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0.451395 | c84c12d40d9a4e1eaf555ed96e0e3537 | Research application: Finite Elements Analysis. Stress distribution (in MPa) induced in an 3D model of a NiTi instrument created using a high-resolution optical scanner by a torque applied at its tip: (a) Polygonal 3D mesh of the surface model; (b) Simulated torsion test at 2 different levels of the model. | PMC10222178 | materials-16-03636-g006.jpg |
0.379775 | 7569231f79b348159c0d4fb37ce7c0a4 | 3D models for commercial or teaching purposes. 3D virtual models of 5 NiTi instruments created using the 3D surface scanning method and artificially texturized with a metal shader to simulate real instruments. | PMC10222178 | materials-16-03636-g007.jpg |
0.482021 | 46eb41e5514f4d0dba4fdd9680d13888 | Biometrical parameters of rapeseed: (a) Dry biomass, (b) Fresh biomass, (c) Shoot and root length, and (d) Cd content in the shoot and root of plants at harvest. Capital and small letters represent significant differences between the treatments at p < 0.05. Data are presented as mean ± SD (n = 4). C: control; BC: biochar; BMC5: biochar + Serratia sp. FV34b; BMC9: biochar + Pseudomonas sp. ASe42b. Nd/(nd): not detected. | PMC10222574 | plants-12-01973-g001.jpg |
0.469544 | 2c3c7e13c76d4f91bef68c959f30f1dc | Photosynthetic pigment content: (a) chlorophyll a (Chl a), (b) chlorophyll b (Chl b), (c) carotenoids (Car), and (d) ratio Chl (a + b)/Car in the leaves of rapeseed before drought (BD) and after drought (AD). Capital and small letters represent significant differences (p < 0.05) between the treatments BD and AD, respectively. Data are presented as mean ± SD (n = 6). C: control; BC: biochar; BMC5: biochar + Serratia sp. FV34b; BMC9: biochar + Pseudomonas sp. ASe42b. | PMC10222574 | plants-12-01973-g002.jpg |
0.423134 | 5fdbc8829c1144819875647d73d11f89 | The content of: (a) malondialdehyde (MDA), and (b) proline in leaves of rapeseed before drought (BD) and after drought (AD). Capital and small letters represent significant differences between the treatments (p < 0.05) BD and AD, respectively. Data are presented as mean ± SD (n = 6). C: control; BC: biochar; BMC5: biochar + Serratia sp. FV34b; BMC9: biochar + Pseudomonas sp. ASe42b. | PMC10222574 | plants-12-01973-g003.jpg |
0.476457 | ff827bfbc2c0428f8596c97f6bac8cd0 | (a) Soil relative moisture content (RMC) and (b) Leaf relative water content (RWC) in B. napus before drought (BD) and after drought (AD). Capital and small letters represent significant differences between the treatments (p < 0.05) BD and AD, respectively. Data are presented as mean ± SD (n = 4). C—control; BC—biochar; BMC5—biochar + Serratia sp. FV34b; BMC9—biochar + Pseudomonas sp. ASe42b. | PMC10222574 | plants-12-01973-g004.jpg |
0.408123 | a87c45a752924153ac5fcd90764c501f | The gestational period is presented in three studied groups, using raincloud plots (in this type of graphical representation, we can see a complete data distribution, by density and by box plots). In group 1, the GP was significantly higher (p = 0.032 < 0.05, p value obtained from Kruskal–Wallis test; groups 1 and 2 contain 51 patients each, group 3 contains 76 patients). | PMC10223159 | medicina-59-00851-g001.jpg |
0.46307 | 7a04932abda24720825041afd201e20b | The newborn weight is presented in three studied groups, using raincloud plots; there were no statistically significant differences between the studied groups (p > 0.05, p value obtained from Kruskal–Wallis test; groups 1 and 2 contain 51 patients each, group 3 contains 76 patients). | PMC10223159 | medicina-59-00851-g002.jpg |
0.439745 | e1268e17c719470f8302a1e764f278bc | The differences between the number of pregnancies and miscarriages in all studied groups, using raincloud plots. A significant decrease was observed (p < 0.001, p value obtained from Kruskal–Wallis test; groups 1 and 2 contain 51 patients each, group 3 contains 76 patients). | PMC10223159 | medicina-59-00851-g003.jpg |
0.546246 | 93d91f7650bb481aaa9ce8168f142d05 | The miscarriage risk, compared between our groups. A significant decrease can be observed within the studied groups, and the lowest rate was reported in group 3 (p < 0.001, p value obtained from Kruskal–Wallis’s test; groups 1 and 2 contain 51 patients each, group 3 contains 76 patients). | PMC10223159 | medicina-59-00851-g004.jpg |
0.489708 | cb810af39c2440a1843bef76ee4a65dc | The D-dimers evolution during pregnancy, based on the type of thrombophilia (groups 1, 2, and 3—p < 0.001, p value obtained from the Friedman test). | PMC10223159 | medicina-59-00851-g005.jpg |
0.371028 | 5a34e6bc17d14d5b8fe127236630e0e4 | Taxonomic composition and diversity of fecal bacterial communities for each patient stratified for responder and non-responder group. The most represented phyla (a), classes (b), and orders (c) identified in the study groups are shown with relative abundance. Only taxa whose relative abundance was >1% in at least one group were included. | PMC10223513 | microorganisms-11-01305-g001.jpg |
0.470033 | 31ee597ef6eb4b39a028f3ebc4c533e4 | Alpha-diversity. Observed richness and Shannon indices are presented at the taxonomic level of phylum (a), class (b), and order (c). Significant (p < 0.05) comparisons between responder (R) and non-responder (NR) patients are indicated in the boxplot. | PMC10223513 | microorganisms-11-01305-g002.jpg |
0.440933 | 75d07a378bd9437092a0310ef8f74336 | Beta-diversity. The microbiota distances were evaluated through the Bray-Curtis dissimilarity matrix at the taxonomic level of phylum (a), class (b), and order (c) and visualized through principal coordinate analysis (PCoA). Each point represents the microbiota composition of one sample stratified for outcome (responder and non-responder). | PMC10223513 | microorganisms-11-01305-g003.jpg |
0.38801 | e9f933a6db2b45b8a821165b501b39c7 | Taxonomic composition and diversity of fecal bacterial communities for each patient who experienced an irAE (AE) or did not (NAE). The most represented phyla (a), classes (b), and orders (c) identified in the study groups are shown with relative abundance. Only taxa whose relative abundance was >1% in at least one group were included. | PMC10223513 | microorganisms-11-01305-g004.jpg |
0.456418 | 6ff5a773fdb9459b9836524be339fbd9 | α-diversity according to the experience of an irAE (AE) or not (NAE). Observed richness and Shannon indices are presented at the taxonomic level of phylum (a), class (b), order (c). Significant (p < 0.05) comparisons between AE and NAE are indicated in the boxplot. | PMC10223513 | microorganisms-11-01305-g005.jpg |
0.444718 | f7626311cd744155bc9dec76b01df7ad | Beta-diversity according to the experience of an irAE (AE) or not (NAE). The microbiota distances were evaluated through the Bray-Curtis dissimilarity matrix at the taxonomic level of phylum (a), class (b), and order (c) and visualized through principal coordinate analysis (PCoA). Each point represents the microbiota composition of one sample. | PMC10223513 | microorganisms-11-01305-g006.jpg |
0.435221 | b5144210d01e4b349d437f5375166ebe | Study participants flow | PMC10223897 | 40360_2023_673_Fig1_HTML.jpg |
0.550062 | f3e3bb50291f4630815127bde1ebcae0 | Mean (SD) serum concentration-time profiles | PMC10223897 | 40360_2023_673_Fig2_HTML.jpg |
0.478039 | 475f737fa0c649b6ac23447b6f559d92 | Schematic diagram of six fusion proteins, denoted as OPMT, OPET, OCET, PM, PE and CE. OprI, complete sequence of bacterial lipoprotein I; p30, complete sequence of p30; p54-1 and p54-2 respectively represents (Met1-Thr29) and (Ser53-Leu184) of p54; p72-E1, p72-E2, p72-E3 and p72-E4 respectively represents (Gln364-Pro395), (Ala518-Lys552), (Tyr179-Leu210) and (Leu242-Pro273) of p72; △pE248R, pE248R (Met1-Lys198); △CD2v, CD2v (Asp17-Tyr206); △pEP153R, pEP153R (Asn49-Lys158); TT-P2, a universal CD4+ T cell epitope; thick yellow line, linker 1 “ (GGGGS)3”; thin yellow line, linker 2 “PG” | PMC10224232 | 12985_2023_2070_Fig1_HTML.jpg |
0.508715 | 9800e20705d642d1b18d7ef15b6839f2 | Identification of purified recombinant fusion proteins by SDS-PAGE and western blotting. A SDS-PAGE analysis of purified recombinant proteins. Lane M, molecular weight markers; lane 1, OPMT; lane 2, OPET; lane 3, OCET; lane 4, PM; lane 5, PE; lane 6, CE. Western blotting confirmation of purified recombinant proteins with anti-polyhistidine mAb (B) or anti-ASFV swine serum (C) as primary antibody and corresponding secondary antibodies. Lane contents are the same as in panel (A) | PMC10224232 | 12985_2023_2070_Fig2_HTML.jpg |
0.44221 | 548fbed2e3ec4752b159eedb25124ab7 | Cytokines secreted by DCs after stimulation. TNF-α (A) and IL-12p70 (B) levels in culture supernatants following stimulation of BMDCs with each recombinant protein (1 or 5 μg/mL), LPS (0.1 µg/mL) or medium (control) for 24 h. All data are displayed as mean ± SD (n = 3); NS = P > 0.05; *P < 0.05, **P < 0.01, ***P < 0.001 | PMC10224232 | 12985_2023_2070_Fig3_HTML.jpg |
0.456295 | 28b0a5b9487248c0b9c709d87fc962d8 | Antigen-specific IgG detection. IgG responses to p30 (A), p54 (B), p72 (C), pE248R (D), CD2v (E) and pEP153R (F) in the sera from each immunized pig at 0, 14, 21, 35 and 42 dpv were detected by indirect ELISAs, with serum dilutions of 1:100 and goat anti-pig IgG-HRP dilutions of 1:10,000. The results are expressed as OD450 (mean ± SD). NS = P > 0.05; *P < 0.05; **P < 0.01; ***P < 0.001 | PMC10224232 | 12985_2023_2070_Fig4_HTML.jpg |
0.523034 | 46a2da4010ee430aae53c47d807ba071 | Lymphocyte proliferation in PBMCs from immunized pigs after in vitro stimulation with inactivated ASFV. A The percentage of CFSE-low lymphocytes (represented by P2) detected by flow cytometry in PBMCs from immunized pigs at 42 dpv after staining with CFSE and incubation with inactivated ASFV, medium (negative control) or concanavalin A (positive control). Group 1 and group 2 respectively represent pigs immunized with O-Ags-T formulation or Ags formulation. B Calculated percentages of proliferative lymphocytes based on CFSE-low lymphocytes in PBMCs from three separate experiments. The graphs show mean results with error bars indicating the SD; **P < 0.01; ***P < 0.001 | PMC10224232 | 12985_2023_2070_Fig5_HTML.jpg |
0.444871 | 44beb78842844c3f8a38ab6f54d2e0a5 | IFN-γ-producing T cells in PBMCs from immunized pigs at 42 dpv. The percentage of IFN-γ-secreting CD4+ T cells (A) and IFN-γ-secreting CD8+ T cells (B) in PBMCs from immunized pigs at 42 dpv after in vitro stimulation with inactivated ASFV, medium (negative control) or a cell activation cocktail (positive control). The graphs show mean results with error bars indicating the SD. NS = P > 0.05; *P < 0.05; **P < 0.01; ***P < 0.001 | PMC10224232 | 12985_2023_2070_Fig6_HTML.jpg |
0.432628 | 2399b6c0c82f40f6938c6a47b77f85f1 | Neutralization of ASFV infection by the sera from immunized pigs at 42 dpv. A The ASFV genome copy number in PAMs infected by ASFV (MOI = 0.01) preincubated with heat-inactivated pre-immune sera, immune sera (both at 1:5 dilution) or equal volume of medium (negative control), respectively. B The percentage of ASFV neutralization by the sera from pigs immunized with O-Ags-T formulation or Ags formulation at 42 dpv. The mean results with standard error are shown. NS = P > 0.05; ***P < 0.001 | PMC10224232 | 12985_2023_2070_Fig7_HTML.jpg |
0.410722 | a0cd5742579841109e12de5c129e25da | Indirect immunofluorescence identification of PAMs infected with ASFV. PAMs infected with ASFV (MOI = 0.01) preincubated with heat-inactivated immune sera (42 dpv) from group 1 (O-Ags-T formulation), group 2 (Ags formulation) and PBS group or medium (negative control) were subjected to indirect immunofluorescence assay, with anti-p30 mAb as primary antibody and goat anti-mouse IgG-TRITC as secondary antibody. DAPI indicates the staining of the nucleus. The lower panel represents the merge of the 2 channels above | PMC10224232 | 12985_2023_2070_Fig8_HTML.jpg |
0.471817 | 1d768b02a1d84586a59b1754fe8be826 | Inhibition of ASFV infection in PBMCs from immunized pigs at 42 dpv. A Copy number of ASFV genome in PBMCs from non-immunized pigs or immunized pigs at 42 dpv infected with ASFV (MOI = 0.01). B ASFV inhibition percentages in PBMCs from pigs immunized with O-Ags-T formulation or Ags formulation at 42 dpv. The mean results with standard error are shown. NS = P > 0.05; ***P < 0.001 | PMC10224232 | 12985_2023_2070_Fig9_HTML.jpg |
0.380489 | db2ac64b353942a3bdd6b8856aa2f01e | A formula for survival in surgery. A The components of the formula for survival in surgery. B A table with hypothetical settings of the formula for survival in surgery, from an ‘utopian’ model to what is potentially achievable | PMC10225082 | 13037_2023_362_Fig1_HTML.jpg |
0.432034 | f5eadd4cb9c1415b94b6cb682a3a645e | A formula for survival in surgery framework for improved quality and safety. The model is generic and should be tailored to fit specific needs for a given surgical condition or surgical specialism | PMC10225082 | 13037_2023_362_Fig2_HTML.jpg |
0.386505 | f59edf0ca637420fbb17c6d2e25c8306 | Association between BMI and the risk of dyslipidemia, allowing for nonlinear effects, with 95%CI. The model shows ORs compared with BMI 24 kg/m2, adjusting for age, gender, residence, hypertension, hyperuricemia, HbA1c abnormal, current cigarette smoking. BMI, body mass index; CI, confidence interval; OR, odds ratio. | PMC10225544 | fpubh-11-1188212-g001.jpg |
0.469337 | 2a5e660d909d4b3a909b41cfc0a6db14 | Phenotypes of parents. (A, B) WQ1 and WQ2 at 10 days after pollination (DAP). (C, D) WQ1 and WQ2 at 18 DAP. (E, F) Pericarp morphology of WQ1 and WQ2 at 10 DAP. (G, H) Pericarp morphology of WQ1 and WQ2 at 18 DAP. (I, J) Rind hardness (RH) and cracking tolerance capacity (CTC) of fruits at 10 and 18 DAP. **p < 0.05. | PMC10225605 | fpls-14-1166008-g001.jpg |
0.489685 | 2f06544caf70435783c1bb1670d2eefd | Phenotypic distribution of recombinant inbred lines (RILs). (A) Cracking tolerance capacity (CTC, in kilograms). (B) Depth of fruit cracking (DFC, in millimeters). (C) Rind hardness (RH in kilograms per square centimeter); (D) rind thickness (RT in millimeters). | PMC10225605 | fpls-14-1166008-g002.jpg |
0.48463 | 4816cc4f5d2a47a09ba8bc01b21981a5 | High-density genetic map. | PMC10225605 | fpls-14-1166008-g003.jpg |
0.395044 | 3978e2d14091469e96daffcf98060258 | Quantitative trait loci (QTLs) detected in the whole genome. (A) Cracking tolerance capacity (CTC). (B) Depth of fruit cracking (DFC). (C) Rind hardness (RH). (D) Rind thickness (RT). | PMC10225605 | fpls-14-1166008-g004.jpg |
0.456055 | c1526ebe91584ded8df3caa3da506e45 | Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses of the differentially expressed genes (DEGs) from the two comparison groups. (A, B) GO enrichment analysis between WQ1 and WQ2 at 10 and 18 days after pollination (DAP). (C, D) KEGG enrichment analysis between WQ1 and WQ2 10 at and 18 DAP. | PMC10225605 | fpls-14-1166008-g005.jpg |
0.46328 | 4caf827883b0432bbf5d1e482b3b4dd8 | Coexisting genes in quantitative trait locus sequencing (QTL-seq) and RNA-seq and the candidate genes identified by quantitative real-time PCR (qRT-PCR). (A) Venn diagram of the differentially expressed genes at 10 and 18 days after pollination (DAP) and the genes within the QTL intervals. (B) Relative expression of the candidate genes between the two parents. M, maternal (WQ1); P, paternal (WQ2). **p < 0.01, **p < 0.001. | PMC10225605 | fpls-14-1166008-g006.jpg |
0.488856 | 63d1387b9e3e4325b277c6d342aa46ce | Study design and flow chart. | PMC10225977 | gr1_lrg.jpg |
0.447277 | e35fc98912964815ae47c79a2ed2d609 | Survival curves of comparisons of medical outcomes between the ND group (n = 311) and the control group (n = 311) after the 1st shot of SARS-CoV-2 vaccine. (A) any OPD or ER visit, (B) emergency department visit, (C) pediatric cardiology OPD visit, (D) rheumatology and immunology OPD visit, (E) pediatric gastroenterology OPD visit, and (F) pediatric neurology OPD visit. | PMC10225977 | gr2_lrg.jpg |
0.428959 | 79b6ae74cd40457680fd5894a0eb9f97 | Sonic Hedgehog (SHh) signaling is regulated by Protein Kinase A (PKA) phosphorylation of glioma-associated oncogene (Gli) transcription factors. (A) When PKA phosphorylates Gli, Gli cannot be processed by Smo into its active state and SHh-dependent transcription does not occur. (B) Binding of Shh to Pitch1 activates phosphatidylinositol (3,4,5)-triphosphate (PIP3), increasing ciliary Ca2+ levels and preventing cAMP synthesis via Ca2+-inhibited adenylyl cyclase 5 and 6 (AC5/6), subsequently decreasing PKA phosphorylation of Gli. (C) Gli moves to the tip of the primary cilium. (D) Smoothened (Smo) is freed to activate Gli, Gli exits the cilium to initiate transcription. | PMC10226274 | fphys-14-1187134-g001.jpg |
0.416045 | a4553da722dd44d98423e75d6652e596 |
(A) Prostaglandin E2 (PGE2) is exported by the ATP-binding cassette transporter protein (ABCC4) across the plasma membrane to the extracellular space where PGE2 can bind the Gαs-coupled receptor, EP4 to promote cilia formation as well as elongation. (B) Pericentriolar material 1 (PCM1) acts as an AKAP for PKA. GPCR activation of PKA leads to phosphorylation of NEK10, a kinase required for ciliary biogenesis. Phosphorylation of NIMA-related Kinase 10 (NEK10) by PKA leads to ubiquitination and proteolysis of the kinase by E3 ligase CHIP leading to cilia retraction. | PMC10226274 | fphys-14-1187134-g002.jpg |
0.549619 | 4af4d232525a4f1faac57d6b385ac611 |
(A) MC4R is a Gαs-coupled receptor which localizes to the primary cilium of hypothalamus neurons to control food intake. Also in cilia of hypothalamus neurons, NPY2R regulates food intake, but in contrast to MC4R, it does so through decrease in cAMP, as NPY2R is Gαi-coupled. (B) Both MC4R and NPY2R, when excluded from the cilium, fail to repress food intake. Many ciliopathies as well as complete loss of primary cilia lead to obesity. | PMC10226274 | fphys-14-1187134-g003.jpg |
0.44617 | b87fc42431f74684afe6c73daff07389 | Vasopressin stimulation of the vasopressin type 2 receptor (V2R) localised to the primary cilium activates PKA-dependent phosphorylation of Aquaporin 2 (AQP2) channels and of the transcription factor cAMP-response element binding protein (CREB), to subsequently drive kidney cystogenesis. PKA, protein kinase A; AC5/6, adenylyl cyclase 5 and 6; PDE4, phosphodiesterase 4. | PMC10226274 | fphys-14-1187134-g004.jpg |
0.425955 | cf620b8cff3244779e40bc0e5e9da21c | Kidney cells are plated in a 3D culture Matrigel/collagen mix and exposed to light, activating ciliary-bPACs. Enhanced ciliary cAMP synthesis due to AC stimulation leads to activation of ciliary PKA. Ciliary PKA phosphorylates downstream targets which drive cystogenesis in in-vitro models of PKD. | PMC10226274 | fphys-14-1187134-g005.jpg |
0.434296 | 02f1c383958d4f3394c8987dcf3a9b38 | Fluoropyrimidine pharmacokinetic and pharmacodynamic pathway. CAP is transformed by CES to 5-dFCR which turns into 5-dFUR by CDA and then to its active form of 5-FU by TP. Tegafur, is metabolized in the liver by CYP2A6 to the unstable form of 5-hydroxytegafur, which spontaneously turns into 5-FU. 5-FU is catabolized by DPD to inactive metabolites in the liver; DPYS catabolizes DHFU to FUPA and UPB1 turns FUPA to FBAL which is excreted in the urine. The remaining 5-FU (approximately 1%–3% of initially administered) ends to the fluorine-substituted derivatives of uracil, FUTP and FdUTP, formed through two distinct pathways in which several enzymes are implicated. FUTP and FdUTP incorporate into RNA and DNA sequence inhibiting thus nucleic acid synthesis. FdUTP additionally inhibits the ternary complex of MTHFR substrate 5,10-MTHF with TS, which converts dUMP to dUTP and dTTP, a vital precursor for DNA replication and repair, inducing thereby cell apoptosis. ENOSF1 downregulates TS expression. 5,10-MTHF, 5,10-methylene tetrahydrofolate; 5-dFCR, 5-deoxy-5-fluorocytidine; 5-dFUR, 5-deoxy-5-fluorouridine; 5-FU, 5-fluorouracil; 5-MTHF, 5-methyltetrahydrofolate; CAP, capecitabine; CDA, cytidine deaminase; CES2, carboxylesterase 2; CYP2A6, cytochrome P450 2A6; DHFU, 5-fluoro-5,6-dihydrouracil; DPD, dihydropyrimidine dehydrogenase; DPYS, dihydropyrimidinase; dTTP, deoxythymidine triphosphate; dUMP, deoxyuridine monophosphate; dUTP, deoxyuridine triphosphate; ENOSF1, enolase superfamily member 1; FBAL, α-fluoro-β-alanine; FdUDP, fluorodeoxyuridine diphosphate; FdUMP, fluorodeoxyuridine monophosphate; FdUTP, fluorodeoxyuridine triphosphate; FUDP, fluorouridine diphosphate; FUDR, fluorodeoxyuridine; FUMP, fluorouridine monophosphate; FUPA, fluoro-β-ureidopropionate; FUR, fluorouridine; FUTP, fluorouridine triphosphate; MTHFR, methylenetetrahydrofolate reductase; NDK, nucleotide diphosphate kinase; NMK, nucleotide monophosphate kinase; OPRT, orotate phosphoribosyltransferase; RR, ribonucleotide reductase; TK, thymidine kinase; TP, thymidine phosphorylase; TS, thymidylate synthase; UK, uridine kinase; UP, uridine phosphorylase; UPB1, β-ureidopropionase 1. | PMC10226670 | fphar-14-1184523-g001.jpg |
0.437007 | a658a26140ba43969acefef244e8bdb4 | Phenotypic characterization of foxtail millet sgd1-1 and sgd1-2 mutants.a–c Wild-type Yugu1 (a), mutant sgd1-1 (b), and mutant sgd1-2 (c) grown in the field at the grain-filling stage. Bar = 10 cm. d Panicles of Yugu1, sgd1-1, and sgd1-2 plants. Bar = 2 cm. e, f Grain width (e) and grain length (f) of Yugu1, sgd1-1, sgd1-2, and F1 (sgd1-1 × sgd1-2) plants. Bar = 2 mm. g Panicle length, grain number per panicle, and 1000-grain weight in Yugu1, sgd1-1, and sgd1-2 plants. Five biological replicates were used for each measurement (n = 5). Error bars indicate mean ± SD. Significant differences between wild-type and mutant plants were determined by unpaired two-sided Student’s t-tests, (*P < 0.01, **P < 0.001). h Grain length and grain width of Yugu1, sgd1-1, and sgd1-2 plants (n > 100, unpaired two-sided Student’s t-tests, *P < 0.01, **P < 0.001. Error bars indicate mean ± SD). i Resin sections of immature grains of Yugu1, sgd1-1, and sgd1-2 plants (from left to right). The white dashed line represents the section position. The black box represents the magnification position. j Scanning electron microscopy (SEM) analysis of lemmas of Yugu1, sgd1-1, and sgd1-2 plants. The black box represents the magnification position with an enlarged view on the right. The red box indicates the cell size. Bar = 1 mm (left), 50 μm (right). These experiments in (i, j) were repeated five times independently with similar results. k Cell length, cell width, and cell number in the major and minor axes in mature seeds of Yugu1, sgd1-1, and sgd1-2 plants. Cell length and width were measured in more than 50 cells. Cells from five seeds were counted. The two ends of the box plot and the upper, middle, and lower box lines represent the upper edge, lower edge, median, and two quartiles of values in each group. Error bars indicate mean ± SD. Significant differences were determined by unpaired two-sided Student’s t-tests. *P < 0.01, **P < 0.001 vs. Yugu1 plants. n.s. means not statistically significant. Source data are provided as a Source Data file. | PMC10226984 | 41467_2023_38812_Fig1_HTML.jpg |
0.418539 | 782261951c66468bbd98e4923f5d3ec9 | Positional cloning and functional characterization of SGD1.a Map-based cloning of SGD1. The gene structure of SGD1 and mutation sites in sgd1-1 and sgd1-2 are indicated. b Wild-type (WT) Ci846, SGD1 knockout plants (CR-sgd1-L1), and rescued plants (Com-SGD1-L1 and Com-ZmSGD1-L1) at the grain-filling stage. All plants were grown in a growth chamber under a 10-h light/14-h dark cycle at 30/26 °C. Bar = 10 cm. c Mature seeds of WT, CR-sgd1-L1, Com-SGD1-L1, and Com-ZmSGD1-L1 plants (from left to the right). Bar = 1 mm. d Panicles of WT, CR-sgd1-L1, Com-SGD1-L1, and Com-ZmSGD1-L1 plants. Bar = 1 cm. e SEM analysis of the lemma of WT, CR-sgd1-L1, Com-SGD1-L1, and Com-ZmSGD1-L1 plants (from left to right). Bar = 30 μm. This experiment was repeated five times independently with similar results. f Thousand-grain weight (n = 5), grain length and width (n > 100), cell length and width (n > 50), and cell number (n = 5) in WT, CR-sgd1-L1, Com-SGD1-L1, and Com-ZmSGD1-L1 plants. The two ends of the box plot and the upper, middle, and lower box lines represent the upper edge, lower edge, median, and two quartiles of values. Data were means ± SD. Significant differences were determined using unpaired two-sided Student’s t-tests. **P < 0.001 vs. WT plants. n.s. means not statistically significant. g SGD1-GFP colocalized with the membrane probe FM4-64. The white box marked with I represents the magnification position with an enlarged view. Bar = 20 μm. h Fluorescence intensity of SGD1-GFP and FM4-64 signals across the cell. i SGD1-GFP colocalized with the ER marker HDEL-mCherry in Nicotiana benthamiana leaf cells, along with a magnified view of the boxed areas. Bar = 20 μm. These experiments in (g, i) were repeated three times independently with similar results. j Fluorescence intensity of SGD1-GFP and HDEL-mCherry signals across the cell. k Expression of SGD1 in foxtail millet organs at different growth stages. Error bars indicate mean ± SD. n = 3 biological replicates. The gene expression profile of different organs of Yugu1 plants is shown in Supplementary Data 1. Source data are provided as a Source Data file. | PMC10226984 | 41467_2023_38812_Fig2_HTML.jpg |
0.419959 | b93606c1e7bc4664bf250e925dc23587 | SGD1 regulates grain yield in major cereal crops.a Generation of two independent rice OsSGD1 CRISPR-edited plant lines. The OsSGD1 gene structure, sgRNA sequence, and resulting mutations are highlighted. b Panicles of wild-type (WT) KitaaKe, CR-Ossgd1-L1, and CR-Ossgd1-L2 rice plants. Bar = 2 cm. c Mature grains of WT, CR-Ossgd1-L1, and CR-Ossgd1-L2 rice plants. Bar = 4 mm. d Grain number per panicle (n = 5), 100-grain weight (n = 5), and grain length and width (n > 15) in WT, CR-ossgd1-L1, and CR-ossgd1-L2 plants. The two ends of the box plot and the upper, middle, and lower box lines represent the upper edge, lower edge, median, and two quartiles of values in each group. Error bars indicate mean ± SD. Significant differences were determined using unpaired two-sided Student’s t-tests. **P < 0.001 vs. WT plants. e Generation of two independent wheat TaSGD1A/1B/1D triple mutants by CRISPR/Cas9. The gene structures, sgRNA sequences, and resulting mutations of TaSGD1A, TaSGD1B, and TaSGD1D lines are illustrated. f Panicles of WT (Fielder), CR-Tasgd1a/1b/1d-L1, and CR-Tasgd1a/1b/1d-L2 plants. Bar = 3 cm. g Mature grains of WT (Fielder), CR-Tasgd1a/1b/1d-L1, and CR-Tasgd1a/1b/1d-L2 lines. Bar = 4 mm. h Panicle length and weight (n = 5), grain number per panicle (n = 5), 100-grain weight (n = 5), and grain length and width (n > 100) in the plant lines described in (e). Error bars indicate mean ± SD. Significant differences were determined using unpaired two-sided Student’s t-tests. **P < 0.001 vs. WT plants. Source data are provided as a Source Data file. | PMC10226984 | 41467_2023_38812_Fig3_HTML.jpg |
0.466678 | 8f3bcf6111284b03b48b73ed61177b82 | SiUBC32 directly interacts with SGD1 and regulates grain yield.a Subcellular localization of SGD1 and SiUBC32 in S. italica protoplasts. Bar = 10 μm. b Split-ubiquitin membrane-based yeast two-hybrid analysis of the interaction between SGD1 and SiUBC32. The asterisks represent empty vector controls. Positive interactions were evaluated using yeast cells grown on a synthetic defined medium lacking Leu, Trp, His, and adenine (–LWHA) in the presence of 10 mM 3-aminotriazole (3-AT). c In vitro pull-down analysis of the interaction between MBP-SGD1 and GST-SiUBC32. GST-tagged proteins were immobilized on glutathione sepharose beads and incubated with maltose-binding protein (MBP)-tagged proteins. Washed beads were immunoblotted with anti-MBP or anti-GST (top two panels). Input proteins are shown by immunoblotting (middle two panels) and Coomassie blue (CBB) staining (bottom). d SGD1 interacts with SiUBC32 in the split luciferase complementation assay. SiBAS1 was used as a negative control. Vectors were paired and co-transformed into tobacco leaves. e Analysis of the SGD1–SiUBC32 interaction using in vivo co-immunoprecipitation (Co-IP) assay. SGD1-HA and SiUBC32-FLAG were co-expressed in S. italica protoplasts. IP was performed using anti-FLAG antibodies, and the associated protein was detected by immunoblotting with anti-HA antibodies. f The E3 ligase activity of SGD1. UBA1-S, SiUBC32-S, E2CK-S, SGD1c-Myc, and His-FLAG-Ub were expressed in E. coli. UBA1, SiUBC32, and E2CK were detected by immunoblotting using anti-S antibodies. SGD1c activity was detected by anti-Myc antibodies. Ub conjugates were detected by anti-FLAG antibodies. These experiments from (a–j) were repeated three times independently with similar results. g Morphological features of wild type (WT), CRISPR-edited sgd1 (CR-sgd1-L1), Siubc32 (CR-Siubc32-L1), and sgd1/Siubc32 grown in a growth chamber for 40 days under a 10-h light/14-h dark cycle. Bar = 10 cm. h Panicles of WT, sgd1, Siubc32, and sgd1/Siubc32 plants. Bar = 1 cm. i Grain size of WT, sgd1, Siubc32, and sgd1/Siubc32 lines. Bar = 2 mm. j SEM analysis of the lemmas of WT, sgd1, Siubc32, and sgd1/Siubc32 plants. Bar = 60 μm. This experiment was repeated five times independently with similar results. k Panicle length (n = 5), 1000-grain weight, grain length and width (n > 100), and cell length and width (n = 50) of WT, sgd1, Siubc32, and sgd1/Siubc32 plants. Error bars indicate mean ± SD. Different lowercase letters indicate significant differences (P < 0.05, one-way analysis of variance with Tukey’s multiple comparisons test). Source data are provided as a Source Data file. | PMC10226984 | 41467_2023_38812_Fig4_HTML.jpg |
0.422528 | 7e0ce1e5d63e47a89ef48d3200f2c12c | The sgd1 mutant shows decreased sensitivity to BR.a Bristle phenotype in wild-type (WT) and sgd1 plants. Bar = 2 mm. b Comparison of bristle length between WT and sgd1 lines (n = 5, unpaired two-sided Student’s t-tests, **P < 0.001. Error bars indicate mean ± SD). c Leaf architecture responses to BR in WT and sgd1 plants. Plants were treated with 5 μM 24-epi-brassinolide (eBL) for 3 days. d, e Leaf angle (d) and leaf drooping (e) of the second leaf from the top as red arrows indicated in (c). Leaf drooping was calculated by the bending site length (BSL) to proximal-distal distance (PDD) ratio (n = 5, unpaired two-sided Student’s t-tests, **P < 0.001; n.s. means not statistically significant; Error bars indicate mean ± SD). f Root growth phenotypes in WT and sgd1 plants grown in the presence of the indicated concentration of eBL for 6 days in a growth chamber under a 10-h light/14-h dark cycle. Bar = 2 cm. g Root length in WT and sgd1 plants under eBL treatment (n > 25, unpaired two-sided Student’s t-tests, **P < 0.001; n.s. means not statistically significant; Error bars indicate mean ± SD). h Number of differentially expressed genes overlap with BZR1 targets in WT-BL/WT, dpy1/WT, and sgd1/WT plants. i Heatmap of the expression patterns of BZR1-target genes (Supplementary Data 6) in WT-BL/WT, dpy1/WT, and sgd1/WT lines. j qRT-PCR analysis of the relative expression levels of SiD2 and SiCYP51G3 in 7-day-old WT and sgd1 seedlings, n = 6, two-sided Student’s t-tests, **P < 0.001. Error bars indicate mean ± SD. k Relative expression levels of SiGLR2.7, SiCBF2, and SiBRH1 in WT and sgd1 plants treated with 0.01 μm eBL. Gene expressions were quantified by qRT-PCR with six replications. Error bars indicate mean ± SD. Different lowercase letters indicate significant differences (P < 0.05, one-way analysis of variance with Tukey’s multiple comparisons test). Source data are provided as a Source Data file. | PMC10226984 | 41467_2023_38812_Fig5_HTML.jpg |
0.457535 | 335efa88bfca42909664e0d04f12abca | SGD1 interacts with SiBRI1 and enhances SiBRI1 protein stability.a Split luciferase complementation assay of the interaction between SGD1 and SiBRI1. The indicated vector pairs were co-transformed into tobacco leaves. SiBIN2 was used as a negative control. b Split-ubiquitin membrane-based yeast two-hybrid analysis of the interaction between SGD1 and SiBRI1. SiBRI1, SiBRI1n, and SiBRI1c represent the full-length, N-terminal transmembrane, and C-terminal kinase domain, respectively. Asterisks indicate empty vectors. Positive interactions were evaluated using yeast cells grown on a synthetic defined medium lacking Leu, Trp, His, and adenine (–LWHA). c In vitro pull-down analysis of the interaction between SGD1 and SiBRI1c. GST or GST-SiBRI1c were immobilized on glutathione sepharose beads and incubated with maltose-binding protein (MBP) or MBP-SGD1. Washed beads were immunoblotted with anti-MBP or anti-GST antibodies (upper two panels). Input immunoblotted proteins are shown in the third and fourth panels, and CBB-stained proteins are shown in the bottom panel. d In vivo Co-IP analysis of the interaction between SGD1 and SiBRI1. SiBRI1-HA and SGD1-FLAG were co-expressed in S. italica protoplasts. Co-IP was performed using anti-FLAG antibodies, and the associated protein was detected by immunoblotting with anti-HA antibodies. e Ubiquitination of SiBRI1 by SGD1. MBP-SiBRI1-HA, E1, E2, SGD1c-Myc, mSGD1c-Myc (C426A and H443A), and His-FLAG-Ub were expressed in E. coli. SiBRI1 ubiquitination was detected by immunoblotting with anti-HA antibodies. Ub conjugates were detected using anti-FLAG antibodies. SGD1c and mSGD1c activity was detected with anti-Myc antibodies. f SiBRI1 ubiquitination level was lower in sgd1 than in WT plants. SiBRI1-HA and FLAG-Ub were co-expressed in WT and sgd1 protoplasts. Following IP with anti-FLAG, SiBRI1 ubiquitination was detected by immunoblotting with anti-HA antibodies. g SGD1 enhances SiBRI1 protein stability in S. italica protoplasts. SiBRI1-HA, SGD1-FLAG, and mSGD1-FLAG were detected by immunoblotting with anti-HA and FLAG antibodies. GFP-Myc was used as an internal transfection control and detected using anti-Myc antibodies. The relative abundance of SiBRI1-HA is shown above the blot. h SGD1 enhances SiBRI1 protein stability in vivo. Fourteen-day-old seedlings collected from Ci846, sgd1, and SGD1-overexpressing plants (OE-SGD1) were used for immunoblots. SiBRI1, SGD1-eGFP, and SiBZR1 (phosphorylated and dephosphorylated) were detected by immunoblotting with antibodies against SiBRI1, GFP, and SiBZR1. Actin was used as a loading control. i SiBRI1 stability was reduced in CRISPR-edited sgd1 mutant lines. SiBRI1 in 14-day-old Ci846 (WT), CR-sgd1-L1, and CR-sgd1-L2 seedling leaves was detected by immunoblotting with anti-SiBRI1 antibodies. j SiBRI1 stability was reduced in EMS-induced sgd1 mutant lines. SiBRI1 in Yugu1 (WT), sgd1-1, and sgd1-2 seedling leaves were detected by immunoblotting with an anti-SiBRI1 antibody. The relative abundance of SiBRI1 in (h–j) is shown above the blot. These experiments in (a–h) were repeated three times independently with similar results. k–p SiBRI1 concentration in 14-day-old Ci846 (WT, k), sgd1 (CR-sgd1, m), and OE-SGD1 (n) seedling leaves treated with 100 μM cycloheximide (CHX) for 0, 3, and 6 h. SiBRI1 was detected using anti-SiBRI1 antibodies. Actin was used as a loading control. Three biological replicates were used for SiBRI1 protein abundance measurements (Supplementary Fig. 12). Quantitation of the relative SiBRI1 immunoblot signals was shown in (l, n, p), n = 3 biological replications. Error bars indicate mean ± SD. q–s Overexpression of SiBRI1 partially rescues the sgd1 phenotype. q Morphological features of WT (Ci846), sgd1, BRI1/sgd1-L1, and BRI1/sgd1-L2 (transformation of pUbi:SiBRI1-eGFP to an sgd1 background) plants are grown in a growth chamber for 40 days under a 10-h light/14-h dark cycle. Bar = 10 cm. r Grain size of WT, sgd1, BRI1/sgd1-L1, and BRI1/sgd1-L2 lines. Bar = 2 mm. s Panicles of WT, sgd1, BRI1/sgd1-L1, and BRI1/sgd1-L2 plants. Bar = 1.5 cm. Source data are provided as a Source Data file. | PMC10226984 | 41467_2023_38812_Fig6_HTML.jpg |
0.407138 | c714257523c84808bdfc96b30c3587c2 | Natural variations of SGD1 associated with grain yield improvement in Setaria.a Whole-genome selective sweep analysis using the Fst index. The black and red dashed lines indicate 5 and 1% thresholds, respectively. The red dots indicate potential genomic regions that met the 1% threshold. b
Fst of SGD1 and a neighboring 400-kb region between wild species and landraces. The red line indicates a 5% threshold. c The nucleotide diversity index (π) of SGD1 and a neighboring 400-kb region between landraces and cultivars. The red line indicates a 5% threshold. The vertical dashed lines in (b, c) represent the SGD1 genomic region. d
π in the SGD1 gene in different Setaria subgroups. The position and gene structure of SGD1 are illustrated in the Y axis. e Haplotype analysis revealed that SGD1 was under human selection. Four SGD1 haplotypes are shown in different colors. n corresponds to the total number of varieties in each pool. f Major agronomic traits (panicle weight, grain weight per panicle, 1000-grain weight, and grain number per branch) were analyzed in 960 of 1681 Setaria germplasms by SGD1 haplotype. Uppercase letters indicate significant differences (P < 0.05, one-way analysis of variance with Tukey’s multiple comparisons test). g–j Morphological features of wild type (WT), sgd1, OE-SGD1H1-L1, and OE-SGD1H1-L2 (two independent transgenic lines overexpressing SGD1H1 in WT background). g Panicles of WT, sgd1, OE-SGD1H1-L1, and OE-SGD1H1-L2. Bar = 3 cm. h Grains per panicle in WT, sgd1, OE-SGD1H1-L1, and OE-SGD1H1-L2 (from left to right) plants. Bar = 3 cm. i Grain width in WT, sgd1, OE-SGD1H1-L1, and OE-SGD1H1-L2 plants. Bar = 2 mm. j Grain length in WT, sgd1, OE-SGD1H1-L1, and OE-SGD1H1-L2 (from top to bottom) lines. Bar = 2 mm. k Measurements of grain area, 1000-grain weight, panicle length, and grain weight per panicle in WT, sgd1, OE-SGD1H1-L1, and OE-SGD1H1-L2 plants. n = 170 for grain area measurement and n = 5 for other measurements. Data were means ± SD. Significant differences were determined using unpaired two-sided Student’s t-tests. *P < 0.05, **P < 0.01 vs. WT plants). Source data are provided as a Source Data file. | PMC10226984 | 41467_2023_38812_Fig7_HTML.jpg |
0.404417 | 632df999d7eb4c15823fc638097703e2 | Flowchart of patient selection | PMC10227118 | 701_2023_5612_Fig1_HTML.jpg |
0.413481 | 6cf343799ebb48d4b4be807f6fffdfdb | Digital subtraction angiographies (DSAs) of the second patient. The patient was referred to the Department of Neurosurgery at the age of 14, and surgery with pre-embolization was planned. (A) Pre-embolization DSA shows arteriovenous malformation (AVM) in the parietal Sylvian fissure on the right side. AVM received feeding from the middle cerebral artery (MCA) branches and drained via two large veins to the superior sagittal sinus (SSS). (B) After embolization, AVM did not fill up, and the early venous filling was no longer observed. (C) Six months later, the patient suffered a new generalized epileptic seizure. DSA showed recanalized AVM. (D) AVM was operated on a few months later. Postoperative DSA confirmed the complete eradication of AVM. (E) Surveillance DSA one year later showed no signs of AVM. The follow-up was concluded. (F) Fourteen years later, at the age of 30, the patient underwent DSA as part of a new follow-up protocol; it showed recurrent AVM in the same location. An elective operation was scheduled | PMC10227118 | 701_2023_5612_Fig2_HTML.jpg |
0.429826 | f0ab557b936349f7bb12711222def78e | Flow chart of literature search and sorting process. | PMC10227490 | HSR2-6-e1239-g001.jpg |
0.474482 | 5f78c58df909482d919500f24efe08a5 | Pairwise sequence comparison matrix. The upper diagonal panel is the number of gaps. The lower diagonal panel is the percent identity. (a) Comparison of old and new world camels. (b) Comparison of dromedary camel LF with whales and other marine mammals LF. (c) Comparison of dromedary camel LF with Bats LF. (d) Comparison of dromedary camel LF with other domestic animals LF. | PMC10229236 | BMRI2023-2322286.001.jpg |
0.459306 | 66c04fe68bbd4f57a71e08655fb88df0 | Phylogram showing the relations of camel LF. | PMC10229236 | BMRI2023-2322286.002.jpg |
0.466489 | 50e342f8ea7c463a930f10fb3c5d306e | RMSD and RMSF of the bovine, camel, and human LF: (a) RMSD; (b) RMSF. | PMC10229236 | BMRI2023-2322286.003.jpg |
0.445025 | 10f3cd3cd9d84c57a773cf3e3930418a | The structural characteristics of bovine, camel, and human LFs: (a) intermolecular hydrogen bonds; (b) SASA; (c) Rg. | PMC10229236 | BMRI2023-2322286.004.jpg |
0.4281 | 220a9939a12b45ce840329804feb2927 | Performance of hydrogel-in-hydrogel printing.a Strategy and set-up for hydrogel-in-hydrogel live bioprinting. HCC-hydrogel 2P-printing can be performed within solid gel of a 3D organ-like culture at any experimentally required time point of cell growth by (i) allowing liquid HCC-polymers to diffuse within the pre-existing solid gel, (ii) fabricating 3D hydrogel objects by using a multiphoton microscope equipped with a motorized xyz stage and a femtosecond near-infrared tightly-focused pulsed laser emission, (iii) removing the un-crosslinked HCC-polymers from the 3D organ-like culture via diffusion. b Quantification of the diffusion coefficient of 40 (grey) or 500 (black) kDa FITC-dextrans within Matrigel. Data are shown as mean ± s.d. of three independent replicates; unequal variance Student’s t-test; *P < 0.0213. c Left, representative confocal z-stack images of sequentially fabricated HCC–gel hydrogels (green) within the same Matrigel drop and printed at different xyz positions by using near-infrared laser pulses through a multiphoton microscope; total Δz = 100 μm or 50 μm or 25 μm. Scale bars, 100 μm. Middle and right, 3D-volume reconstruction reveals the volumetric position of the various objects; coordinates are shown in red. d Quantification of the minimum line width obtained using scan or freeline scanning mode, respectively scan and line scan. Data are shown as mean ± s.d. of three independent replicates. e Multiple HCC–Gel structures of three independent replicates fabricated by near-infrared multiphoton laser pulses. Δz = 20 μm. Scale bar, 20 μm. f Representative 3D reconstruction of three independent replicates of a HCC–Gel spiral-shaped hydrogel fabricated using the free line-scan mode. Δz = 30 μm. Coordinates are shown in red; scale bar, 100 μm. g Quantification of the area of hydrogels sequentially fabricated at fixed laser power (1 mW) and wavelength (800 nm) within the same Matrigel drop; each hydrogel series was analyzed just after photo-crosslinking (day 0) or at 2 days after the last 3D bioprinting. Data are shown as mean ± s.d. of three independent replicates. h Young’s modulus measured by atomic force microscopy of hydrogels photo-crosslinked at fixed laser power (1 mW) and wavelength (800 nm). Each hydrogel series was analyzed just after photo-crosslinking (day 0) or at 2 days after the last 3D bioprinting. Data are shown as mean ± s.d. of three independent replicates; multiple comparison one-way ANOVA was used; n.s., not statistically significant. | PMC10229611 | 41467_2023_37953_Fig1_HTML.jpg |
0.375462 | 500907f38e334c7391385aa463f741a9 | Temporal control of hydrogel-in-hydrogel live bioprinting and controlled axon guidance of oSpCs.a Confocal fluorescence images acquired at different ΔZ (Z0, Z1, Z3, Z4) and relative Z-stack imaging analysis showing the presence of hydrogels (blue) fabricated above the central body of the oSpC cultured in 3D matrigel droplet for 7 days before bioprinting. Phalloidin (green) was used to detect cellular projections. Scale bar, 100 μm. b Confocal fluorescence images acquired at different ΔZ (Z0, Z1) and relative Z-stack imaging analysis showing the presence of multiple hydrogels (blue) fabricated at different Z planes that embed alive (calcein-positive, green) cellular projections of the oSpC cultured in 3D matrigel droplet for 7 days before bioprinting. Scale bars, 100 μm. c Quantification of vital (calceine-positive) neuronal projections embedded within bioprinted hydrogel volume. Data are shown as mean ± s.d. of five independent replicates; unequal variance Student’s t-test was used; P < 0.05 was considered statistically significant. d Representative images showing integrity of single-line bioprinted hydrogel (blue) and vital (calcein-positive, green) cellular projection of the oSpC cultured in 3D matrigel droplet for 7 days before bioprinting. Scale bar, 10 μm. e Representative fluorescence images of a spinal cord culture showing alignment of axons protruding within fabricated hydrogel (i) as opposed to randomly oriented axon organization in absence of the hydrogel (ii). Scale bar, 200 μm. f Quantification of neural projection directionality performed in area where the neural projections were far (no bioprinting) or in proximity (bioprinted hydrogels) of the fabricated hydrogel-in-hydrogel structures. | PMC10229611 | 41467_2023_37953_Fig2_HTML.jpg |
0.388123 | aa86f54680f54671a7aeff27b0b78080 | Hydrogel-in-hydrogel live bioprinting for studying cancer cell migration in organoid 3D cultures.a Brightfield time lap images (0, 8, 20 h) of a hydrogel-embedded tumor spheroid (day 6 post printing) growing within a cage of HCC-PEG pillars fabricated 1 day post organoid culture. Scale bar, 100 μm. b Fluorescent images of the tumor spheroid in c, showing different stages of cellular migration through the pillars day 7 post printing. Scale bars, 100 μm. c Young’s modulus measured by atomic force microscopy of 4-arm (black) or 8-arm (gray) HCC-PEG hydrogels photo-crosslinked at increasing laser power (300 or 500 μW) and wavelength (800 nm). Hydrogels were sequentially fabricated within the same Matrigel drop. Data are shown as mean ± s.d. of three independent replicates; all measurements performed are reported; unequal variance Student’s t-test was used; P < 0.05 was considered statistically significant. d Brightfield time lapse images of hydrogel-embedded tumor spheroid 5 or 7 days after bioprinting of 4-arm (upper panels) or 8-arm (lower panels) HCC-PEG pillars fabricated 1 day of organoid culture. Scale bars, 100 μm. e Quantification of nuclei detected out of the pillars of the hydrogel-embedded tumor spheroid 7 days after bioprinting of 4-arm (black) or 8-arm (gray) HCC-PEG pillars fabricated 1 day of organoid culture. Representative images of 3D reconstructions with xyz coordinates and 50 μm scale bar are shown. f Four-arm HCC-PEG hydrogel pillars were fabricated 1 day or 7 days post organoid culture (days 0 and 6 post printing, respectively) around a hydrogel-embedded growing tumor organoid. The brightfield images show the growth of the caged tumor spheroid at different time points. Scale bar, 100 μm. g Representative fluorescent image of tumor spheroid as in e at 14 days from first bioprinting step (day 15 of organoid culture). Scale bar, 100 μm. h Representative fluorescent images of cancer cells protruding through the bars of the first bioprinted hydrogel cage, invading the surrounding space and migrating through the pillars of the second fabrication step. Scale bars, 100 μm. | PMC10229611 | 41467_2023_37953_Fig3_HTML.jpg |
0.420011 | 045a66e12f884833ada36f905ef9be14 | Supra-organoid driven intestinal organoid morphogenesis via hydrogel-in-hydrogel live bioprinting.a Representative bright field and fluorescence images showing 60°primordial small intestine design and HCC-gel hydrogels (left panel, top view; right panel, 3D reconstruction view). Scale bars 200 μm. b Representative bright field (upper) and fluorescence (lower) images of mSIOs just after primordial small intestine HCC-gel hydrogel printing or 2, 4, 5 or 6 days of culture and bioprinting. Budding was observed according to the defied shape of the hydrogel. Scale bars 100 μm. c Representative bright field and fluorescence images showing mSIO buds invading multiple crypts at different Z-levels of the primordial small intestine design after 6 days of culture post-printing. Scale bar 200 μm. d Quantification of the ratio between the area of the organoid at day 0 of culture (dashed line) and the area of the organoid during the following culture days (1–6 days). Statistical analysis is shown in Supplementary Table 1. e Ratio between the central area of the primordial intestine-shaped hydrogels with the organoid at seeding time (dashed line) and the area occupied by the organoid from day 1–6 of culture. Statistical analysis is shown in Supplementary Table 2.f Quantification of the percentage of central area occupied by the mSIOs during the culture (0–6 days). Calculation of the percentage was shown for 5 independent mSIO cultures. g Quantification of the percentage of branched areas occupied by 5 independent mSIO during the cultures (4–9 days). h Upper panels, representative bright field (upper) and fluorescence (lower) images showing mSIO budding after 10 days of culture within the primordial small intestine-shaped HCC-gel hydrogel. The arrow points at the LGR5 (green) cells. Lower panels, representative images showing immunofluorescence analysis for OLM4 (red) (corresponding to the LGR5-GFP in (i) and FABP1 (yellow) of mSIO cultured for 10 days within the primordial small intestine-shaped HCC-gel hydrogel). Nuclei are stained with Hoechst (blue). The arrows point at the branched (red) or central (yellow) portion of the mSIO in respect to the hydrogel. Scale bars 100 μm (upper panels), 50 μm (lowe panels). | PMC10229611 | 41467_2023_37953_Fig4_HTML.jpg |
0.462825 | a15a62eb44fe4de9b8a24787d08797ce | 3D geometrical constrains imposed by hydrogel-in-hydrogel live bioprinting on organoid and organotypic cultures.a, b Induction of polarization in human fetal hepatocyte organoids. a Bright field images showing two printing strategies: distant walls not touching the growing organoid (above) and adjacent pillars touching the growing organoids (below) after 7 days of culture. Scale bar 100 µm. b Immunofluorescent panels showing non-polarized organoid distant from the printed structures (above) and a polarized organoid in correspondence of the printed pillars (below). Integrin beta-4 (INTβ4) shown in green, multidrug resistance-associated protein 2 (MRP2) shown in red, zonula occludens-1 (ZO-1) shown in cyan. Nuclei are stained with Hoechst (blue). Scale bars, 50 µm (large images, left) and 10 µm (higher magnification, right). c–f Ex vivo culture of mesenchyme-free lung epithelium rudiments, isolated from embryonic mice at stage E12.5. c Schematic of isolated fetal lung tips ex vivo culture and guided branching morphogenesis following 2 P bioprinting of gelatin pillars (red circles) in Matrigel. d 5-h interval snapshots of time-lapse reconstruction of budding lung tip during guided morphogenesis around pillar (red circle, indicated by red arrow). See full time-lapse in Supplementary Video. 3. Scale bar 150 µm. e Plot showing angle of tip bifurcation vs time from tip-pillar contact time (time 0) to 24 h of culture. Data are shown as mean ± s.e.m. of 8 independent replicates. f Bright-field images and immunofluorescent panel showing lung tip branching in between two pillars (red circles) and inner (luminal) polarity maintained (F-actin, green). Nuclei are stained with Hoechst (blue). Scale bar 100 µm. g Immunofluorescent panel showing lung tip branching in between pillar (red circle) with downregulation of sox9 (red) in correspondence of the pillar. Nuclei are stained with Hoechst (blue). Scale bars 50 µm. | PMC10229611 | 41467_2023_37953_Fig5_HTML.jpg |
0.40622 | a4513177ba9d423d90fbfb3c8abe81e8 | Sample flowchart. | PMC10230097 | fmed-10-1151310-a0001.jpg |
0.472386 | 19f81ee372774750992a25dcad31a9d2 | Direct, indirect, and total effect of multimorbidity on HRQoL. | PMC10230097 | fmed-10-1151310-g0001.jpg |
0.45557 | baf9d42664f942f6859285fd322d032f | Themes and sub-themes depicting issues, and multiple factors at various levels of the socioecological framework (adopted and modified) for the integration of HPV associated anal cancer screening in existing HIV care program of Pakistan | PMC10230466 | 12889_2023_15896_Fig1_HTML.jpg |
0.417927 | 8f1f8f0085c645a4aade55b68733e7bf | Mutation frequency in the hotspot-FCS region related to D614 and G614 variants in Indonesia. 371 sequences (319 GISAID and 52 laboratory-isolate sequences) consisting of 71 D614 variants and 300 G614 variants were included in the analysis. A significant increase of mutations was shown in G614 variant. The frequency of mutation for D614 and G614 variants was analyzed cumulatively during the subsequent month | PMC10231289 | 13337_2023_827_Fig1_HTML.jpg |
0.448076 | ded909fe52c04b478a0dcfb0f67231f9 | Analysis of mutations of the Spike region near the FCS active site (FCS region). a Mutations located in 5 different regions near the FCS active site (RRAR). One non-synonymous mutation was found at the FCS region in D614 variant, whereas 11 non-synonymous and three synonymous mutation (not shown) were found in G614 variant. b Mutation frequency and variability at the FCS region in G614 variant and D614 variant (histogram represents mean of the total 5 regions analyzed in this study; error bar represents standard deviation). Mutation frequency and variability at the FCS region in G614 variant was significantly higher than in D614 variant. c Mutation variability and frequency at the FCS region in G614 variant. Region four (675–692) of the FCS region in G614 variant showed the highest mutation variability and frequency | PMC10231289 | 13337_2023_827_Fig2_HTML.jpg |
0.439077 | baa880e0b0d94e6ea8a7d5bc84666cf7 | Amino acid change and mutation rate in Spike. a Amino acid change per site (by percentage) in various region located in Spike protein. D614G Hotspot-FCS region showed the highest amino acid change per site (20.8%). b Clock rate (subs per site per year) of various regions of the Spike protein. D614G Hotspot-FCS region showed the highest mutation rate (1.34 × 10–2 substitution per site per year) | PMC10231289 | 13337_2023_827_Fig3_HTML.jpg |
0.408189 | 76c65b0006c448dbb364681f335670f2 | Mutation proportion at the D614G Hotspot-FCS region. Circle in the image represents a relative percentage of particular mutation at the D614G Hotspot-FCS region. The most frequent mutation found at the D614G Hotspot-FCS region were D614G (81.94%), followed by Q677H (6.20%), S689R (2.96%), N679K (1.35%), and Q675H (1.08%) | PMC10231289 | 13337_2023_827_Fig4_HTML.jpg |
0.448951 | d829c48714414c16a4971a908c7c458b | Fold change of binding affinity (Kd) and binding energy (ΔG) to furin protease caused by mutations at the D614G Hotspot-FCS region of the Spike protein. The shifting of aspartic acid to glycine at position 614 (D614G) reduces the binding energy and affinity to furin protease by 0.1-fold and 3.73-fold times, respectively. Additional mutations near FCS region (Q675H, Q677H, N679K, P681H, and S689R) increase the binding energy and affinity to furin protease | PMC10231289 | 13337_2023_827_Fig5_HTML.jpg |
0.448424 | 6f1ab2b675944fdca1b58668ff8e263b |
(A) D1, Fresh jujube leaves; (B) D2, jujube leaf tea; (C) Jujube leaves used in green tea processing (Left: the fruit bearing shoots, Right: the leaves used in green tea processing). | PMC10231682 | fpls-14-1179553-g001.jpg |
0.471866 | bf51d1d4173b4644b6b33e40404e72be |
(A) Expression map of 11 metabolites in D1 and D2, (B) The PCA scores plot of the D1 group, the D2 group and the QC group, (C) OPLS-DA score plots of the D1 group versus the D2 group. (D) Displacement check diagram for D1 and D2. (E) D1 and D2 classification diagram of KEGG metabolic pathway, the ordinate is the second classification of KEGG metabolic pathway, and the abscissa is the number of metabolites annotated to this pathway. (F) D1 and D2 KEGG enrichment analysis bubble diagram, the abscissa is the enrichment significance p-value, and the ordinate is the KEGG pathway. The bubble size in the figure represents the number of metabolites enriched in the pathway. D1, Fresh jujube leaves; D2, Jujube leaf tea; QC, the quality control samples. | PMC10231682 | fpls-14-1179553-g002.jpg |
0.439777 | 77c3d2291edc47d0bf51ed2e42bebecc |
(A) Volcanic map of differential metabolites in D1 and D2, (B) Pie chart of the number of different types of 107 specific non-volatile metabolites in D1 vs D2, (C) and Heat maps of 107 different nonvolatile metabolites of jujube leaf tea before and after processing. D1, Fresh jujube leaves; D2, Jujube leaf tea. Each contains three repeats. (D) Thermogram of four types of non-volatile components in jujube leaf tea before and after processing. D1, Fresh jujube leaves; D2, Jujube leaf tea. Each contains three repeats. | PMC10231682 | fpls-14-1179553-g003.jpg |
0.369804 | a617d7f2871c4cc4b47fc39432a80219 |
(A) The topographic plot of D1 and D2 based on GC-IMS, The ordinate represents the retention time of gas chromatography, and the abscissa represents the ion migration time. Each point on both sides of the rip peak(the horizontal red line) represents a volatile organic compound. The compound concentration is represented by different colors, with white corresponding to low concentration and red corresponding to high concentration. The darker the color, the greater the concentration. (B) The three-dimensional topographic map of D1 and D2, (C) Difference comparison plots of D1 and D2, (D) Dynamic fingerprints of jujube leaves before and after processing, generated by Gallery Plot. Each row represents the sample signal peak, while each column represents each volatile compound in the different samples. The color represents the volatile compound concentration. The brighter the color, the higher the concentration. | PMC10231682 | fpls-14-1179553-g004.jpg |
0.445575 | bd65835f2a964ff38a9f6bf294ba74cb | Digital Terrain Model (DTM) of the study area at local and regional scale, with indication of the sites mentioned in the text. In (a) and (b) the isolated Udine Castle Hill and the depression of I Maggio Square are evident and are not related to any surface deformation, whereas in (b) the arrows highlight the ridge formed by the blind tectonic thrust of Udine-Buttrio. | PMC10232546 | 41598_2023_35175_Fig1_HTML.jpg |
0.403101 | 5ff8ce225bd14715a576542791bf25b3 | Detailed map of the hill of Udine with indications of the investigations and archaeological findings. Map of archaeological structures according to Buora28. The new stratigraphic cores drilled from the hilltop are indicated in yellow, while the blue dots are the geotechnical cores carried out in 1976 to restore the castle palace after the severe earthquakes that occurred that year. The red star indicates the point of the tunnel A, where a wooden tool had been found in 1943, and we radiocarbon dated it. The map was drawn with software Adobe Illustrator (www.adobe.com). | PMC10232546 | 41598_2023_35175_Fig2_HTML.jpg |
0.408627 | a7c00355504249d594898946278a9140 | Topographic profiles of the Hill of Udine obtained by LiDAR data with indications of the stratigraphic cores and archaeological excavations. Profile A-A’ clearly shows the depression now occupied by I Maggio Square, originally occupied by a small lake, drained in the nineteenth Century. | PMC10232546 | 41598_2023_35175_Fig3_HTML.jpg |
0.461801 | 891cd59c6eaa412f9106ef5f9efdc1c0 | Selection of pictures of the archaeological and stratigraphic excavations carried out on the hill of Udine. (a) Investigations carried out between October and December 2021 identified the sub-superficial occurrence of a prehistoric structure made of alternations of gravelly and clayey lenses (picture by A. Fontana). This area is almost in continuity with the zone depicted in image (b) (Archives of Civici Musei of Udine), where excavation of 1987 all around the building named "Casa della Contadinanza" and near the church of S. Maria found a large pit, named “Fossa Bronzo” (Bronze-Age pit) in Buora28. This structure had an areal extent of about 40 m2 and is located at the edge of the hilltop, suggesting that it was near the slope of the mound even in ancient time. The pit was filled with an organic-rich fine matrix and thousands of potsherds. A selection of the most diagnostic fragments of pottery for chrono-typology is reported in Fig. 5 and in Supplementary Fig. S7. The fragments cover a time span between 1400 and 600 BCE, but with the majority of fragments dating to the RBA and FBA (i.e. 1350–950 BCE). (c) Picture taken in 1953, during the work for excavating the water tanks that now occupy most part of the esplanade of the hilltop, up to a depth of about 6 m (see Supplementary Fig. S2) (Archives of Civici Musei of Udine). The site is close to the monumental stairs of the northern entrance of the building called “the Castle”, and it has been documented that alternations of gravels and clays are present below 1.5–2 m of historical deposits rich in the organic component. A similar situation was found in core CAST-5, which is close to this site (see Fig. 4a). | PMC10232546 | 41598_2023_35175_Fig4_HTML.jpg |
0.498562 | 623599e3c03d4890b235c6b93983fe5c | Selection of potsherds found in the pit “fossa bronzo”, investigated in 1987 during the archaeological excavation carried out along the eastern margin of the hilltop of Udine Castle Hill. The different typo-chronological phases are separated according to G. Tasca29 and the numbers refer to the catalog of fragments published by him29. | PMC10232546 | 41598_2023_35175_Fig5_HTML.jpg |
0.441367 | bcf59480313846088d4bf8b8d5164dd2 | Stratigraphic section of the Udine mound with indications of cores, tunnels and archaeological excavations. The trace of the section is shown in Fig. 3 as A–A’. (a) 2021 archaeological excavation (test trench of 12 × 8 m). The excavation reached a depth of 3 m and enlightened floors, walls and two tombs dating between the fifth and eighth centuries CE, found just below the present ground surface; the section in the upper box shows the traces of a vertical buttress closely paralleled by the so-called “gabions”, forming the wooden framework of those earth embankments. (b) 2020 archaeological excavation under Palazzo Dorta. The investigation uncovered the floor of a hut of RBA dating to about 1300–1200 BCE, under 4 m of later deposits starting with a gravelly colluvium containing Iron Age potsherds and likely originating from the hill30. The RBA deposit overlays the original natural topography; (c) 1943 air-raid shelter tunnels, according to data in Someda De Marco, where a wooden tool was found27 and radiocarbon dated to RBA; the section in the upper box shows the stratigraphic sequence characterized by inclined successions of gravels and clayey lenses; (d) tunnel “Malignani” dug in 1943 into the western flank of the hill, starting at about 10.3 m above the ground level of the neighboring city center. It was dug 8.5 m horizontally into the hill and, in this case too, the stratigraphic sequence was characterized by inclined successions of gravels and clayey lenses27; a detailed section is not available (cf.27), see the text for details; (e) Archaeological excavation in Via Mercatovecchio; the detailed section is not displayed in this figure, see the text for details23,30. | PMC10232546 | 41598_2023_35175_Fig6_HTML.jpg |
0.430811 | 68e0dbef91da49c9a7b753cea8789a38 | DTMs and aerial images of some of the most representative largest earth structures in the alluvial plains of northern Italy and comparison with Silbury Hill (UK) and Cahokia Monks Mound (Illinois, USA). For location of the Italian sites see Fig. 1. Figure (j) modified from41; figure (k) is elaborated from a satellite image of 2003 from Google Earth Maxtar Technologies 2023. The figures were produced elaborating the DEMs and images with software QGIS (https://www.qgis.org) and Adobe Illustrator (www.adobe.com). | PMC10232546 | 41598_2023_35175_Fig7_HTML.jpg |
0.432128 | 2f8d1d31ef004a8fbbe92c63c352eb38 | Child mortality in three major Asian nations during 1991–2016 [3, 4] | PMC10232642 | 41271_2023_413_Fig1_HTML.jpg |
0.463504 | d4417fd09032445294755fd5b196018f | Life expectancy at birth in Bangladesh, South Asia, and Asia [5] | PMC10232642 | 41271_2023_413_Fig2_HTML.jpg |
0.439114 | 186e75664c5d4f04b98d7622de562188 | Neonatal, infant and under-five mortality trends in Bangladesh, 1991–2018 (authors produced the figure from World Bank (2019) databank) [7] | PMC10232642 | 41271_2023_413_Fig3_HTML.jpg |
0.421395 | e93a7f414e044c42ad3beab06cf20805 | Contexts selected count. | PMC10232935 | gr10_lrg.jpg |
0.486171 | 65156689cd9740efa2fc5c56173d27eb | Context collection interfaces. | PMC10232935 | gr1_lrg.jpg |
0.363568 | 237022ac00dc4ddb98909152a7d7426f | Verification interfaces for crowdsourcing tasks. | PMC10232935 | gr2_lrg.jpg |
0.436663 | 45e3bb5d29f242eb84e58161aa7fd5fc | Interfaces to update and verify restaurant information. | PMC10232935 | gr3_lrg.jpg |
0.497994 | 4635a91dea624539beca26f117de8896 | Interfaces for filtering restaurants by context. | PMC10232935 | gr4_lrg.jpg |
0.412919 | e54d89857d2c400789d26e9e2b375b5e | Interfaces of recommendation lists and after-meal rating. | PMC10232935 | gr5_lrg.jpg |
0.4167 | b7a720cb2530476fb5e502af218aa74f | Game designs for self- and social-competitive groups. | PMC10232935 | gr6_lrg.jpg |
0.397861 | d18a0f073204490d86961f5a1709f908 | Tasks completed by the 17 participants in each group. | PMC10232935 | gr7_lrg.jpg |
0.464196 | 9bf7b5007f9541769f4bdb2d6e499ec3 | Log plot of the number of tasks completed by participants in each group. | PMC10232935 | gr8_lrg.jpg |
0.513009 | cdddc540c1294f8c890bc882d3e1c36c | Cumulative number of task types in each group. | PMC10232935 | gr9_lrg.jpg |
0.423901 | 62407df3de1e40a5a037622d5ba5b6cf | PS facilitates HEV replication. A HEV capsid proteins (ORF2) were detected in HepG2 and A549 cells through Western blot analysis at 6 dpi. B The relative expression of ORF2 was analyzed and normalized to that of GAPDH by using Image J software. Student’s t-test was performed to analyze the difference between two groups. *p < 0.05, **p < 0.01, ***p < 0.001 | PMC10233519 | 12985_2023_2080_Fig1_HTML.jpg |
0.488905 | c6570ed49123441e90120a408dd60acc | DEPs in HEV-infected cells supplemented with FBS or PS. A Venn diagram. The red circle indicates the DEPs in HEV-infected cells (HEV vs. Mock); the yellow circle indicates the DEPs in HEV-infected cells supplemented with PS (HEV + PS vs. Mock); and blue circles indicate the DEPs in HEV-infected cells supplemented with PS (HEV + PS vs. HEV). B PPI network of 110 dysregulated proteins among 128 DEPs. C Hierarchical clustering analysis of DEPs in cells with or without HEV infection and with PS or FBS supplementation. Clustering with log2(FC) values; red indicates up-regulated proteins, and green indicates down-regulated proteins. D Functional classification of the 128 dysregulated proteins by GO enrichment analysis. E KEGG pathway analysis was performed to investigate the significant pathways wherein the 128 proteins were enriched in accordance with the related networks for pathway mapping | PMC10233519 | 12985_2023_2080_Fig2_HTML.jpg |
0.392705 | 9443d670e25e464c8b532859fd8508a3 | Comparison of DEPs in HEV-infected cells with or without PS supplementation. A Number of DEPs in different groups. B Hierarchical clustering analysis of 548 DEPs between different groups. Clustering with log2(FC) values; red indicates up-regulated proteins, and green indicates down-regulated proteins. PPI network of the DEPs in the HEV versus Mock (C), HEV + PS versus Mock (D), and HEV + PS versus HEV groups (E). PPI networks built by using the STRING database and Cytoscape software. Each node in the interaction network represents a DEP. Red nodes indicate up-regulated proteins, and green nodes indicate down-regulated proteins | PMC10233519 | 12985_2023_2080_Fig3_HTML.jpg |
0.456517 | dd3eab9faf5e483a981b8883d296e47c | GO enrichment analysis based on Cytoscape software with ClueGO was used to reveal the differences and connections of biological process, cellular component, and molecular function terms enriched in the HEV versus Mock group (A), HEV + PS versus Mock group (B), and HEV + PS versus HEV group (C) | PMC10233519 | 12985_2023_2080_Fig4_HTML.jpg |
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