EMBO/sd-character-level-ner huggingface dataset:
(H) Quantification of nuclear enrichment over time for H3.1-EGFP and mCherry-IPO4 from 5 individual cells. H3.1-EGFP values are green traces, whereas mCherry-IPO4 traces are red traces. Values for the cell shown in (F) is highlight by circles
Bar graphs showing the number of inhibitory (Gephyrin- and VGAT-positive) synapses in the IC of control;Mertk+/+, control;Mertk-/-, Cdc50a cKO;Mertk+/+ and Cdc50a cKO;Mertk-/- mice (n = 4 for each group, P**** < 0.0001, P*** = 0.0002, P** = 0.0021).
Calculated absolute numbers of donor-derived HSPC subsets in transplanted mice (F). (total of n=7-8 mice per genotype). Data information: Data presented as mean ± SEM. *p<0.05, **p<0.005 and ***p<0.001 by two-tailed Student's unpaired t-test analysis.
E. Abundance of MerTK+CD64+ macrophages analyzed by flow cytometry of pre-tumorigenic ear skin from 12 week-old mice expressing the CCR2-CFP-DTR transgene (wt/CCR2) or double-transgenic animals (Act/CCR2), untreated or treated with diphtheria toxin (+DT) 3 times every 48h and analyzed 24h after the last injection. Percentage of CD45+CD11b+MerTK+CD64+ macrophages among live cells is shown. N=3 control wt/CCR2 and Act/CCR2 mice; N=4 DT-injected wt/CCR2 and Act/CCR2 mice. Representative flow cytometry scatter plots are shown in Appendix Fig S1E.
(C) Fresh BM mononuclear cells collected from AML patients were treated with 150 nM Am80 alone or combined with GCSF. Proliferation (left sections) and bacterial killing (right sections) were analyzed on day 12 for each of samples.
A. Current model of ICLpt repair in Xenopus egg extracts (Amunugama et al, 2018).
Western blot of p53 pS15, p53, PHD1, and vinculin in HCT116 treated with 300 μM 5-FU for 8 h and silenced for PHD1 or a scrambled (Scr) control.
(C) Analysis of nucleotide incorporation opposite Tg from replication reactions processed as shown in (B). Three individual experiments were performed, two in the presence and one in the absence of Pol δ (10 nM), giving 99, 97, and 95 successful sequencing reads respectively.
d. Proliferation measured at day 4 of CFSE-labeled responder T cells alone (left histogram) or co-cultured with Tregs that had been pre-incubated with either vehicle or IL-12 alone or with LY294002 or MK2206 at a 1:2 Treg:Tresp ratio. e. Statistical analysis of the percentage of suppression as in d at different Treg:Tresp ratios of n=6 experiments performed. *p < 0.05, **p < 0.005, ***p < 0.0005.
H. Quantification of LCS-GR distribution (linear density, LD) across the stack and in peri-Golgi vesicles (data are means ± SEM, number of Golgi stacks is n=17 at 20 min for the CTRL, n=13 at 20 min for the GOLPH3 KD; *p <0.05, **p < 0.01; ***p <0.001 [Student's t-test]).
Oxygen consumption rate (OCR) upon sequential injection of oligomycin (Oligo), FCCP and rotenone (Rot) + antimycin (AA), in untransfected, sorted "GFP-+" and "GFP++". The error bars represent the mean±SEM of 5-7 separate experiments
F) Average width of fibrils calculated from every particle cropped along the fibrils within each collected tomogram. The data points represent the average width calculated from the total number of particles extracted from multiple tomograms for the aggregates localized for FTLD-TDP-A (n=5 biological replicates) and FTLD-TDP-C, CF (n=6 biological replicates). The total number of particles extracted for each aggregate are shown in Appendix table S3. Error bars represent +/- standard deviation. The total average width calculated from all fibrils from FTLD-TDP-A is 7.8 nm (+/- 1.1 nm), 7.5 nm (+/- 1.3 nm) for FTLD-TDP-C and 5.2 nm (+/- 1.7 nm) for CF.
(I) Graph depicts the expression (indicated as the Mean Fluorescence Intensity) of H-2Kb by Pru Tomato SAG1‐OVA infected XBP1fl/fl IRE1fl/fl treated or not with 4μ8C, XBP1ΔDC IRE1truncDC and XBP1ΔDC BMDCs. Bar graphs depict mean ± S.E.M (n=3 mice, one representative experiment from 2 independent experiments). Tukey's ANOVA one-way test, ns: p>0.05.
Western blotting showing accumulation of proteins as indicated in the samples of E.
C) t-SNE analysis of the human Müller glia cell line MIO-M1 with the retinal cell types identified in this human neural retina atlas.
E) % of cell death induced by TRAIL (1µg/ml), COMBO and their combination at different treatment durations on HCT DKO measured as in panel B. Paired Student's t-test ** p<0,025 and * p<0,05 with respect to MOCK condition.
(I) Representative images of plaque assay in Vero cells performed from the culture supernatant of JEV (MOI 1, 24 h) infected HT-29 control and IRGM knockdown cells.
A. A family tree for the juvenile ALS patient with L95fs mutation in Sigma 1 receptor (Sig1R).
F-H Lysates from HEK293T cells expressing R-Luc-MS2-A95-MALAT1 reporter and MS2-HA tagged proteins were immunoprecipitated using anti-eIF4A2 antibody. The RNAs coimmunoprecipitating with eIF4A2 were analyzed by northern blot. 7SL RNA served as a loading control. R-Luc mRNA levels were normalized to those of the F-Luc control. The normalized values in the IP were divided by those in the input and set to 100 for cells expressing MS2 peptide. (F) Normalized R-Luc activities. The panel shows mean values ± standard deviations from five independent experiments. (G) Representative western and northern blots of input and IP fractions. For the western blot, 2% of the input and 6% of the IP fraction were analyzed. For the northern blots 2% of the input and 40% of the IP were analyzed. (H) Efficacy of the immunoprecipitation. Error bars represent standard errors from five independent experiments.
BDNF secretion in cultured hippocampal neurons untransduced (control) or infected with lentiviruses expressing Tardbp shRNA or human TDP-43 12xQN constructs together with either EGFP or Sortilin rescue viruses. Histogram bars show average ± SEM BDNF levels normalized to a standard curve (N=5 independent experiments; n=5 wells per condition in each experiment). **, p<0.01. Data information: Results are presented as average ± standard error of the mean (SEM). All statistical tests were performed using 2-way ANOVA with Sidak post hoc analysis
B) Body weight changes over time, relative to body weight at 45 days that is set at 100% for each mouse. Parkin knockout delays body weight loss in SOD1-G93A mice. Results are expressed as mean ± SEM; n=19 for Non Tg (9 males and 10 females), n=20 for PKO (10 males and 10 females), n=18 for G93A (8 males and 10 females) and n=19 for PKO/G93A (9 males and 10 females); *p= 0.017 (at 150 days), *p= 0.004 (at 164 days), *p= 0.002 (at 171 days) and **p= 0.001 (at 178 days), by two-way ANOVA with repeated measures and with Holm-Sidak's correction for multiple comparisons.
G PTPσ expression in NB-3+/+ and NB-3−/− pyramidal neurons when co-culturing with NB-3-expressing astrocytes (dashed lines and asterisks) or astrocytes that didn't express NB-3 (dashed lines). Upper inset, high-magnification view of the soma (white arrowhead). Lower inset, high-magnification view of the axon tip (green arrowhead).H Quantification of fluorescence intensity of PTPσ in (G). n.s., not significant, and *p < 0.05; one-way ANOVA followed by Bonferroni post-test.
C Survival curves (percentage of live animals assayed each hour after PA14 exposure) for the indicated mutants at 20oC. Plog-rank<0.0001. Median survival time was 90 hours for wildtype (N=304), 72 hours for dop-1(vs100) (N=180), 78 hours for elt-3(gk121) (N=120), 78 hours for pqm-1(ok485) (N=116), 78 hours for nhr-28(gk568) (N=123), and 42 hours for skn-1(tm3411) (N=33). Eight wild-type animals and six dop-1 mutants were censored (the animals crawled up the side of the plate and dessicated). The media contained 50 µg/ml of 5-fluoro-2′-deoxyuridine (FUdR to prevent the growth of egg offspring during the experiment.
Ribbon representation and topology diagram of the S-Ena1B subunit (blue to red rainbow from N- to C-terminus). The eight β-strands making up the S-Ena core domain are labelled B to I from N- to C-terminus. The first 15 residues form an N-terminal connector (Ntc) that for a subunit i, is in interaction with subunits i-9 (sand) and i-10 (green) through disulfide crosslinking.
L-M'') Representative images showing ci-lacZ is expressed in NBs (yellow arrows). (M-M'') are zoomed in images of (L).
B, New-born double knockout utrophin-dystrophin (mdx/utr-/-) mice and treatment with an CD38 inhibitor. Mdx/utr-/- mice were subcutaneously injected with K-rhein (0.6 and 2.5 mg/kg/d) for 4 weeks. B: Dot plots showing the treadmill performances of K-rhein-treated mdx/utr-/- mice: distance traveled (B1), maximum speed reached (B2) and maximum running time (B3) (WT (NaCl) and mdx/utr-/-+ K-rhein 2.5 mg/kg/d n=10 mice per group; mdx/utr-/-(NaCl) and mdx/utr-/-+ K-rhein 0.6 mg/kg/d, n=12 mice per group). Data information: Each dot of the graphs represents a mouse. one value/mouse; After normality and variance comparison tests, significance was assessed using: ANOVA followed by Fisher's LSD test Values are expressed as means ± SEM. Significance: *p<0.05, **p<0.01, ***p<0.001, #: p<0.001 vs mdx/utr-/- .
An equipotential representation of the IMM. In this model the IMM functions as a continuous electrical cable where cristae and IBM have similar ΔΨm and where all cristae respond simultaneously to any change in ΔΨm occurring in the mitochondrion where they reside. Transition from a hetero-potential to an equipotential, via cleavage of Opa1, for example, could play a role in normal mitochondrial physiology where conditions favor high conductance and low ATP synthesis, such as thermogenesis or adaptation to excess nutrient. Cartoon showing IMM as equipotential. Model of mitochondrial hetero-potential, showing cristae as individual bioenergetic units. Electrochemical autonomy of cristae protects the mitochondrion confronting a bioenergetic crisis, where dysfunction of one or more cristae would not inevitably cause the entire organelle to fail. In this model, cristae and IBM can have different membrane potentials. Closed CJs generate significant differences in charge between the cristae membranes and IBM, which could be related to the concentration of ETC subunits in the lateral side of the cristae and F1Fo ATP Synthase on the cristae rims. Cartoon showing IMM as hetero-potential.
A ERK activation following IL-33 treatment of BM-derived eosinophils. Dusp5+/+ or Dusp5-/- BM-derived eosinophils were stimulated with IL-33 (25 ng/ml) for the indicated times and total cell lysates were analyzed for p-ERK1/p-ERK2 (top) and total ERK1/2 (bottom) (left panels). Quantitation of p-ERK1 normalized to total ERK1 levels shown on left is graphically depicted on the right.
(A) Western blot analysis of GST-pulldown assays with GST-TIP30 fragments of the indicated length (as: amino acids from N-terminus) with Myc-tagged binding partners.
Accumulation of Ub in autophagy-deficient brain. Ub profile from the 1% Triton X-100-soluble and -insoluble fraction of autophagy-deficient brain homogenates captured with P2UBA resin. (A) Age-matched control Atg7 littermates (Atg7flox/+;nestin-Cre:p62+/−; denoted +) at 6 wk (open circles; n = 4) or Atg7 KO (Atg7flox/flox;nestin-Cre:p62+/−; denoted −) at 6 wk (closed diamonds; n = 3) are shown.
Lipid accumulation was quantified using automated image-based analysis in ASK1 knockdown (siASK1; grey bars) or control (siCtrl; black bars) cells treated with BSA, Palm or Palm+Baf and stained as mentioned above (n=4 biological replicates). Values are expressed as mean ± SEM. *
C Immunofluorescence images of T40PL cells transfected with TFEB and stained with anti‐LAMP1/MC1 (top) or PHF1 (bottom). Arrow marks cells with nuclear TFEB and its correlation with higher LAMP1 and lower MC1 (top) or PHF1 (bottom) stainings. Arrowhead indicates nearby cells with cytoplasmic TFEB and opposite LAMP1 and MC1/PHF1 patterns. Scale bar: 10 μm.
PDX tumors in each treatment group were harvested for protein For western blot analysis, three tumors each group (n = 3) were used for protein extraction and mixed with equal ration to detect the indicated antibodies in (D).
G Representative sections of immunohistochemical staining of CD4 and FOXP3 in TERT-ERVshigh and TERT-ERVslow colon tumours. Red arrowheads indicate FOXP3+ cells. Scale bar = 100 μm.
(b) Heatmap of TE expression in several silencing mutants determined by qRT-PCR relative to a housekeeping gene. To be able to display data in log-scale also for samples with zero expression, a value of 1.0e-6 (factor 10 smaller than the smallest value) was added to all values. Data for nuclei and CLV3::H2BmCherry are the same as in (a). For seedling samples, N = 2 (ATCOPIA49, ATHILA3), N = 3 (ATCOPIA39, VANDAL6, ATGP2, ATLINE1, ATCOPIA29, ATGP1-1), and N = 4 (ATLANTYS3, VANDAL12, ATGP1-2, ATHILA6A).
Western blots of FMRpolyA-NL-3xF products with and without DDX3X knockdown across a range of repeat sizes.
B. Body weight changes of WT (n=11) and OMA1-/- (n=12) mice during AOM/DSS treatment. Data are presented as mean ± SEM. Statistical significance was assessed by a two-way ANOVA, **p < 0.01.
I. Frequency (in percentage) of the amount of time embryos spent on black background. Each data point corresponds to one embryo. Total number of embryos analyzed: 43 embryos (co-MO), 45 embryos (miR-181-MO). n=4 independent experiments. Values are mean ± SEM. Abbreviations: co-MO, control morpholino.
Blood glucose levels of InsA-peptide immunized (red: 0:1, n=5 for E and n=10 for F; green: 100:1, n=5 and n=4 for F, d30, d32) and CI (grey, n=5 for E and n=10 for F) mice were assessed at indicated days. Dots represent individual mice. Mean ± SD, statistical significance was calculated by using Kruskal-Wallis test (E) and repeated measure ANOVA test (F), *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.
(C) Schematic model of damaged mitochondria recognition systems by autophagic membrane via NDP52-MTPAP interaction. On depolarized mitochondria, Parkin is activated and generates polyubiquitin chains on the OMM. The accumulation of polyubiquitin chains on the OMM induces the recruitment of mitophagy receptors and OMM rupture by proteasomes. NDP52 irrupts into mitochondria and interacts with MTPAP OMM rupture-dependently. The autophagic membrane recognizes damaged mitochondria by (i) poly-ubiquitin bound mitophagy rerceptors on the OMM (p62-like receptor mediated system), (ii) PHB2 on the IMM (Prohibitin-2 mediated system) and (iii) the NDP52-MTPAP complex (NDP52-MTPAP mediated system) via affinity with Atg8s (LC3 and GABARAP family)
(d) Fluorescence images of WT or Cx43−/− MOBs transfected with mCherry-GFP-LC3 and incubated or not with tamoxifen or lindane. Bottom: Quantification of autophagolysosomes (n = 3 wells, 3 independent experiments, >50 cells per experiment).
Hierarchical clustering of samples (n = 3 for each genotype) and heatmap of differentially expressed genes between the Mex3a-/- and WT mice. The red colour represents over-expression, while the blue colour under-expression.
(E-F) Number of (E) blebs per cell or (F) retracting blebs per cell evaluated by time-lapse microscopy analysis of LLO-treated shCtrl or shGp96 cells. shCtrl n=32 cells and shGp96 n=40 cells, p-values were calculated using two-tailed un-paired Student's t-test *p<0.5. (G) Sequential frames of time-lapse microscopy analysis of LLO-treated HeLa cells expressing GFP-NMHCIIA (shCtrl, shGp96 and shCtrl with 25 μM Blebbistatin - shCtrl-BB). LLO was added to culture medium 10 seconds before t0.
(F, G, H, I, J) Scatter plots depicting the changes between each p-tau biomarker as a function of CSF Aβ42/40. The horizontal-axes directions were inverted; lower CSF Aβ42/40 ratio reflects higher Aβ pathology. For each Aβ status group, we computed the standardized regression coefficients (β) and the P-values, adjusted for age and sex. The solid lines indicate the regression line and the 95% confidence intervals for each of the Aβ status groups. The dashed green lines indicate the CSF Aβ42/40 cutoff. Participants were also colour-coded based on the Aβ PET CL scale (≤12CL, black; >12CL, turquoise; Aβ PET non-available, grey).
A schematic presentation of PfEMP1 domain structure comprising a N-terminal head structure, 2-6 subsequent C-terminal domains, a transmembrane domain (TM) and an intracellular acidic terminal segment (ATS) with known receptors indicated in bold. Receptor specificity is determined by combined DBL and CIDR domains with mutually exclusive binding to EPCR and CD36 by different CIDRα domains in the head structure. Part of group A PfEMP1 and a particular subset of group B/A chimeric PfEMP1 (DC8) bind to EPCR via CIDRα1 domains, whereas Group B and C PfEMP1 bind CD36 via CIDRα2-6 domains. The atypical group E VAR2CSA PfEMP1 binds placental chondroitin sulfate A (CSA) via DBLpam1 and DBLpam2 domains. The binding phenotype of VAR 1, VAR3 and group A CIDRβ/γ/δ domains are unknown, but they do not bind EPCR or CD36. DBLβ domains can be involved in ICAM-1 binding and are from both group A and B. Not much is known about the other DBL domains (γ/δ/ε/ζ), but the DBLε and DBLζ domains are implicated in IgM and α2-macroglobulin binding.
(A) Representative images of wild-type (WT) and mutant (KO) neurospheres obtained from E15.5 neocortices and cultured in vitro. The culture passage ("step") corresponds to 3 days of culture after dissociation and re-plating. KO aggregates are more numerous and larger in size. Data information: Scale bars: 50µm.
(B) Representative images of heart sections of mice kept on a control or ketogenic diet eight weeks after TAC surgery stained against Ki67 and ERG. Scale bar: 50 µm.
qRT-PCR detection of IFNB1 mRNA in THP-1 cells stimulated with indicated eCDNs (5 μg/ml) for 4 h.
d) Cells as in b were kept in full media before being subjected to fixation and immunolabelling with the anti-Atg16L antibody. Atg16L puncta area as a fraction of total cellular area was obtained as described in Methods. This ratio was plotted as arbitrary units. Grey dashed line indicates the value for Atg3−/− cells rescued with wild-type Atg3. n = 2 (for V15K) or 3 (for all others) independent experiments; the precise n values and number of fields visualized per experiment are listed in the Methods. Raw data can be found in Supplementary Fig. 4. Atg3 variants that support lipidation of LC3 family proteins in vitro (Fig. 5) are indicated with black bars, while those that do not support lipidation are indicated with white bars. P values represent difference from wild-type rescue. **P 0.1; *P 0.05. Error bars in c,d represent s.d. for all samples of n > 2. Uncropped versions of all gels are included in Supplementary Fig. 7.
D: The PIKfyve/FIG4 ratio gradually decreased in prion-infected mice (unpaired t-test). **: p<0.01; ***: p<0.001. Each dot represents one mouse.
A. Rabl2Q80L localized in multicilia. Cultured mEPCs were infected with adenovirus to express GFP-Rabl2 or GFP-Rabl2Q80L at 24 h prior to and fixed at day 7 post serum starvation.
B. Positions of c-ring essential glutamic acid residues in wild type and mutant strains c″E108G (Delete), c″S192E (Addition) and c″E108G/S192E (Switch). Small red circles indicate glutamic acid residues and numbered circles indicates the TM helix of each proteolipid chain. Only a part of the c-ring is shown.
(A-C) Representative images of Cellular localization of TLR2-p and scrTLR2-p peptides in BM-derived macrophages were observed using confocal microscopy. (A) Cells were probed with anti TLR2 antibody following by staining with APC-labeled secondary antibody or (B) with TLR1 antibody following by staining with FITC-labeled secondary antibody (left panels, red). For membrane staining, cells were labelled with lipid dye, DiD (C). Then rhodamine-labeled fluorescent peptide was added to the cells (middle panels, green). Merged images are shown in the right panel. Scale bars 10µm. The mean Pearson correlation coefficient observed of TLR2-p or scrTLR2-p peptides with TLR2 TLR1 and DiD presents as mean of 2 independent experiments ± S.EM (n=19-61).
G. Changes in the steady-state level of the reporter encoded HA-tagged protein in upf1Δ, nmd4Δ, ebs1Δ and the nmd4Δ/ebs1Δ strains were estimated by immunoblot from three independent experiments, with one example shown
AGO6 relative enrichment of small RNAs (solid lines) and total small RNAs (dashed lines) are shown for each small RNA size class (21, 22 and 24nt) at four genomic loci.A A representative microRNA, miR158B. The location of miR158B from this locus is shown in orange.
(E) Quantifications of fibrinogen deposition areas in TCM-stimulating wild-type mouse lungs after injection of Vtn+ HepELs. Vtn+ cells were isolated from E0771-bearing wild-type or FX-/-mouse liver by using anti-Vtn beads (1 x 106 cells /mouse). Shown are averages (N=5/ group, 3 fields/ sample) with SEM. Welch"s t-test
Extravasated leukocytes (C) in cremaster tissue from WT or Y731F VE-cadherin mice stimulated intrascrotally with IL-1β and treated i.v. with isotype-control or anti-PECAM-1 (2H8) antibodies for 4 h before intravital microscopy.
The NTF of WT GPR56 contains both PLL and GAIN domains. The S4 variant of GPR56 contains only the GAIN domain. (A) WT GPR56 participates in cortical patterning during brain development. Collagen III, secreted by meningeal fibroblasts, activates GPR56 by binding to its PLL domain and sends a stop signal to migrating neurons once they reached to the pial basement membrane (B) In oligodendrocyte progenitor cells (OPCs), WT GPR56 binds to microglia-secreted tissue transglutaminase-2 (TG2) in the presence of laminin-111 to promote OPC proliferation (C) In microglia, GPR56 S4 binds to externalized PS, which services as an "eat-me" signal for those synapses needed to be removed, and mediates the engulfment of synapses by microglia.
A H4 Cas9 cells were infected with sgRNAs targeting ATG7, TMEM41B or NT control, treated with 500 nM AZD8055 or vehicle control for 24 h, and analyzed by immunoblotting. B Ratio of LC3-II to LC3-I band intensities are depicted as mean ± SD (n=6 independent experiments) with Wilcoxon test values
Serial diluted recombinant S1 proteins of SARS-CoV-2, SARS-CoV and MERS-CoV were coated on 96 well plates, incubated with the recombinant Fc-tagged ACE2 (ACE2-Fc) for binding evaluation.
(B) Distribution of single cells based on fluorescence intensity of XGFP reporter quantified by BD FACSDiva Software, plotted against the X chromosome average allelic ratio per cell. R and p-values calculated by Pearson's correlation are shown. Black line represents linear regression fitting.
A. NIH3T3 cells transfected with KV10.1*EGFP did not show primary cilia. Cells were transiently transfected, after 24 h serum was removed for additional 24 hours to induce ciliogenesis, and finally cells were stained with anti-acetylated α-tubulin. While most cells were ciliated, those showing green fluorescence were devoid of cilia. Scale bar: 10µm.
(d) Immunoblot analysis of lysates of TH1 cells transfected with GFP-Itch or GFP-mu-Itch (top) or with Myc-RCAN1 or Myc-mu-RCAN1 (bottom) and cotransfected with a GFP expression plasmid (to assess transfection efficiency), then activated for 24 h as in a.
F. Brain lysates from FBXO7+/+ and FBXO7-/- mice immunoblotted with the PSMA2 or γ-tubulin antibody. The latter served as loading control. 10 brains from each genotype were included in the quantitative analyses (paired t-test, mean + s.e.m.).
E) Representative immunofluorescence images showing Myc-M18BP1-1161-580 localization at sperm centromeres in extract depleted of endogenous M18BP1. In addition, extract was mock-depleted or immunodepleted of CENP-C (indicated at left). Cell cycle state indicated at left, immunolocalized protein indicated above. Scale bar, 10 μm. Insets magnified 3X. F) Quantification of (E). Graph shows mean Myc-M18BP1-1161-580 intensity at centromeres ± SEM of two independent experiments normalized to the mock-depleted, metaphase condition.
C. LORE Y600 is phosphorylated in plants. Two-week-old pLORE:LORE-FLAG complementation plant leaves were subjected to immunoprecipitation (IP) with anti-FLAG agarose beads. Y600 specific phosphorylation antibody was used to detect Y600 phosphorylation in LORE. The experiment was repeated three times with similar results.
Comparisons of serum triglyceride (TG) and free fatty acids (FFA) at indicated time points in vehicle- and ABX- treated mice (n = 5-7 mice/group).