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0.427661 | 7ddff9c732b545aa9ca4e1870a8a83f8 | a, b A depiction of virtual environment and foot trackers on walkway at the high (a) and low (b) elevation settings. Walkway dimensions matched a real-world walkway sized 0.4 m wide × 2.2 m long × 0.05 m high. Figure adapted with permission from Raffegeau et al. (2020a) | PMC10197029 | 221_2023_6638_Fig1_HTML.jpg |
0.425401 | a7ae7684523a42b5b9a6db6ddfea1508 | The median step length for each participant during each trial at low and high VR elevation and at self-selected (SS) and fastest comfortable (Fast) speeds (i.e., participants colored by age, mapping youngest to oldest from blue to yellow; see right bar). Black diamonds indicate condition means, black lines illustrate the slope of the change in step length across conditions. Post-hoc tests of the Age × Speed × Height interaction are indicated by asterisks reflecting significant condition effects (p < 0.001) and colored lines (age mapping split into median younger (blue line) and older (orange line) values) illustrating Age effects are detected in changes to step length from low to high heights at self-selected speeds, but not fast speeds (Table 2) | PMC10197029 | 221_2023_6638_Fig2_HTML.jpg |
0.402338 | 46dc4329ae2844c59f89904e90006306 | Workflow for brain-derived EV (bdEV) enrichment and characterization from different brain regions. bdEVs from 8 brain regions were separated by collagenase digestion, differential centrifugation, and size exclusion chromatography (SEC). After separation, bdEVs were characterized by particle count, imaging, protein phenotyping and small RNA sequencing. Created with BioRender.com. | PMC10197569 | nihpp-2023.05.06.539665v2-f0001.jpg |
0.407669 | 0f977b2aa9574c7e8318266621a60725 | (a) Particle concentrations of bdEVs from brain regions were measured by NFCM. Particle concentration for each region was normalized by tissue mass (per 100 mg). (b) bdEVs were visualized by negative staining transmission electron microscopy (TEM) (scale bar = 500 nm). TEM is representative of ten images taken of each region. (c) Size (diameter) distributions of bdEVs from brain regions as measured by NFCM and calculated as particles in each 5 nm size bin versus total detected particles in each sample (percentage). (d) Size distributions of bdEVs from brain regions as measured in TEM images and calculated as particles in each 50 nm size bin versus total detected particles in each sample (percentage). | PMC10197569 | nihpp-2023.05.06.539665v2-f0002.jpg |
0.389482 | 694dcd88ba484993b61e12328760dafe | EV surface protein phenotyping. CD63, CD81, and CD9 were detected on the intact bdEV surface by single-particle interferometric reflectance imaging sensor (SP-IRIS) (a) and multiplexed ELISA (b) and normalized per 100 mg tissue input. bdEVs were captured by antibodies to EV membrane proteins and detected by signal from a cocktail of anti-tetraspanin antibodies (CD63, CD81, and CD9). | PMC10197569 | nihpp-2023.05.06.539665v2-f0003.jpg |
0.491803 | ef1b15fd846741d1a557bfce8da9bd97 | Cell-of-origin marker profile on the bdEV surface. (a) Distribution of markers by cell types: neurons, microglia, and astrocytes. Cell-enriched markers were used as bdEV capture antibodies; EVs were then detected by signal from a cocktail of anti-tetraspanin antibodies (CD63, CD81, and CD9). Levels of neuron (b), microglia (c), astrocyte (d), overlapping (e) and non-CNS cell (f) markers were then normalized to the average of tetraspanin capture spot signals. | PMC10197569 | nihpp-2023.05.06.539665v2-f0004.jpg |
0.419745 | 48dad72184324bdebdfc5dcab87ca0b4 | bdEV small RNA profiles. (a) Principal component analysis (PCA) based on quantitative small RNA profiles of bdEVs from different regions. (b) Unsupervised hierarchical clustering of 15 of the most abundant bdEV miRNAs across regions. | PMC10197569 | nihpp-2023.05.06.539665v2-f0005.jpg |
0.437836 | 6de6f0fd45424d889a23c00ee9b32dc2 | Ferroptosis inducer erastin downregulates SNAI3-AS1 expression by increasing DNA methylation level of its promoter. A The expression of eight candidate lncRNAs in U87MG, U251 and A172 cells under erastin (10 μM, 48 h) treatments as measured by RT-qPCR. B Dual-luciferase reporter assays showed the transcription activity of SNAI3-AS1 promoter after erastin (5/10/20 μM, 48 h) treatments. C The correlation between DNA methylation level and gene expression of SNAI3-AS1 according to cBioPortal database. D The expression of SNAI3-AS1 in U87MG, U251 and A172 cells under 5-AZA (1 μM, 24/48 h) treatments as measured by RT-qPCR. E A Prediction analysis of CpG islands in the sequence range of 3100 bp upstream from the transcriptional start site in the SNAI3-AS1 promoter region. F BSP results of SNAI3-AS1 methylation status in U87MG, U251 and A172 cells under erastin (5/10/20 μM, 48 h) treatments. G Heat map of methylation percentage of SNAI3-AS1 in U87MG, U251 and A172 cells under erastin (5/10/20 μM, 48 h) treatments. H The expression of SNAI3-AS1 in U87MG, U251 and A172 cells under erastin (10 μM, 48 h) or erastin (10 μM, 48 h) combined with 5-AZA (1 μM, 48 h) treatments as measured by RT-qPCR and agarose gel image. *P < 0.05, **P < 0.01, ***P < 0.001, and n.s., not significant | PMC10197824 | 13046_2023_2684_Fig1_HTML.jpg |
0.431593 | 468c5882776544f0adc78b7dec9d0502 | SNAI3-AS1 inhibits the proliferation, invasion, and migration of glioma cells in vitro. A RT-qPCR was used to detect the expression of SNAI3-AS1in U87MG and U251 cells transfected with SNAI3-AS1 overexpressed lentiviral vector or control vector. B The growth curves of transfected U87MG and U251 cells were determined by CCK8 assays. C The colony formation assays were performed in transfected U87MG and U251 cells. D The proliferation of transfected U87MG and U251 cells was detected by EdU staining assays. E The transwell assays showed the migration and invasion abilities of transfected U87MG and U251 cells. F Cell cycle distributions of transfected U87MG and U251 cells were measured by flow cytometry. *P < 0.05, **P < 0.01, ***P < 0.001, and n.s., not significant | PMC10197824 | 13046_2023_2684_Fig2_HTML.jpg |
0.440953 | 0859dea2948c42748986aab0655212ce | SNAI3-AS1 promotes erastin-induced ferroptosis in vitro. A-D U87MG and U251 cells stably overexpressing SNAI3-AS1 were treated with erastin (10 μM) ± ferrostatin-1 (2 μM) for 48 h, cell viabilities were detected via CCK8 assays (A), intracellular MDA was determined by MDA assays (B), intracellular Fe2+ was measured by iron detection assays (C), lipid ROS accumulation was analyzed by flow cytometry with C11-BODIPY staining (D). E–H A172 cells with stable SNAI3-AS1 knockdown were treated with erastin (10 μM) ± ferrostatin-1 (2 μM) for 48 h, cell viabilities were detected via CCK8 assays (E), intracellular MDA was determined by MDA assays (F), intracellular Fe2+ was measured by iron detection assays (G), lipid ROS accumulation was analyzed by flow cytometry with C11-BODIPY staining (H). Transmission electron microscopy was performed to evaluate the ultrastructural changes of mitochondria in U87MG stably overexpressing SNAI3-AS1 (I) and A172 cells with stable SNAI3-AS1 knockdown (J) after treated with Erastin (10 μM) for 48 h. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, and n.s., not significant | PMC10197824 | 13046_2023_2684_Fig3_HTML.jpg |
0.439199 | e17fe4eb51044e718bc9c0d82b26e534 | SNAI3-AS1 inhibits mRNA stability of Nrf2. A A Venn Diagram showed the intersection result of correlation analysis between SNAI3-AS1 and ferroptosis-related genes in TCGA and CGGA693 databases. B RT-qPCR was used to detect the mRNA level of Nrf2 after SNAI3-AS1 overexpression or knockdown under DMSO and erastin (10 μM, 48 h) treatments. C The correlation between SNAI3-AS1 and Nrf2 in TCGA and CGGA693 databases. D Western blotting showed the level of Nrf2, GPX4 and 4-HNE after SNAI3-AS1 overexpression or knockdown under DMSO and erastin (10 μM, 48 h) treatments. E U87MG cells with SNAI3-AS1 overexpression and A172 cells with SNAI3-AS1 knockdown were transfected with a dual luciferase reporter plasmid containing Nrf2 promoter. The relative luciferase activity was measured and normalized. F After actinomycin D (5 μg/ml) treatment for 0, 2, 4, 6 h, RT-qPCR was used to analysis the Nrf2 mRNA stability in U87MG cells with SNAI3-AS1 overexpression and A172 cells with SNAI3-AS1 knockdown. G U87MG cells with SNAI3-AS1 overexpression and A172 cells with SNAI3-AS1 knockdown were transfected with a dual luciferase reporter plasmid containing Nrf2 mRNA 3’UTR. The relative luciferase activity was measured and normalized. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, and n.s., not significant | PMC10197824 | 13046_2023_2684_Fig4_HTML.jpg |
0.459227 | 2d9b4695a18d4343a9b46a9ec2dbf8ab | SNAI3-AS1 binds to SND1 protein. A RNA FISH analysis of SNAI3-AS1 localization in U87MG and A172 cells. 18S and U6 were used as positive controls. B After nucleocytoplasmic separation assay, the expression level of SNAI3-AS1 was determined via RT-qPCR. GAPDH and U6 were applied as positive controls. C Silver staining was used to identify the SNAI3-AS1-binding proteins pulled down by synthesized biotin-labeled SNAI3-AS1 probe. D Validation of the interaction between SNAI3-AS1 and SND1 protein through western blotting. E RIP assays were performed using anti-SND1 and IgG antibodies. The enrichments of SNAI3-AS1 by SND1 or IgG were detected via RT-qPCR. F The colocalization between SNAI3-AS1 and SND1 was determined by FISH combined with IF staining. G The predicted secondary structure of SNAI3-AS1. H Deletion mapping of the SND1-binding domain in SNAI3-AS1. Top, diagrams of full-length SNAI3-AS1 and the deletion fragments. Middle, the in vitro–transcribed full-length SNAI3-AS1 and deletion fragments with correct sizes were visualized by agarose gel image in U87MG cells. Bottom, immunoblot analysis for SND1 in the protein samples pulled down by different biotinylated SNAI3-AS1 truncations in U87MG cells. I The diagrams of Flag-tagged full-length or truncation plasmids with various assembled domains of SND1 protein. J Full-length or truncations of recombinant SND1 protein with correct sizes were validated by western blotting using anti-Flag in U87MG cells. K RT-qPCR detected the relative enrichment levels of SNAI3-AS1 in full-length or truncation SND1 RIP assays using anti-Flag and anti-IgG in U87MG cells. **P < 0.01, ***P < 0.001, and n.s., not significant | PMC10197824 | 13046_2023_2684_Fig5_HTML.jpg |
0.44443 | 8f42d029f19e4ddb8380a2b81d732068 | SND1 recognizes Nrf2 mRNA and enhances its stability in an m6A-dependent manner. A RIP assays were performed using anti-SND1 and IgG antibodies. The enrichments of Nrf2 mRNA by SND1 or IgG were detected via RT-qPCR. B After actinomycin D (5 μg/ml) treatment for 0, 2, 4, 6 h, RT-qPCR was used to analysis the Nrf2 mRNA stability in U87MG cells with SND1 overexpression and A172 cells with SND1 silence. C RT-qPCR detected the mRNA level of Nrf2 in U87MG cells with SND1 overexpression and A172 cells with SND1 silence. D Western blotting showed the protein levels of Nrf2 after SND1 overexpression or silence under (E) Schematic illustration was used to explain the design of dual luciferase reporter plasmids containing wild-type or mutant m6A sites in Nrf2 3’ UTR sequence. F Wild-type or mutant plasmids of reformed dual luciferase reporters were transfected into U87MG cells with SND1 overexpression and A172 cells with A172 cells with SND1 silence, respectively. The relative luciferase activity was measured and normalized. G m6A levels of U87MG cells with or without three m6A methyltransferases (METTL3, METTL14, and WTAP) silence were detected using the m6A RNA Methylation Quantification Kit and m6A dot blot assays. H U87MG cells with indicated interventions were treated with actinomycin D (5 μg/ml) for 0, 2, 4, 6 h, and Nrf2 mRNA stability was analyzed via RT-qPCR. I In METTL3-silenced or control U87MG cells, MeRIP assays and RT-qPCR were performed to calculate the relative enrichment of m6A modification. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, and n.s., not significant | PMC10197824 | 13046_2023_2684_Fig6_HTML.jpg |
0.412497 | ccc676c1c66e403286eda976999c929c | SNAI3-AS1 perturbed the recognition of Nrf2 3’UTR by SND1 to exert ferroptosis-sensitizing activity. A RIP assays showed the enrichments of Nrf2 mRNA by SND1 in Nrf2 mRNA in U87MG cells with stable SNAI3-AS1 overexpression or A172 cells with stable SNAI3-AS1 knockdown. B After actinomycin D (5 μg/ml) treatment for 0, 2, 4, 6 h, RT-qPCR was used to analysis the Nrf2 mRNA stability in U87MG and A172 cells with indicated interventions. C Dual luciferase reporter plasmids containing Wild-type or mutant Nrf2 mRNA 3’UTR p were transfected into U87MG and A172 cells with indicated interventions, respectively. The relative luciferase activity was measured and normalized. D RT-qPCR detected the mRNA level of Nrf2 in U87MG and A172 cells with indicated interventions. E After DMSO or erastin (10 μM, 48 h) treatments, the protein levels of Nrf2 in U87MG and A172 cells with indicated interventions were determined by western blotting. F-I U87MG and A172 cells with indicated interventions were treated with erastin (10 μM) ± ferrostatin-1 (2 μM) for 48 h, cell viabilities were detected via CCK8 assays (F), intracellular MDA was determined by MDA assays (G), intracellular Fe2+ was measured by iron detection assays (H), lipid ROS accumulation was analyzed by flow cytometry with C11-BODIPY staining (I). *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, and n.s., not significant | PMC10197824 | 13046_2023_2684_Fig7_HTML.jpg |
0.416632 | 06646577779a4cb69cc0f075fe1cb025 | SNAI3-AS1 overexpression promotes erastin-induced ferroptosis in vivo. A Schematic illustration showing the design of animal experiments. B Body weights of mice in each group were recorded during the experiment. C Kaplan–Meier survival of mice in each group. D Representative bioluminescence images and performed on days 10, 17, and 24 after implantation. Down, statistical analysis of bioluminescent tracking plots. E Representative images of HE staining, IHC assays (SND1, Nrf2, GPX4 and 4-HNE), and TUNEL assays in each group. F Schematic diagram of SNAI3-AS1/SND1/Nrf2 axis regulating ferroptosis in glioma cells. Erastin inhibits SNAI3-AS1 by increasing DNA methylation level of SNAI3-AS1 promoter. Decreased expression of SNI3-AS1 favors SND1 to bind and stabilize Nrf2 mRNA in an m.6A-dependent manner, thereby suppresses ferroptotic cell death. *P < 0.05, and ***P < 0.001 | PMC10197824 | 13046_2023_2684_Fig8_HTML.jpg |
0.431733 | 250d3aad7d754860a6871189ff2c7470 | (a) Bipedicle flap raised and sutured to its original position for creation chronic ischemic wound. (b) Full-thickness wounds created on the cephalic, central, and caudal parts of the flap are seen. | PMC10198350 | TJTES-29-1-g001.jpg |
0.464351 | fbb47b12409f448f818017280aae150c | The view of Clemex Vision Lite software image analyzing program. | PMC10198350 | TJTES-29-1-g002.jpg |
0.409451 | f101015b143241dbb857be60465de5f2 | Histopathological assessment (the arrows symbolizes; V: Vessel, F: Fibroblast, C: Collagen, and L: Lymphocyte). Vessels are more predominant in Group B2 and B3 when compared to Group A2 and A3 indicating neovascularization. (a) HBO non-received fresh PRP applied group (Group A2), (b) HBO non-received frozen PRP applied group (Group A3). (c) HBO received fresh PRP applied group (Group B2). (d) HBO received frozen PRP applied group (Group B3). | PMC10198350 | TJTES-29-1-g003.jpg |
0.472908 | c53c63dddfba437a9322fed2125cd735 | The graphic demonstrates wound surface area measurements on 5-10-15 days in HBO received group. | PMC10198350 | TJTES-29-1-g004.jpg |
0.534963 | 3b0e0398148f4827a1a99a669f0beb8f | The graphic demonstrates wound surface area measurements on 5-10-15 days in HBO non-received group. | PMC10198350 | TJTES-29-1-g005.jpg |
0.453427 | eb7b2dddbf0e44758e508241ec76c03c | Photographs of the wound surface areas evaluated by ImageJ digital analyzing program. The picture is showing wound healing of the created defects on the back of the rats according to the days of the experiment in HBO received fresh (a) and frozen PRP (b) applied groups. | PMC10198350 | TJTES-29-1-g006.jpg |
0.459285 | 970fd9530a8a4dada8d6df563d348dd2 | Aerobic exercise increases endurance but PQQ supplementation does not. We analyzed change in endurance but show final, post-training endurance for illustrative purposes. Different letters over different groups of bars represent a significant effect of training. | PMC10198381 | fphys-14-1165313-g001.jpg |
0.442911 | 85fa9ef9c9654409a16d0eb4e7ee1e13 | Standard metabolic rates increased with PQQ supplement. There was no significant effect of training on SMR, but we note that trained-only lizards had the lowest SMRs. Different letters over different groups connected by brackets represent a significant effect of PQQ supplementation. | PMC10198381 | fphys-14-1165313-g002.jpg |
0.417485 | ab2326f322f74f3097898fa5941ef59a | Mitochondrial DNA copy number in gastrocnemius muscle increased with aerobic exercise training (shown with solid lines) but decreased with PQQ supplements (shown with dashed lines). Different letters over different groups of bars or groups connected with brackets indicate a significant difference. | PMC10198381 | fphys-14-1165313-g003.jpg |
0.426573 | 9e7eaca827654117b5d18d1b58fb68b8 | Whole-organism resting metabolic rate (RMR) decreased with aerobic exercise training. Absolute metabolic rates are shown, but when corrected for body size females had significantly higher RMRs than males. Different letters over different groups of bars represent a significant effect of training. | PMC10198381 | fphys-14-1165313-g004.jpg |
0.499888 | e82ad9459bea4d10b73742c30659e5e2 | Aerobic exercise alters mitochondrial function but not baseline oxygen consumption of muscle fibers. This figure demonstrates the effect of endurance training on oxygen consumption rates (OCR) of gastrocnemius muscle fibers over 140 min. The addition of reagents allows changes to be seen in mitochondrial basal respiration, ATP linked respiration, and maximal respiratory capacity. Trained lizards did not experience as much of an increase in OCR as control lizards after the addition of FCCP and pyruvate, indicating lower maximal respiratory capacity. There was no difference between trained and control lizards OCR at baseline. Oligo = oligomycin, FCCP = carbonyl cyanide-p-trifluoromethoxyphenylhydrazone, Rot/Ant = rotenone and antimycin. *p < 0.05, **p < 0.01. | PMC10198381 | fphys-14-1165313-g005.jpg |
0.45882 | 9afed25c5f814b7395710a53efe6855a | Fourier transform infrared spectroscopy (FTIR) spectra of Chitosan, PNIPAM, Hyaluronic acid and CNH co-polymer, yielded by thermal precipitation followed by EDC/NHS crosslinking with their respective absorption peaks (a). Concentration dependent gelation time of CNH hydrogels (b), Visual observation of thermosensitive behavior of 5% CNH hydrogel at 25 °C (sol-state) and 37 °C (gel-state) with their respective viscosity (c, d) | PMC10199301 | 10856_2023_6732_Fig1_HTML.jpg |
0.499961 | e6b9f444020f493d84df8a8595f70f35 | Representative histogram of water content (a) and volume shrinkage (b) of 5% (w/v) PNIPAM and 5% CNH hydrogels at 37 °C temperature. Absorbance at 470 nm (c) and corresponding relative absorbance (d) of both PNIPAM and CNH thermo-responsive hydrogels at increasing temperature | PMC10199301 | 10856_2023_6732_Fig2_HTML.jpg |
0.445767 | 37df9589d6334d648fced9009ce87848 | Cytotoxicity evaluation by MTT assay after 1, 3, 7 days incubation of L929 fibroblast cells with hydrogel extracted media (a). The cell attachment and proliferation with hydrogel extracted media after 1, 3, 7 days of incubation (b). F-actin and nuclei visualized by FITC and HOECHEST respectively. Scale bar 250 µm | PMC10199301 | 10856_2023_6732_Fig3_HTML.jpg |
0.451135 | abd2b4ce00f14df8a785562385cd974a | McFarlane skin flap model at rat dorsum (a). Complete flap elevation and immediate closure after hydrogel application on the fascia. Three equal zones were divided for post-surgical evaluation. In-vitro papaverine release profile from papaverine loaded CNHP0.4 hydrogel (b) | PMC10199301 | 10856_2023_6732_Fig4_HTML.jpg |
0.392855 | 869746f3e92d4676abe5c7b3a426c375 | Digital photographs of skin flap survival on post operative 3 and 7 days with CNHP0.0 and CNHP0.4 hydrogel groups (a), Digital photographs of the inner side of skin flaps in each group on post operative day 7 showing tissue edema (b), Histograms showing percentage of flap survival, viable/ necrotic surface area (cm2) and percentage of tissue water content on post operative day 7 (c), Mean SOD and MDA levels in both hydrogel groups (d). All the values are expressed as means ± SDs (n = 6 per group). **p < 0.01, ***p < 0.001 and ****p < 0.0001 | PMC10199301 | 10856_2023_6732_Fig5_HTML.jpg |
0.452646 | 92f90d99fe094155a8480799786e5895 | Hematoxylin and eosin (H&E) staining and immunohistochemical (IHC) staining with CD34 and VEGF of CNHP0.0 and CNHP0.4 hydrogel groups showing comparative neovascularization, CD34 positive vessels/mm and % IOD of VEGF in skin flaps along with their co-relative histogram). All the values are expressed as means ± SDs (n = 3 per group). ***p < 0.001 | PMC10199301 | 10856_2023_6732_Fig6_HTML.jpg |
0.422212 | 05f86ac0409e430eae494a66f5151a81 | Immunohistochemical (IHC) staining of CNHP0.0 and CNHP0.4 hydrogel treated skin flaps with CD68 and CCR7 antibody showing reduced macrophage infiltration resulting suppressive inflammatory response in CNHP0.4 hydrogel treated skin flaps along with their co-relative histograms. All the values are expressed as means ± SDs (n = 3 per group). ***p < 0.001 | PMC10199301 | 10856_2023_6732_Fig7_HTML.jpg |
0.430494 | 1e024d4e0edd4916a3d3be5082a86686 | Patients’ enrollment algorithm. | PMC10199368 | JRMS-28-29-g001.jpg |
0.418926 | 97a5207e75774f8582e60d90928a8347 | Postoperative hemoglobin lost in bladder lavage fluid | PMC10199368 | JRMS-28-29-g002.jpg |
0.43314 | 78d49d41a6fa4f5284586952a6922a16 | Simultaneous measurement of the WitMotion sensors and the laser pointer device. A Proprioceptive tests; B The upper computer software | PMC10199988 | 40122_2023_487_Fig1_HTML.jpg |
0.421263 | 0b531f8f8e9d4cf5b5dee04e634ce116 | Bland–Altman plot detailing the comparison between the LPD and WS when rater A was assessing cervical flexion (A) and cervical extension (B). The red line (middle one) indicates the mean difference. Black lines (extremities) indicate upper and lower agreements. LPD universal instrument; WS WitMotion sensor | PMC10199988 | 40122_2023_487_Fig2_HTML.jpg |
0.438935 | 5a4f567d098944e1870daafa3c31fed4 | Bland–Altman plot detailing the comparison between the LPD and WS when rater A was assessing cervical left lateral flexion (A) and cervical right lateral flexion (B). The red line (middle one) indicates the mean difference. Black lines (extremities) indicate upper and lower agreements. LPD universal instrument, WS WitMotion sensor | PMC10199988 | 40122_2023_487_Fig3_HTML.jpg |
0.442883 | bb3b1063f675480ca3910a9b8bd9a189 | Bland–Altman plot detailing the comparison between the LPD and WS when rater A was assessing cervical left rotation (A) and cervical right rotation (B). The red line (middle one) indicates the mean difference. Black lines (extremities) indicate upper and lower agreements. LPD universal instrument, WS WitMotion sensor | PMC10199988 | 40122_2023_487_Fig4_HTML.jpg |
0.425221 | 2e3ad5447e794a13be5b6640f8557342 | Germination of rice seeds treated with different levels of UA. (A) Photograph of germinated seeds; (B) Germination ratios and (C) Lengths of germ and radicle, respectively. * and ** indicate significant levels at p < 0.05 and 0.01, respectively. The unit of 10, 50 and 200 is μg/mL. CK, control check; UA, ustiloxin A. | PMC10200953 | fpls-14-1168985-g001.jpg |
0.412562 | cc0bf69cbe534dc1ae02bd4468c2ece1 | Levels of starch, sucrose, fructose and glucose in embryo (Em) and endosperm (En) under different concentrations of UA treatments. Different letters indicate significant levels at p < 0.05. | PMC10200953 | fpls-14-1168985-g002.jpg |
0.409386 | f2b1c6ccafe64a78ae708b2869290aad | Expression and classification of DEGs. (A) Phenotypic contrast between UA200 and CK; (B) Volcano plot for the up- and down-regulated DEGs; (C) Cluster analysis of all DEGs; (D) The top 5 enriched COG function classification of DEGs based on consensus sequence; and (E) The top 20 enriched KEGG pathways of DEGs. CK, control check; COG, Clusters of Orthologous Groups; DEGs, differentially expressed genes; KEGG, Kyoto Encyclopedia of Genes and Genomes; UA, ustiloxin A. | PMC10200953 | fpls-14-1168985-g003.jpg |
0.409836 | 439243c4a9f4438791a4c916c45a43b9 | Analyses of principal component (A) and cluster heatmap (B) for metabolisms of both endosperm (En) and embryo (Em) detected in positive (POS) and negative (NEG) modes, respectively. | PMC10200953 | fpls-14-1168985-g004.jpg |
0.42761 | 0e53f99d24cb425eb6ee016d80225832 | Identification of DEMs in CK_Em vs UA_Em and CK_En vs UA_En. (A) Venn analysis of DEMs that up- and/or down-regulated in Em, En and both. (B) KEGG annotation of DEMs in Em and En. Abbreviation: DEMs, differential expressed metabolites; Em, embryo; En, endosperm; KEGG, Kyoto Encyclopedia of Genes and Genomes. | PMC10200953 | fpls-14-1168985-g005.jpg |
0.444105 | 0b8970563ff940509fcae5e7f85e2729 | Changes of genes expression related to sugar and amino acid transport between control and UA200. The red and blue represent induced or suppressed, respectively. The *, ** and *** indicate for significant levels at p < 0.05, 0.01 and 0.001, respectively. SWEET, sugars will be eventually exported transporter; MST, monosaccharide transporter; INV, invertase; CIN, cell-wall invertase; VIN, vacuolar acid invertase; SUT, sucrose transporter; CAT, cationic amino acid transporter; ATL, amino acid transporter-like; BAT, bi-directional amino acid transporter; ANT, aromatic and neutral amino acid transporter; LHT, lysine and histidine transporter. | PMC10200953 | fpls-14-1168985-g006.jpg |
0.411641 | 26325c72f5064e2f8636b9fb7ddcc6b8 | Expression patterns of differentially regulated genes of enzymes involved in glycolysis and pentose phosphate pathways under normal and UA treated conditions. The blue means down-regulated, red means up-regulated, and yellow means up- & down- regulated in (A) the pathway; and (B) the details of expression for the up- and/or down-regulated genes were shown. HXK, hexokinase; G6P(1)-E, glucose-6-phosphate 1-epimerase; PGI, phosphoglucose isomerase; FBP, fructose-1,6-bisphosphatase I; PFK, 6-phosphofructokinase 1; PFP, diphosphate-dependent phosphofructokinase; ALD0, fructose-bisphosphate aldolase, class I; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; PGK, phosphoglycerate kinase; gpmB, 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; ENO, enolase; PYK, pyruvate kinase; G6PD, glucose-6-phosphate 1-dehydrogenase; PGLS, 6-phosphogluconolactonase; PGD, 6-phosphogluconate dehydrogenase; TKT, transketolase; rpiA, ribose 5-phosphate isomerase A; TAL, transaldolase; SeBP, sedoheptulose-bisphosphatase; RPE, ribulose-phosphate 3-epimerase; FPKM, fragments per kilobase of transcript per million reads; FC, fold change. | PMC10200953 | fpls-14-1168985-g007.jpg |
0.443609 | 1a76e70547044dcd90164808d95bd566 | Changes of metabolites and related genes expression of galactose and trehalose pathway. (A) Normalized expression abundance of detected metabolites related to galactose metabolism in En and Em. (B) The pathway of raffinose metabolism; (C) The pathway of trehalose metabolism; (D) Changes in gene expression of enzymes related to raffinose and trehalose metabolic pathways after UA treatment compared with the control. The *, ** and *** indicate for significant levels at p < 0.05, 0.01 and 0.001, respectively. Abbreviation: galE, UDP-glucose 4-epimerase; ino(1)-mP, myo-inositol-1-monophosphatase; ino(1)-PS, myo-inositol-1-phosphate synthase; PGM, phosphoglucomutase; galU, UTP–glucose-1-phosphate uridylyltransferase; GOLS, inositol 3-alpha-galactosyltransferase; RFS, raffinose synthase; sacA, β-fructofuranosidase; galA, α-galactosidase; TPS, trehalose-6-phosphate synthase; TPP, trehalose-6-phosphate phosphatase. | PMC10200953 | fpls-14-1168985-g008.jpg |
0.382318 | 35ffde8735be4e7da419e950af940789 | Response of amino acid metabolism to UA treatment. (A) simplified representation of metabolism pathways of amino acid and correlated up-and down-stream changes. Genes in red, blue and yellow represent upregulated, downregulated, and both. Rectangle boxes filled with red, blue and white represent upregulated, downregulated and unchanged metabolites, respectively. (B) Normalized expression abundance of metabolites related to amino acid metabolism. *, ** and *** indicate for significant levels at p < 0.05, 0.01 and 0.001, respectively. amiE, amidase; Arg, arginine; Asn, asparagine; Asp, asparate; CA, citrate; CA4H, cinnamic acid 4-hydroxylase; CHI, chalcone isomerase; CHS, chalcone synthase; Cit, citrulline; Cys, cysteine; G6PD, glucose-6-phosphate 1-dehydrogenase; gld, β-glucosidase; Gln, glutamine; glnA, glutamine synthetase; Glu, glutamate; Gly, glycine; GOT2, aspartate aminotransferase; GSH, glutathione; GSSG, glutathione disulfide; Ile, isoleucine; Leu, leucine; MA, malate; MDH2, malate dehydrogenase; P4HA, prolyl 4-hydroxylase; PAL, phenylalanine ammonia-lyase; Pro, proline; SGXT, L-serine: glyoxylate aminotransferase; Thr, tryptophan; Tyr, tyrosine; YUCCA, indole-3-pyruvate monooxygenase. | PMC10200953 | fpls-14-1168985-g009.jpg |
0.416344 | ee97970ca71241af89afa681382b2faf | Gene expression and metabolic abundance of GA and ABA synthesis pathways. (A) DEGs in the pathway of GAs conversion. (B) Normalized metabolic abundances of GAs and ABA in endosperm and embryo. (C) DEGs in the ABA synthesis pathway. *, ** and *** indicate for significant levels at p < 0.05, 0.01 and 0.001, respectively. GA, gibberellic acid; GA20ox, gibberellin-44 dioxygenase; GA2ox, gibberellin 2beta-dioxygenase; ABA, abscisic acid; CrtZ, β-carotene 3-hydroxylase; VDE, violaxanthin de-epoxidase; AAO3, abscisic-aldehyde oxidase. | PMC10200953 | fpls-14-1168985-g010.jpg |
0.421218 | 2c4c89fdb86f4f73a53e22118f0d4d2a | KEGG enrichment of DEGs on ribosome protein synthesis related RNAs. | PMC10200953 | fpls-14-1168985-g011.jpg |
0.415821 | 0d9bb67237a14ac7affa990c5c102353 | Schematic representation of carbohydrate metabolism during (A) seed germination under ustiloxin A treatment and (B) grain filling hijacked by U. virens. The red and blue indicate for up- or down-regulated genes or metabolites. GA, gibberellic acid; ABA, abscisic acid; SWEET, sugars will be eventually exported transporter; SUT, sucrose transporter; SuSy, sucrose synthase; PGM, phosphoglucomutase; CIN, cell-wall invertase; ADPG, adenosine diphosphate glucose; AGPase, ADPG pyrophosphorylase; GBSS, granule bound starch synthase; SSS, soluble starch synthase. | PMC10200953 | fpls-14-1168985-g012.jpg |
0.410753 | d70fbffb3dc949a5b9bdd70a869ac623 | Data selection process. | PMC10201830 | gr1.jpg |
0.439251 | de80de005fc34997b90bfea4e30a89e0 | (A) Number of majorly cultivated food plants (species, subspecies, varieties, and races); (B) Νumber of native food plants (species, subspecies, varieties, and races) in the selected countries. | PMC10201830 | gr2.jpg |
0.444121 | 509d6b608fae4509a48a50dc07cc52fe | Flow diagram | PMC10202062 | 12903_2023_2908_Fig1_HTML.jpg |
0.469161 | 2ee5c8fd2e784694a75b09c5cb244741 | Study flow chart. | PMC10202921 | 41598_2023_35243_Fig1_HTML.jpg |
0.41655 | 61035177ba0245ff95f7079aa0992708 | Receiver-operating characteristic curve for the relationship between the serum high temperature requirement factor A4 (Htr A4) levels and the diagnosis of preeclampsia [area under curve (AUC) 0.886, p < 0.001, 95% confidence interval 0.830–0.942]. | PMC10202921 | 41598_2023_35243_Fig2_HTML.jpg |
0.430652 | 21b4631d1e004fc298572bd8fe88af52 | Integration of patient-specific organoids, such as intestinal organoids, into microphysiological systems (MPS) provides a powerful platform for early testing of new therapeutic compounds. Also, these in vitro platforms allow identification of pharmacokinetics parameters for the development of highly predictive pharmacokinetic models that improve the clinical translational of new drugs. The image depicts an example of iPSC derived intestinal organoids generated in Cristoforetti’s lab at University of Florida. Crypt-like domains (red arrow), lumen (blue star), and villus domain (green arrow). | PMC10203872 | fphar-14-1198598-g001.jpg |
0.434566 | 4a6c54d7d29844799dbec2e33045a5dd | A schematic of what a “registered multi-lab replication with adversaries” would involve | PMC10204291 | 12915_2023_1567_Fig1_HTML.jpg |
0.428943 | 041732f0e2f9451c900940c0db8b3d41 | The process of LC ink design and printing. (a) Synthesis of the photopolymerizable LCEs. (b) The schematic illustration of temperature-controlled DIW of the LC ink and UV curing of printed samples. | PMC10204425 | biomimetics-08-00196-g001.jpg |
0.389293 | 56e523928e4b43c2b7c83c101caee13d | (a) DSC thermograms of the prepared LC ink. (b) Logarithmic curve of LC ink viscosity versus shear rate. (c) Storage modulus G′ and loss modulus G″ as a function of shear stress. (d) POM images of the printed sample when the printing direction is 0° and 45° to the polarizer. | PMC10204425 | biomimetics-08-00196-g002.jpg |
0.46422 | c8d13e55e5e947fc906bdfce4d07286e | Deformation of LCE at different printing temperatures. (a) Optical images of samples printed under different temperatures (70, 80 and 90 °C) at room temperature and heated to 80 °C. P-70 °C, P-80 °C and P-90 °C represent the printing temperatures selected for the samples, respectively. (b) The relationship between shrinkage strain and printing temperature under different printing speeds. (c) The relationship between the length of axial shrinkage and the number of cycles under different printing temperatures. | PMC10204425 | biomimetics-08-00196-g003.jpg |
0.457819 | fe778432965e415f84216aa1083e9563 | Deformation of LCE at different printing speeds. (a) Optical images of reversible shape change of samples printed at 90 °C with different speeds, under room temperature and 80 °C. (b) The relationship between shrinkage strain and printing speed under different temperatures. (c) The relationship between the length of axial shrinkage and the number of cycles under different printing speeds. | PMC10204425 | biomimetics-08-00196-g004.jpg |
0.430561 | 031ae05ee5fa400b8a7f58cb1f81d678 | Example of 3D printing double-layer LCE film with a printing angle of 0° for one layer and 90° for the other. (a) Schematic of the printing path of two-layer and the printed film at room temperature. (b,c) Optical images of the printed sample after shape changing when the printing angle of the contact layer with the heating platform is 90° and 0°, respectively, and schematic diagrams of their morphology after changing shape. | PMC10204425 | biomimetics-08-00196-g005.jpg |
0.471386 | 0786b63c4f3040b1995710b4c23843d7 | (a,b) Printing path (a), printed structure and the morphed shape after heating (b) of a double-layer rectangular LCE film with the upper and lower layers of ±45° relative to the long axis. (c,d) Schematic with ring filling for printing path (c). Printed three-layer disc structure and the deformed morphology after heating (d). | PMC10204425 | biomimetics-08-00196-g006.jpg |
0.421361 | e182fa1b92704d58be3604e491fd19b5 | The effect of actuation temperature on the strain in length and width direction. | PMC10204425 | biomimetics-08-00196-g007.jpg |
0.479821 | c3cb9251d49941a78c9a2ea50f39b787 | Shape-changing patterns of different LCE double-layer cross structures. (a,b) Two deformation modes for the same structure by replacing the printing sequence of the two layers. (c,d) The deformation mode of cross structure with upper and lower layer printing angles of 0° and 90°, respectively. (e,f) The deformation mode of cross structure with upper and lower layer printing angles of ±45°, respectively. | PMC10204425 | biomimetics-08-00196-g008.jpg |
0.444953 | 69735a94302e4c889a868da29ef0b461 | Application demonstrations of the printed LCE structures. (a,b) Three-dimensional printing of LCE planar porous mesh structure (a) Printing path. (b) Shape transition between printed structure at room temperature and at 80 °C. (c,d) Actuated lifting test of multi-layer LCE strip film. (c) Lifting an object weighing 2.5 g. (d) Lifting an object weighing 9.2 g. | PMC10204425 | biomimetics-08-00196-g009.jpg |
0.375181 | d4b3fe6db47e4be1a0e33bbe35d84ed1 | Kaplan-Meier survival estimates of patients discharged after hospitalization for COVID-19. High-sensitivity troponin I elevation on admission was associated with decreased long-term survival. hs-TnI: high-sensitivity troponin I. | PMC10204838 | 1806-9282-ramb-69-05-e20230116-gf01.jpg |
0.436284 | 398dbd06694c467d90b9c9c7d6602ec5 |
(A) Synthesis of GO; (B) synthesis of (2 and 4 wt%) GO/PVP-doped MoO3 NSs. | PMC10205020 | fchem-11-1191849-g001.jpg |
0.477636 | e1acab1581aa4d699a799e9b2aed7cf8 |
(A) XRD patterns; (B,C) SAED pattern of (2 and 4 wt%) GO/PVP-doped MoO3. | PMC10205020 | fchem-11-1191849-g002.jpg |
0.407571 | c590ca6a2c5743bf8b8f3f2b16f8af17 |
(A) UV–Vis spectra, (B) PL-spectra, and (C) FTIR spectra of (2 and 4%) GO/PVP-doped MoO3. | PMC10205020 | fchem-11-1191849-g003.jpg |
0.444277 | 443f60f5f2c048dfafe7c3a84075c223 |
(A–E) TEM images of (A) MoO3, (B) PVP–MoO3, (C) GO, (D) 2% GO/PVP–MoO3, and (E) 4% GO/PVP–MoO3. | PMC10205020 | fchem-11-1191849-g004.jpg |
0.461898 | 865a67a5935140979324cb29c81ff910 | Catalytic activity of (2 and 4 wt%) of GO- and PVP-doped MoO3 in (A) acidic, (B) basic, and (C) neutral media. | PMC10205020 | fchem-11-1191849-g005.jpg |
0.440988 | 73fc999a01314838809ffb6b41f9d84b | Stability of (2 and 4 wt%) GO/PVP-doped MoO3 in an acidic medium. | PMC10205020 | fchem-11-1191849-g006.jpg |
0.491528 | 55b2829a696d4730a4c2ade47688fb4a | 3D view of a binding pocket (A) and the binding interaction pattern of PVP/MoO3
(B) and GO/PVP/MoO3
(C) inside the binding site of FabI. | PMC10205020 | fchem-11-1191849-g007.jpg |
0.437479 | 2f8073f2df194bb8b2c4fd56037670f8 | 3D view of a binding pocket (A) and the binding interaction pattern of PVP/MoO3
(B) and GO/PVP/MoO3
(C) inside the binding site of FabI. | PMC10205020 | fchem-11-1191849-g008.jpg |
0.484021 | 6ec955e2813745588a31cdc0af4a8ba1 | Platelet activation and disturbances due to ESKD and dialysis. ADP, adenosine diphosphate; ATP, adenosine triphosphate; ESKD, end-stage kidney disease; NO, nitric oxide; PAR, protease-activated receptor; TXA2, thromboxane 2; VWF, von Willebrand factor. | PMC10205120 | tpa-107-1248-g001.jpg |
0.457338 | 518e9076705941f0bdd8781194c74b1d | The process of clot formation and the coagulation cascade with sites of inhibition of antiplatelet and anticoagulant drugs. LMWH, low-molecular weight heparin; NO, nitric oxide; PL, phospholipids; TF, tissue factor; tPA, tissue plasminogen activator; VWF, von Willebrand factor. | PMC10205120 | tpa-107-1248-g002.jpg |
0.403199 | cb527110c76449649e827d90ce2cdd64 | Flow diagram showing cohort creation and exclusions. | PMC10205905 | 195e699f1.jpg |
0.506873 | 580e7d0ec34045f4b68b9a35f1ef2e87 | Quarterly time series showing observed and predicted rates of acute care for cannabis use during pregnancy per (A) 100 000 overall pregnancies, (B) per 100 pregnancies with acute care for a mental health disorder and (C) per 100 pregnancies with acute care for substance use. The dashed line divides the before and after legalization periods. Note: CI = confidence interval. | PMC10205905 | 195e699f2.jpg |
0.472475 | 7900f3e6e0d949699bbd8bcae9975426 | Workflow for the PFFP methodology. | PMC10206034 | fnana-17-1154568-g001.jpg |
0.429041 | 9eda623f848545db8088fdc0e0f41fdf | Set up for deparaffinization and hydration of brain paraffin embedded brain tissues for the PFFP protocol. (A) Tissue sections are placed in vials or in the metal pan and are incubated for a minimum of 10 min in CitriSolv, graded alcohols (100, 95, and 70%) and PBS to achieve hydration. Sections can be transferred to cell culture plates, or a perforated tube [(B), see below], for further processing for histology or immunohistochemistry. (B) Illustrates a streamlined protocol for processing tissues in xylene/CitriSolv–resistant Falcon tubes. The inset shows perforation of a Falcon tube that can be sequentially processed through graded ethanols, PBS hydration. The perforated tubes can also be used for minimal amounts of antibody incubation for immunohistochemistry. (C) Left to right: stereo-microscope images of a coronal section of cerebellum (floating in CitriSolv solution) and striatum (fully hydrated in PBS solution, multi-well plate) of the mouse brain, which demonstrates great morphological preservation using the PFFP method. Morphological integrity of cerebellar tissue is exemplified with the PFFP method through Cresyl violet (Nissl) staining. Bar 100, 200, 100 μm. | PMC10206034 | fnana-17-1154568-g002.jpg |
0.417163 | 2d33e40386eb4e859e5ee8fa7b291cd7 | Immunofluorescence detection of olfactory bulb antigens with the PFFP method (processed in glass vials, see Figures 1, 2A). Deparaffinized coronal sections were processed with overnight incubation with polyclonal antibodies followed by species-specific fluorescent-labeled secondary antibodies. [(A), left to right], coronal section of mouse olfactory bulb (5 micron thickness) localized olfactory marker protein (OMP) in axons of the olfactory nerve layer (ONL) that extend to glomerular layers (GLM) of the main olfactory bulb. Staining of glial fibrillary acidic protein (GFAP) identified characteristic astrocytes interspersed at glomeruli and the mitral cell layer (MCL) of the bulb (8 micron thickness). Similarly, tyrosine hydroxylase expression was identified in juxtaglomerular interneurons of the GLM (8 micron thickness). [(B), left to right], cell type-specific expression of OMP was localized to primary olfactory neurons (ORN) in the olfactory nasal cavity (8 micron thickness), where nerve bundles (NB) coalesced in subepithelial regions. GFAP expression revealed stellate radial astrocytes with long projections throughout the inner, granule cell layer (GCL) of the bulb (8 micron thickness). Robust TH expression localized to neurons of the arcuate nucleus near the hypothalamus (10 micron thickness). Scale bars (left to right): (A) = 100 μm, (B) = 40, 100, 100 μm. | PMC10206034 | fnana-17-1154568-g003.jpg |
0.392102 | 10668e7d1b4243469bec943370de7365 | Dual immunohistochemical labeling for antigens in mouse olfactory bulb tissue using the PFFP method with perforated tubes (see Figure 2B). Deparaffinized coronal sections (5 micron thickness) with a 24 h incubation period with polyclonal antibodies followed by species-specific fluorescent-labeled secondary antibodies, demonstrating single, and or dual labeling of glial fibrillary acidic protein (GFAP) and olfactory marker protein (OMP) expression in astrocytes and neurons of the olfactory nerve layer (ONL) and glomerulus layer (GLM), respectively, and GFAP specificity to deeper layers of the olfactory bulb. The third panel illustrates a merge of the dual labeling for GFAP and OMP. Bar = 100 μm. | PMC10206034 | fnana-17-1154568-g004.jpg |
0.436483 | 35914ea6be50423db06d9d1e251ac1b1 | Deparaffinized coronal sections (8 μm thickness) of midbrain tissues show compatibility for immunofluorescent and chromogenic detection of antigens using the PFFP method. [(A), left to right], coronal sections identified nestin-expressing cells within the subgranular zone (SGZ) of the hippocampus. PFFP method afforded staining with DAPI and TH localization in the striatum (STR). Section thickness in (A) 10 microns. [(B), left to right], tyrosine hydroxylase (TH) and GFAP localization using peroxidase-labeled secondary antibodies and chromogenic (3, 3′-diaminobenzidine) development. Robust TH expression in the striatum correlated with similar pattern of localized expression using fluorescent detection in (A). Arrows identify GFAP labeling of radial astrocytes bordering the lateral ventricle (LV) and tanycytes lining the third ventricle (3V). Section thickness in (B) 10 microns. Scale bars (left to right): (A) = 100 μm, 1, 1, 1 mm; (B) = 1 mm, 300, 300 μm. Coronal sections of tissues processed using multiwell plates (see Figures 1, 2A). | PMC10206034 | fnana-17-1154568-g005.jpg |
0.486597 | 21b95cf80ac4481da0bfba8a4041ce25 | Flowchart showing selection of studies. | PMC10206123 | fcvm-10-1173945-g001.jpg |
0.457817 | 0176cb4e6c7a4910b1edf58eb2f12d4e | An Egger’s funnel plot indicated low level of heterogeneity for evaluating four outcomes: false lumen patency (A), aortic-related death (B), perioperative stroke (C) and reintervention (D) | PMC10206123 | fcvm-10-1173945-g002.jpg |
0.44444 | 7a3ebb0eb3a5444bbce343b0e6cb9967 | Forest plot showing the HR and 95% CI of false lumen patency for studies comparing the anticoagulation and non- anticoagulation after surgery. HR, hazard ratio; CI, confidence interval. | PMC10206123 | fcvm-10-1173945-g003.jpg |
0.461245 | 5b05a4f6271f4349b241d47c219d761c | Forest plot showing the HR and 95% CI of aortic-related death (A), perioperative stroke (B) and reintervention (C) for studies comparing the oral anticoagulation and non-oral anticoagulation after surgery. HR, hazard ratio; CI, confidence interval. | PMC10206123 | fcvm-10-1173945-g004.jpg |
0.444376 | 4f447cee71fa4ff8b7342b027a17dc7e | RIPostC significantly reduced cardiac injury in rat myocardial IR model. (A) The protocol of experimental design. (B,C) Evans blue and TTC staining. Representative five heart slices stained by Evans blue and TTC in two groups. IS, infarct size; AAR, the ischemic area at risk; LV, left ventricle. (D) The level of plasma TnI. *Represents P < 0.05, n = 6 for each group. | PMC10206167 | fcvm-10-1089151-g001.jpg |
0.423376 | 10b5d7366dc6429ba1d8eb8c319064ae | RIPostC significantly reduced the apoptosis of heart. (A) Representative myocardial apoptosis detected by TUNEL assay. (B) The percentage of TUNEL-positive cells in the total cells. Scale bar: 100 µm. *Represents P < 0.05, n = 6 for each group. (C) Detection of caspase-3 levels in heart after RIPostC using western blotting. | PMC10206167 | fcvm-10-1089151-g002.jpg |
0.703503 | 8cebe3dc04784ae5a37f1d7fa62f8693 | The comparison of the levels of cardiac inflammatory factors between the Con and the RIPostC group. (A–D) The comparison of cardiac IL-1β, IL-6, IL-10 and TNFα levels respectively in the RIPostC and the Con group. *Represents P < 0.05, n = 6 for each group. | PMC10206167 | fcvm-10-1089151-g003.jpg |
0.402365 | 72b66f5a26314a72a4bdf6f83a55c33f | Expression differences between the Con and the RIPostC group. (A) Shared and unique expressed genes displayed by Venn analysis. (B) Differences of expression pattern exhibited by PCA analysis. | PMC10206167 | fcvm-10-1089151-g004.jpg |
0.451728 | f85495b250f34465ac267fbcfe3defa4 | DEGs identification and analysis. (A) Red and green dots represented up and down regulated genes by Volcano map. (B) The expression levels of DEGs and similarity between samples as well as DEGs showed by heatmap. | PMC10206167 | fcvm-10-1089151-g005.jpg |
0.458979 | ccc9111d12ce416a9a48a97d97e44a96 | Go and KEGG annotation analysis of DEGs. (A) Annotated GO terms of DEGs. (B) Annotated KEGG pathways of DEGs. | PMC10206167 | fcvm-10-1089151-g006.jpg |
0.51009 | 75252994bc054bf2b04f7ab53ed68d62 | Expression levels of DEGs validated by qRT-PCR. (A–D) The relative mRNA expression comparisons of Caspase-6, Prodh1, Claudin-5 and ADAMTS15 respectively in the RIPostC and the Con group. *Represents P < 0.05, n = 6 for each group. | PMC10206167 | fcvm-10-1089151-g007.jpg |
0.458524 | ae4a312363724c8a81611fd1a5ca2dcd | The correlation between the relative expression of ADAMTS15 and the levels of cardiac inflammatory factors. (A–D) The correlation between the relative mRNA expression of ADAMTS15 and the levels of cardiac IL-1β, IL-6, IL-10 and TNFα respectively in the RIPostC and the Con group. *Represents P < 0.05, n = 6 for each group. | PMC10206167 | fcvm-10-1089151-g008.jpg |
0.405872 | 80d0442020a54310b397aa1af7b7ba18 | Enzyme-catalyzed cobalt insertion reactions for the biosynthesis
of vitamin B12. (a) The two biosynthetic pathways for vitamin
B12 involve early- and late-stage insertion of the catalytic
cobalt ion, respectively.2,7 CoII insertion
into the porphyrin substrate sirohydrochlorin (SHC) to form cobalt-sirohydrochlorin
(CoII-SHC) is catalyzed by the cobaltochelatase CbiK.17 CoII insertion into the ring-contracted
substrate hydrogenobyrinic acid a,c-diamide (HBAD) to form cobyrinic acid a,c-diamide (CBAD) is catalyzed by the cobaltochelatase CobNST,
which requires energy input from ATP hydrolysis and an additional
metallochaperone (CobW) for CoII supply in vivo.(4,9) (b) Absorbance spectra of isolated substrates and
SDS-PAGE analyses of isolated enzymes (full-length gel images shown
in Figure S1). | PMC10206600 | au3c00119_0002.jpg |
0.497669 | 4016444bb6ac49219c4184d32587687f | Buffered metal concentration-dependent
rate of conversion of HBAD
to CBAD by CobNST via steady-state kinetics. (a) UV–visible
absorbance of HBAD (11.6 μM) before (black line) and 3.5 h after
(red line) incubation with CoII (100 μM) and CobNST
(3 μM of each subunit) in the presence of MgCl2 (10
mM) and ATP (5 mM). The inset shows absorbance at 330 nm over time,
following the addition of cobalt. (b) Initial formation of CBAD when
HBAD (10 μM) was incubated with CoII (100 μM),
MgII (10 mM), and ATP (5 mM) in the presence (filled circles)
or absence (open circles) of CobNST (3 μM of each subunit).
(c) CobNST-catalyzed metalation of HBAD (initial concentration 10
μM) when available [CoaqII] was buffered
to different availabilities using l-histidine to achieve
sub-micromolar concentrations (Table S1). Initial rates (v0) were calculated from linear fits
of the data for the first 6 min of reaction at each condition (shown
by dashed lines). (d) Steady-state kinetics for CoII insertion
into HBAD by CobNST. Initial rates of metalation (v0) relative
to enzyme concentration ([E]tot = 0.5μM) were determined
at varying available [CoII] (see Table S1 for experimental conditions). Data are the mean ± s.d.
of three independent experiments. All reactions were carried out in
50 mM Hepes buffer pH 7.0, 100 mM NaCl. | PMC10206600 | au3c00119_0003.jpg |
0.503551 | 5b631e53215542698fdfdc30127ba46d | CobW enhances
corrin biosynthesis in vivo, but
MgIIGTP-CobW quenches the formation of CBAD by CobNST in vitro. (a) Corrin production by engineered E. coli* strains with and without cobW following 4 h exposure to 300 μM CoCl2. Data are
the mean ± s.d. of three biologically independent replicates.
Triangle shapes represent individual experiments. (b) All data refer
to E. coli* cells grown in LB media
with 1–300 μM CoCl2 supplementation. CobW-dependent
corrin synthesis was determined from the difference in measured corrin
production for +cobW versus −cobWE.coli* strains as a proportion of
total corrin produced by the +cobW strain (panel
(a) and ref (4)). CobNST
metalation was estimated using Km for
CoII and measured intracellular CoII availabilities
in E. coli* at each growth condition
(Figure 2d, Table S2 and ref (4)). (c) CobNST-catalyzed formation of CBAD when
CoII (100 μM) was supplied in the presence of a metal
buffering ligand (6 mM L-His; [CoaqII] = 40
nM) without CobW (dashed line), with 3 or 30 μM CobW (open circles,
indistinguishable) or with 100 μM CobW (closed circles). The
solid line shows control experiment when CoII was supplied
in the absence of a buffering ligand. (d) Initial absorbance spectra
of reactions from (c) without CobW (black trace) or with 100 μM
CobW (red trace). Difference spectra (inset) matches the known absorbance
spectrum of CoIIMgIIGTP-CobW with a concentration
of 81 μM inferred from signal intensity at 339 nm.4 All reactions were performed in 50 mM Hepes pH
7.0, 100 mM NaCl with MgII (10 mM), ATP (5 mM), GTP (1
mM), and CobNST (3 μM of each subunit). | PMC10206600 | au3c00119_0004.jpg |
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