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0.424965 | a4b139442825448fb26aaafd7ce8552f | The general framework of proposed approach. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g001.jpg |
0.550948 | fa143107cf15461b81f449555ba82297 | The distribution of data (a) for prediction and (b) for classification. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g002.jpg |
0.400373 | 8f61070d32c747a19fec415d70a26dcd | Stages of 10-fold cross validation. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g003.jpg |
0.450821 | 3cfc82554bb749c89ee8ca631e34e97a | Process of scattered crossover in GA. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g004.jpg |
0.482473 | 2b39b4ad15844a69a890a3360c39d938 | Proposed 1-D CNN architecture. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g005.jpg |
0.394898 | f98ac29897794421b8bc31f707680268 | Proposed LSTM and BiLSTM architectures. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g006.jpg |
0.376459 | c04127c2bcb345d0ba6e8eb0063be7bc | The accuracy results of the ML models on cancer prediction with different numbers of attributes. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g007.jpg |
0.389325 | 7d2d71579072493eb7dc3a40e479f481 | The accuracy results of the ML models on cancer stage classification with different numbers of attributes. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g008.jpg |
0.406765 | b3239021164f41779df34302576eebaa | The accuracy results of the DL models on cancer prediction with different numbers of attributes. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g009.jpg |
0.454001 | 817354c82e424e87b4ca8883e149567f | The accuracy results of the DL models on cancer stage classification with different numbers of attributes. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g010.jpg |
0.457286 | 73e8904e9f544843bedd8ac154b22c48 | Practical applicability of the proposed approach. (Illustrations by the authors). | PMC10052105 | sensors-23-03080-g011.jpg |
0.494049 | b13c363caf954306ab2a9b2c9e6f7771 | Chemical structures of 3,5-diarylpyrazole derivatives: anle138b, [18F]anle138b, [11C]anle253b and [11C]MODAG-001. | PMC10052605 | molecules-28-02732-g001.jpg |
0.48542 | f8dffb78ccab4388ab5248f5c9590475 | Radiolabelling routes to 6-[18F]FP. Conditions: (A) [29] (i) elution of [18F]F− with Et4NHCO3 in MeOH; (ii) evaporation of MeOH; and (iii) 1 in DMSO, 130 °C for 10 min with two SPE and one HPLC purifications; (B) (i) elution of [18F]F− with Bu4NOTf in 2-PrOH directly to the solution of 2a or 2b and Cu(OTf)2(py)4 in CH3CN; (ii) 65 °C for 10 min, and then 110 °C for 10 min; (C) (i) elution of [18F]F− with Et4NHCO3 in MeOH; (ii) evaporation of MeOH; (iii) 3 and Cu(CH3CN)4OTf in DMF, 90 °C for 20 min; (D) (i) elution of [18F]F− with 4a or 4b in MeOH/PC; (ii) 85 °C for 10 min, and then 120 °C for20 min; RCC—radiochemical conversion as determined by radioTLC; RCY—radiochemical yield corrected for radioactive decay; procedures (B) and (D) avoid any azeotropic drying or solvents evaporation steps. | PMC10052605 | molecules-28-02732-g002.jpg |
0.40552 | f0ecff52347c4c60978524644c8f289a | Analytical radioHPLC chromatograms of the reaction mixture (A,B) and final product (C) in the synthesis of [18F]anle138b. (A) 6-[18F]FP; (B) 6-[18F]FTH; and (C) [18F]anle138b. HPLC column X-Bridge C18, 150 × 4.6 mm (Waters), gradient of 0.1%TFA/CH3CN, and flow rate of 2.0 mL/min. | PMC10052605 | molecules-28-02732-g003.jpg |
0.428513 | a99254f042a4497caa26ec64e4c6f8ca | HPLC analysis of the formulated [18F]anle138b. Conditions: HPLC column X-Bridge C18, 150 × 4.6 mm (Waters Corporation (Millford, CT, USA), gradient of 0.1%TFA/CH3CN with a flow rate 2.0 mL/min, UV is254 nm: (A) reference standard [19F]anle138b; (B) the formulated [18F]anle138b. | PMC10052605 | molecules-28-02732-g004.jpg |
0.467507 | 6bba6d3874474d1cb9baac9a081591e1 | Process flow diagram (PFD) for the semi-automated radiosynthesis of [18F]anle138b. (A) a solution of precursor 4b (20 µmol) in 44% MeOH/PC (0.9 mL); (B) a solution of NH2NHTs (40 µmol) in MeOH (1 mL); (C) a solution of Bu4NOH (26 µmol) in MeCN (0.4 mL); and (D) a solution of 3′-bromophenylacetylene (0.4 mmol) in CH3CN (0.4 mL); E and F are not used. | PMC10052605 | molecules-28-02732-g005.jpg |
0.46249 | 64dcdfac548c42b98c9a0bbf94edb765 | Proposed radiosynthesis route for [18F]anle138b (Zarrad, 2017) [29]; RCY—radiochemical yield, decay-corrected. | PMC10052605 | molecules-28-02732-sch001.jpg |
0.459037 | 040e9c74b8754c60bfd4ec2879821980 | Radiosynthesis scheme for [18F]anle138b. Conditions—step 1: Elution of [18F]F− with 20 µmol 4b in 44% MeOH/PC (0.9 mL). Heating for 85 °C, 10 min, then 120 °C, 20 min; step 2: NH2NHTs (40 µmol) in MeOH (1 mL). Heating for 90 °C, 10 min under stirring by N2 flow; step 3: Bu4NOH (26 µmol in 0.4 mL CH3CN, 65 °C, 5 min), then 3′-bromophenylacetylene (0.4 mmol in 0.4 mL CH3CN, 90 °C, 25 min). | PMC10052605 | molecules-28-02732-sch002.jpg |
0.448536 | b5e23cea4af34bd19a4a1047b979f14e | Synthesis of [19F]anle138b. Reagents and conditions: (i) BBr3, DCM, −80–20 °C, 30 h; (ii) CH2Br2, K2CO3, DMF, 110 °C, 5 h; (iii) TsNHNH2, CH3OH, 20 °C, 4 h; and (iv) LiOtBu, CH3CN, reflux, 23 h. | PMC10052605 | molecules-28-02732-sch003.jpg |
0.473956 | 13844b26e5cd4f479843a5da26599fa9 | Schematic diagram of study | PMC10052851 | 12872_2023_3196_Fig1_HTML.jpg |
0.44038 | bd091b10d6cc487195ed3638185ac609 | Differentially expressed gene analysis and protein–protein interaction networks. A Intersection of 668 DEGs and 2013 IRGs. B volcano plot in GSE113079. C volcano plot in merged GP570 datasets. D The PPI network of the 58 DIRGs | PMC10052851 | 12872_2023_3196_Fig2_HTML.jpg |
0.44479 | edcc111a7c7d4f31ae4545d83b014f8a | GO, KEGG, and DO pathway enrichment analysis. A BP of 58 DIRGs. B CC of 58 DIRGs. C: MF of 58 DIRGs. D KEGG pathway of 58 DIRGs. E DO pathway of 58 DIRGs. F PPI of hub genes | PMC10052851 | 12872_2023_3196_Fig3_HTML.jpg |
0.427942 | 6c30b1fd3e564ff0a3f686c2542b67d2 | Significant DIRGs of the RF, PLS, SVM, and KNN models. A Cumulative residual distribution of the RF, PLS, SVM, and KNN models. B Boxplots of the residuals in the RF, PLS, SVM, and KNN models. C The importance of significant DIRGs in the RF, PLS, SVM, and KNN models | PMC10052851 | 12872_2023_3196_Fig4_HTML.jpg |
0.424046 | 3351a68867d44ee8ac2a09696899d0e1 | A Relative expression level of PTGER2, LGR6, IL17B, IL13RA1, CCL4, and ADM. B Correlation among PTGER2, LGR6, IL17B, IL13RA1, CCL4 and ADM | PMC10052851 | 12872_2023_3196_Fig5_HTML.jpg |
0.394581 | 255e4aa789de482192e9372b992b5ed6 | Validation and assessment of a nomogram model for MI diagnosis. A Nomogram model. B The AUC of the nomogram model in predicting the incidence of MI. C Calibration curve to assess the predictive value. D DCA curve to evaluate the clinical value | PMC10052851 | 12872_2023_3196_Fig6_HTML.jpg |
0.423099 | 99f1c3d95b204a80aa2427fa518b5cba | A Distribution of the immune cells of all samples. B Different distribution of 22 immune cells between patients with MI and healthy controls | PMC10052851 | 12872_2023_3196_Fig7_HTML.jpg |
0.410453 | 7279df2f727e4358b6b14bc92841e0e8 | Correlation between IL13RA1 (A), ADM (B), CCL4 (C), PTGER2 (D), IL17B (E), LGR6 (F) and infiltrating immune cells in myocardial infarction | PMC10052851 | 12872_2023_3196_Fig8_HTML.jpg |
0.458698 | 632a83447e014033a37b4c2b6dec2cb8 | The cell separation defect in the dpp3Δ mutant is due to med15Δ mutation. WT and mutant strains of C. lusitaniae were grown in liquid YPD medium at 35 °C under 215 rpm. Cells were visualized and imaged after 48 h using 40× magnification under brightfield. Scale bars represent 10 µm. Please refer to Table 1 for detailed genotypes of the strains. When a WT copy a MED15 was reintegrated into the dpp3Δ mutant, cell separation returned to wild-type levels. | PMC10053558 | jof-09-00333-g001.jpg |
0.435028 | 7a4cc7aeb63b4407ac8752db230d0341 | The pseudohyphal growth defect in the dpp3Δ mutant is conferred by the med15Δ mutation. (A) Strains were grown on YCB plates supplemented with uracil at 30 °C. Colony periphery was visualized at 4× magnification under brightfield and photographed after 24 h. Scale bars represent 1 mm. (B) Filament length was measured at 24 h, 48 h, 72 h and 144 h using Image J. The average length for one experiment was obtained from 20 measurements for each strain. Results are expressed as mean values ± standard error of data from three independent experiments. Values that are statistically different are marked with an asterisk (p-value < 0.05). Please refer to Table 1 for detailed strain genotypes. When a WT copy a MED15 was reintegrated into the dpp3Δ mutant, pseudohyphal growth returned to wild-type levels. | PMC10053558 | jof-09-00333-g002.jpg |
0.428408 | 6bc4227702cd43bea975272efb4114ef | Mating of the WT and dpp3Δ strains with the same tester strain. Images were taken after 48 h of incubation at 30 °C. Scale bars represent 10 µm. (A) Mating between the 5094 MATα and the WT or dpp3Δ MATa strains. Inserts show enlarged views of the cells indicated by arrows. (a,c) Sexual conjugation between two yeast cells. (b) Ascospores. (d) Ascus. (B) Mating between the non-stained 5094 MATα and the CFW-stained WT or dpp3Δ MATa strains. Acceptor cells are indicated by thin arrows, and an ascus is indicated by a thick arrow. | PMC10053558 | jof-09-00333-g003.jpg |
0.423338 | 46b8da7517f54c2b98955d224ba65f9b | The mating defect in the dpp3Δ mutant is conferred by the med15Δ mutation. WT and mutant strains of C. lusitaniae (MATa) were crossed with the CL38 strain (MATα). Images were taken after 48 h of incubation at 30 °C. Scale bars represent 5 µm. Asci are indicated by arrowheads, and conjugation tubes by arrows. | PMC10053558 | jof-09-00333-g004.jpg |
0.399176 | 0da2a9aee7b64ff48955c0d4bafe5397 | Heat map showing the REC strain the expression profile of the proteins deregulated at least 2-fold (p value < 0.05) in the dpp3Δ relative to the WT. Proteins that were not quantified in at least two biological replicates out of the three in both the dpp3Δ and the REC strains were taken out of the analysis. The heat map was generated in Prism8. The fold change (Log10) relative to the WT is color coded as indicated in the side panel. The proteins deregulated in the dpp3Δ mutant were still deregulated in the REC strain despite a wild-type copy of DPP3 being reintegrated, likely reflecting changes attributable to med15Δ mutation. | PMC10053558 | jof-09-00333-g005.jpg |
0.485466 | 3901816508cd40e087136ebed2ff0020 | Functional distribution of the proteins found differentially expressed in the dpp3delta mutant compared with the REC strain. Proteins were classified according to the biological processes (A) or molecular functions (B) with which they are associated based on their predicted functions using gene ontology (GO) annotations of C. lusitaniae (ATCC42720) and C. albicans (SC5314) in the Uniprot database. The number of proteins down-regulated or up-regulated can be read on the horizontal axis. Since proteins can be linked to more than one annotation group, the sum of annotated genes is larger than the number of total up- and down-regulated genes in the set analyzed. The categories found statistically enriched by the DAVID tool (https://david.ncifcrf.gov, accessed on 28 October 2022) are marked with an asterisk (p-value < 0.05). Because the analysis was performed using C. lusitaniae reference genome ATCC42720, enrichment of some biological processes annotated from C. albicans SC5314 could not be addressed. | PMC10053558 | jof-09-00333-g006.jpg |
0.4108 | f6b2d43c9fa946f1bd30fac84d935ed0 | Functional distribution of the proteins found differentially expressed in the REC strain (carrying the med15Δ mutation) compared with the WT (6936) strain. Proteins were classified in biological processes based on their predicted functions using gene ontology (GO) annotations from C. lusitaniae (ATCC42720) and C. albicans (SC5314) in Uniprot database. The number of proteins down-regulated or up-regulated can be read on the horizontal axis. Since proteins can be linked to more than one annotation group, the sum of annotated genes is larger than the number of total up- and down-regulated genes in the set analyzed. The categories found statistically enriched by DAVID tool (https://david.ncifcrf.gov, accessed on 21 February 2023) are marked with an asterisk (p-value < 0.05). Because the analysis was performed using C. lusitaniae reference genome ATCC42720, enrichment of some biological processes annotated from C. albicans SC5314 could not be addressed. | PMC10053558 | jof-09-00333-g007.jpg |
0.449786 | 23c60b3c15ea4232a9dedfc56412720e | Summary of the functions of Med15 and Dpp3 in C. lusitaniae and of the biological pathways involved. Med15 is a subunit of the tail module of the mediator complex. Based on sequence homology with its orthologs in S. cerevisiae and C. albicans, Dpp3 is predicted to be a putative phosphatase in C. lusitaniae. The inactivation of DPP3 repeatedly drove an additional mutation in MED15. Dpp3 was shown to play an important role in virulence [25]. In this study, we show that Med15 controls diverse cellular processes, such as cell separation, mating and hyphal growth. The role of Med15 in virulence was inferred from the partial restoration of virulence in the reconstituted strain dpp3Δ + DPP3 but was not formally demonstrated. Proteomic analyses allowed to uncover the biological processes under the positive or negative regulation of Med15 and Dpp3. Dotted lines and question mark indicate that the links remain to be demonstrated. | PMC10053558 | jof-09-00333-g008.jpg |
0.479354 | 5072c11992eb4fda881a4e5b5e8586af | Soluble free total phenolic content (1), soluble free total flavonoid content (2), soluble free total antioxidant activity (3), sum of soluble (free and conjugated) and insoluble bound phenolic acids (4) of wholemeal (A) and (B) semolina of five durum wheat varieties. The same letter indicates no statistical difference, whereas different letters stand for significant statistical difference (p < 0.05; Tukey’s test). Legend: TPC, total polyphenol content; TFC, total flavonoid content; TEAC, total antioxidant activity. | PMC10053801 | plants-12-01350-g001.jpg |
0.498385 | 3e1dd4fb6d7e438f95e77d616aedda73 | Pearson correlation coefficients among morphological and yield-related traits, quality, and bioactive compounds. Abbreviations: SDF, soluble dietary fibre; SDS, SDS-sedimentation volume; TEAC, total antioxidant activity; GI, gluten index; TFC, total flavonoid content; TPC, total polyphenol content; PC, protein content; GC, gluten content; TKW, thousand kernel weight; IDF, insoluble dietary fibre; TW, test weight; TPAs, total phenolic acids; YP, total carotenoid content. Significance level: ***, 0.001; **, 0.01; *, 0.05. | PMC10053801 | plants-12-01350-g002.jpg |
0.38947 | 2f83826e2f1248c683bfc1f5a8086110 | Biplot of the first (PC1) and second (PC2) principal components showing the variation for 26 traits. Genotypes are represented by different coloured symbols. Trait contributions are shown with arrows. The direction and distance from the centre of the biplot indicate how each trait contributes to the first two components. Abbreviations: TFC, total flavonoid content; TPC, total polyphenol content; TEAC, total antioxidant activity; IDF, insoluble dietary fibre; TKW, thousand kernel weight; TW, test weight; SDS, SDS-sedimentation volume; GI, gluten index; YP, total carotenoid content; TPAs, total phenolic acids. | PMC10053801 | plants-12-01350-g003.jpg |
0.386889 | b8495f786eb24ae2980fa6ef7d1fb0e5 | Field characterization in the plane-versus-plane electrode chamber. (A) Equipotential line and current line distributions in the 1 × 1-mm2 chamber calculated without the sphere. The chamber is energized with 1 V at the right electrode (vertical gray bar on the right) compared to 0 V at the left electrode (vertical gray bar on the left). (B) The potential changes linearly between the electrodes. The potential plots along the x-coordinate are identical for all y-coordinates. The basic sheet conductance LBasic2D is 1 S and 100 mS for the 1 S and 100 mS media, respectively, corresponding to a cell constant of k2D=1.0. (C) The field gradient is zero. | PMC10053818 | micromachines-14-00670-g001.jpg |
0.404811 | 80c73b9901dd4ecb950dad7c7d27dbed | Field characterization in the pointed-versus-pointed electrode chamber. (A) Potential and current line distributions in the 1 × 1-mm2 chamber of two pointed electrodes calculated without the sphere. The chamber is energized with 1 V at the right electrode versus 0 V at left electrode. The basic sheet conductance LBasic2D is 211.5 mS and 21.15 mS for the 1 S and 100 mS media, respectively, corresponding to a cell constant of k2D=0.2115. (B) Sequence of potential profiles along horizontal lines with y = 0 (solid line), 100, 200 and 500 µm (dashed lines). (C) Field gradient plots for the potential profiles in (B). The insert is a zoom-out for y = 0 µm. Field gradients of 1945.3 V/m2 have been calculated before the pointed electrodes. | PMC10053818 | micromachines-14-00670-g002.jpg |
0.539198 | 1b5ba43c036b42b196bf956844a73cec | Potential and current line distributions for different positions of the 1.0-S sphere in 0.1-S medium, in front of the plane electrode ((A) at the edge; (C) at the center) and on the watershed ((B) at the edge; (D) at the saddle point in the center). The overall conductances of the chamber are (A) 105.7 mS, (B) 104.5 mS, (C) 107.0 mS, and (D) 105.3 mS. For an improved visibility of the inhomogeneous polarization of the sphere, equidistant current lines were used at the left electrode (B,D) or in the center plane (A,C). | PMC10053818 | micromachines-14-00670-g003.jpg |
0.442178 | 1edbde1c18864fb5a88066a5694cf411 | Potential and current line distributions for different positions of the 0.1-S sphere in 1.0-S medium, in front of the plane electrode ((A) at the edge; (C) at the center) and on the watershed ((B) at the edge; (D) at the saddle point in the center). The overall conductances of the chamber are (A) 943.7 mS, (B) 933.3 mS, (C) 955.8 mS, and (D) 949.3 mS. Equidistant current lines were used at the left electrode (A,C) or in the center plane (B,D) to improve the visibility of the inhomogeneous polarization of the sphere. | PMC10053818 | micromachines-14-00670-g004.jpg |
0.404728 | 8b61a0f6d03144b7a9e306bd1d229294 | Single 200-µm, 1.0-S sphere (reddish circles in (A)) in the chamber of Figure 1 with 0.1-S medium. (A) Conductance field plot with trajectories (a–e). A watershed (vertical white line in the center) separates the two caption areas of the stable endpoints E1 and E3. E2 is an unstable saddle point in the middle of the watershed. (B) Chamber conductance along the trajectories. The basic, minimum, mean and maximum conductances are 100 mS (w/o sphere), 105.7 mS (Figure 3B), 105.3 mS and 107.0 mS (Figure 3C; E1, E3), respectively. Trajectories a, c and e end at E1. Trajectories b and d end at E2 and E3, respectively. (C) Normalized DEP forces calculated from the conductance values in (B). The DEP force is zero at the saddle point E2 but not at E1 and E3 (see Section 5). The arrows for a and b|c mark the end of the trajectories. | PMC10053818 | micromachines-14-00670-g005.jpg |
0.413667 | 87a5d06623d44229b1c702e06831345c | Single 200-µm 2D sphere of 0.1 S (reddish circles in (A)) in the chamber of Figure 1 with 1.0-S medium. (A) Conductance field plot with trajectories (a–e). A watershed (vertical white line in the center) separates the two caption areas of the stable endpoints E1 and E3. E2 is an unstable saddle point in the middle of the watershed. (B) Chamber conductance along the trajectories. The basic (w/o sphere), minimum, mean and maximum conductances are 1000 mS, 933.3 mS (Figure 4B), 948.73 mS and 955.8 mS (Figure 4C; E1, E3), respectively. The trajectories a, c and e end at E1. Trajectories b and d end at E2 and E3, respectively. (C) Normalized DEP forces calculated from the conductance values in (B). The DEP force is zero at the saddle point E2 but not at E1 and E3 (see Section 5). | PMC10053818 | micromachines-14-00670-g006.jpg |
0.509486 | 199f250123f14583b1bd0dd1107acf6d | Potential and current line distributions for different positions of the 1.0-S sphere in 0.1-S medium at the left edge ((A) at the top; (C) at the electrode) and on the watershed ((B) at the edge; (D) at the saddle point in the center). The overall sheet conductances of the chamber are (A) 21.20 mS, (B) 21.30 mS, (C) 32.74 mS, and (D) 21.47 mS. In all plots, current lines were selected, which are equidistant in the vertical center plane of the chamber. | PMC10053818 | micromachines-14-00670-g007.jpg |
0.492328 | cc7dba78969b4c23aa80849d605ff1e9 | Potential and current line distributions for different positions of the 0.1-S sphere in 1.0-S medium, at the left vertical edge ((A) at the top; (C) at the electrode) and on the watershed ((B) at the edge; (D) at the saddle point in the center). The overall sheet conductances of the chamber are (A) 210.8 mS, (B) 209.1 mS, (C) 53.21 mS, and (D) 208.2 mS. In the plots, the current lines were selected to be equidistant at the left edge (A) and the chamber’s vertical center plane (B–D). | PMC10053818 | micromachines-14-00670-g008.jpg |
0.433091 | 4336655c8dce44ff8093f150229b0ae8 | Single 200-µm, 1.0-S sphere (reddish circles in (A)) in the chamber of Figure 2 with 0.1-S medium. (A) Conductance field plot with trajectories (a–e). A watershed (vertical white line) separates the two caption areas of the stable endpoints E1 and E3. E2 is an unstable saddle point in the middle of the watershed. (B) Chamber conductance along the trajectories. The basic, minimum, mean, and maximum conductances are 21.15 mS (w/o sphere), 21.20 mS (Figure 7A), 21.52 mS, and 32.74 mS (Figure 7C; E1, E3), respectively. The system’s chamber conductance reaches peak values at the endpoints E1 (trajectories a and e) and E3 (trajectory b). Trajectory b ends at E2. (C) Normalized DEP forces calculated from the conductance values in (B). Force peaks are generated at the touch of chamber surfaces and again before (trajectories a, d, and c) or at the touch of the electrode (trajectory e). Trajectory b ends at the saddle point in the middle of the watershed with zero DEP force. | PMC10053818 | micromachines-14-00670-g009.jpg |
0.4014 | c417188eea8748ec9e5defc5538df559 | Single 200-µm sphere of 0.1 S (reddish circles in (A)) in the chamber of Figure 2 with 1.0-S medium. (A) Conductance field plot with trajectories (a–g). The two symmetry lines (vertical and horizontal white lines through the center), which are watersheds, separate four catchment areas with the equivalent, stable endpoints E1, E3, E5, and E7. The endpoints E2, E4 and E6 are unstable saddle points. (B) Sheet conductance along the trajectories. The basic (w/o sphere), minimum, mean, and maximum conductances are 211.47 mS, 53.21 mS (Figure 8C), 207.20 mS, and 210.8 mS (Figure 8A; E1, E3, E5, E7), respectively. Trajectories d and e end at E1, and trajectory b at E3. Trajectory g ending at E5 is largely equivalent to trajectory e. The instable saddle points E2, E4, and E6 can be reached only along one of the symmetry lines, e.g., by trajectories a, c, and f, respectively. (C) Normalized DEP forces calculated from the conductance values in (B). Each curve’s starting points and endpoints are marked with a straight line and an arrow, respectively. | PMC10053818 | micromachines-14-00670-g010.jpg |
0.433536 | f9155cebdd4848bfb362e54c0debe29c | On the DEP force reversibility along the horizontal (A,C) and vertical (B,D) symmetry lines in the plane-versus-plane electrode chambers. (A,B) log-plots of the forces from Figure 5 and Figure 6. (C,D) Ratio of forces (1.0-S sphere divided by the 0.1-S sphere). All forces have the same orientations. The long-dashed lines at 1 in (C,D) mark the force equality. For both conductance cases, the forces are zero in the center of the chamber (x = y = 0). | PMC10053818 | micromachines-14-00670-g011.jpg |
0.439619 | 9e4ce057bb17429badd4127c4a20eb0e | On the DEP force reversibility along the horizontal (A,C) and vertical (B,D) symmetry lines in the pointed-versus-pointed electrode chambers. (A,B) log-plots of the forces from Figure 9 and Figure 10. (C,D) Ratio of forces (1.0-S sphere divided by the 0.1-S sphere). Except for the short trajectory a in Figure 10A, the forces for the 1.0-S and the 0.1-S spheres have opposite orientations. The long-dashed lines at −1 in (C,D) mark the force reversibility. For both conductance cases, the forces are zero in the center of the chamber (x = y = 0). | PMC10053818 | micromachines-14-00670-g012.jpg |
0.441364 | b994a1f27e004df3bb337f48e0bd8abe | Schematic charge distributions for the 1.0-S (A,B) and 0.1-S spheres (C,D) in 0.1-S and 1.0-S media, respectively, approaching the left electrode of the plane-versus-plane electrode chamber. The numbers refer to the locations of the charges mentioned in the text. The charge views were drawn in line with Figure 3C,D and Figure 4C,D. | PMC10053818 | micromachines-14-00670-g013.jpg |
0.428482 | ccd293c513314895b74e783712de6dde | Schematic charge distributions for the 1.0-S (A,B) and 0.1-S spheres (C,D) in 0.1-S and 1.0-S media, respectively, near the left electrode of the pointed-versus- pointed electrode chamber. The bluish arrows in (C,D) indicate the field-induced streaming of the high-conductance medium, thereby providing an extra contribution to the DEP force. The numbers refer to the locations of the charges mentioned in the text. The charge views were drawn in line with Figure 7C,D and Figure 8C,D. | PMC10053818 | micromachines-14-00670-g014.jpg |
0.496448 | 2b21139ff9374c3e8654b61ee207db84 | Phylogenetic tree of 74 partial beta- and gammaherpesviral DNA polymerase gene sequences. For each sequence, the corresponding GenBank accession number (reference sequences), host species and country of origin are indicated. Horizontal lines represent the genetic distances according to the scale at the bottom. Bootstrap values ≥70% are displayed at the nodes. (A) Expanded view of partial betaherpesviral DNA polymerase gene sequences that were detected in 12 oro-pharyngeal swab and fecal samples from gerbils. A total of eight identical sequences were detected in Gerbillus sp. samples and clustered together between Rattus, Bandicota, and Apodemus cytomegalovirus sequences. This novel strain was designated Gerbillus sp. betaherpesvirus 1. There were two identical sequences found in Gerbillus nanus samples that clustered next to this strain and were named Gerbillus nanus betaherpesvirus 1. Another two identical sequences found in Gerbillus nanus samples clustered further away, next to Apodemus flavicollis herpesviruses. This strain was named Gerbillus nanus betaherpesvirus 2. Sequences that were generated in this study are marked with red diamonds. (B) Expanded view of partial gammaherpesviral DNA polymerase gene sequences. Viral strains found in seven murine organ samples were 92–99% identical to Mus musculus rhadinovirus 1 and were tentatively named Mus musculus domesticus gammaherpesvirus 1 and Mus musculus castaneus gammaherpesvirus 1. Novel gammaherpesvirus strains that were detected in seven oro-pharyngeal swabs and fecal samples from gerbils clustered in two close, but separate branches, next to rhadinovirus 1 sequences from several different rodent species. We named them Gerbillus sp. gammaherpesvirus 1 and 2, respectively. Sequences that were generated in this study are marked with blue diamonds. | PMC10054371 | viruses-15-00695-g001a.jpg |
0.47763 | 9f7ae8c115734411bbe4522e2dcacbe0 | Phylogenetic tree of partial genomic sequences of Gerbillus, Dipodillus and Meriones species. Sequences that were generated in this study are indicated by red diamonds and represent groups of several individuals. Four of the herpesvirus-positive gerbils were identified as Gerbillus nanus, and three as Gerbillus cheesmani. Eight individuals clustered together in a separate clade, 90.0% identical to Dipodillus campestris. The sequences of the remaining four individuals were not analyzable. Phylogenetic analysis was performed on a 239-bp fragment within the cytb gene. For each reference sequence, the corresponding GenBank accession number, species name and country of origin are indicated (where known). Horizontal lines represent the genetic distances according to the scale at the bottom. Bootstrap values ≥70% are displayed at the nodes. | PMC10054371 | viruses-15-00695-g002.jpg |
0.426406 | d7c22beedd6f4e73a93e5619303b972d | (a) Schematic representation of the NVU including vascular cells (endothelial cells, pericytes), basement membrane, and astrocyte end-foot in the CNS; (b) structural illustration of the basement membrane components including laminin and collagen type IV, endothelial cells and the pro-resolving signature of Annexin A1 binding to the formyl peptide receptor 2 (FPR2). Created with Biorender.com. | PMC10054605 | ijms-24-05929-g001.jpg |
0.422376 | 1cb9e3f17d44447badb17b920a53d093 | ANXA1 and laminin qualitative scoring (a,c), and integrated density measurements (b,d) on 1, 3 and 7 days after HI insult in the cerebral microvasculature; (e) representative images of consecutive sections of cerebral blood vessels stained with ANXA1 and laminin. An average of 40 fields of view per animal were analyzed. Graphs show the average integrated density per field of view (mean grey value of stained area × percentage of stained area) for ANXA1 and laminin expression in coronal brain sections. Statistical analysis was performed with a Kruskal-Wallis test followed by Dunn’s post hoc test. Bars represent mean ± SEM. Scale bar 50 μm. 400× magnification * p < 0.05, ** p < 0.01, # p = 0.06. | PMC10054605 | ijms-24-05929-g002.jpg |
0.39402 | e7802f2a7bbe4f4bac3c838584345fc6 | Collagen type IV (a) qualitative scoring; (b) integrated density measurement on 1, 3 and 7 days after HI; (c) representative images of consecutive brain sections of cerebral blood vessels stained with collagen type IV. An average of 40 fields of view per animal were analyzed. Graphs show the average integrated density (mean grey value of stained area × percentage of stained area) of collagen type IV expression in coronal brain sections. Statistical analysis was performed using a Kruskal-Wallis test followed by Dunn’s post hoc test. Bars represent mean ± SEM. Scale bar 50 μm. 400× magnification * p < 0.05, # p =0.06. | PMC10054605 | ijms-24-05929-g003.jpg |
0.417022 | 8ec19c2acf9b458ca4eebfd5b82aeb14 | Pericyte coverage surrounding brain microvasculature. (a) Qualitative scoring of PDGFRβ at 1, 3 and 7 days post HI or sham; (b) Representative microscopic images of PDGFRβ in the microvasculature at 3 and 7 days sham and HI treatment. Arrows indicate pericytes surrounding capillaries at 7d HI. Statistical analysis was performed using a Kruskal-Wallis test followed by Dunn’s post hoc test. Bars represent mean ± SEM. Scale bar 50 μm. 400× magnification * p < 0.05, # p = 0.06. | PMC10054605 | ijms-24-05929-g004.jpg |
0.456892 | 84bdb3dbafa2409f96afc1d50aacee1d | (a) Fetal sheep model with placental cotyledons (red dots) and umbilical cord (occluder) depicted; (b) Experimental design. Fetuses were instrumented at GA 102 (d-4) followed by 25 min of umbilical cord occlusion (UCO) or sham occlusion (d0) after four days of recovery. On d1, d3 and d7 fetuses were sacrificed and brain tissue was collected. Abbreviations: END—end of experiment; UCO—umbilical cord occlusion; GA—gestational age; HI—Hypoxia-Ischemia; SAL– saline; IN—instrumentation. Created with Biorender.com. | PMC10054605 | ijms-24-05929-g005.jpg |
0.414197 | e0b08a80b30d4a95a4a9a4188f066465 | Scoring systems of ANXA1, laminin, collagen type IV, and PDGFRβ in cerebral blood vessels (1 = minor, 2 = moderate, 3 = intense immunoreactivity (IR), magnification 400×, scale bar 50 μm). | PMC10054605 | ijms-24-05929-g006.jpg |
0.482782 | 767bd7ec29f944e8a9ada9a97a88c178 | Models for the functions of actin assembly and myosin activity during membrane deformation for clathrin-mediated endocytosisCartoon diagram illustrating the organization of actin filaments and Myo5 molecules at endocytic sites. Actin filaments are bound by coat proteins at the tip of the growing membrane invagination and oriented with their growing ends toward the plasma membrane, powering membrane invagination. The type I myosin Myo5 could either anchor the actin network in a favorable orientation (left) or provide an assisting force (right). | PMC10055380 | nihpp-2023.03.21.533689v3-f0001.jpg |
0.44801 | 59f0924c34e64420847caabccad87caa | In-solution, population biochemical characterization of Myo5(A) Coomassie-stained SDS-polyacrylamide gels showing example preparations of the purified Myo5 motor/lever construct and calmodulin (Cmd1, light chain) used in all experiments. (B) The actin concentration dependence of the steady-state ATPase activity of 100 nM unphosphorylated (grey circles) and phosphorylated Myo5 (black circles). Each data point represents the average of 6–7 time courses, which were 100 s each. The orange line is a best fit of the phosphorylated Myo5 data to a rectangular hyperbola. (C) Schematic pathway for the Myo5 ATPase cycle. Blue motors are in tightly bound conformations, green motors are weakly bound/unbound. (D) Example light scattering transients reporting on ATP-induced dissociation of phosphorylated (left, kobs=17 s−1) and unphosphorylated (right, kobs=64.1 s−1) actoMyo5, obtained by mixing 100 nM actoMyo5 (AM) with 94 µm and 72 µM ATP, respectively, as shown in the inset schematic. The black line is the fit of a single exponential function to the data. (E) ATP concentration dependence of dissociation of 100 nM unphosphorylated (grey circles) and phosphorylated actoMyo5 (black circles). Each data point represents 3–6 time courses averaged and fit to a single exponential decay function. The orange line is a linear best fit of the phosphorylated Myo5 data. The purple line is a best fit of the unphosphorylated Myo5 data to a rectangular hyperbola. (F) Example light scattering transients reporting ATP-induced dissociation of ADP-saturated phosphorylated (left) and unphosphorylated (right) actoMyo5, obtained by preincubating 200 nM actoMyo5 (AM) with 100 µM ADP, then mixing rapidly with 2.5 mM ATP, as shown in the inset schematic. The black line is the fit of a single exponential function to the data. (G) Velocity of actin filament gliding, measured at varying surface densities of Phospho-Myo5 (black circles, orange line) and unphosphorylated Myo5 (gray circles, purple line) in in vitro motility assays. Myosin concentrations indicate the quantity of protein incubated in the flow chamber before washing. Each data point represents the average velocity of 30 – 60 filaments, and the error bars are standard deviations. | PMC10055380 | nihpp-2023.03.21.533689v3-f0002.jpg |
0.412531 | 0e6b31f482f949c8903d39ee7ef36092 | Single molecule, optical trap analysis of Myo5 step size and kinetics(A) Cartoon schematic of the 3-bead optical trapping setup. A biotinylated actin filament is tethered between two neutravidin-coated beads that are trapped in a dual beam optical trap. This bead-actin-bead “dumbbell” is lowered onto pedestal beads that have been sparsely coated with His6 antibody to attach Myo5-motor/lever-Avi-Tev-His9. (B-D) Single Myo5 displacements of a single bead position and covariance traces, calculated using both beads, showing single molecule interactions acquired in the presence of 1 µM (B) 10 µM (C) and 1000 µM ATP. (D). Blue bars indicate attachment events as identified by covariance (gray) decreases. The threshold of event detection by the covariance traces are indicated by dashed gray lines. (E) Schematic of displacement traces depicting the 2-step nature of actomyosin displacements in the optical trap. (F-H) Binding events were synchronized at their beginnings (left) or ends (right) and averaged forward or backward in time, respectively. Measured total displacement of Myo5 was 5.0 nm at 10 µM ATP, with the 1st substep contributing a 4.8 nm displacement (arrow 1. in G) and the 2nd substep contributing a 0.2 nm displacement (arrow 2. In G). (F-H, left) Forward-averaged ensembles synchronized at the beginnings of events. (F-H, right) Reverse-averaged ensembles synchronized at the ends of events. Black and gray lines are single exponential fits in the forward and reverse ensembles, respectively. (I) Cumulative distributions of attachment durations for Myo5 at 1, 10, and 1000 µM ATP. Blue lines show cumulative frequency of attachment durations at the indicated ATP concentrations, and the red, yellow, and green lines indicate fitted exponential distributions at 1, 10, and 1000 µM ATP, respectively. 1 and 10 µM ATP were fit well to single exponentials, and the 1000 µM ATP data were best described by the sum of two exponentials. (J) Summary of rates at 1, 10, and 1000 µM ATP calculated from (F-H). Blue boxes are the fitted exponential distributions from (I), black diamonds are forward ensemble fits from (F-H, left), and gray diamonds are reverse ensemble fits from (F-H, right). At lower concentrations of ATP (1 and 10 µM), the rate of detachment is limited by ATP association, corresponding to the reverse ensemble fits, while at saturating ATP concentration (1000 µM), the detachment rate is limited by the rate of ADP dissociation, corresponding to the forward ensemble fits. (K) Summary of rates determined via single molecule optical trapping. Errors for detachment rates are 95% confidence intervals. Errors for forward and reverse ensemble fits are standard errors of the fits. *Detachment rates at 1000 µM ATP were best fit to the sum of 2 exponents. The major component of the fit (67.8 s−1) comprises 92.1% of the total with the remaining 7.9% having a rate of 11.6 s−1. | PMC10055380 | nihpp-2023.03.21.533689v3-f0003.jpg |
0.379012 | 2843b64bfe0946eebcee8b13c988e72f | Myo5 attachment lifetimes are substantially less force-dependent than other known type I myosinsAn isometric optical force clamp was utilized to determine the force-sensitivity of the detachment of Myo5 from actin. (A) Durations of individual actomyosin attachments as a function of force, plotted on a semi-log scale (B) The solid black line shows the force dependence of the detachment rates determined by MLE fitting of unaveraged points in A. For illustration purposes, attachment durations from (A) were binned by force at every 10 points, averaged, and converted to rates. Best- fit parameters were determined by MLE fitting and 95% confidence intervals were calculated via bootstrapping. The solid black line is calculated from best fit parameters (k=67.6 s−1, d=1.14 nm), while the gray shaded region is the 95% confidence interval (k=67.6−72.9 s−1, d=1.03−1.26 nm). All MLE fitting was performed on unaveraged data and was corrected for instrument deadtime. (C) The force dependent detachment rate of Myo5 (from panel B) plotted alongside the force dependent detachment rates for Myo1b, Myo1c, and β-cardiac muscle myosin, Myh7. (D) Power output for the same four myosins calculated over a range of forces by multiplying the functions from (C) by the applied force F, and the step size and duty ratios of each myosin. | PMC10055380 | nihpp-2023.03.21.533689v3-f0004.jpg |
0.41107 | 4ba95781f88640b4b3b33cd59e846bd9 | Engine scheme with deposits sampling points: engine combustion chamber: 1—cylinder head; 2, 3—pistons; exhaust manifold: 4—first cylinder; 5—fourth cylinder; 6—eight cylinder, collector: 7—exhaust pipe after compressor and cooler; 8–10—roof chimneys. | PMC10055781 | materials-16-02517-g001.jpg |
0.419259 | c6cdf3328b7a45aaab87c05e05e2d8b7 | Deposits formed on different parts of gas engine: (a) cylinder head with valves; (b) exhaust pipe in front of the chimney inlet; (c,d) roof exhaust pipe/flue. | PMC10055781 | materials-16-02517-g002.jpg |
0.450835 | 01abd2c2a2ae4fe2ad7608cea8826a12 | SEM-EDS composition microanalysis of deposits from the combustion chamber: (a) samples 1, 2, and 3 determined by mass fraction (%), K—the excited energy level of an atom; (b–d) morphological characteristics of sample 1, 2, and 3, respectively; (e) EDS spectrum (x axis—Energy (keV), y axis—Intensity (cps)) of (f) selected area for sample 1. | PMC10055781 | materials-16-02517-g003a.jpg |
0.405949 | 31f613f1347b49769aed6b86969e3410 | Deposits collected from exhaust manifold (samples 4, 5 and 6): (a) chemical composition determined by SEM-EDS microanalysis–mass fraction (%); K and L—the excited energy level of an atom; (b–d) morphological characteristics of deposit samples 4, 5, and 6. | PMC10055781 | materials-16-02517-g004.jpg |
0.404451 | 7826b9e7377640bfa00506311bf60b2b | Deposit samples collected from exhaust pipe and chimney: (a) the chemical composition determined by SEM-EDS microanalysis–mass fraction (%), K and L—the excited energy level of an atom; (b–d) Morphology of the deposits collected from exhaust pipe in front of chimney (7) and chimneys (8, 9, 10). | PMC10055781 | materials-16-02517-g005.jpg |
0.445373 | 6a4cad8dcb7240e1ace24d4c363ce3f2 | The structures of compounds 1–8 from M. cichorii. | PMC10056085 | molecules-28-02822-g001.jpg |
0.485268 | e4c141bf03234693bd6d78f9cf9168a9 | Key 1H-1H COSY and HMBC correlations of 1–5. | PMC10056085 | molecules-28-02822-g002.jpg |
0.520171 | 7a76786e40d44b51a8a8445a33285ca9 | Key ROESY correlations of 1–5. | PMC10056085 | molecules-28-02822-g003.jpg |
0.5069 | 91bf14fd605645b39d8e61017763f80e | Comparison of the calculated ECD and experimental CD spectra in MeOH. (A): The calculated ECD spectrum of (1R,2R,3S,6R)-1 at B3LYP/6-31 (d,p) level, σ = 0.20 eV; shift = −9 nm; The calculated ECD spectrum of (1R,2R,3S,6R)-5 at B3LYP/6-31 (d,p) level, σ = 0.20 eV; shift = −9 nm. (B): The calculated ECD spectrum of (1R,2R,3S,6R,1′R)-2 at B3LYP/6-31 (d,p) level, σ = 0.30 eV; shift = 0 nm. (C): The calculated ECD spectrum of (1S,2R,3S,6R)-3 at B3LYP/6-31 (d,p) level, σ = 0.30 eV; shift = +6 nm. (D): The calculated ECD spectrum of (1S,2R,3S,6R)-4 at B3LYP/6-31 (d,p) level, σ = 0.20 eV; shift = +30 nm. | PMC10056085 | molecules-28-02822-g004.jpg |
0.40594 | 30939aadcab44d089a97dc7e403256b0 | NRK-52e cell proliferation in response to compounds at 40 μM by CCK-8 assay. * p < 0.05, ** p < 0.01 compared with Control alone. | PMC10056085 | molecules-28-02822-g005.jpg |
0.42386 | 826e7b8c99f1496c8d8c61cb14240344 | Compounds attenuate renal fibrosis in TGF-β1-induced NRK-52e cells. Cells were incubated in different concentrations of the compound and then exposed to 10 ng/mL TGF-β1 for 48 h. (A–D): The protein level of Fibronectin, Collagen I, and α-SMA in NRK-52e were determined by Western blotting, and GAPDH was used as a control. Data represent mean ± SEM values of three experiments. * p < 0.05, ** p < 0.01 and **** p < 0.0001 compared with TGF-β1 alone. ## p < 0.01 and #### p < 0.0001 compared with Control alone. GW788388 (GW) was used as a positive control. | PMC10056085 | molecules-28-02822-g006.jpg |
0.407195 | ef95aa0be5384061b7f0551dfbb55ee3 | Compounds attenuate renal fibrosis in TGF-β1-induced NRK-52e cells. NRK-52e cells were incubated with TGF-β1 (10 ng/mL) for 48 h in the absence or presence of different concentrations (10 μM, 20 μM, and 40 μM) of compounds 2, 4, and 7. (A–D): The protein level of Fibronectin, Collagen I, and α-SMA in NRK-52e were determined by Western blotting, and GAPDH was used as a control. Data represent mean ± SEM values of three experiments. * p < 0.05, ** p < 0.01 compared with TGF-β1 alone. # p < 0.05 and ## p < 0.01 compared with Control alone. GW788388 (GW) was used as a positive control. | PMC10056085 | molecules-28-02822-g007.jpg |
0.384865 | cc3048554ae34c8c983b4c973e360037 | AOPs reporting Ag NPs as a potential stressor. Four AOPs showing Ag NPs as stressors were analyzed in terms of their molecular initiating events (MIE, green boxes), key events (KE, yellow boxes) and adverse outcomes (AO, orange boxes) [38,39,40,41]. This led to the identification of several pathways that are shared among these AOPs (highlighted in grey), focusing on oxidative stress, DNA damage and repair, and apoptosis. These pathways served as the basis of our AOP-oriented Ag NP toxicity-testing strategy. | PMC10056345 | toxics-11-00199-g001.jpg |
0.478735 | 5cb3bf54368b4146956497b4ad876889 | TEM images of non-digested and digested Ag NMs. Non-digested AgNKD, 0.2 mg/mL in DI H2O (a,b); AgPVP, 10 mg/mL in DI H2O (c); AgHECp, 0.1 mg/mL in DI H2O (d). Digested AgNKD (e), AgPVP (f), digested AgHECp (g), all 1 mg/mL in OGI fluid. | PMC10056345 | toxics-11-00199-g002.jpg |
0.408749 | 4d44cedbfbf043439c5eaefe77fa0dcc | Impact of non-digested and digested Ag NMs on HCT116 cell viability. Cell viability assessed by WST-1 assay 24 h after HCT116 cells were exposed to digested and non-digested Ag NPs (a–c), as well as HEC (no Ag) (d) and OGI fluid (no NMs) (e). PC refers to the positive control, i.e., amino-modified polystyrene nanoparticles (PSNH2) used at 100 µg/mL. Ag intracellular accumulation (f). HCT116 cells were exposed for 24 h to AgNKD, AgPVP and AgHEC, and intracellular Ag content was measured using ICP-MS. Values are the mean ± SD of three independent experiments with five replicates per experiment. Statistical significance, exposed vs. control, (*) p < 0.05, (***) p < 0.001, (****) p < 0.0001. | PMC10056345 | toxics-11-00199-g003.jpg |
0.405818 | 51e76baadeb64fbdac24933de10c21dd | ROS intracellular accumulation. ROS intracellular content was assessed using DHR123 assay 24 h after HCT116 cells were exposed to digested Ag NKD (a), AgPVP (b), AgHECp (c) and HECp (d) at the indicated concentrations. Positive control (PC) refers to Luperox 250 µM. Values are the mean ± SD of three independent experiments with five replicates per experiment. Statistical significance, exposed vs. control, (*) p < 0.05, (****) p < 0.0001. | PMC10056345 | toxics-11-00199-g004.jpg |
0.434423 | 5b9c378c24b049fe8db0a90a0c5b026f | The mRNA expression analysis of HCT116 cells exposed to digested Ag NMs. RT-qPCR analysis was performed in cells exposed to 12.5, 25 or 50 µg/mL of digested AgNKD, AgPVP, AgHECp or HECp, focusing on oxidative stress markers (CAT, SOD2, GCLM, GSR, HO-1), inflammation (IL-8) and metal homeostasis (MT-1 and MT-2). Statistical significance, exposed vs. control, (*) p < 0.05. | PMC10056345 | toxics-11-00199-g005.jpg |
0.408914 | db914d740bf742548418f7ff44d7b421 | Genotoxicity of non-digested and digested Ag NMs and HEC. Genotoxicity was assessed using the comet assay (a) and 53BP1 assay (b), in HCT116 cells exposed for 24 h to 12.5, 25 or 50 µg/mL of non-digested or digested Ag NMs. Positive controls: 300 µM MMS (comet assay), 18.74 ± 3.62%Tail DNA, 50 µM etoposide (53BP1 assay), fold change 8.13 ± 1.03 relative to control. Statistical significance, exposed vs. control, (**) p <0.01, (***) p < 0.001, (****) p < 0.0001. | PMC10056345 | toxics-11-00199-g006.jpg |
0.436168 | e1553464552f479b9dec45aee12a6eb3 | Analysis of cell cycle and distribution of cells in the G2, S, G0/G1 and sub-G1 phases. Cells were exposed to Ag NMs or to 0.3 µM of staurosporine (CTL+) for 24 h, then labelled with propidium iodide and analyzed by flow cytometry. Graph represents mean ± standard deviation for three independent experiments with three replicates per experiment. Statistical significance: (**) p <0.01, (***) p < 0.001, and **** p < 0.0001, exposed vs. control. G1: AgNKD vs. AgPVP, AgPVP vs. AgHEC, S: AgNKD vs. AgHEC, AgPVP vs. AgHEC, G2/M: AgNKD vs. AgPVP, AgPVP vs. AgHEC, all (****) p < 0.0001. | PMC10056345 | toxics-11-00199-g007.jpg |
0.425062 | 83fd395c964443d3b375a6044a70b19a | Characterization of C-ZLCH. (a) SEM photograph. (b) EDS spectra. (c) Zeta potential. (d) Particle size distribution. | PMC10057389 | materials-16-02532-g001.jpg |
0.404306 | 7c4c09ae2dff4b2ca81380afc6a19f00 | FTIR spectra of C-ZLCH before and after Cu(II) and Cr(VI) adsorption. | PMC10057389 | materials-16-02532-g002.jpg |
0.438611 | 13da9e20787e463b9562b7effdb5d820 | Effect of initial pH on Cu(II) and Cr(VI) adsorption. (C-ZLCH: 0.01 g, initial metal ion: 10 mg/L, volume (mL): 50, temperature: 30 °C, and time: 30 min). | PMC10057389 | materials-16-02532-g003.jpg |
0.441835 | 3e350bae00f04907a81012db809938a5 | Effect of initial concentration on metal ions adsorption. (C-ZLCH: 0.01 g, volume (mL): 50, pH: 8.1 for Cu(II), pH: 6.7 for Cr(VI), temperature: 30 °C, and time: 30 min). | PMC10057389 | materials-16-02532-g004.jpg |
0.44431 | 77d832a31bb9470595fabce117f50f39 | Linear curves of adsorption isotherm studies. (a): Langmuir, (b): Freundlich. (C-ZLCH: 0.01 g, volume (mL): 50, pH: 8.1 for Cu(II), 6.7 for Cr(VI), temperature: 30 °C, and time: 30 min). | PMC10057389 | materials-16-02532-g005.jpg |
0.507866 | 804b40042c2948d493f311413cd4fe53 | Effect of contact time on metal ions adsorption. (C-ZLCH: 0.01 g, volume: 50 mL, metal ions concentration: 25 mg/L, pH: 8.1 for Cu(II), 6.7 for Cr(VI), temperature: 30 °C, and time: 30 min). | PMC10057389 | materials-16-02532-g006.jpg |
0.412529 | 8d47d0ed68134fd9b3b498d73e22d5ed | Linear curves of adsorption kinetic studies. (a): pseudo-first order, (b): pseudo-second order. (C-ZLCH: 0.01 g, volume: 50 mL, metal ions concentration: 25 mg/L, pH: 8.1 for Cu(II), 6.7 for Cr(VI), temperature: 30 °C). | PMC10057389 | materials-16-02532-g007.jpg |
0.466867 | 3c0ae8f4490340a49461cad114b58b4c | Effect of chemical substances on Cu(II) and Cr(VI) adsorption. [Blank: no presence of chemical substances, C-ZLCH: 0.01 g, volume: 50 mL, metal ions concentration: 25 mg/L, pH: 8.1 for Cu(II) at 60 min, pH: 6.7 for Cr(VI) at 90 min, temperature: 30 °C]. | PMC10057389 | materials-16-02532-g008.jpg |
0.46419 | 381a065f52b9453c8b811ef288d84021 | Effect of AR88 on Cu(II) and Cr(VI) adsorption. [Blank: no presence of AR88 dye, pH 8.1 for Cu(II) and pH 6.7 for Cr(VI), C-ZLCH: 0.01 g, volume: 50 mL, metal ions concentration: 25 mg/L, pH: 8.1 for Cu(II) at 60 min, pH: 6.7 for Cr(VI) at 90 min, temperature: 30 °C]. | PMC10057389 | materials-16-02532-g009.jpg |
0.466556 | ca5db186f122437bb1462ed266134f60 | Different techniques in tissue culture for plant regeneration can be utilized for the selection and genetic transformation of plants. Starting from explants under selection mediums, direct organogenesis can be achieved (A and B) or indirect organogenesis (C and D) through an intermediate callus phase. Further, callus can be used to form intact plantlets through an embryonic pathway or in suspension culture directly or via protoplast culture techniques in genetic transformation attempts. | PMC10057563 | life-13-00780-g001.jpg |
0.435272 | a1e8c2bd7d8a44f3b1e3ba0269c43e79 | Results of testing the academic model: two asterisks (**) p < .01, three asterisks (***) p < .001. Non-significant cross-lagged paths and within-time covariances are not shown for the parsimony of the model | PMC10057683 | 10734_2023_1029_Fig1_HTML.jpg |
0.452158 | 71fe8220e9054f118bf3881411084dfc | Results of testing the social model: one asterisk (*) p < .05, two asterisks (**) p < .01, three asterisks (***) p < .001. Non-significant cross-lagged paths and within-time covariances are not shown for the parsimony of the model | PMC10057683 | 10734_2023_1029_Fig2_HTML.jpg |
0.481136 | cabd18dc3ec643f083f7be0d2b461af1 | Flowchart of article screen and selection process (PRISMA). | PMC10057722 | life-13-00849-g001.jpg |
0.401146 | 86be9014ede44fb8a03b66349cec80c4 | Risk of bias summary (per protocol): a review of the authors’ assessments of each risk of bias item for each included study. In these traffic light plots green indicates low risk of bias, while yellow indicates some concerns and red indicates high risk of bias. | PMC10057722 | life-13-00849-g002.jpg |
0.450821 | 90158e7a3f9441e48a68cb02da3d3db9 | Risk of bias graph (per protocol): a review of authors’ judgements about each risk of bias item presented as percentages across all included studies. | PMC10057722 | life-13-00849-g003.jpg |
0.433548 | d48aef216aa14ec89d9db1c9375b4184 | Risk of bias summary (intention-to-treat): a review of authors’ judgements about each risk of bias item for each included study. In these traffic light plots green indicates low risk of bias, while yellow indicates some concerns and red indicates high risk of bias. | PMC10057722 | life-13-00849-g004.jpg |
0.378103 | 1c45301c0b1e415286417fe659a7b76a | Risk of bias graph (intention-to-treat): a review of authors’ judgements about each risk of bias item presented as percentages across all included studies. | PMC10057722 | life-13-00849-g005.jpg |
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