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0.423575 | c18e8d80c65e4248af133f6bf5a7be76 | (a) Overview STM image of an area with several Fe ML islands
of
all three types including some of the islands investigated in Figure 2a–d. (b) Fermi
energy and (c) Nb(110) coherence peak spectral weights taken from
spectroscopic grids over the same area recorded by following the tip
height from (a) but with e·V = 1 meV = Δt (b) and e·V = 2.5 meV = Δt + Δs (c). (d) Line
profiles of the height (top panel) and Nb(110) coherence peak spectral
weight (bottom) taken along identical lines across the type I island
shown in (a) and (c), respectively (I = 200 pA, V = 6 mV, Vmod = 0.1 mV
(a); V = 1.13 mV, Vmod = 0.1 mV (b); V = 2.5 mV, Vmod = 0.1 mV (c)). All measurements were
done at Bz = 0 T. | PMC9527798 | nn2c03965_0004.jpg |
0.431704 | 48155b3cc151408f85cecf654c9e3854 | Excitation-emission matrix (EEM) positions of fibril-bound ThT fluorescence (A) and selected fibril sample FTIR spectra (B) and their second derivatives (C).EEM maximum positions were determined as described in the Materials and Methods section (96 samples) after sample aggregation. Red color-coded circles marked with Roman numerals represent samples chosen for further analysis. | PMC9528901 | peerj-10-14137-g001.jpg |
0.418256 | 22ec712ed98f493795ebe3df38491e4e | Fourier-transform infrared (FTIR) spectra and second derivatives of α-syn fibril samples before and after incubation at 60 °C and reseeding at 37 °C.Type 1 (A, E), Type 2 (B, F), Type 3 (C, G) and Type 4 (D, H) fibril sample FTIR spectra and second derivatives. Black lines correspond to the control samples, orange–after 24 h of incubation at 60 °C, blue–after 48 h of incubation at 60 °C and green–48 h incubation samples reseeded at 37 °C. Dotted grey lines indicate the main maximum position of the initial sample FTIR spectrum. Superimposed FTIR spectra of all four fibril types before (I) and after 48 h of incubation at 60 °C (J). | PMC9528901 | peerj-10-14137-g002.jpg |
0.428194 | f01412bb285142139180d658e3b6c5b4 | Comparison of alpha-synuclein aggregation kinetics and resulting structure under different temperatures.The lag time (A) and apparent rate constant of fibril elongation (B) at 37 °C and 60 °C (n = 8). Superimposed FTIR spectra of Type 1–4 incubated fibrils (blue color) and eight spectra of fibrils prepared at 60 °C (red color). | PMC9528901 | peerj-10-14137-g003.jpg |
0.427503 | 28d363df7eef478f875d2b1cf93efdca | Atomic force microscopy (AFM) images of different fibril types before and after incubation.AFM images of Type 1 (A, E), Type 2 (B, F), Type 3 (C, G) and Type 4 (D, H) fibrils, as well as height (I), width (J) and periodicity (K) distribution before and after incubation respectively. All images are of identical 5 × 5 µm scale. Fibril height, width and periodicity were determined as described in the Materials and Methods section. Distribution box plots (n = 50) indicate the interquartile range and error bars are for one standard deviation. | PMC9528901 | peerj-10-14137-g004.jpg |
0.434999 | a9057e8755bc487da11484f6f1d22664 | Alpha-synuclein fibril secondary structure element distribution during incubation at 60 °C.The secondary structures for Type 1 (A), Type 2 (B), Type 3 (C) and Type 4 (D) fibrils were determined by scanning each sample’s CD spectra after different periods of incubation and fitting the data using BeStSel Protein circular dichroism spectra analysis software. The normalized root mean square deviation (NRMSD) of each sample’s secondary structure element distribution is displayed under their respective distribution graphs. | PMC9528901 | peerj-10-14137-g005.jpg |
0.497465 | dd6640c93fcc4fd08580307dd7fcf1a3 | Absorbance and fluorescence spectra of fibril-bound ThT during incubation at 60 °C.Absorbance spectra of Type 1 (A), Type 2 (B), Type 3 (C) and Type 4 (D) fibril-bound ThT before and after incubation at 60 °C for 24 and 48 h. Optical density of all four samples before and after incubation (E), determined at 600 nm. Sample bound-ThT fluorescence EEM position changes over the course of 10 h of incubation (F). The change in EEM positions over time is represented as a color gradient in subfigure F (lighter color–shorter incubation time, darker color–longer incubation time). The initial 0 h sample EEM positions were measured after the samples reached 60 °C (the heating procedure was 10 min). Sample absorbance and fluorescence measurement procedures are described in the Materials and Methods section. Absorbance data is the average of three repeats. | PMC9528901 | peerj-10-14137-g006.jpg |
0.502006 | 321d238e509a481d93c38a0e6e356928 | Comparative atlas of TGD-duplicated regions across 74 teleosts. (A) Phylogenetic tree of the 74 teleost genomes in the comparative atlas and 27 outgroups. The color map represents the proportion of genes from each species annotated in the comparative atlas. Divergence times were extracted from TimeTree (Kumar et al. 2017). (B) Karyotype paintings using the comparative atlas. At the top, we show the inferred ancestral karyotype after the teleost whole-genome duplication (TGD). Below, karyotypes of three teleost genomes are colored by their ancestral chromosome of origin according to the comparative atlas (1a, 1b, …, 13a, 13b). | PMC9528989 | 1685f01.jpg |
0.422405 | 1f8166c9fe534a2f87769665167074ab | Delayed rediploidization following the TGD. (A) Gene tree topologies expected under the AORe and LORe models. The AORe tree topology assumes that rediploidization was complete before the divergence of Osteoglossiformes and Clupeocephala, initiating “a” and “b” gene sequence divergence before speciation. The LORe tree topology assumes that rediploidization was completed only after the divergence of Osteoglossiformes and Clupeocephala, delaying “a” and “b” duplicated sequence divergence to after speciation. (B) Ancestral Chromosomes 3, 10, and 11 are enriched in sequence-synteny conflicts (Methods, [***] P < 0.001, hypergeometric tests with Benjamini–Hochberg correction for multiple testing). Color labels identify ancestrally duplicated chromosomes as in Figure 1B. (C) Examples of an AORe gene tree. For the col12a1a - col12a1b family, the LORe topology is inconsistent with gene sequence evolution (P = 4 × 10−9, AU-test). (D) Example of a LORe gene tree. For the map1aa - map1ab family, AORe was rejected (P-value = 0.001, AU-test). (E) AORe and LORe gene families visualized on the medaka karyotype. Medaka chromosomes are annotated as numbers, whereas color labels represent ancestral chromosomes (Methods), as in (B). Homeologs 3, 10, and 11 almost entirely rediploidized later than the Osteoglossiformes/Clupeocephala divergence. | PMC9528989 | 1685f02.jpg |
0.449693 | f49d3e13fab04ef5a5f65d76ef1a58bf | Differences in gene retention, selective pressure, and gene expression between duplicated chromosomes. (A) Schematic example of gene retention calculation. Using an outgroup genome as an approximation of the ancestral gene order, we assess gene retention on each duplicated chromosome in teleost genomes, by 10-gene bins, regardless of their genomic location (Methods). (B) Gene retention on anciently duplicated chromosome copies in medaka, using the spotted gar genome as a proxy for ancestral gene order. Ancestral chromosomes with a significant bias in gene retention on one of the two copies are highlighted ([***] P < 0.001, [**] P < 0.01, [*] P < 0.05, Wilcoxon paired tests with Benjamini–Hochberg correction for multiple testing). (C) Number of genes experiencing relaxed selection compared with their ohnolog across homeologs (Methods; Fisher's exact tests with Benjamini–Hochberg correction for multiple testing, P-values as in B). (D) Average expression across tissues in medaka. No significant differences in expression were detected between genes of duplicated chromosome copies (Wilcoxon paired tests with Benjamini–Hochberg correction for multiple testing, at α = 0.05). | PMC9528989 | 1685f03.jpg |
0.374681 | 86b1b2e821754cc1a6eb33f1cec12add | Zebrafish gene names are not evolutionarily consistent. (A) Karyotypic localization of zebrafish “a” and “b” TGD ohnologs, according to the ZFIN annotation. ZFIN does not annotate genes as either “a” or “b” when one of the TGD paralogs has been lost, and these genes are not represented here. (B) Complementary annotation of zebrafish “a” and “b” gene copies using the comparative atlas (84% of zebrafish genes annotated, including genes without a TGD ohnolog). | PMC9528989 | 1685f04.jpg |
0.438013 | 4bfbda9864834432b6515acfe047472f | Forest plot of CAD risk associated with the VDR polymorphism.CAD = Coronary artery disease, A: rs2228570 polymorphism; B: rs1544410 polymorphism; C: rs731236 polymorphism; D: rs7975232 polymorphism. VDR = vitamin D receptor, OR = odd ration, CI = confidence interval. | PMC9529108 | pone.0275368.g001.jpg |
0.477237 | f82b3e11f49742f5ae4df89d5c79a584 | Forest plot of CAD risk associated with the VDR polymorphism in the subgroup analysis stratified by race.A: rs2228570 polymorphism; B: rs1544410 polymorphism; C: rs731236 polymorphism; D: rs7975232 polymorphism. CAD = Coronary artery disease, VDR = vitamin D receptor, OR = odd ration, CI = confidence interval. | PMC9529108 | pone.0275368.g002.jpg |
0.480096 | 78b0b363ea2645e5a534fa1e6f558232 | Sensitivity analysis of CAD risk associated with the VDR polymorphism.A: rs2228570 polymorphism; B: rs1544410 polymorphism; C: rs731236 polymorphism; D: rs7975232 polymorphism. CAD = Coronary artery disease, VDR = vitamin D receptor, OR = odd ration, CI = confidence interval. | PMC9529108 | pone.0275368.g003.jpg |
0.419684 | 79bffb7e83b94a0eaa6c88a1f3858dfc | The Begg’s plot of Publication bias for the VDR polymorphism.A: rs2228570 polymorphism; B: rs1544410 polymorphism; C: rs731236 polymorphism; D: rs7975232 polymorphism. CAD = Coronary artery disease, VDR = vitamin D receptor, OR = odd ration, CI = confidence interval. | PMC9529108 | pone.0275368.g004.jpg |
0.44274 | bf0e8355fd75485fb2b198809eabd77d | Trial sequential analysis of VDR rs1544410 polymorphism in overall population.VDR = vitamin D receptor. | PMC9529108 | pone.0275368.g005.jpg |
0.531383 | ed4477042bc140c6971148b035ecf419 | Trial sequential analysis of VDR rs2228570 and rs731236 polymorphisms in the White population.VDR = vitamin D receptor. | PMC9529108 | pone.0275368.g006.jpg |
0.428105 | fa7aa4254dbc43fea180702aabfe7778 | The RNAfold structure analysis of the VDR rs1544410 polymorphism.A: rs2228570 polymorphism; B: rs731236 polymorphism. VDR = vitamin D receptor. | PMC9529108 | pone.0275368.g007.jpg |
0.450473 | 3fec8512d14d4ab8a6f8a9d938100e31 | EGA of comorbidity patterns with bootstrap (nboot = 200) (right). The greater the thickness of the connections, the greater the magnitude of the statistical relationships. The thickness of the line is equivalent to the magnitude of the ratio. (1) Arthritis, (2) Obesity, (3) Diabetes, (4) Kidney disease, (5) High blood pressure, (6) High blood cholesterol, (7) Heart attack, (8) Coronary heart disease, (9) Asthma, (10) Stroke, (11) Respiratory diseases, (12) Depression. | PMC9530468 | fpubh-10-981944-g0001.jpg |
0.459094 | f10dd8e5bf1d4f4389db789a8d26ef0c | Centrality indexes of chronic conditions. Centrality refers to the measure with the highest number of connections together with the sum of the relationships it presents. Numbers refer to a chronic condition identified in Table 3. (1) Arthritis, (2) Obesity, (3) Diabetes, (4) Kidney disease, (5) High blood pressure, (6) High blood cholesterol, (7) Heart attack, (8) Coronary heart disease, (9) Asthma, (10) Stroke, (11) Respiratory diseases, (12) Depression. | PMC9530468 | fpubh-10-981944-g0002.jpg |
0.463504 | 9f30d2661cd4426b9298fe5400f9bbbb | Empirical communities of the 12 chronic conditions of the EGA. The nodes represent each replication of the item (comorbidity) in the original dimension specified by the EGA. (1) Arthritis, (2) Obesity, (3) Diabetes, (4) Kidney disease, (5) High blood pressure, (6) High blood cholesterol, (7) Heart attack, (8) Coronary heart disease, (9) Asthma, (10) Stroke, (11) Respiratory diseases, (12) Depression. | PMC9530468 | fpubh-10-981944-g0003.jpg |
0.441001 | ff7a4a5b4fa44c74af7d04838c0a188f | Flow chart diagram of the study. | PMC9531127 | fmed-09-993086-g001.jpg |
0.407028 | 94a0df39ffce4c13bf04064fb3b797bf | Characterization of exosomes and their internalization into NRCMs. A Representative images of CON-EXO and HHP-EXO under transmission electron microscopy (inlets) and their size distribution by NanoSight NS300. B Western blots showing the significant expression of the exosome markers CD9, TSG101 and Alix in CON-EXO and HHP-EXO. C Exosomes were immunoprecipitated with Anti-FLAG affinity resin and probed with antibodies against the exosome markers CD9, TSG101 and Alix. D Representative images showing the internalization of CM-Dil-labeled HHP-EXO or CON-EXO (red) into FITC-phalloidin stained NRCMs (green) and DAPI counter-stained nuclei (blue). E Typical flow cytometry plots showing the internalization of CM-Dil-labeled HHP-EXO or CON-EXO into NRCMs after 24 h incubation. F Mean fluorescence intensity in E (n = 3). Data are presented as ‘Mean ± SEM’, **P < 0.01 | PMC9531502 | 12951_2022_1630_Fig1_HTML.jpg |
0.421967 | deec086fac8b49f28d872fd8027ae1a1 | In vivo distribution of exosomes. CM-DiL-labeled CON-EXO or HHP-EXO was administered systemically for 24 h, and the hearts, spleens, kidneys, lungs and livers were harvested to evaluate their fluorescent intensity of the whole organs (A), and their mean fluorescent intensity in the hearts (B) and other organs (C) (n = 3). Data are presented as ‘Mean ± SEM’, with ** denoting P < 0.01 | PMC9531502 | 12951_2022_1630_Fig2_HTML.jpg |
0.412329 | d4fb1e1aa2c04f779c98e0ed1c702e0c | HHP-EXO improves cardiac function. A Representative 2D echocardiographic images in mice among groups. B Quantitation of LVEF, LVFS, and LVVs among groups (n = 8). C Quantitation of LVAWd, LVAWs, and left ventricular mass (n = 8). D Quantitation of mean artery blood pressure and serum Ang II level among groups (n = 8). E Quantitation of lung wet/dry weight and serum levels of NT-pro BNP among groups (n = 8). F Quantitation of the ratio of kidney/body weight and serum creatinine level (n = 8). Data are presented as ‘Mean ± SEM’, with *P < 0.05 and **P < 0.01(compared to sham); and #P < 0.05 and.##P < 0.01 (compared to PBS) | PMC9531502 | 12951_2022_1630_Fig3_HTML.jpg |
0.460107 | 477aea2fbf8c4881b5c78762a49983d5 | HHP-EXO improves TAC-induced myocardial hypertrophy and cardiac fibrosis. A Representative gross morphology of the hearts and the HE and WGA stained ventricular sections among groups. B Quantification of relative cell surface area of left ventricular sections stained with WGA in Fig. 4A (left panel). Quantification of the expression of Myh7/Myh6 ratio, Acta1, Nppa and Nppb in left ventricular tissues of different animal groups as described in (A) (right panel) (n = 4–8). C Left ventricular sections stained with Masson’s staining (left panel) (n = 4–8). D Quantitation of fibrotic area in C (right panel) and the expression of fibrotic genes Col1a1, Col3a1, Fn1 and Ctgf in left ventricular tissues among groups (n = 4–8). Gene expression was normalized to that of GAPDH. Data are presented as Mean ± SEM, with *P < 0.05 and **P < 0.01 | PMC9531502 | 12951_2022_1630_Fig4_HTML.jpg |
0.520643 | ee4f338cb6a0492f8d1ce53c772b44b2 | HHP-EXO inhibits TAC-induced expression of hypertrophy markers and the activation of ERK, AKT, STAT3 signaling pathways. A Representative images of Western blot showing the expression of β-MHC, BNP, GP130, STAT3, p-STAT3, ERK, p-ERK1/2, AKT and p-AKT in left ventricular tissues among different treatments. B Quantification of the expression of β-MHC, BNP and GP130 among groups (n = 4–7). C Quantification of the ratios of p-STAT3/STAT3, p-ERK1/2/ERK, and p-AKT/AKT among groups (n = 4–7). Protein expression was normalized to that of GAPDH. Data are presented as Mean ± SEM, with *P < 0.05 and **P < 0.01 | PMC9531502 | 12951_2022_1630_Fig5_HTML.jpg |
0.458102 | 44752dc9ea2443d09def5f078ee3cd4d | Exosomal miRNA-148a mediates the cardiac protective effect of HHP-EXO. A Relative levels of miRNA-148a in left ventricles among different treatment groups (left panel), and in CDCs and CDCs-derived exosomes (right panel). B Representative images of hypertrophic NRCMs induced by 1 µM Ang II and treated with PBS, HHP-EXO, HHP-EXO-NC or HHP-EXO-miRNA148i. NRCMs were stained with FITC-phalloidin and nuclei were counterstained with DAPI. C The mean cell surface area in B (n = 12–21 cells). D Representative images showing the expression of β-MHC, BNP, GP130, p-STAT3, STAT3, p-ERK1/2, ERK, p-AKT and AKT among groups in B (n = 4–6). E Quantitation of the expression of β-MHC, BNP, GP130, and ratios of p-STAT3/STAT3, p-ERK1/2/ERK, and p-AKT/AKT among groups in B (n = 4–6). The expression of miRNA-148a was normalized to that of U6, and protein expression was normalized to that of GAPDH. Data are presented as Mean ± SEM, with *P < 0.05 and **P < 0.01 | PMC9531502 | 12951_2022_1630_Fig6_HTML.jpg |
0.403972 | 3cae4fe0687c4e2abecf87501daa0ecb | Schematic illustration of how exosomal miRNA-148a from HHP-EXO protects against pressure overload-induced cardiac hypertrophy | PMC9531502 | 12951_2022_1630_Fig7_HTML.jpg |
0.415752 | a123b1edd394403fbad9e61fd4e54f67 |
(A) The mutation frequency in each regulator. (B) Heatmap of m6A RNA methylation regulator expression level in each sample. **p<0.01; ***p<0.001. (C) The expression difference of m6A RNA methylation regulator between tumor and normal samples. (D) Correlation among PD-1, PD-L1 and m6A RNA methylation regulators. | PMC9533337 | fonc-12-1004212-g001.jpg |
0.454791 | ceaa917b487b4d929bf895b64b913238 | Correlation of consensus clustering for m6A RNA methylation regulators with the characteristics and survival of PDAC patients. (A) Consensus clustering matrix for k=2 (left panel); Consensus clustering cumulative distribution function (CDF) for k=2 to 9 (middle panel); relative change in area under CDF curve for k=2 to 9. (B, C) Heatmap of correlation of m6A RNA methylation regulators with characteristics of PDAC patients. (D) Kaplan-Meier curves of overall survival (OS) for patients. | PMC9533337 | fonc-12-1004212-g002.jpg |
0.39793 | 6316bfab86994c3498925f5580634e4c |
(A) Heatmap of infiltrating levels of various immune cells in cluster1/2 in pancreatic cancer. (B) Estimated proportion of 22 immune cell types in cluster1/2 in pancreatic cancer. *p<0.05; ns, no significance. | PMC9533337 | fonc-12-1004212-g003.jpg |
0.429587 | 290186ccdb38491984b63469f245011f | StromalScore (A), ImmunoScore (B), EstinateScore (C) in the cluster1/2 subtypes are illustrated. (D): The signaling pathways are involved in cluster1 and cluster2. | PMC9533337 | fonc-12-1004212-g004.jpg |
0.436817 | a52ed9685c0348beabaaca52f08a6fce |
(A) Univariate analysis of 24 regulators. (B, C) LASSO Cox regression algorithm. (D) The Kaplan-Meier curve of high risk and low risk group. (E) Time-dependent ROC curves. (F, G) Univariate and multivariate Cox regression analysis of the risk scores in TCGA. | PMC9533337 | fonc-12-1004212-g005.jpg |
0.409629 | 19042ac60a0d4195987eed7316550a2a |
(A) Heatmap of clinicopathological features of pancreatic cancer cohort. (B) Distribution of risk scores stratified by cluster1/2. (C) The expression of PD-1 and PD-L1 in tumors, cluster1/2 and high/low-risk groups. *p<0.05; **p<0.01; ***p<0.001; ****p<0.0001. ns, no significance. | PMC9533337 | fonc-12-1004212-g006.jpg |
0.497467 | cd34a099456240ae9afc2935904394b6 | The relationship between METTL3, lncRNA MALAT1 and PD-L1 in PADC cells. (A) Western blotting was used to measure the expression of PD-L1 in BxPC-3 and PANC-1 cells after METTL3 modulation. (B) RT-PCR was used to measure the expression of lncRNA MALAT1 in BxPC-3 cells after METTL3 modulation. (C) RT-PCR was used to test the expression of PD-L1 in BxPC-3 cells after lncRNA MALAT1 changes. D-E: RT-PCR was used to measure the expression of MALAT1 in BxPC-3 (D) and PANC-1 cells (E) after MALAT1 modulation. **p<0.01. | PMC9533337 | fonc-12-1004212-g007.jpg |
0.469023 | e3a137702b1142efb4550404b2edaab2 | LncRNA MALAT1 regulates viability of pancreatic cancer cells. (A) CCK-8 assay was used to measure the viability of BxPC-3 and PANC-1 cells after MALAT1 overexpression. (B) CCK-8 assay was conducted to measure the viability of BxPC-3 and PANC-1 cells after MALAT1 downregulation. **p<0.01. | PMC9533337 | fonc-12-1004212-g008.jpg |
0.426857 | 843b2b6e46704f35953bbe5ec751ff75 | RNF31 Q622H polymorphism in patients with lung cancer and ABC-DLBCL. (A) DNA sequence electropherograms of the region corresponding to the Q622H polymorphism in lung cancer and blood. (B) Clinical course of the patients with the Q622H polymorphism. UFT, uracil tegafur; ABC-DLBCL, activated B cell-like subtype of diffuse large B-cell lymphoma; R-CHOP, rituximab, cyclophosphamide, doxorubicin, vincristine, prednisone; VNR, vinorelbine; PEM, pemetrexed; DTX, docetaxel; TS-1, tegafur/gimeracil/oteracil; RNF31, RING finger protein 31. | PMC9533369 | ol-24-05-13514-g00.jpg |
0.373683 | 08af885b75364c34b1529538d496f88e | Histological findings of lung cancer and ABC-DLBCL with the RNF31 Q622H polymorphism. HE staining and IHC of RNF31 and p65. HE staining showed well differentiated adenocarcinoma with lepidic growth for the lung cancer specimen (case 1); lung adenocarcinoma with solid component for the lung cancer, tumor cells surrounded with fibrous tissue for the lymph node recurrence, and large, atypical cells with high nuclear-cytoplasmic ratio for the ABC-DLBCL specimen (case 2). Scale bar for HE staining=200 µm, IHC images for p65 staining are magnified (×400) to clarify nuclear localization. HE, hematoxylin and eosin; IHC, immunohistochemistry; ABC-DLBCL, activated B-cell-like subtype of diffuse large B-cell lymphoma; RNF31, RING finger protein 31. | PMC9533369 | ol-24-05-13514-g01.jpg |
0.495042 | 87d659e5fa64460a84deb98cdc5ad25c | Genetic analysis of lung cancer and ABC-DLBCL in a patient with the RNF31 Q622H polymorphism. Mutations detected in lung adenocarcinoma, ABC-DLBCL and adjacent normal lung tissue. Mutations identified by COSMIC v.70 selection are indicated with an asterisk. ABC-DLBCL, activated B-cell-like subtype of diffuse large B-cell lymphoma; RNF31, RING finger protein 31. | PMC9533369 | ol-24-05-13514-g02.jpg |
0.424471 | 388fe44c61f54e96a85942761bd34a43 | In vitro assessment and predicted crystal structure model of RNF31 Q622H polymorphism. (A) Activation of NF-κB by RNF31 WT/Q622H/Q622L/Q584H. NF-κB activation by LUBAC was evaluated using luciferase reporter assay (upper panel) in RNF31-KO 293T cells. The expression of each protein was evaluated using western blotting (lower panel). (B) Linear ubiquitin formation by RNF31 WT/Q622H/Q622L/Q584H. The LUBAC expression vectors were co-expressed in RNF31-KO 293T cells, and cell lysates were immunoblotted with the indicated antibodies. (C) Effect of RNF31 Q622H/Q622L/Q584H polymorphisms on RNF31, RBCK1 and SHARPIN binding. FLAG-RNF31, RBCK1-myc, and HA-SHARPIN were overexpressed in RNF31-KO 293T cells, as indicated. The cell lysates and anti-FLAG immunoprecipitates were immunoblotted with the indicated antibodies. (D) Crystal structure of human RNF31 UBA domain (cyan) in complex with RBCK1 UBL domain (green) (PDB: 4dbg). (E) Mouse RNF31 UBA domain (magenta) in ternary complex with RBCK1 (green) and SHARPIN (yellow) (PDB: 5y3t). (F) Superposition of human and mouse RNF31 UBA domains. Interaction between human E618 and Q622 is shown in black dotted line. WT, wild-type; RNF31, RING finger protein 31; LUBAC, linear ubiquitin chain assembly complex; KO, knockout; RBCK1, RANBP2-type and C3HC4-type zinc finger containing 1; SHARPIN, SHANK-associated RH domain interactor; HA, hemagglutinin. | PMC9533369 | ol-24-05-13514-g03.jpg |
0.442229 | d53ebd1817f0477991bb6e2013fd0d2a | Examen del nervio facial que denota parálisis facial izquierda con clasificación de tipo II en la escala de House-Brackmann: a. Desviación de la comisura labial izquierda. b. Imposibilidad de cerrar el ojo izquierdo completamente | PMC9534523 | 2590-7379-bio-42-03-6308-gf1.jpg |
0.477985 | a06e3a64c21a4f82bcfba234f8d245d9 | Analysis of the characteristics of teenagers' physical and mental health in the digital humanistic environment. | PMC9534699 | JEPH2022-2464083.001.jpg |
0.440404 | 19a56e8338dd41b5aae1665fee608524 | Effect analysis of internationalization of Chinese literature in different ages on shaping physical and mental health of teenagers. | PMC9534699 | JEPH2022-2464083.002.jpg |
0.418802 | bb6cfe1f46b544b5bd99803515da8b41 | An analysis of the influence of literary communication on teenagers' physical and mental health in different environments. | PMC9534699 | JEPH2022-2464083.003.jpg |
0.471033 | 987dc009c884439ebf24874c2bd87311 | Analysis of the coupling degree of the influence of Chinese literature internationalization on the physical and mental health of teenagers. | PMC9534699 | JEPH2022-2464083.004.jpg |
0.47661 | d6331990f75b4102853d2e3c637e765c | Patient flowchart. Hb, haemoglobin; ICU, intensive care unit; P(v-a)CO2/C(a-v)O2, the ratio of venous-arterial carbon dioxide tension difference to arterial-venous oxygen content difference. | PMC9535211 | bmjopen-2021-059454f01.jpg |
0.393781 | 9391a03e484d451d88e09a65d3ff31d9 | Audiogram (case 1). | PMC9535481 | gr1.jpg |
0.437664 | 9c635c58fad84967a36b5d3bd637de61 | High-resolution computed tomography scan showing fusion of ear incus-malleolar joint and high jugular bulb to the right (case 4). | PMC9535481 | gr10.jpg |
0.497003 | 4458cab86a544f9597b114a7b863076f | Audiogram (case 5). | PMC9535481 | gr11.jpg |
0.503606 | 8e0f569812d14c7da53447065a3d55cd | High-resolution computed tomography scan of left ear, demonstrating hypoplasia of round window (case 5). | PMC9535481 | gr12.jpg |
0.422652 | b64153b4a1854f23804a12a156919c74 | High-resolution computed tomography of the left ear (case 1), coronal (a), sagittal (b), bone window (c). | PMC9535481 | gr2.jpg |
0.454486 | bd6a55dc8e2448ca90c72f0c76097bf7 | Tympanogram and audiogram (case 2). | PMC9535481 | gr3.jpg |
0.439728 | 5e1ab96b87a34e8ba6dd220e10ece9eb | High-resolution computed tomography of the left ear (case 2), demonstrating absence of the oval window and change in the course of facial nerve. | PMC9535481 | gr4.jpg |
0.435602 | 1503fb4c27814f8ea3a1e3cf4e14ae04 | Audiogram andtympanogram (case 3). | PMC9535481 | gr5.jpg |
0.455943 | 26c26ceebb0e47fa8736c23821730195 | High-resolution computed tomography of the left ear (case 3), demonstrating absence of stapes and of incus lenticular apophysis. | PMC9535481 | gr6.jpg |
0.444697 | 57d5caf7c04344528559d754d9aacf1b | High-resolution CT scan of left ear (case 3), demonstrating dehiscence of facial nerve canal. | PMC9535481 | gr7.jpg |
0.400479 | f9e2b9e86d02490d8262620e5e6602b5 | High-resolution CT scan of left ear (case 3) showing a persistent stapedial artery. | PMC9535481 | gr8.jpg |
0.486892 | 89b2384f03974f81a3bacaf2e7158c84 | Audiogram (case 4). | PMC9535481 | gr9.jpg |
0.454297 | d5c8a4ec615d4c1db77da98428af6344 | Cofilin-actin rods in neurons. Actin and cofilin bind to each other in a 1:1 ratio. Persistent cofilin-actin rods can occur under stress conditions, such as ATP depletion or oxidative stress brought upon by ROS. In neurons, these rods accumulate in the cytoplasm of processes (cytoplasmic rods) and in the nucleus (nuclear rods). Created with www.biorender.com. | PMC9535683 | fncel-16-982074-g001.jpg |
0.477141 | 7c53ade08d674572bd54a92ea10919fe | Cofilin-actin rod causes and effects. Cytoplasmic rods can be induced by multiple types of stress, such as ATP depletion, oxidative stress, and a decrease in cellular pH. Dephosphorylation of cofilin and association with actin in a 1:1 ratio leads to rod formation in the presence of oxidative stress. Post-translational modifications (PTM) of actin and cofilin may also be an emerging area for rod regulation. The rods block critical intracellular trafficking of organelles such as mitochondria and results in ATP depletion and impaired synaptic activity. The disruption of actin dynamics due to sequestered cofilin decreases dendritic spines and loss of synaptic plasticity, leading to loss of memory and cognitive ability over time. Interestingly, nuclear rods are similarly formed in the nucleus after nuclear translocation due to heat shock, DMSO, or ATP depletion. Other actin-binding proteins (ABPs), including the Huntingtin mutant, associate with the nuclear rods and form persistent rods that can affect transcription and chromatin remodeling. Both cytoplasmic and nuclear rods can lead to AD, HD, and PD pathologies. | PMC9535683 | fncel-16-982074-g002.jpg |
0.445274 | aeb1bc88e84a449e964b1c20065d6e27 | Cofilin-actin rod forming pathways with activators and inhibitors. Cofilin-actin rods can be induced through multiple separate pathways. Calcineurin (PP2B) or RanBP9 stimulation of SSH1 or chronophin (CIN) dephosphorylates and activates cofilin, which under stress can form aberrant rods with actin. Inhibitors of SSH1, such as 14-3-3 and pS3 peptide, can prevent rod formation. Miuraenamide and profilin overexpression can prevent actin from associating with cofilin, and tetracycline can disrupt rods. Aβ induction of integrin/RanBP9 or NOX with PrPc promotes rod formation, but Vas2870 can inhibit NOX generation of ROS. CuB activates the Gα13/RhoA/VASP pathway and increases actin assembly. LIMK, activated by PAK and RhoA/ROCK, phosphorylates and inactivates cofilin. Inhibitors of LIMK, such as the S3 peptide or Pyr-1, can promote cofilin-actin rod formation. Created with www.biorender.com. | PMC9535683 | fncel-16-982074-g003.jpg |
0.423741 | 4703d3a4d7af46d2aa8477fc6d91f747 | Genetically encoded cofilin-actin rod reporters. (A) CofilinR21Q-mRFP incorporates into cofilin-actin rods formed under various stress-inducing stimuli. The association is reversible once the stress solution is removed from cells. (B) CofActor (Cry2-Cof.S3E and Actin-CIB) forms rod-like structures in response to a combination of stress-inducing stimulus and blue light. The clusters revert to the non-associated state once the blue light is turned off. Created with www.biorender.com. | PMC9535683 | fncel-16-982074-g004.jpg |
0.484973 | 2ef7e91158b94f14be1558b388779fba | Sustainable rabies control plan. (a, b, c) Routes of rabies transmission. | PMC9537038 | JTM2022-5942693.001.jpg |
0.406078 | 64e67a186c984da19dc42e731f33743d | (a, b) Close interface between dogs and humans (photos kindly provided by Dikpal Karmacharya, Third Pole Conservancy, Bhaktapur, Nepal). The photographs represent the common situation of human-domestic animal existence globally. | PMC9537038 | JTM2022-5942693.002.jpg |
0.454201 | 58c393f0dde6406eb4abee612eaafad0 | (A) Representative traces of neurons from the Asian citrus psyllid (ACP) RP4 sensillum during exposure to a 1-s stimulus of water vapor alone (top), or water vapor coapplied with dimethylamine (middle) and 2-phenylethanamine (bottom). The stimulation period is indicated by the solid bars. Odorant headspace from a 10–2 concentration solution was tested for each. (B) Mean responses for a 1-s period of stimulation from each ACP RP sensillum in response to water vapor alone. n = 3 sensilla from 3 psyllids. Error bars indicate s.e.m. (C) Mean percent inhibition of ACP RP4 neural activity caused by 1% concentration of each of the three displayed compounds. n = 3 sensilla from 3 psyllids. Error bars indicate s.e.m. (D) Mean neuronal activity in spikes per second of the ACP RP4 neuron caused by the three displayed compounds across several concentrations. n = 3 sensilla from 3 psyllids. Error bars indicate s.e.m. | PMC9537525 | 41598_2022_20488_Fig1_HTML.jpg |
0.44798 | 3fab2ef78eef4d47ba50fb1ec0791e7a | (A) Representative traces from the ac1 neurons for a 1-s period of stimulation with water vapor (top) and hexylamine (middle) in a dry air stream, as well as hexylamine (bottom) in a humidified air stream. Odorant headspace from a 10–2 concentration solution was tested for each. (B) Mean responses. Each count was begun at the start of the increase in spike frequency. All compounds were dissolved in paraffin oil. All recordings were obtained from 3–5 days old wildtype (CS) flies. n = 5–6 sensilla from 5–6 flies. Error bars indicate s.e.m. *p < 0.05; **p < 0.01. (C) Representative traces from the ac3 neurons for a 1-s period of stimulation of propionic acid (top) or hexylamine (middle) in a dry air stream, and hexylamine (bottom) in a humidified air stream. Odorant headspace from a 10–2 concentration solution was tested for each. (D) Mean counts begun at the start of the increase in spike frequency. All recordings were obtained from 3–5 day old wildtype (CS) flies. n = 6 sensilla from 6 flies. Error bars indicate s.e.m. *p < 0.05. All compounds were dissolved in paraffin oil. | PMC9537525 | 41598_2022_20488_Fig2_HTML.jpg |
0.390184 | 8a4a65b698d940bfb1c2c1ab1a2184a1 | (A) Schematic drawing of the Y-maze used for ACP two-choice behavioral assays. Behavioral preference index of ACP to humid air at the indicated concentrations versus dry air, and dry air (dry/dry) or moist air at 75% (wet/wet) pumped into both arms as controls. N = 5–12 trials of 20 male psyllids for each dose. Error bars indicate s.e.m.; ** p < 0.01; *** p < 0.001. (B) Behavioral preference index of ACP to dry air (dry/dry, Left) or moist air at 75% (wet/wet, Right) pumped into both arms as controls and wet or dry air versus wet or dry air with 1% pentylamine. n = 6–12 trials of 20 male psyllids for each humidity level. Error bars indicate s.e.m.; ***p < 0.001. (C) Schematic representation of two-choice mosquito oviposition assay. (D) Left. Oviposition preference index in Aedes aegypti mosquitoes to the indicated concentration of pentylamine versus water alone. n = 4–6 trials with 15 mosquitoes per trial. Error bars represent s.e.m. *p < 0.05. Right. Oviposition preference index in Anopheles mosquitoes to the indicated concentration of pentylamine versus water alone. n = 4 and 6 trials respectively, with 15 mosquitoes/trial. Error bars represent s.e.m. *p < 0.05. | PMC9537525 | 41598_2022_20488_Fig3_HTML.jpg |
0.480345 | 99c8cd4d856c4b6e9f699efea0221861 | Combinatorial effects of a low dose of SB and IR on clonogenic potential and proliferation of DU145 cells.(A) Human PCa DU145 cells were seeded in a 6-well culture plate at a density of 600 cells/well and treated with either SB (25 µM) or IR (5 Gy) or in combination and were maintained in a humidified CO2 incubator. After 10 days, plates were processed for the clonogenic assay as described in MATERIALS AND METHODS. Representative images for each treatment group and (B) quantitative data are represented as the total number of colonies/well. (C, D) Fourty thousand cells/well seeded in a 12-well plate were treated with SB (25 µM) and IR (5 Gy). After the 48-hour treatments, cells were trypsinized, harvested and processed for trypan blue staining and live and dead cells were counted using haemocytometer. (E, F) At ~70% confluency, DU145 cells were treated with SB (25, 50, and 100 µM) and harvested after 12 and 24 hours. Whole cell lysates were prepared as described in MATERIALS AND METHODS, and immunoblotting was done for Rad51 protein expression and β-actin was used as loading control. Data are presented as mean ± SE of triplicate samples for each treatment. Results are representative of three sets of independent experiments. Gy, gray; SB, silibinin; IR, ionizing radiation; PCa, prostate cancer; SE, standard error; ns, not significant. *P < 0.05, **P < 0.01, ***P < 0.001. | PMC9537578 | jcp-27-3-170-f1.jpg |
0.47704 | 687f558d464542368d6bfe5231c92b60 | SB enhanced IR-induced cytotoxicity in EGFR-knockdown DU145 cells.Briefly, pLKO.1 (vector control) and shEGFR DU145 cells were seeded at a density of 4 × 104 cells/well and treated with either SB (25 µM) or IR (5 Gy) or their combination. After the 48-hour treatments, cells were harvested and counted by using the trypan blue assay. Data were quantified and represented as the total number of cells (A) and percent cell death (B). Briefly, 600 cells/well were seeded in a 6-well plate for pLKO.1 and shEGFR DU145 cells and after 24 hours, treated with silibinin and/or IR for the clonogenic assay. (C) Representatives images of the colonies assesed through crystal violet (0.05%) staining at 10 days for various treatment groups. (D) Quantitative data represented as the total number of colonies per well. (E) DU145 knockdown cells were treated with SB (25 µM) and/or IR (5 Gy) and harvested after 48 hours. Cell lysates were prepared and Immunoblotting was done for PCNA and β-actin was used as loading control. Data are presented as means ± SE of triplicate samples for each treatment. Results are representative of three independent experiments. VC, vector control; SB, silibinin; IR, ionizing radiation; EGFR, EGF receptor; Gy, gray; ns, not significant; shEGFR, short hairpin EGFR; PCNA, proliferating cell nuclear antigen; SE, standard error. *P < 0.05, **P < 0.01, *** P < 0.001. | PMC9537578 | jcp-27-3-170-f2.jpg |
0.477182 | 00da4e54d30d448997d3ec760a8f3609 | SB augments IR-induced G2/M arrest in EGFR-knockdown DU145 cells.pLKO.1 and EGFR-knockdown DU145 cells were seeded at a density of 4×104 cells/well in 12-well culture plates and treated with SB (25 µM) and/or IR (5 Gy). After the 48-hour treatments, cells were harvested and processed for cell cycle analysis by flow cytometry as described in MATERIALS AND METHODS. (A) Representative histogram showing cell cycle phase distribution in various treatments. (B) Quantitative data represented as a percent cell cycle distribution of different phases of cell cycle in various treatments. (C) pLKO.1 and EGFR-knockdown DU145 cells were seeded and treated with a low dose of SB (25 µM) and/or IR (5 Gy), and whole cell lysates were prepared and analyzed for the expression of Cdc25C, CDK1, p-CDK1 (Tyr15) and Cyclin B1 proteins. β-actin was used as a loading control. Data are presented as mean ± SE of duplicate independent wells and are representative of three independent sets of experiments. SB, silibinin; IR, ionizing radiation; EGFR, EGF receptor; VC, vector control; S, synthesis; G1, first gap; G2, second gap, M, Mitosis phases of the cell cycle; shEGFR, short hairpin EGF receptor; CDK1, cyclin-dependent kinase 1; p-CDK1, phospho-CDK1; Gy, gray; SE, standard error; ns, not significant. *P < 0.05, **P < 0.01, ***P < 0.001. | PMC9537578 | jcp-27-3-170-f3.jpg |
0.395543 | 016b1c333ad649c78177d0c12526f0d7 | Effect of SB and IR on induction of DNA damage in EGFR-knockdown DU145 cells.At the end of the treatments, cells were trypsinized briefly and fifteen thousand cells/0.5 mL in low melting point agarose were coated on the surface of a microscopic slide and processed in single cell gel electrophoresis. Slides were further stained with ethidium bromide (4 µg/mL) and subsequently visualized with fluorescent microscope for the images. (A) Representative fluorescent images for various treatments taken at ×100 magnification. Quantitative data represented as (B) comet tail length, and (C) percent content of DNA in tail in respective treatments. Quantitative data presented as mean ± SE of triplicate for each treatment group. Results are representative of three independent experiments. SB, silibinin; IR, ionizing radiation; EGFR, EGF receptor; shEGFR, short hairpin EGF receptor; Gy, gray; SE, standard error; ns, not significant. *P < 0.05, **P < 0.01, ***P < 0.001. | PMC9537578 | jcp-27-3-170-f4.jpg |
0.406626 | 1a1c27eaa3474bd4b99c5415f9ec594d | Effect of SB and IR on expression of DNA repair and pro-survival signaling proteins in EGFR-knockdown PCa cells.At ~70% confluency, pLKO.1 and EGFR knockdown DU145 cells were treated with SB (25 µM) and/or IR (5 Gy) for 12 hours and cells were harvested and whole cell lysate was prepared. (A) Whole cell lysates were analyzed for the protein expression of EGFR, DNA-PK, Rad51, Ku70, Ku80, p-p53 and p53 by immunoblotting. β-actin was used as a loading control. (B) Cell lysates were analyzed for p-Akt, Akt, p-STAT3, STAT3, p-ERK1/2, ERK and β-actin proteins. Bands were quantitated using Image J software and represented as fold change with respect to control below each respective band. All the experiments were repeated at least three times. SB, silibinin; IR, ionizing radiation; EGFR, EGF receptor; PCa, prostate cancer; DNA-PK, DNA-dependent protein kinase; p-Akt, phospho-Akt; ERK1/2, extracellular signal-regulated kinases1/2; p-ERK1/2, phospho-extracellular signal-regulated kinases1/2; ND, not detected. | PMC9537578 | jcp-27-3-170-f5.jpg |
0.410838 | 83c88cf8bf594b9683bc813d3ea24ba3 | Schematic representation of radiosensitizing effects of a low non-toxic dose of SB in radioresistant DU145 PCa cells.SB-induced radiosensitization of PCa cells via down-regulating DSBs DNA repair pathways (HR and NHEJ) proteins, Rad51 and DNA-PK, and this effect was further increased in EGFR-deficient cells. Further, SB inhibited pro-survival signaling molecules, ERK1/2, Akt and STAT3 in EGFR-deficient PCa cells exposed to radiation. SB, silibinin; IR, ionizing radiation; PCa, prostate cancer; DSB, double strand break; HR, homologous recombination; NHEJ, non-homologous end joining; DNA-PK, dependent protein kinase; ERK1/2, extracellular signal-regulated kinases1/2; EGFR, EGF receptor. | PMC9537578 | jcp-27-3-170-f6.jpg |
0.469598 | e1485b0c25154561b043e6cb732060c8 | Study flow chart. | PMC9538902 | fsurg-09-989644-g001.jpg |
0.476911 | af259651753b48a695b1a8e0337d32ec | Changes in heart rate and mean arterial pressure during the study. Data are shown for control and TCR groups at 4 time points during the study: T1, 5 min before anesthetic induction; T2, 1 min before DMSO/Onyx injection; T3, at the moment of DMSO/Onyx injection; T4, at the end of the operation. *P < 0.05, **P < 0.01, TCR group vs. the control group at certain time points. Abbreviations: HR, heart rate; MAP, mean arterial pressure. | PMC9538902 | fsurg-09-989644-g002.jpg |
0.404206 | 3eb764f0f53c40f1b9edb57ff4494993 | Predicted probability of closure of the patent ductus arteriosus vs. PNA at treatment initiation based on the logistic regression analysis on the complete study population, for infants with different GAs. GA, gestational age; PNA, postnatal age. | PMC9540485 | CPT-112-307-g001.jpg |
0.413517 | d99b560ed3a7400394ac2f9b45e102a2 | Lowest ibuprofen trough concentration in the 72 hours after start of treatment (left) and ibuprofen area under the curve (right) for each patient included in the logistic regression analysis. Circles represent appropriate for GA infants, and squares represent small for GA infants. AGA, appropriate for gestational age; GA, gestational age; SGA, small for gestational age. | PMC9540485 | CPT-112-307-g002.jpg |
0.457631 | b804d46ebe9b4b7ea90036ed0ad4c45d | Data selection flowchart. PDA, patent ductus arteriosus. | PMC9540485 | CPT-112-307-g003.jpg |
0.437192 | 242deb50385143a5b3386940c17f7754 | Probability of closure of the ductus arteriosus vs. PNA at treatment initiation during the first week of life, predicted by the logistic regression model based on the subset of the dataset with a maximal PNA at treatment initiation of 7 days. Dashed lines represent extrapolations of the study population, since the 20‐10‐10 mg/kg regimen was not administered to infants below a PNA of 4 days. PNA, postnatal age. | PMC9540485 | CPT-112-307-g004.jpg |
0.384577 | 027ea9096d284a05955ea25a30c473dd | MRI images of various patterns of polymicrogyria. Source: http://www.genereviews.org/. Copyright © 1993-2022 University of Washington | PMC9540929 | AIAN-25-616-g001.jpg |
0.506338 | 845f81fabc2e4ff8ae74cb0928c627fd | A flow chart for genetic testing and counseling of families with brain malformations | PMC9540929 | AIAN-25-616-g002.jpg |
0.528199 | e2f81aa025ee4eedb0d76a67947afa8c |
Human cDC1s co‐opt the IRE1/XBP1s axis in steady state (A). Protein levels of IRE1 and BiP were assessed through western blot in OP9‐DL1‐differentiated cDC1s compared to CD34+ hematopoietic precursors and monocyte‐derived DCs (moDCs). Cord blood mononuclear cells (CBMC) untreated or treated with tunicamycin (1 μg/mL) or thapsigargin (500 nM) for 8 h were used as negative and positive controls of ER stress‐induced UPR activation. Data are representative of two independent experiments (n = 2). (B) In vitro OP9‐DL1‐differentiated cDC1s and cDC2s and cord blood pDCs were identified and isolated using multiparametric flow cytometry and fluorescence activated cell sorting, respectively. XBP1 splicing was determined using conventional PCR. CBMC treated with tunicamycin and CD3+ T cells were used as positive and negative controls, respectively. Data are representative of four independent experiments (n = 4), compared to cDC2s and pDCs. (C) mRNA expression of IRE1, XBP1, and BiP relative to GAPDH in human DC subsets. Graph shows a pool of six independent experiments (n = 6), in which each dot represents one independent sample. (D) mRNA expression of PERK, ATF6 and downstream signaling effectors relative to GAPDH in human DC subsets. Graph shows a pool of five independent experiments, in which each dot represents one independent sample (n = 5). (E) IRE1 and XBP1s protein expression in DC subsets from cord blood mononuclear cells using flow cytometry. Graphs show a pool of four independent experiments, in which each dot represents one independent sample (n = 4). (F) Expression of Regulated IRE1‐dependent decay (RIDD) targets BLOS1 and PER1 relative to GAPDH was determined by qPCR. Graph shows a pool of five independent experiments in which each dot represents one independent sample (n = 5). (G) Conventional PCR of XBP1 spliced/unspliced from cDC1s treated with the IRE1 inhibitor STF‐083010 (60 μM, 6 h) or DMSO (vehicle). CBMC treated with tunicamycin were used as positive control. Data are representative of six independent experiments (n = 6). (H) Gene expression of RIDD targets BLOS1, PER1, and SPARC was assessed in cDC1s treated with the IRE1 inhibitor STF‐083010 through qPCR. Vehicle‐treated cDC1s were used as control. Graph shows a pool of five independent experiments in which each dot represents one independent sample (n = 5). Error bars in (C; D; E; F; and H) indicate the mean ± SEM. Statistical test in (C; D; E; F; and H: Mann‐Whitney nonparametric test ***p < 0.001; **p < 0,01; *p < 0.05). | PMC9541385 | EJI-52-1069-g001.jpg |
0.458821 | b8089861f6314a4e9bf6325096a7823a |
Activation of the IRE1/XBP1s axis by cDC1s modulates innate responses. (A) Experimental scheme of cDC1 activation with toll‐like receptor agonists in presence of an IRE1 RNase (STF‐083010) inhibitor. (B, C) cDC1s differentiated from OP9‐DL1/DC cultures were treated for 2 h with the IRE1 inhibitor STF‐083010 (60 μM) prior to 16 h stimulation with LPS (1 μg/mL) or R848 (5 μg/mL) and poly(I:C) (5 μg/mL); and IL‐12 and TNF expression was determined using flow cytometry. Flow cytometry plots are representative of six independent experiments (n = 6) and graphs show a pool of six independent experiments in which each dot represents one independent sample (n = 6). (D) IL‐12 and TNF expression was also determined by flow cytometry in cDC2s from the OP9‐DL1/DC cultures treated with STF‐083010 prior to LPS and poly(I:C) stimulation. Graphs show a pool of five independent experiments, in which each dot represents one independent sample (n = 5). (E) CD83 and CD86 expression in cDC1 treated with R848 and poly(I:C) with or without IRE1 inhibition with STF‐083010. Histograms are representative of four independent experiments (n = 4) and graphs show a pool of four independent experiments in which each dot represents one independent sample (n = 4). Error bars in (C, D, and E) indicate the mean ± SEM. Statistical test used in (C‐E) was Wilcoxon matched‐pairs signed rank ***p < 0.001; **p < 0,01; *p < 0.05. | PMC9541385 | EJI-52-1069-g002.jpg |
0.472859 | 7d7de8e8ceda4c288fd8a9bbf9233003 | CONSORT diagram to illustrate participant flow in the study. | PMC9542753 | ooac081f1.jpg |
0.526694 | ea85ec7b331e4fe39ad87955185cfb81 | CONSORT flow diagram. | PMC9544702 | BJEP-92-1109-g001.jpg |
0.46214 | 86faeecf068941ecb8c4c4a256f82524 | GOTI composite scores of the teachers in the experimental group at Sessions 2, 6, and 10. | PMC9544702 | BJEP-92-1109-g002.jpg |
0.402023 | 8947fcf1cb1e47b99250af75f0b01c28 | Teachers’ mediation skills at Session 2, Session 6, and Session 10. GOTI scores at 1, 2, 3, and 4 denote teacher’s mediation not evident yet, evident at emergent level, evident at moderate level, and evident at high level respectively. I= Intent; M=Meaning; T=Transcendence; JR=Joint Regard; SE=Shared Experience; TR=Task Regulation; P&F=Praise & Feedback; CHAL=Challenge; CHGN=Change; D=Differentiation; CR=Contingent Responsivity; AI=Affective Involvement. | PMC9544702 | BJEP-92-1109-g003.jpg |
0.4289 | 0b295259a20042408b02bbce5c00140d | Sample items of the three types of training tasks in the Think Bright intervention. | PMC9544702 | BJEP-92-1109-g004.jpg |
0.460764 | 77c4847e93ee4a22951526ad17e6cf52 | Mean scores and standard errors of the outcome variables at Time 1 and Time 2. | PMC9544702 | BJEP-92-1109-g005.jpg |
0.388163 | 8656d7f2aa5f4f3fb3bc450a2acb7251 | Molecular model of the thrombin‐dsDNA‐diPyOx construct to rationalize the observed modifications. A) Details of the model, with emphasis on the linker between protein and dsDNA; the linker is shown in sticks, the diPyOx catalyst in ball‐and‐stick, the modified Lys residues and one Ser residue in balls, and the unmodified Lys residues in sticks; surfaces of the protein and DNA are depicted in green, except for the previously described details. In the model, the dsDNA unit is shown on top and the protein at the bottom. B) Resulting 10 structures of sampling the dihedral angles of the spacer between protein and dsDNA, and of diPyOx‐functionalized T1. Modified Lys residues are shown as green balls, modified Ser residue as magenta balls, unmodified Lys residues as red balls. The position of the protein is fixed, the 10 differently positioned dsDNA‐diPyOx units are coloured from blue to red, their surfaces are shown in grey. C and D) Zoomed parts of the interface between dsDNA‐diPyOx and thrombin. | PMC9546015 | CHEM-28-0-g001.jpg |
0.441965 | d838d8d96d3e492ba1e1c10db773e6e6 | A) Synthesis of thrombin‐DNA (TRM‐DNAtemp) and chymotrypsin‐DNA (CHY‐DNAtemp) by using paraoxon derivative 1 (or 2); B and C) Graphs showing the decline in conversion percentages of B) CHY‐DNAtemp and C) TRM‐DNAtemp by DNAdiDMAP or DNAdiPyOx when positioned further away from the protein surface (T1 is 3’ end). The shapes indicate ⧫ for ethyl and • for EG2 linkers, where the colors indicate blue for diDMAP and red for diPyOx. Conversions in B) are normalized values. Conditions: 20–26 μM protein‐DNAtemp with (i) 23–28 μM PMET‐diDMAP and 100 μM thioester 1, pH: 8.0, at 37 °C for 2 h or (ii) 23–28 μM DNA‐diPyOx and 300 μM ANANS 2, pH: 7.2, at 37 °C for 6 h; D and E) Crystal structure of thrombin showing its Lys (green) and Ser (pink) residues with respect to the active site where DNAtemp is attached (S195) (PDB‐code: 5EW1
[32]
). LC=Light Chain. D) Modification sites by diDMAP. E) Modification sites by diPyOx. Light colored numbers indicate residues modified with only bound catalysts and dark colored numbers indicate residues also modified with unbound catalyst. | PMC9546015 | CHEM-28-0-g003.jpg |
0.394488 | 33fa6506fa6e4a6392992a34330e39eb | A) Structures of acyl donors 1 and 2 for diDMAP and diPyOx, respectively; B) Diagram showing the decline in conversion percentages of GRX‐DNAtemp by diDMAP or diPyOx when positioned further away from the protein surface with T1 being the closest. The numbers in the boxes show the distance between nucleobase and protein surface in nm. C) Crystal structure(s) of GRX (PDB code: 1EGO) showing Lys residues (green) with the numbers of catalyst positions that modify them (D=diDMAP (blue), P=diPyOx (red), all=including free catalyst) as well as the attachment site on the DNA strand. Conditions: 20 μM GRX‐DNAtemp with (a) 22 μM DNAdiDMAP and 100 μM thioester 1, pH: 8.0, at 37 °C for 2 h or (b) 22 μM DNAdiPyOx and 300 μM ANANS 2, pH: 7.2, at 37 °C for 6 h. | PMC9546015 | CHEM-28-0-g004.jpg |
0.411502 | 9e13769cd5bb46aa895b1156c9c54bfb | A) The G‐Quadruplex‐forming sequence PW17 is included in the hybridizing strand and by addition of hemin, a protein‐bound hGQ DNAzyme is formed. When H2O2 is present, the DNAzyme conjugates N‐methyl‐luminol 3 (NML) to tyrosine residues on the protein, which can be visualized after removal of the hGQ‐containing DNA strand. B) The different positions where PW17 was included with the percentages of single and double modification that the DNAzyme generated. Conditions: 20 μM GRX‐DNAtemp, 22 μM DNA‐hGQ, 30 μM NML 3 and 100 μM H2O2, pH: 7.0, at 25 °C for 30 min. | PMC9546015 | CHEM-28-0-g005.jpg |
0.463349 | 76d29611c5db4b6faec6aaf54597523f | The effects of pregnancy on MAFLD development.Evidence suggests that factors such as maternal adiposity, pre-existing obesity, hypercholesterolemia, gestational diabetes, pre-existing metabolic syndrome, and genetic predisposition in pregnant women may promote increased inflammatory responses, hormonal dysregulation, increased lipotoxicity and dyslipidemia, epigenetic alterations and insulin resistance. In utero exposure to these factors can increase the risk of childhood MAFLD through placental transfer. Also, such factors may affect adipogenesis and disrupt metabolism in the mother leading to maternal MAFLD development. Lastly, exposure to these factors may lead to MAFLD development in premenopausal women. MAFLD, Metabolic-associated fatty liver disease. | PMC9547252 | JCTH-10-0947-g001.jpg |
0.432546 | a03f8020667e41b299f1546d4c334ef5 | Effects of metabolic dysregulation of pregnancy, MAFLD and maternal nutritional factors on the fetus.IR, insulin resistance; FFA, free fatty acid; VLDL, very low-density lipoprotein; TG, triglyceride; SCD1, stearoyl-CoA desaturase 1; MAFLD, Metabolic-associated fatty liver disease. | PMC9547252 | JCTH-10-0947-g002.jpg |
0.431566 | c4ba53e5a80645f9886fe7bbe49c5153 | Architecture and mechanism of CRISPR-Cas13 systems. Three main stages constitute the CRISPR-Cas13 immune response: adaptation, expression and interference. During the adaptation stage, a complex of Cas proteins binds the invading genome, which is shown as an RNA virus. The bound part of the target RNA is cleaved out and is inserted into the CRISPR array of the prokaryotic genome as a new spacer through a reverse transcriptase. The expression stage involves the transcription of the CRISPR array as a large, single transcript and this pre-crRNA is processed into a mature crRNA containing a target spacer and a flanking repeat. The mechanisms and components involved in the pre-crRNA processing of CRISPR-Cas13 systems have not been experimentally resolved yet. At the last stage of the immune response, the interference stage utilizes the crRNA as a guide to recognize invading genomes based on sequence complementarity, recruiting the complex of Cas proteins. The Cas13a/b/d proteins have two higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domains of RNase activity, which cleave the target sequence and inactivate the RNA virus | PMC9547417 | 13062_2022_339_Fig1_HTML.jpg |
0.437105 | 7d0a9d739715464ea22e7cffa7801d59 | In silico docking of crRNAs with Cas13 proteins to assess the RNA–protein interactions. This study is divided into two parts: the validation study to optimize the in silico docking of crRNAs and Cas13 proteins, and the candidate study to apply the optimized pipeline of in silico docking to test a list of candidate crRNAs on each Cas13 protein for RNA–protein interactions, as a preliminary step prior to experimental validation | PMC9547417 | 13062_2022_339_Fig2_HTML.jpg |
0.420656 | 4f99ae25df134f88a3e4d8239089c72a | Performance analysis of RNA structure prediction of CRISPR repeats with PyMOL align. Heatmap of the means of the RMSD values by superimposition of each predicted crRNA 3-D structure with the ground truth (GT) structure. The RNA 2-D structure prediction programs are shown on the y-axis, and the PDB name of each Cas13 protein is shown on the x-axis, with the RNA 3-D structure program as a RNAComposer and b Rosetta. c Superimposition of the GT structure 6IV8_B predicted by ContextFold and RNAComposer (best), and 6AAY predicted by ContextFold and RNAComposer (worst). d Superimposition of the GT structure 6DTD predicted by RNAstructure and Rosetta (best), and 6IV8_D predicted by RNAstructure and Rosetta (worst). Grey = GT structure; Magenta = predicted structure | PMC9547417 | 13062_2022_339_Fig3_HTML.jpg |
0.428272 | f67a7c7dac024edc96438bc5dd0cfa82 | In silico docking evaluation of the Cas13a proteins of the best experimental metrics. The iRMSD from the in silico docking experiments of the crRNAs with the Cas13a protein using HDOCK. The 10 best models were retained from HDOCK and the experiments were performed template-free or template-based. Each box represents the results of 60 docking experiments. The 3-D structure below each box shows the GT structure (magenta), the computer selected best model (blue), and the human selected best model (green) docked on the corresponding Cas13a protein (grey). Except for 5W1H, the computer selected best model coincided with the human selected best model (green) | PMC9547417 | 13062_2022_339_Fig4_HTML.jpg |
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