EMBO/soda-nel huggingface dataset:
Identification of a novel PPARβ/δ / miR-21-3p axis in UV-induced skin inflammation (2016)
Figure 2

Figure 2: Activation of miR-21-3p by PPAR/ requires TGFβ-1.

(A) RT-qPCR quantification of relative pri-miR-21 level in HaCaT human keratinocytes treated with the PPAR/ agonist GW0742 (+) or vehicle (-), with (+) or without (-) cycloheximide (Cyclo) as indicated. Pri-miR-21: Veh vs GW0742 P = 0.009. N=3 biological replicates, one representative experiment is shown out of two independent replicates. (B) RT-qPCR quantification of relative pri-miR-21, pre-miR-21, miR-21-5p and miR-21-3p levels in HaCaT cells treated for 24h with 2 or 5ng/ml of recombinant human TGFβ-1 (+) or vehicle (-) as indicated. Pri-miR-21: Veh vs TGF-1 5ng/ml P = 0.029; Pre-miR-21: Veh vs TGF-1 5ng/ml P = 0.001; miR-21-5p: Veh vs TGF-1 5ng/ml P = 0.002; miR-21-3p: Veh vs TGF-1 5ng/ml P = 1.7E-05. N=3 biological replicates, one representative experiment is shown out of two independent replicates . (C) RT-qPCR quantification of pri-miR-21, pre-miR-21, miR-21-5p and miR-21-3p levels in HaCat cells treated for 24h with the PPAR/ agonist GW0742 (+), TGFβ receptor inhibitor SB431542 (+), or vehicle (-) as indicated. Pri-miR-21: GW0742 vs SB431542 P = 0.004, GW0742 vs GW0742/SB431542 P = 0.015; Pre-miR-21: Veh vs GW0742 P = 0.022, GW0742 vs SB431542 P = 0.036, GW0742 vs GW0742/SB431542 P = 0.024; miR-21-5p: GW0742 vs SB431542 P = 0.034, GW0742 vs GW0742/SB431542 P = 0.024; miR-21-3p: Veh vs GW0742 P = 0.036, GW0742 vs SB431542 P = 0.011, GW0742 vs GW0742/SB431542 P = 0.008. N=3 biological replicates, one representative experiment is shown out of two independent replicates. (D) RT-qPCR quantification of relative Tgfb1 level in the epidermis of acutely irradiated (Ac-UV) and non-irradiated Ppard +/+ and -/- mice. Tfgb1: Ppard +/+ no UV vs Ac-UV P= 0.034, Ppard +/+ Ac-UV vs Ppard Ac-UV P= 0.030. N=2-3 animals per group, one representative experiment is shown out of three independent replicates. (E) RT-qPCR quantification of relative miR-21-5p and miR-21-3p levels in the skin of Ppard +/+ mice treated with the TGFβ receptor inhibitor SB431542 (+) or vehicle (-), with (+) or without (-) acute UV exposure (Ac-UV). miR-21-5p: no UV vs Ac-UV P = 0.038, Ac UV vs Ac UV/SB431542 P = 0.028; miR-21-3p: no UV vs Ac-UV P = 0.017; Ac-UV vs Ac-UV/SB431542 P = 0.035. N=3 animals per group, one representative experiment is shown out of three independent replicates.
Identification of a novel PPARβ/δ / miR-21-3p axis in UV-induced skin inflammation (2016)
Figure 3

Figure 3: SMAD7 is a target for miR-21-3p.

(A) RT-qPCR quantification of relative SMAD7 expression level in the epidermis of acutely irradiated (Ac-UV; +) ex vivo biopsies of human normal skin. SMAD7: no UV vs Ac-UV P = 0.032. N=4 biological replicates, one representative experiment is shown out of three independent experiments performed with the skin of three different donors. (B) Left panel: wild-type (WT SMAD7 3’UTR) and mutated (MUT SMAD7 3’UTR; *: mutated nucleotides) miR-21-3p binding sequences in the human SMAD7 3’UTR. Right panel: Luciferase reporter assay with wild-type (WT SMAD7 3’UTR) or mutated (MUT SMAD7 3’UTR) SMAD7 3’UTR in HEK 293 cells overexpressing miR-21-3p (miR-21-3p mimic) or a scrambled sequence (Control). (C) Left panel: normalized expression data of SMAD7 mRNA obtained from genomic microarray analysis of human HaCaT cells treated with a miR-21-3p mimic (miR-21-3p mimic) or a scrambled sequence (control). N=3 biological replicates. Middle panel: western blot quantification of SMAD7 protein level (normalized to GAPDH protein level) in human HaCaT cells treated with a miR-21-3p mimic (miR-21-3p mimic) or a scrambled sequence (control). SMAD7: control vs miR-21-3p mimic P = 0.031. N=3 biological replicates, Right panel: western blot of SMAD7 and GAPDH proteins in human HaCaT cells treated with a miR-21-3p mimic (miR-21-3p mimic) or a scrambled sequence (control), N=3 biological replicates; one representative experiment is shown out of two independent replicates. (D) Western blot of Smad7 from epidermis of acutely irradiated (Ac-UV; +) Ppard +/+ and -/- mice. Loading control: GAPDH. (E) RT-qPCR quantification of relative TGFB1, SERPINE1, p21, RUNX and SNAI2 levels in human HaCaT cells treated with a miR-21-3p mimic (miR-21-3p mimic) or a scrambled sequence (control) with (+) or without (-) treatment with 2ng/ml recombinant TGF-1. SERPINE1: TGF-1 2ng/ml control vs miR-21-3p mimic P = 0.004; p21: TGF-1 2ng/ml control vs miR-21-3p mimic P =0.03; RUNX: TGF-1 2ng/ml control vs miR-21-3p mimic P = 0.04. N=3 biological replicates.
Identification of a novel PPARβ/δ / miR-21-3p axis in UV-induced skin inflammation (2016)
Figure 4

Figure 4: Gain of miR-21-3p function activates inflammation in HaCaT human keratinocytes.

(A) Proportion of inflammatory- and immune processes- associated mRNA in regard to the total number of significantly deregulated mRNA in miR-21-3p mimic versus scrambled control treated HaCaT cells. (B) Go term enrichment analysis based on the significantly up- and down-regulated mRNA in miR-21-3p mimic treated compared to scramble control treated HaCaT cells. (C) RT-qPCR analysis of IL6, IL1B, IL1RAP, PTGS2, CCL5, CXCL10 and CASP14 levels in HaCat cells transfected with a miR-21-3p mimic or a scrambled sequence (control). IL6: control vs miR-21-3p mimic P = 0.05; IL1B: control vs miR-21-3p mimic P = 0.005; IL1RAP: control vs miR-21-3p mimic P = 0.008; PTGS2: control vs miR-21-3p mimic P = 0.050; CCl5: control vs miR-21-3p mimic P = 0.001; CXCL10: control vs miR-21-3p mimic P = 0.012; CASP14: control vs miR-21-3p mimic P = 9E-05. N=3 biological replicates, one representative experiment is shown out of three independent replicates.
Identification of a novel PPARβ/δ / miR-21-3p axis in UV-induced skin inflammation (2016)
Figure 5

Figure 5: Elevated miR-21-3p level correlates with exacerbated inflammation in murine skin exposed to acute UV.

(A) RT-qPCR quantification of Il6, Il1b, Ptgs2 and Ccl5 levels in the epidermis of acutely irradiated (Ac-UV; +) and non-irradiated (-) Ppard +/+ and -/- mice. Il6: Ppard +/+ no UV vs Ac-UV P = 7E-04, Ppard +/+ Ac-UV vs Ppard -/- Ac-UV P = 0.008; Il1b: Ppard +/+ no UV vs Ac-UV P = 0.010, Ppard +/+ Ac-UV vs Ppard -/- Ac-UV P = 0.016, Ppard -/- no UV vs Ac-UV P = 0.015; Ptgs2: Ppard +/+ no UV vs Ac-UV P = 0.028, Ppard +/+ Ac-UV vs Ppard -/- Ac-UV P = 0.028, Ppard -/- no UV vs Ac-UV P = 8E-04; Ccl5: Ppard +/+ no UV vs Ac-UV P = 0.002, Ppard +/+ Ac-UV vs Ppard -/- Ac-UV P = 0.014, Ppard -/- no UV vs Ac-UV P = 0.010; ns: non significant. N=4 animals per group, one representative experiment is shown out of three independent replicates. (B) Left panel: Immunostaining for infiltrating F4/80-positive macrophages in acutely irradiated (Ac-UV) and non-irradiated (no UV) Ppard +/+ and -/- mice skin sections. Magnification bar: 200m. Right panel: RT-qPCR quantification of relative levels of the macrophage marker Emr1 mRNA in total skin of acutely irradiated (Ac-UV; +) and non-irradiated (-) Ppard +/+ and -/- mice. Emr: Ppard +/+ no UV vs Ac UV P = 0.034; Ppard +/+ Ac UV vs Ppard -/- Ac UV P = 0.033. N=4 animals per group, one representative experiment is shown out of three independent replicates. (C) RT-qPCR quantification of relative levels of Il6, Il1b, Ptgs2 and Tnfa in mouse epidermis acutely irradiated (Ac-UV; +) and non-irradiated (-), treated with miR-21-3p inhibitor (+) or mismatched control (-) as indicated.
Identification of a novel PPARβ/δ / miR-21-3p axis in UV-induced skin inflammation (2016)
Figure 6

Figure 6: Elevated miR-21-3p and its inhibition are of clinical relevance to human skin inflammatory disorders.

(A) RT-qPCR quantification of relative levels of pri-miR-21, pre-miR-21, miR-21-5p and miR-21-3p levels in healthy human skin and human squamous cell carcinomas (SCC). pri-miR-21 Healthy skin vs SCC P = 0.043; pre-miR-21 Healthy skin vs SCC P = 3E-05; miR-21-5p Healthy skin vs SCC P = 7E-05; miR-21-3p Healthy skin vs SCC P = 1.4E-06. ≥ 5 independent biopsies per condition. (B) RT-qPCR quantification of relative levels of pri-miR-21, pre-miR-21, miR-21-5p and miR-21-3p levels in healthy human skin and human psoriasis lesions. pri-miR-21 Healthy skin vs Psoriasis P = 0.034; miR-21-5p Healthy skin vs Psoriasis P = 0.034; miR-21-3p Healthy skin vs Psoriasis P = 0.036; ns: non significant, ≥ 4 independent biopsies per condition. (C) RT-qPCR quantification of relative levels of IL6, IL1B, PTGS2 and TNFA levels in epidermis of abdominal healthy human skin biopsies exposed to acute UV ex vivo, with or without topical treatment with miR-21-3p inhibitor (+) or mismatched control (-) as indicated. ns: not significant. IL6: no UV vs Ac-UV P = 0.036, Ac-UV vs Ac-UV/miR-21-3p inhibitor P = 0.019; IL1B: no UV vs Ac-UV P = 0.002, Ac-UV vs Ac-UV/miR-21-3p inhibitor P = 0.023; PTGS2: no UV vs Ac-UV P = 0.008, Ac-UV vs Ac-UV/miR-21-3p inhibitor P = 0.022; TNFA: no UV vs Ac-UV P = 0.032, ns = non significant. ≥ 7 replicates, a pool of three independent experiments performed with the skin of three different donors is shown.
Asparagine reinforces mTORC1 signaling to boost thermogenesis and glycolysis in adipose tissues (2021)
Figure 1

Figure 1. Increased asparagine availability promotes thermogenic and lipogenic program in brown adipocytes

Immortalized brown preadipocytes were induced to mature adipocytes with supplementation of asparagine during differentiation. Gene expression was analyzed on differentiation day 6.

Gene expression analyzed by quantitative PCR in brown adipocytes that were fed with or without 1mM asparagine as in (A). n=3 independent experiments.

Oxygen consumption rate measured by clark electrodes for mature brown adipocytes as in (B). n=4 independent experiments.

Left: UCP1, PGC1α and PPARγ protein levels were analyzed in brown adipocytes (day 6). Cells were supplemented with 1mM asparagine from day 4 to day 6. Right: quantification of protein levels. n=3 biological replicates.

Preadipocytes bearing the shRNA targeting Pgc1α were induced differentiation with or without 1mM asparagine. Protein expression was analyzed on day 6. n=3 biological replicates.

Primary preadipocyes isolated from mice BAT were induced to differentiation in DMEM media with or without 1mM asparagine. Left: UCP1 and PPARγ protein levels were analyzed on day 6. Right: quantification of protein levels. n=3 biological replicates.

Brown preadipocytes were infected by lentiviral shRNAs against Asns. Cells were differentiated in culture media with or without 1mM asparagine. Western blot was performed on day 6.

Data information: Data represent means±SEM. *P<0.05; **P<0.01; unpaired two-tailed Student's t test.
Asparagine reinforces mTORC1 signaling to boost thermogenesis and glycolysis in adipose tissues (2021)
Figure 2

Figure 2. Increase of asparagine supply stimulates adipose thermogenesis in vivo

C57BL/6J male mice fed on a chow diet drank water with or without asparagine at a concentration of 1.5g L-1 for 3 weeks. Mice were acutely exposed to 4˚C for 6 h to measure rectal temperature or intraperitoneally (i.p.) injected CL316,243 (1mg kg-1 body weight) for one time for other assays.

Mice serum amino acid concentration after 3-weeking asparagine feeding. n=5 mice each group.

Asparagine content in BAT of mice in (B). n=5 mice each group.

Rectal temperature was measured when mice in (A) was challenged to 4˚C. n=5 mice each group.

E,F. Serum insulin (E) and triglyceride (F) concentration was assayed in mice 24 h after one dose of CL316243 injection. n=5 mice each group.

UCP1 and PPARγ protein levels in BAT and inguinal WAT (iWAT) from mice in (E).

Representative pictures of BAT and inguinal WAT (iWAT) hematoxylin and eosin staining from mice in (E). Scale bar: 20μm for BAT, 50μm for iWAT.

I,J. Mice supplemented with asparagine in drinking water for 3 weeks were subjected to the indirect calorimetry analysis at both basal (I) and CL316,243-stimulated (J) states. n=5 mice each group.

Data information: Data represent means±SEM. *P<0.05; **P<0.01; ***P<0.001; unpaired two-tailed Student's t test.
Asparagine reinforces mTORC1 signaling to boost thermogenesis and glycolysis in adipose tissues (2021)
Figure 4

Figure 4. Feeding asparagine sensitized diet-induced obese mice to β3-adrenergic agonist

C57BL/6J male mice fed on a high-fat diet drank water with or without asparagine (1.5g L-1) for 18 weeks. In the last 4 weeks, mice were injected CL316,243 daily (0.5mg kg-1 body weight).

Body weight of mice in (A) during the high-fat diet feeding. n=5 mice each group.

Glucose tolerance test was performed after a high-fat diet feeding for 17 weeks in mice of (A). n=5 mice each group.

Serum insulin levels in mice of (A). n=5 mice each group.

Serum triglyceride levels in mice of (A). n=5 mice each group.

Fat mass weight in mice of (A). n=5 mice each group.

Representative histology pictures for BAT, inguinal WAT (iWAT) and epididymal WAT (eWAT) in mice of (A).

BAT and inguinal WAT (iWAT) UCP1 and PPARγ protein levels in mice of (A).

Data information: Data represent means±SEM. *P<0.05; **P<0.01; unpaired two-tailed Student's t test.
Asparagine reinforces mTORC1 signaling to boost thermogenesis and glycolysis in adipose tissues (2021)
Figure 5

Figure 5. Supplementation of asparagine spurs glycolysis in adipocytes

Heat map of metabolite relative levels in brown fat cells treated with or without 1mM asparagine.

Quantification of representative metabolic intermediates of glycolysis in brown fat cells as in (A). n=3 independent experiments.

Schematic illustration of key enzymes in glycolysis and tricarboxylic acid (TCA) cycle.

D-G. Immunoblot detection of the glucose transporters, glycolysis and TCA key enzymes in primary (D) and immortalized brown fat cell line (E), BAT from mice fed asparagine (F) and injected asparaginase (G). Asparagine was supplemented to cells during differentiation. The HSP90 data shown in Figure 5G is a redisplay of Figure 3D as the same samples and experimental conditions were probed.

Data information: Data represent means±SEM. *P<0.05; unpaired two-tailed Student's t test.
Asparagine reinforces mTORC1 signaling to boost thermogenesis and glycolysis in adipose tissues (2021)
Figure 7

Figure 7. Asparagine facilitates glycolysis via mTORC1 activation and exchange of amino acids.

Quantification of intracellular amino acid levels in brown fat cells (day 6) treated with or without 1mM asparagine. n=4 independent experiments.

B-D. mTORC1 pathway activity was analyzed by immunoblotting for the phosphorylation of 4E-BP1 and S6K in brown adipocytes (B), BAT from mice fed asparagine (C) or asparaginase (D). (B) Asparagine was added to cultured media from day 4 to day 6.

A Click-iT AHA labeling assay to detect newly synthesized glycolytic enzymes. The level of HSP90 in total cell lysates was used as a loading control.

Brown preadipocytes were induced to differentiation with or without 1mM asparagine. Rapamycin (75nM) was added to cells for 48h. Then western blot detected protein expression on day 6.

Brown preadipocytes were knocked down Raptor following standard induction to mature adipocytes with or without asparagine supplementation. Protein expression analysis was performed on day 6.

Data information: Data represent means±SEM. *P<0.05; **P<0.01; ***P<0.001; unpaired two-tailed Student's t test.

Expanded View Figure Legends
Host range and structural analysis of bat-origin RshSTT182/200 coronavirus binding to human ACE2 and its animal orthologs (2022)
Figure 2

Figure 2. Mutation analysis of key residues of the RshSTT182/200 RBD interaction with hACE2.

A Insertion or deletion mutation sites of the RshSTT182/200 RBD or SARS-CoV-2 RBD mutants.

B The binding affinities of the wild-type RshSTT182/200 RBD, insert2 and their mutants for hACE2-hFC.

C The hydrophobic interaction regions of the RshSTT182/200 and SARS-CoV-2 RBDs are shown.

D The β4β5 loop comparison of the RshSTT182/200 RBD/hACE2 complex structure with the RshSTT182/200 RBD-insert2/hACE2 and SARS-CoV-2 RBD/hACE2 complexes (PDB: 6LZG). The backbone of the RBD is colored as gray. The β4β5 loop of the RshSTT182/200 RBD, RshSTT182/200 RBD-insert2 and SARS-CoV-2 RBD are shown as salmon, light blue and green, respectively. The RBD residues interacting with hACE2 and their corresponding ACE2 residues are shown as sticks in the corresponding colors.

E,F Comparison of hydrogen bonding interactions in the β4β5 loop region between RshSTT182/200 RBD-insert2 or RshSTT182/200 RBD-insert2-T346R-Y496G and the SARS-CoV-2 RBD.

G The entry efficiency of SARS-CoV-2 and RshSTT182 pseudoviruses in HeLa-hACE2 cells. Green fluorescence indicates the entry of the pseudoviruses into the Hela-hACE2 cells. Unaltered HeLa cells were used as a negative control. The scale bar indicates 400 μm.

H Statistics for transduction of pseudoviruses. Data represents the results of five replicates in one representative assay. All data are presented as mean ± SD. Pseudovirus infection assays were performed at least twice.
Host range and structural analysis of bat-origin RshSTT182/200 coronavirus binding to human ACE2 and its animal orthologs (2022)
Figure 3

Figure 3. Comparison of binding spectrum of bat-ACE2 orthologs with the RshSTT182/200 or SARS-CoV-2 RBDs.

A Flow cytometry characterization of binding between bat-ACE2 orthologs and the SARS-CoV-2 or RshSTT182/200 RBDs. BHK cells expressing eGFP-fused ACE2s were stained with the indicated His-tagged proteins. The SARS-CoV-2 NTD was used as a negative control.

B The binding affinities between bat ACE2s and the RshSTT182/200 RBD are shown with the mean ± SD. Mean ± SD represents the average values and standard deviation of the KD across three independent experiments. The a or b superscript of affinity data indicate that the KD value was calculated by kinetics model fitting or steady-state model fitting, respectively. "---" indicates not determined.

C The ring histogram shows the comparison of the binding affinity among bat ACE2 orthologs to the RshSTT182/200 RBD. The size of the column indicates the strength of the interaction.
Host range and structural analysis of bat-origin RshSTT182/200 coronavirus binding to human ACE2 and its animal orthologs (2022)
Figure 4

Figure 4. SPR characterization of the binding affinities of ACE2 (except bat) for the RshSTT182/200 or SARS-CoV-2 RBDs.

A Flow cytometry characterization of binding between ACE2s and the RshSTT182/200 or SARS-CoV-2 RBDs. Cells stained with the RshSTT182/200 RBD, the SARS-CoV-2 RBD and the SARS-CoV-2 NTD proteins are shown in orange, marine and red, respectively. The SARS-CoV-2 NTD was used as a negative control.

B The binding affinities between ACE2s and the RshSTT182/200 RBD are shown with the mean ± SD of three independent experiments. The "a" superscript of affinity data represents that the KD value was calculated by kinetics model fitting; "b" represents that the KD value was calculated by steady-state model fitting. "---" indicates not determined.

C The ring histogram shows the comparison of the binding affinities of ACE2 orthologs with the RshSTT182/200 RBD. The size of the column indicates the strength of the interaction.

D The entry efficiency of SARS-CoV-2 and RshSTT182 pseudoviruses into HeLa-hACE2 cells. Green fluorescence indicates the entry of the pseudoviruses into the Hela-hACE2 cells. Unaltered HeLa cells were used as a negative control. The scale bar indicates 400 μm.

E Statistics for transduction of pseudoviruses. Data represents the results of five replicates in one representative assay. All data are presented as mean ± SD. Pseudovirus infection assays were performed at least twice.
Targeting the LOX/hypoxia axis reverses many of the features that make pancreatic cancer deadly: inhibition of LOX abrogates metastasis and enhances drug efficacy. (2015)
Figure 1

LOX/hypoxia marks poor prognosis in resectable PDAC

Kaplan–Meier analysis showing cases from the Australian cohort (n = 73) delineated on the basis of expression of a set of hazardous genes, termed PC-1. Patients with the highest expression had a significantly poorer prognosis (red line, median survival: 11.6 months) compared with those patients with the lowest expression (blue line, median survival: 34.4 months, P = 0.01). The black line shows those with medium expression.

Kaplan–Meier analysis showing that cases in the Australian cohort that fell in the highest quartile of a hypoxia signature (red line, median survival: 11.4 months) have significantly decreased survival compared with those in the lowest quartile (blue line, median survival: 25.2 months; P = 0.03).

Kaplan–Meier analysis showing that cases in the APGI cohort (n = 266) with high LOX expression above the 3rd quantile (red line) have significantly decreased survival compared to those with low expression below the 1st quantile (blue line).

Kaplan–Meier analysis showing that cases in the Glasgow cohort with high LOX expression (red line, n = 24) have significantly decreased survival compared with those with low expression (blue line, n = 23; P = 0.005).

Kaplan–Meier analysis showing that fibrillar collagen is significantly associated with reduced survival in human PDAC (20 months vs. 28.3 months, P = 0.033).

Mean decay distance of the second harmonic generation (SHG) signal emitted by human PDAC-associated collagen. Mean decay distance is represented by boxplots showing the second and third quartile of the data with the whiskers indicating the maximum and minimum data points. Outliers are indicated by individual markers. Stage T3 tumors have a higher collagen mean decay distance score compared with Stage T2 tumors (P = 0.02). Lymph node-positive tumors have a higher collagen mean decay distance score vs. lymph node-negative tumors (P = 0.047). Tumors showing vascular invasion have a higher collagen mean decay distance score than non-vascular invasive tumors (P = 0.037).
Targeting the LOX/hypoxia axis reverses many of the features that make pancreatic cancer deadly: inhibition of LOX abrogates metastasis and enhances drug efficacy. (2015)
Figure 2

LOX expression is required for invasion in a mutant p53-driven model of PDAC

PC-1 signature is predictive of metastatic disease in mouse models of pancreatic cancer. Log-transformed expressions of signature transcripts from mouse tumor microarrays were mean-centered across samples and scaled to unit variance. These values were then multiplied by the matching loading values from the PC-1 signature and summarized for each sample across all transcripts to yield the risk score for that sample.

Inverted invasion assays were performed with PDAC tumor cell lines from KPC and KPflC mice. Tumor cell lines bearing mutant p53R172H (KPC) invade significantly further than tumor cells with deletion of 1 copy of p53 (KPflC) (P ≤ 0.01). Data are shown as the average of four wells + SEM.

Introduction of shRNA targeting Lox into KPC tumor cells significantly inhibits invasion (P ≤ 0.01 by unpaired Student’s t-test). Data are shown as the average of four wells + SEM.

Introduction of exogenous LOX into KPflC tumor cells significantly promotes invasion (left panel, P ≤ 0.01 by unpaired Student’s t-test). LOX expression was assessed by immunoblotting (right panel). Columns indicate the mean of four well and error bars indicate SEM.

Integration of heterogeneous data sets identifies LOX as a therapeutic target in pancreatic cancer. Components of the hazardous PC-1 signature are overlaid with genes found to be overexpressed in a microarray and hits that cause a reduction in viable cell number in an RNAi functional screen. Overlap is shown as a proportional Venn diagram.

Source data are available online for this figure.