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0.436765 | f70740c12f374a8eb5c03b1a55a6bae8 | Complexity of RAGE signaling. A multitude of RAGE ligands exist that activate numerous intracellular signaling pathways through various adapter proteins recruited to the intracellular domain. Through increased gene transcription, RAGE activation leads to inflammation, survival or apoptosis, migration and/or invasion, and proliferation and/or differentiation. Signal amplification is achieved through enhanced expression of RAGE itself as well as of various RAGE ligands, in which activation of NAPDH oxidase and NF-κB play a role. RAGE can also be present in the nucleus, where it has been shown to contribute to the repair of DNA double-strand breaks. Figure created with Biorender.com (accessed on 24 April 2023). | PMC10219583 | jcm-12-03366-g003.jpg |
0.400443 | b6cd25c201d5444a93288c24746f5075 | RAGE isoforms and genetic variants. The AGER gene contains 11 exons. The full-length RAGE protein consists of two constant domains (C1, C2) and a variable (V) immunoglobulin domain, which together are involved in ligand binding. A transmembrane domain (TM) elicits ligand-induced oligomerization, and a cytoplasmic domain (CT) interacts with the various downstream effectors. Full-length RAGE can be cleaved into soluble RAGE by ADAM10 and MMP3, 9, and 13. Alternative splicing gives rise to endogenous soluble RAGE (esRAGE), which lacks the TM and CT, a dominant negative (DN) variant that lacks the CT, and an N-truncated variant that lacks the V-domain. Polymorphisms in the AGER promotor increase AGER expression. A SNP leading to an amino acid substitution in the V domain (G82S) increases ligand affinity and downstream signaling. Figure created with Biorender.com (accessed on 8 May 2023). | PMC10219583 | jcm-12-03366-g004.jpg |
0.440222 | a701a60f2b464698af77e2ddb41097ad | Causes of AGE accumulation. Dietary intake of AGEs and exposure to glycotoxins through cigarette smoke lead to AGE accumulation in tissues. Endogenous AGE formation starts with the condensation of a reducing sugar with a free amine group in a protein and proceeds through various chemical reactions and molecular rearrangements. It is accelerated under conditions of inflammation, oxidative stress, and hyperglycemia, which stimulate the formation of dicarbonyls. AGE-modified proteins are cleared by receptor mediated uptake and intracellular degradation through the ubiquitin-proteasome system, or autophagy. The resulting AGE-modified peptides are cleared from the body by the kidneys. The glyoxalase system detoxifies MGO, which is a dicarbonyl and an important AGE precursor. These clearance and detoxification systems are negatively impacted by aging and inflammation/oxidative stress. Figure created with Biorender.com (accessed on 24 April 2023). | PMC10219583 | jcm-12-03366-g005.jpg |
0.493885 | ad1cc2fa4dde4a2f9bffd5eae150fbca | Overview of the pathophysiological effects of AGEs through modification of the extracellular matrix. AGE modification of ECM proteins leads to alterations in ECM turnover and tissue stiffness and influences various cells in contact with the ECM. Figure created with Biorender.com (accessed on 24 April 2023). | PMC10219583 | jcm-12-03366-g006.jpg |
0.436951 | 17834803a1e84a0a8f645ec735e6833c | Overview of interorgan crosstalk mediated by circulating AGEs. Circulating AGEs affect blood and endothelial cells through the induction of RAGE signaling, whereas AGE modification also directly influences platelets and red blood cells, as well as the function of plasma proteins including HDL, LDL, and albumin. Figure created with Biorender.com (accessed on 24 April 2023). | PMC10219583 | jcm-12-03366-g007.jpg |
0.457563 | e12e1a32c7464a0da98f43ad6bae04ed | Overview of the effects of AGEs and RAGE on various organs and their potential contribution to disease development and progression. Figure created with Biorender.com (accessed on 24 April 2023). | PMC10219583 | jcm-12-03366-g008.jpg |
0.525278 | 704a5a273af8402cbd3061d12cb1f9ed | Overview of interventions aimed at AGE-RAGE. The left panel provides an overview of strategies that prevent the intake or formation of AGEs or remove AGE-induced crosslinks. The right panel provides an overview of various strategies that target RAGE. Figure created with Biorender.com (accessed on 8 May 2023). | PMC10219583 | jcm-12-03366-g009.jpg |
0.410724 | 7e69944fd60d4a839de2a65531f4b214 | The expression level of PRR11 in different tumors and corresponding adjacent normal tissues. (A) The expression status of the PRR11 in different cancers or specific cancer subtypes was analyzed through TIMER2.0. Blue dots indicate the normal tissue and red dots represent tumors. (B) The expression of PRR11 in the tumor types lacking normal samples in the TIMER2.0 database was analyzed in the GEPIA2 database. Red boxes represent tumor tissue and black boxes represent normal tissue (* means P < .05, ** means P < .01, *** means P < .001). GEPIA2 = Gene Expression Profiling Interactive Analysis, version 2, PRR11 = proline rich protein 11, TIMER2.0 = Tumor Immune Estimation Resource, version 2. | PMC10219720 | medi-102-e33755-g001.jpg |
0.42105 | d557b386d7a24ea394b61e23f62dd772 | Relationship between PRR11 expression level and patient survival. (A–C) The Kaplan–Meier Plotter database was used to demonstrate the impact of PRR11 expression on the survival and prognosis of FPS, OS, and PPS. (D and E) The relationship between PRR11 and survival (OS and RFS) were assessed by GEPIA2. FPS = first progression survival, GEPIA2 = Gene Expression Profiling Interactive Analysis, version 2, OS = overall survival, PPS = post progression survival, PRR11 = proline rich protein 11, RFS = relapse free survival. | PMC10219720 | medi-102-e33755-g002.jpg |
0.443063 | 41322e3dca1943699b66040b44e18b01 | The association of PRR11 with LUAD clinicopathologic characteristics. Relationship between PRR11 expression level and (A) individual cancer stage, (B) N stage, (C) race, (D) gender, (E) smoking habits, and (F) histological subtypes. LUAD = lung adenocarcinoma, PRR11 = proline rich protein 11. | PMC10219720 | medi-102-e33755-g003.jpg |
0.440322 | 3f69c65752f64888959b7a1fb4ac7f4c | Correlation of PRR11 expression with immune cell infiltration in LUAD. The correlation of immune infiltration with (A) CAF, (B) CLP, (C) CMP, (D) T cell CD8+, and (E) MDSC was analyzed in the TIMER2.0. (F) PRR11 expression level and MDSC infiltration degree on survival. CAFs = cancer-associated fibroblasts, CLP = lymphoid progenitor cells, CMP = myeloid progenitor cells, LUAD = lung adenocarcinoma, MDSC = myeloid-derived suppressor cell, PRR11 = proline rich protein 11, TIMER2.0 = Tumor Immune Estimation Resource, version 2. | PMC10219720 | medi-102-e33755-g004.jpg |
0.458938 | 5237933219204f5faa0f762afc13e41b | Relationships between the expression level of PRR11 and classic tumor suppressor or oncogene in LUAD. (A) The correlation between the expression level of PRR11 and the expression levels of EGFR, KRAS, EML4, MET, TP53, ROS1, and ALK in LUAD. (B) The correlation between KRAS, EML4, ALK, PTEN, TP53, ROS1, MET mutations and PRR11 expression level. LUAD = lung adenocarcinoma, PRR11 = proline rich protein 11. | PMC10219720 | medi-102-e33755-g005.jpg |
0.422935 | 1bca4f9999f04f03b153e8612981f26f | Enrichment analysis of PRR11 in LUAD. (A) Heat map of the correlation between PRR11 and the top 50 PRR11-related genes in LUAD from LinkedOmics database, and overlapped with the top 200 genes with the highest correlation with PRR11 were screened from the GEPIA2. (B and C) The top 200 genes with the highest correlation with PRR11 were screened from the GEPIA2 database for GO and KEGG analysis. (D) The experimentally determined protein-protein interaction (PPI) network of PRR11-binding proteins. GEPIA2 = Gene Expression Profiling Interactive Analysis 2, GO = Gene Ontology, KEGG = Kyoto Encyclopedia of Genes and Genomes, LUAD = lung adenocarcinoma, PRR11 = proline rich protein 11. | PMC10219720 | medi-102-e33755-g006.jpg |
0.511333 | 8c48ceba7c364a8e91bf952a811c3aaf | Analysis of correlation between PRR11 and p53 signaling pathway. (A) The association of PRR11 expression and CCNB1, CCNB2, CDK1, CHEK1, GTSE1, or RRM2. (B) The KM survival curves by the expression level of CCNB1, CCNB2, CDK1, CHEK1, GTSE1, or RRM2 in LUAD. LUAD = lung adenocarcinoma, PRR11 = proline rich protein 11. | PMC10219720 | medi-102-e33755-g007.jpg |
0.464592 | a322d8228b9340a5870a3e7e8601afff | Schematic illustration of the enzymatic oxidation of chiral DOPA molecules inspired by natural mussels to generate different polymerization states and enantiomeric coating with excellent properties.The structure of tyrosinase from Agaricus bisporus is derived from PDB files (PDB ID: 2Y9X). | PMC10219960 | 41467_2023_38845_Fig1_HTML.jpg |
0.450569 | 422f7a9ab69e46858170ec593a85aa47 | Chemical and molecular structural characterization of the enzymatic oxidation products of chiral DOPA substrates.a Schematic diagram of the enzymatic oxidation of chiral DOPA, in which the poly(L+D-DOPA) has a higher molecular weight, intermolecular interaction force and crystallinity, leading to the formation of tightly stacked supramolecular materials. We represent poly(L/D/L+D-DOPA) using green, blue, and red polymeric balls, respectively. b–d MALDI-TOF-MS analysis of the oxidative products of L-DOPA, D-DOPA, and L+D-DOPA, respectively. The peaks marked in red are the presumed main oxidation products (e) and the orange ones are other possible products (Supplementary Fig. 4), and the blue-labeled peaks can be attributed to the matrix 2,5-dihydroxybenzoic acid (DHB). e The proposed basic building blocks for the formation of eumelanin and the possible structures assigned to the main peak detected by MALDI-TOF-MS, which correspond to the enzymatic oxidation products of L-DOPA, D-DOPA, and L+D-DOPA, respectively. f CPMAS 13C NMR spectrum (75 MHz) of poly(L-DOPA), poly(D-DOPA), and poly(L+D-DOPA), respectively. | PMC10219960 | 41467_2023_38845_Fig2_HTML.jpg |
0.398626 | e887d3169fcd4a9d9ef3889369e2b142 | Micromorphological characterization and molecular dynamics simulation of three poly(DOPA) systems.a–f High-resolution transmission electron microscopy (TEM) (a–c) and selected-area electron diffraction (SAED) images (d–f) of the poly(L-DOPA) (a), poly(D-DOPA) (b), and poly(L+D-DOPA) (c) solutions. The scale bars are 20 and 10 nm for TEM. g–i Snapshot of the simulated aggregates constructed from DOPA oxidized polymers at the steady state of self-assembly. | PMC10219960 | 41467_2023_38845_Fig3_HTML.jpg |
0.420382 | efafe3fa55d04a0f9ed0a8bc2037ce7d | Preparation and characterization of poly(DOPA) films.a Photograph of the mussel byssus viewed from the base of the foot that distally attaches to the substratum and sequence of common mussel adhesion protein Mefp-5, among which DOPA, an important sequence that plays a role in adhesion, is enlarged by box selection. b–d AFM images of the surface modified by (b) poly(L-DOPA), (c) poly(D-DOPA), and (d) poly(L+D-DOPA). (Scanning area size = 1.6 × 1.6 µm, scale bar = 300 nm). e–g 2D-GIWAXS patterns of (e) L-DOPA, (f) D-DOPA, (g) L+D-DOPA polymers. h Schematic illustration of the preparation of poly(DOPA) film samples with inner layer-to-layer stacking, where the racemic system has the highest crystal strength and lamellar stacking effect. | PMC10219960 | 41467_2023_38845_Fig4_HTML.jpg |
0.468673 | 5971dbebdc4d448cbadd516ffa802d67 | Intermolecular forces and binding energies analysis of chiral DOPA monomers.a–c Measured normal interaction forces of AFM tips with a poly(L-DOPA), b poly(L-DOPA), and c poly(L+D-DOPA) (the inset is the force curve measurement scheme.). d–f Adhesion distribution of the different surfaces coated with d poly(L-DOPA), e poly(L-DOPA), and f poly(L+D-DOPA). g Adhesive forces comparison of the poly(DOPA) films using different chiral DOPA monomers. h Schematic diagrams of the optimized geometric configurations of the three DOPA polymers obtained by DFT calculations and their binding energies during the two-molecule assembling process. | PMC10219960 | 41467_2023_38845_Fig5_HTML.jpg |
0.383973 | 0ae8e1c8f01c43cdadaf9f343f3e2716 | Characterization and adhesion stability of poly(DOPA) films.a Schematic diagram of the process of obtaining stable coating by DOPA chiral oxidation, in which the racemic system exhibits excellent stability. b–d The SPR sensorgrams of the oxidized b
L-DOPA, c
D-DOPA and d
L+D-DOPA molecules adsorbed on the surface of bare gold chips. e Real-time monitoring of DOPA polymers-modified surfaces exposed to different solutions (0.01 M NaOH, 0.01 M HCl and 1 M NaCl). | PMC10219960 | 41467_2023_38845_Fig6_HTML.jpg |
0.410126 | 09ad65ac6b314a789cc3bc3a2b2fa84e | Mechanical properties and thermal stability of poly(DOPA) films.a–c AFM nanoindentation image and surface mechanical strength of poly(DOPA) films. d Comparison of surface Young’s moduli of different biological and non-biological materials. e AFM mechanical strength of poly(DOPA) films prepared by the enzymatic oxidation of DOPA with a different enantiomeric excess (χ%). f, g TGA spectra (f) and differential scanning calorimetry curves (g) of the poly(L-DOPA), poly(D-DOPA) and poly(L+D-DOPA), respectively. | PMC10219960 | 41467_2023_38845_Fig7_HTML.jpg |
0.428114 | 5aee348a0ca84af19411eb1019c4a57b | Distribution of ancestry in 845 patients enrolled in the Program in Prenatal and Prenatal Genomic Sequencing (P3EGS) study.Each chart shows the distribution of ancestry according to the arm of the study (Pediatric and Prenatal) and the sex of the participant. Ancestries depicted are American Indian, Native American (blue), Alaskan Native (Asian (orange), White/European (light blue), Middle Eastern/North African (green), Hispanic/Latino or Latina (dark blue), More than one race/ethnicity (brown), Unknown, none of the above (gray). A Pediatric patients, maternal ancestry. B Pediatric patients, paternal ancestry. C Prenatal patients, maternal ancestry. D Prenatal patients, paternal ancestry. | PMC10220040 | 41525_2023_353_Fig1_HTML.jpg |
0.421672 | 5073e5519725467ab87db00a34cc9f3b | Diagnostic yield by sequencing approach in 845 patients enrolled in the Program in Prenatal and Prenatal Genomic Sequencing (P3EGS) study.The percentages of definitive positive (orange), probable positive (yellow), inconclusive (green) and negative (brown) results are shown for proband first, duo and trio sequencing approaches. There was no statistically significant difference in diagnostic yield with any sequencing approach. A Diagnostic yield with ‘proband first’ sequencing in pediatric patients. B Diagnostic yield with duo sequencing in pediatric patients. C Diagnostic yield with trio sequencing in pediatric patients. D Diagnostic yield with ‘proband first’ sequencing in prenatal patients. E Diagnostic yield with duo sequencing in prenatal patients. F Diagnostic yield with trio sequencing in prenatal patients. | PMC10220040 | 41525_2023_353_Fig2_HTML.jpg |
0.423826 | d7d05197f4184444a68e0c159daba5a9 | The seven small holes with a diameter of 5 mm in the precordia (red arrow). (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.) | PMC10220405 | gr1.jpg |
0.446644 | bd6b8d5b85794ff0816c75a27a28dbb2 | A chest computed tomography image taken by the previous doctor showing a pulmonary contusion at the apex of the lungs (red arrow). (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.) | PMC10220405 | gr2.jpg |
0.442727 | a0d859cd91b24db1ad67b24d1ae34382 | A chest computed tomography image taken by the previous doctor showing extensive subcutaneous emphysema in the neck and chest. | PMC10220405 | gr3.jpg |
0.443116 | bed23f959b5a42b08aa499f27074847e | Pieces of clothing removed from the vicinity of the perforated pleura. | PMC10220405 | gr4.jpg |
0.556709 | 137bf0100b77472a810aa5f3a7c16d88 | Slit-lamp image of (a) ring-shaped infiltrate in the right eye on presentation, (b) resolving to infiltrate at 1 week, (c) scarring infiltrate with mild corneal edema at 2 weeks, (d) completely scarred infiltrate at 1 month, (e) recurrence of anterior uveitis with inflammatory hypopyon at 4 months, (f) resolution of uveitis after steroid treatment, (g) paracentral stromal infiltrate of the left eye at 1 week, (h) granulomatous uveitis at 2 weeks, and (i) resolution of uveitis on steroid therapy at 1 month | PMC10220441 | TJO-13-84-g001.jpg |
0.390403 | 91fe56ed92f2408c9d06485eee8d358d | (a) Gram stain of the right eye showing Gram-negative bacilli, (b) white mucoid colonies of Klebsiella pneumoniae on blood agar, and (c) lactose-fermenting colonies of Klebsiella pneumoniae on MacConkey agar | PMC10220441 | TJO-13-84-g002.jpg |
0.458824 | 245df07783b84803afed3b30fdb195a8 | Fundus photograph at 1-week follow-up with normal optical coherence tomography scans of the right eye (a and c) and left eye (b and d) | PMC10220441 | TJO-13-84-g003.jpg |
0.532873 | 732db0b1641f490fb13465fb71485c21 | Patients with Acinetobacter baumannii infection between January 2012 and December 2019. The numbers of patients detected with A. baumannii, including multidrug‐resistant A. baumannii (MDR‐AB) and extensively drug‐resistant A. baumannii (XDR‐AB) significantly decreased after drug susceptibility‐based infection control. Data are expressed as mean ± SEM and compared by Student's t‐test. *p < 0.05. Non‐DR‐AB, non‐drug‐resistant A. baumannii. | PMC10220501 | AMS2-10-e855-g001.jpg |
0.467388 | 6721205b61bc4c56a921ab3f14b2f462 | Schematic overview of experiments. The timeline (A) of interventions and measurements is applicable to all three models. The specific surgical procedures and intervention are described in detail in the methods section. A gross schematic representation of the vagus nerve (B) and level of the vagotomy [7,8,34,35]. The cervical vagotomy was performed at the level of the trachea after division of the submaxillary glands. The abdominal (selective) vagotomy was performed by transecting the anterior and posterior trunks subdiaphragmatically. In sham rats (controls), the vagus nerves were also exposed, but spared. | PMC10220714 | nutrients-15-02327-g001.jpg |
0.492419 | d9cee8001ef3441c842673a4288a457d | Model A. Lung injury score. There was an increased trend in histopathological lung injury after a cervical vagotomy (even after an α7nAChR-gonist), but not selective vagotomy. Histological sections of the lungs were stained with H&E at ×400 magnification (scale bars represent 50 µm). Control (A): alveolar walls are relatively thin (double headed arrows), and the alveoli contain occasional alveolar macrophages (thick arrows); (B) AVGX: somewhat thickened alveolar walls infiltrated with macrophages and neutrophils (circles); (C) CVGX and (D) GTS-VGX: alveolar walls are thickened with intramural macrophages and neutrophils. Some hyaline membranes and proteinaceous debris filling the airspaces can be observed (small single-headed arrow). Values are medians with interquartile range. p-values as compared to the control group (after Bonferroni correction). Abbreviations: H&E, hematoxylin and eosin; LIS, lung injury score; Control, sham procedure; AVGX, abdominal (selective) vagotomy; CVGX, cervical vagotomy; GTS-VGX, cervical vagotomy with an α7nAChR-agonist (GTS-21). N = 4 in each group. | PMC10220714 | nutrients-15-02327-g002.jpg |
0.494906 | f538a2c96c0844e7ba6559d6976195d4 | Model A. Number of inflammatory cells in BALF (×104) and plasma (×105). Cell count of (B) macrophages was higher in the CVGX group and there was an increased trend in the GTS-VGX group. There were no statistically significant differences between the groups in (A) total cell count or (C) neutrophils in BALF. Similarly, there were no differences between the groups in (D) total cell count, (E) monocytes and (F) polymorphonuclear cells in plasma. Values are medians with interquartile range. p-values as compared to the control group (after Bonferroni correction); a p-value < 0.05 was considered statistically significant (*). Abbreviations: BALF, broncho-alveolar lavage fluid; Control, (N = 11) sham procedure; AVGX, (N = 12) abdominal vagotomy; CVGX, (N = 10) cervical vagotomy; GTS-VGX, (N = 12) cervical vagotomy with an α7nAChR-agonist (GTS-21). | PMC10220714 | nutrients-15-02327-g003.jpg |
0.447513 | 2564ba440da2451589bc3db422ee2a22 | Model A. Cytokines in lung homogenates. Levels (pg/mL) of (A) TNF-α and (B) IL-6 in lung homogenates did not differ between the groups. Values are medians with interquartile range. p-values as compared to the control group (after Bonferroni correction). Abbreviations: TNF, tumor necrosis factor; IL, interleukin; Control, (N = 12) sham procedure; AVGX, (N = 11) abdominal (selective) vagotomy; CVGX, (N = 12) cervical vagotomy; GTS-VGX, (N = 11) cervical vagotomy with an α7nAChR-agonist (GTS-21). | PMC10220714 | nutrients-15-02327-g004.jpg |
0.492505 | 4f4f6e1de85a4fae891af8733fb04cf7 | Model A. Pulmonary function. A vagotomy—irrespective of the level at which it was transected—did not affect (A) airway resistance. However, there was a trend toward an increased airway resistance after GTS-21, while lung compliance (B) was unaffected in this group. Contrarily, in the CVGX group, dynamic lung compliance was increased compared to a sham procedure and selective vagotomy, while airway resistance was unaffected. Values are medians (interquartile range is not shown for clarity). p-values as compared to the control group (after Bonferroni correction); a p-value < 0.05 was considered statistically significant (*). Control, (N = 10) sham procedure; AVGX, (N = 7) abdominal (selective) vagotomy; CVGX, (N = 10) cervical vagotomy; GTS-VGX, (N = 8) cervical vagotomy with an α7nAChR-agonist (GTS-21). | PMC10220714 | nutrients-15-02327-g005.jpg |
0.423748 | 91083515eecf44dbb2f6da39701c7aa5 | Model B. Lung injury score. Histopathological lung injury was similar between CSD-sham and the control group. In the CSD-vagotomy group, histopathological lung injury was more severe compared with controls and there was an increased trend compared with CSD-sham (p = 0.058). Values are median with interquartile range. p-values as compared to the control group (after Bonferroni correction); a p-value < 0.05 was considered statistically significant (*). Abbreviations: Control, sham procedure; CSD-sham, sham cervical procedure with Chlorisondamine (α7nAChR-antagonist); CSD-VGX, cervical vagotomy with Chlorisondamine. N = 8 in each group. | PMC10220714 | nutrients-15-02327-g006.jpg |
0.46034 | a671662869d54c81b0204d37927702da | Model B. Number of inflammatory cells in BALF (×104) and plasma (×105). Cell count of (B) macrophages was higher in the CVGX-CSD group. There were no statistically significant differences between the groups in (A) total cell count and (C) neutrophils in BALF. Similarly, there were no differences between the groups in (D) total cell count, (E) monocytes and (F) polymorphonuclear cells in plasma. Values are medians with interquartile range. p-values as compared to the control group (after Bonferroni correction); a p-value < 0.05 was considered statistically significant (*). Abbreviations: BALF, broncho-alveolar lavage fluid; Control, (N = 8) sham procedure; CSD-Sham, (N = 7) sham procedure with an α7nAChR-antagonist (Chlorisondamine); CSD-VGX, (N = 8) cervical vagotomy with Chlorisondamine. | PMC10220714 | nutrients-15-02327-g007.jpg |
0.472982 | 56a34a1d9a224155a911b3146456ba12 | Model B. Concentration of TNF-α over time in serum. Levels (pg/mL) of TNF-α in serum did not differ between the groups preoperatively, directly postoperatively, at 2 h postoperatively or postmortem. Values are medians with interquartile range. p-values as compared to the control group (after Bonferroni correction); a p-value < 0.05 was considered statistically significant. Abbreviations: TNF, tumor necrosis factor; Control, (N = 6) sham procedure; CSD-Sham, (N = 7) sham procedure with an α7nAChR-antagonist (Chlorisondamine); CSD-VGX, (N = 8) cervical vagotomy with Chlorisondamine. | PMC10220714 | nutrients-15-02327-g008.jpg |
0.447717 | 8a47c4a594204e9b895273d4c56b8d65 | Model C. Lung injury score. Histopathological lung injury was lower in high-fat sham group, compared with the control group, even after a selective vagotomy. LIS between HFs and HFv groups did not differ (p > 0.999). Values are means with standard deviation. p-values as compared to the control group (after Bonferroni correction); a p-value < 0.05 was considered statistically significant (*). Abbreviations: Control, fasting sham procedure; HFs, high-fat sham procedure; HFv, high-fat selective (abdominal) vagotomy. N = 8 in each group. | PMC10220714 | nutrients-15-02327-g009.jpg |
0.481311 | 281b9f5d486a4c9eab00cfc54a003609 | Model C. Number of inflammatory cells in BALF (×104) and plasma (×105). There were no statistically significant differences between groups in (A) total cell count, (B) macrophages and (C) neutrophils in BALF. Similarly, there were no differences between groups in (D) total cell count, (E) monocytes and (F) polymorphonuclear cells in plasma. Values are medians with interquartile range. p-values as compared to the control group (after Bonferroni correction); a p-value < 0.05 was considered statistically significant. Abbreviations: BALF, broncho-alveolar lavage fluid; Control, fasting sham procedure; HFs, high-fat sham procedure; HFv, high-fat selective (abdominal) vagotomy. N = 8 in each group. | PMC10220714 | nutrients-15-02327-g010.jpg |
0.438221 | 28e4f217a359425abc016c421e875ff4 | Model C. Levels of TNF-α and IL-6 in plasma and lung homogenates (pg/mL). Levels of TNF-α did not differ between the groups in plasma (A) at 2 h (2 h) after lipopolysaccharide (LPS) administration, (B) after rats were sacrificed (s) and (C) in lung homogenates. Similarly, levels of IL-6 did not differ in plasma (D,E) or lung homogenates (F). Values are medians with interquartile range. p-values as compared to the control group (after Bonferroni correction); a p-value < 0.05 was considered statistically significant. Abbreviations: TNF, tumor necrosis factor; IL, interleukin; Control, (N = 6) fasting sham procedure; HFs, (N = 6) high-fat sham procedure; HFv, (N = 4) high-fat selective (abdominal) vagotomy. | PMC10220714 | nutrients-15-02327-g011.jpg |
0.44487 | 5aaae9e2b0774845b6f35cc9e955fd4c | Flow diagram of study design. Left-hand side depicts how data from the 30 subjects assigned to model training were used, while right-hand side shows how data from the 20 subjects in the model testing group were utilized. Abbreviations: AUC, area under the concentration–time curve; AUCmodel, area under the curve from model-predicted concentrations; AUCobs, area under the curve from observed concentrations; CL, clearance; MMOpt, multiple-model optimization algorithm; NCA, noncompartmental analysis; PK, pharmacokinetic. Created with BioRender.com. | PMC10220925 | pharmaceutics-15-01336-g001.jpg |
0.471515 | 188269e79d5a401bb3555769ba51d606 | Observed versus posterior (individual) predicted concentrations for the full (A), Hoek (B), and Schwartz (C) models. | PMC10220925 | pharmaceutics-15-01336-g002.jpg |
0.444831 | 4602433a0c88416886e33adc44c05e41 | Schematic flowchart of the experiment and duration of control and high-fat diet in mothers and offspring of Sprague Dawley rats. | PMC10221326 | medicina-59-00888-g001.jpg |
0.462092 | 680687a797ed466d805491333aa1c1db | Collagen content (%) in: (a) subcutaneous, (b) epididymal and (c) perirenal adipose tissue; with statistical significance between groups. Data are presented using Whiskers bar graphs (mean, 5–95 percentile). Post hoc LSD test was used to test two independent groups, * p < 0.05 was considered significant. CD—standard laboratory chow, HFD—high-fat diet. | PMC10221326 | medicina-59-00888-g002.jpg |
0.45863 | 2082493a0e3b44089b29519d9e963f31 | Representative images of collagen staining with Mallory’s trichrome staining in subcutaneous adipose tissue (collagen is visible in green color) of the groups of male rat offspring: (a) CD-CD group, (b) CD-HFD group, (c) HFD-CD group, and (d) HFD-HFD group. Magnification: 200×. Scale bar: 200 µm. CD—standard laboratory chow, HFD—high-fat diet. | PMC10221326 | medicina-59-00888-g003.jpg |
0.423144 | acc4d678205b44288248c04ee853c42b | Representative images of CD163+ cells (arrow) in perirenal adipose tissue: (a) CD-CD group, (b) CD-HFD group, (c) HFD-CD group, and (d) HFD-HFD group of male rat offspring. Magnification: 200×. Scale bar: 200 µm. | PMC10221326 | medicina-59-00888-g004.jpg |
0.488384 | 43fc4274d65c4e4fa350a10c4ce6db62 | Polarization of macrophage markers among groups of offspring where the number of CD163+ cells is presented relative to the number of CD68+ cells in: (a) subcutaneous, (b) epididymal and (c) perirenal adipose tissue, with statistical significance comparing groups. Data are presented using Whiskers bar graphs (mean, 5–95 percentile). Post hoc LSD test was used for testing two independent groups, * p < 0.05 was considered significant. CD—standard laboratory chow, HFD—high-fat diet. | PMC10221326 | medicina-59-00888-g005.jpg |
0.492302 | c3c264fd703249fd9b367c6ff2e5e225 | Diagram of the ultrasonic data and energy transmission system. It consists of outside and inside blocks. The outside block is responsible for sending energy to the inside block by means of ultrasonic waves. The inside block is responsible for modulating the acoustic impedance of its transducer as digital data. The driver generates the electrical signal to be applied to the transducer; the transducer converts the electrical signal into mechanical vibration and vice-versa; the transmitter modulates the transducer’s acoustic impedance by short-circuiting its terminals; the physical barrier acts as the acoustic channel. | PMC10221568 | sensors-23-04697-g001.jpg |
0.469813 | 33cf7125c870424a86719e1197498e4c | Automatic gain control algorithm tasks. Task 1 is responsible for checking if a message is received within the predefined timeout interval. Task 2 checks if a timeout occurred. Task 3 checks the Gain problem flag. | PMC10221568 | sensors-23-04697-g002.jpg |
0.448814 | 26e2119b6b4d47baad6f9db346c87d98 | Automatic carrier control algorithm implemented in the microcontroller in order to control the carrier level transmitted from the outside to the inside block. | PMC10221568 | sensors-23-04697-g003.jpg |
0.430093 | 30b57105ff6c440280c25083bc041835 | Designed modem circuitry as inside or outside blocks. This one is configured as an outside block. | PMC10221568 | sensors-23-04697-g004.jpg |
0.467693 | 82c929e391d84635867d25e14cc5e244 | Inside (a) and outside (b) block diagrams with the main components, voltage and signals transferred within each block. | PMC10221568 | sensors-23-04697-g005.jpg |
0.43067 | 86bab5965618497191d6ed1afe23a1f1 | Experimental setup consisting of two transducers axially aligned, mounted in two 5 mm-thick steel walls separated by a 100 mm fluid column. Photograph of the experiment in the water recipient (a), corresponding schematic diagram of the multilayer acoustic channel (b) and detailed diagram of the experimental setup with components and connections (c). | PMC10221568 | sensors-23-04697-g006.jpg |
0.398868 | 55eb38a78ee24ecd9132d3d2439afa56 | Complete system in operation for the acoustic channel formed by the combination of layers of multiple materials highlighting its main components: (a) bench power supply; (b) power amplifier; (c) outside block modem board; (d) acoustic channel in the water recipient; (e) inside block modem board; (f) pressure and temperature sensor; (g) computer displaying the transmitted data; (h) band-pass filter. | PMC10221568 | sensors-23-04697-g007.jpg |
0.440482 | b6af65b80e2a4b29828c9a70caaa91f7 | (a) Frequency selectivity response for the acoustic channel measured by the insertion loss with an E5063A network analyzer. (b) Acquired signal at the input of the electronic circuit of the outside block circuit, highlighting the noise. The yellow curve is the signal present on the outside block transducer and the blue curve is the signal at the output of the outside block comparator. | PMC10221568 | sensors-23-04697-g008.jpg |
0.495149 | 805b76a37fa34387b3000dc645b1909a | Automatic gain control actuation, obtained with a DSO1072B oscilloscope. Signal outputted from the PGA applied to the voltage comparator input with some increases in magnitude due to the gain applied by the PGA, in orange; and the signal at the output of the voltage comparator in blue. The orange level increases due to the PGA gain when the signal achieves the preconfigured comparator-specific threshold level. The blue line indicates the exact instant when this level is reached and then the signal can be decoded. | PMC10221568 | sensors-23-04697-g009.jpg |
0.454935 | 7b49ecd9d9cd4859b4c339d88169e1d2 | Gradual increase of carrier level. Signal sampled over the outside block transducer terminals obtained with a DSO1072B oscilloscope. It presents the increment of the output voltage on the power amplifier. The increase or decrease in the transmission carrier power is ruled by the algorithm present in Figure 3. | PMC10221568 | sensors-23-04697-g010.jpg |
0.457393 | c34983ace84a4759a73f5f70dc489c86 | The last actuation of the automatic carrier control. Signal sampled over the outside block transducer terminals obtained with a DSO1072B. It is possible to observe that, after a few interactions, the algorithms can achieve a transmission power level sufficient to power the inside block and the transmitted data start to appear at the outside block signal. | PMC10221568 | sensors-23-04697-g011.jpg |
0.40587 | 0470762c4f864972b5a0a5f50e6ef372 | Schematic presentation of the experimental layout. Illustration showing (a) the vaccination and challenge scheme of the experiment and (b) sample types and collection days. PBS-phosphate buffered saline, i/n: intranasal, i/o: intraocular, S/C: subcutaneous. The illustration was prepared using BioRender (https://www.biorender.com/). | PMC10221827 | vaccines-11-01005-g001.jpg |
0.473425 | 69a1662f85224994b5a85343fe935b5e | Antibody titers in sera of chickens vaccinated with different formulations of NDV vaccines. (a) Dot plot showing HI titers of control and LaSota (live) vaccinated chickens at days 7, 28, 42, and 60. (b) Dot plot showing HI titers of booster-vaccinated chickens at day 74 (2 weeks after booster vaccination). (c) Dot plot showing HI titers of chickens at day 88 (2 weeks after challenge). Data indicates mean ± SEM. Two-way (a,b) and one-way (c) ANOVA with Bonferroni multiple comparison test, *** p ≤ 0.01, **** p ≤ 0.0001, ns = not significant. | PMC10221827 | vaccines-11-01005-g002.jpg |
0.473399 | 409a55498ea04db39cc3e9a42c0958e6 | Survival curve of NDV challenged chickens receiving three different booster vaccine formulations. | PMC10221827 | vaccines-11-01005-g003.jpg |
0.46295 | 989377b99e08407d8a8e933a602a7d70 | Gross pathological lesions in unvaccinated (a–d) and BD-C161/2010 booster immunized (e–h) chickens following challenge with NDV strain BD-C161/2010. Unvaccinated NDV-challenged chickens showing (a) marked hemorrhages and congestions in lungs; (b) hemorrhages on the tips of proventricular glands (arrows); (c) mottling (numerous necrotic white spots) of the spleen (arrows) with atrophy, and (d) button-like ulcers (arrows) in the intestine. Chickens from the BD-C161/2010 booster immunized group showing slight congestion in the lungs (e) and normal-appearing proventriculus (f), spleen (g), and intestine (h). Chickens receiving both the LaSota (live) and LaSota (killed) booster immunizations had gross lesions similar to the BD-C161/2010 (killed) booster immunized group. | PMC10221827 | vaccines-11-01005-g004.jpg |
0.449708 | c62336d08da84d2d923720946582b9d0 | Effect of bleomycins nanoparticles (BLM NAPs) on murine melanoma growth and metastasis in vivo. C57BL6 mice were inoculated s.c. on the right flank with 0.5 mL of 10% B16F10 melanoma suspension. The mice were exposed to BLM NAPs or glucose NAPs (control) for 5 h daily for 14 days. (A) Mice inhaled with BLM NAPs had significantly smaller tumor volumes compared with control mice beginning from 10 to 20 days after the start of treatment. (B) The survival of mice in the BLM NAP group is 26% higher than in the control group. (C) The number of lung metastases in mice in the control and experimental groups. Error bars represent the standard errors of the mean (SEM). | PMC10221970 | molecules-28-04157-g001.jpg |
0.467152 | ca074212c5074cea8f2e5430750bc87a | Effect of BLM NAPs on murine melanoma B16F10 (am) growth in vivo. C57BL6 mice were inoculated s.c. with 0.5 mL of 10% B16F10 melanoma tissue suspension. The treated groups were exposed to BLM NAPs for 5 or 2.5 h or BLM was injected i.p. 8 or 4 mg/kg daily for 14 days. (A) Mice treated with intraperitoneal BLM had significantly smaller tumor volumes compared with control mice. BLM NAPs induced unsubstantial TGI. (B) Mice treated with i.p. BLM had lower body weights compared to mice of control or BLM NAPs groups. Error bars represent the standard errors of the mean (SEM). | PMC10221970 | molecules-28-04157-g002.jpg |
0.406593 | 774e63f4b213428e901a5dee2c3651a0 | Effect of BLM NAPs on murine lung carcinoma LLC growth in vivo. C57BL6 mice were inoculated s.c. on the right flank with 0.5 mL of 10% LLC tissue suspension. The treated groups of mice were exposed with BLM NAPs for 5 days or were injected with 4 mg/kg BLM i.p. daily for 14 days. | PMC10221970 | molecules-28-04157-g003.jpg |
0.416368 | ec1cb8f3b26d4076b9b5fd363a41e5fd | Pharmacokinetics of BLM delivered by nanoaerosol (A) and i.p. injection (B) measured in serum. Bars indicate standard error for a group of five mice. (A) Total BLM dose was 300 ng per mouse. (B) The administered BLM dose was 4 mg/kg. | PMC10221970 | molecules-28-04157-g004.jpg |
0.536139 | 1f4bc75c341142a98400b88d21a5758a | A schematic illustration of nanoaerosol generator and exposure chamber used in the experiments on inhalation of BLM nanoaerosol. | PMC10221970 | molecules-28-04157-g005.jpg |
0.448525 | 99972afe79d142da9f64d85c3a4b6f7c | Size distribution of BLM NAPs in aerosol generated by spraying of 0.5% solution of BLM sulfate in 50% ethanol. | PMC10221970 | molecules-28-04157-g006.jpg |
0.483047 | b1ab93fdbd66433b84e7c484cef26e87 | A brief illustration showing the design classification for biothiol fluorescent probes. | PMC10222014 | molecules-28-04252-g001.jpg |
0.425193 | 4cd20684d9204217b4b9db9f669d11dd | (A) Schematic of probe 1 responding to GSH via the thiolysis reaction. (B) Fluorescence spectra of 10 μM probe 1 in the absence and presence of 30 μM GSH in PBS buffer (10 mM, pH 7.4) with CTAB (surfactant, 0.20 mM) at 37 °C. The inset pictures show the visual fluorescence color of probe 1 before (left) and after (right) the addition of GSH under a UV lamp at 365 nm. (C) Absorption and fluorescence spectra of 10 μM probe 1 incubated with 30 μM GSH. Ref. [37] Copyright © 2020 Elsevier B.V. All rights reserved. | PMC10222014 | molecules-28-04252-g002.jpg |
0.42961 | c5245810126d4c8289d16bd8b2355928 | (A)The structure and response of probe 3 to biothiols and HAS. (B) Fluorescence spectra of probe 3 (20.0 μM) with the addition of HSA (20 μM) or/and GSH (2 mM) at the excitation of 500 nm. (C) Fluorescence spectra of probe 3 (20.0 μM) with the addition of HSA (20 μM) or/and GSH (2 mM) at the excitation of 400 nm. Ref. [42] Copyright © 2022 American Chemical Society. | PMC10222014 | molecules-28-04252-g003.jpg |
0.431358 | 0b728df88f8048fa9a4c108147a02059 | (A) The structure and reaction mechanism of probe 25. (B) Fluorescence spectra of probe 25 (R13), Nap-SG, and Nap-Cys. The photograph in the inset was taken under UV illumination (365 nm). Ref. [64] Copyright © 2023 American Chemical Society. | PMC10222014 | molecules-28-04252-g004.jpg |
0.419731 | 1a6231044df54b4a9c5b992966fdab03 | (A) The structure and reaction mechanism of probe 26 (B,C) Concentration-dependent fluorescence spectra of (B) probe 26 (10 μM) toward GSH and (C) probe 26 (10 μM) toward Na2SO3. Ref. [65] Copyright © 2023 American Chemical Society. | PMC10222014 | molecules-28-04252-g005.jpg |
0.392576 | 76c8168a52f04a4c905f1e2642ad4aa4 | (A) Structure and response of probe 27. (B) Fluorescence spectra of probe 27 upon addition of NO (200 μM) and GSH (200 μM) for 1 h. (C) Fluorescence imaging of probe 27 (2 μM, 5 min) in HUVECs: (a1–a3) pretreated with NEM (1 mM, 30 min), (b1–b3) pretreated with DEA·NONOate (200 μM, 15 min), (c1–c3) non-pretreated, and (d1–d3) pretreated with NEM (1 mM, 30 min) and then DEA·NONOate (200 μM,15 min). Ref. [70] Copyright © 2021 American Chemical Society. | PMC10222014 | molecules-28-04252-g006.jpg |
0.451566 | 9ca7339ba2dc42b6963e5d5bf44e0c17 | (A) The structure and reaction mechanism of probe 28 and DPC as a product. (B) The UV-vis spectra of probe 30 (10 μM), probe 28 (10 μM) + GSH (100 μM) after 30 min, and DPC (10 μM). The color change of probe 28 or GSH was inserted. (C) The fluorescence spectral changes of probe 28 (10 μM) in 30 min after adding GSH (100 μM). The spectrum was recorded every 1 min, and the emission color change was inserted. Ref. [71] Copyright © 2022 Elsevier B.V. All rights reserved. | PMC10222014 | molecules-28-04252-g007.jpg |
0.423488 | 36fb9e493d8e42df9825104bdfb6002f | (A) Fluorescence spectra (λex = 615 nm) of probe 30 in the presence of different levels of GSH (0–500 μM). (B) Fluorescence spectra (λex = 450 nm) of probe 30 treated with GSH (1.0 mM) for 30 min and then reacted with different concentrations of ONOO− (0.0–10.0 μM) for 5 min. (C) Mitochondrial colocalization with NTG and MitoTracker Green in MCF-10A cells. (D) Confocal fluorescence images of exogenous GSH and ONOO− in zebrafish. Ref. [75] Copyright © 2022 American Chemical Society. | PMC10222014 | molecules-28-04252-g008.jpg |
0.445108 | 9eb62b0989b547958ec85b6afb53fda0 | Reaction mechanism of thiolysis-based fluorescent probes for biothiols and their chemical structures. | PMC10222014 | molecules-28-04252-sch001.jpg |
0.532668 | 9e9ee44c2ea04ee3aefcaf902ab36166 | The structure and response of probe 2 via the thiolysis reaction. | PMC10222014 | molecules-28-04252-sch002.jpg |
0.512411 | 993002d8c7c44750983725f82093fcfa | Chemical structure and reaction mechanism of probe 4 via the Michael addition reaction. | PMC10222014 | molecules-28-04252-sch003.jpg |
0.451865 | dcd86a8e90a14a54acb705479898726c | Chemical structure and reaction mechanism of probe 5 via the Michael addition reaction. | PMC10222014 | molecules-28-04252-sch004.jpg |
0.444454 | f43a7ee58b5e4bad8879f3b615ccd6a4 | Chemical structure and response mechanism of probe 6 via the disulfide reduction reaction. | PMC10222014 | molecules-28-04252-sch005.jpg |
0.535621 | 0d3662addc0e4ebdba12a766811e27a3 | Mechanism of acrylate-based probes specifically responding to Cys. | PMC10222014 | molecules-28-04252-sch006.jpg |
0.473432 | a118d71558aa4f7781252ca91ee79e3f | Chemical structure of an acrylate-based fluorescent probe for Cys. | PMC10222014 | molecules-28-04252-sch007.jpg |
0.512936 | 4e9747c53f73483b9b9f5d4f657c9001 | Chemical structure and reaction mechanism of probes 20 and 21 with Cys. | PMC10222014 | molecules-28-04252-sch008.jpg |
0.415499 | b92f4e0d0db048e1be19b9010300cf1f | Chemical structure and reaction mechanism of probe 22 with Cys. | PMC10222014 | molecules-28-04252-sch009.jpg |
0.437836 | 4ada72d9d4ad49c8a41d6057e586f31b | Chemical structure and reaction mechanism of probe 23 with Cys. | PMC10222014 | molecules-28-04252-sch010.jpg |
0.532464 | 723687f33fb348b1b86e28dbba3cb540 | Chemical structure and reaction mechanism of probe 24 with Cys and ·OH. | PMC10222014 | molecules-28-04252-sch011.jpg |
0.439717 | b601e25ff8b94cdbb942774c492b00b5 | Chemical structure and reaction mechanism of probe 29 with GSH. | PMC10222014 | molecules-28-04252-sch012.jpg |
0.424226 | 88bd6e943b8a4d5f98f7ba8fb6132399 | Structure of mitochondria-specific fluorescent probes for biothiols. | PMC10222014 | molecules-28-04252-sch013.jpg |
0.433613 | a2ee833ca8404fa9936f31a57f00bfe6 | Representative biothiol fluorescent probes based on the Michael addition reaction. | PMC10222014 | molecules-28-04252-sch014.jpg |
0.452074 | 5f009ca552474198902bb46aa2b5dc2f | Reversible reaction mechanism of probe 35 to GSH. | PMC10222014 | molecules-28-04252-sch015.jpg |
0.479991 | 0a5c7c9fb7d54e359d449885f1acc772 | (A) Distinguishing response mechanisms of NBD-probes to biothiols. (B) Structures of probes 41 and 42. | PMC10222014 | molecules-28-04252-sch016.jpg |
0.382567 | a606a43ae6564024b6a1aebffb88e1fa | Illustration of probe 43 and its distinguishing response to biothiols. | PMC10222014 | molecules-28-04252-sch017.jpg |
0.469281 | 444b1a5bb6f9420997f0d151df718132 | Illustration of probe 44 and its distinguishing response to biothiols. | PMC10222014 | molecules-28-04252-sch018.jpg |
0.414027 | 7d1fcc40d29846c8ae4759ea45b4970e | Structure of probe 45 and its response mechanism towards thiols. | PMC10222014 | molecules-28-04252-sch019.jpg |
0.473891 | 13c978ea51d54297849e58dca068faa3 | Structure of probe 46 and its response mechanism towards thiols. | PMC10222014 | molecules-28-04252-sch020.jpg |
0.39562 | d8e9ed90b09e4a36bbd113e172ad5384 | Structure of probe 47 and its response mechanism towards thiols. | PMC10222014 | molecules-28-04252-sch021.jpg |
0.491514 | e2f0146333424750baf59365ecb9f7c0 | Illustration of probe 48 and its distinguishing response to biothiols. | PMC10222014 | molecules-28-04252-sch022.jpg |
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