EMBO/sd-character-level-ner huggingface dataset:
Gene sets associated with ATRA sensitivityUsing the microarray and RNA-seq data associated with the breast cancer cell lines, two ATRA score-associated gene lists ranked for their variable importance were generated. Upper Panels: The gene-expression results of the first 100-ranking genes in the RNA-seq (left) and microarray (right) datasets were used to perform a cluster analysis of the breast cancer cell lines according to the gene-expression profiles. Data are expressed using a log2 scale of the expression signal intensity after normalization of the data across the different cell lines. The genes marked in red are present in both the microarray and the RNA-seq gene sets. The cell lines marked in red are those belonging to the ATRA score T1 group and are sensitive to ATRA, while the ones marked in blue belong to the T3 group and are refractory to the retinoid. The left dark blue lines indicate the genes with higher levels of constitutive expression in the ATRA-sensitive cell lines, while the light blue lines indicate the genes with higher levels of basal expression in the ATRA-refractory cell lines. Lower Panels: The box plots show the enrichment score (single sample Gene Set Enrichment Analysis, ssGSEA) of the microarray (left) and RNA-seq (right) gene sets in the TN (patients 9, 22, 23, 31, 50) and Lum (patients 13, 18, 27, 36, 41, 44, 55, 60, 61, 62, 64) tumors cultured in the absence of ATRA for 48 h. The P-values of the enrichment are indicated.
Figure 2. Mmi1 binding to nam1 lncRNA controls MAPK-mediated entry into sexual differentiation. (G) Western blots showing the level of Flag-Byr2 protein over the first 4 hours of sexual differentiation in WT and nam1-1 cells. Tubulin (Tub1) level was used as a loading control.
(G) Venn diagram displaying the overlap of Ig domain genes expressed in MNs that are bound by Ubx identified in a neuronal tissue specific ChIP-Seq (Domsch et al, 2019). p-value was calculated as described in (F).
B) Deletion of the N-terminal domain of Sen1 provokes dramatic defects in transcription termination in vivo. Northern blot analyses of three well-characterized NNS-targets, the CUT NEL025c and the snoRNAs SNR13 and SNR33, in a Sen1-AID (auxin-induced degron) strain carrying an empty vector or a plasmid expressing either the wt or the indicated versions of SEN1. Sen1-AID was depleted for 2h by the addition of 500 μM indole-3-acetic acid (IAA) to monitor the capacity of the plasmid-borne versions of SEN1 to induce transcription termination. The expected RNA species resulting from inefficient termination (RT for readthrough species) are indicated. assays were performed in a ∆rrp6 background to detect the primary products of NNS-dependent termination and the U4 RNA is used as a loading control.
B TLR9 recruitment was assessed in WT BMDMs 30 min after infection with eGFP-expressing swollen conidia by confocal microscopy. Scale bar: 10 μm. The arrow indicates a TLR9-positive AF-containing phagosome.
D Caspase activity in HCT116 cells treated as indicated for 24h (NEN 0.6 µM, Imipramine (Imi), Desipramine (Desi) and Amitriptyline (Ami), each 20 µM, Clomipramine (Clomi) 10 µM, A77126 (A77) 50 µM). Data information: data are presented as mean (SD) (N=3) and were analyzed by two-way ANOVA with Tukey post-hoc test
Images COX histochemistry (B) in gastrocnemious of Coq9+/+, Coq9R239X and Coq9Q95X mice; scale bars: 100 μm.
B. Effect of USP44 on USP7 levels. HEK293T cells were transfected with MYC-FOXP3. Cells also received combinations of FLAG-USP7 and varying doses of pLVX-USP44 encoding plasmids. FOXP3 was immunoprecipitated using anti-MYC, and immunoblots were analyzed using anti-FLAG, anti-USP44 or anti-MYC antibodies.
C. RNA Pol II binding at hTR promoter in SI14/TEL+, SI24/ALT+ and 8G12/ALT+ cell lines, normalized to H3 ChIP. Control loci with, respectively, high or low transcriptional activity: c-fos promoter and subtelomeric 4qHox locus (n=3). Statistical analyses were performed using one-way ANOVA with post-hoc Tukey's test for multiple comparisons. Data information: Data are presented as mean ± SD. Statistical analyses were performed with Student's two-tailed unpaired t-test with Welch's correction for normality of distribution unless specified otherwise. PTM, post-translational modification.
D Quantification of ATG9A and AP2 co‐localization. Cells were starved in EBSS media (45 min) or pretreated with Dynasore (15 min) and subsequently starved for 45 min in combination with Dynasore. Control cells were treated with DMSO.
B Test of clotting activity by aPTT and PT at 8 weeks following hydrodynamic tail vein injection of 120 µg pX458 and 120 µg donor plasmids (or 120 µg ssODN) per mouse.
F. GSEA network graph with nodes representing the enriched reactome pathways (at 25% FDR). Node sizes correlate to the normalized enrichment scores, node colors indicate P values (as in color legend) and edge widths correspond to the number of overlapping genes between the connected nodes.
(E) Electron micrographs of kidney proximal tubules in Atg5 F/F and Atg5F/F;KAP mice treated with UA+OA. Yellow arrowhead: autophagosome; asterisk: lysosome; Mt: mitochondrion. Bar: 1 μm.
C Distribution of IDO1.WT and the IDO1.Y149F mutants in homogenates of P1.HTR cells along the isopycnic sucrose gradient as in Fig 3D. Fractions were immunoblotted using antibodies specific for IDO1.
D. Representative images for TIF quantification, as in (A), in U2OS or U2OS-hTR cells, treated as indicated with DMSO or 5 μM ATRi or 5 μM ATMi for 20 h. White arrows indicate TIF. Data information: All scale bars: 5 μm. Data are shown as mean ± SD.
(A) Deletion of EUC1 does not lead to ub-HS adjacent gene deregulation, but rather widespread transcriptome changes. Total RNA isolated from WT and euc1∆ cells was polyA-enriched and sequenced (RNAseq, triplicates). Significance testing was based on the Wald test, see Materials and Methods for details. See also Appendix Fig. S8A for quantification of selected transcripts by qPCR.
C p53+/+ HCT116 cells transfected with control siRNA or SREBP2 siRNA for 72 hours were analyzed by ChIP assay with the indicated antibodies.
M. Proposed therapeutic paradigm. From a therapeutic perspective, intravitreal injection of NRP1-derived traps reduces pathological angiogenesis associated with CNV.
(b) Wild type or STG-p62 Hap1 cells were mock or puromycin treated for 2 hours and stained for ubiquitin. The endogenous p62 was stained with an anti-p62 antibody in the parental Hap1 cells, while the fluorescence of the GFP tag was recorded in STG-p62 cells. Arrowheads indicate co-localizing puncta
(A) Cell lysates from Δapg10 cells (TFD10‐L1) harboring HAAPG12 and each mutant form of HAAPG10 on CEN plasmids were subjected to Western blotting analysis with anti‐HA antibody (mAb 16B12).
F) 3rd instar larval fat bodies were stained by BODIPY (green) for lipid droplets and DAPI (blue) for nuclei. Scale bars represent 25 µm. (F) Lipid droplet size is increased in CSN7 RNAi larvae fed on a 30% high-fat diet. ND: normal diet; HFD: high-fat diet.
A. Average miR expression levels in naive CD4 T cells (purity >97%) before and after 72h TCR-stimulation. Lines indicate changes of +/- 1 log2 fold between samples (n=2, paired pools of three and nine individual samples per library). Library normalization performed using the mean normalization method available in Deseq package of Bioconductor (Anders Huber, 2010). miRs with significant changes are highlighted (black) and with insets presenting mean read counts in unstimulated samples (mean), log2 fold change values in stimulated samples (log FC) and corresponding adjusted p value (p; Fisher test implemented in Deseq). The two most highly expressed miRs (mir-21-5p and miR-146b-5p) are also indicated.
(g) Proliferation of WT and Samhd1 KO clones after stimulation with CIT (n = 2; mean ± sd; two tailed unpaired Student's t-test; ns = not significant).
(A-C) After transfection with UVRAG shRNA or control shRNA for 48 h, HL60 (A), HCT116 (B) and HeLa (C) cells were treated with doxorubicin (Doxo, 1 μg/ml), cisplatin (Cis, 10 μm) and UV irradiation (5 min after 50 mJ/cm2) for 12 h or starvation (HBSS) for 3 h, and then apoptosis and autophagy were assayed (n=3, *P0.05).
D-F: Primary humanCD4T cells were transfected with control or FIP3.1 siRNA. D, E: Cells were allowed to spread on poly-lysine-coated coverslips for 5 min. Intracellular Lck was detected by immunofluoresecence. D: A single optical section at the level of the contact surface is shown. Bar, 10 µm. E: Population analyses of the spreading area of cells at the level of the contact surface.
D. Extracted ion chromatogram of glycero-P-glycerol, an observed metabolite that was not predicted from genomic reconstructions and is significantly elevated in iRBC compared to uRBC. X-axis corresponds to retention time (RT) and y-axis corresponds to arbitrary ion intensity of the extracted peak. Inset indicates the integrated peak area across each cell type and biological replicate.
B This region is represented in more detail, where extended regions of homozygous genotypes in contiguous biallelic polymorphisms are highlighted with a green background.
(D) UVRAG C2 domain deletion terminates BAX binding. HCT116 cells were transfected with Flag‐UVRAG or its mutants (ΔC2, ΔCCD), and then assayed for protein expression levels as indicated by IP or western blot.
Immunoblot of Rad53 mobility shift assay in cells treated with 0.02% MMS expressing either DPB11BRCT3/4 alone or the BRCT3/4-SGS1 chimera. Dilution assay of wild-type, ddc1Δ, or ddc1-T602A cells expressing BRCT3/4-SGS1 in the presence of 0.005% MMS.
(B-F) Representative H&E staining of the histological changes in heart, stomach, tongue and thigh muscle tissues harvested from mice of indicated groups (B). Scale bar, 200 μm. The quantification of histological score was shown in (C-F). Mann-Whitney U-test was used for statistical analysis of two independent groups. Values represent means ± SEM, each symbol indicates the value of 1 mouse from n = 5 mice per group. *, P<0.05; **, P<0.01; ns, not significant.
F. Cellular extracts from MDA-MB-468 were immunoprecipitated with rabbit polyclonal YAP, sheep polyclonal p53 and rabbit polyclonal NF-YB antibodies. Rabbit (for YAP and NF-YB IPs) and sheep (for p53 IP) IgGs were used as negative control of IPs.
(F) QRT-PCR assay of SOX1 after Bufexamac treatment in V1-PAKI cells on day 16 of dorsal neural differentiation, p=0.0283 (V1-PAKI), p=0.0288 (+Buf). Data information: Data are presented as mean ±SEM from three independent experiments (n=3). *p<0.05, **p<0.01, ***p<0.001 versus Ctrl group ; #p<0.05, ##p<0.01, ###p<0.001 versus V1-PAKI group (one-way ANOVA).
(D) Primary β‐cells expressing mtPA‐GFP were photoactivated in seven different regions (squares) and imaged after 2 min and again after 2 h of incubation. Scale bar, 10 μm. *P0.001.
(b) FLAG-EV or RAB2A were transiently co-transfected with EGFP-VPS39 or VPS41 into HEK293T cells. Immunoprecipitated (IP) fraction from cell lysates with anti-FLAG antibody and total lysates were immunoblotted with the antibodies indicated on the right.
A RT-qPCR analysis of the expression of TFEB target genes in WT, GCN5 KO and GCN5/TFEB DKO HEK293 cells. Data information: In this Figure, data are presented as mean ± SEM; n = 3 independent experiments; *p < 0.05, **p < 0.01, ***p < 0.001, Student's t-test.
(E) Sirt5 deficiency leads to higher sensitivity of MEFs to Paraquat. The levels of cleaved PARP and Caspase-3 were determined by western blot analysis.
(A) Immunoblots of protein lysates from ARPE-19 cells infected with either adenovirus expressing Null, TFEB-S211A, or TFE3 upon incubation with DMSO (Control), Tunicamycin (5 µg/ml) or starved in EBSS for 16 h. Data are representative of five independent experiments.(B) Quantification of ATF4, CHOP and GADD34 protein levels in ARPE-19 cells treated as indicated in (A) (mean ± SD of the fold change of the indicated protein to actin ratio from three independent experiments, one-way ANOVA analysis versus the corresponding treatment condition in the adenovirus-Null infected cells, *p < 0.05, **p < 0.01, ***p < 0.001).
B HeLa cells transfected with GFP−parkin (green) and siRNA targeting PINK1 (siPINK1) or non−targeting control (ctrl siRNA), were treated with 25 μM antimycin A for 90 min, then fixed and immunostained for PDH E2/E3 bp (red) and TOM20 (blue). PDH E2/E3 bp−positive/TOM20−negative MDVs colocalizing with GFP−parkin (arrows) or not (circles) are indicated. Arrowheads indicate parkin−positive MDVs adjacent to mitochondria, possibly budding. Scale bar, 20 μm.
G Measurement of cell size, n = 5 per condition. *P = 0.008 versus Ad-cont, #P = 0.02, ##P = 0.03.
Immunoblot of whole cell lysates from multiple human lineage-committed cell-lines using a C-terminal anti-JARID2 antibody. The size of canonical form is 140kDa but an additional strong band was detected at around ~80kDa. The blot is divided according to cell-types, which are indicated in the figure.
C Relative cell density was determined by crystal violet assay. Cells were treated with TAM (10-6 M) or ICI (10-9 M) for 6 days in the presence and absence of E2 (β-estradiol; 10-10 M). Data (mean + SD) were calculated using two-way ANOVA based on three independent biological replicates.
o) Schematic depicting experimental design for panels p and q. 3 month old wild-type mice were injected with murine Cxcl1 for 7 days;
A RNA-seq. of freshly isolated, proliferating and differentiating satellite cells reveals an increased expression of linc-MYH in proliferating and differentiating MuSCs, but no expression is found in in freshly isolated MuSCs.
(F-G) sRNA-seq profiles from EVD de-repressed in the ddm1 (F) or ddm1 dcl1 (G) backgrounds. Different siRNA size categories are stacked. Nomenclature as in (B).
(E) Lysates of Drosophila S2 cells expressing full-length Plin1 or Plin1 with a C-terminal deletion (Plin1ΔC) were immunoprecipitated with anti-Flag antibody and then probed by anti-GFP or anti-Flag antibody in a western blot. Plin1ΔC coimmunoprecipitated with RDH/CG2064.
i-l, Atg5-/- MEFs were transfected with the siRNAs related to the Ulk1 complex (i, j) for 24 h and treated with etoposide for 18 h. Induction of macroautophagy was assessed by Lamp2 IF (i, k)
The amount of CAPZB in mock and Spatc1lΔC-transfected cells. Anti-GAPDH antibody was used as control. Overexpression of SPATC1L in TM4 cells was confirmed by immunoblotting with anti-SPATC1L antibody. Graph shows densitometric analysis of CAPZB in pcDNA3.1 vector-transfected control cells (mock; white bar) and SPATC1LΔC-transfected cells (black bar), expressed relative to control cells (mock) as a percentage. The density of CAPZB in immunoblot analysis was calculated in relation to density of GAPDH.
K Cell survival assay of METTL3-knockdown SMMC7721 cells with overexpressing FOXO3 after treated with sorafenib for 24h under hypoxia condition.
(D) Reduced GABAAR/GlyR intensity ratio at mixed inhibitory synapses (KS test, p < 0.0001). Number of synapses: n = 9416 in TTX and n = 6949 in 4-AP conditions from three independent experiments.
H Immunostaining analysis of the expression of pluripotency marker POU5F1, lineage-specific markers FOXA2, T and NESTIN in Day7 c-MYC-induced EBs at the presence or absence of 10 ng/ml Dox. Scale bars represent 100 μm.
The percentage of E-cadherin+ cells in Oct4GFP+ cells was listed in (D), while the percentage of Oct4GFP+ cells in E-cadherin+ cells was listed in (E).
G. The representative bioluminescence images (left panel) and quantitative growth curves (right panel) of an orthotopic colorectal cancer mouse model, CT26-Luc model (n = 4).
Model of the enzymatic pathway for the Apg12p-Apg5p conjugation system. Apg12p is activated by Apg7p with ATP hydrolysis; the carboxy group of the C‐terminal glycine of Apg12 is conjugated to the thiol group of the cysteine‐507 residue of Apg7p via a high‐energy thioester bond (∼). Subsequent transfer of Apg12p to the thiol group of the cysteine‐133 residue of Apg10p results in the formation of the Apg12p-Apg10p thioester. Finally, the C‐terminus of Apg12p is covalently attached to the lysine‐149 residue of Apg5p via an isopeptide bond, which may require hypothetical Apg5p‐recognizing protein(s).
Tissue topology is affected by disruption of Canoe, but not Mud (D) Statistical significance for cell side distributions was calculated using a chi-squared test. Number of cells analyzed: w1118 1.4-1.6 n=284; Canoe-shRNA 1.4-1.6 n=310; mud3/mud4 1.4-1.6 n=251
B, C Principal component analysis (B) and hierarchical clustering (C) of the transcriptomic datasets of different tissues from young and aged worms in three biological replicates. D1: day 1 of adulthood, D8: day 8 of adulthood. Neu: neuron, Int: intestine, BWM: body wall muscle, Hyp: hypodermis, Coel: coelomocyte.
in vitro binding assays showed the binding activity of TRAF2 and LRPPRC. GST-TRAF2 and His-LRPPRC proteins were prepared from E. coli BL21 cells.
(C) SMAD3 expression in these four subtypes of melanoma cells (U, undifferentiated; NC, neural crest-like; T, transitory; M, melanocytic). Number in each group: U = 10, NC = 14, T = 12, M = 17. Multiple
B. Effect of USP44 knock down on FOXP3 ubiquitination. Two distinct shRNA lentiviral constructs each containing a G418 resistance cassette were delivered into HEK293T cells. After selected for 7d, cells were transfected with MYC-FOXP3 and His-Ubiquitin, then treated with 20 μM MG132 for 4 hrs before harvest and lysis. Ubiquitinated FOXP3 proteins were visualized as in A.
Epidermal thickness of back skin was quantified in H&E stained sections of indicated mice treated with rIL-23 (i.d., 1µg) and/or IMQ for two consecutive days. (n = 4-7; 3 independent experiments). Data information: Data are shown as mean ± SEM. P‐values were calculated by one-way ANOVA with Tukey multiple comparison test Statistical significance: ns > 0.05, *P < 0.05, **P < 0.01, ***P < 0.001, **** P < 0.0001. See Appendix Table S3 for exact P‐values.
P. Quantification of excretion numbers of Drosophila with indicated genotypes. Excretions are quantified in 30 fields for each group of 12 Drosophila. Tests were repeated as three independent experiments. Data information: Error bars represent SDs. p-values for lifespan curves (N) were calculated by the log-rank test. The statistical tests used in other panels were student's t-tests. *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001, and non-significant (NS) represents p > 0.05.
(B) Additional Parp1 knockout in Ews knockout cells (DKO) were subjected to viability test after MMS treatment. Error bars represent as mean ±SEMs, and technical repeats (n=3). Significance determined by Two-way ANOVA, ***P < 0.001. *** indicated differences between DKO with EWS-KO.
(A) cBioPortal was used to access and visualize TCGA data for MIG-6 (ERRFI1) gene expression in 81 cases of invasive carcinoma of basal-like breast cancer Cancer Genome Atlas, 2012(). Each column represents an individual sample.
A. hTR and NHP2 mRNA expression in U2OS-hTR cells 72 h post-transfection with siLuc or siNHP2, normalized to ACTB mRNA and to SI14/TEL+ cells (n=2). Data information: All scale bars: 5 μm. Data are shown as mean ± SD, with the red line marking the mean value.
Quantification of percent Nanog-GFP cells of WT, Kdm3b-KO and Kdm3b-KO pre-iPSC clones expressing Tet1 catalytic domain (Tet1CD), Nanog, or both.
TILs isolated from HER-2-E0771 mammary tumour versus lymphocytes isolated from the contralateral mammary fat pad were analysed for c) CD11b+ F4/80hiLy6ChiLy6Glo myeloid derived suppressor cells (MDSC) by flow cytometry.
Neurons expressing M18Y473D are not impaired at SV docking. Autaptic munc18-1 null hippocampal neurons expressing M18Y473D or M18WT as controls were analysed with electron microscopy on cryofixed samples (I) The active zone (AZ) length is similar (M18WT: 740.2 ± 29.7 nm; M18Y473D: 771.4 ± 28.1 nm, multilevel analysis, p = 0.871).(G-J) M18WT : N=3 independent cultures, n=159 synapses; M18Y473D: N=3 independent cultures, n=156 synapses.
Averaged rundown time constants obtained from fits with monoexponential decay functions as shown in (A).
Interaction between SPATC1L and PKA subunits. Samples precipitated with an anti-SPATC1L antibody were analyzed by immunoblotting with anti-RIα and anti-Cα antibodies. Immunoprecipitation of SPATC1L was confirmed by immunoblotting with anti-SPATC1L antibody. IgG was used as a control. IP, immunoprecipitation; In, input; IgG, immunoglobulin G from normal rabbit serum.
Hypothetical depiction of the Dpb11-STR complex engaged at 5' recessed ends. See text for details. For simplicity, the ssDNA-binding heterotrimer RPA and the obligatory Mec1 cofactor Ddc2 have been omitted from the diagram.
g) p21 positive hepatocytes; h) % p21 positive PCNA negative hepatocytes; i) % p16 mRNA positive hepatocytes; j) % Cxcl1 mRNA positive hepatocytes; k) % of karyomegalic hepatocytes;
B, Cartoon schematic of the two possible translocon outcomes for binding of ColE9 W39A to BtuB and their implications on vitamin B12 import in E. coli 113/3. The W39A mutation within the TBE of ColE9 (orange) impairs TolB (blue) binding thereby uncoupling the OM components of the translocon from the energized TolQ-TolR-TolA complex in the inner membrane. If threading of the ColE9 IUTD through OmpF (green) has no impact on ColE9 binding to BtuB (grey) then vitamin B12 (red) cannot enter cells to support growth. In contrast, if OmpF threading disengages ColE9 from BtuB then vitamin B12 can enter cells to support growth.
E The mRNA levels of Akt2 in WT (n=3) and Ifnar1 KO (n=3) PEMs stimulated with VSV and lipo-ISD for 6 hours were detected by qRT-PCR. Data information: *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001 and ns, not significant (P > 0.05); using two-way ANOVA test Data are from three independent biological replicates Error bars mean ± SEM).
D Immunoblot analysis and quantification of LC3 in HCT116 cells (mean ± SEM). Cultured cells were treated with DMSO (Control (Ctrl)), NEN or NEN and Domperidone (NEN+Domp) as indicated (NEN, 1.2 µM; Domp, 30 µM) for 16 h, followed by control or 20 µM chloroquine treatment for 3 h. Protein band signal intensities were normalized to vinculin (loading control) and the ratios LC3-II bands in presence or absence of chloroquine treatment (N=6) were analyzed by Kruskal-Wallis with Dunn´s post-hoc test. * p< 0.05; *** p<0.001.
Pseudo-coloured scanning electron micrographs of individual outer and inner hair cell bundles from clarinet mice at P8 and P16, showing that gross morphology of OHC and IHC bundles is similar between Clrn2+/+ and Clrn2clarinet/clarinet mice. Representative images from the mid region of the cochlear spiral are shown and close-up views illustrate the three full rows, tallest (red), middle (blue) and short (yellow), of stereocilia in IHC and OHC hair bundles. At P8 and P16 (upper panels in A and B), the three stereocilia rows are observed in Clrn2clarinet/clarinet OHCs (A) and IHCs (B), although the shortest and middle row of IHC stereocilia appear less prolate compared to controls. (C,D) Distribution of individual stereocilia measures across genotypes at P8 and P16.
C. Normalized endpoint NFAT translocation (mean±s.e.m) of control constructs and STIM variants with deleted PBD (∆KK) with or without addition of 1 µM PF-04957325, Kruskalis-Wallis Anova, n=18-19 for ∆KK constructs +/-PF, 56-120 for STIM1, STIM1A controls obtained from three independent transfections. **p<0.01, ***p<0.001 Kruskal-Wallis Anova with Dunn's multiple comparisons test. For clarity, not all differences are shown.
A summary graph of averaged tail current amplitudes as a function of the depolarizing step duration (the numbers on the right indicate the numbers of recorded cells, data are presented as mean values ± s.e.m.)
Summary bar graphs of the frequency and amplitude of the sEPSCs of IPN neurons in TMEM16A cKO (cKO) mice and littermate controls (CTL). Data are presented as mean values ± s.e.m. (paired Student t-test). The numbers inside each bar indicate the numbers of recorded cells.
(A) Schematic depicting the experimental workflow for quantifying p-eEF2 levels and FUNCAT intensity changes on DHPG and NMDA treatment in low-density cortical neurons (DIV 15).