EMBO/sd-character-level-ner huggingface dataset:
F-I. Representative images of the midgut section from the R4 region of Drosophila carrying esgts-GAL4-driven expression of lacZ cDNA (F, control), Las RNAi (G), Las RNAi and Atg5 cDNA (H), or Las RNAi with spermidine administration (I). GFP (green) and Dl staining (red) was used to visualize ISCs. Data information: DAPI stained nuclei are shown in blue. Scale bars represent 10 μm
Autaptic munc18-1 null hippocampal neurons were rescued with a phosphomimetic Munc18-1 mutant, Y473D or wild-type Munc18-1 as control and assessed on morphology and synaptic transmission using whole-cell patch clamp electrophysiology (D) Left: typical responses to hyperosmotic sucrose application (500 mM, 3.5 sec.) used to assess the RRP. Average RRP charge (M18WT: 1.68 ± 0.64 nC, n=13; M18Y473D: 0.08 ± 0.02 nC, n=10, t-test with Welch correction, p = 0.0274).
B Differential gene expression analysis of ESRP1 knockdown compared to resistant control cells using HTA 2.0 platform; downregulated genes in ESRP1 knockdown (left panel) and upregulated genes in ESRP1 knockdown (right panel) common in 2-control versus 2C3, and 9-control versus 9C2.
(A) Relative cell viability of cells transfected with siCon (WT), siEWS (EWS KD), PARP1 (PARP-1 KD), and double siRNA (DKD) after MMS treatment. Error bars represent as mean ±SEMs, and technical repeats (n=3). Significance determined by Two-way ANOVA, ***P < 0.001. Analysis (***) indicates differences between DKD with EWS KD.
HEK293T cells were transfected with empty FLAG-tag vector as a control or FLAG-Nup50 N-terminal fragment (aa 1-120 of the human sequence). 24 h post transfection cells were lysed, FLAG-tagged proteins immuno-isolated and analyzed by mass spectrometry with the Volcano blot showing the identified interactors of Nup50 (yellow, data from three independent experiments) Data points from individual experiments are indicated. KPNA2 is the gene name of importin α.
A Structure overview of the Munc18-1/Syx1 complex (pdb entry: 3C98). Mutating residues are highlighted in red below the domain depiction and shown as yellow sticks in the structure.
Gene ontology (GO) analysis of biological processes associated with common (C) down-regulated genes in Zfp207-depleted ESCs (sh1 and sh2); NHEJ: Non-homologous end joining.
d. Images of SARS-CoV- and SARS-CoV-2 S-mediated cell-cell fusion on 293T/ACE2 cells at 2 h (left) and 24 h (right).
C Lysates of U2OS cells transfected with siRNA targeting AP2A1, or siRNA control AllStars analyzed by SDS-PAGE.
(J) Quantification of the percentage of ATF4 depleted ARPE-19 cells with nuclear TFE3 upon Tunicamycin treatment for 16 h (mean ± SD of two independent experiments, one-way ANOVA analysis versus siNon-target treated cells within the indicated treatment***p < 0.001; n>400 cells per condition).
(F) Oxygen consumption rate (OCR) normalized to the amount of protein in WT, Mfn1 KO and Mfn2 KO fibroblasts. Proton leak was measured after application of oligomycin (1 μM), maximal after CCCP application (10 μM) and oligomycin (n= 3 independent experiments). Data are presented as mean ± SEM. Data information: *p<0.05, one-way ANOVA followed by Tukey's post hoc test.
A Cell morphology using high-power magnification (40x) of the cultured cell lines under a microscope in LCC2 model-2-control and 2C3 cells. Scale bar: 50 µm.
F Schematic diagram of DJA6 with five different constructs: grey, TP (chloroplast transit peptide, residues 1-85); blue, J domain (residues 86-147); steel blue, GR domain (residues 148-223); cyan, CR domain (residues 224-287); green, C-terminal domain (residues 288-442). The different truncations of DJA6 are shown in detail below.
(B) Plasma magnesium concentration in 34-week-old untreated and treated LmnaG609G/+ mice (n=16).
clone 131 were treated with the indicated concentrations of PH02 (left panels) or PH02 in combination with 10 nM PEP005 (right panels) for 24 h and cells analysed by flow cytometry. Results presented as Δmean fluorescence intensity (ΔMFI) of DsRed expression and fold increase in DsRed expression for solo and combination treatments, respectively. Data Information: Mean and SE are determined from three biological replicates (n=3) and technical duplicates. Statistical significance, as determined by one-way ANOVA is indicated: ****, P<0.00005. The exact P-values are listed in the Appendix Table S1.
(C) Cell lysates from wild‐type cells with empty vector pRS316 (lane 1) or HAAPG12 (lane 2), and also apg10‐1 (lane 3) and Δapg10 cells with HAAPG12 (lane 4) were subjected to Western blotting analysis with anti‐HA antibody (16B12).
E. The normalized in vivo motility of T47DeGFP and T47DDsRed reporter cells in mixed tumors. A Non‑parametric Mann-Whitney U test was used to derive statistical significance. Data information: All data are from n=3 independent experiments. Data are analyzed by Student T-test and represented as mean ± SEM.* p ≤ 0.05, ** p ≤ 0.01, *** p ≤ 0.001, **** p ≤ 0.0001.
A schematic presentation of various signalling pathways leading to AMPK activation and AMPK‐dependent autophagy.
Histological examination of Rosa26_Alkal2;Th-MYCN, Alk-F1178S;Th-MYCN and Th-MYCN tumours was confirmed for NCAM1 and SYP along with MYCN, ALK and ALKAL2 by immunoblotting (E). Immunoblots are representative of 3 independent technical analyses.
(A) Representative sections of spinal cords from tadpoles injected with EdU at 3 dpa and fixed at 5 dpa. After sectioning, the samples were labelled with antibodies against Sox3 (green), EdU (magenta) and DAPI (blue). White arrowheads show Sox3 positive extensions.
AT-3-OVA mammary tumour cells (1x106) were injected into the fourth inguinal mammary fat pads of female Ly5.1+ mice. Seven days after tumour injection FACS-purified 2x106 naïve CD8+CD44loCD62Lhi lymph node T cells from Ly5.2+;OT-1;Ptpn2fl/fl versus Ly5.2+;OT-1;Lck-Cre;Ptpn2fl/fl mice were adoptively transferred into tumour-bearing Ly5.1+ mice. After 9 days the proportion of Ly5.2+IFNγ+TNF+ versus Ly5.2+GrzB+ TILs was determined.
(f, g) MCF10-CA1a (g) cells were transfected with scrambled siRNA (siNC) or siRNA against RAB2A, and immunostained with antibodies indicated on the top (green) and DAPI (blue). Bars, 10 μm.
(A) Confocal images of FIS1 RNAi, DRP1‐DN and control cells coexpressing the AP marker LC3:GFP (green), and stained with MTR (red, control and FIS1 RNAi group) or mtDsRed (red, DRP1‐DN) and treated with pepstatin A and E64d to arrest digestion in late APs. A magnified area within a FIS1 RNAi cell shows APs with and without mitochondria (white and blue circles respectively). Scale bar, 5 μm.
A. SG area in mock, TRAPPC2 TRAPPC3, TRAPPC8, and TRAPPC9-depleted cells treated with SA. Data are shown in box-and-whisker plots: Box-plot central line, median; box limits, upper and lower quartiles; whiskers show the minimum to maximum. N=3. ***p<0.001, ****p<0.0001, One-way ANOVA with Dunnett's multiple comparison test.
D Co‐immunoprecipitation of HA‐Flag‐TBC1D5 with myc‐VPS29, transiently overexpressed in 293T cells, DMSO or KU0063794 (6 h) treated.
Relative levels of c-di-GMP in matched cell biomass host-independent (HI) cultures of bd1971::kan compared with fliC1 merodiploid KnR HI control strain (Wild-Type for bd1971). The bd1971 mutant strain contains significantly more c-di-GMP than the control. Data are from 3 independent experiments.
mRNA expression of target genes, n=5 or 6 independent human samples. Paired student t-test.
(f) Liver function tests of the mice used in d. The serum levels of aspartate aminotransferase (AST), alanine aminotransferase (ALT) and alkaline phosphatase (ALP) were measured. (IU/L, international unit per liter). Data are means ± s.d. for seven mice from each group. Asterisk, P 0.05; three asterisks, P 0.001.
(G) The activities of G6PD/6PGD and IDH1/2 are reduced in stable HEK293T cells with SIRT5 knockdown. Activities of the indicated endogenous proteins were determined in cell extracts as described in 'Materials and Methods'. The results are average ± SD of 3 independent experiments *p<0.05, **p<0.01, ***p<0.001, n.s.: not significant (two-tailed unpaired t-test).
E. Number of filopodia detected in co-cultured HUVECs (n=30 cells; **P<0.01; unpaired t test)
B, Cartoon of the ColE9 OM translocon. ColE9 (orange) exploits the vitamin B12 transporter BtuB (grey) as its extracellular receptor and the porin OmpF (green) for threading its N-terminal IUTD (solid black line) through to the periplasm where it captures TolB (blue). Star, represents the primary site on the ColE9 DNase domain (K469C) where fluorophores were covalently attached throughout this study.
(F) Upper panel, Distribution of distance to nucleus, normalized on cell size, quantified by image (as in e) segmentation (see Material and Method, Confocal microscopy and early/late quantification) of LAMP-1+ endosomes. Results are from of two independent experiments for a total of 436 late endosomes in 13 shCTL/GFP cells (34 ± 6 endosomes per cell), 1452 late endosomes in 12 shSTIM1/GFP cells (121 ± 13 endosomes per cell) and 498 late endosomes in 10 shSTIM1/GFP-STIM1 WT cells (50 ± 5 endosomes per cell) and analyzed by a parametric two-tailed analysis of variance (ANOVA) with Bonferroni post hoc analysis. ANOVA p≤ 0,01; Bonferroni for shCTL/GFP and shSTIM1/GFP p≤ 0,001 *** (orange) and for shSTIM1/GFP and shSTIM1/GFP-STIM1 WT p≤ 0,001 *** (green). Lower panel, Distribution of distance to nucleus, normalized on cell size, quantified by image (as in e) segmentation (see Material and Method, Confocal microscopy and early/late quantification) of LAMP-1+ endosomes. Results are from of two independent experiments for a total of 498 late endosomes in 10 shSTIM1/GFP-STIM1 WT cells (50 ± 5 endosomes per cell), 1057 late endosomes in 11 shSTIM1/GFP-STIM1 NN cells (96 ± 12 endosomes per cell) and 346 late endosomes in 10 shSTIM1/GFP-STIM1 AA cells (35 ± 2 endosomes per cell) and analyzed by a parametric two-tailed analysis of variance (ANOVA) with Bonferroni post hoc analysis. ANOVA p≤ 0,01; Bonferroni for shSTIM1/GFP-STIM1 WT and shSTIM1/GFP-STIM1 NN p≤ 0,05 * (orange) and for shSTIM1/GFP-STIM1 NN and shSTIM1/GFP-STIM1 AA p≤ 0,05 * (green).
(A,B) HL60 and HCT116 cells were treated with UV irradiation for 24 h and then assayed for protein expression levels as indicated by co‐immunoprecipitation (RIPA or CHAPS buffer) or western blotting.
c, Immunohistochemistry of liver sections from control (Atg5flox/+; CAG-Cre) and Atg5flox/flox; CAG-Cre (Atg5flox/flox) mice at four months of age, using an anti-ubiquitin antibody. Scale bar, 25 µm.
Tor, Tsc1, Rheb, Atg5 and Atg7 genes expression was silenced in per-positive cells. Period of locomotor activity rhythm was measured in DD conditions (mean +/- SE). Representative actograms were presented. As a control, the progeny of per-Gal4 and UAS-Val10-GFP crossing was used. After silencing the Tor gene, the period of locomotor activity rhythm was significantly shorter than in the control [U Mann-Whitney Test, *** for p≤0,001]. Silencing the Tsc1 gene caused a slight lengthening in the period of the rhythm.
(A) ssDNA repair efficiency of cells expressing RAD18 from the GAL1 promoter as determined from the maximal and final percentages of cells with Rad52 foci during the time course (right panel). Cells were synchronized in G1 from galactose-containing medium and released into S phase in the presence of 0.033% MMS for 1 hour, treated with 2.5% sodium thiosulfate to inactivate the MMS, washed and released into fresh medium for different times. Cells were shifted to glucose-containing medium 1 hour after MMS inactivation. The percentage of cells with foci at each point was normalized to the highest value of the wild type, taken as 100 (left panel). See Figure EV1A for control cells released in galactose-containing medium during the entire time course. Data information: The mean and SEM of 4 independent experiments are shown. Statistically significant differences according to an unpaired two-tailed Student's t-test are shown, where one, two and three asterisks represent p-values <0.05, <0.01 and <0.001, respectively.
(c,d) Animals overexpressing LIPL-1 or LIPL-3 were incubated at 25 °C and transferred every other day until cessation of reproduction. Data presented as in Fig. 7a show that activated lysosomal lipolysis extends C. elegans lifespan. a Survival presented as mean lifespan (LS) ± s.e.m. b Number of uncensored animals (animals that crawled off the plate, bagged, exploded or became contaminated were censored).
(B) Quantification of vessel sprouts (mean values ± S.E.M.) upon VEGF treatment (30ng/mL) of embryoid bodies (EB) derived from murine ES cells (mESCs) with sense integrations in the Apelin gene (Apln STOP) of the splice acceptor described in Appendix Figure S1B or Cre-reverted antisense (Apln GO) sister cells. Apln GO (Day 2 n=6; Day 4 n=40, Day 6 n=54, Day 8 n= 32, Day 10 n=35, Day 11 n=31), Apln STOP (Day 2 n=4; Day 4 n=15, Day 6 n=31, Day 8 n= 28, Day 10 n=32, Day 11 n=37); ** P<0.01, *** P<0.001, two-way ANOVA. Representative brightfield images and automated analysis of vessel sprouts by Definiens software are shown in the bottom panels. Scale bars = 200 μm
(C) PHR1 enhances the growth of Pto DC3000 under Pi-starvation conditions. Col-0, phr1 mutant and PHR1-Myc overexpression seedlings grown in either HP or LP media were root inoculated (by soaking) with a bacterial suspension (OD600 = 0.2) for 2 min, and the number of bacteria from individual roots was quantified at 5 dpi. The data shown indicate the means ± SDs (n = 18, n refers to the number of roots per group). The different lowercase letters indicate statistical significance (one-way ANOVA). Data information: All experiments were repeated three times with similar results.
Eight weeks after AAV injection into right EC of aged Mapt0/0 mice (=3), immunostained brain sections showed that huTauP301L (red) propagated to a few DG "recipient neurons" (white arrows). Scale bar 50 µm.
d, Localisation of Atg18-GFP 5 min after salt shock. Experiment as in a. Scale bar: 1 µm.
C, A549 and H358 cells expressing mCHerry-GFP-LC3B were treated with vehicle (DMSO), AZD 4547 (5 µM) and BI2536 (5 nM), alone or in combination for 24h before flow cytometry-based analysis for mCherry and GFP (upper). Shown underneath is quantification of the data. **P<0.01 and ***P<0.001 by two-way ANOVA with Tukey's multiple comparisons test. Data are shown as mean ± SD (error bar) of three independent experiments (n=3).
M238P cells were treated 72 h with BRAFi (Vemurafenib, 3 µM) or with a combination of BRAFi (Vemurafenib, 0.5 µM) and MEKi (Trametinib, 1 µM). Effect of BRAFi or BRAFi plus MEKi on MRTFA (D) nuclear translocation by immunofluorescence. Data are represented as scatter plot with mean ± SD (n≥30 cells per condition). Each point represents the nuclear/cytoplasm ratio. Mann-Whitney U test was used for statistical analysis. ***P≤0.001, ****P≤0.0001. Scale bar 40 μm.
(D) Immunoblots of protein of a GST pull-down from nuclear fractions of MEF cells treated with DMSO or Tunicamycin (5 µg/ml) (Tun.) for 16 h. Data are representative of three independent experiments.
A) Boxplots showing all-atom analysis of GK energetic contributions to a set of native folds from the E. coli cytoplasmic proteome. The upper whiskers indicate the largest value no further than 1.5 times the Inter-Quartile Range (IQR) from the upper hinge, the lower whiskers show the smallest value at least 1.5 * IQR from the lower hinge. Notches extend 1.58 * IQR / sqrt(n) from either side of the median and represent a 95% confidence interval for the median value. Grey shaded area indicates total energy associated with the placement of GKs in the native fold, the remainder of the plot shows the breakdown of this total energy into constituent energy terms. The number of observations per GK is indicated above the boxes depicting the distribution of the total energy for each of the GKs.
Representative BCECF-AM 490/440 nm ratio trace. Ratio of 545 nm fluorescence intensity at either 440 or 490 nm excitation. Dashed lines are where light or FCCP treatment occurred. Light green trace is from mitochondria with ATR, gray traces are without. Quantification of change in BCECF-AM fluorescence ratio normalized to maximum change given by succinate matrix alkalization. Two-way ANOVA with Sidak's test for multiple comparisons, -ATR succinate vs. -ATR, +light *p = 0.0212, +ATR succinate vs. +ATR light p = 0.999, +ATR succinate vs. +ATR,-light p = 0.0237, +ATR, +light vs, +ATR, -light p = 0.0474, n = 3 mitochondrial isolations. Some individual points overlap. Data show mean ± SEM.
J. qRT-PCR analysis of the relative mRNA expression levels of AKT2 (left panel) and IFNA (middle panel) or IFNβ1 (right panel) in CD14 positive monocytes isolated from SLE patients (n=9) or healthy donors (n=9). Data information: *P < 0.05, **P < 0.01 and ****P < 0.0001; using unpaired t-test or correlation analyses Data are pooled from different individuals Error bars mean ± SD).
B) Time-resolved Dynamic Light Scattering (DLS) analysis indicating average particle size over time for each of the peptides in the β-Gal peptide set (aggregating core sequence SVIIWSLGN).
Generation of oncospheres in SUM159 cells expressing constitutively active JNK or inactive mutated JNK. Values are mean from 10 wells per group ± SD.
Saturating MET currents recorded from a P7 Clrn2clarinet/+ (F) and a P8 Clrn2clarinet/clarinet (G) apical-coil IHC using the same experimental protocol described above.
(a-c) Reprogramming is more efficient after MBd enrichment. Differentiated cells (dH1f) and embryonic fibroblasts (IMR90) are reprogrammed after stable expression of either NBR1 shRNA or shNT. Emerging iPSC colonies are scored on the basis of TRA-1-60 expression. Cells depleted of NBR1 to increase MBd levels show an increase in iPSC colony formation (a,b, dH1f, 3.1±0.5-fold, n=15, P=0.00035; IMR90, 3.4±0.8-fold, n=3, P=0.02; data are mean±s.e.m.) but insignificant changes in autophagic activity (c) over shNT control. (b) Representative plates with TRA-1-60-immunostained iPSC colonies. The immunoblot (c, top) and densitometry (c, bottom; percentage of autophagic flux) show representative results (n=3); α-tubulin, loading control.
B. Frequency of newly formed filopodia formed within 5 µm intervals relative to the nearest MCP-GFPnls particle or a randomised (ctrl) position (n=99 filopodia; **P<0.01, ns: not significant; Pearson r correlation).
D. Representative confocal images (upper row) and quantification of fluorescent intensity of ALDH1 expression in MDA-MB-231 cells expressing RASSF1C (black bar in the graph) or after siRNA treatment against RASSF1 (grey bar). Lower row shows merged images with DAPI (blue), ALDH1 (green) and RASSF1C (red). Scale bars represent 20 μm. Data Information: All data are from n=3 independent experiments. Data are analyzed by Student T-test and represented as mean ± SEM.* p ≤ 0.05, ** p ≤ 0.01, *** p ≤ 0.001.
C Quantification of PDHE2/E3 bp−positive/TOM20−negative structures from (B); both the total number (white bars) and the number colocalizing with GFP−parkin (gray bars) are indicated. Error bars represent the mean ± s.e.m. P−values are given first for GFP−/GFP−parkin−positive vesicles, then for total vesicle number (n = 42-60 cells in three experiments); ns, not significant; ***P < 0.001).
(C) Altering fission does not impair ER autophagy and AP or lysosomal mass. INS1 cells expressing LC3:GFP were stained with ER Tracker to assess AP‐containing ER. The number of AP‐containing ER was not significantly different between control and FIS1 RNAi cells (P=0.51; n=11). Lysosensor stain (75 nM, 30 min) reveals no difference between control and FIS1 RNAi cells (P=0.21). The total AP number in DRP1‐DN cells is similar to that of the control (n=11, P=0.53).
RT-PCR results showing that YAP stimulates the mRNA expressions of EGFR, AREG, and TGF-α in ME180 cervical cancer cell. Data were analyzed for significance using one-way ANOVA in GraphPad Prism 5 with Tukey's post hoc tests. Each bar represents mean ± SEM (n = 4). Bars with different letters are significantly different from each other (YAP mRNA: MXIV vs. YAP, P = 0.0003; MXIV vs. YAPS127A, P = 0.0001; EGFR mRNA: MXIV vs. YAP, P = 0.0066; MXIV vs. YAPS127A, P = 0.0003; TGF-α mRNA: MXIV vs. YAP, P = 0.0235; MXIV vs. YAPS127A, P = 0.0040; AREG mRNA: MXIV vs. YAP, P = 0.0002; MXIV vs. YAPS127A, P < 0.0001).
(B) U2OS and two Ewing Sarcoma cells were treated MMS (0.02%, 30 minutes) and subjected to immunofluorescence by PARP1 antibody after chromatin bound fraction. Scale bar indicates 20 μm (left). Red line indicates mean and more than 300 cells were analyzed. Significance determined by Two-way ANOVA, ***P < 0.001.
Magnetic resonance imaging (MRI) analysis was performed on five animals/experimental group on day 24. The picture shows representative 2D images of tumor sections from one animal treated with vehicle and one animal treated with 15.0 mg/kg ATRA. The bar graph shows the volume of the tumors calculated after 3D reconstruction of the MRI images. Each point is the mean ± SE of five tumors. The P-value of the comparisons of ATRA versus vehicle is shown.
(A-F) HeLa cells stably expressing GFP‐LC3 were transfected with mStrawberry‐Gal3, and treated with 1000 μM LLOMe for 1 h. Then, cells were fixed and observed by confocal microscopy (A). The same specimens were further examined by transmission electron microscopy (B-F). Green: LC3; magenta: Gal3; blue: DAPI.
B Animals were injected by rAAV9-CUEDC2 in a different amount of viral genomes (VG). Heart tissues were then analyzed by immunoblotting to detect CUEDC2 transduction. Tubulin protein level was examined for normalization purposes.
C, Mean ChIP-seq signal for USP22, GCN5, and ATXN7L3 surrounding gene promoters from B. Nonparametric Mann-Whitney analysis of 7 bins (grey shade) surrounding maximal peak in Thaps treated conditions are reported.
Schematic cartoons showing the proposed positive feedback loop in cervical cancer cells. Data in this study support the existence of an autocrine loop involving EGF-like ligands/EGFR pathway/Hippo pathway/EGF-like ligands in regulating the proliferation and motility of cervical cancer cells, which plays a critical role in cancer progression. Under normal conditions, low levels of EGF-like ligands such as TGF-α and AREG are not sufficient to activate EGFR. The inactive EGFR ensures the activation of Hippo signaling pathway, which in turn results in ubiquitination-dependent degradation of YAPprotein. In cervical cancer tissues, especially the advanced-stage cancer tissues, the elevated nuclearYAPprotein stimulates the expressions of TGF-α and AREG, which in turn activates the EGFR, leading to suppression of LATS1 and MOB1 phosphorylation. Dephosphorylation of LATS1 and MOB1 results in the dissociation of LATS1/2-MOB1 complex, leading to inactivation of the Hippo pathway and subsequent activation of the growth-promoting co-activator YAP. Activated YAP induces expression of growth factors such as TGF-α and AREG to drive cervical cancer growth. YAP-induced growth factors such as TGF-α and AREG complete the autocrine loop by activating EGFR and YAP to drive the proliferation of cancer cell and the production of growth-promoting factors in cervical cancer cells. HPVE6 protein maintains YAPprotein level in the HPV-infected normal and cancerous cervical cells by preventing YAP from proteasome-dependent protein degradation.Schematic cartoons showing the clinical relevance of the proposed positive feedback loop in cervical cancer. Multidimensional cancer genomics data analysis indicates that very high frequency of alterations has been observed in genes involved in the Hippo/YAP/EGFR positive feedback loop in cervical cancer (we acknowledge The Cancer Genome Atlas (TCGA) Data Portal for the datasets and the cBioPortal for Cancer Genomics for the online analysis tools).
Schematic representation of the UPAX strategy for phosphopeptide enrichment and MS/MS analysis.
D‑F, Linear regression analysis of SAGA member recruitment to target gene promoters following induction of ER stress.
(B) The categories of the compound library. 3,375 compounds were printed on the chip, including 1,527 FDA-approved drugs, 1,053 natural products and 795 known inhibitors.