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0.469709 | d4ab4ff255ee472e97062a5527cdf00e | (a) General concept of nanosensors for in vivo creatinine level detection through body fluids such as urea and sweat. (b) Working mechanism of triboelectric nanogenerator-based nanosensors [71]. 2021 Elsevier. (c) Cellulose-based conductive hydrogel for self-powered sweat sensing [72]. 2022 John Wiley and Sons. | PMC10295964 | biosensors-13-00604-g005.jpg |
0.432193 | f0c44cfef84f424c8cd20d8bd639f31b | (a) Fabrication process of cellulose/BT aerogel paper [73]. 2020 John Wiley and Sons. (b) Structural design of wearable TENG and SEM image of PA6 and PVDF nanofiber membrane [74]. 2019 Elsevier. (c) Schematic illustration of PPy−PVDF TENG fabrication process: 3D PPyNAs deposited on carbon paper via electrochemical deposition and combined with porous PVDF film [75]. 2022 ACS. (d) Walking with a sudden tumble [76]. 2023 Elsevier. | PMC10295964 | biosensors-13-00604-g006.jpg |
0.402808 | 5264fac13ce6405cad27b68260196507 | (a) Schematic diagram of micro-crack-assisted wrinkled PEDOT:PSS dual-sensor fabrication process [96]. 2022 John Wiley and Sons. (b) Schematic illustration of MGP CHs synthetic procedures [97]. 2020 Elsevier. (c) Photograph of CNH−3 at 24 °C [58]. 2021 Elsevier. (d) Schematic of MAGP hydrogels preparation process [98]. 2022 ACS. | PMC10295964 | biosensors-13-00604-g007.jpg |
0.409642 | 0d6ff6ac31364e7bbe624518957d63b0 | (a) PANI deposition process on WCT surface [99]. 2019 Elsevier. (b) Polypyrrole-coated cotton textile [100]. 2019 ACS. | PMC10295964 | biosensors-13-00604-g008.jpg |
0.490593 | 744207fd55a84a4e90e5e6a364688769 | P—Protuberance, A—point of junction, A1—artery 1, A2—artery 2. | PMC10296087 | brainsci-13-00966-g001.jpg |
0.467208 | c59ada68661b4ec8be269ebb47e02c35 | P—Concavity, A—point of junction, A1—artery 1, A2—artery 2. | PMC10296087 | brainsci-13-00966-g002.jpg |
0.502745 | 1aa20f733f4d45b3b92e08ccb102cbed | Coanda Effect Inside the Main Aneurysmal Areas of the Willis Polygon. | PMC10296087 | brainsci-13-00966-g003.jpg |
0.416938 | e77c5a0417a0455ebfc9162e6f8da086 | Involvement of cannabinoid signaling cascades in regulation of physiological mechanisms. Legend: cAMP: cyclic adenosine monophosphate; MAPK; Mitogen-activated protein kinase; MEK: Mitogen-activated protein kinase kinase; ERK: Extracellular signal-regulated. | PMC10296259 | biomedicines-11-01667-g001.jpg |
0.460994 | 73449e9c5686427cba778985c16ab85b | Involvement of CB1Rs in the complications of diabetes mellitus. Legend: R: receptor; T1DM: Type 1 diabetes mellitus; DM: Diabetes mellitus; DN: Diabetic nephropathy; STZ: streptozotocin; TNF-α: tumor necrosis factor-α. | PMC10296259 | biomedicines-11-01667-g002.jpg |
0.476979 | d542eaecf1e04a16a7a48ed0387b2c48 | (a) Blood is the most commonly used body fluid for liquid biopsies. The most studied liquid biopsy biomarkers are depicted, namely circulating tumor cells (CTCs), circulating tumor DNA (ctDNA), cell-free RNA (cfRNA), extracellular vesicles (EVs) and tumor-educated platelets (TEPs). Cell-free DNA (cfDNA) is also shown. (b) ctDNA carries the same genomic (point mutations, insertions/deletions, translocations, copy number variations) and epigenomic (DNA methylation) alterations as the tissue tumor DNA. This image was created with the use of BioRender (https://biorender.com/) (accessed on 20 April 2023). | PMC10296563 | cells-12-01573-g001.jpg |
0.471058 | 858b624b65a2493fa1de02223f796117 | Highly sensitive molecular techniques for ctDNA detection and characterization. Droplet digital PCR (ddPCR) is based on the partitioning of the sample into millions of water-in-oil droplets, so that each droplet contains a single DNA molecule that is amplified individually. BEAMing stands for beads, emulsion, amplification, and magnetics and is a type of dPCR, where amplified wild-type and mutant alleles are differentially labeled and are separated through flow cytometry. Next-generation sequencing (NGS) approaches that employ massive parallel sequencing with improved technical and bioinformatics protocols to reduce errors have gained ground in ctDNA analysis. This image was created with the use of BioRender (https://biorender.com/) (accessed on 20 April 2023). | PMC10296563 | cells-12-01573-g002.jpg |
0.444703 | e8a751daeb49440faedeee9c26b10476 | Analysis of ctDNA at various time points can contribute to the clinical management of early-stage breast cancer (BC). Early diagnosis by ctDNA detection could be followed by administration of neoadjuvant therapy (NAT), and ctDNA testing in post-surgical samples could help in the detection of minimal residual disease (MRD). Longitudinal ctDNA analysis in patients after NAT and/or adjuvant therapy (AT) could also be used in monitoring therapy response, early detection of resistance and prediction of metastatic relapse. This image was created with the use of BioRender (https://biorender.com/) (accessed on 22 April 2023). | PMC10296563 | cells-12-01573-g003.jpg |
0.478818 | e39cc8bb8d2d4d058f25ec4e93266a12 | Growth of SAS cells after BNCT or neutron irradiation alone. SAS cells were irradiated with neutrons (BPA−) or as BNCT (pretreatment with BPA at 25 ppm [10B]). The cell growth ratio after 8 days culture was analyzed as shown in Table 1. | PMC10296566 | cells-12-01562-g001.jpg |
0.460669 | 0100a3782e9643b7b7e76a68aed27054 | Hierarchical Clustering and PCA of proteomic profiles of EVs derived from SAS cells treated or not with BPA and with different times and doses of neutron irradiation. In Panel (a), the dendrogram was obtained by computing the peptide spectrum matches (PSMs) of statistically significant proteins selected by Linear Discriminant Analysis (LDA); Euclidean’s distance metric and Ward ’s methods were applied. In purple are highlighted BPA− samples, while in green are highlighted BPA+ samples. In Panel (b), the Principal Component Analysis was performed on the average proteomic profiles for each examined condition. Categories were reported in different colors and shapes according to the represented conditions. | PMC10296566 | cells-12-01562-g002.jpg |
0.385764 | 44497dd5e8624c32aff852bb419d1316 | Functional enrichment analysis for BPA+ and BPA− conditions. GO enrichment was performed with DAVID database, and the resulting list of GO terms, filtered for p-value confidence and gene count, was plotted with ImageGP. GO enrichment was performed for biological process (panel (a)) and cellular component (panel (b)). In plots, the size of circles represents the number of genes associated with a GO term, while the color scale represents the negative Log of p-value as the confidence for the association. | PMC10296566 | cells-12-01562-g003.jpg |
0.539248 | 268f22228d724de7bdb4609be4f216fe | Differentially expressed proteins extracted through label-free quantification with MAProMa tool comparing BPA− and BPA+ conditions with different times and doses of neutron irradiation. Panel (a) shows the comparisons without irradiation (0 min, 0 Gy); Panel (b) shows the comparisons with low irradiation (10 min, 1.9 Gy), and panel (c) shows the comparisons with high irradiation (60 min, 11.3 Gy). In each plot, comparisons at 6 h (darker bars) and 24 h (lighter bars) are reported. Blue bars and negative DAve values refer to upregulated proteins in BPA− conditions, while red bars and positive DAve values refer to upregulated proteins in BPA+ conditions. For each protein, gene name and the related DAve value (ratio of protein expression) are reported. Only proteins with DAve values greater than 0.2 or lower than −0.2 had to be considered DEPs. | PMC10296566 | cells-12-01562-g004.jpg |
0.534381 | 88792c424ce34bb299f60ba5ca659f6a | Differentially expressed proteins extracted through label-free quantification with MAProMa tool, comparing conditions of 0 Gy with 11.3 Gy (panel (a)) and 1.9 Gy with 11.3 Gy (Panel (b)), within BPA+ group. In each plot, comparisons at 6 h (darker bars) and 24 h (lighter bars) are reported. Blue bars and negative DAve values refer to upregulated proteins in conditions with no or low irradiation dose (Panel (a,b), respectively), while red bars and positive DAve values refer to upregulated proteins in high irradiation dose (11.3 Gy). For each protein, gene name and the related DAve value (ratio of protein expression) are reported. Only proteins with DAve values greater than 0.2 or lower than −0.2 had to be considered DEPs. | PMC10296566 | cells-12-01562-g005.jpg |
0.479807 | 6f811c45685d42549055c859933a9ff6 | Levels of DEPs through the examined conditions. In each plot, Y-axis represents the average peptide spectrum match (aPSM) of the protein in the different conditions. BPA− and BPA+ conditions are highlighted in different colors (purple for BPA− and green for BPA+). Error bars represent standard deviation. | PMC10296566 | cells-12-01562-g006.jpg |
0.427162 | f2bf2f20518c4ee9b24c80e4b63ce5c7 | Network analysis. Protein–protein interaction (PPI) network of the proteins obtained combining LDA and MAProMa results. Physical or/and functional interactions are highlighted by thicker edges and considering experimental (STRING score > 0.15) and database (STRING score > 0.35) annotated interactions. The networks were visualized by Cytoscape v.3.9.1 software, while biological processes were retrieved by STRING enrichment. The color code of distinct nodes reflects their sources: orange bound nodes represent proteins extracted from LDA (statistically significant), green nodes represent DEPs and blue nodes represent proteins from LDA that are not DEPs. | PMC10296566 | cells-12-01562-g007.jpg |
0.425578 | 5f2d68e563cd45a2b2388ab7b5605a7b | The PRISMA flow diagram. | PMC10297663 | children-10-00927-g001.jpg |
0.451334 | 2a2f1978cc36418dadc09397a048b076 | Forest plot of the in-brace correction angle in studies comparing “manually manufactured braces” and “CAD/CAM-manufactured braces” (Cottalorda et al. [31] and Wong et al. [30]). | PMC10297663 | children-10-00927-g002.jpg |
0.459207 | 0b5c8274b7c9444785bbd1315ae545e5 | Forest plot of the thoracic curve group in-brace correction angle in studies comparing “manually manufactured braces” and “CAD/CAM integrating with biomechanical simulation manufactured braces” (Labelle et al. [23] and Blais et al. [22]). | PMC10297663 | children-10-00927-g003.jpg |
0.437765 | 1cf5c4aa9fa14c6ba49d17d71e7d6eca | Forest plot of the thoracolumbar/lumbar curve group in-brace correction angle in studies comparing “manually manufactured braces” and “CAD/CAM integrating with biomechanical simulation manufactured braces” (Labelle et al. [23] and Blais et al. [22]). | PMC10297663 | children-10-00927-g004.jpg |
0.400724 | 65fcbaf109294516ac156c175d473160 | Endoscopic, sonographic, radiologic, and histologic imaging of IPMN patients diagnosed with gastric cancer in their first EGD. (a) Case 1; (b) Case 2; (c) Case 3; (d) Case 4. | PMC10297689 | diagnostics-13-02127-g001a.jpg |
0.471111 | 2b3b8c0e5afb420b82bed5c32136a15b | Bilateral Spigelian hernia in a male patient (yellow dotted ovals). | PMC10299048 | jcm-12-03866-g001.jpg |
0.467134 | 18bc632f7b534853911f50f022e47dd0 | (A) Tentacle-shaped implant Freedom Octomesh VHR Type XS with a central oval body and 8 straps at the edge of the prosthesis. (B) The needle passer used for the delivery of straps from preperitoneal space across abdominal wall structures to subcutaneous layer. | PMC10299048 | jcm-12-03866-g002.jpg |
0.454667 | b3961ac5792346859de28f9367db8f15 | Right-sided partly obstructed Spigelian hernia protrusion emerges from the fascial defect in arcuate line. Stricture at the basis of the protrusion (yellow arrows) causes the obstruction of hernia content within the sac. | PMC10299048 | jcm-12-03866-g003.jpg |
0.479139 | b346f87c52eb4fafb32d3e5a06e3ded5 | (A) After opening the fascia, an obstructed Spigelian hernia with tightened basis is detected in the lateral margin of rectus abdominis muscle. A lipoma is also visible at the opposite margin. (B) After lateral dislodgement of hernia sac and displacing the rectus muscle medially, the thickened stricture of the sac constraining the hernia opening is clearly visible. | PMC10299048 | jcm-12-03866-g004.jpg |
0.418541 | 78de2038f9bc4360811e6007a1843a77 | (A) Protrusion is returned to abdominal cavity by means of forceps. Hernia defect is clearly detectable (yellow dotted oval). (B) Tentacle mesh is brought close to operation site prior to delivery. Note: wide surface of the implant that will be placed in preperitoneal sublay. | PMC10299048 | jcm-12-03866-g005.jpg |
0.468552 | b99e7cc06c374b6cb72be24df688b1e5 | (A) After blunt dissection of the preperitoneal space to achieve a wide space for mesh placement, the tip of the needle passer pierces fascia penetrating though the muscle layer to the preperitoneal space (yellow arrow). Maneuver is facilitated by introduction of forefinger tip in the preperitoneal interstitium between muscle and peritoneum. Fingertip guides the advancement of the needle outside the lateral margin of rectus muscle (blue arrow), avoiding a tear of the peritoneal sheath. (B) First strap of the tentacle mesh is inserted into the eye of the needle passer (red arrows) passing through the preperitoneal space, crossing muscular layer distant from the defect border. Yellow arrows indicate the overlap ensured by this procedural step. | PMC10299048 | jcm-12-03866-g006.jpg |
0.471427 | 64b417d3347e47a9b4fa312b3978d6c6 | All eight straps are delivered across the muscle layers. Body of the mesh lies in the preperitoneal space posteriorly of abdominal wall (yellow dotted oval). Pulling the straps high allows the mesh to be automatically deployed flat over the peritoneal sheath. | PMC10299048 | jcm-12-03866-g007.jpg |
0.462031 | 992a3b9f20f44dceb59b1190377e1d7d | After positioning the tentacle mesh preperitoneally, fascia is closed with continuous resorbable suture. Here, each strap (blue *) is cut short leaving a stump of ca. 2 cm in the subcutaneous space. Yellow oval indicates the surface of the preperitoneal space occupied by the tentacle mesh ensuring a wide overlap on the already sutured defect line (dotted blue line). | PMC10299048 | jcm-12-03866-g008.jpg |
0.419744 | 7b3fae359c7a4e7cb80a2dfc53c346ba | Postoperative pain intensity (visual analogue scale). | PMC10299048 | jcm-12-03866-g009.jpg |
0.428949 | 360d7ce41f9a4742ac9e884102ad3224 | Representative optical coherence tomographic (OCT) B-scan images of an eye with typical epiretinal membrane (ERM) (A), ERM foveoschisis (B), macular pseudohole (MPH, (C)), and lamellar macular hole (LMH, (D)). (E) Number and percentage of eyes of each subtype among 432 eyes with ERM-related diseases. | PMC10299286 | jcm-12-04009-g001.jpg |
0.423852 | 6f8c9b15b7544c3a90333c0343d3a144 | OCT B-scan images of eyes with an ERM foveoschisis. (A) Representative OCT B-scan images of ERM foveoschisis with presence of fibrous membrane on the retinal surface at the fovea (yellow asterisk). (B) Representative OCT B-scan images of ERM foveoschisis with absence of fibrous membrane at the fovea (yellow asterisk). (C,D) Two representative OCT B-scan images of ERM foveoschisis with vitreous adhesion to the macula. Yellow arrows indicate the posterior vitreous membrane with adhesion to the macula. | PMC10299286 | jcm-12-04009-g002.jpg |
0.431278 | b49e905b6343492dbf7281ea46bdfa99 | (A) Changes in the BCVA (logMAR units) before and three months after the surgery in the ERM foveoschisis group (n = 16, left panel) and the typical ERM group (n = 152, right panel). Baseline BCVA did not differ significantly between the two groups (p = 0.70). (B) Comparison of the degree of improvement in BCVA 3 months after the surgery between two groups. | PMC10299286 | jcm-12-04009-g003.jpg |
0.497771 | d6caf17f247a4c65bceeafcccfe45f64 | Central macular thickness (CMT) in the ERM foveoschisis and the typical ERM eyes. (A) Changes in the central macular thickness (CMT) before and three months after the surgery for the ERM foveoschisis group (n = 16, left panel) and the typical ERM group (n = 152, right panel). The baseline CMT was significantly thinner in the ERM foveoschisis group than in the typical ERM group (p < 0.01). (B) Comparison of the percentage reduction in the CMT three months after the surgery between two groups. | PMC10299286 | jcm-12-04009-g004.jpg |
0.410612 | 416623260b374585b46dbbd7aa54281c | Two representative horizontal scan OCT images before and three months after the vitrectomy for the ERM foveoschisis group and typical ERG group. The postoperative CMT reduction is more apparent in the typical ERG group. ERM foveoschisis group also showed thinner CMT postoperatively, but the reduction of CMT was less evident. In the ERM foveoschisis group, we also noticed that the space of retinoschisis became smaller three months after the surgery (yellow asteriks). | PMC10299286 | jcm-12-04009-g005.jpg |
0.433081 | 34447fb602c34e48ad8bf8d9c7d11e3c | CONSORT flow diagram for patient enrolment. PET = Positron Emission Tomography; CT = Computer Tomography. | PMC10299392 | jcm-12-03942-g001.jpg |
0.414432 | 015cd1ef01bc428a88a5671df96cbc0a | Representative example of multiparametric [18F]FDG PET-imaging of a patient (Study-ID 33) suffering from an adenocarcinoma of the lung (dotted arrow). A single liver metastasis was detected with PET and was histologically confirmed (solid arrow). Of note is the high DV-FDG of the liver metastasis compared to the lung tumor in combination with homogeneous imaging of the surrounding tumor-free liver parenchyma. DV-FDG = Distribution Volume of FDG; FDG = Fluorodeoxyglucose; Ki = Influx Rate Constant; PET = Positron Emission Tomography; SUV = Standardized Uptake Value. | PMC10299392 | jcm-12-03942-g002.jpg |
0.382194 | e89f3bcc90ff44e5a4c63fa13e627612 | Boxplots illustrating gender-specific SUVmean (A,B) Patlak Kimean (C,D) MR-FDGmean (E,F) and DV-FDGmean (G,H) measurements in the function of lung lesions (A,C,E,G) and lymph nodes (B,D,F,H). Asterisk (⋆) represents an extreme value. Circle (o) represents an outlier. DV-FDG = Distribution Volume of FDG; FDG = Fluorodeoxyglucose; Ki = Influx Rate Constant; MR = Metabolic Rate; PET = Positron Emission Tomography; SUV = Standardized Uptake Value. | PMC10299392 | jcm-12-03942-g003a.jpg |
0.442869 | bae19260ad01478882d5528c26cad5df | Scatterplots illustrating the correlation between SUVmean, MR-FDGmean, and DV-FDGmean of different types of lung lesions (A,C) and lymph nodes (B,D). Interestingly, DV-FDGmean (B) and MR-FDGmean (D) of the lymph nodes were proportionally half of the values of primary lesions (A,C), while the magnitude of SUVmean of lymph nodes and primary lesions was found similar. DV-FDG = Distribution Volume of FDG; FDG = Fluorodeoxyglucose; Ki = Influx Rate Constant; MR = Metabolic Rate; PET = Positron Emission Tomography; SUV = Standardized Uptake Value. | PMC10299392 | jcm-12-03942-g004.jpg |
0.385401 | 4401f721041e4f96828186adcafcf29a | Scatterplots illustrating the correlation between SUVmean and MR-FDGmean (A); and SUVmean and DV-FDGmean (B) measurements in the function of the type of distant metastases and primary tumor histology. Metastases of NSCLC are coded as small circle, SCLC as large circle. DV-FDG = Distribution Volume of FDG; FDG = Fluorodeoxyglucose; MR = Metabolic Rate; NSCLC = Non Small Cell Lung Cancer; SUV = Standardized Uptake Value; SCLC = Small Cell Lung Cancer. | PMC10299392 | jcm-12-03942-g005.jpg |
0.457388 | 8c3c4fd8cb8f4fafa556262c1e8e37f4 | ROC analyses of CT morphologic, static as well as parametric, PET data to differentiate between malignant and benign lung lesions. CT = Computer Tomography; DV-FDG = Distribution Volume of FDG; FDG = Fluorodeoxyglucose; Ki = Influx Rate Constant; MR = Metabolic Rate; NSCLC = Non Small Cell Lung Cancer; SUV = Standardized Uptake Value; SCLC = Small Cell Lung Cancer. | PMC10299392 | jcm-12-03942-g006.jpg |
0.442737 | 5b61b8254ce74c26adc06b5ccf15cf58 | ROC analyses of CT morphologic, static as well as parametric, PET data to differentiate between malignant and benign lymph nodes. CT = Computer Tomography; DV-FDG = Distribution Volume of FDG; FDG = Fluorodeoxyglucose; Ki = Influx Rate Constant; MR = Metabolic Rate; NSCLC = Non Small Cell Lung Cancer; SUV = Standardized Uptake Value; SCLC = Small Cell Lung Cancer. | PMC10299392 | jcm-12-03942-g007.jpg |
0.395304 | d06e5dd761a24174ac849a3f7e3b349c | The ECM-induced biomechanical force promoted breast tumor stemness. a Representative images and H&E staining images of MCF-7, 4T1 and MDA-MB-231 cells seeded in a flask system and different 3D gels (collagen, fibrinogen, and Matrigel) for 3 days. The scale bar was 50 μm. b, c MCF-7, 4T1 and MDA-MB-231 cells were cultured in a flask system or 3D gels (collagen, fibrinogen, and Matrigel) for 3 days. In vitro colony formation (b) and in vivo tumor formation assay (n = 10) (c) were performed. d Heatmap of stemness-associated genes (SOX2, c-Myc, Nanog, POU5F1, Notch3, Notch4, Tert, CD133, Wnt2, YAP1, AKT1, and ALDH1) expression in MCF-7 cells cultured in flask and different 3D gels (collagen, fibrinogen, and Matrigel) for 3 days, determined using qPCR. e MCF-7, 4T1 and MDA-MB-231 cells were cultured in a flask system or 3D gels (collagen, fibrinogen, and Matrigel) for 3 days. ALDH1+ cell subpopulations were determined by flow cytometry. f MCF-7 cells were seeded in different 3D gels (collagen, fibrinogen, and Matrigel) with different stiffness (0, 30, 45, 90, and 450 Pa) for 3 days. Following this, the in vitro colony formation assay was performed. Representative images of tumor cells during atomic force microscopy analysis are shown. g Viability of MCF-7 cells seeded in a flask or 3D Matrigel (90, 450, and 1050 Pa). Representative image and H&E staining of MCF-7 cells seeded in 3D Matrigel (1050 Pa, 3 days) are shown. The scale bar is 50 μm. Three independent experiments were performed. Data are represented as mean ± SEM. P < 0.05, statistical significance | PMC10300038 | 41392_2023_1453_Fig1_HTML.jpg |
0.389016 | 04277ddced8041aeb6ed1653154ad651 | ECM compounds bind to integrins to transduce biomechanical force signals. a Immunostaining of F-actin in the MCF-7, 4T1 and MDA-MB-231 cells cultured in a flask and 3D Matrigel for 3 days. The scale bar is 20 μm. b Heatmap of integrin β1 ~ 8 expression in MCF-7 cells cultured in a flask and different 3D gels (collagen, fibrinogen, and Matrigel) for 3 days. c Western blotting of integrin β1 and β3 in MCF-7, 4T1 and MDA-MB-231 cells cultured in a flask and different 3D gels (collagen, fibrinogen, and Matrigel) for 3 days. d, e in vitro colony formation (d) and in vivo tumor formation (n = 10) (e) assays for MCF-7/4T1/MDA-MB-231 cells seeded in different 3D gels (collagen, fibrinogen, and Matrigel) and treated with PBS and integrin β1- and β3-neutralizing antibodies, respectively. f Heatmap of stemness-associated gene (SOX2, c-Myc, Nanog, POU5F1, Notch3, Notch4, Tert, CD133, Wnt2, YAP1, AKT1, and ALDH1) expression in MCF-7 cells (3D Matrigel culture) treated with PBS and integrin β1- and β3-neutralizing antibodies. g ALDH1+ cell subpopulations were determined in MCF-7 cells (3D Matrigel culture) treated with PBS and integrin β1- and β3-neutralizing antibodies. Three independent experiments were performed. Data are represented as mean ± SEM. P < 0.05, statistical significance | PMC10300038 | 41392_2023_1453_Fig2_HTML.jpg |
0.443276 | 369b62a87b0744d69b922ed4e00ddfe6 | Integrin-cytoskeleton-AIRE signals are crucial for stemness gene upregulation. a Volcano plots showing the differentially expressed genes in 4T1 cells cultured in a flask and 3D Matrigel for 3 days. b Heatmap of top 15 upregulated genes in 3D Matrigel-cultured 4T1 cells in comparison with that of cells cultured in a flask. c Western blotting for AIRE in MCF-7, 4T1 and MDA-MB-231 cells cultured in a flask or 3D Matrigel (treated with PBS, integrin β1/3-neutralizing antibodies, or 5a-Pregnane-3,20-dione). d Western blotting for AIRE in MCF-7 cells cultured in a flask or 3D collagen/fibrinogen gels for 3 days. e AIRE expression at the mRNA level in 3D Matrigel-cultured MCF-7/4T1/MDA-MB-231 cells, treated with scramble or AIRE siRNA. f, g in vitro colony formation potential (f) and in vivo tumor formation (n = 10)(g) potential of 3D Matrigel-cultured MCF-7/4T1/MDA-MB-231 cells treated with scramble or AIRE siRNA. h Heatmap of stemness-associated gene (SOX2, c-Myc, Nanog, POU5F1, Notch3, Notc4, Tert, CD133, Wnt2, YAP1, AKT1, and ALDH1) expression in 3D Matrigel cultured MCF-7 cells treated with scramble or AIRE siRNA. i ALDH1+ cell subpopulations were determined in MCF-7 cells (3D Matrigel culture) treated with scramble or AIRE siRNA. j Schematic representation of the integrin-cytoskeleton-AIRE signals in breast cancer cells. Three independent experiments were performed. Data are represented as mean ± SEM. P < 0.05, statistical significance | PMC10300038 | 41392_2023_1453_Fig3_HTML.jpg |
0.421131 | 445dc0e6c49546778bb72dfe30355892 | ECM-induced biomechanical force drives stem cell-like tumor cell quiescence. a MCF-7/4T1 cells were seeded in a flask and 3D Matrigel, following which the cells were harvested for the cell proliferation assay in a 96-well plate (flask and 3D-flask groups). Some of the 3D-cultured MCF-7/4T1 cells were re-seeded in 3D Matrigel and subjected to cell proliferation determination at the same time points (3D group). b Proliferation of MCF-7 cells cultured in a flask, 3D-flask, and 3D gel (3D collagen and fibrinogen culture system). c Cell cycle analysis of MCF-7/4T1/MDA-MB-231 cells cultured in a flask, 3D gels, and 3D-flask. d Immunostaining for Ki67 and CoupTF1 in the flask, 3D gel, and 3D-flask groups. The scale bar is 20 μm. e GO and KEGG enrichment analysis of differentially expressed genes in the 4T1 cells cultured in the flask and 3D culture system, with a significance threshold of p-value < 0.05. f 1 × 103 4T1 cells were encapsulated in a 450-Pa 3D Matrigel (or not) and subcutaneously implanted into mice. On days 3 and 5, the mice were treated with PBS or dispase administered via subcutaneous injection. H&E staining of the hypodermis in each group was performed on days 10 and 20 (n = 10). The scale bar was 500 μm. g MCF-7 cells were cultured in the 3D Matrigel for 3 days and isolated for flask culture. After 0, 24, 48, 72, and 96 h of flask culture, cell proliferation or cycle was examined. h MCF-7 cells were seeded in 45-, 90-, and 450-Pa Matrigel for 3 days. Cell cycle and proliferation (in Matrigel) were examined. Three independent experiments were performed. Data are represented as mean ± SEM. P < 0.05, statistical significance | PMC10300038 | 41392_2023_1453_Fig4_HTML.jpg |
0.497426 | 72c400191c9a45ca8e8f38756a15128c | The biomechanical force promoted tumor cell quiescence through DDR2 signaling. a 3D Matrigel-cultured MCF-7 cells were treated with PBS and integrin β1/3-neutralizing antibodies. Following this, the cell cycle was determined. b Western blotting for DDR1 and DDR2 in MCF-7/4T1/MDA-MB-231 cells cultured in a flask or 3D Matrigel. c DDR2 expression at the mRNA and protein level in 3D Matrigel-cultured MCF-7/4T1/MDA-MB-231 cells treated with scramble or DDR2 siRNA. d Proliferation of 3D Matrigel-cultured MCF-7/4T1/MDA-MB-231 cells treated with scramble or DDR2 siRNA (in 3D Matrigel). e Cell cycle of 3D Matrigel-cultured MCF-7/4T1/MDA-MB-231 cells treated with scramble or DDR2 siRNA. f In vitro colony formation of MCF-7/4T1/MDA-MB-231 cells treated with scramble or DDR2 siRNA. g Western blotting of integrin β1, integrin β3, and AIRE in 3D Matrigel-cultured MCF-7/4T1/MDA-MB-231 cells treated with scramble or DDR2 siRNA. h Western blotting of phosphorylated STAT1, total STAT1, and P27 in flask/3D Matrigel-cultured MCF-7/4T1/MDA-MB-231 cells treated with scramble or DDR2 siRNA. i Schematic diagram of biomechanical force regulating breast cancer cell behaviors through DDRs and integrins signals. Three independent experiments were performed. Data are represented as mean ± SEM. P < 0.05, statistical significance | PMC10300038 | 41392_2023_1453_Fig5_HTML.jpg |
0.379342 | 7abb84aebab64eaf9142cf9dbf42c02b | The novel ECM-score predicts clinical outcomes in patients with breast cancer. a Kaplan–Meier overall survival curves are shown according to the high and low expression of COL1A1, COL1A2, FGA, FGB, FGG, ELN, FN1, and VTN in 1358 patients with breast cancer, based on data obtained from TCGA. b LASSO coefficient profiles of eight genes (COL1A1, COL1A2, FGA, FGB, FGG, ELN, FN1, and VTN). c The Kaplan–Meier overall survival curve was shown according to the high and low ECM score in 1358 patients with breast cancer derived from TCGA data. d Information of 86 patients with breast cancer. e Tumor tissues were collected from the 86 patients after standard treatment. The patients were divided into recurrent and non-recurrent groups according to findings from an 8-year follow-up visit. f Immunohistochemistry of collagen I, fibrinogen, elastin, fibronectin, and vitronectin in tumor tissues from patients with recurrent and non-recurrent breast cancer. g The ECM score (protein level) was determined in 86 patients divided into the recurrent and non-recurrent groups. h The Kaplan–Meier overall survival curve was shown according to the high and low ECM scores (protein level) of 86 patients with breast cancer. i Immunostaining of AIRE, YAP1, ITGB1, ITGB3, Notch3 and DDR2 in tumor tissues divided into non-recurrent/recurrent or ECM high/low groups. The scale bar was 500 μm. Three independent experiments were performed. Data are represented as mean ± SEM. P < 0.05, statistical significance | PMC10300038 | 41392_2023_1453_Fig6_HTML.jpg |
0.455053 | 84408c6e01d446bfa54cf87102e44242 | Microscopic anatomy of dentigerous cyst (DC), odontogenic keratocyst (OKC), and autosomal dominant polycystic kidney disease (ADPKD): (A, A′) The wall of DC consists of a thin epithelial layer and dense connective tissue with a variable number of fibroblasts. Pigment deposition (hemosiderin) or cholesterol crystals are located in the connective tissue. The epithelial lining consists of non-keratinized stratified epithelium with a moderate degree of cellular dystrophy. (B, B′) DCs exhibit low proliferation activity mainly in the basal layer of the epithelium. (C, C′) The apoptotic rate (TUNEL-positive cells) is low, and rare apoptotic bodies (black arrowhead) are dispersed in the epithelium (pigment deposition – grey arrowhead). (D, D′) Epithelial lining of DC exhibits a moderate expression of p53. (E) There are only sparse primary cilia in the basal layer of the epithelial lining of the DC (arrowhead). (F, F′) The epithelial component of OKC is more prominent compared to the DC, the epithelium is stratified and keratinized with parakeratosis and intracellular edema. (G, G′) OKC exhibits mitotic activity similar to DC, with prominent nests of proliferating cells. (H, H′) The apoptotic rate of OKC is low, with only occasional apoptotic bodies located in the outer layers of the epithelium (arrowhead). (I, I′) Epithelial lining of OKC demonstrates moderate expression of p53. (J) The OKC displays large numbers of primary cilia in the basal layer of epithelium, with random orientation and different lengths (arrowheads). (K, K′) Glomerular cysts and large cysts lined by simple cuboidal epithelium are typical features of ADPKD. (L, L′) The epithelium lining of cysts in ADPKD displays very low mitotic activity with only occasional Ki-67 positive cells (arrowhead) and the apoptotic activity is similarly low (arrowhead) (M, M′). (N, N′) The epithelium of tubules and the epithelial lining of cysts are positive for p53. (O) Short primary cilia are present on the cells of the flattened epithelial lining of cysts in ADPKD (arrowheads). | PMC10300219 | gr1.jpg |
0.416853 | d23460160a5044c68eee6fb94dbfd804 | Hypothesis for dentigerous cyst (DC) formation: (A) Developed permanent retained tooth (the third molar) in the mandible. (B) Due to a specific mutation, such as the loss of heterozygosity caused by a second hit in the encoding gene for Patched receptor homolog 1 (PTCH1), the Sonic Hedgehog pathway in the primary cilia is over-activated, causing a monoclonal proliferation of the mutated cell (red color) in the stellate reticular layer of enamel organ [2,6,9]. (C) In the specific microenvironment, local hypoxia develops in the center of the monoclonal cell cluster (purple color). Hypoxia activates the expression of the hypoxia-inducible factor-1 alpha (HIF-1α), which leads at the same time to apoptosis and proliferation [51]. (D) The proliferation is dominant on the margins, while the cells of the reduced enamel epithelium in the center cease to proliferate; in this way, a cavity is formed. The caspase-3, as a promotor of apoptosis, is overexpressed [51,54]. The hyperosmolar environment created by the accumulation of cell breakdown products absorbs fluids from the vicinity (green-brown color) and exerts pressure on the epithelial lining [3]. The epithelial cells produce cytoplasmic polycystin (PC1), which upregulates the expression of α2β1 integrins, thus increasing the cell adhesive rate [26,31]. The cyst is lateral to the crown of the tooth (the crown may be entirely included in the cyst sac), while the root is outside the cystic sac. (E) The cyst is attached to the tooth neck at the cement-enamel border, which limits its further growth in this direction but it can continue to grow into the bone. In this phase, enamel epithelial cells, which are in contact with the crown of the tooth, die because they are under pressure and have no nutrition (hypoxia). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.) | PMC10300219 | gr2.jpg |
0.4343 | caf60805cc514f879bf65f2fac5baf35 | Distribution of Cat-315-positive PNNs and AB1031-positive PNNs in the PFC of SAMR1, SAMP8, and SAMP10 mice. Representative double immunofluorescence images show the distribution of Cat-315-positive PNNs (A-C) and AB1031-positive PNSs (A'–C') in the dAC of SAMR1 mice (A, A'), SAMP8 mice (B, B'), and SAMP10 mice (C, C'). Higher-magnification images of Cat-315 (D-F) and AB1031 (D’-F') in L5/6 of the dAC of SAMR1 mice (D, D'), SAMP8 mice (E, E'), and SAMP10 mice (F, F'). The layer-specific patterns of Cat-315-positive PNN density (G) and AB1031-positive PNN density (H) in the dAC are shown. Data are expressed as box plots (n = 10 mice/group). P-values were calculated using a one-way ANOVA. *p < 0.05 for comparison of the same regions in SAMR1, SAMP8, and SAMP10 mice. Scale bar = 200 µm in C' (A-C, A’-C'), and 40 µm in F' (D-F, D’-F'). | PMC10300471 | gr1.jpg |
0.366578 | f5711a10b1c44144b3bc9b94f000ac90 | Distribution of tenascin-R-positive PNNs and brevican-positive PNNs in the PFC of SAMR1, SAMP8, and SAMP10 mice. Representative higher-magnification images of tenascin-R (A-C) and brevican (A’-C') in L5/6 of the dAC of SAMR1 mice (A, A'), SAMP8 mice (B, B'), and SAMP10 mice (C, C'). Layer-specific patterns of tenascin-R-positive PNN density (D) and brevican-positive PNN density (E) in the dAC are shown. Data are expressed as box plots (n = 10 mice/group). P-values were calculated using a one-way ANOVA. *p < 0.05 for comparison of the same regions in SAMR1, SAMP8, and SAMP10 mice. Scale bar = 40 µm in C’ (A-C, A’–C’). | PMC10300471 | gr2.jpg |
0.425178 | c67eb2971c0c4dd68a2f845339f26fd0 | Distribution of PV-positive neurons and WFA-positive PNN in the PFC of SAMR1, SAMP8, and SAMP10 mice. Representative double immunofluorescence images show the distribution of PV-positive neurons (A-I) and WFA-positive PNNs (A’-I') in the dAC (A-C, A’-C'), PL (D-F, D’-F'), and IL (G-I, G’-I') of SAMR1 mice (A, A', D, D', G, G'), SAMP8 mice (B, B', E, E', H, H'), and SAMP10 mice (C, C', F, F', I, I'). Higher magnification images of PV (J-L) and WFA (J’-L') in L5/6 of the dAC of SAMR1 mice (J, J'), SAMP8 mice (K, K'), and SAMP10 mice (L, L'). Scale bar = 200 µm in I’ (A-I, A’-I’), and 40 µm in L’ (J-L, J’-L’). | PMC10300471 | gr3.jpg |
0.39451 | 56429f4b8a8a44beb1ce42d4b0741d64 | Quantitative analyses of PV-positive neurons and WFA-positive PNNs in the PFC of SAMR1, SAMP8, and SAMP10 mice. Region-specific patterns of PV-positive neuron density (A-C), WFA-positive PNN density (D-F), and percentage of PV-positive neurons surrounded by WFA-positive PNN (G-I) in the dAC (A, D, G), PL (B, E, H), and IL (C, F, I) are shown. Data are expressed as box plots (n = 10 mice/group). P-values were calculated using a one-way ANOVA. *p < 0.05 for comparison of the same regions in SAMR1, SAMP8, and SAMP10 mice. | PMC10300471 | gr4.jpg |
0.419209 | 81552f0deec948dea0f9fcb3670ad93f | Distribution of PV-positive neurons and GAD67-positive neurons in the PFC of SAMR1, SAMP8, and SAMP10 mice. Representative double immunofluorescence images show the distribution of PV-positive neurons (A-I) and GAD67-positive neurons (A’-I') in the dAC (A-C, A’-C'), PL (D-F, D’-F'), and IL (G-I, G’-I') of SAMR1 mice (A, A', D, D', G, G'), SAMP8 mice (B, B', E, E', H, H'), and SAMP10 mice (C, C', F, F', I, I'). Higher magnification images of PV (J-L) and GAD67 (J’-L') in L5/6 of the dAC of SAMR1 mice (J, J'), SAMP8 mice (K, K'), and SAMP10 mice (L, L'). Scale bar = 200 µm in I’ (A-I, A’-I’), and 40 µm in L’ (J-L, J’-L’). | PMC10300471 | gr5.jpg |
0.397638 | a71a78ce6e6942bb8dc489ebe531e1b5 | Quantitative analyses of GAD67-positive neurons in the PFC of SAMR1, SAMP8, and SAMP10 mice. Region-specific patterns of GAD67-positive neuron density (A-C) and the percentage of PV-positive neurons co-localized with GAD67-positive neurons (D-F) in the dAC (A, D), PL (B, E), and IL (C, F) are shown. Data are expressed as box plots (n = 10 mice/group). P-values were calculated using a one-way ANOVA. *p < 0.05 for comparison of the same regions in SAMR1, SAMP8, and SAMP10 mice. | PMC10300471 | gr6.jpg |
0.424443 | 1f450676b51946f384092baa0c6a7b18 | Proton density fat-suppressed axial (A) and proton density non-fat-suppressed sagittal (B) magnetic resonance images in a right knee depicting the method using a localizer line on the axial slice (A) to determine the midsagittal position of the quadriceps tendon to then measure thickness in the sagittal plane (B). | PMC10300585 | gr1.jpg |
0.421328 | 69f8ff40ec524609b0d869828d47ecf9 | Proton density fat-suppressed axial (A) and proton density non-fat-suppressed sagittal (B) magnetic resonance images in a left knee showing the method for measuring the thickness of the patellar tendon at 1, 2 and 4 cm from the distal patella in both the axial and sagittal planes. | PMC10300585 | gr2.jpg |
0.389302 | 51bb11f8209d4aaea878ad96b1d86c97 | Proton density fat-suppressed axial (A) and proton density non-fat-suppressed sagittal (B) magnetic resonance images in a left knee depicting the method for measuring the thickness of the quadriceps tendon at 1 cm from the proximal patella in both the axial and sagittal planes. | PMC10300585 | gr3.jpg |
0.406034 | 1c665219540c41bf9d40ec242aaa0810 | Proton density fat-suppressed axial (A) and proton density non-fat-suppressed sagittal (B) magnetic resonance images in a left knee depicting the method for measuring the thickness of the patellar tendon at 1 cm from the distal patella in both the axial and sagittal planes. | PMC10300585 | gr4.jpg |
0.380743 | c213496c518e49b08b5bc7a5501ec23a | Foraging behaviour of Nyctalus aviator recorded by the microphone array. (a) Y-shaped four-microphone array arranged 1 m above the ground at Tokiwa Park in Asahikawa city, Hokkaido, Japan. (b) Typical foraging path along pulse emission point (black circle) while an attack is identified by feeding buzz sounds. The origin of the axes in the graph is the central microphone of the microphone array. (c) Spectrogram of echolocation pulses emitted before and after an attack. The red arrow indicates the starting point of the approach phase (see text). (d) Changes in interpulse-interval (IPI), pulse duration, flight speed and flight altitude as a function of distance to the attack point. Data were taken from all echolocation call sequences containing feeding buzzes (n = 45 from 38 tracked flights). The red line corresponds to the sound data shown in (c). The red arrow indicates the starting point of the approach phase of this data. | PMC10300664 | rsos230035f01.jpg |
0.417598 | 575612a0c446494c9d81271efa2f03e8 | Summary of results based on acoustic GPS logger tracking of an adult female. (a) Map shows the 40 min long flight trajectory including attack points (red cross) determined by feeding buzz occurrences. White arrows indicate the flight direction of the bat. The middle inset-graph shows a typical temporal change in IPI before an attack. The location of the exemplary attack point that was selected for this graph is circled in black in the black bordered inset-map. (b) Temporal change in flight altitude (blue line) above sea level. Grey vertical lines indicate attack points. (c) Enlarged view of (b) (indicated by the red square). (d) Temporal change in flight speed. | PMC10300664 | rsos230035f02.jpg |
0.446549 | 78880eae370644848b9033a789338d03 | Graph shows the model-based results on (a) attack probability, (b) flight altitude and (c) flight speed as a function of the habitat type. Coloured circles indicate the estimated means and probabilities, respectively, with coloured whiskers indicating the 95% confidence intervals. Grey dots represent the raw data points. Raw data (presence/absence data) were not plotted in (a) to ensure optimal representation of model results. Asterisks indicate statistically significant differences (***p < 0.001; **p < 0.01; *p < 0.05) | PMC10300664 | rsos230035f03.jpg |
0.55354 | 54a5045f02d146a0bfc307a69bb66e77 | Model outcomes for each type of model and set of priors under 100%, 90% and 75% threshold for moving jobs (Agent remains in current job if it pays 100/90/75% or more of alternative). (Note scale of axis differs for Models 5 and 6). Figure created using ggplot2 [36]. | PMC10300665 | rsos221346f01.jpg |
0.40152 | 126406ce81824499977a39a87ecf0569 | Final segregation distributions for each model type. (Note models 5 & 6 presented on different y axis scale). Dotted lines show approximate level of segregation observed when agents have perfect knowledge of skill levels under Model 1 conditions (top dotted line), Model 2 (conditions (middle dot-dash line) and Model 3 conditions (lower dashed line). Note only the lower two lines are shown for models 5 and 6. | PMC10300665 | rsos221346f02.jpg |
0.481994 | 25ca5c6112184fe99560f9860fcf9adf | 1HNMR spectra of HL ligand (a) and its [Zn(L)(NO3)(H2O)3] (b) and [La(L)(NO3)2(H2O)2] (c) complexes. | PMC10301192 | molecules-28-04777-g001.jpg |
0.486076 | b256b9a5a2b545e7b982ac327f788e5e | EI-mass spectral analysis of (a) [Cu(L)(NO3)(H2O)3], (b) [Zn(L)(NO3)(H2O)3], (c) [La(L)(NO3)2(H2O)2], and (d) [VO(L)(OC2H5)(H2O)2] complexes. | PMC10301192 | molecules-28-04777-g002a.jpg |
0.478185 | 550743321f9942e79347fbea74087bb7 | pH stability profile of the [Cu(L)(NO3)(H2O)3], [Cr(L)(NO3)2(H2O)2], [La(L)(NO3)2(H2O)2], [VO(L)(OC2H5)(H2O)2], and [Zn(L)(NO3)(H2O)3], complexes in DMF at different pH values. | PMC10301192 | molecules-28-04777-g003.jpg |
0.519867 | 5f594019942e4b988953aa15733a52fe | Natural charges on atoms, the molecular electrostatic potential (MEP) surface by density function B3LYP/6-311++g(d, p), the vector of the dipole moment, and the optimal ligand structure. | PMC10301192 | molecules-28-04777-g004.jpg |
0.507022 | 4fbdb8a5a9c04aaeb44142922d37da68 | The optimized structure, the vector of the dipole moment, the natural charges on atoms, and the molecular electrostatic potential (MEP) surface on active centers of [CuLNO3(H2O)3] and [ZnLNO3(H2O)3] complexes. | PMC10301192 | molecules-28-04777-g005a.jpg |
0.450959 | c7337f4fb7bd4c12a194e9a7503217b7 | The molecular electrostatic potential (MEP) surface on active centers of the optimized structure of [CrL(NO3)2(H2O)2] and [LaL(NO3)2(H2O)2] complexes, the dipole moment’s vector, the atoms’ natural charges. | PMC10301192 | molecules-28-04777-g006.jpg |
0.479774 | 7288b112a49d4e2da4d4cb2ad70b9be4 | The optimized structure, the vector of the dipole moment, the natural charges on atoms, and the molecular electrostatic potential (MEP) surface on active centers of [VOL(H2O)OEt] complex. | PMC10301192 | molecules-28-04777-g007.jpg |
0.412448 | 7f93650109464502b2a3431e8fe964be | HOMO and LUMO charge density maps of HL, [CuLNO3(H2O)3], [ZnLNO3(H2O)3], [CrL(NO3)2(H2O)2], [LaL(NO3)2(H2O)2], and [VOL(H2O)OEt]. | PMC10301192 | molecules-28-04777-g008.jpg |
0.395977 | 4172c9c25bca4925b49939e8f316dfe4 | (a) Graphical representation of antimicrobial activity results of HL ligand and its new [Cu(L)(NO3)(H2O)3], [Zn(L)(NO3)(H2O)3], [VO(L)(OC2H5)(H2O)2], [Cr(L)(NO3)2(H2O)2], and [La(L)(NO3)2(H2O)2] complexes at 20 µg/mL concentration and (b) zone of inhibition of [Zn(L)(NO3)(H2O)3], [La(L)(NO3)2(H2O)2], and [VO(L)(OC2H5)(H2O)2] against C. albicans. | PMC10301192 | molecules-28-04777-g009.jpg |
0.458756 | b3d1792a777d45758ebe7b80811d56a3 | Absorption spectra of the complexes [VO(L)(OC2H5)(H2O)2], [Cu(L)(NO3)(H2O)3], [La(L)(NO3)2(H2O)2], [Cr(L)(NO3)2(H2O)2], [Zn(L)(NO3)(H2O)3], and HL in the presence of increasing concentrations of CT-DNA (in Tris-HCl/NaCl buffer). With increasing concentrations of CT-DNA, the absorbance of the complex changes at [complex] = 10 μM and [DNA] = 10–100 μM. | PMC10301192 | molecules-28-04777-g010a.jpg |
0.48407 | f6bd49757cb745e9a310c53c5c35bf9e | The relative viscosity of CT-DNA is affected by the quantity of ethidium bromide (EB) and the metal complexes. | PMC10301192 | molecules-28-04777-g011.jpg |
0.409127 | c3f0826e7f624db0abbedf66468066db | Gel electrophoresis pattern showing the interactions of the new complexes with DNA based on gel electrophoresis. Lane 1: DNA Ladder, Lane 2: HL + DNA, Lane 3: [Cu(L)(NO3)(H2O)3] + DNA, Lane 4: [VO(L)(OC2H5)(H2O)2] + DNA, Lane 5: [La(L)(NO3)2(H2O)2] + DNA, and Lane 6: [Zn(L)(NO3)(H2O)3] + DNA, Lane 7: [CrL(NO3)2(H2O)2] + DNA. | PMC10301192 | molecules-28-04777-g012.jpg |
0.401247 | 5354f721b070446cb06cd3a80a037bf3 | Concentration-dependent IC50 values of metal complexes’ DPPH radical-scavenging activity. | PMC10301192 | molecules-28-04777-g013.jpg |
0.403638 | 7123efe21a5049a8b828ca8c9ce03480 | Inhibition % of protein denaturation of HL ligand and its metal complexes compared to ibuprofen at different concentrations. | PMC10301192 | molecules-28-04777-g014.jpg |
0.459684 | 294d81076c544e4a9d8d0d72555d7166 | Two-dimensional and three-dimensional plots of the interactions between HL, [CuLNO3(H2O)3], and [ZnLNO3(H2O)3] with the active site of the receptor of Candida albicans (PDB ID: PDB ID: 5V5Z). Hydrophobic interactions with amino acid residues are shown with dotted curves. | PMC10301192 | molecules-28-04777-g015.jpg |
0.41264 | d06ac1903218448d943759ac8135cc86 | Two-dimensional and three-dimensional plots of the interactions between [CrL(NO3)2(H2O)2], [LaL(NO3)2(H2O)2], and [VOL(H2O)OEt] with the active site of the receptor of Candida albicans (PDB ID: PDB ID: 5V5Z). Hydrophobic interactions with amino acid residues are shown with dotted curves. | PMC10301192 | molecules-28-04777-g016a.jpg |
0.527303 | 707dc16191d844a6a6a7a0e0c714b720 | (a) The effect of Cu(II) Schiff base complex on MB photocatalytic degradation, [complex] = 2.5 mg, 30 mL of MB. (b) The temporal absorption spectrum changes of MB taking place under visible light irradiation for CuMGO catalyst, initial concentration of MB: 6.25 × 10−3 M, 30 mL, CuMGO: 2.5 mg and pH: 10. (c) Optimization of the pH for the degradation of MB. (d) Optimization of the amount of catalyst for degradation and (b) the recyclability of the catalyst. | PMC10301192 | molecules-28-04777-g017a.jpg |
0.417369 | 9a02d26c885d4f18b41ad3979371413b | The possible photocatalytic mechanism for the degradation of MB in the presence of Cu(II) Schiff base complex loaded on graphene oxide and H2O2. | PMC10301192 | molecules-28-04777-g018.jpg |
0.537104 | d221774b9011482f8e1d805b02407087 | Mass fragmentation pattern of the HL Schiff base ligand. | PMC10301192 | molecules-28-04777-sch001.jpg |
0.553513 | e4118c02b7984e4ca8789c5684dbf553 | Schematic representation for the synthesis of HL Schiff base ligand and its metal complexes. | PMC10301192 | molecules-28-04777-sch002.jpg |
0.659913 | b94514a7b3514adabc6b39886ec35f88 | X-ray structure of compound 3a (CCDC-2264554). | PMC10301255 | molecules-28-04751-g001.jpg |
0.439136 | 1449dd1fcb544f16a5bea88289b7c8c7 | Representative biologically active naphtho[2,3-b]furan-4,9-diones. | PMC10301255 | molecules-28-04751-sch001.jpg |
0.392526 | d1b3e114bf884798a077725a339704de | Synthetic approaches starting from 2-hydroxy-1,4-naphthoquinones: (a) multi-component reaction, (b) thermal cyclization with enamines, (c) CAN-mediated oxidative cycloaddition with enol ether, (d) transition-metal promoted thermal cyclization, (e) strong-base promoted thermal cyclization, (f) strong oxidantpromoted thermal cyclization. | PMC10301255 | molecules-28-04751-sch002.jpg |
0.433495 | b0ae9af9c8fb4566abcce042854d6e58 | Visible-light-mediated green synthesis of naphtho[2,3-b]furan-4,9-diones. | PMC10301255 | molecules-28-04751-sch003.jpg |
0.455574 | 8625574c2ff54cca90ae7069288451ca | Scope of the photochemical synthesis of naphtho[2,3-b]furan-4,9-diones (3). | PMC10301255 | molecules-28-04751-sch004.jpg |
0.457565 | b5794d246779486bb0bdf455ce521dbf | Scope of the photochemical synthesis of dihydronaphtho[2,3-b]furan-4,9-diones (5). | PMC10301255 | molecules-28-04751-sch005.jpg |
0.413524 | 56c5c44e884447798c96b9c8c23e2eec | Control experiments for the photocatalyzed [3+2] cycloaddition reaction: (a) experiment was performed under standard conditions, (b) experiment was performed in the absence of light, (c) experiment was performed in the presence of TEMPO. | PMC10301255 | molecules-28-04751-sch006.jpg |
0.481351 | db97fad809a545af9cc233d6d649974d | Proposed mechanism for the photocatalyzed [3+2] cycloaddition reaction. | PMC10301255 | molecules-28-04751-sch007.jpg |
0.59565 | fd4134d124414f5aa08f62435a5da0e7 | Molecular structures of BTM-1DCz, BTM-2DCz, TTM-1DCz, TTM-2DCz, and deuterated carbazole (DCz). | PMC10301369 | molecules-28-04805-g001.jpg |
0.443082 | 1cc5f5d1412a4abb9505d17a3eb1d564 | UV-Vis absorption and normalized PL spectra of four deuterated radicals in cyclohexane solvent (1 × 10−5 M). | PMC10301369 | molecules-28-04805-g002.jpg |
0.480722 | 8b89b35a4cd1425baee0d57da26944e7 | Cyclic voltammetry (CV) curves of (a) BTM-1DCz and BTM-2DCz; (b) TTM-1DCz and TTM-2DCz. Ferrocene cation/ferrocene (Fc+/Fc) couples were used as reference. | PMC10301369 | molecules-28-04805-g003.jpg |
0.471277 | 1c047d45eb6f4e199cdb08ef5e853de8 | (a) Optimized molecular structures of deuterated radicals. The frontier orbitals of deuterated radicals (b) BTM-1DCz, (c) BTM-2DCz, (d) TTM-1DCz, and (e) TTM-2DCz. | PMC10301369 | molecules-28-04805-g004.jpg |
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