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0.497354 | edce4a1ceee14a3abd0b42323a00f67a | The electrochemical properties for the LVO and P-LVO. (a) the comparison of CV curves of LVO and P-LVO stepped at 0.1 mV/s; the CV curves of (b) LVO and (c) P-LVO at different scan rates; (d) linear relationships between the anodic peak current densities (i) and the square root of the scan rate (ν1/2); (e) Nyquist plots of the pristine LVO and P-LVO (inset: equivalent circuit model used to fit the EIS data); and (f) plots of real parts of the complex impedance versus ω−1/2. | PMC10255298 | polymers-15-02502-g004.jpg |
0.448212 | ef999fe3970e4efd8c1ab84de11e8104 | The energy storage performance of the LVO and P-LVO. The GCD profiles of (a) pristine LVO and (b) P-LVO in the range between 0.2 and 3.0 V (vs. Li+/Li) at various current densities from 0.5 to 8 C rate; (c) the rate performance of LVO and P-LVO; and (d) cycling performance of LVO and P-LVO at 5 C. | PMC10255298 | polymers-15-02502-g005.jpg |
0.460249 | 343d4c186f8b464f9ae16ad98cbbcad4 | The electrochemical performance of the LIC based on AC and different negative electrodes. (a) Schematic illustration of the assembled structure of the P-LVO//AC LIC; the CV curves of (b) LVO//AC LIC and (c) P-LVO//AC LIC with various scan rates; (d) linear relationships between the anodic peak current densities and the square root of the scan rate (ν1/2); (e) CV curves (25 mV/s); and (f) GCD curves of the LICs with different negative electrodes at 0.1 A/g. | PMC10255298 | polymers-15-02502-g006.jpg |
0.44692 | 6ba20ede10e94756b206657d9f76bab9 | The performance of P-LVO//AC LIC. (a) CV curves and (b) GCD curves of the P-LVO//AC LIC, recorded in various potential windows; (c) GCD curves of the P-LVO//AC LIC at different current densities; (d) specific capacitances of P-LVO//AC LIC recorded at various current densities; (e) Ragone plots of the P-LVO//AC LIC (inset: digital photograph of an LED lighted by the LIC); and (f) cycling performance of the LIC at 1.0 A/g for 2000 cycles (The inset shows the corresponding GCD curves of the initial 3 cycles and the last 3 cycles). | PMC10255298 | polymers-15-02502-g007.jpg |
0.545381 | f18aa3aece7a42d8960cadc93662b51f | The schematic diagram of the collection device. Where 1 means the sight, 2 means the mirror control system bracket, 3 means the collimator, and 4 means the collimator installation bracket. | PMC10255307 | sensors-23-05039-g001.jpg |
0.478294 | ec07f13207164a6ca0807a943920a529 | The schematic diagram of the collimator collection device. Where 1 is the frosted glass, 2 is the milky glass, 3 is the reticle, 4 is the filter, and 5 is the objective lens group. | PMC10255307 | sensors-23-05039-g002.jpg |
0.419453 | 0fee7e9f30c94dc191de11e16d558aa6 | The aiming line image acquisition example. | PMC10255307 | sensors-23-05039-g003.jpg |
0.414659 | 413a129e5028438fb76f917c88797d60 | Data enhancement. | PMC10255307 | sensors-23-05039-g004.jpg |
0.442811 | ef03b6c244684029991c0eeec3396d07 | Diagram based on the modified YOLOv5s model to aiming line detection. | PMC10255307 | sensors-23-05039-g005.jpg |
0.466711 | 8c764248ff734ecbbf617a187e198c56 | YOLOV5 network structure. | PMC10255307 | sensors-23-05039-g006.jpg |
0.541442 | 3afa6e636f1e458a9c8ba9918a27f1dd | The schematic diagram of SPPF and SPPCSPC structure. | PMC10255307 | sensors-23-05039-g007.jpg |
0.413946 | d0039e126e0b439c949f57461cb6f47e | The structure of the CA attention module. | PMC10255307 | sensors-23-05039-g008.jpg |
0.439943 | 145745c845ca4262803da2a464467d14 | The structure of the C3 module. | PMC10255307 | sensors-23-05039-g009.jpg |
0.492645 | 2c98f26ed7924f32b218878170272458 | The structure of the C3CA module. | PMC10255307 | sensors-23-05039-g010.jpg |
0.534896 | 4d7f2f986349498788429ea3fea0dd4e | The schematic diagram of the feature fusion network. | PMC10255307 | sensors-23-05039-g011.jpg |
0.488509 | 8d222e1155634e15860dc4be27b3e89c | The schematic diagram of the other parameters and operations. | PMC10255307 | sensors-23-05039-g012.jpg |
0.417532 | ae49a37d043545dbb9db03ab36e4c25f | The structure of improved YOLOv5 network. | PMC10255307 | sensors-23-05039-g013.jpg |
0.487788 | dcfa843638c147c7a5fa70ad021db7af | Different regression loss curves of SIOU. | PMC10255307 | sensors-23-05039-g014.jpg |
0.478615 | 34ab3488aa16431b855c6e869caec3c7 | The schematic diagram of SIOU. | PMC10255307 | sensors-23-05039-g015.jpg |
0.467705 | 085a2789590849d1b0dfd069d52b4f4d | Comparison of regression loss curves of SIoU and δ-SIOU. | PMC10255307 | sensors-23-05039-g016.jpg |
0.536838 | dc54047a6eac470da166d0498a1966e8 | Comparison of loss curves of different coefficients on the SIoU. | PMC10255307 | sensors-23-05039-g017.jpg |
0.483337 | c844379dbf9646aeb8da8d40d28ed135 | Comparison of training results with YOLOv5. (a) Correlation curve of train_bbox. (b) Correlation curve of Precision. (c) Correlation curve of Recall. (d) Correlation curve of mAP. | PMC10255307 | sensors-23-05039-g018.jpg |
0.597699 | c67183b564ee45cca2ec46fec5e01543 | Comparison of average accuracy of different detection models. | PMC10255307 | sensors-23-05039-g019.jpg |
0.408152 | 51a8eaba83ae421cbc0e73fda8ebd9c5 | YOLOv5 gun leader’s sight line detection results. | PMC10255307 | sensors-23-05039-g020.jpg |
0.497461 | 860b204b930f48c29417b72d36b8e072 | Error curve of the horizontal direction. | PMC10255307 | sensors-23-05039-g021.jpg |
0.421675 | c9ef46bbef0242809cabf6079a87ba92 | Error curve in the vertical direction. | PMC10255307 | sensors-23-05039-g022.jpg |
0.471644 | 49b03f480a4047f9a496664d046430ec | Comparison of the functionality of PSII and PSI in four barley cultivars with varied Fe deficiency tolerance levels: PSII maximum quantum yield, Fv/Fm (A); the quantum yield of light-induced non-photochemical fluorescence quenching induced for photoprotection of PSII, Y(NPQ) (B); the quantum yield of non-light-induced non-photochemical fluorescence quenching related to PSII photoinhibition; Y(NO) (C); the maximal P700 signal, Pm (D); PSI donor-side electron transfer limitation, Y(ND) (E); PSI acceptor-side electron transfer limitation, Y(NA) (F). Data are represented as the means ± SE of three to four independent measurements. * p < 0.05, ** p < 0.01, and *** p < 0.001, indicate significant differences between +Fe and −Fe treatments (according to Student’s t-test). Different letters are shown on individual columns when p is <0.05 among the four barley cultivars based on Tukey multiple testing. | PMC10255597 | plants-12-02111-g001.jpg |
0.400867 | 003f09c6a0c64936954c521c968ef6cc | Western blot analysis normalized on a per total leaf protein to compare whole thylakoid proteins and functional PSI levels in four barley cultivars with different Fe deficiency tolerance: (A) Immunoblot analysis of PSII reaction center proteins (D1, D2, and cyt b559 [PsbE]) and PSI reaction center proteins (PsaA, PsaB, and PsaC), Ferredoxin, and CBB-stained RubisCO large subunits. Whole proteins extracted from leaves were separated by SDS-PAGE (1 μg protein/lane for D1, 5 μg protein/lane for the other proteins) and detected with specific antibodies for each protein; (B,C) Immunoblots detected with specific antibodies against each PSII subunit (D1, D2, and cyt b559) (B) or PSI subunit (PsaA, PsaB, and PsaC) (C) in panel A was quantified by Image J software and calculated as relative values for the Fe-sufficient condition (Fe-sufficient condition = 1); (D) The retention rate of functional PSI under the Fe-deficient condition is expressed as the relative value of Pm per PSI subunit content under Fe-deficient conditions (value of Figure 2C) to that under Fe-sufficient conditions. Data are presented as means ± SE of three independent leaves, with different letters shown on individual columns when p < 0.05 among four barley cultivars based on Tukey multiple testing. * p < 0.05. | PMC10255597 | plants-12-02111-g002.jpg |
0.42679 | 2167a4a24dd843d5b1fa77337b4143f5 | The ratio of stromal and granal thylakoids in Fe-sufficient chloroplasts. TEM images of Fe-sufficient chloroplasts were obtained from SRB1 and EHM1. All original images are shown in Figure S4. We sampled four independent chloroplasts images per cultivar, and selected grana stacks with stroma lamellar membranes clearly recognized in each image. Then, granal thylakoid and thylakoid membranes in stroma connected to selected grana were measured by line length using ImageJ. Typical magnified images of yellow lines tracing the membrane of grana and stroma are shown in (A). All tracing lines on membranes are shown in Figure S4. Summations of line lengths to grana or stroma were calculated for each image, then averages of the stromal thylakoid/granal thylakoid ratio, as shown in (B). Values represent the mean ± SE of the four images. * p < 0.05 indicates significant differences (according to Student’s t-test) between two cultivars. | PMC10255597 | plants-12-02111-g003.jpg |
0.58108 | 33b6a037700e42b5a3d83e2f64e8d8ed | Analyses of fractions obtained from SDG using the thylakoid membranes derived from SRB1 and EHM1. Thylakoid membrane samples from 0.4 mg/mL of chlorophyll were solubilized with β-DM (4.8 mg β-DM for 0.1 mg chlorophyll) and loaded on the top of the SDG tube. Total amounts of proteins or Fe in each fraction are presented in the bar graphs. The amount of Fe was determined by two test solutions prepared from one fraction and measurement was conducted twice for one test solution. A dot shows the average of one test solution and a bar shows the average of two test solutions. A total of 1/1000 of each fraction was loaded for Western blot analysis, except for anti-PsaC. For anti-PsaC, 1/500 of each fraction was loaded. | PMC10255597 | plants-12-02111-g004.jpg |
0.440061 | 9aa438a246274812bcfc13528cc9f713 | Chlorophyll, Fe, and proteins present on high- and low-density thylakoids from SRB1 and EHM1. (A,C) SRB1 and (B,D) EHM1. (A,B) Chlorophyll content and (C,D) Fe contents derived from 2.5 g or 5 g of control or Fe-deficient leaves, respectively. Solid bars and hatched bars represent H-Thy and L-Thy, respectively. Values represent the mean ± SE of three independent fractions. Small counts on bars indicate the ratios of L-Thy to H-Thy. (E) Western blot analysis. Loading amounts: 1/2000 of the fraction for the control sample and 1/500 of the fraction for the Fe-deficient sample, except anti-PsaC. For anti-PsaC, 1/1000 or 1/250 fractions were loaded for the control sample or Fe-deficient sample, respectively. Higher amounts of Fe-deficient materials than control materials were used to obtain a clear signal. Lanes of images from SRB1 were rearranged to match the order of those from EHM1. Corresponding CBB stain images are shown in Figure S8C, and original blot images of three replicates are shown in Figure S8A. Relative signal intensities of L-Thy to corresponding H-Thy were calculated and average and SE (n = 3) were shown. | PMC10255597 | plants-12-02111-g005.jpg |
0.452173 | 9bef7b16074748bf8822c81bf4f64e4b | Representativeness of the feeling of stress experienced by oral and maxillofacial surgeons in the dental office and/or hospital setting. | PMC10256140 | pone.0286853.g001.jpg |
0.448569 | 7045049bc007496e89ac5d6a7ff15156 | EGD view from the gastric pouch showing a narrowing of the gastrojejunal anastomosis caused by extensive fibrosis and a deep marginal ulcer on the jejunal limb. | PMC10256954 | gr1.jpg |
0.401052 | b9d675760bd44a7bbd16cff7a06cd3dc | EGD view from the gastric pouch showing a large marginal ulcer extending to the jejunal limb. | PMC10256954 | gr2.jpg |
0.481465 | 42bd753d6c1b4731b225f9ec54813753 | EUS showing the injection of the gastric remnant with a mixture of contrast and saline. | PMC10256954 | gr3.jpg |
0.415137 | 9bad9d26c811407ea4d97c14815a821d | Fluoroscopic image showing the gastric pouch and remnant stomach filled with contrast after a guidewire was inserted in the gastric remnant. Contrast can also be seen in the duodenum. | PMC10256954 | gr4.jpg |
0.414206 | 6a52ae1b78f440d691e44e1dbf14745c | EGD view from the gastric pouch showing the lumen-apposing metal stent in place forming the gastro-gastric anastomosis. | PMC10256954 | gr5.jpg |
0.431128 | fffc550488b64e9e8dcb9194a5012d42 | EGD view from the gastric pouch showing the gastrojejunal anastomosis suturing using the Apollo Overstitch. | PMC10256954 | gr6.jpg |
0.409967 | de9b750e5e8a4a68a5ad89c91a0d9fbe | EGD view from the gastric pouch showing complete closure of gastrojejunal anastomosis and the gastro-gastric stent in place. | PMC10256954 | gr7.jpg |
0.409451 | ae3e7759663043489fc93298aae986f5 | EGD view inside the jejunal limb showing significant healing of the marginal ulcer 4 months after the EUS-guided Roux-en-Y gastric bypass reversal procedure. | PMC10256954 | gr8.jpg |
0.369661 | 58e1f9330e4842d5a36c411a234a805d | EGD view from the gastric pouch showing the gastro-gastric stent in place and the gastrojejunal anastomosis almost entirely closed 4 months after the EUS-guided Roux-en-Y gastric bypass reversal procedure. | PMC10256954 | gr9.jpg |
0.408924 | 6a446578f0964ada9678e5fcb325e0fc | Structure of the used ANN. Gimp 2.10.32. | PMC10257355 | medscimonit-29-e939462-g001.jpg |
0.462918 | 2e4de3f4f71c40469dfb2111baeccfef | Malignant and benign tumors chosen for the test dataset (arterial phase). Raw image created in Google Sheets, TIFF version – Gimp 2.10.32. | PMC10257355 | medscimonit-29-e939462-g002.jpg |
0.495889 | a671fff544af418bb8c90b4f5a36a0eb | Tumor size distribution. Raw image created in Google Sheets, TIFF version – Gimp 2.10.3. | PMC10257355 | medscimonit-29-e939462-g003.jpg |
0.431245 | 6b8691299d254736b248ba7f8eb2175e | dsDNA interacts with cyclic GMP–AMP synthase (cGAS), which converts ATP and GTP to the second messenger 2′3′ cyclic GMP–AMP (cGAMP). In the endoplasmic reticulum, cGAMP binds and activates STING, leading to activation and phosphorylation of IRF3 by TANK-binding kinase 1. IRF3 forms homodimers and trans-locates into the nucleus to induce type I IFN expression. The RNA sensing pathway is also involved in AGS as a result of activation of the MDA5/MAVS pathway. STING stimulator of interferon genes, IRF3 interferon regulatory transcription factor 3, IFN interferon, AGS Aicardi–Goutières syndrome, MDA5 melanoma differentiation-associated gene 5, MAVS mitochondrial antiviral signaling | PMC10258176 | 12519_2022_679_Fig1_HTML.jpg |
0.427886 | 3e6284a6d924443fb059b5efa2799834 | CaCl2 treatment and CO2-laser-induced carbonization of chitin nanopaper. (a) Procedure schematic, (b) optical image of chitin nanopaper with or without the CaCl2 treatment after CO2 laser irradiation, and (c) Raman spectra of the (i) original chitin nanopaper, (ii) CaCl2-treated chitin nanopaper, and (iii) CO2-laser-carbonized chitin nanopaper. | PMC10258603 | d3ra03373b-f1.jpg |
0.420778 | e3d5a353c9554dacb3c1df8338a4106f | Chemical structures of the CO2-laser-carbonized chitin nanopaper. (a) FT-IR and (b) wide XPS spectra of the (i) original chitin nanopaper, (ii) CaCl2-treated chitin nanopaper, and (iii) CO2-laser-carbonized chitin nanopaper. (c) C 1s XPS spectrum of the CO2-laser-carbonized chitin nanopaper. | PMC10258603 | d3ra03373b-f2.jpg |
0.433683 | c8e31d7ce0ba4b56922b61702562c65a | Ca 2p XPS spectra of the (i) original chitin nanopaper, (ii) CaCl2-treated chitin nanopaper, and (iii) CO2-laser-carbonized chitin nanopaper. | PMC10258603 | d3ra03373b-f3.jpg |
0.378939 | 03675afafb094102b2a13f117712ddcf | Morphologies of the CO2-laser-carbonized chitin nanopaper. Oblique-view FE-SEM images of the (a) original chitin nanopaper, (b) CaCl2-treated chitin nanopaper, and (c) CO2-laser-carbonized chitin nanopaper. (d and e) Cross-section FE-SEM image of the CO2-laser-carbonized chitin nanopaper. | PMC10258603 | d3ra03373b-f4.jpg |
0.420504 | 4cf4b05028af470cba3cf844b1d8d85e | Solar absorption of the CO2-laser-carbonized chitin nanopaper. (a) Solar spectral irradiance (AM1.5G) and UV-vis-NIR absorption, (b) reflection, (c) transmittance spectra, solar (d) absorption, (e) reflection, and (f) transmittance of the (i) original chitin nanopaper, (ii) CaCl2-treated chitin nanopaper, and (iii) CO2-laser-carbonized chitin nanopaper. | PMC10258603 | d3ra03373b-f5.jpg |
0.456777 | b1a4241cc2454bb5b6ac64166ef3f578 | Solar thermal heating performance of the CO2-laser-carbonized chitin nanopaper. (a) Experimental setup for the surface temperature measurement during 1 sun irradiation by a solar simulator, (b) surface temperature versus 1-sun irradiation time of the (i) original chitin nanopaper, (ii) CaCl2-treated chitin nanopaper, and (iii) CO2-laser-carbonized chitin nanopaper. | PMC10258603 | d3ra03373b-f6.jpg |
0.455966 | ff2f28a99a344595b1aba17d9329f751 | Job strain model by Karasek [14]. | PMC10259082 | 10.1177_14034948211030352-fig1.jpg |
0.500808 | fe9777b4d9764b27baa051934fd6add0 | Systolic blood pressure according to job strain categories.Unadjusted comparison (analyses of variance) between job strain groups, Bonferroni post hoc tests. ***p>0.001; **p>0.005. | PMC10259082 | 10.1177_14034948211030352-fig2.jpg |
0.491033 | 15efe671169c431ebcb1ba1bb8ddaa7a | Preference for proportion of consultations with KDT team to be by video versus in person (n = 40). | PMC10259179 | gr1_lrg.jpg |
0.432907 | 72f087ba727249249d15a121bfbacefa | (a) Advantages of VCs (b) Disadvantages of VCs (n = 40). Abbreviation: VA Video appointment. | PMC10259179 | gr2_lrg.jpg |
0.422959 | 21a8bcd77c3f40e2b9356e48368d6952 | Serine proteases cleave competence-stimulating peptide of S. pneumoniae.(A) Sequence of competence-stimulating peptide 1 (CSP1) and peptide 2 (CSP2). Red arrows indicate potential cleavage sites by trypsin-like serine proteases. (B) Mass spectrometry analysis of cleaved residues of CSP1 upon incubation with no trypsin (grey) or with porcine trypsin (black) for 30 minutes. (C) Mass spectrometry analysis of cleaved residues of CSP1 upon incubation with no trypsin (grey) or with human airway trypsin (HAT) (black) for 30 minutes. (D) Mass spectrometry analysis of cleaved residues of CSP2 upon incubation with no trypsin (grey) or with porcine trypsin (black) for 30 minutes. (E) Mass spectrometry analysis of cleaved residues of CSP2 upon incubation with no trypsin (grey) or with HAT (black) for 30 minutes. (B-E) The fraction of each peptide detected by mass spectrometry was calculated by dividing the area of the cleaved peptide by the total area of all peptides. In the case of two cleavage sites on the same peptide, the fraction was equally attributed to both cleavage sites. Each bar represents the fraction of identified peptides that contained a cleavage event after the amino acid depicted under the bar. Bars above the final amino acid represent uncleaved CSP1 or CSP2. | PMC10259803 | ppat.1011421.g001.jpg |
0.558667 | 8cb299ddb5c2413f8c2c14695c6a6530 | Serine proteases reduce recombination frequency of S. pneumoniae in a dose dependent manner.Recombination frequency upon incubation of CSP1 or CSP2 with increasing concentrations of serine proteases with and without 0.1mM of the serine protease inhibitor, AEBSF. D39x transformed with CSP1 incubated with (A) porcine pancreatic trypsin (PPT) or (B) human airway trypsin (HAT). D39x comC- transformed with CSP1 incubated with (C) PPT or (D) HAT. TIGR4 transformed with CSP2 incubated with (E) PPT or (F) HAT. TIGR4 comC- transformed with CSP2 incubated with (G) PPT or (H) HAT. Negative controls included no addition of CSP1 and no addition of gDNA. Lines represent median value. Dotted line represents lowest point of detection. Recombination frequencies of increasing concentrations of protease within each group (0 mM AEBSF or 0.1 mM AEBSF) were compared using Kruskal-Wallis one-way ANOVA; *p = 0.05–0.01, **p = 0.01–0.001, ***p = 0.001–0.0001. | PMC10259803 | ppat.1011421.g002.jpg |
0.420656 | e044ecd0fd8f4bf18623e23abfe7096f | Serine proteases reduce expression of CSP induced luciferase in S. pneumoniae.Luminescence (RLU) of DLA3 grown in the presence of CSP1 incubated with increasing concentrations of serine proteases with and without inhibitor AEBSF. Incubation of CSP1 with PPT (A) without AEBSF or (B) with AEBSF. Incubation of CSP1 with HAT (C) without AEBSF or (D) with AEBSF. Experiment was repeated in triplicate. The mean value of RLU of each 30-minute timepoint is reported; error bars are SEM. Luminescence of increasing concentrations of protease within each group (0 mM AEBSF or 0.1 mM AEBSF) were compared using two-way ANOVA; ****p<0.0001. | PMC10259803 | ppat.1011421.g003.jpg |
0.432113 | a521e911d7df449f81f8e36f59c1573f | Modified CSP alters impact of protease on recombination frequency.Recombination frequency with modified CSP1. (A) Transformation of D39x comC- with CSP1 with modifications R3H, K6H, R9H, and R15H. Transformation of D39x comC- with modified CSP1 incubated with increasing concentrations of (B) PPT or (C) HAT. Recombination frequency reported as % of 0 trypsin. Negative controls included no addition of CSP1 and no addition of gDNA. Lines represent mean value. Recombination frequencies of increasing concentrations of protease within each modified CSP were compared using one-way ANOVA; ***p = 0.001–0.0001, ****p<0.0001. Changes in the concentrations of protease between modified CSP was compared using two-way ANOVA; ##p = 0.01–0.001, ###p = 0.001–0.0001. | PMC10259803 | ppat.1011421.g004.jpg |
0.521209 | 7a8247de09504abab3fee9de65593a7a | Modification of R9 of CSP1 alters protease digestion profile.Mass spectrometry analysis of cleaved residues of CSP1 (black) or CSP1 R9A (striped) upon incubation with (A) porcine trypsin or with (B) HAT. The fraction of each peptide detected by mass spectrometry was calculated by dividing the area of the cleaved peptide by the total area of all peptides. In the case of two cleavage sites on the same peptide, the fraction was equally attributed to both cleavage sites. Each bar represents the fraction of identified peptides that contained a cleavage event after the amino acid depicted under the bar. Bars above the final amino acid represent uncleaved CSP1. | PMC10259803 | ppat.1011421.g005.jpg |
0.444846 | 6b14ae18907745f78b242a76805662ef | Inhibition of proteases from mouse lungs increase recombination frequency of S. pneumoniae.Recombination frequency and protease levels upon incubation of CSP1 with homogenized mouse lungs with increasing concentrations of inhibitor AEBSF. (A) Recombination frequency of D39x transformed with CSP1 incubated with homogenized mouse lungs. (B) Protease levels in homogenized mouse lungs upon incubation with AEBSF used in D39x transformation; determined by fluorescence of substrate t-Butyloxycarbonyl Phe-Ser-Arg 7-amino-4methyl coumarin (BOC). (C) Correlation of recombination frequency of D39x with the protease levels in the same homogenized mouse lung. (D) Recombination frequency of D39x comC- transformed with CSP1 incubated with homogenized mouse lung. (E) Protease levels in homogenized mouse lungs upon incubation with AEBSF used in D39x comC- transformations; determined by fluorescence of substrate BOC. (F) Correlation of recombination frequency of D39x comC- with the protease levels in the same homogenized mouse lung. (A,D) Line represents median; dotted line represents lowest point of detection; recombination frequency of 1 mM and 2 mM AEBSF were compared to 0 mM AEBSF using Kruskal-Wallis one-way ANOVA; ****p<0.0001. (B,E) Lines represent mean; protease levels of 1 mM and 2 mM AEBSF were compared to 0 mM AEBSF using one-way ANOVA. (C,F) Correlation was compared using two-tailed spearman; *** p = 0.0004, **** p<0.0001. | PMC10259803 | ppat.1011421.g006.jpg |
0.422566 | 8a19310884284b37ad166340db245f31 | Stimulation of proteases in vivo reduces ex vivo recombination frequency of S. pneumoniae.Recombination frequency upon incubation of CSP1 with homogenized lungs from mice that were administered poly (I:C) in vivo, treated with inhibitor AEBSF in vivo, and then treated ex vivo with increasing concentrations of inhibitor AEBSF. (A) Recombination frequency of D39x transformed with CSP1 incubated with homogenized lungs from mice that received no stimulant (water) or poly (I:C), and either received no inhibitor (PBS) or inhibitor AEBSF. (B) The same lungs were then treated with either 0, 1, or 2 mM AEBSF ex vivo prior to incubation with CSP1 and recombination frequency was determined. The 0 mM AEBSF are the same data used in Fig 7A and were included here for comparison. (C) Recombination frequency of D39x comC- transformed with CSP1 incubated with homogenized lungs from mice that received no stimulant (water) or poly (I:C), and either received no inhibitor (PBS) or inhibitor AEBSF. (D) The same lungs were then treated with either 0, 1, or 2 mM AEBSF ex vivo prior to incubation with CSP1 and recombination frequency was determined. The 0 mM AEBSF are the same data used in Fig 7C and were included here for comparison. Line represents median; dotted line represents lowest point of detection. (A,C) Recombination frequencies were compared pairwise using nonparametric Mann-Whitney t test; *p = 0.05–0.01, **p = 0.01–0.001. (B,D) Recombination frequency of 1 mM and 2 mM AEBSF were compared to 0 mM AEBSF of each group using Kruskal-Wallis one-way ANOVA; *p = 0.05–0.01, **p = 0.01–0.001, ***p = 0.001–0.0001, ****p<0.0001. | PMC10259803 | ppat.1011421.g007.jpg |
0.444756 | 96abe2493b2a41b7affe50c917baf40e | Stimulation of protease production in vivo reduces recombination frequency of S. pneumoniae.Recombination frequency of S. pneumoniae from (A) the lungs and (B) the blood of mice that received no stimulant (water) or poly (I:C), and either received no inhibitor (PBS) or inhibitor AEBSF. Protease levels in the same mouse lungs (C) and blood (sera) (D); determined by fluorescence of substrate BOC. Correlation of recombination frequency in lungs (E) and blood (F) with the protease levels in the same tissue. (A,B) Line represents median; dotted line represents lowest point of detection; recombination frequencies of all groups were compared pairwise for each tissue using nonparametric Mann-Whitney t test; **p = 0.01–0.001, ***p = 0.001–0.0001. (C,D) Lines represent mean; protease levels of all groups were compared pairwise for each tissue using unpaired t test; **p = 0.01–0.001, ****p<0.0001. (E,F) Correlation was compared using two-tailed spearman; **p = 0.004, ***p = 0.0001. | PMC10259803 | ppat.1011421.g008.jpg |
0.427295 | fc352230325444cda7b99f9716aa214b | Co-infection with influenza in vivo reduces recombination frequency of S. pneumoniae.Recombination frequency of S. pneumoniae from (A) the lungs and (B) the blood of mice infected with and without influenza (Flu). The total number of recombinant colonies per mL used to calculate recombination frequency enumerated from (C) the lungs and (D) the blood of mice infected with and without influenza (Flu). Lines represent median. Dotted line represents lowest point of detection. Recombination frequency and total number of recombinants from mice infected with influenza was compared to that without influenza for each tissue using nonparametric Mann-Whitney t test; **** p<0.0001. | PMC10259803 | ppat.1011421.g009.jpg |
0.483301 | 61f4474c6716443ab2e437351f80fd01 | Proposed model of impact of host serine proteases on S. pneumoniae adaptation to host epithelium and invasion.Created with BioRender.com. | PMC10259803 | ppat.1011421.g010.jpg |
0.451714 | 9d24532412564ee4ac755a1188e894cf | Three stages of data collection and analysis | PMC10259808 | 11119_2023_10037_Fig1_HTML.jpg |
0.406479 | 3df9a46ff80741b0be1bf44a59307da7 | Procedure of the focus-group discussions | PMC10259808 | 11119_2023_10037_Fig2_HTML.jpg |
0.417803 | a534d56d4c8e4d618225b32523734074 | Important SWOT factors* for the adoption of ALWS from stakeholders’ perspective (n = 55). *Factors were considered important if they were among the top five voted for by the focus-group participants. Factors that received few votes are not displayed | PMC10259808 | 11119_2023_10037_Fig3_HTML.jpg |
0.396747 | 4f554d0dd4184721afe17ae19c40020b | Representative examples and criteria for proper selection of solvents and antisolvents | PMC10260726 | 40580_2023_375_Fig1_HTML.jpg |
0.573185 | bf7d02d755da46af87a48cb32367e25d | Schematic illustration of perovskite formation processes: perovskite precursor deposition, phase conversion, and crystallization | PMC10260726 | 40580_2023_375_Fig2_HTML.jpg |
0.500925 | 2f0d87a5b03041eabfcb22b808491e26 | a Schematic illustration of a solution-shearing method and cross-sectional Scanning Electron Microscope (SEM) images of perovskite layer on FTO/c-TiO2/mp-TiO2 substrate prepared at different conditions of DMF/DMSO solution and ACN/MA solution. Reprinted with permission from [29]. Copyright 2022, Elsevier. b the full and c enlarged FTIR spectra result of TEP, intermediate phase, and perovskite (annealed). Reprinted with permission from [30]. Copyright 2022, Elsevier d Schematic of the perovskite layer deposition processes based on ETL substrate. Reprinted with permission from [36]. Copyright 2023, Royal Society of Chemistry | PMC10260726 | 40580_2023_375_Fig3_HTML.jpg |
0.381699 | 28877a215cdb4681bcd45fc74d61f45d | a Schematic illustration of device architecture and cross-sectional SEM image of a PSC fabricated from the DMSO solution system. Reprinted with permission from [32], Copyright 2021, American Chemical Society. b UV—vis spectra of perovskite precursors in GVL and GBL. Reprinted with permission from [34], Copyright 2021, The Authors. Energy Technology published by Wiley-VCH GmbH c Solubility test of FAPbI3 dissolved in EtOH, EtOH/DMA mixed solvent, and EtOH/DMA solution with PACl d FTIR spectra of the precursor solutions. Characteristic peaks between 1620 and 1635 cm− 1 are assigned to the C = O stretching peaks of DMA. e Change of perovskite films with containing different types of RNH3Cl. Reprinted with permission from [37], Copyright 2022, The Author(s), under exclusive license to Springer Nature Limited. f Schematic of perovskite crystal formation in 2-ME-CHP solution system. Reprinted with permission from [39], Copyright 2021, Elsevier. g SEM images of perovskite film change according to the amount of NMP additives. Reprinted with permission from [38], Copyright 2022, American Chemical Society | PMC10260726 | 40580_2023_375_Fig4_HTML.jpg |
0.404468 | c4153671f794449abd20617b951e631f | a Film morphologies depending on antisolvents. Reprinted with permission from [47], Copyright 2021, The Authors. SusMat published by Sichuan University and John Wiley & Sons Australia, Ltd. b Illustration of in-situ and post- CTAC treatment. Reprinted with permission from [48], Copyright 2021, Science China Press. c Illustration depicting the interaction between DMSO and FA+, and the preferred (111) crystal orientation. Reprinted with permission from [49], Copyright 2022, Wiley-VCH GmbH d Interaction between the C = O functional groups of acetylacetone and PbI2. Reprinted with permission from [51], Copyright 2021, Science Press and Dalian Institute of Chemical Physics, Chinese Academy of Sciences. e Illustration of hydrogen bond between a C= O group of diethyl carbonate and DMSO and FTIR spectrum presenting interaction between them. Reprinted with permission from [52], Copyright 2022, Elsevier B.V. f Uniform and pinhole-free perovskite films, made via green solvents. Reprinted with permission from [53], Copyright 2021, Elsevier B.V | PMC10260726 | 40580_2023_375_Fig5_HTML.jpg |
0.436444 | 296374ebf48a4e059334135acf4e1c08 | Schematic representation of perovskite film formation processes, and La Mer diagram with corresponding illustration of film morphologies for different cases. The degree of supersaturation level determines the number of seeds formed by “burst” nucleation and final morphology of the film after growth stage | PMC10260726 | 40580_2023_375_Fig6_HTML.jpg |
0.42822 | 0b711e273adb4649997dc23e69e51758 | Schematic illustration of a vacuum-assisted solution processing, and d spin coating. Reprinted with permission from [58], Copyright 2016, American Association for the Advancement of Science. b Illustration showing surface treatment of vacuum-assisted perovskite films. Reprinted with permission from [59], Copyright 2021, Royal Society of Chemistry. c Illustration of 4-guanidinobutanoic acid forming 2D perovskites at the grain boundaries. Reprinted with permission from [60], Copyright 2021, The Authors. Advanced Science published by Wiley-VCH GmbH e Pre-synthesized 3D MAPbCl3 and 1D ABTPbI3) microcrystals as seed crystals during the film formation. Reprinted with permission from [61], Copyright 2022, Wiley-VCH GmbH f Schematic illustration of inkjet printing perovskite films and SEM images depicting film morphologies given by the balance between amounts of PbAc2 and PbCl2. Reprinted with permission from [47], Copyright 2021, Wiley-VCH GmbH g Schematic illustration of gravure printing process and the resulting films. Reprinted with permission from [62], Copyright 2021, The Author(s), published by Elsevier | PMC10260726 | 40580_2023_375_Fig7_HTML.jpg |
0.480497 | 387246e0ac4a44c185dfbe4e54e5b9b8 | a Gas-mediated solid-liquid conversion process and D-bar coating of the solution. Reprinted with permission from [63], Copyright 2019, American Chemical Society. b The crystallization process of perovskite precursor solution employing ACN and 2-ME as the solvent and its rapid blading method. Reprinted with permission from [17], Copyright 2019, The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. c Fabrication of perovskite films with 2-ME and CHP mixed solution. Reprinted with permission from [39], Copyright 2021, Elsevier Inc. d The role of NMP in precursor solution. Reprinted with permission from [38], Copyright 2022, American Chemical Society. e The addition of RNH3Cl, enabling the formation of a soluble PbI2-HCl complex. Reprinted with permission from [37], Copyright 2022, The Author(s), under exclusive license to Springer Nature Limited. f Effect of MABr, releasing residual lattice strain to stabilize the crystal structure. Device structure with green solvents used for each layer. Reprinted with permission from [64], Copyright 2021, Royal Society of Chemistry | PMC10260726 | 40580_2023_375_Fig8_HTML.jpg |
0.438946 | c540f5f4162c40c68d0039a65eaea57d | Layer’s structure of the Multi-Layer Perceptron | PMC10261829 | 10639_2023_11831_Fig1_HTML.jpg |
0.449723 | dc54e4889c6d4e45bb4f31680ab50bef | Basic example of the Support Vector Machines | PMC10261829 | 10639_2023_11831_Fig2_HTML.jpg |
0.477821 | dddeea134c6f4debb91a128c5d08b4fc | Example of random forest | PMC10261829 | 10639_2023_11831_Fig3_HTML.jpg |
0.514716 | 7370666c91be45259d9ab0f7889112c1 | Example of convolutional neural network architecture | PMC10261829 | 10639_2023_11831_Fig4_HTML.jpg |
0.429605 | e9dc4768e03a445ab79839fe55dfd657 | Confusion Matrices | PMC10261829 | 10639_2023_11831_Fig5_HTML.jpg |
0.44988 | ce4a2b2953584724a5210c0cbd74a111 | HYDRA study design: two parallel, noncomparative, open label phase-I trials. Randomization is performed for translational research purposes. * Radiotherapy with/without concurrent radiosensitizer. Oropharyngeal and hypopharyngeal carcinoma are amenable for inclusion. Laryngeal carcinomas are initially excluded until these patients are also considered eligible after interim analysis. Abbreviations: BL: baseline. LD: last day of treatment. SOC: standard of care. HNSCC: head and neck squamous cell carcinoma. MBI: model-based indication for proton therapy, according to the Dutch model-based selection criteria. R: randomization by minimization based on HPV status (positive vs. negative), stage (I-II vs. III-IV), and concurrent radiosensitization (yes vs. no) | PMC10262496 | 12885_2023_11031_Fig1_HTML.jpg |
0.408235 | 25d50cbfd9e24e4f9cb2ab6911e9a830 | Tremor and movement speed calculated from fixed- and random-pattern intraoperative visual-motor tasks.(A) Left: Schematic of task target (green) and cursor (gray) traces from a single trial of the fixed- (top) or random- (bottom) pattern task. Center-top: Bandpass filtered cursor traces from a task trial. Ca refers to the amplitude of the analytic signal (a) of the cursor trace (C). Center-bottom: Lowpass filtered cursor traces from a task trial. Right-top: One-dimensional projection of bandpass filtered traces (black), with tremor amplitude measured from the envelope (orange). Right-bottom: Cursor speed measured from lowpass filtered traces (black). Figure adapted from Figure 1 of Ahn et al., 2020. (B, C) Distributions of 7 s tremor amplitude (top) and cursor speed (bottom) epochs for control subject and Parkinson's disease (PD) patient populations in the fixed-pattern (B) (n=5375 epochs across 35 subjects) and random-pattern (C) (n=1123 epochs across 9 subjects) task. ° – degrees of visual angle. (D, E) Task-based tremor amplitude (D) and slowness (E) corresponded to UPDRS measures of tremor (D) or bradykinesia (E) (n=24 subjects). ρ=Spearman correlation statistic. | PMC10264071 | elife-84135-fig1.jpg |
0.43749 | ffa3c8eb869e4844a8068b8e11490ba8 | Tremor and slowness represented two non-overlapping motor states with differing timescales.(A) Examples from three individual subjects of cursor (solid lines) and target (translucent lines) traces (top row) and calculated motor metrics (bottom three rows) within single trials. Periods of increased expression of individual motor metrics are highlighted by their respective color. (B) (Left) Scatter plot of all cursor speed and tremor measurements in 7 s epochs across subjects. (Right) Histogram of subject-wide behavioral Spearman correlation with tremor and slowness metrics (n=27 subjects). (C) Autocorrelograms of symptomatic (tremor, slowness) and non-symptomatic (effective motor control) metrics. Colored vertical dashed lines indicate full-width half-maximum (FWHM) for each metric. Top-left inset depicts a zoomed-in window of the autocorrelogram. (D) Histogram of sustained motor metric period duration (i.e., symptomatic state duration) across subjects. Solid lines indicate gamma distribution fit to each motor metric state histogram, while dashed vertical lines indicate the median symptomatic state length for each metric. | PMC10264071 | elife-84135-fig2.jpg |
0.416402 | 105c5eacaeb74dc59f9f96842fd408ee | Subthalamic tremor decoding models emphasized lower frequencies whereas slowness models emphasized higher frequencies.(A) Average tremor decoding and slowness model coefficients for all subthalamic nucleus (STN) microelectrode (left) (n=203 microelectrode recordings, 27 subjects) and macroelectrode (right) recordings (n=176 macroelectrode recordings, 27 subjects). Solid lines indicate average weights, with positive/negative values reflecting a positive or negative relationship with the metric. Error bars indicate s.e.m. across subjects. Black lines (top) represented contiguous spectral features that significantly differed between tremor and slowness decoding models. (B) Average model coefficients for effective motor control and tremor for all STN microelectrode (left) and macroelectrode (right) recordings. (C) Average model coefficients for effective motor control and slowness for all STN microelectrode (left) and macroelectrode (right) recordings. | PMC10264071 | elife-84135-fig3.jpg |
0.384007 | c68ccaa6cdaf402b8b00be0d2ed32433 | Optimal subthalamic tremor decoding sites were dorsolateral to optimal slowness decoding sites.(A) Recording density of stationary microelectrode recordings across patients (n=182 microelectrode recording sites, 25 subjects) and task sessions overlaid on an MNI reference volume (approximate outline of the subthalamic nucleus [STN] in bolded black, zona incerta outlined above, substantia nigra outlined below). L: left. y-value corresponds to coronal slice in MNI space. (B) Tremor decoding model r2-values for stationary microelectrode recordings. (C) Slowness decoding model r2-values for stationary microelectrode recordings. (D) Difference in tremor vs. slowness decoding r2-values for stationary microelectrode recordings. Warmer colors indicate voxels where tremor decoding was superior, whereas cooler colors indicate where slowness decoding was superior. (E) Recording density of moving microelectrode recordings across all patients and task sessions overlaid on an MNI reference volume. (F) Tremor decoding model r2-values for high-density STN survey recordings. (G) Slowness decoding model r2-values for high-density STN survey recordings. (H) Difference in tremor vs. slowness decoding r2-values for high-density STN survey recordings. r2-Values depicted here are site-specific r2-values generated from the whole-STN model applied to individual depth recordings. Warmer colors indicate voxels where tremor decoding was superior, whereas cooler colors indicate where slowness decoding was superior. | PMC10264071 | elife-84135-fig4.jpg |
0.522918 | 1faa6518cc1546119120ed2b9af1841c | Cortical tremor and slowness decoding models exhibited opposing weights for multiple frequency bands, and co-expressed specific features with subthalamic recordings.(A) Average cortical tremor and slowness decoding model coefficients for every recording along sensorimotor cortex (n=85 electrocorticography [ECoG] recordings, 10 subjects). Colored lines indicate average weights, with positive/negative values reflecting a positive or negative relationship with the metric. Error bars indicate s.e.m. across subjects. Black lines (top) represented contiguous spectral features that significantly differed between tremor and slowness decoding models. (B) Average model coefficients for effective motor control and tremor. (C) Average model coefficients for effective motor control and slowness. (D) Average subthalamic nucleus [STN]-cortical coherence tremor and slowness decoding model coefficients for every pairwise recording along sensorimotor cortex and macro contacts within the STN (n=85 ECoG recordings, 10 subjects). (E) Average coherence model for effective motor control and tremor. (F) Average model coefficients for effective motor control and slowness. | PMC10264071 | elife-84135-fig5.jpg |
0.39764 | dcba35a0b40a4960b73616b50cd9c8cc | Cortical tremor and slowness decoding models were distributed throughout cortex, and generally were superior to subthalamic nucleus (STN) decoding models.(A) Recording density of electrocorticography (ECoG) contacts (n=31 ECoG sites, 10 subjects) on an MNI reference surface. (B) Difference in tremor vs. slowness decoding r2-values for all cortical recordings. Warmer colors indicate surface vertices where tremor decoding was superior, whereas cooler colors indicate where slowness decoding was superior. (C) Decoding performance across metrics and recording types (n=85 ECoG recordings, 81 macroelectrode recordings, 81 microelectrode recordings, 10 subjects). Box represents interquartile range (25th–75th percentile), while whiskers indicate 5th–95th percentile of data range. Brackets indicate significant (*, p<0.05 in linear mixed model comparisons) differences in metric decoding r2-values. (D) Examples of tremor (top) and slowness (bottom) decoding for top-performing ECoG contacts. Each row within the panel represents a different subject. (E) Examples of tremor (top) and slowness (bottom) decoding for top-performing macroelectrodes. (F) Examples of tremor (top) and slowness (bottom) decoding for top-performing microelectrodes. | PMC10264071 | elife-84135-fig6.jpg |
0.557634 | 0e2f6b2215e9473087552a5a67518ee1 | Reproduced from Fig. 2 in Amadei et al. [1] showing the relative cumulative fluctuation against eigenvector number for an essential dynamics analysis on a 900 ps solvent MD simulation of lysozyme. This demonstrates the dominance of a relatively small number (out of a possible 3792) of “essential” eigenvectors. A Cα atoms only. B All atoms | PMC10264293 | 10930_2023_10113_Fig1_HTML.jpg |
0.427678 | 29e6ebc3f807469aad7f2428a4f49fcd | Domain movement in MBP from docking maltose to MBP with DockIT[3] using the linear response model [see Eq. (13)] to model the conformational change upon maltose binding. Only 26 eigenvalues and eigenvectors were used which were derived from a 100 ns explicit solvent MD simulation of MBP in its maltose free state. Colouring shows domains (red and blue) and hinge bending regions (green) as assigned by DynDom for the movement between the maltose-free (PDB: 1OMP) and maltose-bound structure (PDB: 1ANF). A The relaxed structure of MBP without maltose. B A closed domain MBP structure with maltose (ball-and-stick) docked into its binding site | PMC10264293 | 10930_2023_10113_Fig2_HTML.jpg |
0.444049 | 7033b1bcb0624a1b8d875c7872443b02 | From de Groot et al. [2] showing the projections onto the 2D plane defined by the first two modes of a PCA of 38 crystallographic structures of T4 lysozyme. The top left plot shows the crystallographic structures themselves and the other plots show the projected trajectories from three independent MD simulations | PMC10264293 | 10930_2023_10113_Fig3_HTML.jpg |
0.413765 | 7fd66f1344d048a48c852491931b99fa | Consequences of TMX4 silencing on NE dynamics.a CLSM analyses of endogenous SEC62 (Inset1) and HALO-NESPRIN3α-positive ONM subdomains (Inset2) delivery within LAMP1-positive endolysosomes in MEF recovering from ER stress, 12 h after interruption of the pharmacologic treatment with CPA and exposed to 50 nM BafA1. Scale bars: 10 μm. b Same as (a), in cells where TMX4 expression has been silenced by RNA interference. Also, refer to Supplementary Fig. 5a, b. c Quantification of (a) and (b) in mock-treated cells and in cells with reduced expression of TMX4. n = 34 and 45 cells for mock-treated and TMX4 knockdown cells, respectively. N = 3 independent experiments, mean ± SEM; unpaired, two-tailed t-test, ns. P = 0.3073 for SEC62. n = 34 and 45 cells for mock-treated and with TMX4 knockdown cells, respectively. N = 3 independent experiments, mean ± SEM; unpaired, two-tailed t-test, ****P < 0.0001 for NESPRIN3α. d Same as (a) in wild-type MEF overexpressing TMX4. Representative of three independent experiments. Scale bars: 10 μm. e RT-TEM micrographs of NE of two different CRISPRTMX4 MEF at steady state. Scale bars: 500 nm. f Same as (d) 2 different CRISPRTMX4 MEF during pharmacologically-induced ER stress. | PMC10264389 | 41467_2023_39172_Fig10_HTML.jpg |
0.373624 | d691087a88e94cc5a99327676a7b24dc | Morphometric changes of the NE upon ER stress and during recovery from ER stress.a Schematic representation of the ER and the NE. The inset shows the LINC complex that spans the perinuclear space (PNS) between the INM and the ONM. NPC is a nuclear pore complex. b RT-TEM micrograph showing two representative MEF at steady state. Nucleoplasm (NP in the inset), cytoplasm (CP) and the double lipid bilayer (ONM and INM) constituting the NE are shown. c Upper panel showing a slice through a CET of the NE from a lamella through a MEF at steady state. Scale bar: 50 nm. The lower panel represents the isosurface representation of the corresponding segmented volumes for NE at steady state. ONM in salmon; INM in light purple. d Quantifications of corresponding ONM-INM distances at steady state (see Tomogram 14, Supplementary Fig. 1a). e Same as (b) during the perturbation of ER homeostasis with CPA. f Same as (c) under ER stress. Scale bar: 50 nm. g Same as (d) for a cell under ER stress (see Tomogram 1, Supplementary Fig. 1b). h Same as (b) in MEF recovering from ER stress (5 h after interruption of CPA exposure). i Same as (c), for a recovering MEF. Scale bar: 50 nm. Please also refer to Movie 1. j Same as (d) for a recovering MEF (see Tomogram 1, Supplementary Fig. 1c). k Same as (b) 48 h after interruption of the pharmacologic treatment. l Violin plot showing INM:ONM distances in five representative MEF examined by RT-TEM for each condition. The dotted line shows the average width of the PNS. | PMC10264389 | 41467_2023_39172_Fig1_HTML.jpg |
0.507636 | 351c37a863b2440290877cefde3add2f | Asymmetric vesiculation of the NE and capture by endolysosomes.a Room temperature-electron tomography of a subdomain of the NE in a MEF recovering from ER stress (12 h after interruption of CPA exposure). INM and ONM are shown with arrowheads. (1) The initial stage of ONM deformation, (2) the formation of an ONM-derived vesicle, (3) a vesicle has just been released from the ONM. Refer to Movie 2. b Selected frames of Movie 3 showing the capture of a HALO-NESPRIN3-positive ONM-derived vesicle (arrowheads) by GFP-RAB7-positive endolysosomes during recovery from ER stress. | PMC10264389 | 41467_2023_39172_Fig2_HTML.jpg |
0.376297 | e0e4b0b615d74677956102c707caf963 | Lysosomal delivery of ONM subdomains.a CLSM analyses of HALO-NESPRIN3α-positive ONM subdomains delivery within LAMP1-positive endolysosomes in WT MEF at steady state (upper panels) or in MEF recovering from ER stress, 12 h after interruption of the pharmacologic treatment with CPA (lower panels). Cells incubation with BafA1 prevents clearance of cargo eventually delivered within endolysosomes. Scale bars: 10 μm. b Quantification of (a) by LysoQuant52. n = 32 and 47 cells for steady state and recovery, respectively. N = 3 independent experiments. Mean ± SEM; unpaired, two-tailed t-test, ****P < 0.0001. c Same as (a), to monitor lysosomal delivery of GFP-SUN1. Refer to Supplementary Fig. 2b, c for lysosomal delivery of endogenous SUN2. d Quantification of (c). n = 37 and 25 cells for steady state and recovery, respectively. N = 3 independent experiments, mean ± SEM; unpaired, two-tailed t-test, ns. P > 0.05. e Same as (a) in MEF lacking the autophagy gene product ATG556. f Quantification of (e). n = 33 and 29 cells for steady state and recovery, respectively. N = 2 independent experiments, mean ± SEM; unpaired, two-tailed t-test, ns. P > 0.05. g Same as (a) in MEF lacking the autophagy gene product ATG14L57–60. h Quantification of (g). n = 21 and 19 cells for steady state and recovery, respectively. N = 2 independent experiments, mean ± SEM; unpaired, two-tailed t-test, ***P < < 0.0001. | PMC10264389 | 41467_2023_39172_Fig3_HTML.jpg |
0.392721 | b7179a6ef5b346fe86fad827591199f3 | Subcellular distribution of endogenous SEC62.a RT-TEM micrograph showing immunogold labeling of endogenous SEC62 in the ER (arrowheads) and in the ONM (arrows) of MEF at steady state. b Same as (a) in MEF recovering from ER stress (12 h after interruption of the CPA treatment and exposure to 50 nM BafA1). Arrow and Inset show SEC62 in a bulge formed by the ONM. c Same as (b), where SEC62 (arrow 1) labels the limiting membrane of a vesicle caught in the act of detaching from the ONM. An endolysosome capturing SEC62-positive vesicles (a and b) by micro-autophagy is shown. Arrow 2 shows the site of vesicle engulfment. d Same as (b), where endogenous SEC62 is in a site of contact between the ONM and the endolysosome. e Same as (b), for HALO-NESPRIN3α at the ONM (arrow) and within an endolysosome next to the NE (arrowheads). | PMC10264389 | 41467_2023_39172_Fig4_HTML.jpg |
0.378333 | 7518afdbfc9c48148aaf145a274a3a5e | SEC62 is the autophagy receptor involved in the lysosomal clearance of ONM subdomains.a CLSM analyses of HALO-NESPRIN3α-positive ONM subdomains delivery within LAMP1-positive endolysosomes in MEF at steady state (upper panels) or in MEF recovering from ER stress, 12 h after interruption of the pharmacologic treatment with CPA and exposure to 50 nM BafA1 (lower panels). Scale bars: 10 μm. b Quantification of (a) by LysoQuant52. n = 23 and 27 cells for steady state and recovery, respectively. N = 3 independent experiments. Mean ± SEM; unpaired, two-tailed t-test, ****P < 0.0001. c Same as (a) in MEF lacking the autophagy receptor SEC6226,28. Also refer to Supplementary Fig. 3. d Quantification of (c) n = 20 and 27 cells for steady state and recovery, respectively. N = 3 independent experiments, mean ± SEM; unpaired, two-tailed t-test, ns. P = 0.4279 and of (e) and (f) n = 44 and 27 cells for SEC62 and SEC62LIR, respectively. mean ± SEM; unpaired, two-tailed t-test, ****P < 0.0001. e Same as (c) in CRISPRSEC62 MEF back-transfected with SEC62. f Same as (c) in CRISPRSEC62 MEF back-transfected with SEC62 with a mutation in the LIR domain preventing LC3 association. g Same as (a) in MEF at steady state, to monitor the co-localization of HALO-NESPRIN3α and endogenous SEC62. h Same as (g) in MEF recovering from ER stress. Scale bars: 10 μm. | PMC10264389 | 41467_2023_39172_Fig5_HTML.jpg |
0.444743 | 8f9e409f1e014c2f88c9fa75776baa9c | Visualizing LINC complex filaments.a Slice through cryo-electron tomogram of a NE in a FIB-milled MEF at Steady state. Scale bars represent 100 nm. b Isosurface representation of the corresponding segmented volume (ONM in salmon, INM in light purple). Filaments traced assisted by a density threshold mask on deconvoluted tomograms in Avizo in the perinuclear space are depicted in green (continuous from ONM to INM). Indicative distances between ONM and INM are given along the membrane. See tomogram 1, Supplementary Fig. 1a. c Same as (a) for cells under ER stress. d Same as (b). See tomogram 13, Supplementary Fig. 1b. e Same as (a) for recovering cells. f Same as (b). See tomogram 30, Supplementary Fig. 1c. g Schematic representation of the NE before, during and after stress. α-helical coiled-coil perinuclear domains of SUN proteins can extend for a maximal length of 45–50 nm21. Enlargement of the PNS is allowed by the reduction of the disulfide that links SUN proteins in the INM with NESPRIN proteins in the ONM. (g) was partly drawn by using pictures from Servier Medical Art in Adobe Illustrator. Servier Medical Art by Servier is licensed under a Creative Commons Attribution 3.0 Unported License (https://creativecommons.org/licenses/by/3.0/). | PMC10264389 | 41467_2023_39172_Fig6_HTML.jpg |
0.402851 | 609125733991419d973608e6933894f3 | Distribution of PDI family members in the ER and in the NE.a CLSM analysis to monitor the subcellular distribution of endogenous PDI in MEF. Scale bars: 10 µm. b Same as (a) for ERp57. c Same as (a) for ERp72. d Same as (a) for ectopically expressed TMX3-V5. e Same as (a) for ectopically expressed TMX4-V5. f Same as (a) for ectopically expressed TMX5-V5. g RT-TEM micrograph showing immunogold labeling of endogenous TMX4 in the ER (arrowheads) and in the ONM of MEF (arrows). h RT-TEM micrograph showing immunogold labeling of endogenous TEX264 in the ER (arrowheads), in the ONM and INM of MEF (arrows). The CLSM experiments were performed once. | PMC10264389 | 41467_2023_39172_Fig7_HTML.jpg |
0.451242 | e4908585c3b445239a25dcdf22719309 | Endogenous clients of TMX3, TMX4 and TMX5.a Anti V5-antibody was used to immunoisolate from HEK293 cell lysates V5-tagged versions of TMX3 (lane 2), TMX3C56A (lane 3), TMX4 (lanes 4), TMX4C67A (lanes 5) and TMX5 (lanes 6). Part of the immunoisolates has been separate in non-reducing/reducing gel (lanes 1–6 and 7–12, respectively). The gel has been silver stained. Uncropped gel in Supplementary Fig. 6. The polypeptide bands in the black and red rectangles are disulfide-bonded complexes (mixed disulfides) associated with the respective TMX protein. The complexes disappear (yellow boxes), i.e., are disassembled, when the samples are run under reducing conditions (lanes 7–12). Part of the immunoisolates has been processed for mass spectrometry (see “Methods” section) to determine the composition of the mixed disulfides and identify the endogenous proteins trapped in mixed disulfides with the given TMX protein. b Graphical representation of Supplementary Table 1. Red dots show NESPRIN proteins. | PMC10264389 | 41467_2023_39172_Fig8_HTML.jpg |
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