EMBO/sd-character-level-ner huggingface dataset:
The percentage of HIV-Gag p24+ cells from four independent experiments for CEM (n=4) and two for Jurkat (n=2) analysed by flow cytometry were graphically represented as means of HIV-Gag+ cells ± SD. When applicable, student t-test was performed to determine statistical significance (**P<0.01;***P<0.001).
(A) Spontaneous IPSCs were recorded from striatal MSNs (wt=6; R6/2 ACSF=5; R6/2 chol-high=5) at a holding potential of 0 mV.
Scatterplot of DamID-seq signals (log2 ratio) for EGFP (control)-KD (x-axis) or Nxf2-KD (y-axis) samples. Values were calculated for 90 TE consensus sequences (one value per one type of TE) (left). Scatterplot of RPKM values for the same 90 TE consensus sequences in EGFP-KD (control, x-axis) or Piwi-KD (y-axis) samples examined by RNA-seq (right). The signals for mdg1, gypsy, and roo are labelled within the plots.
A, Cell viability of BT308NS, measured 48 h after IR (2 or 5 Gy) in the absence (mock) or in the presence of 10 ng/ml HGF (fold vs. non-irradiated mock treated cells, mock). Ctrl: non-irradiated cells. *: t-test (5 Gy + HGF) vs. (5 Gy), p<0.0001.
C) Computational simulations and microscopy analysis of death time distributions (left, representative data of three independent experiments) and death rates (right, mean of three independent experiments ± standard deviation) in TNF-treated L929 (C) RelA-knockout (KO) cells.
Representative images of IHC staining for CYP46A1 protein in normal brain and different pathological grades of gliomas (n = 64). Scale bar = 30 μm. Quantification of CYP46A1 IHC staining in normal brain (n = 6) and different pathological grades of gliomas (n = 58).
Human S100A9 expression in CHO cells was analysed by immunoblotting or flow cytometry as in Figure 7.
(J-L) Subcutaneous tumor volumes of (J) SW1573, (K) LKR10, and (L) LKR13 cells transfected with sgTom or sgNf1.3 (n=18 each).
B Flow cytometry analysis of cardiacneutrophils 24 hours after ZT13 MI. The dotted line indicates cardiacneutrophil counts 24h after ZT5 MI, shown in Fig. 2A. Student`s t-test; n = 3 mice for isotype and n = 5 for Ly6G injected mice; *P = 0.0004.
B,C. Northern blot analysis of the expression of miR-23a, miR-27a and miR-24 during EB formation (B) and RA induced differentiation of V6.5 ESCs (C). The heatmap was representive of the results of quantitative analysis.
A. Glycogen assay in TFEB-injected gastrocnemii and in the contralateral muscles. In TFEB-injected musclesglycogen levels were significantly decreased compared to those in untreated muscles. * indicates statistically significant differences (p = 1.0 × 10−4; n = 6; Student's t-test).
(J) RNAi mediated depletion of MAVS, RIG-I or MDA-5, reduced their expression levels as compared to siControl (siCtrl) Mean +/- SEM, n=3. Two-Way ANOVA with Sidak's multiple comparisons test, **** (p<0.0001).
CAR (3rd generation) T cells were plated on supported lipid bilayers coated with CD19 and ICAM-1 and imaged by TIRF microscopy. B. Phosphorylated SLP76, recognized by an anti-SLP76 pY145 antibody, was enriched in CAR microclusters in both the wild-type and LAT-deficient cells. In contrast, phosphorylated SLP76 was not enriched in TCR microclusters in LAT-deficient cells. n = 50 cells. Shown are the means ± SE. n.s., p = 0.95 by unpaired two-tailed t-test.
A) Larval VNCs at 24 h ALH from the control (grh-Gal4 UAS-CD8-GFP) and msps810 with grh-Gal4 UAS-CD8-GFP were labeled with E-cadherin, Dpn, and GFP. NSC-neuropil contact were marked by dashed lines, and NSC-neuropil contact points were circled. B) Quantification of E-cadherin basal localization at NSC-neuropil contact sites in qNSCs from genotypes in (A). "No E-cad" means absent or strongly reduced E-cad observed at the basal region of qNSCs. n=32 NSCs for control; n=61 NSCs for msps810. **p=0.0028. C) Quantification graph of the basal E-cad intensity at NSC-neuropil contact sites by normalizing against Dpn intensity in qNSCs from genotypes in (A). n=34 NSCs for control; n=40 NSCs for msps810. ****p<0.0001.
Effects on BDNF promoter III or TrkB promoter. Cells transfected with pIIIBDNF (n = 9), pTrkB (n = 7) or pCRE (n = 5), as a control, were processed as above but using 20 µM NMDA for 4 h. Data are presented and analyzed as in panel A (pCRE, **p = 0.0098; pIIIBDNF, *p = 0.029; pTrkB, *p = 0.033).
(A) PPARγ target genes expression measured by qPCR (n=5-12 each group, two-way ANOVA, post hoc Holm-Sidak comparisons *p<0.05, **p<0.01).
(C) Real-time PCR analysis of the mRNA level of TRIM59 in SNU719 and SNU-4th cells.
(H) Poly I:C did not activate EGFR. STING-/- MEF cells were transfected with cGAMP or Poly (I:C); after 3h, p-EGFR were detected by Western blot.
a) HEK293T cells were transfected with an empty vector (EV) or the indicated FLAG-tagged constructs. 24 h after transfection, cells were treated with either MG132 or solvent for 3 h before collection for immunoblotting as indicated.
Correlation plot showing an anti-correlation between the percentage of CD34+GPR56+ cells in an AML sample and the corresponding IC50 for THZ1 determined in the respective sample. Pearson correlation. Each dot represents one sample.
Left panel) H2A.Z.1 promotes the expression of several cell cycle genes whilst repressing the G1/M checkpoint proteins p21 and p27 thus favouring cell cycle progression. Upon downregulation of H2A.Z.1, the expression of these genes is altered leading to G1/S cell cycle arrest and cellular senescence. Right panel) H2A.Z.2, through its post-translational modifications, regulates the recruitment of several centromeric proteins and contributes to the regulation of the spindle assembly checkpoint. H2A.Z.2 depletion leads to a defective SAC, premature sister chromatid separation and chromosome segregation errors.
(A) 786-0 cells lacking GDH1 with restored expression of WT, ED or 3KR mutant GDH1 were subjected to aa starvation for 24 hours. PI/Annexin V double staining of the indicated cells was performed, and the number of apoptotic cells in each group was calculated. The data are represented as the mean ± SEM of three independent experiments. Unpaired t-test was used with **p < 0.01.
(F) The pedigree is depicted. The patient (II-2) is the second child of non-consanguineous parents.
(A) EI24 knockout promotes ER stress-induced apoptosis. Control (sgCtrl) and EI24 knockout (sgEI24) HeLa cells were treated with the indicated concentrations of tunicamycin (TM) for 8 hr. Percentages of early apoptotic cells were measured by flow cytometry. Data information: N ≈ 10000 cells for one biological replicate. Data are mean ± SEM (n = 3 or 4 biologically independent replicates). ns, no significant difference; ***P < 0.001; two-tailed Student's t-test
VEGFR2 expression is regulated by TFEB. Immunoblots of total lysates from scr-shRNA and sh-TFEB ECs probed with anti-VEGFR2 and α-tubulin Abs. The bar graph shows the densitometric analysis expressed as the ratio between VEGFR2 and α-tubulin
Immunoblot of M2 anti-FLAG immunopurifications from conditioned media of HEK293T cells overexpressing FTTTRA25T and ERdj3WT in the presence of the indicated concentrations of Tafamidis, a kinetic stabilizer of TTR tetramers. Media inputs (1:400) are shown as a control.
M Quantitative analysis of normalized Msps fluorescence intensity in ddaC somas.
(B) Expression of a full‐length MEC‐4::GFP reporter fusion under the control of the mec‐4 promoter in touch receptor neurons of wild‐type, unc‐116 and unc‐104 mutant animals. Representative photos of touch receptor neuron cell bodies are shown. Bar denotes 6 μm. The quantification (%) of GFP signal intensity from the animals examined is graphed below (n=100 neurons per assay; P0.05 compared with wild type; t‐test).
(D) Barplot showing the number of TT-seq enhancer regions per Med1-defined super-enhancer region in LoVo cells. Super-enhancers spanning a protein-coding TSS (n=32) are excluded from this comparison as regions TSS ± 1 kbp were excluded from TT-seq enhancer calling.
CEP41-depleted hTERT-RPE1 cells were transfected with vectors encoding nothing (MOCK), AURKA-T288D, or AURKA-K162R and then immunostained with ARL13b-specific antibodies after serum starvation or serum retrieval. Images were taken from the results of staining done 18 h after serum retrieval. Rectangles indicate the representative cells that appear in the magnified images in the right panels. Scale bars, 20 μm. A quantification of ARL13b-labeled ciliated cells under the indicated conditions in (J). These are the results of three independent experiments with ≥ 200 cells per condition (mean ± SD). *P < 0.05, ***P < 0.01, ns: non-significant (Two-way ANOVA with Tukey's post hoc test).
(U, V) Levels of intracellular Aβ1−42 are significantly upregulated in neurons overexpressing the HA-BACE1-LL/AA-GFP comparing to neurons expressing the HA-BACE1-GFP (BACE1: 0.78±0.90, BACE1-LL-AA: 1.99±0.33, p=000, 28-29 neurons per condition, N=3 biological replicates). Scale bar, 50µm. 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.
(B) Quantification of colocalization of RD-YFP material with p62-positive structures (left graph) or LAMP1-positive vesicles (right) upon K18 fibril-induced aggregation. Confocal pictures were analyzed in 3D with Imaris software from pictures obtained as in A, the graphs represent the mean percentage (+ SEM) of green material overlapping with p62 or LAMP1: aggregates if cells have been converted (agg) or soluble material otherwise. Below each graph, the corresponding Pearson correlation coefficient (PCC) is indicated. The number of cells analyzed over 2 independent experiments is 40, 51, 63, 34 for each respective condition for p62, 36, 59, 44, 27 for LAMP1.
(A) Schematic of the experimental strategy to assess the effects of COCO in the Oxygen-induced Retinopathy model.
CCCP-induced parkin-mitochondrial aggregate formation is an intermediate step for mitophagy. (A) MEFs expressing WT GFP-parkin were treated with CCCP or CCCP and nocodazole (NOC, 10 µM) for 8, 16, and 24 h as indicated. Cells were immunostained with anti-Tom20 to visualize mitochondria. GFP-parkin-positive cells are marked by dotted lines. Arrows indicate parkin-positive mitochondria or mitochondrial aggregates. Bar, 25 µm. (B) The average percentages of cells with mitochondrial aggregates or without mitochondria from three independent experiments from A are presented with standard deviation as error bar. **, P < 0.01.
A, Flow cytometry analysis of PKH-26 staining in irradiated BT308NS, 24 h after the last irradiation. The percentage of PKH-26pos cells is indicated. Ctrl: non-irradiated cells. The mean fluorescence intensity (MFI) was as follow: ctrl, 58.21; 1.5 Gy × 4, 69.35; 2 Gy × 3, 68.20; 5 Gy, 60.29.
B) Epididymal adipose tissueweight in young and old control and Mfn2KO mice (n=6 mice per group).
(D). Role of Lon and FtsH under heat shock stress conditions. ΔIndLon and ΔIndFtsH mutants were grown under inducing (Lon+ or FtsH+) or depleting conditions (Lon+ or FtsH+, 60h of depletion for both, Lon and FtsH), and then exposed at 45°C during 0, 5, 10, 15 or 20 min. Then, growth after the heat treatment was monitored over time under inducing conditions by the 430/560 absorbance rate index that shows pH changes in the medium. The average from two independent biological replicates is shown for each condition.
A) Gene expression of multiple cachexia-associated markers in gastrocnemius muscles of individual animals from Study 1 (n=5 for tumor-bearing groups; n=6 for tumor-free groups). Expression was determined by qRT-PCR and presented as described in the Materials and Methods (Geometric Mean ± Geometric STD). B) Androgen receptor (AR) mRNA expression in gastrocnemius muscles from Study 1. Statistics: p values provided in Appendix Table S5A-B. Dunnett's multiple comparison test. CEBPδ, n=4, insufficient sample to analyze all tumor-bearing GTx-024-treated animals.
A. Enrichment of H3.3 in the rearranged allele of the Ig light chain (IGVLR) compared with the unrearranged allele (IGVLUR). Each bar represents the mean of 3 independent ChIPs each assayed with 3 repeat qPCRs (**** = p<0.0001, unpaired T-test).
C) The human apoptosis antibody protein array supported the important role of the IGF binding proteins (IGFBP-1 to IGFBP-6), the TNF receptor family, and the TRAIL receptors in both cell lines.
A Schematic diagram of humanINPP5E. PRD, proline-rich domain; IPPc, inositol polyphosphate phosphatase domain.
(f) Cells stably expressing WT and D620N GFP-VPS35 were transfected with GFP-α-synuclein A53T and GFP for 48 h and analyzed by western blotting.
Therapeutic effects of GSK-650394 in SNCA-PD model mice. Behaviors (L-N) of the SNCA-PD mice were assessed at 6-12 weeks post- SNCA injection Significantly different at p=0.008#, 0.021*, 0.00001##, 0.0009** in graph L and p=0.00002#, 0.0344*, 0.0005##, 0.0067** in graph M and p=0.0057#, 0.0345* (total distance), 0.0001#, 0.0375##, 0.0338* (average speed) in graph N.
Venn diagrams reporting genes up- or down-regulated by dieldrin or PMA as compared to DMSO.
e. Retrospective immunohistochemistry DAB staining of IgG4 and IgG on archival temporal lobe resection tissue. As suggested by the consensus statement on the pathology of IgG4-RD (Deshpande et al, 2012), three 40x fields with the highest number of IgG4+ and IgG+ cells were selected, counted and averaged within these fields. Cell counts as indicated.
A) The 130 kb human IL3/CSF2 BAC transgene. The insulator (Ins) and enhancer elements (E) are shown as boxes.
E. Carfilzomib, Bortezomib and MLN9708 activate Il-1β-luciferase in M0 macrophages in a dose-dependent manner. BMDMs from Il-1β-luciferase transgenic mice were stimulated by DMSO, Carfilzomib, Bortezomib, or MLN970 at indicated concentrations. Luciferase activity was monitored 12 hours later. Data from three experiments are presented as the mean ± SD.
A schematic summary of our cryo-ET imaging results illustrating how the high-torque motors of Beta-, Gamma-, (top) and Epsilonproteobacteria (bottom) are assembled.
C-D. the yeast strain KT259 (ste11Δ hog1Δ) was used. Data information: Representative results from three independent experiments. Error bars are SEM (n=3).
(C) Representative bright field and immunofluorescence images for localization and expression levels of EMT marker proteins after four days (d4) of siRNA-mediated depletion of factors compared to non-targeting control (NTC). Staining was performed with antibodies against epithelial markers E-cadherin and ZO1, mesenchymal markers Fibronectin 1, with Phalloidin to visualize the actin cytoskeleton and against Paxillin to detect focal adhesion plaques. Scale bar, 100 μm, 40X magnification. Plotted Mean ± SEM of three biological replicates. * p<0.05, ** p<0.01, *** p< 0.001, Student's t-test.
(D) NIH-3T3 cells transduced with retroviral vectors expressing M45 or GFP were stimulated with IL-1β (20 ng/ml, 15 min) or TNFα (10 ng/ml, 5 min). Phosphorylated and total p38 in cell lysates was detected by immunoblotting.
(A-D) Low expression of miR-515-5p is linked to survival in both Lung and Breast cancer. (A) Survival analysis of miR-515-5p from 195 lung adenocarcinoma samples from the TCGA. (B) Survival analysis of miR-515-p from 34 lung squamous cell carcinoma from the TCGA. (C) Survival analysis of miR-515-5p from 60 Breast cancer samples from the Lyng Ditzel Breast Study (GSE37405). (D) Survival analysis of miR-515-5p from 33 Breast cancer from the GSE7405 Breast study. Analysis and plot were obtained with SurvMicro http://bioinformatica.mty.itesm.mx:8080/Biomatec/Survmicro.jsp for (A-C) and with MIRUMIR for (D).
J. HEK293 cells treated for 8 h or 24 h with 100 μM H2O2 in the presence or absence of puromycin (tyrosyl-tRNA mimic used to label nascent proteins), or cycloheximide (CHX, used to block protein translation). Nascent polypeptides were assessed by Western blot performed with an anti-puromycin (anti-PMC) antibody. Vehicle: PBS. β-actin was used as loading control.
vegfr2 (G) mRNA levels were quantified by qRT-PCR in eGFP-positive ECs of control- or cep41-MO-injected Tg(kdrl:eGFP) zebrafish subjected to either normoxia or hypoxia at 30 hpf. The expression of zebrafish β-actin was quantified for the normalization of these qRT-PCR results.
Plasma level of metabolites (other than lipids) that are significantly different between Day 70 vs Day 0 in the CMA and placebo groups after weight loss adjustment are presented. A) Venn-diagram represents the number of significantly different metabolites (other than lipids) on Day 70 vs Day 0 in the CMA and placebo groups. Statistical significance is defined based on paired Student's t test. p< 0.05. 66 and 31 metabolites (other than lipids) were significantly different on Day 70 vs Day 0 in CMA and placebo groups, respectively. The two lists of metabolites had four overlaps.
(A) The ROD-A and ROD-B protomers are related by 2-fold symmetry and interact through two main regions positioned between residues 485-690 and 1790-2125.
(D) COPI vesicles were reconstituted using the two-stage incubation system (detailed in the Methods section). After the second-stage incubation, samples were centrifuged to obtain the pellet fraction that contains Golgi membranes and the supernatant fraction that contains reconstituted COPI vesicles. Both fractions were immunoblotted for LCS, GCS and transferrin receptor (Tfr) to show their relative distributions on Golgi membranes and in COPI vesicles.
E, Bi-FC-based assessment of the inter-neuronal propagation and aggregation of SNCA. Bi-FC+ inclusions (puncta) were counted in E. Data are represented as mean ± SEM. n=5. Significantly different at p=0.0446* in graph E.
Measurements of tumour volume of the respective cohorts (n = 6 animals per cohort). SM represents Birinapant. Error bars represent SD.
J, K Cells expressing tau constructs together with GFP-Parkin (24 h) with and without CCCP treatment. Parkin clusters were counted, illustrating that Parkin translocation was impaired by ∆Tau, but not MTBD. Data were analysed with a Kruskal-Wallis test χ2 (2) = 10.4, p = 0.0056, followed by Dunn's post-hoc, n = 67, 42, 53 cells/ group for for hTau, ∆Tau, and MTBD, respectively. Data information: Scale bars = 10 μm. Data are given as mean and SEM, ** = p < 0.01, **** = p < 0.0001.
B Food intake within 1 h following treatment with candidate genes (dsNPF1-treated, n=4 biological replicates; dsCG10621-treated, n=5 biological replicates; dsMFS3-treated, n=5 biological replicates), the data are shown as the mean ± SEM (Student's t-test, **P<0.01).
Representative micro-CT images at the fracture site showing (from left to right): lateral view of tibia, cross-section, and cross and longitudinal sections with color overlay and 3D reconstruction. In the color overlays, the shade of blue corresponds to percentage mineralization: light blue denotes soft immature callus, whereas dark blue denotes hard mineralized callus. Scale bar, 2 mm.
Immunoblot detection of the glucose transporters, glycolysis and TCA key enzymes in immortalized brown fat cell line (E), BAT from mice fed asparagine (F) and injected asparaginase (G). Asparagine was supplemented to cells during differentiation.
Similarly, IL‐8 secretion from THP1 EV and Sig5 cells was evaluated by ELISA after concurrent exposure with LPS and 10 μg/ml Hsp70. Secretion of IL‐8 was also reduced in only THP1 Sig5cells exposed to both LPS and Hsp70 but not LPS alone.
B. Scatter plot of the mean fold change of transcripts in nmd4∆ RNAseq experiment against transcript mean fold change in ebs1∆ (Pearson correlation, r = 0.66, p-value < 2.10-16). Black dots correspond to NMD substrate examples for which individual traces are shown in Fig. EV3. Dashed lines represent boundaries of five bins of equal numbers of transcripts (2046 transcripts or notable features per bin), with bin 5 containing the transcripts that were most increased in the mutant condition compared with wild type
(Left) Western-blot analysis of CYLD, ROQUIN1/2, MALT1, and BCL10 in total protein lysates from GSC#9 treated for 4 hours with vehicle (H2O) or Z-VRPR-FMK (75 μM). GAPDH served as a loading control. (Right) Densitometric analysis of c'd/FL was performed for ROQUIN1/2 and CYLD. Data are presented as the mean + s.e.m. on 3 independent experiments. Schematic drawing of MALT1 structures highlighting the C464A substitution in the protease-dead version. DD: Death Domain, C-like D: Caspase-like Domain, Ig: Immunoglobulin domain.
LDH-release from MDMs treated as in A. Bars represent the mean percentage of LDH release relative to the total cells lysed, ± S.D. n = 10 and 11 independent blood donors for nigericin and CPPD, respectively.
Kinetics of cluster growth in low salt (25 mM HEPES, 10 mM NaCl) at 30 μM and 50 μM Tau using the same fitting model as in (E).
(A) Fgf8 mRNA expression in E4 chicken right limb bud embryo was analysed by whole-mount in situ hybridisation. The two independent samples of control (2-hydroxypropyl-beta-cyclodextrin (HBC), n = 4, upper panel) and thalidomide-treated (1 µg/µl (3.9 mM), n = 7, lower panel) chicken embryos are shown. Data in bar graph were calculated as relative Fgf8 mRNA expressions with Fgf8 mRNA expressions of HBC as 100. Error bars denote ± standard deviation (HBC, n = 3 or thalidomide, n = 4). P-values were calculated by one-way ANOVA with Tukey's post-hoc test (**P < 0.01).
Pa (Pseudomonas aurantiaca) and Aci2 (Acinetobacter sp.) were co-cultured with a 104 dilution every 24 hours and 0.1%w/v alanine supplied as the only carbon source. Two biological replicates were performed for each of four initial Pa fractions: 0.1, 0.25, 0.75, and 0.9. Population sizes were measured via colony counting after the first, third, fifth, and seventh days (Materials and Methods). With only alanine supplied, Aci2 competitively excluded Pa. An identical experiment was performed with 0.1%w/v glutamate supplied as the only carbon source. Aci2 again competitively excluded Pa.
(D) Quantitative analysis of the efficiency of NHEJ-repair in a reporter cell line, as described in Methods. Cells were cultured in low glucose (5.5mM) or high glucose (30mM) for 5 days, fructose (30mM), ribose (20mM), for 3 days (graph bar 4). I-SceI, untransfected cells served as a negative control. Shown is the average from three independent experiments (mean ± SEM, : p<0.01 : p<0.001).
Quantification of β-MHC transcript abundance N=4 to 18 mice/group, all 6 weeks after TAC or sham surgery.
M, N qPCR analysis of CD38 mRNA levels in heart (M) and diaphragm (N) of WT (n=6) and mdx (n=5) mice. Data information: Each dot of the graphs represents a mouse and measured in duplicate After normality and variance comparison tests, significance was assessed using: M: unpaired Student's t-test; N: unpaired Welch's t-test. Values are expressed as means ± SEM. Significance: *p<0.05, **p<0.01, ***p<0.001.
(C) Poly‐ubiquitinated proteins are reduced in WASH−/− MEFs. WASH+/+ and WASH−/− MEFs were starved in EBSS for 2 h treated with or without 20 nM BafA1 or 10 μM MG132. Cells were harvested for immunoblotting with anti‐poly‐ubiquitin antibody (Enzo, clone FK1) that only recognizes poly‐ubiquitinated ubiquitin chains.
(d) Clearance of soluble EGFP-HDQ74 in stable PC12 cells as in Figure 1b, treated with drugs (concentrations in a) for 96 h. Densitometry is relative to actin. Error bars show s.e.m.
(C) Left- Expression levels of ArfGAP1 and phosphorylation of S6K1 (pS6K1) at threonine 389 (mTORC1 activity) were analyzed by immunoblotting. Vinculin was a loading control. Right- MIA Paca-2 cells stably expressing shRNAs against ArfGAP1 or GFP as a control were treated with mTOR inhibitor Torin 1 (250 nM) or vehicle control for 24 hours, and then cell diameters were determined using a particle size counter. The curves show the overall distribution of cell size in each group. Mean of average size ± SD (N = 4): shGFP Vehicle 19.55 ± 0.10, shGFP Torin 1 18.76 ± 0.12, shArfGAP1 Vehicle 20.63 ± 0.16, shArfGAP1 Torin 1 19.05 ± 0.09. Student's t-test P values: shGFP Vehicle vs. shGFP Torin 1 (P = 4.891E-05), shGFP Vehicle vs. shArfGAP1 Vehicle (P = 2.546 E-05), shArfGAP1 Vehicle vs. shArfGAP1 Torin 1 (P = 2.38 E-06), and shGFP1 Torin 1 vs. shArfGAP1 Torin 1 (P = 0.007).