCT4+PGCs. Both Ctrl and PCKO PGCs show the absence of H3K9me2 (green) staining. Scale bar, 20 μm.
(F) C-terminally tagged Mcp3-HA is located to mitochondria. A mitochondria enriched fraction (Mito.) and the post mitochondrial supernatant (PMS) of wild-type cells carrying the empty plasmid () or over-expressing the C-terminally HA-tagged Mcp3 (Mcp3-HA) were analysed by SDS-PAGE and immunodecortion with antibodies against the HA-Tag, the mitochondrial protein Tom40 and a marker protein for the cytosol (Hxk1). m, mature protein.
(E) The molecular mechanisms in fatty acid synthesis (Wakil et al, 1983), and the relevance of the position of the ACP (see Fig. 6 for details) and carboxylase to the catalytic cycle is indicated (see text). ACP, acyl carrier protein; CoA, acetyl-Coenzyme A; MPT, malonyl/palmitoyl transferase; KS, ketoacyl synthase; KR, ketoacyl reductase; DH, dehydratase; ER, enoyl reductase; AT, acetyltransferase.
g-l, SEM images of fly eyes expressing the indicated transgenes. RNAi knockdown (KD) of atg6 and atg12 enhances degeneration in DTS7 flies reared at 28 °C (compare h, i to g) and AR52 flies reared on DHT (compare k, l to j). 200 to >1,000 fly eyes of each genotype were examined. Quantitative analyses of eye phenotypes are presented in Supplementary Fig. S2. (N, nucleus; Rh, rhabdomere.)
Scatter plots as in (A) highlighting in black subsets of known genes expressed in phagocytosis
(B) ER-mitochondria associations and the VAPB-PTPIP51 interaction are disrupted by wild-type and ALS/FTD mutant FUS. NSC34 cells were transfected with EGFP control vector (CTRL), EGFP-FUS, EGFP-FUSR521C or EGFP-FUSR518K and proximity ligation assays performed using VAPB and PTPIP51 antibodies. FUS were detected via their EGFP tags. Scale bar=10 m. Bar chart shows relative number of proximity ligation assay signals/cell. Data were analysed by one-way ANOVA and Tukey's post-hoc test; n=47-53 cells from 5 experiments. Error bars are s.e.m.; ***p<0.001.
A. Ribbon diagram showing the 2-fold dimerization interface of Mdm12. Oxygen and nitrogen atoms are shown in red and blue, respectively. The orange dotted lines indicate intermolecular hydrogen bonds between two protomers of Mdm12. The sequence alignment of yeastMdm12 orthologs is shown to highlight the sequence conservation in the N-terminus β1-strand. Ten orthologs are aligned from residues 1 to 11. Absolute and highly conserved residues are indicated in red and orange, respectively.
A. Immunofluorescence images of 10 μm-thick sections from lateral ventricle CP villi of Mpdz+/+ and Mpdz-/- P14-P16 mice immunolabeled by anti-LDLR. Scale bars, 50 (top) and 25 (bottom) μm. B. Mean fluorescence intensities (normalized relative to the highest recorded intensity) per cell in several LDLR-immunolabeled CP sections (mean ± SD, n=101).
(B) Automatic cluster-mapping of the temperature-dependent splicing changes in CHX, based on changes in PSI (percent spliced in). Categories (right) were manually assigned.
D) Y1H identified TFs that interact with promoters of genes in each pathway in central carbon and in the specialized metabolic pathway.
(D) 293T cells were co-transfected with expression plasmids for either LacZ or m152 together with the indicated murine STING mutants described in (B). An anti-V5 IP was performed and samples were analyzed by IB with the indicated antibodies. IB shown in (D) representative of three independent experiments.
A. HuH7 cells were transfected with control siRNAs (siCtrl) or siRNAs that target RIG-I (siRIG-I), 48h later cells were infected with a moi 0.3 of HCV and evaluated at 48hpi.
CFSE proliferation assay among naive 2D2 CD4+ T cells stimulated with MOG(35-55) plus DCs treated
16S rRNA gene analysis of luminal samples of wild‐type, ANA‐positive, and ANA‐negative Ltbr−/− mice. Left panel: Beta diversity plot using multidimensional scaling on Bray-Curtis dissimilarities distances. Right panel: Hierarchical cluster analysis using Pearson's correlation. Bacteria community compositions differ in the different groups. Please note that Candidatus arthromitus, according to Thompson et al (), should be renamed Candidatus savagella.
D. Images from primary cilia of MEFs from KV10.1 knockout mice obtained using mAb62 and a rabbit polyclonal anti acetylated a-tubulin antibody. No recognizable structures were stained by mAb62. Scale bar: 1 µm.E. In contrast, mAb62 did stain ciliary-related structures (acetylated-tubulin-positive) in wild type mice. Scale bar: 1 µm.
E Proximity ligation assay (PLA) detecting interaction of ISP1-HA and β-Tubulin at ookinete. Episomal vector as control. Scale bar = 5 μm.
J. siRNA mediated knockdown of VEAL2 significantly changes efflux of dextran conjugated FITC measuring permeability levels. Bar graph representing relative quantification of efflux of dextran conjugated FITC for measuring permeability levels in control siRNA and VEAL2 siRNA transfected HUVECs. Data obtained from 3 different biological replicates and plotted as mean percentage fold change values ± standard deviation.
(B) Representative images of donor (upper panels) and acceptor neurons (bottom panels) after 72 hours in co-culture. Donor neurons were loaded with α-synuclein fibrils prior to co-culture with CTG-labelled acceptor neurons and then cells were labelled either with MAP-2 (first and third panels) or Lamp1 (second and fourth panels). In red: α-synuclein fibrils, in green: CTG, in white: MAP-2/ Lamp1 and in blue: nuclei. Scale bar represents 5 μm.(C) The graph bar shows the percentage of donor (white bar) and acceptor (black bar) neurons containing α-synuclein puncta. Data show mean ± s.e.m.(D) The box plot depicts the number of puncta in donor (white) and acceptor (grey) neurons.(E) Box plot showing the distribution of the average size of α-synuclein puncta in donor (white) and acceptor (grey) neurons.(F) The graph bar represents the percentage of α-synuclein puncta co-localized with lysosomes in donor (white) and acceptor (black) neurons. Data show mean ± s.e.m. Graphs in C, D, E and F correspond to data from 3 independent experiments analysed after 72 hours of co-culture (****, p < 0.0001 compared to donor by two-tailed Mann Whitney test).
b. The K63-linked chain building enzyme Ubc13 with its cofactor Uev1a or the Ubc1 homologue Ube2K (h. sapiens) were employed in single turnover ubiquitination experiments in presence of K63-Ub2 with Ub(K48R) at the proximal or distal position or in presence of K48‑Ub2. Initial rate determination c. Experiment as in (B) but with the Ubc1 homologue ubc-20 (c. elegans).
A) The glycome fingerprint of GluK2/3 was analyzed by lectin chip microarray (LecChip). Lectin PHAL and PHAE (indicated with asterisks) detected reduced amounts of the oligosaccharide Galβ1-4GlcNAcβ1 on GluK2/3 in SEZ6KO neurons (plot shows mean ± S.E.M., 3 WT replicates and 4 SEZ6KO replicates were used, discoveries were determined using the FDR method of Benjamini and Hochberg, with Q = 2%).
(a) Cartoon of the FPP assay illustrating the cellular localization of RFP-SKL (red) and Pex3p-GFP (green) and the position of the fluorescent protein tag relative to its respective membrane. (b) N2a cells coexpressing RFP-SKL and Pex3p-GFP were subjected to the FPP assay. Images were taken before and after 1-min treatment with 20 μM digitonin and 100-s treatment with 4 mM trypsin as indicated. Scale bar, 10 μm.
(B). Protein aggregation in ΔIndLon (upper plot) and ΔIndFtsH (lower plot) mutants grown under inducing (blue) or depleting conditions (red, 48h and 72h of depletion for Lon and FtsH, respectively). Protein aggregates in Triton-X100 insoluble fractions of untreated or heat shock (15min at 45°C) treated cells were measured by thioflavin (ThT) staining. Bars represent the mean of three biological replicates (dots). Significance of comparisons was assessed by two-sided independent t-test (exact p-values are shown).
f-g, Influence of MKS3 depletion on cilia length of RPE WT and SEPT2-KO cells. Cells are treated with the indicated siRNA and serum starved (SS) for 48h before immunostaining with the indicated antibodies. Representative images (f) and quantifications of proximal segment (Glu tub) and whole cilia (ARL13B) length (g) are shown. The numbers above the cartoons in (g) show the ratio of the calculated distal segments/whole cilia length. Scale bar: 2µm. Three 3 biological replicates, n=100 cilia per sample and repetition. Data include mean ±s.d. and P values are calculated by two-tailed unpaired student t-test.
B. Weighted cognitive score of the 132 individuals shows the expected variability. Bar and Error bars indicates mean ± standard deviation.
Flow cytometric analysis of lymph node γδ T cells in RORγtCRE-STAT3F/F (Cre+) and littermate control mice (Cre−). In graphs, each symbol represents a mouse or experiment and line the median. Representative dot plots showing IL-22 and IL-17A production in γδ T cells (A) and frequency of IL-22+ γδ T cells (B) before (steady-state) and after (IMQ) IMQ-induced psoriasis. Steady-state: n = 6; 3 experiments, IMQ: n = 8-9; 3 experiments.
F) Cells were transfected with siRNAs and treated with 10 nM R5020 as indicated, and the levels of repressed genes was measured by RT-PCR. The extent of knockdown was analyzed by western blotting using specific antibodies (lower panel). * P-value < 0.05.
BR1-mediated expression of NEMO or eGFP was driven by the CAG promoter. All animals were at the age of 8-12 weeks.F Effect of AAV-BR1 vector on BBB permeability. No vector (left) or empty AAV-BR1 vector (right) was injected i.v. to wild type mice and BBB permeability was assessed by extravasation of the fluorescent tracer sodium fluorescein (n=7 animals per group). No significant difference was detected (n.s.).
M, N Quantitative analysis of normalized Nod-lacZ intensity for 20 μm of major dendrite located 55 μm or 40 μm away from the soma respectively.
(f) BJAB mCherry-GFP-LC3 cells were sorted for autophagic flux as above and apoptosis was measured at 1 h by flow cytometry using AnnexinV and DAPI (mean ± s.e.m., n = 3 wells, *P = 0.0046).
Western blot analysis of hnRNPLL protein during EB formation of WT ES cells at indicated days.
L The percentage of SEPA‐1 puncta co‐localizing with LGG‐1 in each strain. At least 10 embryos were scored per strain. Data are shown as mean ± SD. **P 0.0001; N.S.: not statistically different.
A. Schematic of drug pulse and wash-out experiment. PeTa cells were treated with 100 nM GSK-LSD1 or DMSO. After 24h, a cell sample was harvested (T0, ON-drug) and the remaining cells were washed and changed into fresh medium without drug. Cell samples were taken 24h, 72h, 6 days (D6) and 8 days (D8) after drug wash-out (OFF-drug) for downstream readouts.
(J and K) Glutamatergic projection neurons derived from FKRP and corrected (5D17, 5D23 and 3B17) progenitor cells. The vast majority of neurons contain vGlut1+ punctae in their neurites (labelled by Tuj1). Right panels are enlarged images from the insets of left panels. Data information: Scale bars, 50 μm.
(C) 3D reconstruction of a high-resolution Z-series confocal image showing PML entrapment of a HSV-1EdC vDNA foci. Scale bar, 2μm. Enlargement of PML entrapped vDNA outlined by white dashed box. Scale bar, 0.5μm. Quantification of PML-NB volume in SCG neurons infected with HSV-1EdC in the presence or absence of IFNα (600 IU/ml). n=64 biological replicates.
Heat map showing the relative expression levels after drug treatment for 48 h in Panc1. Values measured by qRT-PCR were depicted with the software GENE-E. Only mocetinostat upregulated the miRNAs and downregulated ZEB1.
Analysis of nuclear RNA granules in A549 cells with RNase L targeted to the nucleus (NLS-RL-WT) either mock transfected or treated with poly(I:C) (PIC) for 4 to 5 hours. G. FISH analysis to detect poly(A)+ RNA and nuclear speckle-localized MALAT1 RNA and IF analysis with anti-sc35 antibody to detect nuclear speckle protein SRRM2. H. Graph of the mean and value of the intensity of MALAT1 signal divided by the nuclear volume of individual nuclei. 51 nuclei mock treated cells, 56 nuclei PIC treated cells. I. Graph of the median and value of the volume of individual SRRM2 foci in nuclei. Mock 1526 SRRM2 foci in 51 nuclei. PIC 136 SRRM2 foci in 20 nuclei that contain <10 SRRM2 foci.
D: Endogenous MOSPD2 (green) staining in HeLa cells expressing the ER marker GFP-ER (magenta) Data information: (A, D-F): The subpanels on the right are higher magnification (3.5x) images of the area outlined in white. The Overlay panel shows merged green and magenta images. The Coloc panel displays a colocalization mask on which pixels where the green and the magenta channels co-localize are shown in white. Right: Linescan analyses with fluorescence intensities of the green and magenta channels along the white arrow shown on the subpanel Overlay Scale bars: 10 µm
A. The mRNA levels of the indicated ISGs were evaluated by qRT-PCR in RNA isolated from the HuH7 cells described in Fig. 7A.
Pearson and Spearman correlation of the expression of IL6 and TGFBR2 in PDA patients from TCGA (n = 223) using R.
C-D. Evaluation of the effects of UPF2 deletion on Upf3-TAP levels (C in total extracts, in comparison with a loading control (G6PDH) was done by immunoblot
E. U937 (promonocytes) were pre-treated with 50 ng/μL of Vs for 15 min followed by infection with 1 moi of CCR5 using HIV-1 (NL-AD8) and viral replication was measured by gag RT-qPCR at 24 h post-infection (hpi).
A Scatter plot showing the protein levels in wild type cells after 40 minutes of Torin1 (5 µM) addition plotted against the corresponding values for the same protein in Torin1-resistant cells after 40 minutes. Dark grey dashed lines at x = ±1 indicate the 2-fold threshold, of which no proteins exceeded in the study. The light grey dashed line represents y = x, plotted as guide to indicate positive correlation in protein levels between wild type and Torin1-resistant cells.
(C) Phase-contrast images of PABPDHFR cells, or PABPDHFR cells transfected with a plasmid coding for wild-type PABPC1, 48 hours post-TMP removal. Scale bar, 100 μm.
(O, P) Accumulation of endogenous BACE1 in RAB5-positive early endosomes, quantified using Pearson's colocalization coefficient (WT: 0.41±0.01, KO: 0.46±0.02, pWT vs pKO=0.021, 58 WT and 54 KO neurons, N=4 biological replicates). Scale bar: 10 µm. Arrows indicate BACE1 accumulation within RAB5-positive endosomes. Data information All graphs show mean ± SEM, statistical analysis was performed by unpaired two-tailed Student's t‐test n.s.-non-significant. * indicates p≤0.05, ** indicates p≤0.01, *** indicates p≤0.001.
(A-C) Chronological lifespan (CLS) analyses in SC 2% glucose medium of wild-type (WT) cells compared to Δmpc1 (B) cells (see also Figure S3). Survival was determined by colony-forming capacity (clonogenicity). Data represent means ± SEM (n = 4) of a representative aging experiment.(D-F) Propidium iodide (PI)-positive cells analyzed by flow cytometry to quantify age-induced cell death of experiments shown in (A)-(C). Data represent means ± SEM (n = 4) (see also Figure S4).(G-I) Extracellular acetate assessed from crude culture supernatants obtained at indicated time points of experiments shown in (A)-(C). Data represent means ± SEM (n = 4).∗p < 0.05 and ∗∗∗p < 0.001.
D Basal excitatory synaptic transmission of CA3-CA1 connections in acute hippocampal slices treated with DMSO (0.03%), Roscovitine (Ros, 10 µM) or VPS34IN1 (3 µM) plus Roscovitine. Representative fEPSP traces (above) and the relative slope of fEPSPs (below) are shown. Concomitant application of VPS34IN1 and Roscovitine facilitates excitatory synaptic transmission, akin to Roscovitine alone, and in contrast to VPS34IN1 alone N = 6 slices per condition from 6 mice; Student's t-test. Data information: Data presented as mean ± SEM n.s. not significant; *p < 0.05; **p < 0.01; ***p < 0.001
(n-q) IL-17A promotes filamentation in the mutant crf1Δ (o) but not the wild-type AF293 (q) strain after 24-h exposure in liquid culture. Scale bars, 500 μm.
(D, E) Quantification of autophagosomes and autophagolysosomes by transmission electron microscopy. Representative images of HeLa cells transfected with siUNR or with TAB2‐ or TAB3‐targeting siRNAs are shown in (D), and quantitative results are depicted in (E) (mean values±s.d., n=3; *P0.01 versus siUNR‐transfected cells).
(D) Binding activity detection of heterozygous and homozygous CLK19 human BCR KI mice to eOD-GT8. 8-week-old mice were detected by FACS. X and Y axes represent as in (B). (E) Quantification of eOD-GT8 binding in HCLK19/WT κCLK19/WT KI mice. X-axis represents F0 (n=3) and F1(n=2) animals, Y-axis represents as in Figure 2E. Bars indicate mean ± SD from mice in each group.
(H-J) Confocal images of the ventral surface of a Drosophila embryo expressing endogenously tagged mVenus::βH-spectrin (H), the myosin-II marker Sqh::mCherry (I) and a merge of the two (J) with βH-spectrin in green and Sqh::mCherry in magenta. Scale bars: 20 μm.
(A) Simulated changes in the free energy of K+ binding to GltPh induced by different mutations. Values are calculated as differences of free energy changes during alchemical transformations of amino acid side-chains with the protein either in the K1 bound or in the apo state (Mean ± SD of 1000 bootstrap samples).
Elevated PR gene expression in pat1 mutants is suppressed by summ2‐8. Four‐week‐old plants were used for RNA extraction, followed by qRT‐PCR. Fold‐change in PR1 (gray bars) and PR2 (black bars) expression is relative to Col‐0, normalized to UBQ10. Standard error of the mean is indicated by errors bars (n = 3).