nopperl/pmc-image-text · Datasets at Hugging Face

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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

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

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Low shaft rotational speed versus low-speed shaft power.

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Tip speed ratio versus high speed shaft power.

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Tip speed ratio versus low speed shaft power.

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Tip speed ratio versus time.

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Power coefficient versus time.

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Intraoperative incidental finding of bilateral arcuate line hernias.

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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).

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Posterior layer is composed only of transversalis fascia (below the arcuate line).

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Herniation at the arcuate line into the pre-transversalis fascial plane.

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Arcuate line hernia (intraoperative view).

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CT imaging demonstrates separation of the posterior sheath from the rectus abdominis at the arcuate line with herniated fat or viscus (sagittal imaging).

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PRISMA Flow Diagram of study search and selection (Shanghai, China, 2022).

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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

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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]

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