EMBO/sd-character-level-ner huggingface dataset:
D) Assembly of sEcGFP-tagged subunits CoxVIIIa-sEcGFP (CIV#) into complex IV, and assembly of subunits γ-sEcGFP (SUγ#) and SU e-sEcGFP (Sue#) into ATP synthase. Proteins were separated by BN-PAGE and immunoblotted. Lanes #1-#10 were cut into three pieces for further evaluation. Lanes 1-2: complex IV assembly in WT and CoxVIIIa-sEcGFP-expressing cells, detection of CIV with anti-Cox1. Lanes 3-4: complex V assembly in WT and SUγ-sEcGFP-expressing cells, detection with anti-SU γ. Lanes 8-10: assembly of CIV# into CIV, SU γ-sEcGFP (SUγ#) into CV, and SU e-sEcGFP (SUe#) into CV. At lane #6 in the Coomassie-stained gel, the positions of molecular weight markers (M) are shown. SC: respiratory supercomplexes; CIV2: complex IV dimers; CIV: complex IV monomer; s1: F1-c8 subcomplexes; s2: subcomplexes of CV containing subunits b, e and g He et al., 2018(). Blue **: dimeric F1F0 ATP synthase; blue*: monomeric F1F0 ATP synthase. Red asterisks: respiratory supercomplexes
(b) Atom tracing of TCA cycle metabolites from [U-13C]-glucose (blue) and [U-13C]-glutamine (red).
Overexpression of IRE1α K481R induced apoptosis. or subjected by immunoblotting with indicated antibodies (D).
(A-C) Kyoto Encyclopedia of Genes and Genomes (KEGG), Gene Ontology (GO) and REACTOME Pathways (27.02.2019) enrichment analyses of differentially expressed genes in stimulated sh-NC vs sh-p38IP Jurkat E6.1 T cells (fold change >2, P<0.05), showing the top 8 significantly enriched terms.
C. HY5 directly binds to the ACE-box of FER promoter in vitro. Recombinant HY5 was purified from E. coli cells and used for DNA binding assays with probes of FER-wt, and FER-mut. The protein purified from empty vector was used as the negative control. One thousand-fold excess of unlabeled probe was used for competition. WT and HY5-OE plants were exposed to white light (200 µmol m-2s-1) grown under Fe-deficient (2 µM, -Fe) conditions for 7 d.
Quantification of the pAMPK to AMPK ratio (left) and the pACC to ACC ratio (right) relative to the untreated control (n=3). Cellular ATP content quantified as a percentage of the untreated control (n=3).
C. Quantification of colocalized GFP-LC3 and mCherry-capsid puncta normalized to the number of mCherry-capsid puncta per cell (% colocalization) in the experiment shown in (B). Bars are mean ± SEM of triplicate samples (~100 cells analyzed per sample). Similar results were observed in more than three independent experiments. ***p<0.001; one-way ANOVA with adjustment for multiple comparisons. See Fig EV1A and B for quantification of mCherry-capsid puncta per cell and GFP-LC3 puncta per cell from the same experiment.
BR1-mediated expression of NEMO or eGFP was driven by the CAG promoter.D Body weight of vector-treated mice. WT control or Nemo-/+ mice at P8 treated with AAV-BR1-NEMO or AAV-BR1-eGFP (n= 18 animals/ group, *p = 0.0038).
(A) Stills from time-lapse sequence of representative Hela cells expressing Lifeact-GFP and H2B-mCherry, exiting mitosis under different conditions i.e. Control siRNA and knock-down of centralspindlin protein RACGAP1. Scale bar- 10µm
(B, C) RNA-seq experiment on WT (JLB130) and ΔsigV (JLB154) strains, showing quantification of the absolute expression of individual genes in the presence and absence of lysozyme stress. The shaded grey box represents a ± 5 fold change. DEseq was used to identify genes which were differentially expressed with a 5% p-value cutoff between the WT and ΔsigV mutant in response to lysozyme treatment (default DEseq test was used). (B) Only the sigV operon is strongly activated (>5 fold change) in response to lysozyme stress in WT (JLB130), as previously reported (Guariglia-Oropeza and Helmann 2011). (C) No genes were strongly upregulated in ΔsigV (JLB154) by lysozyme stress.
Lipid peroxidation was measured by C11-BODIPY 581/591 after cold stress for 5 h. Representative plots are shown in (B Quantification data (C whose raw value were normalized by the C11-BODIPY 581/591 without cold stress of non-treatment, are presented as mean ± SEM; n = 4 (C) biological replicates. ***p < 0.001, **p < 0.01 by unpaired T-test.
Gene ontology (GO) enrichment of the above 29 RBPs. The node size of enriched GO terms indicates the number of enriched RBPs, RBPs with the same domains (e.g. RPM) are clustered and filled with the same background color. The domain names are labeled around enriched RBPs.
(B) Confocal analysis of the indicated proteins in Min6 cells. Min6 cells were intracellularly stained with anti-Pdia4 and anti-Ndufs3 antibodies plus MitoRed (top). Min6 cells were surface stained with anti-Pdia4 antibody, followed by intracellular staining with anti-p22phox antibody (bottom). Scale bar = 5 μm.
C. Topology diagrams of a classical Rab GTPase and of IFT22. Positions of the conserved nucleotide-binding G-motifs (G1-G5) as well as switch regions are indicated.
(C) Probability density distribution for HP2 opening in WT and R479A EAAT1 (GltPh R397).
Screen captures from UCSC genome browser showing regulatory elements containing HERV-derived sequences with transcription correlating with that of a nearby gene annotated as linked in the GeneHancer database.
B. Seurat UMAP of MM074 treated with siCTL or siSOX10 (24h, 48h and 72h post-treatment). The arrow indicated the trajectory from control to 72h post siSOX10 transfection.
(B) Gene Ontology (GO) analysis of genes analyzed in the previous panel. Shown is a list of process networks with statistical significance of enrichment in Black HKCs. The complete list is provided in Dataset EV1.
(D, Tumor progression in mice, transplanted with Pax5Jak2-Luc/+ tumor cells, in the presence or absence of the JAK1/2 inhibitor ruxolitinib. At day 14 after cell transfer, the transplanted mice were treated twice daily with ruxolitinib or vehicle, and the tumor mass was monitored by bioluminescence measurements. Images of three representative mice with or without ruxolitinib treatment are shown
(D) HMGB1 direct interactions with Bcl-2 are dependent on Beclin1. Knockdown of Beclin1 and Bcl-2 by siRNA in HMGB1 wild-type MEFs was performed, and protein expression levels were then assayed as indicated by co-IP or Western blotting. Ctrl, control.
b. Multivariate modelling of the lipidome in cells treated with DFP over time. Sparse PLS-DA (sPLS-DA) was performed using Metaboanalyst from LC-MS datasets from three independent biological experiments each with four technical replicates per time point in each experiment.
(A) ADAR2 is most strongly expressed in vascular tissues. Graph showing ADAR2 gene expression data derived from GTEx for few representative human tissues. Note the highest expression of ADAR2 in the tibial artery followed by colon and esophagus. Boxes represent the 25th and the 75th percentile with median represented by the black line in the box. The whiskers depict the minimum and the maximum value.
A Quantitative RT‐PCR analysis of EMT‐related markers obtained from tumors derived from mice of the indicated genotypes (n = 3, means ± SD).
A ABR thresholds recorded prior to (gray plot) or at day 28 in HBCx-90 (TP53 wt) bearing-mice received systemic treatment with: DMSO (black plot), PFT-α (yellow plot), CDDP (green plot), CDDP+PFT-α (pink plot).B Mean ABR threshold from 4 kHz to 32 kHz derived from A. Data are expressed as mean ± SEM (before: n=20; DMSO: n=5; PFT-α: n=5; CDDP: n=5; CDDP+PFT-α: n=5). One-way ANOVA test followed by post hoc Tukey's test (***P = 0.0002, CDDP vs. before; CDDP vs. CDDP+PFT-α.E ABR thresholds recorded prior to (gray plot) or at day 35 in HBCx-14 (TP53 mutant) bearing-mice received systemic treatment with: DMSO (black plot), PFT-α (yellow plot), CDDP (green plot), CDDP+PFT-α (pink plot).F Mean ABR threshold from 4 kHz to 32 kHz derived from E. Data are expressed as mean ± SEM (before: n=30; DMSO: n=5; PFT-α: n=5; CDDP: n=10; CDDP+PFT-α: n=10). One-way ANOVA test followed by post hoc Tukey's test (***P = 0.0003, CDDPvs. before or CDDPvs. CDDP+PFT-α.
i & j, Representative images of depth colour coding (ImageJ) of x,y,z live imaging of Nrl.Gfp+/+ photoreceptor cultures showing (i) neurites (blue arrows) growing along the substrate (asterisks denote secondary branching of long GFP+ neurites), and in (j), a free-floating PhNT (magenta arrow). Scale bar = 10 µm;
(C) Colocalization between bacteria, TMEM59-HA and Cherry-ATG16L1. HeLa cells stably expressing TMEM59-HA and Cherry-ATG16L1 were infected with SA (2 h, moi=10), and processed for anti‐HA immunofluorescence. Shown are confocal pictures displaying two representative examples. Asterisks indicate overlays as in B.
G-H. Confocal single plane images of 1151>mCherry-RNAi and 1151>Ama-RNAi wing discs stained with anti-Zfh1 (green) and (G) anti-Nrt (white) at wandering third instar larval stage (110 - 135 h AEL) or (H) DAPI (red) at early third instar larval wing discs (72 - 110 h AEL).
D Induction of the secondary (2nd) axis by hwa or znrf3 as indicated in Xenopus embryos. One ventral blastomere of 4-cell stage embryos was injected with hwa mRNA (5 pg) or hwa10KR mRNA (5 pg) and znrf3 mRNA (100 pg). Up: Classes of embryos. Down: Ratio of classified embryos. The 2nd axis (red arrowhead). Scale bars: 1mm.
Sholl analysis of basal dendritic length reveals a significant group effect (repeated measures ANOVA: genotype F(2, 29)=5.038, p<0.05) and a significant distance effect (repeated measures ANOVA: genotype F(5, 145)=250.2, p<0.0001). Due to a significant interaction effect (repeated measures ANOVA: genotype F(10, 145)=4.466, p<0.0001), a post-hoc Sidak's multiple comparison test was performed to further evaluate effects between groups at distinct distances from soma. Compared to Venus injection, AAV-APPsα injection of cDKO significantly increased basal dendritic length at 60 µm (*p<0.05). H Sholl analysis of apical dendritic length reveals an overall significant group effect (repeated measures ANOVA: genotype F(2, 37)=4.776, p<0.05) and a significant distance effect (repeated measures ANOVA: genotype F(18, 666)=47.54, p<0.0001). Due to a significant interaction effect (repeated measures ANOVA: genotype F(36, 666)=1.640, p<0.05), a post-hoc Sidak's multiple comparison test was performed to further evaluate effects between groups at distinct distances from soma. AAV-APPsα expression increased midapical dendritic length at 300 µm (**p<0.01) and 330 µm (**p<0.01) distance from soma compared to AAV-Venus injected cDKO mice.
Distribution of DCVs in dendrites and axons of sparse-labeled network cultures. (P) ChgB puncta per μm dendrite or axon. Lines next to individual data points show mean ± SEM. Mann-Whitney U test: **** p = < 0.0001. (Q) Mean ChgB fluorescence intensity per puncta in dendrites and axons. Unpaired t-test: *** p = < 0.0001.
Schematic of the Atto565-labeled tailed duplex substrate and PSC assembly procedure for homology search assays.
(A) HeLa cells were infected with S. Typhimurium (Salmonella) for 1 h or transfected with Effectene-coated latex beads for 3 h and then subjected to immunocytochemistry for LC3 and transferrin receptor (TfR). Bar, 10 µm.
E. LincGET overexpression in mouse ESCs had no effect on RNA levels of Hnrnpu, Fubp1, Ilf2, and Srsf1 measured by SG-qPCR. Three experimental replicates were performed and about 1 106 cells were used for each time. Two tailed student's t-test was used for the statistical analysis. n.s., p > 0.05.
(G) Asynchronously growing HEK293T cells co-transfected with Flag-β-catenin WT and either HA-Plk1 WT or control (vector only) were harvested and subjected to immunoblot analysis using the indicated antibodies. Asterisk, a nonspecific cross-reacting band.
C. Schematic of the non-canonical BAF (ncBAF) complex, with factors identified with high confidence (SaintExpress Score ≥ 0.99) by proximity labeling to be specific interactors of BRD9 (as compared to mCherry) colored in red.
(A) Domain structures of human ORP5 and ORP8. PH, Pleckstrin homology domain; ORD, OSBP-related lipid binding domain; TM, transmembrane domain.
Western blot protein analysis (I) of supernatants collected from Gata6-WT and Gata6-KOmye pMɸ stimulated with 100 ng.ml-1 LPS and either vehicle control (Vh, DMSO) or 10 µM MCC950 for 24 h (n=5).
B Control nub.Gal4 wing.C, D Expression of UAS.CrbExTM-GFP with Gal4.Gal4 (C) or UAS.Wts with nub.Gal4 (D) results in a small wing.E RNAi knock-down of α-Spectrin results in an overgrown wing.F, G Expression of UAS.CrbExTM-GFP (F) or UAS.Wts (G) blocks the effect of α-Spectrin RNAi.H RNAi knock-down of βH-spectrin/karst results in an overgrown wing.I, J Expression of UAS.CrbExTM-GFP (I) or UAS.Wts (J) blocks the effect of α-Spectrin RNAi.K, L RNAi knock-down of Wts results in a strongly overgrown wing (K) and expression of UAS.CrbExTM-GFP does not block the effect of wts RNAi (L).M, N RNAi knock-down of Ajuba results in a small wing (M), and expression of UAS.CrbExTM-GFP enhances the effect of ajuba RNAi (N).O Quantification of various wing sizes. Error bars show standard deviation.
(A) Representative images of collagen deposition determined by collagen I immunofluorescent staining in A375 xenografts treated as indicated. Bar graphs indicate the collagen I+ area/tumor area (n=5 tumors), ***P < 0.001 versus vehicle (P = 2.93E-06).(B) Representative images of CAF density determined by α-SMA immunofluorescence staining in A375 xenografts treated as indicated. Bar graphs indicate α-SMA+ area/tumor area (n=5 tumors), ***P < 0.001 versus vehicle (P = 0.0006).(C) Representative images of Lysyl Oxidase enzyme determined by LOX immunofluorescence staining in A375 xenografts treated as indicated. Bar graphs indicate the LOX+ area/tumor area (n=3 tumors), *P < 0.05 versus vehicle (bevacizumab P = 0.033; COMBO P = 0.040).
(I, J) Detection (I) and quantification (J) of CD8 TIL in lung metastasis of NeuNT WT and TNCKO mice (N = 3 mice, n = 7 and 12 lung metastases, respectively). Scale bar, 100 µm. ** p = 0.0097, Mann Whitney test. Mean ± SEM.
HAPI microglial cells were incubated for 1 h in glucose-free XF24 assay medium that was supplemented with 2-deoxyglucose (50 mM) and pyruvate (10 mM). RK-33 (10 μM), oligomycin (0.5 μg/ml), or vehicle control was additionally present as indicated. Results are mean ± SD from 12 replicates pooled from experiments using two consecutive passages. Significance was assessed by two-sided, unpaired t-test.
A. Confocal microscopy analysis showing the localization of endogenous Rab22a (green) and different endocytic markers (red): early endosomal marker EEA1, late endosome/lysosomal marker Lamp1 and the recycling compartment marker TfR in BMDCs at steady state. The means ± SEM of the Pearson correlation coefficients (Pcc) from Rab22a and EEA1 (0.4317 ± 0.05101), Lamp1 (0.8412 ± 0.03562) and TfR (0.6409 ± 0.02999) were estimated from 15 images analyzed for each marker. Scale bars: 5 µm.
A single RBD "down" monomer of 2019-nCoV S is shown in ribbons, colored according to Figure 1. A monomer of SARS-CoV S is also shown in ribbons, colored white (PDB ID: 6CRZ).
(A) Western blot analyses for the protein level of key regulators of actin polymerization in the cytoplasm and nucleus of HCC cells with treatment as indicated. Tublin and Lamin B1 were used as loading controls for the cytoplasm and nucleus, respectively (n = 3 independent experiments).
A. Titration of oligo#5. An increasing amount of oligo#5 was added to HEK293 cells stably expressing the serotonin 2C receptor reporter minigene and the RNA was analyzed by RT-PCR. -RT: negative control without reverse transcriptase.B. Quantification of three independent experiments. The half-maximal effect was seen at 13.1 nM concentration.
(C) Cells were treated as in panel B but included reconstitution with ATG13 ∆2AA mutant. The graph on right shows quantification of normalized ATG101 infrared signal. Mean ± SEM, n=3 (biological replicates). Significance measured using RM one-way ANOVA test followed by Fisher's LSD tests. (right).
(B) Volcano plot of a genome-wide association using mixed-model linear regression of antimycin A resistance for 118,527 genetic variants. Variants with moderate or high impact are shown in blue. Red dot: the variant at locus I:3845516, which causes a T343A change in the Pyk1 amino-acid sequence. This variant was among the top scoring (effect size=-0.645, rank 34; p=0.0008, rank 70).
(b) Scheme for expressed protein ligation and list of the peptides used for semisynthesis.
(G) Cells expressing B56δ full length (FL), Δ91-102, L183A and H282A mutants were pulled down with streptavidin beads and interaction with PPM1G was detected by western blotting.
D) 293T cells were transfected with a series of plasmids expressing ospD3 point mutants. After 24 h, cells were harvested and subjected to immunoblotting. Arrows indicate cleaved RIPK1.
C, D mRNA expression of ion channel genes KCNA5, KCNJ3 and KCNJ5 after knockdown of (C) COUP-TFI or (D) COUP-TFII in AM at day 30.
C. Ribbon diagram showing lipid coordination by Mdm12. Mdm12 residues and lipid fatty acids are colored in green and yellow, respectively.
B HeLa cells expressing Dox-inducible RIPK3 WT or 3xKR were treated with 1 µg/ml Dox overnight before pre-treatment with 20 µM zVAD.fmk, 5 µM BV6 for 1 h. After pre-treatment, 10 ng/ml TNFα were added for 1, 2, 3 and 4 h. Protein levels of inducible RIPK3 expression and phosphorylated MLKL were analyzed by Western blotting. β-Actin served as loading control.
Significant down-regulation of the protein level of TNFR1 in liver (n = 20), spleen (n = 20) and serum (n = 5) by 50 μg DEX (grey) compared to PBS (black).
Wild type (WT) mouse cortical neurons cultured for 10 days in vitro (A were serum-starved in Hank's balanced salt solution for 2 hours. Next, the cells were imaged immediately (starved), after which either amino acids (R+L) or insulin were added. Thirty minutes later the cells were imaged again. Finally, the mTOR inhibitor, Torin1 was added, and after an additional 30 minutes, the cells were imaged for the last time. Histograms represent changes in the fraction of enzyme-bound NAD(P) H (a2%) for each condition. Note that insulin and amino acids significantly increased the a2% values, which was reversed by Torin1-mediated inhibition of mTORC1. Average data from 5 fields of view per condition are shown. Statistical analyses were performed using Student's two-tailed unpaired t-test
(d) Ulk1 is highly phosphorylated at Ser 317 and Ser 777 by glucose starvation in vivo. To determine the Ulk1 phosphorylation level in vivo, immunopurified HA-Ulk1 protein was phosphorylated by AMPK in vitro (100% represents full phosphorylation of Ulk1 by AMPK). In vitro phosphorylated HA-Ulk1 was diluted as indicated, and was immunoblotted along with the immunoprecipitated HA-Ulk1 from cells grown in either glucose-rich (+ Glu) or glucose-free (- Glu, 4 h) medium. The density of the bands was then quantified. By this measurement, approximately 50% of Ulk1 isolated from glucose-starved cells was phosphorylated on Ser 317 and Ser 777.
A) Schematics of engineered FoxO3 constructs. KD measurements of the LxxIxE motifs fused to the C-terminus of FoxO3 were performed previously (Hertz et al., 2016; Kruse et al., 2018).
(A) Primary sequences of the WT peptide (red) and P182L peptide (blue). The IxI/V motif is indicated with white text. Below: regions of 2D 1H-15N HSQC spectra of 15N-labeled cHSP27 (black) in the presence of increasing amounts of WT (red) or P182L peptide (blue). Resonances in the β4 and β8 strands broaden and disappear upon peptide binding, indicative of intermediate exchange. (B) Zoomed-in regions of resonances during the peptide titrations. The color bars indicate the amount of added WT or P182L peptide. (C) The combined 1HN and 15N chemical shift changes, denoted as chemical shift perturbation (CSP), are plotted as a function of added peptide concentration. (D) CSPs shown as a function of residue number for the WT (red) and P182L peptide (blue). (E) X-ray structure of cHSP27 bound to the WT peptide (PDB: 4mjh), shown in white sticks, with the results from (D) plotted onto the structure.
Inhibition of β-IgSF binding to DB.CC1 by anti-CC1-N mAb (clone CC1/3/5-Sab), but not by anti-CC1-A1B1 mAb (clone B3-17). β-IgSF-biotin was coupled to SPE. Mean and SD values are reported for n = 6 replicates.
Nanog>GFP intensity of WT and Hdac3-/- TNG-A cells in 2iL and at d2 and d5 of SL exposure.
B. Interaction of endogenous MITOL and Parkin in HeLa cells stably expressing HA-Parkin. HeLa cells stably expressing HA-Parkin were treated with DMSO or CCCP (10 µM) for 12 h and subjected to an IP-IB assay with the indicated antibodies.
Phylogenetic tree of the alignment of representative Mettl5 orthologs from selected species (see Materials and Methods for details). Prokaryotic sequences from archaea (Pyrococcus, Bathyarchaeota) and bacteria (Acidobacteriales) are included as outliers. Multiple sequence alignment of Mettl5 orthologs showing conservation of the NPPF motif.
(A) Beclin 1 is essential for the early stage of autophagy and its depletion suppresses the Spns1 defect by blocking the 'autophagic process' and its progression. BafA can decelerate 'lysosomal biogenesis', which subsequently presumably prevents autophagosome-lysosome fusion, through the inhibition of the v-ATPase, and contributes to amelioration of the Spns1 defect at least temporarily. Basal p53 activity may suppress the intersection between the 'autophagic progress' and 'lysosomal biogenesis' where the Beclin 1 depletion was not sufficient, but the v-ATPase inhibition was still effective enough, to compete with the p53 loss to suppress the Spns1 deficiency. By switching the basal p53 state to the activated version with UV irradiation, p53 can promote autophagy. Spns1 might be a gatekeeper of autolysosomal maturation followed by lysosomal biogenesis. It remains unknown how p53 can mechanistically be linked to the lysosomal 'efflux' function of Spns1 as well as the lysosomal 'influx' function of v-ATPase, and further investigations will be required to explore this connection.
Patient-derived and control fibroblasts were used. (D) Cells were stimulated with TNF for 24 hours and IL-6 was determined by ELISA. Data are presented as mean ± SD of 3 individual experiments performed in two technical replicates; *, P = 0.014; **, P = 0.007; multiple t-test corrected for multiple comparisons using the Holm-Sidak method.
(a, b) Bif-1+/+ and Bif-1−/− MEFs or Bax+/+Bak+/+ and Bax−/−Bak−/− MEFs were infected with Beclin 1 shRNA or control shRNA (SCR shRNA) lentiviruses. Twenty-four hours after infection, the medium was replaced with fresh culture medium and the cells were allowed to recover for an additional 48 h. The cells were then cultured in EBSS for 0, 6 or 12 h, and the percentage of dead cells was determined by trypan blue exclusion assay (mean ± s.d.; n = 3). Knockdown of Beclin 1 expression was confirmed by immunoblot analysis (insets).
(I) Levels of Oxytocin plasma and tissue concentration in Shank2+/+ and Shank2-/- mice. Left panel: No significant difference was detected between Oxytocin plasma concentration comparing Shank2+/+ with Shank2-/- mice, unpaired, two-tailed Student's t-test, P=0.276, Shank2+/+ n = 5, Shank2-/- n = 5. Right panel: Additionally, Shank2-/- mice displayed no significant differences in hypothalamic or pituitary Oxytocin concentrations, unpaired, two-tailed Student's t-test, P=0.536, Shank2+/+ n = 6, Shank2-/- n = 5; two-tailed Student's t-test, P=0.585, Shank2+/+ n = 5, Shank2-/- n = 5. Data information: All data are presented as mean ± SEM, NS: not significant.
C and D) Representative images of SDHstaining (D) in muscle sections from young and old control and Mfn2KO mice (n=3 mice per group).
D-F. Fe contents of whole plants, FER expression in roots and relative FCR activities in the roots of plants grown under Fe-sufficient (20 µM, +Fe) or Fe-deficient (2 µM, -Fe) conditions for 7 d. Plants were exposed to high (H-, 2.0) or low (L-, 0.5) red (R) to far red (FR) ratios.
F Basal and stimulated (+200 nM isoproterenol) lipolysis in isolated adipocytes from 10-week-old WT and FADD-D mice (n = 4 for each genotype) treated with or without 10 μM BAY. Data are expressed as mean ± SEM. *P = 0.0033, **P = 0.0051, ^P = 0.004, ^^P = 0.0057 (one-way ANOVA). NS, not statistically significant.