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0.356451 | fcb660d0acee4243b1d1e26c498ab58c | Subcellular localization of NH2NBS, EtNBS, and NMe2NBS (100 nM, λex = 633 nm, λem = 650–750 nm). (a) LTG: LysoTracker Green DND 26 (75 nM, λex = 488 nm, λem = 500–550 nm). (b) MTG: Mito-Tracker Green (200 nM, λex = 488 nm, λem = 500–550 nm). | PMC9965410 | molecules-28-01714-g002.jpg |
0.389569 | 03ff9303c2354aff80679b66b4da2d0e | Confocal image of photoinduced ROS detection in HepG2 cells incubated with three PSs and different fluorescence probes under normoxia and hypoxia. (a) DCFH-DA for ROS. (b) SOSG for 1O2. (c) DHE for O2−• radical. | PMC9965410 | molecules-28-01714-g003.jpg |
0.412802 | 80427892325f401684b7e7c8f358d2d9 | (a) CLSM images of AO (5 μM) staining. (b) The confocal fluorescence images of NH2NBS, EtNBS, and NMe2NBS (100 nM), after (different times of) 635 nm irradiation at a power density of 20 mW/cm2. (c) Cellular colocalization images after NIR light irradiation. (d) MMP determination after NIR light irradiation by JC-1. J-A represents the aggregation type and J-M represents the monomer type of JC-1. The concentrations of NH2NBS, EtNBS, and NMe2NBS are 100 nM. | PMC9965410 | molecules-28-01714-g004.jpg |
0.428668 | 40049150696c476491913dc06bc09218 | (a) The photocatalytic oxidation rate of NADPH (160 μM) with three PSs (10 μM) in the PBS solution (A0 and A represent the absorption intensities of NADPH at 330 nm before and after 635 nm laser irradiation at different times, respectively). (b) Total NADPH level in HepG2 cells incubated with three PSs (100 nM) in dark or light conditions. Light: 635 nm laser irradiation, 20 mW cm−2, 10 min. | PMC9965410 | molecules-28-01714-g005.jpg |
0.422454 | 64862dddba73499b95b557ca0b6c75bf | (a) In vivo imaging; (b) the quantitative fluorescence signal intensities of NMe2NBS at different time intervals in the solid tumor. (c) Ex vivo fluorescence imaging and fluorescence intensity of major organs and the tumor after intratumoral injection for 24 h. | PMC9965410 | molecules-28-01714-g006.jpg |
0.413002 | 59607db89ed2494ca6e941d57f669fda | (a) Schematic illustration of NMe2NBS used for in vivo PDT. (b) Tumor photographs of different groups after various treatments. (c) Time-dependent body weight curves, tumor growth curves, and tumor weights of different groups. | PMC9965410 | molecules-28-01714-g007.jpg |
0.47756 | 29d39404894446e292fda492f0af0b25 | Schematic illustration of the intracellular dynamic process by complexes NH2NBS, EtNBS, and NMe2NBS during photoirradiation. | PMC9965410 | molecules-28-01714-sch001.jpg |
0.399425 | a87f1cdbb4f5472ba4a47ec8c275b4a0 | Synthesis scheme for NH2NBS, EtNBS, and NMe2NBS. | PMC9965410 | molecules-28-01714-sch002.jpg |
0.358395 | e38f40f54e01482bb597bd404a6e099f | FT-IR spectra of DPPDA and [Yb(DPPDA)2](DIPEA) in the 1800~1350 cm−1 range. | PMC9965908 | molecules-28-01632-g001.jpg |
0.509311 | 4efb8d35148943868b9fa9f19929010d | UV-Vis absorption spectra of DPPDA (in 1 × 10−5 mol/L CH2Cl2 solution) and [Ln(DPPDA)2](DIPEA) (in 1 × 10−5 mol/L CHCl3 solution) at room temperature. | PMC9965908 | molecules-28-01632-g002.jpg |
0.511283 | ccdf2e11132342afab2fa9ba6d116ba0 | TG and DTG curves of [Yb(DPPDA)2](DIPEA) at a heating rate of 10 °C/min. | PMC9965908 | molecules-28-01632-g003.jpg |
0.452168 | b88c8b51b39841debe1e28dd736bc419 | (a) Excitation and emission spectra of [Yb(DPPDA)2](DIPEA) (in 1.1 × 10−4 mol/L CHCl3 solution) at room temperature. (b) UV-Vis emission spectra of [Gd(DPPDA)2](DIPEA) and [Yb(DPPDA)2](DIPEA) (in 1.1 × 10−4 mol/L CHCl3 solution, λex = 348 nm) at room temperature. | PMC9965908 | molecules-28-01632-g004.jpg |
0.443145 | 3f20e6fb0f3a416d902c52c0a1cbd592 | Schematic representation of energy transfer mechanism of ytterbium complexes (A = absorption, F = fluorescence, P = phosphorescence, nr = non-radiative, ISC = intersystem crossing, ET = energy transfer, 1S1* = singlet state, 3T* = triplet state). | PMC9965908 | molecules-28-01632-g005.jpg |
0.495231 | eaf994977dc3476a94f12178a2929631 | Schematic representation of internal redox mechanism of [Yb(DPPDA)2](DIPEA). | PMC9965908 | molecules-28-01632-g006.jpg |
0.47031 | 9504d81942134dd794508525aebc0f5f | The synthetic routes of the ligand DPPDA and the Ln complexes [Ln(DPPDA)2](DIPEA). | PMC9965908 | molecules-28-01632-sch001.jpg |
0.494953 | 68d2f8fdf9994ac28183d48f6473066a | Peripheral nerve structure. Each axon is enveloped by endoneurium and Schwann cells. Groups of these nerve filaments are organized into fascicles by perineurium, and these fascicles are finally sheathed in epineurium to form a peripheral nerve. | PMC9966153 | jcm-12-01555-g001.jpg |
0.51145 | 7913a5bc25734b45bad44826b52b72a5 | (A). Intact peripheral nerve. (B). Nerve transection leads to events in the proximal stump and distal stump. Proximally, the cell nucleus moves to the periphery and Nissl bodies disperse with increased protein synthesis to help repair the damage and seal the proximal membrane. Distally, Wallerian degeneration occurs which includes de-differentiation of Schwann cells, recruitment of macrophages that help breakdown and clear the debris in preparation of axonal regeneration. | PMC9966153 | jcm-12-01555-g002.jpg |
0.483014 | f67d7c17e6164b26b18ea65e0ac2afa3 | (A). Nerve coaptation via epineural suturing technique demonstrating sutures in the epineurium. (B). Nerve coaptation via fascicular repair demonstrating sutures in individual fascicles. | PMC9966153 | jcm-12-01555-g003.jpg |
0.503883 | a68f9f96c44b4265b4fe75e6f92a9fc0 | The key molecular players in peripheral nerve regeneration. In blue are factors that favor End-To-End (ETE) repair and in orange are factors that favor End-To-Side (ETS) repair. Factors that favor both ETE and ETS repair are in black. RAGs= Regeneration Associated Genes; GDNF = Glial Derived Neurotrophic Factor; NGF = Nerve Growth Factor; VEGF = Vascular Endothelial Growth Factor; BDNF = Brain-Derived Neurotropic Factor; NT3 = Neurotrophin-3; ARTN = Artemin. | PMC9966153 | jcm-12-01555-g004.jpg |
0.4628 | f70ee90c80e340b4baf16a852c9ecb0c | End-to-side nerve repair. Traditional end-to-side nerve coaptation involves the coaptation of the distal denervated stump into the side of the intact donor nerve. Any axons that are present in the distal recipient nerve stump exclusively originate from the donor nerve. | PMC9966153 | jcm-12-01555-g005.jpg |
0.499731 | 52d71c7af38b469ebb4000b09afcb04a | Proposed mechanism for axonal regeneration in End-To-Side (ETS) repair. Schwann cells from donor nerve and/or recipient nerve de-differentiate into the reparative phenotype and align themselves at the coaptation site. Collateral axonal sprouting occurs at the node of Ranvier closest to the coaptation site. NTFs = Neurotropic Factors. | PMC9966153 | jcm-12-01555-g006.jpg |
0.555396 | 1a6dd2b13d684c05a89180a76d54d43c | End-to-end (ETE) nerve repair technique demonstrating the coaptation of the injured nerve distal to the site of injury to an intact donor nerve (DN) through an epineural window. (A) Nerve injury. (B) Injury with downstream STS repair. (C) Injury with ETE repair at the site of injury and downstream STS repair. (D) Injury with ETS repair at the site of injury and downstream STS repair. Arrow points to the level of injury. | PMC9966153 | jcm-12-01555-g007.jpg |
0.417436 | 42a1e00201564b5e9d88bd76796aeefa | Ras-MAP signaling pathway for Schwann cell dedifferentiation as proposed by Napoli et al. Ras activates protein kinase Raf, which then activates mitogen-activated protein kinase-kinase (MEK), in turn promoting mitogen-activated protein kinase (ERK) signaling that then maintains the de-differentiated state of Schwann cells. TR = Tamoxifen-inducible RAF-Kinase; HSP = Heat Shock Protein; RAF = Rapidly Accelerated Fibrosarcoma (Adapted from Napoli et al. [60]). | PMC9966153 | jcm-12-01555-g008.jpg |
0.445219 | 463c3889d1fd4ad3a10b9bf561b47865 | Schematic representation of cytokine expression in the indeterminate and cardiac clinical forms of Chagas disease. In the indeterminate clinical form, an increased expression of anti-inflammatory cytokines, such as IL-10 and IL-17 is observed. However, in the cardiac clinical form, the increased expression of pro-inflammatory cytokines, such as IFN-gamma and TNF, favor the establishment of the inflammatory environment. Cytokines, such as IL-7 and IL-15, have been associated with the cardiac clinical form. | PMC9966322 | pathogens-12-00171-g001.jpg |
0.422421 | fc24bd0b610a4ea5b7587d6560f50936 | Cytotoxic and inflammatory immune response in chronic Chagas cardiomyopathy. T cells mediate cytotoxicity in chronic Chagas cardiomyopathy. These cells are recruited to the heart by adhesion molecules and chemokines, and can release inflammatory cytokines and cytotoxic molecules, such as granzymes and perforins, that contribute to cardiac tissue damage, fibrosis, and disease severity (Designed with Biorender). | PMC9966322 | pathogens-12-00171-g002.jpg |
0.458793 | ab996639c258404faae57f406f91f0c4 | Cytokine activation of STAT and association with Th1/Th2 development. The engagement of inflammatory cytokines, such as IFN-gamma, IL6, IL12, and TNF, with their receptors favors the activation of transcription factors STAT1, STAT3, STAT4, and NF-kB, which contributes to the production of Th1 cytokines. While in modulatory environments, the presence of IL4 cytokine activates STAT6, which contributes to the production of Th2 cytokines. The association of STAT with cytokines (right corner of figure) emphasizes the main STAT associated with the cytokine, although other STAT may also be activated by the same cytokine (Designed with Biorender). | PMC9966322 | pathogens-12-00171-g003.jpg |
0.475198 | db30ad7b9d654932a6dbe0bbcd3aae60 | The hypothesized model. | PMC9966528 | ijerph-20-03426-g001.jpg |
0.444654 | 74d4a836f006478fba34f43a6d7a0818 | Johnson-Neyman regions of significance and confidence bands for mother-rated CU traits along teacher-child conflict in relation to aggressive behavior. Note. Solid diagonal line represents the regression coefficient for CU along with teacher-child conflict. Dashed diagonal yellow lines are confidence bands—upper and lower bounds of 95% confidence interval for CU coefficient along teacher-child conflict. The dashed vertical blue line indicates the point along teacher-child conflict at which the CU regression coefficient transitions from nonsignificance (left of the dashed vertical line) to statistical significance (right of dashed vertical line). The value of the dashed vertical line is 0.30. | PMC9966528 | ijerph-20-03426-g002.jpg |
0.503553 | d3e180141a72432e9cb2ab3d5f41b42d | Johnson-Neyman regions of significance and confidence bands for mother-rated CU traits along teacher-child conflict in relation to prosocial behavior. Note. Solid diagonal line represents the regression coefficient for CU along with teacher-child conflict. Dashed diagonal yellow lines are confidence bands—upper and lower bounds of 95% confidence interval for CU coefficient along teacher-child conflict. The dashed vertical blue line indicates the point along teacher-child conflict at which the CU regression coefficient transitions from nonsignificance (left of dashed vertical line) to statistical significance (right of dashed vertical line). The value of the dashed vertical line is −0.28. | PMC9966528 | ijerph-20-03426-g003.jpg |
0.443931 | 966dbc6b3a094595ace1bb5a63688ad4 | Johnson-Neyman regions of significance and confidence bands for mother-rated CU traits along teacher-child conflict in relation to asocial behavior. Note. Solid diagonal line represents the regression coefficient for CU along with teacher-child conflict. Dashed diagonal yellow lines are confidence bands—upper and lower bounds of 95% confidence interval for CU coefficient along teacher-child conflict. The dashed vertical blue line indicates the point along teacher-child conflict at which the CU regression coefficient transitions from nonsignificance (left of dashed vertical line) to statistical significance (right of dashed vertical line). The value of the dashed vertical line is 0.20. | PMC9966528 | ijerph-20-03426-g004.jpg |
0.500515 | fd20d2dbf17f4817badc663d25af115b | Portion of S gene sequence (of the SARS-CoV-2 genome): Wild type and variant showing the deletions 69–70 and portion of ORF1a gene with deletion 3675/3677. | PMC9966895 | viruses-15-00353-g001.jpg |
0.384853 | 1a2e1c71a4a94dbe94b47b615b3c9014 | Electropherogram showing the sequence of samples in which more than one SARS-CoV-2 variant was present. | PMC9966895 | viruses-15-00353-g002.jpg |
0.529627 | e5948884ebe44a85b1120bfd8d66041f | Specificity test of our assay. | PMC9966895 | viruses-15-00353-g003.jpg |
0.416352 | 9f2e883304f94c7ea7915ae109067d88 | Sensitivity test of our assay. | PMC9966895 | viruses-15-00353-g004.jpg |
0.458799 | 74cc9aa6766349379cac087d0a677637 | Proposed models for ICRAC, ISOC, and ICRAC−like currents. In the absence of extracellular stimulation, STIM1 is homogeneously distributed within ER cisternae, whereas Orai1, TRPC1, and TRPC4 are located on the PM. Upon depletion of the ER Ca2+ store, STIM1 aggregates and translocates in close apposition to the PM, thereby recruiting Orai1 hexamers into spatially confined puncta and activating the ICRAC. Orai1−mediated extracellular Ca2+ entry can cause TRPC1 insertion into the plasma membrane (shown in Figure 2), thereby enabling TRPC1 activation by STIM1 and activating the ISOC. Finally, STIM1 can determine the assembly of a complex ion channel signalplex consisting also of Orai1, TRPC1, and TRPC4 and responsible for the development of ICRAC−like currents. As explained in Section 6.1, this supermolecular channel complex includes 1 TRPC1 subunit and 2 TRPC4 subunits. The lower current density of the ICRAC as compared to the ISOC and the ICRAC-like current reflects the single-channel conductance of Orai1 channels, which is 1000-fold lower as compared to TRPC channels. The current density is defined by the ratio between the magnitude of an ion current, in pA, and the cell membrane capacitance, in pF. | PMC9967124 | ijms-24-03259-g001.jpg |
0.382417 | 1f318a0692584fa5b261e64194afa312 | Illustrations describing the two proposed models of Orai1-dependent TRPC1 activation. In the absence of extracellular stimulation, TRPC1 is located both on the PM and on submembrane vesicles (A). Depletion of the ER Ca2+ store prompts STIM1 to oligomerize, extend the cytosolic COOH-terminal domain towards the PM, translocate to ER-PM junction, and physically engage Orai1 to mediate the ICRAC (B, left panel). The following influx of Ca2+ can induce the exocytosis of TRPC1-containing vesicles. TRPC1 is inserted into the PM in close apposition to Orai1 and is thereafter activated by STIM1 to mediate the ISOC (B, left panel). Alternately, TRPC1 can physically interact with Orai1 and indirectly become store-operated (B, right panel). Adapted from [88]. | PMC9967124 | ijms-24-03259-g002.jpg |
0.438208 | dcf811f0a39c4e1798b839ab75c72d32 | The molecular architecture of the ISOC in vascular endothelial cells. (A), the endothelial ISOC is mediated by a complex ion channel signalplex that is located on plasmalemmal caveolae. The ion channel pore is contributed by TRPC1 and TRPC4 channels, which are informed about changes in [Ca2+]ER by STIM1. The signalling microdomain is enriched with InsP3Rs, which interact with the TRPC1 and TRPC4 subunits via caveolin-1. For sake of clarity, only the interaction between InsP3Rs and TRPC1 has been shown. The monomeric GTP−binding protein, RhoA, also supports the interaction between InsP3Rs and TRPC1 via F−actin polymerization (two bundles of F-actin were drawn beneath the plasma membrane). (B), the IV relationship of the endothelial ISOC. | PMC9967124 | ijms-24-03259-g003.jpg |
0.447655 | f6c14b6f2da14647b58aa784a24c083e | The molecular architecture of the ICRAC-like channel in vascular endothelial cells. A series of studies carried out on rPAECs demonstrated that the ion channel signalplex mediating the endothelial ICRAC−like currents is contributed to by one TRPC1 subunit and two TRPC4 subunits, as well as by Orai1, and is located within caveolae. TRPC4 is physically associated with both Orai1 and the actin-binding protein, protein 4.1. The latter, in turn, must be associated with the spectrin membrane skeleton (A). A reduction in [Ca2+]ER (not shown) causes the STIM1-dependent activation of the ion channel signalplex on the PM (B). STIM1 is likely to physically interact with Orai1, TRPC1, and TRPC4, but this hypothesis remains to be experimentally probed. Orai1 incorporation into the STIM1/TRPC1/TRPC4 complex determines the Ca2+−selectivity of the store-operated current, which can therefore be defined as ICRAC-like (C). For sake of clarity, the spectrin−F-actin network beneath the plasma membrane has not been shown in Panel B. | PMC9967124 | ijms-24-03259-g004.jpg |
0.44386 | 3bfe7def56224922bc3a1076e3d95152 | Endothelial functions regulated by Ca2+ entry through the diverse SOCE mechanisms. This illustration summarizes the different endothelial functions regulated by the ICRAC (Orai1 in green), ICRAC-like currents (TRPC4 in blue plus TRPC1/Orai1 in red/green), and ISOC (TRPC1 in red). | PMC9967124 | ijms-24-03259-g005.jpg |
0.393511 | 710b7606930a43ad92bbe8487d02ec26 | Illustration of the synthesis of LLZO&LNO@LCO. | PMC9967944 | membranes-13-00216-g001.jpg |
0.505054 | b9b6ddcb61aa4a8e8af589238a7b17b9 | SEM image of LLZO&LNO@LCO with different magnification, 1000 (A), 3000 (B), 5000 (C), 10,000 (D). | PMC9967944 | membranes-13-00216-g002.jpg |
0.436194 | 6bc1a6915bd041f0aca5ce891e061510 | (A) selected particles, and elemental O (B), Co (C), Zr (D), Nb (E), and La (F) mapping of LLZO&LNO@LCO. | PMC9967944 | membranes-13-00216-g003.jpg |
0.440095 | 1c1efbc9b0c347c3b861d21c4ae825e1 | XRD pattern (A) and Raman spectra (B) of LLZO&LNO@LCO and LCO. | PMC9967944 | membranes-13-00216-g004.jpg |
0.43745 | f868801d0d95475bb07d0cb8ed722b2d | Volume resistance and density of LLZO&LNO@LCO (A) and LCO (B) under different pressures. | PMC9967944 | membranes-13-00216-g005.jpg |
0.439616 | d5cd5b37821c46bfaace25729211a29c | Charging and discharging curve of LCO||LPSC||Li-In (A) and LLZO&LNO@LCO||LPSC||Li-In (B,C) discharging capacity of LLZO&LNO@LCO at a different rate, (D) lifecycles of LLZO&LNO@LCO||LPSC||Li-In at 0.05 C. | PMC9967944 | membranes-13-00216-g006.jpg |
0.453632 | 931f07ed87b7408b8236cdca67bc49a2 | EIS curve of LCO||LPSC||Li-In and LLZO&LNO@LCO||LPSC||Li-In before (A) and after 20 cycles (B). | PMC9967944 | membranes-13-00216-g007.jpg |
0.401745 | 9ce900787d124fe486f822cc1ca0d3aa | Charging GITT profiles (A) and discharging GITT profiles (B) of LLZO&LNO@LCO and LCO samples measured at the first cycle. Charging polarization voltage profiles (C) and discharging polarization GITT profiles (D) of LLZO&LNO@LCO and LCO samples measured at the first cycle. | PMC9967944 | membranes-13-00216-g008.jpg |
0.514124 | 0c2c1cfdf5aa472a95b535388bae3ad0 | Schematic representation of adjuvant (A) or palliative (B) treatment settings (patients with no evidence of disease and those with distant metastases respectively). | PMC9968744 | fimmu-14-1065767-g001.jpg |
0.497037 | f1185277a56f4379a63af231f97dc22d | Characteristics of PMN- and M-MDSC from melanoma patients before ICI therapy. PBMCs were isolated from the peripheral blood of melanoma patients and HD. MDSC and their counterparts in HD were assessed by flow cytometry. (A) The results in metastatic (n=19) and non-metastatic (n=8) patients as well as their counterparts in HD (n=10) are presented as the percentage of HLA-DRlow/−CD33dimCD66b+Lin− PMN- and HLA-DRlow/−CD33highCD14+ M-MDSC among live PBMC. (B) OS of metastatic melanoma patients with high (>0.54% of live PBMC; n=10) and low (<0.54%; n=9) PMN-MDSC frequencies at the baseline is shown as a Kaplan-Meier curve. (C) OS of metastatic melanoma patients with high (>0.73%; n=10) and low (<0.73%; n=9) M-MDSC frequencies at the baseline is shown as a Kaplan-Meier curve. (D, E) Expression of PD-L1 and ectoenzymes CD39 and CD73 on PMN- and M-MDSC from metastatic and non-metastatic patients was shown as the percentage of PD-L1+ cells (D) or CD39+CD73+ cells (E) among the respective MDSC subset. (F) Immunosuppressive capacity of PMN- and M-MDSC was determined upon the co-culture with activated CD3 T cells labeled with CP-Dye405. After 96 h of incubation, T cell proliferation was assessed by CP-Dye405 dilution measured by flow cytometry. Cumulative data for T cell proliferation are presented as the percentage of divided T cells normalized (norm.) to the respective control of stimulated T cells alone (n=3-8). *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001. | PMC9968744 | fimmu-14-1065767-g002.jpg |
0.42177 | 52963b73a27541639e30557f3835df94 | Baseline characteristics of PMN- and M-MDSC from responders and non-responders. (A) Results are presented as the frequency of circulating PNM- and M-MDSC among live PBMC from responders (n=12) and non-responders (n=6). Representative histograms for the proliferation of unstimulated (unstim) and stimulated (stim) T cells incubated alone or in the presence of isolated PMN- or M-MDSC from a non-responding (B) and responding patient (C). (D) Immunosuppressive capacity of PMN- and M-MDSC was determined upon the co-culture with activated CD3 T cells labeled with CP-Dye405. Cumulative data for T cell proliferation are shown as the percentage of divided T cells normalized (norm.) to the respective control of stimulated T cells alone (n=2-8). | PMC9968744 | fimmu-14-1065767-g003.jpg |
0.421694 | 06882a25b6434e47a968740846d8b2f1 | Production of inflammatory factors in melanoma patients at the baseline. Concentrations of IL-6, IL-8, TNF-α (A) and CCL5 (B) were detected in plasma of metastatic (n=16) and non-metastatic (n=7) patients as well as HD (n=10) by bio-plex assay and expressed as pg/ml. The frequency PMN-MDSC among PBMC were plotted against the level of IL-6 (C), IL-8 (D) and TNF-α (E) in metastatic melanoma patients (n=15). The correlation was evaluated by a linear regression analysis. (F) The frequency M-MDSC within PBMC were plotted against the level of IL-6 in metastatic melanoma patients (n=15). The correlation was evaluated by a linear regression analysis. (G) Concentrations of IL-6, IL-8, TNF-α and CCL5 in plasma from metastatic patients, responding (n=10) and non-responding (n=4) to the ICI treatment are expressed as pg/ml. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001. | PMC9968744 | fimmu-14-1065767-g004.jpg |
0.453074 | 286fca909e9348538ee589ce5a4a303a | Analysis of MDSC in melanoma patients during the ICI therapy. PBMC were isolated from metastatic (n=16) and non-metastatic (n=5) patients before each ICI application (point 0 - prior the treatment; point 1 - after the first infusion; point 2 - after the second infusion; point 3 - after the third infusion) and assessed by flow cytometry. (A) Levels of circulating PMN-MDSC in metastatic and non-metastatic patients are expressed as the percentage within live PBMC. (B) Immunosuppressive capacity of PMN- and M-MDSC was determined upon the co-culture with activated CD3 T cells labeled with CP-Dye405. Cumulative data for T cell proliferation are shown as the percentage of divided T cells normalized to the respective control of stimulated T cells alone (n=5-16). Levels of circulating PMN- (C) and M-MDSC (D) in metastatic patients, responding (n=12) and non-responding (n=4) to the ICI therapy are expressed as the percentage of corresponding subsets among live PBMC. PD-L1 expression on PMN- (E) and M-MDSC (F) in responders (n=12) and non-responders (n=4) is presented as the percentage of PD-L1+ cells among the respective MDSC subset. (G) Immunosuppressive activity of PMN- and M-MDSC was measured at different time points during the ICI therapy upon the co-culture with activated CD3 T cells labeled with CP-Dye405. Cumulative data for T cell proliferation are shown as the percentage of divided T cells normalized to the respective control of stimulated T cells alone (n=1-10). *P < 0.05, **P < 0.01. | PMC9968744 | fimmu-14-1065767-g005.jpg |
0.455464 | 9619a107aa074e158b81235370a69914 | Evaluation of cytokine and chemokine concentrations in melanoma patients during the ICI treatment. Levels of IL-6 (A), IL-8 (B), TNF-α (C) and CCL5 (D) were measured in plasma of metastatic patients responding (n=12) and non-responding (n=4) to the ICI therapy (point 0 - before the treatment; 1 - after the first injection; 2 - after the second injection; 3 - after the third injection) by bio-plex assay and expressed as pg/ml. *P < 0.05, **P < 0.01. | PMC9968744 | fimmu-14-1065767-g006.jpg |
0.449961 | f93cfc9bd9904c4cbb5a3896685c51c5 | Protein expression of H2S-generating and degradation enzymes in aorta of Cth/Mpst
−/−
mice. Proteins were extracted from aorta of WT and double Cth/Mpst knockout mice and subjected to SDS-PAGE and western blotting. Representative western blots and quantification of (A) MPST, CTH, CBS, (B) ETHE1, TST, SQRDL and (C) protein persulfidation levels in aorta. Protein expression is presented as ratio over WT group. Data were normalized to GAPDH or β-ΤUBULIN and presented as means ± S.E.M. N = 4 mice per group. | PMC9969096 | fphar-14-1090654-g001.jpg |
0.44893 | 1f50c9092c6c4ae1a6f6607a46afe98d |
Cth/Mpst double deletion does not affect the expression of CBS and sulfide-metabolism enzymes in heart. WT and Cth/Mpst
−/−
mice were sacrificied, proteins were extracted from heart tissues and enzymes leves were determined by western blot. Representative western blots and quantification of (A) MPST, CTH, CBS and (B) ETHE1, TST, SQRDL levels in heart. Protein expression is presented as ratio over WT group. Data were normalized to GAPDH and presented as means ± S.E.M. N = 6 mice per group. | PMC9969096 | fphar-14-1090654-g002.jpg |
0.518615 | 9c47ebe8c8514cd494d4c22929b75694 |
Alterations in serum-biochemical parameters after the Cth/Mpst double ablation. Serum levels of (A) alkaline phosphatase (ALP), alanine transaminase (ALT), aspartate aminotransferase (AST), (B) creatine kinase (CK), lactate dehydrogenase (LDH), α-amylase, (C) creatinine, urea, uric acid, albumin, (D) transferrin, ferritin, (E) total-bilirubin, direct-bilirubin, (F) glucose, cholesterol, high-density lipoprotein (HDL) cholesterol, low-density lipoprotein (LDL) cholesterol and triglycerides of WT and Cth/Mpst
−/−
mice. Data are presented as means ± S.E.M, *p < 0.05 and ***p
≤
0,001, N = 5–7 mice per group. | PMC9969096 | fphar-14-1090654-g003.jpg |
0.426897 | f83af65a3d69473d9aa4025bf67c1dd0 |
Cth/Mpst
−/−
mice exhibit reduced blood pressure. (A) Systolic, (B) diastolic and (C) mean arterial blood pressure of WT and Cth/Mpst
−/−
mice. Data are presented as means ± S.E.M, *p < 0.05 and **p
≤
0.01, N = 7 mice per group. | PMC9969096 | fphar-14-1090654-g004.jpg |
0.423524 | 51b3ec7a530c42fd89fc49bd39bb48d4 | Normal cardiac function parameters after the double Cth/Mpst inhibition in mice. (A) Heart rate (HR), (B, C) left ventricular (LV) end-diastolic and end systolic diameter (LV EDD, LV ESD), (D, E) LV posterior wall thickness at diastole and systole (PWd, PWs), (F) fractional shortening (FS%), (G) ejection fraction (EF) and (H) LV radius to LV posterior wall thickness ratio (r/h) analyzed by echocardiography in WT and knockout mice. Data are presented as means ± S.E.M, *p < 0.05, **p ≤ 0.01 and ***p ≤ 0.001, N = 7 mice per group. | PMC9969096 | fphar-14-1090654-g005.jpg |
0.480958 | 0a28898f3ef040e7a5289f4a08c120ab | Vascular reactivity measurements of aortic rings from WT and Cth/Mpst
−/−
mice. (A) vasodilatatory response to Ach, (B) vasodilatory responses to (C) the NO donor, DEANONOate and (D) the sulfide-donor, NaHS, and (D) contractile responses to PE. (E) Increase in tension induced by the exposure of PE-pre-contracted aortic rings (300 nM) to L-NIO (10 µM, 20 min). Data are presented as means ± S.E.M, *p < 0.05 and ***p ≤0.001, N = 4-6 mice per group. | PMC9969096 | fphar-14-1090654-g006.jpg |
0.410191 | 4f9d17be536449dda3713d2f95301349 |
Cth/Mpst double ablation results in upregulation of eNOS/sGC signaling in aorta. Representative western blots and quantification of eNOS, peNOSs1176, sGCα1, sGCBβ1 and PKG-Ι protein levels in (A) aorta and (B) heart protein lysates of WT and Cth/Mpst
−/−
mice. Protein expression is presented as ratio over WT group. Data were normalized to GAPDH or eNOS and presented as means ± S.E.M. *p < 0.05, **p
≤
0.01 and ***p
≤
0,001, (A) N = 3-4 and (B)
N = 6-7 mice per group. | PMC9969096 | fphar-14-1090654-g007.jpg |
0.395333 | 8ae762f51a274ad6bcdf21f6e4a061c4 | No differences in blood pressure between WT and double Cth/Mpst knockout mice after eNOS inhibition. WT and Cth/Mpst
−/−
mice were exposed to eNOS-inhibitor, L-NAME (0.5 g/L in drinking water) for 10 days and blood pressure was measured. (A) Systolic, (B) diastolic and (C) mean arterial blood pressure of WT and Cth/Mpst
−/−
mice after L-NAME administration. Data are presented as means ± S.E.M, N = 5 mice per group. | PMC9969096 | fphar-14-1090654-g008.jpg |
0.421167 | ccc99d5a9dab4a8aa0fedcfaa912fa25 | Flow diagram of literature search. | PMC9969171 | gr1.jpg |
0.471688 | 7c478e2ba0814561ad4fdb566e049fbc | A: The surface structure of pentameric envelope glycoprotein (7K3G). B: The molecular docking of 7K3G-TM. | PMC9969538 | gr10_lrg.jpg |
0.426002 | 117e3b07c0de464d87dc35bcfe3dc4fb | Molecular docking of 7MSW-TM. A: 2D interaction shows types of fusion in specific residues. B: Crystal structure of nsp2 (7MSW) shows the interaction location with TM. C: Molecular docking residues of 7MSW-TM, residues of conventional hydrogen bond (green), residues of carbon-hydrogen bond (cyan), and alkyl and pi-alkyl residues (magenta). | PMC9969538 | gr11_lrg.jpg |
0.448729 | e0723e025ee44816a5b78fc282edfdfd | Molecular docking of RBD (6M0J)-TM. A: 2D interaction shows types of fusion in specific residues. B: Crystal structure of RBD of spike glycoprotein (6M0J) shows the interaction location with TM. C: Molecular docking residues of RBD (6M0J)-TM, residues of conventional hydrogen bond (green), unfavorable donor residue (red), and alkyl and pi-alkyl residues (magenta). | PMC9969538 | gr12_lrg.jpg |
0.406994 | b92d49ead4d04f449fe9e93c0b6e0683 | Molecular docking of TM-RBD-ACE2. A: Cartoon structure of molecular docking of RBD-ACE2 (7K3G). B: Cartoon structure of the molecular docking of 7K3G-TM. C: The surface structure of 7K3G and TM shows the interaction residues of TM with RBD, hydrogen bond (green), unfavorable donor residue (red), and alkyl and pi-alkyl residues (magenta). | PMC9969538 | gr13_lrg.jpg |
0.521829 | 43e64887150a4f909f485140b07892fc | A: Chemical structure of tunicamycin. B: crystal structure of TM. C: 3D structure of TM after docking with a protein. | PMC9969538 | gr1_lrg.jpg |
0.447416 | ec2c0421003b4209a0cd2ee0c6c64b74 | Molecular docking of 1P9S-TM. A: 2D interaction shows types of fusion in specific residues. B: Crystal structure of proteinase (1P9S) shows the interaction location with TM. C: Molecular docking residues of 1P9S-TM, residues of conventional hydrogen bond (green), residues of carbon-hydrogen bond (cyan), and alkyl residues (magenta). | PMC9969538 | gr2_lrg.jpg |
0.451826 | da269a4f166c430796f084d86ef7c9d2 | Molecular docking of 1Q2W-TM. A: 2D interaction shows types of fusion in specific residues. B: Crystal structure of protease (1Q2W) shows the interaction location with TM. C: Molecular docking residues of 1Q2W-TM, residues of conventional hydrogen bond (green), residues of carbon-hydrogen bond (cyan), alkyl residues (magenta), and unfavorable acceptor bound (red). | PMC9969538 | gr3_lrg.jpg |
0.446558 | 0c9db11887204b99bcc83dbf884cceb3 | Molecular docking of 1QZ8-TM. A: 2D interaction shows types of fusion in specific residues. B: The crystal structure of nsp9 (1QZ8) shows the interaction location with TM. C: Molecular docking residues of 1QZ8-TM, residues of conventional hydrogen bond (green), residues of carbon-hydrogen bond (cyan), alkyl residues (magenta), pi-donor hydrogen bond (dark cyan), and unfavorable acceptor or donor bond (red). | PMC9969538 | gr4_lrg.jpg |
0.47066 | 59a678e09c9b4c87be1fee9a1e3748a5 | Molecular docking of 1XAK-TM. A: 2D interaction shows types of fusion in specific residues. B: The crystal structure of ORF7a (1XAK) shows the interaction location with TM. C: Molecular docking residues of 1XAK-TM, residues of conventional hydrogen bond (green), residues of carbon-hydrogen bond (cyan), alkyl, and pi-alkyl residues (magenta), and pi-sulfur bond (pale orange). | PMC9969538 | gr5_lrg.jpg |
0.419804 | dc717b35a7ab4347b827fb1a12f89d02 | Molecular docking of 6XDC-TM. A: 2D interaction shows types of fusion in specific residues. B: The crystal structure of ORF3a (6XDC) shows the interaction location with TM. C: Molecular docking residues of 6XDC-TM, residues of conventional hydrogen bond (green), residues of carbon-hydrogen bond (cyan), alkyl residues (magenta), pi-alkyl bond (dark magenta), and pi-pi-stacked bound (red). | PMC9969538 | gr6_lrg.jpg |
0.43184 | 206e9bc081d54912b25c9f123c9bbb05 | Molecular docking of 7DHG-TM. A: 2D interaction shows types of fusion in specific residues. B: The crystal structure of ORF9b (7DHG) shows the interaction location with TM. C: Molecular docking residues of 7DHG-TM, residues of conventional hydrogen bond (green), residues of carbon-hydrogen bond (cyan), alkyl, and pi-alkyl residues (magenta), and unfavorable acceptor bond (red). | PMC9969538 | gr7_lrg.jpg |
0.396845 | 7153c876279f4e2bb4dc41a608941896 | Molecular docking of 7JX6-TM. A: 2D interaction shows types of fusion in specific residues. B: The crystal structure of ORF8 (7JX6) shows the interaction location with TM. C: Molecular docking residues of 7JX6-TM, residues of conventional hydrogen bond (green), alkyl residues (magenta), and unfavorable donor residue (red). | PMC9969538 | gr8_lrg.jpg |
0.404298 | a649f681bc6742c0abc2ff419fd7e2d1 | Molecular docking of 7K3G-TM. A: 2D interaction shows types of fusion in specific residues. B: The crystal structure of envelope protein (7K3G) shows the interaction location with TM. C: Molecular docking residues of 7K3G-TM, residues of conventional hydrogen bond (green), residues of carbon-hydrogen bond (cyan), and alkyl and pi-alkyl residues (magenta). | PMC9969538 | gr9_lrg.jpg |
0.428177 | d048172479fb42dab5035fcc98dbde6c | Mechanical power versus rotor speed. | PMC9970108 | pone.0281116.g001.jpg |
0.443891 | c1fe5d3f0f164a18830a1b4fb5e590b2 | Schematic of the overall system, i.e., PMSG-based WECS. | PMC9970108 | pone.0281116.g002.jpg |
0.388025 | ad5139320f7f4c22a1b8886006d87fbf | Delta estimation versus time. | PMC9970108 | pone.0281116.g003.jpg |
0.462728 | f689e15d7b1e4ad6bcfe95fe12e735fe | High speed shaft rotational speed. | PMC9970108 | pone.0281116.g004.jpg |
0.417969 | f51ccc97fc3e45799a12baa58e4fa642 | Low-speed shaft rotational speed versus low-speed shaft power. | PMC9970108 | pone.0281116.g005.jpg |
0.417746 | f955c538a1e6468980964e9dbc16cf87 | Tip speed ratio versus high speed shaft power. | PMC9970108 | pone.0281116.g006.jpg |
0.477803 | e35165630b2649879327f8108a47119a | Tip speed ratio versus low speed shaft power. | PMC9970108 | pone.0281116.g007.jpg |
0.468062 | 8f2b4c79b21a4edb97acb19060a8e892 | Tip speed ratio versus time. | PMC9970108 | pone.0281116.g008.jpg |
0.464244 | f6512e3f3377493eb3c1d10b39dc5aae | Power coefficient versus time. | PMC9970108 | pone.0281116.g009.jpg |
0.40051 | bf983c7c69634bff9dd69c97527715e4 | Delta estimation versus time. | PMC9970108 | pone.0281116.g010.jpg |
0.464597 | fcfade66ef2c472b9a6559034fbb2100 | High speed shaft rotational speed. | PMC9970108 | pone.0281116.g011.jpg |
0.425411 | 3d770498bebb4fb2bfe6633e10e7799d | Low shaft rotational speed versus low-speed shaft power. | PMC9970108 | pone.0281116.g012.jpg |
0.437452 | 7125c7ee7d3f42a0b05b15833244de8a | Tip speed ratio versus high speed shaft power. | PMC9970108 | pone.0281116.g013.jpg |
0.465463 | 7cd15fc4a44c4036bccb1acc4f2ff71c | Tip speed ratio versus low speed shaft power. | PMC9970108 | pone.0281116.g014.jpg |
0.440254 | 293428fb79dd4ed2af71cab35be26d92 | Tip speed ratio versus time. | PMC9970108 | pone.0281116.g015.jpg |
0.472377 | f7a46e9bd1a0466e9e13b50013a3c206 | Power coefficient versus time. | PMC9970108 | pone.0281116.g016.jpg |
0.42628 | f6d954bd97be4ca89fcac62fc4a1dd77 | Intraoperative incidental finding of bilateral arcuate line hernias. | PMC9970695 | rjad076f1.jpg |
0.491151 | c60a39e5ec814d5f832afd1f4d041b41 | Posterior sheath is comprised of fibers from the aponeurosis of the transversus abdominis and the posterior lamella of the internal oblique (cranial to the arcuate line). | PMC9970695 | rjad076f2.jpg |
0.436137 | 4595c06c66644c5d9ec2e02e127a5db7 | Posterior layer is composed only of transversalis fascia (below the arcuate line). | PMC9970695 | rjad076f3.jpg |
0.444575 | b6e3840905b243f0b89a65cfb1e93e88 | Herniation at the arcuate line into the pre-transversalis fascial plane. | PMC9970695 | rjad076f4.jpg |
0.45902 | 8bd591dea5f54f63b6892108ffbf4aa1 | Arcuate line hernia (intraoperative view). | PMC9970695 | rjad076f5.jpg |
0.488932 | 8484d7a9be8245be9791faf905856498 | CT imaging demonstrates separation of the posterior sheath from the rectus abdominis at the arcuate line with herniated fat or viscus (sagittal imaging). | PMC9970695 | rjad076f6.jpg |
0.504428 | ef6280aa521146848c14a4ca891d515f | PRISMA Flow Diagram of study search and selection (Shanghai, China, 2022). | PMC9970990 | ijph-68-1605606-g001.jpg |
0.437731 | c66df4db25954d0f980a4feba4745b43 | Light spectra and wavelengths. (a) The NIR spectrum lies between 780 and 2500 nm. Currently, almost all fluorescently labeled probes for FME are designed to emit in the NIR-I spectrum (780–900 nm). This design choice addresses three fundamental challenges: photon scattering by tissues, tissue autofluorescence, and tissue damage. First, the long wavelengths associated with both excitation and emission allow for deep-tissue imaging due to reduced scattering and increased penetration. Second: probes emitting in this spectral region benefit from high signal-to-background ratio, due to avoiding spectral regions associated with tissue autofluorescence. Third: the lower photon energies result in reduced tissue damage. (b) Example of excitation and emission spectra of the fluorescent dye IRDye 800CW. Due to vibrational relaxation in the excited or ground state orbitals, emitted photons must be equal to or lower in energy than the excitation photons. The emission spectrum is therefore red-shifted to longer wavelengths | PMC9971088 | 11307_2022_1741_Fig1_HTML.jpg |
0.453651 | 8e6f575c8f7b4ca5b1f76ee213ce4c69 | Schematic overview of a NIR-FME system. This figure illustrates the integration of a fiber bundle and an external NIR-fluorescence camera with a clinical endoscope. The NIR-system fiber bundle is inserted through the working channel of a standard clinical HD video endoscope (HDE). 750 nm laser light and short-pass filtered (SPF) white light from a LED are delivered through the illumination fibers of the fiber bundle to the distal end of the endoscope. Fluorophore-emitted and reflected white light return through the imaging fibers of the fiber bundle and are subsequently split by a dichroic mirror. Visible light is then detected by a color camera, and emitted fluorescent light is passed through a band-pass filter before being detected by an NIR-fluorescence camera. Previously published in Gut [13] | PMC9971088 | 11307_2022_1741_Fig2_HTML.jpg |
Subsets and Splits