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0.387796 | a07566bb81864c1aa4c3d0f223425ee7 | Effect of the printing parameters on the filament width. Pressure (110, 120 and 130 kPa) and speed (1, 2 and 3 mm/s) effects on the filament (A) printability and (B) width. | PMC10338535 | 41598_2023_38323_Fig6_HTML.jpg |
0.475225 | 26d7a1969dac45d896e0e2188065dae9 | Comparison of mechanical properties of printed and molded samples: (A) fabricated samples; (B) stress-stretch behavior during the third cyclic compression-tension; (C) maximum nominal stresses in compression and tension; (D) hysteresis area, significance value **p < 0.01, ***p < 0.001 (n=5). | PMC10338535 | 41598_2023_38323_Fig7_HTML.jpg |
0.428298 | e9fd78d36d664e6182f246db96eb06f5 | Normalized stress relaxation behavior of printed and molded samples in compression and tension (n=5). | PMC10338535 | 41598_2023_38323_Fig8_HTML.jpg |
0.451013 | 936485b6fdb44a41898e1137e8ddc74e | Design parameters and CAD models for printing different mesostructures using AG bioinks. The filament diameter, pore size and layer height were varied to obtain seven different structures. | PMC10338535 | 41598_2023_38323_Fig9_HTML.jpg |
0.439158 | b842b3c8ce234307896f345a5aa78a19 | The MOM1 complex colocalizes with RdDM sites.a Metaplots and heatmaps representing ChIP-seq signals of Pol V, MOM1-Myc, PIAL2-Myc, PHD1-FLAG, and AIPP3-FLAG over Pol V peaks (n = 10,868). ChIP-seq signal of control samples were subtracted for plotting. b Screenshots of Pol V, MOM1-Myc, PIAL2-Myc, AIPP3-FLAG and PHD1-FLAG ChIP-seq signals with control ChIP-seq signal subtracted and CG, CHG, and CHH DNA methylation level by whole genome bisulfite sequencing (WGBS) over representative RdDM sites. c Volcano plot showing proteins that have significant interactions with MOM1 as detected by crosslinking IP-MS, with RdDM pathway components and MOM1 complex components labeled. Crosslinking IP-MS of Col-0 plant tissue was used as control. The empirical Bayes test performed by LIMMA was used for statistical analysis. d AIPP3-FLAG ChIP-seq peaks were divided into two groups: Group 1 peaks (n = 3,075) have MOM1-Myc ChIP-seq signal enriched and Group 2 peaks (n = 523) have no enrichment of MOM1-Myc ChIP-seq signal. Metaplots and heatmaps representing ChIP-seq signals of MOM1-Myc, AIPP3-FLAG, PHD1-FLAG and PHD3-FLAG over these two groups of AIPP3 peaks. ChIP-seq signal of control samples were subtracted for plotting. Source data are provided as a Source Data file. | PMC10338684 | 41467_2023_39751_Fig1_HTML.jpg |
0.431652 | 941a18f7d43c4a6d83e37ca75994d628 | ZF tethering of the MOM1 complex to the FWA promoter triggers DNA methylation and FWA silencing.a Flowering time of fwa, Col-0 and representative T2 lines of MOM1-ZF, MOM2-ZF, PIAL1-ZF, PIAL2-ZF and PHD1-ZF in the fwa background. The numbers of independent plants (n) scored for each population and detailed statistics of flowering time comparison between different populations are listed in Supplementary Data 5. b qRT-PCR showing the relative mRNA level of FWA gene in the leaves of fwa plants, and four T2 plants of MOM1-ZF, MOM2-ZF, PIAL1-ZF, PIAL2-ZF and PHD1-ZF in the fwa background. Bar plots and error bars indicate the mean and standard error of three technical replicates, respectively, with individual technical replicates shown as dots. c CG, CHG, and CHH DNA methylation levels over FWA promoter regions measured by BS-PCR-seq in Col-0, fwa and representative T2 plants of MOM1-ZF, MOM2-ZF, PIAL1-ZF, PIAL2-ZF and PHD1-ZF in the fwa background with (+) or without (-) corresponding transgenes. Pink vertical boxes indicate ZF binding sites. d Metaplots showing relative variations (sample minus fwa control) of CG, CHG, and CHH DNA methylation levels over ZF off-target sites in representative T2 plants of MOM1-ZF, MOM2-ZF, PIAL1-ZF, PIAL2-ZF and PHD1-ZF in the fwa background measured by WGBS. Source data are provided as a Source Data file. | PMC10338684 | 41467_2023_39751_Fig2_HTML.jpg |
0.408329 | 2ca333529e694c81a5b3485c74da2dea | MOM1-ZF recruits the Pol V arm of the RdDM machinery via MORC6.a Flowering time of fwa, Col-0, and T1 lines of PIAL2-ZF and MOM1-ZF in the fwa mutant backgrounds as well as in backgrounds of fwa introgressed mutants, including nrpd1, suvh2/9, morc6, dms3, drd1, rdm1, nrpe1 and drm1/2. The numbers of independent plants (n) scored for each population and detailed statistics of flowering time comparison between different populations are listed in Supplementary Data 5. b Metaplots and heatmaps representing ChIP-seq signals of Pol V and MORC6-Myc over Pol V peaks (n = 10,868). ChIP-seq signal of control samples were subtracted for plotting. c Screenshots of Pol V, MORC6-Myc, MOM1-Myc and PIAL2-Myc ChIP-seq signals with control ChIP-seq signals subtracted and CG, CHG, and CHH DNA methylation level by WGBS over a representative RdDM site. d Yeast Two-Hybrid assay showing in vitro direct interactions between PIAL1 and PIAL2 with MORC6 and the MOM1 CMM2 domain, as well as between PIAL2 and MOM2. This experiment was repeated twice independently with similar results. e PIAL2 and MORC6 in vivo interaction shown by co-immunoprecipitation (Co-IP) in MORC6-FLAG and PIAL2-Myc crossed lines. This experiment was repeated twice independently with similar results. Source data are provided as a Source Data file. | PMC10338684 | 41467_2023_39751_Fig3_HTML.jpg |
0.484323 | c7e921d6f8b2438292a44e453ce2fda4 | The MOM1 complex facilitates the process of transgene silencing.a Flowering time of FWA transgene T1 plants in the Col-0, nrpe1-11, mom1-3, pial1/2, mom2-2, aipp3-1 and phd1-2 genetic backgrounds. b Relative FWA mRNA level (upper panel) and relative FWA promoter DNA quantity after McrBC treatment (lower panel) of four late-flowering FWA transgene containing T1 plants in the mom1-3 and pial1/2 genetic backgrounds. FWA transgene containing T1 plants in the Col-0 and nrpe1-11 backgrounds were used as controls. Bar plots and error bars indicate the mean and standard error of three technical replicates, respectively, with individual technical replicates shown as dots. c Flowering time of FWA transgene T2 plants in the Col-0, nrpe1-11, mom1-3 and pial1/2 genetic backgrounds. For a, c, the numbers of independent plants (n) scored for each population and detailed statistics of flowering time comparison between different populations are listed in Supplementary Data 5. Source data are provided as a Source Data file. | PMC10338684 | 41467_2023_39751_Fig4_HTML.jpg |
0.492775 | 99640f0d2885474d8ebea395e69358fe | The MOM1 complex influences DNA methylation and chromatin accessibility at some endogenous RdDM sites.a Boxplots and heatmaps showing the variation of CG, CHG, and CHH DNA methylation in phd1-2, aipp3-1, mom2-2, mom1-3, pial1/2, morc6-3 and morchex mutants vs Col-0 wild type over hypo CHH hcDMRs of the morchex mutant (n = 520). b the number and heatmap of overlapping of hypo CHH hcDMRs among aipp3-1, mom2-2, mom1-3, pial1/2, morc6-3 and morchex mutants over morchex mutant hypo CHH hcDMRs (n = 520). c Boxplot representing the expression level (RNA-seq signal normalized by RPKM) of the genomic bins of 1 kb from hypo CHH hcDMRs (n = 520) of the morchex mutant in Col-0, aipp3-1, phd1-2, pial1-2, pial2-1, mom2-2, mom1-3, pial1/2, morc6-3 and morchex mutants. d Metaplots and heatmaps representing ATAC-seq signal (mom1-3 minus Col-0), MOM1 ChIP-seq signal and Pol V ChIP-seq signal (subtracting control ChIP-seq signal) over regions with higher ATAC-seq signals in mom1-3 (n = 342) and shuffled regions. e Screenshots of ATAC-seq signals of Col-0 and mom1-3, ChIP-seq signals of MOM1-Myc and Pol V (subtracting control signal) as well as CG, CHG, and CHH DNA methylation level by WGBS over a representative RdDM site. In box plots of a and c, center line represents the median; box limits represent the 25th and 75th percentiles; whiskers represent the minimum and the maximum. Source data are provided as a Source Data file. | PMC10338684 | 41467_2023_39751_Fig5_HTML.jpg |
0.474328 | ba5664ef92e043619ffdc0b7e1ca3321 | MOM1 complex components and MORCs shows genomic distribution patterns distinct from that of the RdDM component Pol V.a Metaplots of ChIP-seq signals of Pol V, PIAL2, MOM1, MORC4, MORC6, and MORC7 over TEs in euchromatic arms (n = 16,661) and TEs in pericentromeric regions (n = 14,525), with control ChIP-seq signals subtracted. b Metaplots and heatmaps of ChIP-seq signals of Pol V, MOM1, PIAL2, MORC4, MORC6, MORC7, PHD1, and AIPP3 over Cluster 1 and Cluster 2 ChIP-seq peaks of MOM1 and Pol V, with control ChIP-seq signals subtracted. c, Metaplots of ChIP-seq signals of H3K4me3 and H3Ac (normalized to H3), as well as ATAC-seq signal of Col-0 over Cluster 1 and Cluster 2 peaks of MOM1 and Pol V. d Metaplots and heatmaps of MOM1 ChIP-seq signal (with control ChIP-seq signal subtracted), H3K4me3 ChIP-seq signal (normalized to H3) and ATAC-seq signal of Col-0 plants over genes close to Cluster 2 peaks and shuffled control regions. e Screenshots of Pol V, MOM1, PIAL2, MORC6 ChIP-seq signals with control ChIP-seq signals subtracted, H3K4me3 and H3Ac ChIP-seq signals, ATAC-seq signal of Col-0 plants, as well as CG, CHG, and CHH DNA methylation level by WGBS over a representative genomic region containing both Cluster 1 and Cluster 2 ChIP-seq peaks. | PMC10338684 | 41467_2023_39751_Fig6_HTML.jpg |
0.472713 | 7aaa25fd2f5643a693f48e6a7a450275 | Working model of MOM1 complex.The MOM1 complex is first loaded onto RdDM target sites through an unknown mechanism to facilitate the binding of the MORC6 protein. MORC6 would then enhance the recruitment the Pol V arm of the RdDM machinery to methylate target DNA, by topologically entrapping the DNA as well as directly interacting with RdDM components, thus serving as a tethering factor29,37,51,52. | PMC10338684 | 41467_2023_39751_Fig7_HTML.jpg |
0.429507 | cdeb779ea5034a79b077db423d2adac7 | Schematic of the invitation model in an example where (for simplicity) the site is served by three GP practices (clusters). There is an age/sex distribution of people to potentially invite within each cluster. This is illustrated using a histogram, where the solid blocks represent the male population and the hatched blocks the female population, with increasing age from left to right and from lighter to darker shades. The problem is to determine the number to invite to attend appointments at the site from each age/sex band (group) and GP (cluster). | PMC10338700 | 10.1177_17407745231167369-fig1.jpg |
0.472052 | 4f542ed85835435e8cfcdf6f08967262 | Diagram of study enrollment from 2016 to 2018 | PMC10339501 | 13044_2023_160_Fig1_HTML.jpg |
0.536295 | dcd4764031274b7e8bc8d4f13a2d5abd | (A) TSH levels decrease from hyper-acute to acute and chronic stages of stroke; (B) fT3 levels decrease from hyper-acute stage to acute stage, and then increase in chronic stage of stroke; (C) fT4 levels decrease from hyper-acute stage to acute stage, and increase in the chronic stage of stroke | PMC10339501 | 13044_2023_160_Fig2_HTML.jpg |
0.421766 | acfa4b30753141c3ae307e40dfd632c1 | Study timeline flowchart with time points and filming time points, local anesthesia, and analgesia protocol. | PMC10339886 | animals-13-02136-g001.jpg |
0.491288 | 05d02bac72564234ac15a858635b6bf3 | Percentage distribution of scores for each item on the UGAPS in the perioperative period. (A–F) Pain-related behaviors in which 0—absent and 1—present; (G–J) Maintenance behaviors where 0—present and 1—absent. | PMC10339886 | animals-13-02136-g002a.jpg |
0.560298 | cb98e0525c864843a5a482e2563c2bd8 | Boxplots of the scores (median/amplitude) of the UGAPS over time. The top and bottom box lines represent the interquartile range (25 to 75%); the line within the box represents the median; the extremes of the whiskers represent the minimum and maximum values; black lozenges (♦) represent the mean, and black circles (●) represent outliers. Different letters express significant differences between time points where a > b > c > d. | PMC10339886 | animals-13-02136-g003.jpg |
0.499351 | ce0d418d83bd49faa208bf64e2f6183d | Receiver operating characteristic (ROC) curve of two graphs with the diagnostic uncertainty zone for the UGAPS. The diagnostic uncertainty zone scores ranged from 2.5 to 3.5; therefore, scores ≤2 indicate truly negatives (goat without pain) and ≥4 indicate truly positives (goat suffering pain). A Youden index ≥3 (>2.5) represents the cut-off point for indication of rescue analgesia. | PMC10339886 | animals-13-02136-g004.jpg |
0.366311 | 182435180322453c884bc93641861855 |
Number of treatment cycles per treatment group.
(A) Number of treatment cycles received by NSCLC patients in the the extended dosing of pembrolizumab group during the COVID-19 pandemic group. (B) Number of treatment cycles received by NSCLC patients in the standard dosing of pembrolizumab group during the COVID-19 pandemic.ED: Extended dosing; NSCLC: Non-small-cell lung cancer; SD: Standard dosing. | PMC10340130 | figure1.jpg |
0.444575 | 0dd0bb1ca01449aaaefe72c23d81554f |
Overall survival: Kaplan–Meier curve for extended versus standard dosing of pembrolizumab in patients with non-small-cell lung cancer during the COVID-19 pandemic.
IO: Immuno-oncology (i.e., pembrolizumab). | PMC10340130 | figure2.jpg |
0.427108 | 085c69b27d0d492894797df6c18e40ac | Change in serum ferritin levels between ECMO survivors and non-survivors—ICU admission vs. lab results within 6 h before ECMO cannulation (RM-ANOVA, survivors vs. non-survivors at pre-ECMO, PTukey = 0.034). | PMC10340404 | diagnostics-13-02203-g001.jpg |
0.44065 | 7e09a849f2ce45fa905aa05ca1c2f0e7 | Change in WBC count between ECMO survivors and non-survivors—ICU admission vs. lab results within 6 h before ECMO cannulation (RM-ANOVA, non-survivors at admission vs. pre-ECMO, PTukey < 0.001). | PMC10340404 | diagnostics-13-02203-g002.jpg |
0.445185 | ada34f7ec36145e2b27e60a03cf0089d | Kaplan–Meier survival curve depicting survival rates of patients treated with ECMO and the propensity matched cohort of patients ventilated using conventional lung protective mechanical ventilation (Log-rank, p = 0.4). | PMC10340404 | diagnostics-13-02203-g003.jpg |
0.435748 | 771ba61a5ce34a749c949c2024b8c9d1 | Social Support and Commitment to Life and Living over 2 years, Israelis ≥75 Years of Age. | PMC10341178 | healthcare-11-01965-g001.jpg |
0.415558 | 51b730ea077e45cdb128805f8614a1c6 | Bioinformatics analysis of the gene ClNAC100: (a) Prediction of ClNAC100 coding protein domain. (b) Prediction of ClNAC100 protein signal peptide. (c) Prediction of ClNAC100 protein transmembrane domain. (d) Sequence alignment of ClNAC100 and NACs from other plants, and the black box represents 100% homology. * means the intermediate value scale between two numerical scales. | PMC10341961 | ijms-24-10486-g001a.jpg |
0.434031 | 5213dc9ad884402dac837266b52a6c2a | Analysis of ClNAC100 transcriptional activity: (a) Cloning of ClNAC100 NAC domain and TR-region. (b) Validation of transcriptional autoactivation of ClNAC100: different truncations of ClNAC100 fused to the GAL4 DNA binding domain in pGBKT7 vector. Transactivation activity assay of ClNAC100 in yeast strain Y2H Gold on the SD/-Trp/-Leu/-Ade/X-α-gal medium. | PMC10341961 | ijms-24-10486-g002.jpg |
0.489096 | 6af5ebd95053423f8b2a46a1fb9f265a | Expression profile of ClNAC100: (a) Expression of ClNAC100 in the Pi-deficient treatment transcriptome of Chinese fir root (CK*–NP*), ClNAC100 expression in the roots of Chinese fir under the same treatment as the Pi-deficient transcriptome (CK-NP, ** p < 0.01). (b) Expression patterns of ClNAC100 at different phosphate deficiency times (A~I respectively represent 0 h (CK), 2 h, 4 h, 8 h, 12 h, 1 d, 3 d, 5 d, 7 d. (c) Expression patterns of ClNAC100 under ABA. (d) Expression patterns of ClNAC100 under JA. (e) Analysis of specific expression of ClNAC100 in different parts of Chinese fir. Note: lowercase letters on the error line (a, b, and c) respectively represent significant differences between groups. | PMC10341961 | ijms-24-10486-g003.jpg |
0.466066 | 632c0dead1a746cfbb383a0677595052 | ClNAC100 promoter analyses: (a) Visualization of ClNAC100 promoter cis-element. (b) The expression vectors P1-PBI121, P2-PBI121, P3-PBI121, and P4-PBI121 with deletion of 5 promoters were constructed. (c) Analysis of promoter activity of ClNAC100: 35S-PBI121 is the positive control, no treatment (promoter less) is the negative control. The blue spots show the expression of the GUS gene driven by promoter fragments of different lengths in the vector on tobacco leaves. | PMC10341961 | ijms-24-10486-g004a.jpg |
0.416882 | 8e34145d11ab4a05999c22e4251f1d05 | Insert promoter clone and validation of bait strains: (a) The cloned long promoter fragments were divided into three short fragments Pro1, Pro2, and Pro3 according to the cis-element distribution. (b) Identification of positive strains (amplified band size 1346 bp+ insert length), Pro1: pAbAi-Pro1 linearized plasmid transformed Y1H positive monoclonal PCR product; Pro2: pAbAi-Pro2 linearized plasmid transformed Y1H positive monoclonal PCR product; Pro3: pAbAi-Pro3 linearized plasmid transformed Y1H positive monoclonal PCR product. | PMC10341961 | ijms-24-10486-g005.jpg |
0.395607 | ea6b0f0bb90f48ea9d2c8691175ebc90 | (a) Expression of AbAr gene in bait strain, identification of the minimum inhibitory concentration of AbA in different bait strains. (b) PCR validation of several colonies: bands of different sizes indicate different proteins to which the ClNAC100 promoter may bind. | PMC10341961 | ijms-24-10486-g006.jpg |
0.425647 | 66db1aed6af345109f96515a31cf78dd | An 82-year-old patient presenting with a fragility fractures of the pelvis (FFP) type IV or OF4 (OF-Pelvis classification) with displaced bilateral posterior lesions. The bilateral fractures are seen in the computer tomography (CT) (left side) and magnetic resonance imaging (MRI) (right side). The patient suffered from a low-energy trauma, falling on her back. | PMC10342505 | jcm-12-04445-g001.jpg |
0.454487 | db1fcc09635f4c4c9156a93801cb562a | Modified after [23,24]: The spinopelvic parameters are lumbar lordosis (LL), pelvic incidence (PI), pelvic tilt (PT) and sacral slope (SS). | PMC10342505 | jcm-12-04445-g002.jpg |
0.420492 | 25d4ca54d05843c89c3b6965322d8e2c | Spinopelvic parameters of LL, PT, SS and PI were analyzed for all patients. Measurement was conducted in a standing lateral radiograph of the spine and pelvis in which the spine from T12 to S1 and both femoral heads were visible. | PMC10342505 | jcm-12-04445-g003.jpg |
0.433912 | 8bb5e0b3b3944363b5876bf99ef18896 | Type II FFP (fragility fracture of the pelvis) was observed in 44 patients (77.2%) according to the FFP classification system [9] and OF-Pelvis classification system [10]. | PMC10342505 | jcm-12-04445-g004.jpg |
0.46247 | cba52431171b4bdb9f43cfd0be3996e1 | The mean lumbar lordosis and pelvic incidence of the study’s population were significantly (p < 0.01) different. | PMC10342505 | jcm-12-04445-g005.jpg |
0.399896 | 7c1dfa03ad594d02af7b271992854a20 | The spinopelvic parameters in the present study compared to the spinopelvic parameters in previous studies. LL (47.9°) and SS (34.2°) in the present study were significantly reduced (p < 0.01). PI (64.4°) and PT (29.4°) were significantly increased (p < 0.01). | PMC10342505 | jcm-12-04445-g006.jpg |
0.393941 | 642d9619dfb548279acc40545bbfb160 | Modified after [23,24]: The spinopelvic parameters of asymptomatic patients are drawn on the left side. The spinopelvic parameters of patients suffering from FFPs are drawn on the right side. In patients with FFPs, LL and SS are reduced, whereas PI and PT are increased. A higher PT and lower SS result from the backward rotation of the pelvis as a compensatory mechanism. | PMC10342505 | jcm-12-04445-g007.jpg |
0.496278 | 35af68877d1c44f9843b2b4e43540c0f | Kaplan–Meier analysis for all-cause mortality of HFrEF patients in relation to plasma catestatin concentration. | PMC10342751 | jcm-12-04208-g001.jpg |
0.479677 | 670e64ecd6544c529715069b6fe291b6 | Kaplan–Meier analysis for all-cause readmission of HFrEF patients in relation to plasma catestatin concentration. | PMC10342751 | jcm-12-04208-g002.jpg |
0.496864 | d14848c0ccac4f20b36da2faf1117c49 | Kaplan–Meier analysis for composite endpoint of HFrEF patients in relation to plasma catestatin concentration. | PMC10342751 | jcm-12-04208-g003.jpg |
0.436709 | ad80b4c5041040368051671f79aedc97 | Correlation of catestatin and NT-proBNP, R = 0.439, p < 0.001. Individual data points represent Box-Cox transformed values. Solid red line—regression line estimated from the sample population. Red dashed lines—confidence curves = 0.95. | PMC10342751 | jcm-12-04208-g004.jpg |
0.428108 | 829cfc824c744bd386675a7f1b6b31f2 | Examples of stimuli used in Experiment 1.Upper: the upright (left) and inverted (right) images in the intact scene condition where a face appears in an intact scene. Lower: the upright (left) and inverted (right) images in the scrambled scene condition where a face appears in a jumbled scene. | PMC10343060 | pone.0288253.g001.jpg |
0.401602 | dbe37e094c6641f5bf46b4ac59076c5c | (A) Mean preference scores for the upright face in infants aged 4 to 5 months and 6 to 7 months. The gray bars indicate the upright preference in an intact scene, and the white bars represent the upright preference in a scrambled scene. The error bars show mean standard errors (SE). Significant differences versus a chance level of 50% are indicated by asterisks (p-value for multiple comparisons, using Bonferroni correction for multiple comparisons, α level of 0.05 / 4 = 0.0125). (B) Individual data showing the percentage of preference for upright images. The horizontal axis represents age in days. The red circles and the blue squares represent the results for the intact and scrambled scene conditions, respectively. The red line is the regression line fitted to the red circles. The blue line is the regression line fitted to the blue squares. | PMC10343060 | pone.0288253.g002.jpg |
0.398203 | bc8b7a20681347f589120a5019f4011d | Examples of stimuli used in Experiment 2.Left: intact scene image from which the cell containing a face has been removed. Right: scrambled scene image from which the cell containing a face has been removed. | PMC10343060 | pone.0288253.g003.jpg |
0.444403 | 31a27566d0d249a3af23dce018bcf6fe | Mean preference scores for the intact scene images without faces.The error bars indicate mean standard error (SE). | PMC10343060 | pone.0288253.g004.jpg |
0.483756 | 7995ef48455d44cbad49f48afb403428 | Schematic diagram of robot and environment. | PMC10343087 | pone.0287484.g001.jpg |
0.436876 | 7ee5845283ae4646b6cd03d6030aa4fe | Parameter identification and control algorithm. | PMC10343087 | pone.0287484.g002.jpg |
0.41178 | 3018ff8982324975afcc2c446ae57993 | Excitation trajectory. | PMC10343087 | pone.0287484.g003.jpg |
0.449591 | bfec72c642d24fc3bcb16625302ef697 | Joint torque. | PMC10343087 | pone.0287484.g004.jpg |
0.440646 | 5a9134e86bd040178e02e58c7580fb3e | Errors in the measured and computed torques. | PMC10343087 | pone.0287484.g005.jpg |
0.440772 | 480e99e2560a4975ba8cbb1d66c516ed | Excitation trajectory for further verification. | PMC10343087 | pone.0287484.g006.jpg |
0.431638 | b88a5b470112478baaaa4fd6f1a00ce5 | Joint torque for further verification. | PMC10343087 | pone.0287484.g007.jpg |
0.427197 | 6481e0a336504d9e86e0f61b0b2a2549 | Errors in the measured and computed torques for further verification. | PMC10343087 | pone.0287484.g008.jpg |
0.429815 | 7820412d6cfa4af6a293038b1de57e20 | Trajectory of 1st joint. | PMC10343087 | pone.0287484.g009.jpg |
0.501476 | fe735a4e41454c69a0b2b4933b833592 | Trajectory of 2nd joint. | PMC10343087 | pone.0287484.g010.jpg |
0.487745 | f8917551b39c4d8a85b9ff4b18ffead8 | Trajectory of 3rd joint. | PMC10343087 | pone.0287484.g011.jpg |
0.482608 | 03df2e183a934451a5c959f6eaea94e7 | Trajectory of 4th joint. | PMC10343087 | pone.0287484.g012.jpg |
0.47467 | 4c0192872a464ff3b07349a0fc1769b5 | Trajectory of 5th joint. | PMC10343087 | pone.0287484.g013.jpg |
0.459296 | 452da79d6dfd44a1b7575f40202c274c | Trajectory of 6th joint. | PMC10343087 | pone.0287484.g014.jpg |
0.428903 | 7586201ff7964867af35cadd8f9122e7 | Transmittance according to the wavenumber for the precursor material and AC. | PMC10343689 | molecules-28-05232-g001.jpg |
0.593597 | db104c8ad3bc46cea22e3f81d44bfae7 | XRD patterns for precursor and AC. | PMC10343689 | molecules-28-05232-g002.jpg |
0.421735 | 92299d3dcbd649c6bd7fa6c476e33359 | SEM images of precursor material (A,C), and activated carbon (B,D). | PMC10343689 | molecules-28-05232-g003.jpg |
0.476533 | d046ba0bb0d244a08fbe70df6be6900b | Effect of AC dosage on PROP adsorption (V = 25 mL, T = 298.15 K, natural solution pH, C0 = 25 mg L−1, and t = 120 min). | PMC10343689 | molecules-28-05232-g004.jpg |
0.41996 | da3571a6f7494e7a8c4302aa9517e591 | Effect of pH on PROP adsorption (V = 25 mL, T = 298.15 K, Dads = 0.7 g L−1, C0 = 25 mg L−1, and t = 120 min). | PMC10343689 | molecules-28-05232-g005.jpg |
0.49814 | b3766328385e4d7abf6148718d5c247f | Equilibrium adsorption data and Langmuir model prediction for PROP adsorption on activated carbon according to the system temperature (T = 298.15, 308.15, 318.15, and 328.15 K, pH = 10, Dads = 0.7 g L−1, and t = 300 min). | PMC10343689 | molecules-28-05232-g006.jpg |
0.495748 | aafdebb7b0254ae8bffd25bc77df57f2 | PROP adsorption kinetic curves on activated carbon (T = 298.15 K, Dads = 0.7 g L−1, pH = 10, and V = 25 mL). | PMC10343689 | molecules-28-05232-g007.jpg |
0.422408 | 7e76a7cb0b774541904d66c6a1503573 | Percentage of removal change according to the cycle number (T = 298.15 K, Dads = 0.7 g L−1, pH = 10, and V = 25 mL). | PMC10343689 | molecules-28-05232-g008.jpg |
0.4875 | 16253e07c64e4954826e05ac94d336ce | Proposed adsorption mechanism that may occur at the surface of the activated and the adsorbed propranolol molecules. | PMC10343689 | molecules-28-05232-g009.jpg |
0.486196 | a7b1eb70614343f089a1189ba7627037 | Schematic of shear test: (a) sample preparation; (b) testing device. | PMC10343823 | materials-16-04809-g001.jpg |
0.408692 | aa0ab111cbe5455fbc85cf09c21e4b6e | Microstructure of specimens: (a) SSCP-H, (b) SSCP-HQT, (c) SSCP-HS, and (d) SSCP-HST after electrochemical etching in 10% oxalic acid. | PMC10343823 | materials-16-04809-g002.jpg |
0.400888 | 5df1c8a0ba8e4ed3b7b93c3444beefa3 | Line scanning near the bonding joint of specimens: (a) SSCP-H, (b) SSCP-HQT, (c) SSCP-HS, (d) SSCP-HST. | PMC10343823 | materials-16-04809-g003.jpg |
0.467188 | 5f7b18f9b8ec4b24a9c399cb828a14a4 | SEM images of grain boundaries at the SS cladding’s outside surface: (a1) SSCP-H, corresponding EDS elemental mappings of (a2) Fe, (a3) C, and (a4) Cr, (b1) SSCP-HQT, corresponding EDS elemental mappings of (b2) Fe, (b3) C, and (b4) Cr. | PMC10343823 | materials-16-04809-g004.jpg |
0.37518 | 36bedf954f734b61877413497c5078cf | Microhardness distribution of bonding joints: (a) SSCP-H, (b) SSCP-HQT, (c) SSCP-HS, (d) SSCP-HST. | PMC10343823 | materials-16-04809-g005.jpg |
0.3852 | 02205ab326834914a28c2908a0b83c52 | Mean shear strength of joints under different heat treatment conditions. | PMC10343823 | materials-16-04809-g006.jpg |
0.458501 | 75d89eeb47f54a1ebce2ea6dda56d713 | Shear fracture morphologies of SS cladding: (a) SSCP-H, (b) SSCP-HQT, (c) SSCP-HS, (d) SSCP-HST. | PMC10343823 | materials-16-04809-g007.jpg |
0.454034 | 399e3800a1b944f9a8bdb8d05afcf372 | DL-EPR curves for the SS cladding surface with various heat treatment conditions. | PMC10343823 | materials-16-04809-g008.jpg |
0.510621 | 3028aaf4185b465eafdb158eade573e2 | Corrosion morphology of the SS cladding surface after DL-EPR test: (a) SSCP-H, (b) SSCP-HQT, (c) SSCP-HS, (d) SSCP-HST. | PMC10343823 | materials-16-04809-g009.jpg |
0.531516 | 5232f64136984b90adf07594009da26f | Potential polarization curves for the SS cladding surface with heat treatment conditions. | PMC10343823 | materials-16-04809-g010.jpg |
0.435829 | bd3a00a6e2d34244a72a72613aba1b38 | EIS test results for the SS cladding surface with heat treatment conditions: (a) Nyquist plot; (b) equivalent circuit. | PMC10343823 | materials-16-04809-g011.jpg |
0.444178 | dd546fcee83e4458b441f50a559c6821 | ncRNAs in cancers ncRNAs in cancer can affect cancer initiation, progression via three ways: act as oncogenes, cancer suppressors or affect cancer metastasis. When it is used as oncogene, lncRNA H19, miR-21 and miR-17-92 mainly promote the target, while lncRNA PVT1, miR-372/373 and lncRNA HOTAIR inhibit the target. As tumor suppressor, miR-34 and lncRNA MEG3 both promote target P53, and lncRNA MEG3, it can affect autophagy and inhibit cancer, and miR-15a and miR-16-1 affect BCL-2 and inhibit cancer. When lncRNA plays a role in influencing tumor metastasis, it affects the target, thus affecting the occurrence of cancer | PMC10344860 | 12672_2023_728_Fig1_HTML.jpg |
0.427239 | 7c2e7c8640b440948ef7b7344a1a0f09 | The TRPV4 IDR forms an extensive ‘belt’ along the membrane plane and encodes a hierarchy of antagonistic regulatory modules.a, b Superimposed IDR conformations from coarse-grained MD simulations (pink licorice) integrated into a full-length TRPV4 tetramer (AlphaFold94 prediction of G. gallus TRPV4 transmembrane core (gray) and ARDs (cyan)) viewed from the side a and from the intracellular side b. For better visualization of the extent of the IDR ‘belt’, the IDR conformations of the front facing TRPV4 monomer have been deleted. For a view of the IDR conformations on a single TRPV4 subunit, see Supplementary Fig. 13 as well as Supplementary Movies 2 and 3. c The TRPV4 N-terminus encodes multiple antagonistic regulatory elements that regulate TRPV4 function through ligand, protein, lipid or intra-domain contacts. d PIP2-binding site interactions with the membrane exert a pull force on the IDR C-terminus. Likewise, pulling on the IDR can lead to membrane deformation. Crosstalk between the PIP2-binding site and the autoinhibitory patch modulates PIP2 binding and thus IDR membrane interactions, thereby influencing channel activity. | PMC10344929 | 41467_2023_39808_Fig10_HTML.jpg |
0.40048 | 8cbe007923324c1e8af6100e30a1c31e | Structural ensemble of the TRPV4 N-terminal domain.a TRPV4 N-terminal constructs used for structural analyses. b–d Purified TRPV4 N-terminal constructs analyzed by Coomassie-stained SDS-PAGE b, SEC-MALS c, and CD spectroscopy d. SDS-PAGE in b comparing all constructs side by side was carried out once to evaluate sample purity and respective molecular weight. e [1H, 15N]-TROSY-HSQC NMR spectrum of 15N-labeled TRPV4-IDR (see Supplementary Fig. 2 for backbone assignments). f, g SAXS pair-distance-distribution f and SAXS EOM (Ensemble Optimization Method) g, both in arbitrary units (arb. units), of TRPV4 N-terminal constructs (Supplementary Fig. 3). The real-space distance distribution yields a radius of gyration of Rg = 3.4 nm with a maximal particle dimension of Dmax = 14.0 nm for the IDR, Rg = 4.1 nm and Dmax = 19 nm for the NTD as well as Rg = 2.5 nm and a Dmax = 11.5 nm for the ARD. Every protein exhibits levels of conformational heterogeneity and the p(r) profiles should be interpreted as the summed volume-fraction weighted contribution within the sample population, and not as single-particle distributions. The statistical analyses of the fit in g was carried out using the reduced χ2 method93 (one-tailed distribution) and CorMap64 (one-tail Schilling distribution) test methods. The determined χ2 and CorMap p values are indicated in the corresponding graph. h NTD ensemble refined by EOM (Ensemble Optimization Method)37,38. Using a chain of dummy residues for the IDR and the X-ray structure of the TRPV4 ARD (PDB: 3W9G) as templates, a library of 10,000 NTD structures was generated and refined against the experimental data, allowing the comparison of the fitted versus the random pool and selecting a sub-set of ensemble-states representing the experimental data. Ten IDR conformers best representing the experimental scattering profile are depicted. Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig1_HTML.jpg |
0.498618 | a162d37804b3445c8f82d831cf744300 | Structural dynamics of the TRPV4 ARD.a HDX of TRPV4 NTD and its isolated subdomains. Low (blue) to high (red) HDX shown for four time points. Areas without HDX assignment are colored white. For the ARD, HDX was visualized on the available X-ray structure of the G. gallus TRPV4 ARD (PDB: 3W9G). The six ankyrin repeats (AR) are indicated on top of the heat map diagram. b, c Root-mean-square fluctuations (RMSF) obtained from atomistic molecular dynamics (MD) simulations of the isolated G. gallus TRPV4 ARD in solution. RMSF at 42 °C mapped onto the ARD X-ray structure (PDB: 3W9G) b and RMSF per residue in simulations at increasing temperatures c. For comparison, HDX profiles after 102 s from a are displayed in the plot background. d, e RMSF of the ARD with respect to the central TRPV4 axis obtained from 1 µs long MD simulations of the complete TRPV4 core (see also Supplementary Movie 1). d Schematic depiction of the MD simulation setup. The channel principal axis (defined as z) is indicated as a dashed vertical line. The RMSF was calculated as the square root of the variance of the motion along this axis (∆z). e RMSF of TRPV4 residues 134–450 comprising the ARD. The solid line represents the average RMSF from all four protomers, the light area indicates the standard error of the mean. Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig2_HTML.jpg |
0.431542 | 6bf4111d9536496089e1ce07dd8ffb0b | Long-range intra- and interdomain interactions of the TRPV4 NTD.a, b Cross-linking mass spectrometry was used to probe interactions within and between IDR and ARD using either a the entire NTD or b isolated IDR (gray) and ARD (cyan) in a 1:1 ratio. Lysine residues are indicated by black tick marks, the PIP2-binding site is marked light blue. Intradomain crosslinks are shown by curved lines in dark gray, interdomain crosslinks in light gray. c Heat map of Cɑ-Cɑ distances for an NTD conformational ensemble consisting of 15 EOM-refined conformers based on SAXS data of the NTD (Fig. 1h). Crosslinks are highlighted by white squares (NTD), black crosses (equimolar ARD:IDR mixture) or white squares filled with black crosses (both experimental set-ups). d TRPV4 N-terminal constructs used for tryptophan fluorescence (PBS: PIP2-binding site, PRR: proline rich region). e, f Tryptophan fluorescence spectroscopy of TRPV4 N-terminal constructs (IDR, NTD, NTDΔN54 and NTDΔN97 lacking the first 54 or 97 amino acids, respectively, and IDRΔN97 (comprising PIP2 binding site, surrounding basic residues and proline rich region) or isolated amino acid in buffer (Trp). Residue W109 in the PIP2 binding site is the sole tryptophan residue in the entire NTD. Fluorescence intensity is presented in counts per second (cps). Bars represent the intensity weighted fluorescence emission wavelength <λ > (left axis). Data are presented as the mean value ± SEM from n = 3 individual experiments. The fluorescence emission maximum λmax is shown by black circles connected through dotted lines (right axis). g, h
1H chemical shift differences of W109 sidechain amide between IDR and IDRΔN97 as well as their respective counterparts harboring the PIP2 binding site (107KRWRR111) mutation to 107AAWAA111. Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig3_HTML.jpg |
0.45307 | e73705bbc1a24a1fbd61c81f27fba3f9 | The PIP2-binding site promotes compact IDR conformations.a Constructs used in SEC-SAXS experiments. b Real-space pair-distance distribution functions, or p(r) profiles, in arbitrary units (arb. units), calculated for IDR and IDRAAWAA (gray curves) as well as NTD and NTDAAWAA (blue curves). p(r) functions were scaled to an area under the curve of 1. The real-space distance distribution of IDRAAWAA yields a radius of gyration of Rg = 3.5 nm with a maximal particle dimension of Dmax = 14.5 nm (native IDR: Rg = 3.4 nm, Dmax = 14.0 nm). NTDAAWAA has a Rg = 4.5 nm and a Dmax = 19.5 nm (native NTD: Rg = 4.1 nm, Dmax = 19.0 nm). c Fit between EOM-refined IDR and NTD models and experimental scattering data, in arbitrary units (arb. units). The statistical analyses of the fits were carried out using the reduced χ2 method93 (one-tailed distribution) and CorMap64 (one-tail Schilling distribution) test methods. The determined χ2 and CorMap p values are indicated in the corresponding graphs. d Comparison between Rg values of IDR and NTD variants between random pool structure library (solid area) and EOM refined models (dotted line). Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig4_HTML.jpg |
0.40961 | 8af2462285da4387b3b934030e84a2a1 | The distal N-terminus affects the structural NTD ensemble and TRPV4 channel activity.a Topology of NTD truncations showing the charge distribution z (www.bioinformatics.nl/cgi-bin/emboss/charge) and sequence conservation (ConSurf50) along the IDR. b Overall charge (z) in the IDR at physiological pH (7.4) depending on the IDR length (values determined with ProtPi, www.protpi.ch). c Normalized real-space distance distribution p(r), in arbitrary units (arb. units), of NTD and NTD deletion constructs. d Dimensionless Kratky plot of NTD and NTD deletion mutants. e Radius of gyration (Rg) and Stokes radius (RS) determined from the real-space distance distribution in a and the SEC analysis (Supplementary Fig. 5c), respectively, plotted versus the number of IDR residues the NTD constructs. The maximum particle dimension (Dmax) is plotted on the right y-axis. f N-terminal deletion mutants in the in vitro (G. gallus) and in cellulo (H. sapiens) systems. g Activation of TRPV4 constructs with the synthetic agonist GSK101 shows plasma membrane targeting and structural integrity of all constructs. Data are presented as mean values ± SEM from n = 6 biologically independent experiments, each with 10–30 cells per field of view. h Basal Ca2+ levels in MN-1 cells expressing different TRPV4 constructs. Data are presented as mean values ± SEM from n = 12 biologically independent experiments, each with 10–30 cells per field of view. The **** indicates a p value of p < 0.0001 (one-way ANOVA with Dunnett’s multiple comparison test). i Stimulation of Ca2+ flux by hypotonic saline at t = 20 s in MN-1 cells expressing different TRPV4 constructs. Data are presented as mean values ± SEM from n = 6 biologically independent experiments, each with 10–30 cells per field of view. Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig5_HTML.jpg |
0.439439 | 313cdb0982f042b28a079e3d952f0d2e | A highly conserved patch in the N-terminal TRPV4 IDR transiently interacts with the C-terminal PIP2 binding site and autoinhibits TRPV4 function.a Chemical shift differences at high and low salt between 15N-labeled native IDR and IDRAAWAA with a mutated PIP2 binding site (PBS) shows that mutagenesis of the PBS leads to chemical shift changes in the conserved N-terminal patch. At the higher salt concentration (light gray), these chemical shift perturbations are significantly reduced. b Degree of conservation in TRPV4 IDR determined with ConSurf50 (Supplementary Fig. 11). c Chemical shift differences at high and low salt between 15N-labeled IDR and IDRPatch with a mutation in the conserved N-terminal patch shows that mutagenesis leads to chemical shift changes in the PBS. At the higher salt concentration (light gray), these chemical shift perturbations are significantly reduced. d Relative peak intensity of IDR, IDRAAWAA and IDRPatch residues in the isolated IDR or in context of the ARD (i.e., NTD, NTDAAWAA or NTDPatch). All protein concentrations used were 100 µM. A value of 0.5 indicates that peak intensities for a respective IDR residue are halved when the ARD is present, a value of zero represents complete line broadening in the context of the NTD. Accordingly, lower values are indicative of IDR/ARD interactions. e, f Ca2+ imaging of hsTRPV4 variants expressed in MN-1 cells. e Basal Ca2+ and f hypotonic treatment at t = 20 s show increased activity of the patch mutant. For better comparison, data for TRPV4ΔN68 are replotted from Fig. 5h, i. Data in e are presented as mean values ± SEM from n = 13 (TRPV4), 11 (TRPV4ΔN68), 14 (TRPV4Patch) and in f from n = 12 (TRPV4, TRPV4ΔN68, and TRPV4Patch) biologically independent experiments, each with 10–30 cells per field of view. Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig6_HTML.jpg |
0.402537 | 66529d9aa92c4454a8775571f924981d | Extensive lipid binding in the IDR is negatively affected by the distal N-terminus.a Topology of N-terminal deletion mutants used for liposome sedimentation assay. b Protein distribution between pellet (“bound protein”) or supernatant fraction after centrifugation, quantified via densitometry of SDS-PAGE protein bands using imageJ51. Data are presented as the mean value ± SEM from n = 3 individual experiments. c Distribution of charged and hydrophobic residues in the TRPV4-IDR shows a gradient of a consecutively more basic and hydrophobic protein from N- to C-terminus. Plotted with the PepCalc tool (https://pepcalc.com/). d, e NMR signal intensity differences for 15N-labeled IDR variants (100 µM) in the absence and presence of POPC (light gray circles) or POPC-POPG containing liposomes at low (filled yellow circles) or high salt concentration (open yellow circles). Higher values are indicative of lipid binding. Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig7_HTML.jpg |
0.495842 | c21bc87b32d14827bf70dab73fd38889 | The conserved N-terminal patch modulates lipid binding to the IDR.a, b, c Chemical shift perturbation of 15N-labeled a IDR, b IDRAAWAA, and c IDRPatch titrated with short-chain PIP2. Mutated regions are indicated in gray boxes, chemical shift changes are depicted by colored spheres, residues showing line broadening are highlighted by gray bars. d Average number of membrane contacts for each residue of the native IDR (dark gray), the IDRAAWAA mutant (light gray) and the IDRPatch mutant (mauve) on a lipid bilayer composed of POPC (69%), CHOL (20%), DOPS (10%), PIP2 (1%) (Supplementary Table 4). The location of the N-terminal patch and the PIP2-binding site (PBS) are highlighted by gray boxes. In the upper panel, contacts for all lipids, in lower panel, only contacts with PIP2 are shown. Four replicate simulations per IDR sequence were carried out for 38 µs and contact averages were calculated from the last ~28 µs of each simulation. e
31P NMR spectra of diC8-PIP2 (light blue) with increasing amounts of IDR, IDRΔN97 or IDRPatch. Chemical shift changes are indicated by arrows. f Chemical shift perturbations of P4 and P5 lipid headgroup resonances upon addition of IDR (gray), IDRΔN97 (blue), or IDRPatch (mauve). Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig8_HTML.jpg |
0.427417 | c91e80d66d7f4fb2b0f1292913b9dc14 | PIP2 binding to the TRPV4 IDR’s PIP2-binding site exerts a pulling force on the ARD.a Coarse-grained MD simulation system setup using a lipid bilayer membrane consisting of PIP2 (1%, dark orange) as well as POPC (69%, dark gray), DOPS (10%, light gray) and cholesterol (20%, white). Headgroup phosphates are shown as orange spheres), the IDR (pink liquorice) was kept at defined distances from the membrane midplane by its most C-terminal residue V134 (blue sphere) to emulate anchoring by the ARD. The PIP2-binding site (PBS) is highlighted in cyan. b Force displacement curves from restrained simulations of TRPV4 IDR, IDRAAWAA and IDRPatch. Four 38 µs replicate simulations were carried out for each condition. The mean restraint force is plotted against the mean distance between residue V134 and the membrane midplane. Dotted lines show linear fits of the force contribution of the PIP2-binding site. Averages were calculated from the last ~28 µs of each of the 4 replicate simulations per IDR genotype and per height restraint. Error bars show the standard errors of the mean (SEM) of the replicate simulations. c Number of membrane lipid contacts for each residue of the native IDR at a given height restraint (for results with IDRAAWAA and IDRPatch, see Supplementary Fig. 10c). Averages are calculated from the last 28 µs of each of the four replicate simulations. d Composite figure of a structure of the native IDR (from an MD simulation at a restraint distance of 7 nm) and an AlphaFold94 model of the transmembrane core of the G. gallus TRPV4 tetramer. The force displacement curves in b indicate that the interaction of the PIP2-binding site with the membrane exerts a pull force on the ARD N-terminus (solid arrow). Source data are provided as a Source Data file. | PMC10344929 | 41467_2023_39808_Fig9_HTML.jpg |
0.44726 | 2754690f754d4f369b32bdf257cbd7dc | (A) Geographic distribution of Schreibers’s bats and identified locations of LLOV detection. The map shows the currently known distribution range of Schreibers’s bats (darker blue). Countries in which LLOV has been found are named on the map. The year and methods of detection are indicated below the countries of sample origin. Bat pictograms in normal position (green) indicate samples from live animals while upside down bats (black) indicate samples from bat carcasses. (B) Phylogenetic analyses of mammalian-associated filovirus reference genomes, including the available bat-derived LLOV sequences. The Maximum Likelihood tree was built using general time reversible model of substitution with gamma distributed rate variation and was tested with 1000 bootstrap replicates. Novel sequence data is highlighted with bold letters and available in the GenBank database under the accession number: ON186772 (C) SuBK12-08 cells were left uninfected (mock) or infected with the Italian LLOV isolate. At 1-day post-infection, cells were fixed with 10% formalin and stained by RNA FISH using probes targeting the negative sense viral genome (magenta) and the positive sense VP35 mRNA (green). Cell nuclei are stained with DAPI (blue). The map was created using the open-source software QGIS Desktop 3.24.1 (https://qgis.org/en/site/) and was modified by incorporating geographic distribution parameters of Miniopterus
schreibersii sourced from the IUCN database (The IUCN Red List of Threatened Species, Version 2022–2). | PMC10344946 | 41598_2023_38364_Fig1_HTML.jpg |
0.431971 | 7faa6cc17d68489ea85d8707d3bdf152 | Advantages and disadvantages of lateral flow assays. “Reprinted from [17], with permission from Elsevier”. | PMC10346655 | sensors-23-06201-g001.jpg |
0.414405 | 5a670bef40ee484799d533b4dcaacca4 | Estimated frequency of Caesarian sections (with 95% confidence intervals) based on Poisson regression with adjustment for gestational age at delivery, maternal age, and infant sex in singleton pregnancies affected by type 1 diabetes and controls from 1996 to 2018. | PMC10369353 | fendo-14-1232618-g002.jpg |
0.446164 | 4a3101f47b4d4f14ba28a43fcefab1ec | Estimated frequency of low APGAR (Appearance, Pulse, Grimace, Activity and Respiration) score (with 95% confidence intervals) based on Poisson regression with adjustment for gestational age at delivery, maternal age, and infant sex in singleton pregnancies affected by type 1 diabetes and controls from 1996 to 2018. | PMC10369353 | fendo-14-1232618-g003.jpg |
0.50103 | a658557b999b45e2b18d64681b248f37 | Estimated frequency of admission to neonatal infant care unit (with 95% confidence intervals) based on Poisson regression with adjustment for gestational age at delivery, maternal age, and infant sex in singleton pregnancies affected by type 1 diabetes and controls from 1996 to 2018. | PMC10369353 | fendo-14-1232618-g004.jpg |
0.447289 | 47d404ee3ca348ad883bc2a960db7e3e | A) Effect of spatially distributed “one-way” amplification on signal and internal noise. The model consists of a chain of linear amplifiers (multipliers) with gain g; the effect of internal noise is simulated by adding noise before and after each amplification stage. B) SNR enhancement (R) at the N-th output of the amplifier chain (shown for N=10 and N=20) as a function of the amplifiers gain g. C) Bidirectional noisy amplification model. In this model, internal noise propagates (while identically amplified) in both directions. D) Equivalent one-way amplification model to study noise and signal response at the n-th node. E) Example of enhancement factor at different nodes in a chain of N=10 bidirectional amplifiers. In this example the amplifiers gain is chosen to improve SNR at node 5 (see text), by imposing gm=3 for m<5 and gm=0.1 for m≥5. | PMC10370218 | nihpp-2306.11931v2-f0001.jpg |
0.463019 | 8b7b08d9acaa479eb89296b7125f9c81 | A) Simplified anatomical view of the mammalian cochlea. B) BM magnitude responses in vivo (amplifier on) and post-mortem (amplifier off) to 10 kHz and 30 kHz calculated in a 2D finite difference model of the mouse cochlea. C) Apical and basal noise propagation functions, for narrowband noise centered around of 10 kHz. These functions quantify at each location the expected noise power due to basal and apical noise sources (assuming equal power sources), respectively. D) BM response magnitude to sound signal and narrowband internal noise at 10 and 30 kHz, for a postmortem and in vivo models. The curves are normalized so that the response magnitude to signal and noise is the same postmortem at the CF place—in this way the difference between signal and noise response in vivo visually illustrates that turning on the amplifier boosts SNR at the CF place. E) Enhancement factor (ratio between SNR with amplifier on and amplifier off) along the cochlea, calculated for narrowband near-CF signal and noise, and for broadband signal and noise (white in [4,70] kHz). This figure shows that the near-CF positive SNR enhancement caused by turning on the amplifier, produces a broadband, global SNR enhancement. | PMC10370218 | nihpp-2306.11931v2-f0002.jpg |
0.459947 | 22a167be8ee74487877187551504ed13 | A) Example of Green’s function for a 2D model with reflective basal boundary Rst≈0.14, calculated numerically in a finite difference model (solid line) or with the WKB approximation [Eqs. (A11,A12), dashed lines]. The source locations for the various curves are indicated with vertical arrows; the source frequency is 10 kHz. B) Approximate Green’s function for a simplified 3D model (see text). | PMC10370218 | nihpp-2306.11931v2-f0003.jpg |
0.436212 | 5bcbcd62153d4e0e98c404338c3774d5 | Schematic of PAW generation and PAW egg washing. | PMC10371827 | gr1.jpg |
0.551439 | dd8249dd92dc4036b7ad4cf1b637ae84 | Schematic of set up to measure mechanical properties of eggs. | PMC10371827 | gr2.jpg |
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