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0.448634 | e4225c554c854ce0be294e71e2b95fdc | Arrangement and formation process of the crypt rows of the midgut symbiotic organ on the alimentary tract of P. stali. (a) Adult insects reared on peanuts and soybeans. (b) A 2nd-instar nymph. (c and d) A dissected alimentary tract of the 2nd instar nymph (c) and its schematic representation (d). M1, midgut 1st section; M2, midgut 2nd section; M3, midgut 3rd section; M4b, bulb-like midgut section anterior to M4; M4, midgut 4th section with crypts (symbiotic organ); HG, hindgut; MT, Malpighian tubule. (e) A microscopic image of the M4 symbiotic region, on which 3 of 4 crypt rows are seen with a crypt row hidden behind. (f) FISH of adult’s symbiotic organ. (g) Schematic diagrams of the crypt morphogenesis in the symbiotic organ. Also see reference 19. Blue and orange indicate the host intestinal epithelium and the symbiotic bacteria, respectively. (h) FISH of symbiotic organ of newborn nymph. (i) FISH of symbiotic organ of 1st instar nymph 1 day after hatching. (j) FISH of symbiotic organ of 2nd instar nymph 1 day after molting. In panels f and h to j, red indicates symbiotic bacteria and blue indicates cell nuclei, respectively. | PMC10127593 | mbio.00522-23-f001.jpg |
0.407319 | 31465df87b1a4d179156e8f100b9660a | Cell proliferation dynamics of the symbiotic organ in the nymphal development of P. stali. (a to f) Visualization of DNA-synthesizing cells by EdU labeling (green), dividing cells by H3P antibody staining (red) and all intestinal cells by DNA staining (white) in dissected midgut preparations. (g to l) Enlarged images corresponding to panels a to f at the midgut symbiotic region where crypts are formed. (m to r) FISH of the symbiotic organ. Red indicates symbiotic bacteria and blue indicates cell nuclei. (a, g, and m) First instar nymph 0 days after hatching. (b, h, and n) First instar nymph 1 day after hatching. (c, i, and o) First instar nymph 2 days after hatching. (d, j, and p) First instar nymph 3 days after hatching. (e, k, and q) Second instar nymph 0 days after molting. (f, l, r) Second instar nymph 1 day after molting. (s) EdU-positive cell counts per symbiotic organ at the different developmental stages. (t) H3P antibody-positive cell counts per symbiotic organ at the different developmental stages. In panels s and t, different alphabetical letters indicate statistically significant differences (Steel-Dwass test, P < 0.05; n = 4 each). | PMC10127593 | mbio.00522-23-f002.jpg |
0.411749 | d07f5632e68d4a548d60fa67f4cdddac | Arrangement of visceral muscle fibers on the nymphal alimentary tract of P. stali. (a) A schematic diagram displaying the arrangement of visceral muscles on the insect midgut. Green and orange show circular muscles and longitudinal muscles, respectively, while the blue tube shows the intestinal epithelium. (b) A transmission electron micrograph of the longitudinal section of the outer surface of the midgut in a 1st instar nymph, on which the circular muscle and the longitudinal muscle are seen. (c to f) Visualization of visceral muscle fibers on the midgut M1 region (c), M2 region (d), M3 region (e), and symbiotic M4 region (f) in late (3-day) 2nd instar nymphs. Actin fibers (green) and cell nuclei (blue) are visualized by phalloidin staining and DAPI staining, respectively. Note that typical patterns of circular and longitudinal muscles are seen in M1, M2, and M3, whereas atypical patterns are observed in M4. (g) Longitudinal section of the M4 region of a 1st instar nymph. Asterisks show crypts and arrowheads show circular muscles. (h) Enlarged image of panel g. Muscle fibers are seen between crypts. | PMC10127593 | mbio.00522-23-f003.jpg |
0.407767 | 520a92aa06be4e7dacb22fa0d86b4349 | Arrangement of visceral muscle fibers on the midgut symbiotic organ of newborn nymphs of P. stali. (a to c) Three typical patterns of visceral muscle arrangement observed on the symbiotic organ of newborn nymphs without crypts. (a) Circular muscles are bifurcated, connected, and arranged alternately. (b) Circular muscles are curved and separated locally. (c) Both the bifurcated patterns and the curved patterns are observed simultaneously. In panels a to c, actin fibers (green) and cell nuclei (blue) are visualized by phalloidin staining and DAPI staining, respectively. (d to f) Schematic diagrams of the arrangement of the circular muscle fibers corresponding to panels a to c. (g) Schematic representation of the arrangement of the circular muscle fibers on the midgut symbiotic organ of newborn nymphs. The bifurcated circular muscles (green lines) delineate the intestinal epithelium into the areas arranged alternately in two prepatterned rows (orange and blue areas), although the patterns are morphologically unrecognizable at this developmental stage. | PMC10127593 | mbio.00522-23-f004.jpg |
0.433973 | b95a5befa59d4c4f9697341512ca148d | Arrangement of visceral muscle fibers during the crypt morphogenesis in the nymphal development of P. stali. (a to c) 1st instar nymph 1 day after hatching. (d to f) 1st instar nymph 2 days after hatching. (g to i) 1st instar nymph 3 days after hatching. (j to l) Second instar nymph 0 days after molting or 4 days after hatching. (m to o) Second instar nymph 1 day after molting or 5 days after hatching. (p to r) Third instar nymph 1 day after molting or 9 days after hatching. Panels a, d, g, j, m, and p show the patterns in which the circular muscles are bifurcated. Panels b, e, h, k, n, and q show the patterns in which the circular muscles are curved. Panels c, f, i, l, o, and r show the patterns in which both the bifurcated and curved sites are seen. At the time point of Second instar molt and on, crossing muscle fibers that connect adjacent circular muscles are newly formed (arrowheads). Actin fibers (green) are visualized by phalloidin staining, whereas cell nuclei (blue) are visualized by DAPI staining. | PMC10127593 | mbio.00522-23-f005.jpg |
0.440493 | 3dc2e4371bc44c24a8631fb63b23b552 | FIB-SEM tomography of the newly formed muscle fibers connecting adjacent circular muscles in the nymphal symbiotic organ of P. stali. (a) Single cross-section (xy-direction) image of the midgut M4 region of a 2nd instar nymph 1 day after molting. Muscle fibers bridging the adjacent circular muscles are highlighted in the dotted box. (b) Magnified image of the dotted box in panel a. (c) Z-directional reconstructed image of the dotted line region in panel a, in which a thin cellular projection connecting two adjacent circular muscle cells is highlighted in red. (d) Z-directional reconstructed 3D image of the dotted box region in panel a. See also Movie S1. | PMC10127593 | mbio.00522-23-f006.jpg |
0.440389 | f504101e2f3c46c2b3e348cc1e7f18a7 | Cell proliferation, crypt formation, and visceral muscle arrangement in the symbiotic organ of symbiont-free nymphs of P. stali. Symbiont-free nymphs of P. stali were generated by egg surface sterilization as described previously (16). (a to f) Visualization of DNA-synthesizing cells by EdU labeling (green), dividing cells by H3P antibody staining (red) and all intestinal cells by DNA staining (white) in dissected midgut preparations. (g to l) Enlarged images corresponding to panels a to f at the midgut symbiotic region where crypts are formed. (m) EdU-positive cell counts per symbiotic organ at the different developmental stages. (n) H3P antibody-positive cell counts per symbiotic organ at the different developmental stages. In panels m and n, different letters indicate statistically significant differences (Steel-Dwass test, P < 0.05; n = 4 each). (o to t) Visualization of muscle fibers by phalloidin staining (green) and cell nuclei by DAPI staining (blue) at the midgut symbiotic region where crypts are formed. (a, g, and o) First instar nymph 0 days after hatching. (b, h, and p) First instar nymph 1 day after hatching. (c, i, and q) First instar nymph 2 days after hatching. (d, j, and r) First instar nymph 3 days after hatching. (e, k, and s) Second instar nymph 0 days after molting. (f, l, and t) Second instar nymph 1 day after molting. The intense green signal in panel f is autofluorescence of food material. | PMC10127593 | mbio.00522-23-f007.jpg |
0.465182 | a6f06d1dc34e4420aab22718d3833913 | Hypothetical model of crypt morphogenesis in the symbiotic organ of P. stali. (a) Delineation of crypt boundaries defined by positioning of visceral muscles. (b) Crypt protrusion and formation driven by epithelial cell proliferation. The processes shown in panels a and b proceed in this order with some overlap, thereby forming crypts arranged in four rows in the posterior midgut of P. stali. | PMC10127593 | mbio.00522-23-f008.jpg |
0.473147 | 07ecc999b230495d9e2d84ea0a9d6a78 | GW-5074 reduces initial JCPyV infection in glial cells. (A) The chemical structure of GW-5074. (B) The toxicity of GW-5074 was evaluated in SVG-A cells after GW-5074 treatment for 72 h. (C) SVG-A cells were pretreated with GW-5074 for 2 h before infection with JCPyV, and cells were maintained in drug-containing media for 72 h. Infection was scored by indirect immunofluorescent quantification of VP1+ cells. (D) The 50% cytotoxic concentration (CC50), 50% inhibitory concentration (IC50), and 50% selectivity index (SI50) are calculated. The 95% confidence interval is specified in parentheses. (E) Early GW-5074 treatment is protective against JCPyV infection. SVG-A cells were treated with GW-5074 or highest concentration vehicle control at various times relative to JCPyV infection. Cells were maintained in drug-containing complete media for 72 h, and infection was scored by indirect immunofluorescent detection of VP1+ cells. Data represent the mean of 3 independent experiments, and error bars represent the standard deviation. Asterisks (*) represent P < 0.05 by Student’s t Test. | PMC10127638 | mbio.03583-22-f001.jpg |
0.446854 | c7a67959c7fc40f9940b3d9a581a97fc | GW-5074 inhibits viral spread. (A) Naive SVG-A cells were infected with JCPyV. At 3 days postinfection (dpi), GW-5074 or volume-matched vehicle control were added. Supplemental doses of GW-5074 were administered every 3 days, and infection was scored by indirect immunofluorescent detection of VP1+ cells every 3 days. (B) Culture media was collected every 3 days and used to reinfect naive SVG-A cells. Infection was scored at 72 h postinfection. (C) To calculate the concentration of infectious virions released by drug-treated and vehicle-treated glial cells, gDNA was isolated from culture media and quantified with a JCPyV-VP2-specific primer/probe set. Data represent the mean of 3 independent experiments, and error bars represent standard deviation. Asterisks (*) represent P < 0.05 by Student’s t Test. | PMC10127638 | mbio.03583-22-f002.jpg |
0.463778 | 743a1d971a1a493aaadebcc96bc5b3bd | GW-5074 reduces JCPyV infection in normal human astrocytes. (A) The toxicity of GW-5074 was evaluated in normal human astrocytes (NHAs) after GW-5074 treatment for 120 h. (B) NHAs were pretreated with nontoxic doses of GW-5074 for 2 h before infection with JCPyV. Cells were maintained in drug-containing media for 120 h, and infection was scored via indirect immunofluorescent quantification of VP1+ cells. Data represent the mean of 3 independent experiments, and error bars represent the standard deviation. Based on these data, the SI50 of GW-5074 in normal human astrocytes is at least 20.2. Asterisks (*) represent P < 0.05 by Student’s t Test. | PMC10127638 | mbio.03583-22-f003.jpg |
0.418181 | df0c9449dabf4a23ab368c207a32f223 | GW-5074 reduces initial infection by human and simian polyomaviruses. SVG-A (JCPyV and SV40) or Vero cells (BKPyV) were pretreated with GW-5074 for 2 h before infection with JCPyV, BKPyV, or SV40. Infection was scored at 72 h postinfection by indirect immunofluorescent detection of VP1+ cells. Asterisks (*) represent P < 0.05 by Student’s t Test. | PMC10127638 | mbio.03583-22-f004.jpg |
0.434725 | 8ab104911c6045ceaf9bc993e6b5df70 | GW-5074 alters JCPyV-induced MAPK-ERK signaling events. (A) GW-5074 inhibits endogenous ERK phosphorylation by the Protein Kinase C agonist PMA. SVG-A cells were pretreated with GW-5074 or highest concentration vehicle control for 3 h. PMA was then administered alone or in the presence of GW-5074 for 1 h. ERK phosphorylation was visualized by Western blot. (B) Quantified results from (A). Data represent the band intensity from 3 independent experiments, and error bars represent the standard deviation. (C) PMA treatment cannot rescue initial JCPyV infection. Data represent the mean of 3 independent experiments, and error bars represent the standard deviation. (D) Proposed mechanism of the anti-JCPyV activity of GW-5074. GW-5074 is known to inhibit C-Raf, and these data suggest that GW-5074 treatment reduces viral infection by antagonizing MAPK-ERK signaling (19). PKC = Protein Kinase C. Image created with BioRender.com. Asterisks (*) represent P < 0.05 by Student’s t Test. | PMC10127638 | mbio.03583-22-f005.jpg |
0.458178 | edd349cb42fe4e90a4336978a84a1752 | CONSORT diagram showing enrollment and follow-up of study subjects. | PMC10129324 | elife-83694-fig1-figsupp1.jpg |
0.417078 | 4b67fbd4224f4e2c846d22eec3598b34 | Immunogenicity of third dose of coronavirus disease 2019 (COVID-19) vaccine in seronegative cancer patients.(A) Figure showing change in anti-SARS-CoV-2 (anti-S) antibody titer at 4 weeks for entire cohort n=106. (B) Figure showing change in anti-S antibody titer at 4 weeks split by cancer type (solid cancer, lymphoid cancer, and myeloid cancer) n=106. (C) Figure showing effect of Bruton’s tyrosine kinase inhibitor (BTKi) therapy on anti-S antibody titer at baseline and 4 weeks of third dose n=12 patients that received BTKi Kruskal-Wallis test. (D) Figure showing effect of anti-CD20 antibody therapy on anti-S antibody titer at baseline and 4 weeks of third dose n=25 patients that received anti-CD20 antibody, Kruskal-Wallis test. (E) Figure showing effect of prior COVID-19 infection on anti-S antibody titer at baseline and 4 weeks of third dose n=9 patients with COVID infection, Kruskal-Wallis test. (F) Figure showing effect of booster type (BNT162b2 vs mRNA 1273) on anti-S antibody titer at baseline and 4 weeks of third dose. (G) Line diagram showing correlation between anti-spike IgG titer and baseline T-cell activity at baseline and 4 weeks n=88 for baseline, n=89 for 4 weeks; Spearman’s test. (H) Line diagram showing correlation between anti-S titer and signal inhibition for neutralization against wild-type (WT) virus at baseline and 4 weeks. n=103 for baseline, n=100 for 4 weeks; Spearman’s test. (I) Anti-spike IgG titers at baseline, 4 weeks, and 6 months after third dose of COVID-19 vaccine in cancer patients. Line shows means with error bars (SD).n=47. All statistical tests performed at a pre-determined threshold of p<0.05 for statistical significance. | PMC10129324 | elife-83694-fig1.jpg |
0.413457 | 5cd78fb8c290487486e9435bc71cc9b0 | Immunogenicity of the fourth dose of coronavirus disease 2019 (COVID-19) vaccine in cancer patients with seronegativity after three doses.(A) Anti-spike IgG levels after the fourth dose of COVID-19 vaccine for the entire cohort n=18. (B) Correlation of baseline IgM levels with response to fourth dose of vaccine, n=18 Kruskal-Wallis test. (C) Line diagram showing correlation between anti-SARS-CoV-2 (anti-S) titer and neutralization activity for wild-type (WT) virus at baseline and 4 weeks, n=18, Spearman’s test. (D) Line diagram showing correlation between titer and neutralization activity for Omicron strain at baseline and 4 weeks n=18, Spearman’s test. All statistical tests performed at a pre-determined threshold of p<0.05 for statistical significance. | PMC10129324 | elife-83694-fig2.jpg |
0.420565 | ee62c7b9328c494894eb47c79c32f809 | Nitrogen removal performance and microbial community profiles of High_BS (high loading) and Low_BS (low loading).Species-specific nitrogen conversion rates during the long-term operation of High_BS (a) and Low_BS (b): nitrite removal rate by anammox bacteria (rAN), nitrite removal rate by n-DAMO bacteria (rDB), and nitrate removal rate by n-DAMO archaea (rDA). Batch tests were performed on day 974 to validate the variations of nitrogenous substrates and methane of High_BS in 1 h (c) and of Low_BS in 6 h (d). e Microbial community structures of High_BS and Low_BS were revealed from 16S rRNA gene amplicon sequencing data, 16S rRNA genes from the metagenomic reads and recovered MAGs. f Relative expression of MAGs. DAMOA1 is the only MAG of n-DAMO archaea affiliated with “Ca. M. nitroreducens”, while DAMOB1 and DAMOB2 are the MAGs of n-DAMO bacteria belonging to “Ca. Methylomirabilis”. AMXK1, AMXB1 and AMXB2 are anammox MAGs. BAC2, VER1, CHL3 and PRO7 are MAGs with expression above 1% in either High_BS or Low_BS, belonging to Bacteroidota, Verrucomicrobiota, Chloroflexota and Proteobacteria, respectively. Numbers in the cell indicate the relative abundance or TPM fraction. | PMC10130057 | 43705_2023_246_Fig1_HTML.jpg |
0.419746 | d4b0c167d71d4880aa24f235237a791c | Phylogenetic and genomic features of n-DAMO bacteria.a Phylogenetic placement of the two n-DAMO bacteria MAGs recovered in this study (DAMOB1 and DAMOB2) using 120 bacterial-specific marker genes with publicly available non-redundant candidate division Methylomirabilota genomes (see method for details). The tree was inferred using the maximum-likelihood method, and bootstrap values were calculated using nonparametric bootstrapping with 100 replicates. The scale bar represents amino acid substitutions per site. The shaded area is clade a of Methylomirabilota phylum. b Average amino acid identity (AAI) as indicated by the values in cells. c Schematic representation showing the arrangement of genes for denitrification and methane oxidation in two recovered genomes of n-DAMO bacteria in the present study and “Ca. M. oxyfera” (GCF_000091165.1). Arrows represent genes and indicate the transcriptional direction. | PMC10130057 | 43705_2023_246_Fig2_HTML.jpg |
0.406741 | 3be114ccbb8f4cbfbe4c797c89b19be6 | Relative expression of genes involved in major methane and nitrogen metabolic pathways encoded by each MAG.Colour intensity represents gene expression. Gene expression was relativized by median TPM value across all CDS within a given genome (see details in Methods). A value of one means two times of median expression among all CDS in a given genome. Orange cell indicates the expression of the encoded gene is undetectable. Bubble diameter represents the gene count. Only the MAGs with expression >1% were presented. The TPM values of encoded genes by each MAG were listed in Supplementary Dataset 2. | PMC10130057 | 43705_2023_246_Fig3_HTML.jpg |
0.433344 | 9c16a87b6fe34d1faf1e853e6ae7577a | Expression of predicted peptides, transporters and amino acids biosynthetic and degradation pathways encoded by the active populations in high-nitrogen loading system High_BS.a Gene count (bubble diameter) and expression (colour intensity, compared to median gene expression of genome) of peptidases possibly involved in EPS matrix degradation across active MAGs. The subcellular location of peptidases was predicted using the subcellular localisation predictor (CELLO 2.5) [55]. b Gene count (bubble diameter) and expression (colour intensity, compared to median gene expression of MAGs) of amino acid, peptide and protein transporters across active genomes. c Presence and expression of amino acid biosynthesis and degradation pathways across active MAGs. Bracketed numbers rank the metabolic cost of amino acid biosynthesis based on [45], with 1 being the most costly. Top, middle and bottom panels include amino acids that are hydrophilic, hydrophobic and with special structured side chains, respectively. Amino acid types of glucogenic, ketogenic or both are highlighted in black, green and red, respectively. A detailed summary can be found in Supplementary Dataset 2. | PMC10130057 | 43705_2023_246_Fig4_HTML.jpg |
0.442021 | 6396a33d0e4f42c096a7c96c3c4d5552 | Schematic of metabolic networks.a Schematic of microbiota metabolic network under high-loading and b low-loading conditions: bubble size indicates the relative abundance, while the colour intensity indicates the expression fraction. c Integrating metabolic network related to nitrogen and methane conversions in high-loading system High_BS: blue arrows indicate nitrogen cycling, while red arrows indicate carbon cycling. | PMC10130057 | 43705_2023_246_Fig5_HTML.jpg |
0.482831 | 13ff50c2180d4cffb103774414d5cd38 | Study overview. COSMIN: consensus-based standards for the selection of health measurement instruments; Posbindu PTM; Pos Pembinaan Terpadu Penyakit Tidak Menular. | PMC10131706 | resprot_v12i1e41146_fig1.jpg |
0.488099 | 72cb2f73b84443049cc888c9f4217860 | Effects of web-based access on the number of consultations, administrative actions, and patient questions in general practices. | PMC10131748 | jmir_v25i1e41832_fig1.jpg |
0.507581 | 687832bdbfe148eb89b8142d6f93fe65 | Effects of web-based access on specified general practice workflow processes. | PMC10131748 | jmir_v25i1e41832_fig2.jpg |
0.407869 | de3c4369347b4a049d92b1a94922ce35 | Effects of web-based access on time burden in general practices, specified by function. | PMC10131748 | jmir_v25i1e41832_fig3.jpg |
0.439887 | f432bac6416e40aca8ae1e25cf5a72eb | Liver‐specific deletion of PMVK inhibits HCC growth in mice. A) Schematic overview of DEN/CCl4‐induced HCC mice model. During this period, adeno‐associated virus containing PMVK were given via tail‐vein injection. B) Liver images extracted from the indicated mice. C) Tumor number of each liver from (B). D) Average tumor volume of each liver from (B). E) Serum TC levels in mice from (B). F) Serum TG levels in mice from (B). G) Representative IHC images of H&E and Ki67 in tumor tissues from (B). H) Adeno‐associated virus containing the indicated plasmids were delivered via tail‐vein injection. Liver images extracted from the indicated mice. I) Tumor number of each liver for (H). J) Average tumor volume of each liver for (H). K) Percent survival of mice for (H). | PMC10131864 | ADVS-10-2204909-g001.jpg |
0.44945 | a1518e0e9c7543dabc94a3295a715903 | The PMVK inhibitor, PMVKi5, suppresses HCC growth in vitro and in vivo. A) Chemical structure formula of PMVKi5. B) Kd values were determined as the binding of PMVKi5 to purified human PMVK or PMVK mutant (K17A, S20A, G21A, K22A, and D23A) proteins using MST. C) In vitro kinase activity assays D) Reco9mnbinant GST‐β‐catenin‐His and PMVK‐His were used for in vitro kinase reactions, with or without the addition of 20 µ
m PMVKi5. β‐catenin phosphorylation was identified with β‐catenin p‐Ser184 antibody. E) Immunoblot for the indicated proteins in Huh7 and Hep3B cell lines following exposure to 20 µ
m PMVKi5 for 6 h. F) Schematic overview of DEN/CCl4‐induced HCC mice model. For the prevention group, mice were treated between 16 and 20 weeks, with 30 mg kg−1 PMVKi5 i./p. every 2 days for a total of 14 doses for. In the treatment group, mice were treated from 23 to 27 weeks. After 28 weeks, livers were extracted. G) Liver images from the indicated mice. H) Tumor number of each liver for (G). I) Average tumor volume of each liver for (G). J) Immunoblot analysis for the indicated proteins in tumor tissues from (G). K) Representative IHC images of H&E and Ki67 in tumor tissues from (G). Scale bar, 50 µm. | PMC10131864 | ADVS-10-2204909-g002.jpg |
0.418395 | 82d9aef090804dfab00cda9d656bc557 | PMVK‐produced MVA‐5PP competitively binds CKIα to stabilize β‐catenin. A) HEK293 cells were transfected with the indicated plasmids and then lysed in RIPA buffer. Immuno‐precipitated HA‐β‐catenin proteins were subjected to immunoblot assay. B) MVA‐5PP was added to Huh7 and Hep3B cells at the indicated final concentrations and subjected to immunoblot assay β‐catenin (total and p‐S184 form), c‐Myc and Cyclin D1 protein levels. C) HEK293 cells were transfected with the indicated plasmids, supplemented with MVA‐5PP (200 µ
m) and then lysed in RIPA buffer. Immuno‐precipitation of HA‐β‐catenin proteins were subjected to immunoblot assay. D) The molecular docking of MVA‐5PP and CKIα is shown based on the crystal structure of CKIα (PDB code: 6GZD). Lys 46, Tyr 64, and Asp 157 indicate the bound residues. E) Kd values were determined by MST for MVA‐5PP bound to purified human CKIα or CKIα mutant (K46A, Y64A and D157A) proteins. Data are shown as mean ± SD. F) Purified recombinant GST‐β‐catenin‐His protein and FLAG‐CKIα protein were subjected to in vitro phosphorylation assays at different concentrations of MVA‐5PP. Immunoblotting was performed using β‐catenin p‐Thr41/Ser45 antibody. G) Recombinant GST‐β‐catenin‐His and FLAG‐GSK3β proteins were subjected to in vitro phosphorylation assays at different concentrations of MVA‐5PP followed by immunoblotting using β‐catenin p‐Thr41/Ser45. H) Immunoblot assay of β‐catenin (total and p‐S184 form), c‐Myc, Cyclin D1, and CKIα protein levels after MVA‐5PP (200 µ
m) treatment in the indicated PMVK‐knockdown or control cancer cell lines. | PMC10131864 | ADVS-10-2204909-g003.jpg |
0.438771 | 789391c019634fd0ba7627350c9d3484 | PMVK expression is increased in human HCC and correlates with poor survival. A) Western blot analysis for the indicated proteins in human HCCs. T, tumor; N, adjacent normal tissue. B–F) The intensities of PMVK, β‐catenin (total and p‐S184), c‐Myc and Cyclin D1 for (A) were quantified by densitometry, with β‐actin as a normalizer. Data are shown as mean ± SD. G–O) Correlation of different protein levels in HCC tissues from (A). Each point is an individual sample. P) PMVK mRNA levels in normal liver and HCCs from TCGA. Q) PMVK gene copy number in normal liver and tumor tissues from TCGA. R) Correlation of PMVK mRNA level with its DNA copy number in HCC tissues from TCGA dataset. Each point is an individual sample. S) Kaplan–Meier curves with univariate analysis of the survival of patients with HCC based on high versus low expression of PMVK. Data are shown as mean ± SD. The P values were determined by paired two‐sided Student's t‐test for (B–F) and unpaired two‐sided Student's t‐test for (P) and (Q). The correlation coefficient (r) and p values in (G–O and R) were determined using two‐tailed Pearson correlation analysis. | PMC10131864 | ADVS-10-2204909-g004.jpg |
0.507586 | de7d2d73193849b48e730c9c9d996787 | Knockdown of PMVK reduces β‐catenin signaling and inhibits tumor growth. A) β‐catenin, c‐Myc, Cyclin D1, and PMVK protein expression in the indicated cancer cell lines. B) mRNA expression of β‐catenin in the indicated cancer cell lines. C) HEK293 cells were transfected with the indicated vectors. Cells were treated with CHX (50 µg mL−1) for the indicated time and the expression of PMVK and β‐catenin were analyzed by western blotting. D) The intensity of β‐catenin expression for each time point in (C) was quantified by densitometry, with β‐actin as a normalizer. E) Distribution of PMVK and β‐catenin protein levels in the nucleus or cytoplasm in the indicated PMVK‐knockdown or control cancer cell lines. β‐actin as a cytoplasm normalizer and Histone H3 as a nucleus normalizer. F) qRT‐PCR analysis was performed to measure the mRNA levels of PMVK and β‐catenin target genes in Huh7 cells. G) Cell proliferation assays were performed in Huh7 (up) and Hep3B (down) cells stably expressing the indicated plasmids. rWT, rescued wild type PMVK. H) Subcutaneous xenograft experiments were performed in Huh7 (up) and Hep3B (down) cells stably expressing the indicated plasmids. n = 5 mice per group. I) Subcutaneous xenograft tumor weight for (H). Data are shown as mean ± SD. | PMC10131864 | ADVS-10-2204909-g005.jpg |
0.480961 | 78814181a5ce42aa93ba9f7399f2cc83 | PMVK‐mediated β‐catenin Ser184 phosphorylation, protein stability and nuclear localization. A) Endogenous interaction between PMVK and β‐catenin in Huh7 and Hep3B cell lines. Anti‐PMVK Antibody (H‐9) from mouse as an IP antibody. Mouse lgG was used as a negative control. WCL, Whole cell lysate. B) Tandem mass spectrometry spectrum of β‐catenin pSer184. Detected productions are indicated in red (b ions) and blue (y ions). See Table S2, Supporting Information, for details. C) Recombinant purified GST‐β‐catenin‐His and PMVK‐His proteins were subjected to an in vitro kinase reaction. β‐catenin phosphorylation was identified with β‐catenin p‐Ser184 antibody. Fast AP, Fast alkaline phosphatase. D) HEK293 cells were transfected with the indicated vectors. Cells were treated with CHX (50 µg mL−1) for the indicated times and the levels of different β‐catenin mutants were analyzed by Western blotting. E) The expression intensity of different β‐catenin mutants at each time point in (D) was quantified by densitometry, with β‐actin as a normalizer. Data are shown as mean ± SD. F) HEK293 cells were transfected with the indicated plasmids, treated with MG132 for 6 h and then lysed in RIPA buffer. Immuno‐precipitated HA‐β‐catenin proteins were subjected to immunoblot assay with Myc‐tag antibody. G) Distribution of different β‐catenin mutants protein levels in the nucleus or cytoplasm in Huh7 and Hep3B cells transfected with the indicated plasmids. β‐actin as a cytoplasm normalizer and Histone H3 as a nucleus normalizer. H) HEK293 cells were transfected with the indicated plasmids and then lysed in RIPA buffer. Immuno‐precipitation of different β‐catenin mutants proteins with anti‐HA magnetic beads and subjected to immunoblot assay. | PMC10131864 | ADVS-10-2204909-g007.jpg |
0.43176 | aa75faeee52c4031b571f04abf29fe11 | CRISPR‐Cas9 library screens for PMVK stabilizing β‐catenin protein levels in Huh7 cells. A) Workflow of GeCKO in Huh7 cells screens to identify potential resistance genes to β‐catenin inhibitors. B) Venn diagram showing 174 negative genes (significantly depleted sgRNAs), 264 metabolite interconversion enzymes, and 5386 oncogenes upregulated in HCC. See Table S1, Supporting Information, for details. C) Volcano map showing sgRNA library screening distribution. Blue dots indicate significant deletion of sgRNAs (negative selection). Orange dots indicate significant enrichment of sgRNAs (positive selection). Red dots show screening of positive gene representatives. FC, Fold change. D) Each PMVK sgRNA was analyzed in pairs in the DMSO and XAV‐939 groups. E) Cell viability was determined by MTT after 2 µg shRNA#1 PMVK plasmid transiently transfected with Huh7, DMSO or XAV‐939 (30 µ
m) treated for 72 h. Data are shown as mean ± SD. F) Representative IHC images of H&E, Ki67, PMVK, total β‐catenin and β‐catenin p‐Ser184 in wild‐type, PMVK+/− and PMVK−/− E12.5 embryos. Scale bar, 1 mm or 50 µm. The IHC staining experiment was performed twice. | PMC10131864 | ADVS-10-2204909-g008.jpg |
0.435145 | abc3e37795a54b28947bb23c4bb954d3 | Linear regression coefficients for the features selected by the single-task FSHD Clinical Score and TUG models. Features with a coefficient of zero are not shown. FSHD: facioscapulohumeral muscular dystrophy; TUG: Timed Up and Go. | PMC10131943 | formative_v7i1e41178_fig1.jpg |
0.436062 | 205a99e04a5348aca6896ee4a4ba3972 | True FSHD Clinical Scores and TUG times against the predicted scores using the respective FSHD Clinical Score and TUG regression models. The lines represent a regression line with a 95% CI band. FSHD: facioscapulohumeral muscular dystrophy; TUG: Timed Up and Go. | PMC10131943 | formative_v7i1e41178_fig2.jpg |
0.380348 | 51bbba1b86634ce889ebbec48812a945 | SHAP (SHapley Additive exPlanations) variable importance plot showing the feature importance of the top 20 most important features, in which the features are ranked in descending order. Each scatter point represents one prediction. The color of the scatter point reflects the value of the real data. If the actual value of the data point was high, then the color was red. If the value was low, then the color was blue. The SHAP value, as illustrated on the x-axis, shows the direction and magnitude of each feature’s contribution toward predicting the facioscapulohumeral muscular dystrophy symptom severity. | PMC10131943 | formative_v7i1e41178_fig3.jpg |
0.431997 | 90002c29b0f640e7b658981edc4a8380 | Scatterplot of the estimated FSHD Clinical Scores and TUG times in relation to the actual FSHD Clinical Scores and TUG using the multi-task learning regression model. The lines represent the regression lines with a 95% CI band. FSHD: facioscapulohumeral muscular dystrophy; TUG: Timed Up and Go. | PMC10131943 | formative_v7i1e41178_fig4.jpg |
0.446709 | af732687f2dd446bb20eaac52b4d1bb2 | Evaluating the performance of the single-task FSHD Clinical Score, TUG, and the multitask FSHD Clinical Score and TUG regression models trained on an incrementally increasing time window. The colored lines represent the 3 types of regression models trained on the data (Elastic Net, Random Forest Regressor, and Gradient Boosting Regressor). For each model and each incremental time window, the top and bottom plots show the R2 and RMSE, respectively. The lines represent the median performance, and the bands represent the 95% CI. FSHD: facioscapulohumeral muscular dystrophy; RMSE: root mean square error; TUG: Timed Up and Go. | PMC10131943 | formative_v7i1e41178_fig5.jpg |
0.415472 | 81b02a68eefb4090bbfc52d45e9cef58 | Evaluating the performance of the single-task FSHD Clinical Score, TUG, and the multitask FSHD Clinical Score and TUG regression models trained on the first week of data to estimate symptom severity for the subsequent weeks. The colored lines represent the 3 types of regression models trained on the data (Elastic Net, Random Forest Regressor, and Gradient Boosting Regressor). For each model and each week, the top and bottom plots show the R2 and RMSE respectively. The lines represent the median performance, and the bands represent the 95% CI. FSHD: facioscapulohumeral muscular dystrophy; RMSE: root mean square error; TUG: Timed Up and Go. | PMC10131943 | formative_v7i1e41178_fig6.jpg |
0.501893 | 9123eabdb7e145fab8dcaac4a591ce4b | Flow chart of study design and data analysis.AKI, acute kidney injury according to KDIGO criteria; RRT, renal replacement therapy. | PMC10132159 | jciinsight-8-165740-g014.jpg |
0.411223 | edc14d0ff5d245d98ae1513ea54df055 | Blood suPAR levels discriminate between maximum AKI stages, varying AKI courses, and poor (kidney) outcome in human sepsis at any time within 7 days of sepsis diagnosis.(A–C) Outcome-related course of serum creatinine (SCr) and soluble urokinase plasminogen activator receptor (suPAR) over 7 days after sepsis diagnosis (0 hours, n = 200; 12 hours, n = 190; 24 hours, n = 190; 48 hours, n = 186; 3 days, n = 177; 4 days, n = 175; 5 days, n = 167; 7 days, n = 155) and (D–F) outcome in relation to suPAR quartiles at baseline. *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001. NS, P > 0.05. AKI, acute kidney injury; IQR, interquartile range; MAKE7, major adverse kidney events within 7 days of sepsis diagnosis; RRT, renal replacement therapy. Data are reported as box-and-whisker plots (interquartile range, minimum to maximum) (A–C), unadjusted odds ratio (95% CI) (D), and percentage (E and F). One-way ANOVA (A–C) and χ2 (E and F) tests were used for group comparisons. | PMC10132159 | jciinsight-8-165740-g015.jpg |
0.419994 | 39697127bff84daba2612320e6ae5b04 | Elevated blood levels of suPAR are associated with enhanced kidney tissue damage, kidney function impairment, and poor (kidney) outcome in murine sepsis.Sepsis was induced via i.p. injection of 250 μL cecal slurry (CS) in C57BL/6 WT (n = 16), uPAR-knockout (KO, n = 15), and transgenic C57BL/6 with overexpression of suPAR (OE, n = 14). Glycerol (GLY, 15%) served as control in WT (vehicle control, n = 10). (A) H&E staining of kidneys from different mouse strains 24 hours after sepsis induction. Original magnification, ×40. Scale bar: 100 μm. (B) Maximum serum creatinine (SCr) changes from baseline within 24 hours and (C) urea 24 hours after sepsis induction. (D) suPAR levels at baseline and (E) 24 hours after sepsis induction. (F) IL-6 levels 6 hours after sepsis induction. (G) Survival analysis of different mouse strains. Survival: WT GLY, 10/10 (100%); WT CS, 11/16 (69%); KO CS, 13/15 (87%); OE CS, 7/14 (50%). Data are reported as mean ± SEM. One-way ANOVA test was used for group comparisons (B–F), and the Kaplan-Meier method and log-rank testing were used for survival analyses (G). | PMC10132159 | jciinsight-8-165740-g016.jpg |
0.520595 | 2b89cd866f8a4622b55b605e3724fcd3 | Characterization of kidney leukocyte subsets in C57BL/6 WT, uPAR-KO, and transgenic C57BL/6 with overexpression of suPAR reveals a link between increased blood suPAR levels and kidney T cell accumulation, kidney function impairment, and local upregulation of inflammatory cytokines.(A–D) Strain-dependent characterization of leukocyte subsets by flow cytometry after 24 hours of sepsis induction (left) via i.p. injection of 250 μL cecal slurry (CS) and untreated mice (right). Injection of 15% glycerol (GLY) served as control (vehicle solution). (E) Exemplary double immunofluorescent staining for podocin (green) and CD8+ T cells (red) of kidney tissue from different mouse strains after 24 hours of sepsis. Nuclei were stained with DAPI (blue). Spleen tissue served as positive (primary and secondary antibody) and negative (secondary antibody only) control (data not shown). To quantify kidney immune cell aggregation, the mean cell number was determined from 10 representative high-power fields per animal (see supplemental material). Original magnification, ×40. Scale bar: 100 μm. (F) Correlation analysis of kidney T cells and corresponding blood serum creatinine (SCr) and suPAR levels in WT sepsis. (G) Kidney Luminex analysis of homogenized kidney tissue of untreated WT and suPAR-OE mice. CCL, C-C motif chemokine ligand 3; MFI, median fluorescence intensity; TSP4, thrombospondin 4. Data are reported as mean ± SEM. One-way ANOVA test was used for multiple group comparisons (A–D), correlations were assessed by using Pearson’s correlation analysis (F), and 2-tailed Student’s t test was used for pairwise comparisons (G). | PMC10132159 | jciinsight-8-165740-g017.jpg |
0.404424 | ce4d4e77ae0440fe9f3d540b8d69f720 | Effects of MZD on tissue morphology of UTI induced by ESBLs E. coli in rats. (A) Representative images showing HE staining of bladder and kidney in rats. Magnification, ×400. (B) Representative images showing Masson staining of bladder and kidney in rats. Magnification, ×400. (C) Percentage of fibrotic tissue in the bladder and kidney of rats stained by Masson. Data were shown as mean ± SD. *p < 0.05, **p < 0.01, ***p < 0.001, compared with the control group; #p < 0.05, ##p < 0.01, ###p < 0.001, compared with the model group; &p < 0.05, &&p < 0.01, &&&p < 0.001, compared with the MZD + LVFX group. MZD: modified Zhibai Dihuang pill; LVFX: levofloxacin. | PMC10132235 | IPHB_A_2199786_F0001_C.jpg |
0.435295 | 2e4c952289784e2793b37135e9094f6c | Urine bacterial culture of rats with UTI caused by ESBLs E. coli. (A) Representative plate showing the bacterial culture of urine. (B) The number of bacterial culture colonies in the urine of rats. Data are shown as mean ± SD. *p < 0.05, **p < 0.01, ***p < 0.001, compared with the control group; #p < 0.05, ##p < 0.01, ###p < 0.001, compared with the model group; &p < 0.05, &&p < 0.01, &&&p < 0.001, compared with the MZD + LVFX group. MZD: modified Zhibai Dihuang pill; LVFX: levofloxacin. | PMC10132235 | IPHB_A_2199786_F0002_C.jpg |
0.414111 | b5df5589c90b48d59ce3dc8ed5b5b081 | Comparison of the biofilm formation ability of ESBLs E. coli. (A) The biofilm formation was quantitatively determined by crystal violet staining. (B) Representative images showing biofilm formation observed by laser scanning electrolysis. Magnification, ×20,000. Data are shown as mean ± SD. *p < 0.05, **p < 0.01, ***p < 0.001, compared with the SHRN group; #p < 0.05, ##p < 0.01, ###p < 0.001, compared with the MS-MZD + LVFX group. SHRN: negative serum control group; MS-MZD: medicated serum of modified Zhibai Dihuang pill group; LVFX: levofloxacin group. | PMC10132235 | IPHB_A_2199786_F0003_B.jpg |
0.387268 | 50a338d05c6c4a8495e1601f0c0900c3 | Effects of MS-MZD on the relative gene expression of luxS, pfS, and ompA in ESBLs E. coli. Data are shown as mean ± SD. *p < 0.05, **p < 0.01, ***p < 0.001, compared with the SHRN group; #p < 0.05, ##p < 0.01, ###p < 0.001, compared with the MS-MZD + LVFX group. SHRN: negative serum control group; MS-MZD: medicated serum of modified Zhibai Dihuang pill; LVFX: levofloxacin. | PMC10132235 | IPHB_A_2199786_F0004_B.jpg |
0.473587 | 056a5ab431c84291b99524ae3f56baef | ‘Heat map’ showing frequency of phenotype–genotype associations with gene mutations most often identified in individuals presenting with congenital hypogonadotropic hypogonadism (CHH) or Kallmann Syndrome (KS).Colour code for organ involvement: Red, typically present; orange, mostly present; yellow, sometimes seen; green, not described. Previous gene name given in brackets. | PMC10133250 | 41431_2022_1261_Fig1_HTML.jpg |
0.426611 | e72f9ce63eb24c6cbf58c7c799ef754b |
Flow diagram of the study. mTECIST: Modified response evaluation criteria in solid tumors criteria; CTCAE: Common Terminology Criteria for Adverse Events; HCC: Hepatocellular carcinoma; AFP: Alpha fetoprotein; DSA: Digital subtraction angiography; OS: Overall survival; TTP: Time to progression; BCLC: Barcelona Clinic Liver Cancer; PD-1: Programmed death 1; CT: Computed tomography; MRI: Magnetic resonance imaging; irAE: Immune-related adverse event. | PMC10134210 | WJGO-15-689-g001.jpg |
0.409493 | e7332a150494493abc863cdc549b17b5 |
Kaplan-Meier curves describing the overall survival of all patients (n = 190) and the time to progression of patients who achieved disease control (n = 99). A: Survival curve; B: Time to progression curve. OS: Overall survival; TTP: Time to progression. | PMC10134210 | WJGO-15-689-g002.jpg |
0.406252 | feb9076a31484c8aa282c1b2a929285c |
Waterfall plots of percentage change in tumor burden from baseline (n = 190). The “y” axis represents the percentage change in tumor burden from baseline by treatment. The immune-related adverse events are distinguished by different colors. Negative/positive values represent maximum tumor reduction or minimum tumor increase, respectively. A: 91 patients had progressive disease; B: 99 patients achieved complete response, partial response, or stable disease. irAE: Immune-related adverse event. | PMC10134210 | WJGO-15-689-g003.jpg |
0.481088 | dedb5620deb444b793170b83ac9b0249 |
Spider plot displaying tumor response in 25 patients with hypothyroidism. PD: Progressive disease; SD: Stable disease; PR: Partial response; TBS: Tumor burden score. | PMC10134210 | WJGO-15-689-g004.jpg |
0.417053 | cfcec4967bc94009bd6fb963cf7317ce |
Prognosis comparison between hypothyroidism group and non-hypothyroidism group. A: Survival curve; B: Time to progression curve. | PMC10134210 | WJGO-15-689-g005.jpg |
0.448746 | 7134441e24874068abfdf0b0fca468d6 | Overview of the variety of 3D AMP structures. (a) Crotamine from PDB code 1Z99; (b) fowlcidin from PDB code 2AMN; (c) circullin B from PDB code 2ERI; (d) LEAP-2 from PDB code 2L1Q. Yellow bonds represent disulfide bridges. | PMC10135148 | antibiotics-12-00725-g001.jpg |
0.536652 | d3c0ec15ab9e40b689c2f398d3ba6e3f | Number of experimental assays retrieved for the top five species by category (a). Venn diagram showing the distribution of peptides per category (b). | PMC10135148 | antibiotics-12-00725-g002.jpg |
0.443091 | dfb093bbeb2a49158463b54549590791 | Comparison of amino acid composition (a), global net charge (b), and molecular weight (c) between AMPs and Non-AMPs. | PMC10135148 | antibiotics-12-00725-g003.jpg |
0.444625 | 7079785fdcc64d319e652beb862b136e | Matrix of labels for the common peptides between Gram− and Gram+ categories. | PMC10135148 | antibiotics-12-00725-g004.jpg |
0.379152 | e563501495954cfca88903e7af3c5d0d | PCA (a) and t-SNE (b) projections of physicochemical descriptors between common peptides of Gram+ and Gram− categories. In blue are peptides are labelled as AMP in both categories, in red are peptides are labelled as Non-AMP in both categories, in green are peptides labelled AMP for Gram+ and Non-AMP for Gram−, and in black is the opposite. | PMC10135148 | antibiotics-12-00725-g005.jpg |
0.380477 | a798bb9f01d241a98bf4f7ab44ece58a | Top 20 features importance plot and their impact on the external test set prediction for CalcAMP+ (a) and CalcAMP- (b). Shown are physicochemical properties such as molecular weight (MW), Charge, or Length. However, the majority of the top features were from CTD descriptors. They are identifiable by their names beginning with an underscore character, followed by the property and finally the component characteristics: composition (C), transition (T), and distribution (D). | PMC10135148 | antibiotics-12-00725-g006.jpg |
0.401936 | d944a6f47bd24f8a861db9b529f6ec36 | Confusion matrix for CalcAMP+ model prediction versus CalcAMP- (a) and AMP probability score by predicted class (b). | PMC10135148 | antibiotics-12-00725-g007.jpg |
0.446089 | d7097bfe7a3b427da3ebe7dbd6351bcd | Receiver operator characteristic (ROC) curves of the different AMP classifiers and their area under the curve score. | PMC10135148 | antibiotics-12-00725-g008.jpg |
0.371801 | 75f41978a3ee45e48d383f3b37dc724d | Top 20 feature importance plot and their impact on the external test set prediction for CalcAFP. | PMC10135148 | antibiotics-12-00725-g009.jpg |
0.61241 | 75dc4127b75e46978b5ab302de555d7b | Different examples of peptides with their reported experimental activities and their label. | PMC10135148 | antibiotics-12-00725-g010.jpg |
0.460334 | c4b7d1edbb8547e49d05c023e826804d | PCA projections of the training set (blue) and external test set (red) for Gram+ (a) and Gram− (b) categories. | PMC10135148 | antibiotics-12-00725-g011.jpg |
0.497621 | a4ecff23f05c46c2b8b707c98316df40 | CONSORT Diagram: patient inclusion and exclusion process are displayed. | PMC10135963 | biomedicines-11-01087-g001.jpg |
0.40161 | f2c0996722c649bb99f381c4d02b993d | Liver damage in NAFLD. | PMC10136128 | antioxidants-12-00903-g001.jpg |
0.435502 | 2877611145c54cb38e568ed342ef1f32 | The impact of vitamins on hepatocytes affected by NAFLD. | PMC10136128 | antioxidants-12-00903-g002.jpg |
0.473944 | 848e44f48b9b42f9877d0a4a84a92bc8 | The metabolic pathway of tetrahydrobiopterin (BH4). AADC, aromatic amino acid decarboxylase; DHFR, dihydrofolate reductase; DHPR, dihydropteridine reductase; GTPCH, GTP cyclohydrolase 1; ne, non-enzymatic; PAH, phenylalanine hydroxylase; PCD, pterin-4a-carbinolamin dehydratase; PTPS, 6-pyruvoyltetrahydropterin synthase; SR, sepiapterin reductase; TH, tyrosine hydroxylase; TPH, tryptophan hydroxylase (adapted from Ref. [3], Figure 1). | PMC10136628 | children-10-00727-g001.jpg |
0.493461 | 8a2926574d744e6dbe2640d67560a4cf | Dynamic representation of the phenylalanine levels in our patients. The dotted line represents the normal upper limit of serum phenylalanine concentrations (66.5 µmol/L). The arrows represent the start of the specific treatment (Sapropterin). | PMC10136628 | children-10-00727-g002.jpg |
0.385078 | 75f8cc5a922b400eb55b5a0627b4fe15 | Immune function genes from AA and EA breast cancer exosomes show a racial disparity. (A) Nanostring PanCancer Immune gene analysis, which includes 730 immune function genes, showed that, relative to EA breast cancer exosomes, AA breast cancer exosomes had lower expression of overall immune genes as well as innate immune response genes and adaptive immune response genes. (B) A volcano plot showed the differential expression of immune genes in AA and EA breast cancer exosomes, where a few genes such as CD47, CCL5, PPBP, and TGFB1 were increased in AA exosomes, whereas CD24, IL26, CTSL, and GAGE1 were increased in EA exosomes. (C) Cytoscape analysis showed that genes interacting through the chemokine signaling pathway, the cytokine–cytokine receptor pathway, the MAPK signaling pathway, and the NF-kB signaling pathway were upregulated in AA exosomes as compared to EA exosomes (D) Differential expressions of chemokine, cytokine, and interleukin function genes in AA and EA breast cancer exosomes, notably PPBP, CXCL5, CCL5, and TGFB1 (involved in cancer progression) were increased in AA exosomes. (E) Hierarchical clustering showed that T-cell activation genes and CD8+ T cell genes were increased in EA exosomes, whereas macrophage marker genes, especially the expression CD47, were increased in AA exosomes. | PMC10136634 | cancers-15-02282-g001.jpg |
0.426112 | 79b4c977892c4518956287147aa03c9f | Kaiso represses the expression of several immune genes, including THBS1. (A). Hierarchical clustering of differentially expressed genes from PanCancer Nanostring Immune Profiling showed that there were fewer immune genes expressed in sh–Kaiso cells as compared to control sh-Scr cells. (B). Cytoscape analysis shows that genes interact through the chemokine signaling pathway, the cytokine–cytokine receptor pathway, the MAPK signaling pathway, and the NOD–like receptor signaling pathway, and the NF–kappa B signaling pathway was downregulated in sh-Kaiso cells as compared to sh-Scr cells. (C). A Venn diagram shows the association of immune genes between genes that were upregulated in AA exosomes and genes downregulated in sh-Kaiso cells (identified by color code). A total of 31 genes, including CD47 and TGFB1, were common genes among these two groups. (D). Kaiso-depleted cells showed significantly lower expression of CD47 with significantly higher expression of THBS1 as compared to sh–Scr cells. The statistical method used was the two–tailed paired t test. (E). Nanostring immune profiling showed that Kaiso repressed several genes, including THBS1, based on the downregulated gene expression in sh–Scr cells. | PMC10136634 | cancers-15-02282-g002.jpg |
0.418788 | 26cb8831a8854f95aab37be4962f8ec4 | Kaiso directly regulates the expression of the tumor suppressor, THBS1. (A) Kaiso depletion resulted in significantly higher expression of THBS1 in exosomes from MDA-MB-231 cells, whereas the expression of CD47 and SIRPA was decreased. The statistical method used was the two-tailed paired t test. (B) As consistent with exosomes, both gene expression, and protein expression analysis revealed that Kaiso depletion resulted in a significantly high expression of THBS1 in MDA-MB-231 cells, whereas the expressions of CD47 and SIRPA were decreased. The statistical method used was the two-tailed paired t test. (C) Schematic illustration of the THBS1 promoter showing the Kaiso binding site on the CpG island. Two oligonucleotides were designed as CHIP primers from two different sites where Kaiso binds in a methylation-dependent manner. (D,E) CHIP experiments with MDA-MB-231 chromatin demonstrated that Kaiso binds to the methylated region of the THBS1 promoter and that 5-aza reversed the binding. Both PCR and gel electrophoresis confirmed the binding. Input, 1% input DNA; Positive, anti-RNA Polymerase II and Negative, normal mouse IgG; 5-aza, 5-aza-2′-deoxycytidine. The uncropped blots are shown in Supplementary File S1. | PMC10136634 | cancers-15-02282-g003.jpg |
0.429388 | 147ea7106f5c4c678670d004e2dedce6 | Kaiso depletion attenuates the growth of TNBC cells. (A) Kaiso-depleted MDA-MB-231 xenograft tumors (sh-Kaiso) showed delayed tumor onset (~4 weeks) and development compared to control MDA-MB-231 (sh-Scr) xenograft tumors, as demonstrated by time-course analysis of tumor volumes in nude mice. The statistical method used was the F test to compare variances between sh-Scr and sh-Kaiso groups (** statistically significant p < 0.01) (B) sh-Kaiso cells also developed smaller tumor sizes and reduced tumor weights as compared to sh-Scr cells. The statistical method used was the two-tailed paired t test. (C) IHC-stained images of xenograft tissues with Kaiso, CD47, and SIRPA antibodies showed a marked decrease in intensity but an increase in THBS1 in Kaiso-depleted (sh-Kaiso) tumor tissues. (D,E) Hematoxylin and eosin (H&E) staining showed significantly increased phagocytosis (green arrow showed phagocytosis) in sh-Kaiso xenograft tissues as compared to sh-Scr xenograft tissues. The statistical method used was the two-tailed paired t test. (F) Immunofluorescence images of xenograft tissues showed that sh-Kaiso tissues have a high intensity of CD86 and a low intensity of CD206, an M1 macrophage marker, whereas Kaiso control sh-Scr tissues had a low intensity of CD86 and a high intensity of CD206, an M2 macrophage marker. | PMC10136634 | cancers-15-02282-g004.jpg |
0.417408 | ead640d3e9a848979913cf1b11cbf7b2 | Exosomes act as cell-to-cell communication vehicles influencing MCF7 cells following treatment with exosomes. (A) Internalization of exosomes from MDA-MB-231 cells was confirmed by the uptake of exosomes in recipient MCF7 cells by using PKH67 polylinker dye (white arrows highlight exosome in Z-stack image). (B) MCF7 cells treated with Kaiso-depleted exosomes showed low expression of Kaiso, CD47, and SIRPA, but high expression of THBS1. The statistical method used was one-way ANOVA. (C) Polarization of THP1 cells using exosomes from Kaiso-depleted cells was assessed to demonstrate the influence of exosomes as communication vehicles by observing the expression of M1 and M2 macrophage markers. (D) Consistent with sh-Kaiso xenograft tissues (Figure 4F), THP1 cells treated with exosomes from sh-Kaiso cells showed a high expression of CD86 and a low expression of CD206, a marker for M1 macrophages; in contrast, THP1 cells treated with exosomes from sh-Scr cells showed a low expression of CD86 and a high expression of CD206, a marker for M2 macrophages. The statistical method used was the two-tailed paired t test. (E,F) BMDM treated with sh-SCR and sh-Kaiso cells showed higher phagocytosis (white arrow indicates phagocytosis) of sh-kaiso cells as compared to sh-SCR cells. The statistical method used was the two-tailed paired t test. | PMC10136634 | cancers-15-02282-g005.jpg |
0.459887 | e04e54141f574487b351ab8d98557d47 | TCGA data validate the increased expression of Kaiso and CD47, with decreased expression of THBS1 correlating with TNBC breast cancer patients and linked with AA race. (A) High expression of Kaiso, CD47, SIRPA, and low expression of THBS1 was correlated with Basal-like BRCA and ER-negative patients. (B) Kaiso, CD47, and SIRPA expressed highly in Basal like patients as compared to non-basal patients, whereas THBS1 expression was deceased in Basal like patients as compared to non-basal patients. (C) The higher level of protein for Kaiso, CD47, and SIRPA and lower level of THBS1 observed in BRCA TNBC samples as compared to other subtypes collected from the PANCAN RPPA dataset. (D) The higher level of protein for Kaiso, CD47, and SIRPA in AA patient samples as compared to other races. (E) TCGA survival analysis identified that a high level of combined Kaiso, CD47, and SIRPA with a low level of THBS1 (Red line) indicate even poorer patient survival in AA BRCA patients compared to a low level of combined Kaiso, CD47, and SIRPA with a high level of THBS1 (Dark blue line). | PMC10136634 | cancers-15-02282-g006.jpg |
0.470192 | 19039aecaa94474f931e96240e61153d | Summary. | PMC10136634 | cancers-15-02282-g007.jpg |
0.452579 | d35fada55a1040df87875e2be637ac8e | Personalised marker model (rubber “crown” set up). FH: frontal head marker; CH: central head marker; PH: posterior head marker; RAH and LAH: right and left anterior head markers; RPH and LPH: right and left posterior head markers; RAc and LAc: right and left acromion; SJN: sternum jugular notch. Two bullet-like laser pointers, projecting a red light beam, are fixed on a pair of glasses tightened posteriorly. The participant wears a sleeping mask to prevent visual cues. The subject’s gaze points downwards in the bottom panel (horizontal view) and rightwards in the right panel (sagittal view). The subject’s spatial orientation can also be inferred by looking at the corresponding marker labels. | PMC10136693 | brainsci-13-00604-g001.jpg |
0.412394 | 00058d4f85a547d2b54b91dc1654f395 | Target reference points in the panel reference frame. NR and NL: positions of the right and left lasers’ projections, respectively, with the head in the neutral position (NHP). Target reference points for the left laser pointer at 25° for neck extension (EL) and flexion (FL) and at 30° (RL) for left rotation. R’R represents the right laser pointer when rotating to the left side. An analogous procedure was followed for right rotation (not shown). | PMC10136693 | brainsci-13-00604-g002.jpg |
0.431382 | 7fca135e6f3247eb877ec7f4a6f0046d | Panel (a) shows the vectors chosen to assess the head’s positions in the three classic anatomical orthogonal planes: RAH;LAH→ allows evaluation of the rotation movements in the horizontal plane, PH;FH→ for flexion-extension movements in the sagittal plane, and SJN;CH→ for side-bending movements in the frontal plane. Panel (b) provides a graphical visualisation of the planar JPEs calculated with respect to each plane: TP and RP refer to the vector “fixed” in its coordinates at the Target Position (TP; the one set by the operator during the assisted movement) and at the Reached Position (RP; the one attained during the actively performed movement), respectively. In this representation, examples of movements are shown separately in the frontal, sagittal, and horizontal views. Subject’s spatial orientation as in Figure 1. | PMC10136693 | brainsci-13-00604-g003.jpg |
0.447193 | 6186464b4a47443daa374e7784c799fa | Representative synchronous tracings of the time course of the angles between RAH;LAH→, PH;FH→, and SJN;CH→ versors and the Neutral Head Position during four consecutive trials (i.e., flexion, followed by right rotation, extension, and left rotation). From top to bottom, horizontal RAH;LAH→ (referring to right and left neck rotations), vertical PH;FH→ (referring to neck flexion and extension), and horizontal SJN;CH→ (referring to neck right and left side-bending) coordinates are shown. On the ordinate, coordinates are expressed in angular degrees (°). On the abscissa, time is reported (in seconds). The vertical lines indicate time events manually identified during the analysis for a right rotation movement. The grey-shaded area highlights the intended component (horizontal coordinate) during a right rotation trial. The pink-shaded areas highlight the synchronous unintended components of flexion-extension and side-bending in the second and third panels from the top, respectively. For each trial, two repetitions were performed in the same direction (an operator-assisted repetition, followed by an autonomous repetition). For each repetition, a plateau in the tracings was manually identified. The TP or the RP corresponded to the mean, computed over two seconds, of the versor trace in the mid of the plateau (vertical segments). If more plateaus were present, the furthest plateau from the ideal target (for TP) or from the TP (for RP) was considered. | PMC10136693 | brainsci-13-00604-g004.jpg |
0.432906 | d60358bc85f1414e8c68ae81572cd191 | The figure illustrates the target reference points (0,0 coordinates), the Target Positions (TPs) and Reached Positions (RPs) in a representative sequence of 32 repetitions (16 trials) performed by a participant–operator couple. Axes give angular errors in degrees. TP is the head’s final position when the participant’s head was moved by the operator; RP is the position reached autonomously by the participant. Each small dot corresponds to the TP (blue) or the RP (red) of a single repetition. Big dots with a bold border represent the average of the four repetitions. In a trial, the operator first rotated the participant’s head from the neutral head position to the target reference point (30° for left or right rotation, 25° for flexion or extension). If the operator was errorless, TP coincided with the target reference point (0,0 coordinates). Then, after the operator-assisted repetition, the participant autonomously turned their head from the neutral head position to TP. If the participant was errorless, RP coincided with TP. Thus, if both the operator and the participant were errorless, RP and TP coincided with the target reference point. To stress, the operator had to be accurate and precise with respect to the target reference point, while the participant had to be accurate and precise with respect to TP. For each trial, OPE was calculated as the difference in degrees between the coordinates of the TP and 0,0. Participants completed (in quasi-random sequence) neck extensions (upper graph), left-right rotations (middle graphs), and neck flexions (lower graph). These intended directions are indicated in red shaded background. Squared graphs: TPs and RPs in the sagittal (y) and horizontal (x) planes, in degrees (°). Dotted circumferences in the square graphs encase a 5° radius centred on the target reference point. Rectangular graphs: (unintended) side-bending rotations in the frontal plane, in degrees (°). CW: clockwise from the participant’s (and the operator’s) perspective; CCW: counterclockwise. Horizontal dashed segments in the rectangular graphs mark 5° from the target reference point. It is worth stressing that JPE was the difference between RP and TP from the same trial. Take, for instance, the extension task (upper square panel). The average of the operator’s errors (big blue dots, bold border) was about 4° towards the left in rotation, 1° in extension, and 2° in CW (e.g., towards the participant’s right) side bending (top rectangular panel). Regarding the participant’s autonomous repetitions, the big red dot (average value marked with bold borders) indicates the positions reached by the participant with respect to the 0,0 coordinates, i.e., the positions “seen” by the optoelectronic system. However, the error is computed with respect to the TPs (i.e., the operator-assisted repetitions). For instance, in the top square graph, the average position shown by the participant is very close to the 0,0 coordinates, but it is rather far from the position requested by the operator. There, an error of about 3° was found. | PMC10136693 | brainsci-13-00604-g005.jpg |
0.425126 | 326537e822b148809aec46b6b583f7e9 | Bland–Altman plot (N = 26) of JPEint-component, JPEsagittal, JPEhorizontal, and JPEfrontal with respect to the two operators. From top to bottom, the first row refers to JPEint-component, the second row refers to JPEsagittal and JPEhorizontal, and the third row refers to JPEfrontal. In the uppermost row, each panel refers to one of the four directions: (A) right rotation; (B) left rotation; (C) extension; (D) flexion. Below (A,B), the corresponding unintended components in the sagittal and frontal planes ((E,F); (I,J), respectively) are considered. Below (C,D), the corresponding unintended components in the horizontal and frontal planes ((G,H); (K,L), respectively) are considered. Abscissa axes report between-operators average (°), and the ordinate axes report between-operators difference (°). The continuous line refers to the mean of the differences; the dashed lines represent 95% limits of agreement. | PMC10136693 | brainsci-13-00604-g006.jpg |
0.402756 | 30ba65211a444450aa4cb10978cd3507 | JPEint-component bar plot for the four movement directions. Hypermetric (white bars) and hypometric (grey bars) JPEint-component (mean and standard deviation) are represented. The corresponding number of hypermetric vs. hypometric trials is shown inside each bar. | PMC10136693 | brainsci-13-00604-g007.jpg |
0.459104 | 28ce28b5641c40c8a8284b5980f45b29 | Sphingolipid profiles of normal adjacent uninvolved tissues and tumors of male patients diagnosed with LUAD, COAD, HCC, and HNSCC and of female patients with EEC. The indicated chain-length sphingolipids were quantified by LC-ESI-MS/MS in normal adjacent uninvolved tissues (unin.) and tumors of self-identified AA and NHW subjects (data combined in plots) with primary histopathologic confirmed diagnoses of lung adenocarcinoma (LUAD; panels (A–D,U)), endometrial endometroid carcinoma (EEC; panels (E–H,V)), colorectal adenocarcinoma (COAD; panels (I–L,W)), hepatocellular adenocarcinoma (HCC; panels (M–P,X)), and head and neck squamous cell carcinoma (HNSCC; panels (Q–T,Y)). Lipid levels are shown as the amount of picomoles of indicated chain length and lipid species per mg of tissue. For LUAD, unin. n = 34, tumor n = 40; EEC, n = 22; COAD, n = 54; HCC, n = 21; HNSCC, unin. n = 24, tumor n = 23. Graphs are box plots showing medians (black line) and whiskers of min to max. Uncorrected p-values for associations considered significant (α ≤ 0.05) are shown, with values of the predicted mean difference (ANOVA) between unin. and tumor tissue lipid levels shown in parenthesis. The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the false discovery rate (FDR; Q = 0.05) and the two-step controlling procedure of Benjamini, Krieger, and Yekutieli (BKY), see Supplementary Tables S1 (LUAD), S2 (EEC), S3 (COAD), S4 (HCC), and S5 (HNSCC). For panels (U–Y), the y-axis is in log2 scale. | PMC10136787 | cancers-15-02238-g001.jpg |
0.474709 | 141e8cbe789147b7a1dd61c87913a07b | Sphingolipid profiles of normal adjacent uninvolved tissues and tumors of self-identified AA males diagnosed with LUAD, COAD, HCC, and HNSCC and of self-identified AA females with EEC. The indicated chain-length sphingolipids were quantified by LC-ESI-MS/MS in normal adjacent uninvolved tissues (unin.) and tumors of self-identified AA subjects with primary histopathologic confirmed diagnoses of lung adenocarcinoma (LUAD; panels (A–D,U)), endometrial endometroid carcinoma (EEC; panels (E–H,V), colorectal adenocarcinoma (COAD; panels (I–L,W)), hepatocellular adenocarcinoma (HCC; panels (M–P,X)), and head and neck squamous cell carcinoma (HNSCC; panels (Q–T,Y)). Lipid levels are shown as the amount of picomoles of indicated chain length and lipid species per mg of tissue. For LUAD, unin. n = 12, tumor n = 14; EEC, n = 10; COAD, n = 30; HCC, n = 10; HNSCC, unin. n = 12, tumor n = 11. Graphs are box plots showing medians (black line) and whiskers of min to max. Uncorrected p-values for associations considered significant (α ≤ 0.05) are shown, with values of the predicted mean difference (ANOVA) between unin. and tumor tissue lipid levels shown in parenthesis. The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Tables S6 (LUAD), S7 (EEC), S8 (COAD), S9 (HCC), and S10 (HNSCC). For panels (U–Y), the y-axis is in log2 scale. | PMC10136787 | cancers-15-02238-g002.jpg |
0.464454 | 8587736b74f34703b35f187a1bbef55b | Sphingolipid profiles of normal adjacent uninvolved tissues and tumors of self-identified NHW males diagnosed with LUAD, COAD, HCC, and HNSCC and of self-identified NHW females with EEC. The indicated chain-length sphingolipids were quantified by LC-ESI-MS/MS in normal adjacent uninvolved tissues (unin.) and tumors of self-identified NHW subjects with primary histopathologic confirmed diagnoses of lung adenocarcinoma (LUAD; panels (A–D,U)), endometrial endometroid carcinoma (EEC; panels (E–H,V)), colorectal adenocarcinoma (COAD; panels (I–L,W)), hepatocellular adenocarcinoma (HCC; panels (M–P,X)), and head and neck squamous cell carcinoma (HNSCC; panels (Q–T,Y)). Lipid levels are shown as the amount of picomoles of indicated chain length and lipid species per mg of tissue. For LUAD, unin. n = 22, tumor n = 26; EEC, n = 12; COAD, n = 24; HCC, n = 11; HNSCC, n = 12. Graphs are box plots showing medians (black line) and whiskers of min to max. Uncorrected p-values for associations considered significant (α ≤ 0.05) are shown, with values of the predicted mean difference (ANOVA) between unin. and tumor tissue lipid levels shown in parenthesis. The lower limit of p- and q-value calculations was set to 1.0 E-15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Tables S11 (LUAD), S12 (EEC), S13 (COAD), S14 (HCC), and S15 (HNSCC). For panels (U–Y), the y-axis is in log2 scale. Alterations considered significant (α ≤ 0.05) are in bold text. | PMC10136787 | cancers-15-02238-g003.jpg |
0.447528 | c38aa72cf76d463f83c3997454beb35f | Secondary analysis comparisons of unin. vs. unin. and tumor vs. tumor sphingolipid profiles of self-identified AA and NHW males with LUAD. Data presented in Figure 2A–D,U and Figure 3A–D,U were analyzed to examine differences in the indicated lipids between unin. and tumor tissues of AA and NHW with LUAD. In each panel (A–E), the upper graphs are box plots showing medians (black line) and whiskers of min to max (top), and the bottom graphs are plots of the 95% family-wise significance and confidence intervals for predicted means difference calculated following ANOVA. Corresponding unadjusted p-values (Fisher’s LSD; Prism) for the indicated comparisons are shown to the right of the 95% confidence interval plots. The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Table S16. For panel (E), the y-axis is in log2 scale. Alterations considered significant (α ≤ 0.05) are in bold text. | PMC10136787 | cancers-15-02238-g004.jpg |
0.45478 | 322aa621d07145469f651e3321594918 | Secondary analysis comparisons of unin. vs. unin. and tumor vs. tumor sphingolipid profiles of self-identified AA and NHW females with EEC. Data presented in Figure 2E–H,V and Figure 3E–H,V were analyzed to examine differences in the indicated lipids between unin. and tumor tissues of self-identified AA and NHW females with EEC. In each panel (A–E), the upper graphs are box plots showing medians (black line) and whiskers of min to max (top), and the bottom graphs are plots of the 95% family-wise significance and confidence intervals for predicted means difference calculated following ANOVA. Corresponding unadjusted p-values (Fisher’s LSD; Prism) for the indicated comparisons are shown to the right of the 95% confidence interval plots. The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Table S17. For panel (E), the y-axis is in log2 scale. Alterations considered significant (α ≤ 0.05) are in bold text. | PMC10136787 | cancers-15-02238-g005.jpg |
0.418938 | 066d714045a44624b6ed633881876b06 | Secondary analysis comparisons of unin. vs. unin. and tumor vs. tumor sphingolipid profiles of self-identified AA and NHW males with COAD. Data presented in Figure 2I–L,W and Figure 3I–L,W were analyzed to examine differences in the indicated lipids between unin. and tumor tissues of self-identified AA and NHW males with COAD. In each panel (A–E), the upper graphs are box plots showing medians (black line) and whiskers of min to max (top), and the bottom graphs are plots of the 95% family-wise significance and confidence intervals for predicted means difference calculated following ANOVA. Corresponding unadjusted p-values (Fisher’s LSD; Prism) for the indicated comparisons are shown to the right of the 95% confidence interval plots. The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Table S18. For panel (E), the y-axis is in log2 scale. Alterations considered significant (α ≤ 0.05) are in bold text. | PMC10136787 | cancers-15-02238-g006.jpg |
0.428667 | f943ac0872cf4224a2629d2830787cc3 | Secondary analysis comparisons of unin. vs. unin. and tumor vs. tumor sphingolipid profiles of self-identified AA and NHW males with HCC. Data presented in Figure 2M–P,X and Figure 3M–P,X were analyzed to examine differences in the indicated lipids between unin. and tumor tissues of self-identified AA and NHW males with HCC. In each panel (A–E), the upper graphs are box plots showing medians (black line) and whiskers of min to max (top), and the bottom graphs are plots of the 95% family-wise significance and confidence intervals for predicted means difference (means diff.) calculated following ANOVA. Corresponding unadjusted p-values (Fisher’s LSD; Prism) for the indicated comparisons are shown to the right of the 95% confidence interval plots. The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Table S19. For panel (E), the y-axis is in log2 scale. Alterations considered significant (α ≤ 0.05) are in bold text. | PMC10136787 | cancers-15-02238-g007.jpg |
0.42428 | 3c2b948e51154bacbf290345cd6c2c7c | Secondary analysis comparisons of unin. vs. unin. and tumor vs. tumor sphingolipid profiles of self-identified AA and NHW males with HNSCC. Data presented in Figure 2Q–T,Y and Figure 3Q–T,Y were analyzed to examine differences in the indicated lipids between unin. and tumor tissues of self-identified AA and NHW males with HNSCC. In each panel (A–E), the upper graphs are box plots showing medians (black line) and whiskers of min to max (top), and the bottom graphs are plots of the 95% family-wise significance and confidence intervals for predicted means difference calculated following ANOVA. Corresponding unadjusted p-values (Fisher’s LSD; Prism) for the indicated comparisons are shown to the right of the 95% confidence interval plots. The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Table S20. For panel (E), the y-axis is in log2 scale. Alterations considered significant (α ≤ 0.05) are in bold text. | PMC10136787 | cancers-15-02238-g008.jpg |
0.436992 | 8f68b91b394843dab383590173f1c7af | Race-independent pan-cancer analysis of alterations in tumors of subjects with LUAD, COAD, HCC, EEC, and HNSCC. Data from AA and NHW presented in Figure 2 and Figure 3 were pooled by sphingolipid class and acyl chain length and analyzed to examine pan-cancer alterations in human cancers. In each panel (A–E), the upper graphs are box plots showing medians (black line) and whiskers of min to max (top), and the bottom graphs are plots of the 95% family-wise significance and confidence intervals for predicted means difference calculated following ANOVA. The mean fold-change between unin. tissue and tumor was calculated by dividing the mean lipid level in tumors by the mean lipid level in unin. tissues and shown between parenthesis next to the corresponding unadjusted p-values (Fisher’s LSD; Prism). The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Table S21. For panel (E), the y-axis is in log2 scale. Alterations considered significant (α ≤ 0.05) are in bold text. | PMC10136787 | cancers-15-02238-g009.jpg |
0.424515 | 06419673bde14fb5a42699c4017b3c18 | Race-dependent pan-cancer analysis of differences in the unin. and tumor tissues of AA and NHW subjects with LUAD, COAD, HCC, EEC, and HNSCC. Data from AA and NHW presented in Figure 2 and Figure 3 were pooled by race, sphingolipid class, and acyl chain length and analyzed to examine differences between the unin. and tumor tissues of AA and NHW with pan-cancer. In each panel (A–E), the upper graphs are box plots showing medians (black line) and whiskers of min to max (top), and the bottom graphs are plots of the 95% family-wise significance and confidence intervals for predicted means difference (means diff.) calculated following ANOVA. The mean fold-change between unin. tissue and tumor was calculated by dividing the calculated mean lipid level in tumors by the mean lipid level in unin. tissues and shown between parenthesis next to the corresponding unadjusted p-values (Fisher’s LSD; Prism). The lower limit of p- and q-value calculations was set to 1.0 × 10−15 (Prism), so no values are reported lower than this limit. For p-adjusted (q) values corrected for multiple comparisons using the FDR (Q = 0.05) and the two-step controlling procedure of BKY, see Supplementary Table S22. For panel (E), the y-axis is in log2 scale. Alterations considered significant (α ≤ 0.05) are in bold text. | PMC10136787 | cancers-15-02238-g010.jpg |
0.457644 | 2871f8963dfe41e6b6fa8e0350f60529 | PRISMA flow diagram. | PMC10137018 | curroncol-30-00331-g001.jpg |
0.393376 | 72bda625a13a40ff8966c6b98c30a443 | Comparison of the quality of life in the subscales “psychosocial”, “sexuality” and “satisfaction-upper arms” of the two patient groups weight loss by conservative measures vs. weight loss by surgical measures. The box plots represent the median, the interquartile range and the distribution. Statistical differences were examined using the Wilcoxon test. The significance level is * p < 0. | PMC10138039 | healthcare-11-01147-g001.jpg |
0.550127 | b8c6735fdc434f4e8859ce4d20dae1d0 | Regression analysis and Pearson’s correlation of the patients’ BMI and selected headings of the BODY-Q questionnaire: body image, sexuality, society, satisfaction-abdomen (Z Abdomen), satisfaction-body (ZK), satisfaction-upper arms (ZOA), satisfaction-back (ZR), satisfaction-buttocks (Z Buttock), satisfaction-hips and outer thighs (ZHOA), satisfaction-inner thighs (ZOI), assessment of excess skin (Skin). | PMC10138039 | healthcare-11-01147-g002.jpg |
0.467855 | ef1379bc5bb64773bb56f84fc149a405 | Representation of satisfaction-back/-body/-hip and outer thigh/-inner thigh categorized according to the amounts of weight lost. The boxplots show the median with the corresponding interquartile range and the distribution of the group. The statistical differences were calculated using the Kruskal–Wallis test and the subsequent post-hoc analysis was performed using the pairwise Wilcoxon test; significance level: * p < 0.1; ** p < 0.05, *** p < 0.01. | PMC10138039 | healthcare-11-01147-g003.jpg |
0.418446 | 4da688b49089412eb40b810a6357912e | Length and body area in relation to age for larvae of European eel, Anguilla anguilla, fed three experimental diets 1, 2 and 3.Effect of age for each diet on standard length (A-C) and body area (E-G) and effect of diets at each age for standard length (D) and body area (H). Assessment occurred at specific developmental points such as hatch (0 days post hatch (dph)), before first-feeding (9 dph), during first-feeding (15 dph), end of the first-feeding period (22 dph) and beyond the first-feeding period (28 dph). Values represent means (± SEM), while different lower-case letters represent significant differences (p < 0.05). | PMC10138473 | pone.0283680.g001.jpg |
0.415296 | b1ed894deaae4b0d804ee555cc954aa2 | Effect of age for each diet (A, B, C) and effect of diets at each age (D) on European eel, Anguilla anguilla, larval survival.Values represent means (± SEM), while different lower-case letters represent significant differences (p < 0.05). | PMC10138473 | pone.0283680.g002.jpg |
0.443783 | 0f7a01ebffaf4be9a569ea870bcaef80 | Effect of age and treatment (diet) on larval European eel, Anguilla anguilla, feeding incidence (%) and gut fullness (%).Values represent means (± SEM), while different lower-case letters represent significant differences (p < 0.05). | PMC10138473 | pone.0283680.g003.jpg |
0.434681 | 9fe60176f71846c8adfd45bd4fbb1fc0 | European eel, Anguilla anguilla, dry weight (mg/ind) during larval development.Effect of age at each diet (A-C) and effect of diets at each age (D). Values represent means (± SEM), while different lower-case letters represent significant differences (p < 0.05). | PMC10138473 | pone.0283680.g004.jpg |
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