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

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0.496072	007d95aedfd141af97b75c26bc5075d5	(Left): release profile of polypill design MiniTab; modified basket apparatus, 1000 mL 0.1 N HCl, 50 rpm, 37.0 ± 0.5 °C, x ± s; n = 3. (Right): Image of MiniTab: red: PDM-PVA, blue: LD/BZ-EVA.	PMC9145509	pharmaceutics-14-00931-g011.jpg
0.480261	a17c0e6780fb4aaeb04e564a244d3058	(Left): release profile of MiniHCwC 1 (top) and 2 (bottom); modified basket apparatus, 1000 mL 0.1 N HCl, 50 rpm, 37.0 ± 0.5 °C, x ± s; n = 3. (Right): Image of MiniHCwC1 + 2: red: PDM-PVA, blue: LD/BZ-EVA.	PMC9145509	pharmaceutics-14-00931-g012.jpg
0.413065	9a2375644c74404e9e8059b8f8720bf1	Floating properties of MiniHCwC in 300 mL 0.1 N HCl, 37 ± 0.5 °C.	PMC9145509	pharmaceutics-14-00931-g013.jpg
0.451122	3be173f2e03446f89bcba67caeb87245	Food intake frequency before sleeve gastrectomy (SG) and after 10 months follow-up. Change in the frequency of meat and fish consumption in females (A), and males (B); change in the frequency of bread and crackers consumption in females (C), and males (D); change in the frequency of dairy products and fats consumption in females (E), and males (F).	PMC9145557	nutrients-14-02060-g001a.jpg
0.445988	82ac54bdbfcf4b04aad76ce989fab04f	Food intake frequency before sleeve gastrectomy (SG) and after 10 months follow-up. Change in the frequency of sweet and snacks in females (A), and males (B); change in the frequency of vegetables and fruits consumption in females (C), and males (D); change in the frequency of soft drinks consumption in females (E), and males (F).	PMC9145557	nutrients-14-02060-g002a.jpg
0.451895	015e16f63e8647c1821022f57f6ef136	Change in taste, desire, and enjoyment 12 months after SG in females.	PMC9145557	nutrients-14-02060-g003.jpg
0.435457	cd8c0b6c080f41a988d04e0cf079b097	Change in taste, desire, and enjoyment 12 months after SG in males.	PMC9145557	nutrients-14-02060-g004.jpg
0.451911	0f73555558b048f59594f7d4bc6aeda5	(a) Schematic illustration of a GO-coated SOI nanowire with a monolayer GO film. (bi) Schematic illustration of the cross section and (bii) the corresponding TE mode profile of the GO-coated SOI nanowire in (a). (c) Microscope image of an SOI chip uniformly coated with a monolayer GO film.	PMC9145626	micromachines-13-00756-g001.jpg
0.395909	23c9f0a878b14cae95609224115970f5	Experimental setup for measuring loss and SPM of GO-coated SOI nanowires. CW laser: continuous-wave laser. FPL: fiber pulsed laser. PC: polarization controller. VOA: variable optical attenuator. OPM: optical power meter. DUT: device under test. CCD: charged-coupled device. OSA: optical spectrum analyzer.	PMC9145626	micromachines-13-00756-g002.jpg
0.455014	435bad2a7b5b44d59e5c240215c8dfe8	(a) Measured excess insertion loss (EIL) of GO-coated SOI nanowires versus input power of optical pulses. (b) Excess propagation loss induced by the SA (∆SA) versus peak power of input optical pulses. In (a,b), the results for uncoated (N = 0) and hybrid SOI nanowires coated with one and two layers of GO (N = 1, 2) are shown for comparison. The data points depict the average of measurements on three samples, and the error bars illustrate the variations among the different samples.	PMC9145626	micromachines-13-00756-g003.jpg
0.406055	5427cf61bd0e4a1091c85c6702c1a7ae	SPM experimental results. (a) Normalized spectra of optical pulses before and after propagation through the GO-coated SOI nanowires with one and two layers of GO at an input peak power of ∼160 W. (b,c) Optical spectra measured at different input peak powers for the hybrid waveguides with one and two layers of GO, respectively. (d) BFs of the measured output spectra versus input peak power for the hybrid waveguides with one and two layers of GO. In (a–d), the corresponding results for the uncoated SOI nanowires (N = 0) are also shown for comparison.	PMC9145626	micromachines-13-00756-g004.jpg
0.390844	7c58b594309749eeaadd9cc7dad3e050	(a) BFs of femtosecond optical pulses versus GO film length (Lc) for the hybrid waveguides with one and two layers of GO. The peak power is ~160 W. (b) BFs of picosecond optical pulses versus GO film length (Lc) for the hybrid waveguides with one and two layers of GO. The peak power is ~13 W. In (a,b), the corresponding results for uncoated waveguides (N = 0) are also shown for comparison.	PMC9145626	micromachines-13-00756-g005.jpg
0.45998	9dcdedd26a5142eea8e1d5d744927dfb	(a) Effective interaction length (Leff) versus waveguide length (L) for GO-coated SOI nanowires uniformly coated with one and two layers of GO. (b) FOM2 versus waveguide length (L) for hybrid waveguides uniformly coated with one and two layers of GO. In (a,b), the corresponding results for uncoated waveguides (N = 0) are also shown for comparison.	PMC9145626	micromachines-13-00756-g006.jpg
0.519159	283eda8f04a84d4b8aceeb63b0c5bbe6	Classification of pulp testing methods.	PMC9145630	medicina-58-00665-g001.jpg
0.486829	f494a7d0490a4576b87288a0ff0ee2b8	Pulp test selection chart for different clinical situations in primary teeth.	PMC9145630	medicina-58-00665-g002.jpg
0.459089	bc71bb72300a4c33898c56e55854a302	Pulp test selection chart for different clinical situations in immature permanent teeth.	PMC9145630	medicina-58-00665-g003.jpg
0.41332	502bf005d87a43b785f192f6da04ecba	Flowchart showing the exclusion and inclusion criteria of studies analyzed.	PMC9145646	microorganisms-10-00900-g001.jpg
0.477855	b13a349f5d8447f3a48a1e50413d9b13	The geographical distribution of studies that did genomic characterization of influenza type-A viruses (H1N1, H1N1pdm09, and H3N2) sampled in Africa. Each country is highlighted based on the absolute number of studies that analyzed sequences of influenza viruses collected from that country. For each country, the study count also includes any study that included at least one sequence from that country in their virus clade classification using the European Center for Disease Control (ECDC) guidelines [27]. Abbreviations: CAR = Central African Republic. Countries not shown: Cape Verde (n = 1), Reunion (n = 3), Seychelles (n = 4), Mauritania (n = 1), Mauritius (n = 10), and Mayotte (n = 1).	PMC9145646	microorganisms-10-00900-g002.jpg
0.469858	69ccbef9c09e4405ba0a589d850bb035	Temporal and geographical distribution of genetic clades of seasonal H1N1 virus strains that circulated in Africa between 2001 and 2009. Details on the characteristic genomic markers (amino acid substitutions in the HA1 proteins) for each clade are described in Table S8.	PMC9145646	microorganisms-10-00900-g003.jpg
0.414148	211c8715363f48efaf0f10d43d490ee0	Temporal and geographical distribution of genetic clades of pandemic H1N1pdm09 (2009–2010) and seasonal H1N1pdm09 (2011 onwards) virus strains that circulated in Africa between 2009 and 2018. Abbreviations: Burkina Faso (BurkF), Cameroon (Cam), Cape Verde (CapeV), Central African Republic (CAR), Ivory Coast (IvoryC), Madagascar (Madg), Mauritania (Mauritn), Mozambique (Mozab), South Africa (SA), Tanzania (Tanz), and A/Madrid/SO8171/2010(H1N1)-like clade (Madrid). Details on the characteristic genomic markers (amino acid substitutions in the HA1 proteins) for each clade are described in Table S9.	PMC9145646	microorganisms-10-00900-g004.jpg
0.391897	4f87e0459e4e4f2ab6e22bc0a01abb36	Temporal and geographical distribution of genetic clades of seasonal H3N2 virus strains that circulated in Africa between 2003 and 2018. Abbreviations: Burkina Faso (BurkF), Cameroon (Cam), Cape Verde (CapeV), Central African Republic (CAR), Ivory Coast (IvoryC), Madagascar (Madg), Mozambique (Mozab), South Africa (SA), Tanzania (Tanz). A/Brisbane/10/2007(H3N2)-like clade (Brisbane), A/Fujian/411/2002(H3N2)-like clade (Fujian), A/Perth/16/2009(H3N2)-like clade (Perth), A/Victoria/208/2009(H3N2-like clade (Victoria), and A/Wellington/1/2004(H3N2)-like clade (Wellington). Details on the characteristic genomic markers (amino acid substitutions in the HA1 proteins) for each clade are described in Table S11.	PMC9145646	microorganisms-10-00900-g005.jpg
0.431623	ac15b16fe6914be09c73a36d72181c40	Study flow diagram of participants in focus groups.	PMC9145650	sensors-22-03621-g001.jpg
0.543138	847ae12176d94019847e9a3010c7109e	Wing planform shapes for different aspect ratios and non-dimensional radial centroid locations.	PMC9145969	insects-13-00459-g001.jpg
0.462297	b3c5feebcb2742619c921e91a9eea2a4	Employed wing kinematics waveforms for flapping and pitching.	PMC9145969	insects-13-00459-g002.jpg
0.474918	12b109e4f9044192b7eaa07c0dfcfcbc	Computational domain and mesh setup. (a) Domain and boundary definitions; (b) mesh distribution near the wing surface; note that extra refinement was applied at both the wing’s leading- and trailing-edges.	PMC9145969	insects-13-00459-g003.jpg
0.4737	7bbc5428afe84097977711f07e297801	Mesh and time step convergence results. Negligible difference between cases is evident.	PMC9145969	insects-13-00459-g004.jpg
0.409113	87d8cd2a412d44a5b2021e3d777dff7a	Flow evolution at different time instances for the baseline case. (a) Complete flow structure on the wing surface. (b) Flow structure at different spanwise locations. Colour map represents kinematic pressure on the wing surface. For clarity of visualisations, the wing view angle is kept constant, and thus is not reflective of the wing’s instantaneous angle of attack.	PMC9145969	insects-13-00459-g005.jpg
0.465231	9eb866b6015047f9bf2c3ee08eaa44a8	(a) Fruit fly wing planform shape employed within the validation study. (b) Comparison of the lift coefficients from the current simulation set-up against experimental (from Dickinson et al. [5]) and numerical (from Erzincanli and Sahin [44], Kweon and Choi [43], and Sun and Tang [29]) results for advanced, symmetric, and delayed pitching kinematic cases.	PMC9145969	insects-13-00459-g006.jpg
0.430548	e109c36529d54f209a341f3b689a36d5	Time histories of the lift and drag coefficients for different aspect ratios. The non-dimensional radial centroid location is set to 0.5 and the wing root offset to zero.	PMC9145969	insects-13-00459-g007.jpg
0.432145	47a27be5ecb84a3c914fafa87a166582	Flow structures at different time instances for the different aspect ratio cases. (a) Flow structure near mid-stroke (t^ = 4.8), (b) Sectional vortical structure and surface pressure field near the beginning, near the middle, and at the end of the half-stroke.	PMC9145969	insects-13-00459-g008.jpg
0.46638	ff040fd9abe14de4b4413ddb0b962c1b	Time histories of the lift and drag coefficients for different radial centroid locations and three different aspect ratios. Wing root offset is set to zero in this demonstration.	PMC9145969	insects-13-00459-g009.jpg
0.396107	f0200cd18b6949229a15b201d913d24c	Flow structures near mid half-stroke (t^ = 4.8) for radial centroid location values of 0.4 and 0.6 at different aspect ratios.	PMC9145969	insects-13-00459-g010.jpg
0.445231	e8f10d2516544cacb35de1812584f243	Sectional vortical structures and surface pressure fields near the beginning, near the middle, and at end of half-stroke for r^1 = 0.4 and 0.6 cases. (a) AR = 1.5, (b) AR = 3, (c) AR = 7.5.	PMC9145969	insects-13-00459-g011.jpg
0.472469	a348115f74dd439794a1ddfc71d5bf91	Time histories of the lift and drag coefficients for the different wing root offset cases at three aspect ratios.	PMC9145969	insects-13-00459-g012.jpg
0.469293	bdf8ef872e7d4cfeb76d8c58fe0891e1	Flow structures near mid half-stroke (t^ = 4.8) for r^R = 1 and 3 cases at different aspect ratios.	PMC9145969	insects-13-00459-g013.jpg
0.405022	979aed70cc564f9c853074b7332d6e37	Sectional vortical structures and surface pressure fields near the beginning, near the middle, and at the end of the half-stroke for r^R = 1 and 3 cases. (a) AR = 1.5, (b) AR = 3, (c) AR = 7.5.	PMC9145969	insects-13-00459-g014.jpg
0.440066	45f721d96e2a436994d618b61c3ced76	Average lift and drag coefficients as well as aerodynamic efficiency (measured in terms of the proposed power factor) variations against: (a) aspect ratio for different radial centroid locations, and (b) radial centroid locations for different aspect ratios.	PMC9145969	insects-13-00459-g015.jpg
0.400274	35a2d26e48ce4b87b65c57147878c09a	Average lift and drag coefficients as well as aerodynamic efficiency (measured in terms of the proposed power factor) variations against: (a) aspect ratio for different wing root offsets, and (b) wing root offset for different aspect ratios.	PMC9145969	insects-13-00459-g016.jpg
0.401762	210aec57a7a144a7b943f0ace0d05ddb	The structure of polymanuronic acid.	PMC9145981	marinedrugs-20-00289-g001.jpg
0.436612	11138a78326147eb90c7a3147397cc5e	Separation and purification of PM. (a) Elution curve (210 nm) of PM on the Q-Sepharose ion column; (b) phenol–sulfuric acid method monitoring diagram of PM.	PMC9145981	marinedrugs-20-00289-g002.jpg
0.568766	70ab7e04463a4e9dbfbcda0f6e29569a	Results of high-performance liquid chromatography of PM. Elution curve (210 nm) of PM on TSK-gel G4000 PWxl type column.	PMC9145981	marinedrugs-20-00289-g003.jpg
0.429014	f40338af9a174f1387daa6bb407ccaf5	Result of FITC-PM after agarose electrophoresis. Lanes A and B, FITC-PM; lane C, FITC.	PMC9145981	marinedrugs-20-00289-g004.jpg
0.465765	5498ea93001d4f35b3265dba3ca5beb4	Electropherograms of FITC-PM after incubation at different pH values for 24 h. pH: Lanes A, 2; Lanes B, 4; Lanes C, 6; Lanes D, 7; Lanes E, 8; Lanes F, 10; Lanes G, 12; Lanes H, FITC.	PMC9145981	marinedrugs-20-00289-g005.jpg
0.469061	98c3fae26df1404b81369ca7a8181864	The standard curves for FITC-PM in blood and tissues. (A): Heart; (B): Lung; (C): Liver; (D): Kidney; (E): Spleen; (F): Blood.	PMC9145981	marinedrugs-20-00289-g006.jpg
0.464169	287c423c235e4a59b6a6bf7bc33bc3d8	Concentrations of FITC-PM in each tissue sample at different times (mean ± SD, n = 6). (A): Heart; (B): Liver; (C): Spleen; (D): Lung; (E): Kidney; (F): Blood.	PMC9145981	marinedrugs-20-00289-g007.jpg
0.420548	f698c94d2c554aac97ca8cd488f7e8c9	Structure of botulinum neurotoxin A2 cell-binding domain. (A) Crystal structure of HC/A2 (pale green). (B) Crystal structure of HC/A2 in complex with GD1a (HC/A2:GD1a). (Molecule B is displayed in orange, and molecule A in magenta.) (C) Electron density map (2Fo-Fc) of GD1a contoured to 1 σ level. (D) Opening of the R1269-T1277 loop upon binding, and associated flip of F1278. The difference in Cα distance between R1269 and T1277 of molecule A and B is highlighted by a solid and dotted arrow, respectively. (E) Hydrophobic pocket formed by F1117, F1252, and F1278 that binds GD1a (ball and stick). Dashed lines indicate unmodelled regions.	PMC9146395	toxins-14-00356-g001.jpg
0.41675	1af8c822faea483f9bd76074ab99136d	Ligplot+ representation of HC/A2:GD1a interactions. Hydrogen bonding interactions are represented by a dotted line. The cyan sphere indicates a water-molecule-mediated interaction. The first glucose was not modelled due to weak electron density, 2 & 4 = galactose, 3 = N-acetylgalactosamine 5 & 6 = sialic acid.	PMC9146395	toxins-14-00356-g002.jpg
0.416546	522a25e64a2143729d7d55b197d5dc33	Structural comparison of HC/A2 and HC/A2:GD1a. (A) Superimposition of Cα atoms of HC/A2 (pale green) and HC/A2:GD1a (orange). The ganglioside binding site (GBS) is highlighted by the box. (B) Residues comprising the GBS before (pale green) and after binding to GD1a (orange).	PMC9146395	toxins-14-00356-g003.jpg
0.453199	fcf13730d20f4361af020464dbfb506e	Structural comparison of HC/A2 and HC/A2:SV2C. (A) Global superimposition of Cα atoms of HC/A2 (pale green) and HC/A2:SV2C (purple; PDB: 5MOY). (B) Residues of the HC/A2 SV2C binding site, indicating the position of key residues (sticks) prior to binding. (C) Residues of the HC/A2 SV2C binding interface, indicating the position of key residues (sticks) after binding.	PMC9146395	toxins-14-00356-g004.jpg
0.414402	a98621a3ee384b0cb31e7e8aeea7f9f3	Hinge motion between the HCN and HCC subdomain. Superimposition of the HCC subdomain of HC/A2 alone (pale green) with HC/A2 in complex with GD1a (orange) (A) or SV2C (purple; PDB: 5MOY) (B) indicates the presence of a hinge motion between the HCC and HCN subdomains.	PMC9146395	toxins-14-00356-g005.jpg
0.420958	52c6fcd047eb4a42ac1fdf4131eefd6d	Lys 1236-X-Cys 1280 Bridge. (A) 2Fo-Fc electron density (contoured to 1 σ) was observed between C1280 and K1236 of HC/A2 when bound to GD1a (HC/A2:GD1a) (A) and alone (HC/A2) (B), which indicated the presence of a Lys-X-Cys bridge. When bound to SV2C, however, one structure (PDB: 6ES1) showed the formation of a disulphide bond between C1280 and C1235 (C) and another (PDB: 5MOY) showed no electron density between these two residues (D).	PMC9146395	toxins-14-00356-g006.jpg
0.464219	20342374ba5d4fcf93f0824c5b3beb85	Analysis of the Lys 1236-X-Cys 1280 bridge in HC/A2 (present structure). (A) The 2Fo-Fc map (contoured at 1 σ level) of Lys-X-Cys modelled as Lys-O-Cys; the B-factors for each atom across the bridge are displayed. (B) The 2Fo-Fc map (contoured at 1 σ level) of Lys-X-Cys modelled as Lys-CH2-Cys; the B-factors for each across the bridge are displayed. (C) Omit map for Lys 1236 and Cys 1280 side chains, contoured at 3 σ level.	PMC9146395	toxins-14-00356-g007.jpg
0.400262	caec6577fb0e4fa1ae65baef7f4194cd	Conformational changes associated with the Lys-X-Cys bridge. Comparison of the structure of the 1220–1240 β-hairpin of HC/A2 alone (B), in complex with GD1a (A), and bound to SV2C ((C), PDB: 5MOY; and (D), PDB: 6ES1). The 1224–1236 loop is highlighted by the dotted circle, and the red arrow indicates the location of the bridging interaction (either Lys-X-Cys or Cys-Cys).	PMC9146395	toxins-14-00356-g008.jpg
0.454498	c9a2025536014e4fb4663ff32ed62206	Framework of our proposed approach.	PMC9146538	sensors-22-03760-g001.jpg
0.436365	31d2bd0682f248d9ad8236d9870b62c7	Example of a genuine face and corresponding print and replay attacks in grey-scale and BS.	PMC9146538	sensors-22-03760-g002.jpg
0.460588	3d9580da5191404fa868690da2f14e07	Samples from the CASIA FASD database.	PMC9146538	sensors-22-03760-g003.jpg
0.434903	e73970e2266c44cdbc00e540ca827e89	Examples of real accesses and attacks in different scenarios.	PMC9146538	sensors-22-03760-g004.jpg
0.398318	a3468f1c0dae435795b4e96b63f64664	Example images of genuine and attack presentation of one of the subjects in the MSU-MFSD database.	PMC9146538	sensors-22-03760-g005.jpg
0.410307	94a9ef8871d94756881259281c37c720	Effect of quality and spoofing media on the performance on the CASIA-FASD. (a) Quality and (b) spoofing media.	PMC9146538	sensors-22-03760-g006.jpg
0.454248	1715118213c24fb3b67c3ed0f0e8adc6	DET curve of the proposed approach on CASIA, MSU, and REPLAY databases.	PMC9146538	sensors-22-03760-g007.jpg
0.429677	ac79ac6c97984c8c813458d10c60948f	Experimental design. Animal model and inclusion criteria for 56 Wistar male rats (Rattus norvegicus): adults of 90 days old, weight of approximately ± 250 g; experimental model of bone defect in calvaria, exposure of parietal bones; surgical procedure: fabrication of a 5 mm diameter bone defect with a trephine drill; defect filled with biomaterial BCP (G1/B and G3/B + PBM); defect filled with biomaterial BCP and heterologous fibrin biopolymer (G2/BFB and G4/BFB + PBM); underlying soft tissue repositioned and sutured. A1: illustration of post-immediate photobiomodulation (PBM) therapy, followed by 3x per week until the corresponding euthanasia period for the G3/B + PBM and G4/BFB + PBM groups. Experimental periods were 14 and 42 days, with 7 animals/group/period.	PMC9146558	polymers-14-02075-g001.jpg
0.531555	8e4c85e95ad440558ed8883733b8d05b	(a) FEG-SEM micrographs obtained for the BCP sample (yellow arrows shows porous structure). The inset reveals the aspect almost spherical particles. (b) EDS spectrum of the BCP sample.	PMC9146558	polymers-14-02075-g002.jpg
0.377647	440adf5c56d84f699746ece91816a27f	(a) SEM image and EDS mapping showing the (b) oxygen, (c) calcium, and (d) phosphor distribution of the BCP sample.	PMC9146558	polymers-14-02075-g003.jpg
0.387595	522dd9f2c9a2462098be7288d13d8c53	X-ray diffraction patterns of the BCP samples (75% hydroxyapatite−25% TCP).	PMC9146558	polymers-14-02075-g004.jpg
0.386641	a2a659a7778147f8b9404f18b69b54cd	Two-dimensional (2D) reconstructed microtomographic images in transaxial and coronal sections of the bone defects in rat calvaria at 14 and 42 days, respectively. Defect filled with biomaterial (G1/B), biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB), biomaterial and PBM (G3/B + PBM), and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). Bone formation (blue arrow) and biomaterial particles (red arrow).	PMC9146558	polymers-14-02075-g005.jpg
0.409171	65358d2761734a9aa08259dee24ae841	Panoramic histological views at 14 (A) and 42 (B) days in the cranial defects filled with biomaterial (G1/B), biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB), biomaterial and PBM (G3/B + PBM), and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). Immature trabecular formation (asterisk) occurring at the edge of the defect (dashed line) and overlying the dura mater surface. Biomaterial particles (B) permeating the reaction connective tissue (red arrow). The transition from bone maturation to mineralized tissue (triangle), with primary bone areas (asterisk) and biomaterial particles in densely fibrous connective tissue (red arrow). HE; original magnification × 4; bar = 2 mm.	PMC9146558	polymers-14-02075-g006.jpg
0.504479	30113908e0864409afd85152d292531e	Details of the evolution of the bone repair process of the cranial defects at 14 days filled with biomaterial (G1/B), biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB), biomaterial and PBM (G3/B + PBM), and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). The deposition of the osteoid matrix (asterisk) from the edges of the defect (b), particles of the biomaterial (B) interspersed with densely cellular reactive connective tissue (RT) and vascular budding (V). HE and Masson Trichrome; original magnification × 10; bar = 500 µm and insert, magnified images × 40; bar = 100 µm.	PMC9146558	polymers-14-02075-g007.jpg
0.478336	c67fdf78c94041248d5489899d1b1e82	Details of the evolution of the bone repair process of the cranial defects at 42 days filled with biomaterial (G1/B), biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB), biomaterial and PBM (G3/B + PBM), and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). Mature lamellar tissue (triangle) was restricted to the edge of the defect (b) and areas of immature bone trabeculae (asterisk) in the fibrous connective tissue (CT). Biomaterial particles (B) surrounded by thicker collagen fibers, with a fibrous interface between the particles and newly formed bone (arrow). HE and Masson Trichrome; original magnification × 10; bar = 500 µm and insert, images magnified × 40; bar = 100 µm.	PMC9146558	polymers-14-02075-g008.jpg
0.433724	7ea1ea4b4a0145fcb7e0e4a20ef62f53	Histological sections of the edge (A’,A”) and center (B’,B”) of the bone defect of rat calvaria stained by Picrosirius-red under polarized light at 14 and 42 days ((A,B), respectively). Biomaterial (G1/B); biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB); biomaterial and PBM (G3/B + PBM); and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). RGB green-yellow-red colors. Mature bone, type I collagen fibers: yellowish-green color; immature bone, type III collagen fibers: reddish color. Dashed line = edge of remaining bone; B = synthetic biomaterial particles (dark background); asterisk = collagen fibers in advanced maturation phase. Original magnification × 10, scale bar 200 µm.	PMC9146558	polymers-14-02075-g009.jpg
0.409796	5e1212cd4eb343499569a395504cc282	Percentage of new bone formation, biomaterial, and non-mineralized tissue in the experimental groups at 14 days. The different letters (A ≠ B) indicate a statistically significant difference (p < 0.05).	PMC9146558	polymers-14-02075-g010.jpg
0.403898	9718551e602147debd0e2c3714c6619d	Percentage of new bone formation, biomaterial, and non-mineralized tissue in the experimental groups at 42 days. The different letters (A ≠ B) indicate a statistically significant difference (p < 0.05).	PMC9146558	polymers-14-02075-g011.jpg
0.44302	33d631258d9e472592a8deab3965adb5	Percentage of new bone formation, biomaterial, and non-mineralized tissue in each experimental group in the two experimental periods (14 vs. 42 days). The different letters (A ≠ B) indicate a statistically significant difference (p < 0.05).	PMC9146558	polymers-14-02075-g012.jpg
0.425	529d5efcc70948819bae79e2ff6a0191	Multiple amino acid sequence alignment of ADRV 12L with its homologs in iridoviruses and FEN1 of Xenopus tropicalis and human. CMTV, common midwife toad virus; EHNV, epizootic hematopoietic necrosis virus; ATV, Ambystoma tigrinum virus; RGV, Rana grylio virus; FV3, frog virus 3; SGIV, Singapore grouper iridovirus; ISKNV, infection spleen and kidney necrosis virus; LCDV-C: lymphocystis disease virus isolated from China. The GenBank accession numbers of these proteins are shown in Table S2. The black shaded regions indicate completely conserved residues. The conserved putative active sites (aspartic acid, D; glutamic acid, E) are marked with triangles at the bottom. The predicted α-helices (blue helical lines) and β-sheets (blue arrows) of ADRV 12L are indicated above the sequence. The α-helices (gray helical lines) and β-sheets (gray arrows) of human FEN1 are indicated below the sequence. The predicted helical clamp motif and H3TH motif are indicated with red boxes. The sequence identity between ADRV 12L and other proteins is shown at the end.	PMC9146916	viruses-14-00908-g001.jpg
0.437153	8e8c29ba695f4adda7c97dda71944c4c	Temporal expression pattern of the 12L gene and protein in ADRV infected cells. (A,B) Mock or ADRV infected cells were collected at the indicated time points and analyzed by RT-PCR (A) and Western blotting (B), respectively. (C) Western blot analysis of ADRV 12L expression in the presence or absence of Ara-C. Detection of 85L and MCP expression was used as control.	PMC9146916	viruses-14-00908-g002a.jpg
0.385243	04520bd0c4e24f61b6e358052cff3f17	Analysis of the co-localization between ADRV 12L and nascent DNA or ADRV 85L. (A) Mock or ADRV infected cells were labeled with EdU at indicated time points, and then serially stained with Alexa Fluor 488 azide, anti-12L antibody, Alexa Fluor 546 conjugated goat anti-mouse IgG, and Hoechst 33342. EdU labeled nascent DNA was presented in green color. ADRV 12L was presented in red color. (B) Mock or ADRV infected cells were fixed and serially stained with anti-12L antibody (mouse), anti-85L antibody (Rabbit), Alexa Fluor 488 conjugated goat anti-mouse IgG, Alexa Fluor 546 conjugated goat anti-Rabbit IgG, and Hoechst 33342. ADRV 12L was presented in green color and 85L in red color. The visible Hoechst-stained viral factories were indicated by white arrows. Bar = 10 μm.	PMC9146916	viruses-14-00908-g003a.jpg
0.461382	8a2a4cda6ff247e7948ca1d8dec73685	Construction of 12L deleted recombinant virus ADRV-Δ12L. (A) Schematic diagram of ADRV-Δ12L structure. The EGFP gene driven by the virus P50 promoter replaced the coding region of 12L. (B) Light and fluorescence micrographs of ADRV-Δ12L infected cells. The green color overlapped with viral plaques. (C) PCR analysis using primers for 12L and P50-EGFP. The 12L was only detected in wild type ADRV and P50-EGFP was only detected in ADRV-Δ12L. (D) Western blot analysis of ADRV-Δ12L and ADRV infected cells. The 12L band was not detected in ADRV-Δ12L infected cells. β-actin was used as an internal control.	PMC9146916	viruses-14-00908-g004a.jpg
0.448384	3b4ffaeea1b64f9c8b2fba06d414f7ee	Luc-HR assay. (A) Schematic diagram of the viral P18 promoter driving plasmids. The plasmid P18-lucT(1–2103) containing the full length of the P18 promoter, firefly luciferase gene, and SV40 terminator has a size of 2103 bp. The other plasmids were constructed based on the plasmid, and their contained regions are shown in parentheses. (B) Relative luciferase activity. The cells were infected with ADRV or ADRV-Δ12L for 6 h, and then transfected with different plasmid combinations, respectively. A plasmid containing P18 driving Renilla luciferase was transfected simultaneously as an internal control. The detected firefly luciferase activity was normalized to the Renilla luciferase activity in each group. In the present figure, the firefly luciferase activity in the ADRV-Δ12L infected and lucT(734–2103) + pUC19 transfected group was set as 1. Experiments were conducted in triplicate and analyzed using Student’s t-test. Significant differences are marked with * (p < 0.05).	PMC9146916	viruses-14-00908-g005a.jpg
0.433866	ec548f6f910946c7b27662c754ac1530	Luciferase-based DSBR assay. (A) Schematic diagram of the viral P18 promoter driving plasmids and other constructs. DSB1 had a nick (indicated by a black arrow) between P18 and the ATG of the firefly luciferase gene. DSB2 lacked the C-terminal of the firefly luciferase gene. (B) Relative luciferase activity. The cells were infected with ADRV or ADRV-Δ12L for 6 h, and then transfected with different DNA combinations, respectively. A plasmid containing P18 driving Renilla luciferase was transfected simultaneously as an internal control. The detected firefly luciferase activity was normalized to the Renilla luciferase activity in each group. In the present figure, the firefly luciferase activity in the ADRV infected and DSB2 + pUC19 transfected group was set as 1. Experiments were conducted in triplicate and analyzed using Student’s t-test. Significant differences are marked with * (p < 0.05).	PMC9146916	viruses-14-00908-g006.jpg
0.420287	e784951dd34a46dfa5430804839bbbb8	Virus infection was impaired with the deletion of 12L. (A) Plaque assay of ADRV and ADRV-Δ12L. (B) One-step growth curves of ADRV and ADRV-Δ12L in GSTC cells. Cells were infected with ADRV or ADRV-Δ12L at an MOI of 1 and then harvested at different times for titration. The average titers of three independent experiments are shown as logTCID50 ± SD.	PMC9146916	viruses-14-00908-g007a.jpg
0.463322	d50994927f4f46c6a9a99bc572d861c0	(a–c), Cell lines were prophylactically treated with probenecid 24 h prior to infection of RSV A2, RSV B1, or Memphis-37. Probenecid prophylaxis significantly (** p < 0.0001) inhibited the virus replication in Vero E6 cells, HEp-2 cells, and NHBE cells compared to control (DMSO only). Viral titers were determined by plaque assay which has a limit of detection of 1 × 10² PFU/mL. The IC50 and IC90 values are shown in Table 1. (d–f), Cell lines were treated with probenecid 24h after infection of RSV A2, RSV B1, or Memphis-37. Treatment significantly (** p < 0.0001) inhibited the virus replication in Vero E6 cells, HEp-2 cells, and NHBE cells compared to control (DMSO only). Viral titers were determined by plaque assay. The IC50 and IC90 values are shown in Table 1. For RSV B1 the IC90 values are not available as the virus was not reduced by 90%.	PMC9147281	viruses-14-00912-g001.jpg
0.447279	83fbb22fe89c4fd2ba1ac82c3f2f6551	Lung virus titers from female BALB/c mice. The mice received 2 mg/kg or 200 mg/kg probenecid 24 h before infection (prophylaxis) or 24 h pi (treatment). The mice were i.n. infected with 106 PFU of RSV A2. On days 3, 5, and 7 pi, the lungs were harvested, and virus titers were determined by plaque assay having a limit of detection of 1 × 10² PFU/mL. There is significant (**** p < 0.0001) reduction in lung viral titers with all probenecid treatments compared to control (PBS).	PMC9147281	viruses-14-00912-g002.jpg
0.416976	2d8e54b1a6064013a979ba20a5dfbb77	Lung virus titers from male BALB/c mice. The mice received 2 mg/kg or 200 mg/kg probenecid 24 h before infection (prophylaxis) or 24 h pi (treatment). The mice were i.n. infected with 106 PFU of RSV A2. On days 3, 5, and 7 pi, the lungs were harvested, and virus titers were determined by plaque assay having a limit of detection of 1 × 10² PFU/mL. There is significant (**** p < 0.0001) reduction in lung viral titers with all probenecid treatments compared to control (PBS).	PMC9147281	viruses-14-00912-g003.jpg
0.448974	55dd319f27ba4367893e999655fbda14	Structure of the AO system for LSCM.	PMC9147356	sensors-22-03755-g001.jpg
0.459155	9c77bdb04cb044b5b12d4b3e808f8834	Flow of SPGD algorithm for LSCM.	PMC9147356	sensors-22-03755-g002.jpg
0.44347	ff6f8a7ccb8a4cf7af5a1335c0ea5bb2	Photograph of the AO imaging system for LSCM.	PMC9147356	sensors-22-03755-g003.jpg
0.510207	02c10579b77e484db106e68834025cf6	Image of the leech specimen at −0.0415 mm in the z-axis direction.	PMC9147356	sensors-22-03755-g004.jpg
0.375822	71e1ef0cb0f24c92a6f5725c5edff8cb	Initial imaging result of the specimen at −0.0815 mm in the z-axis direction, and the grayscale variance value is about 6.0.	PMC9147356	sensors-22-03755-g005.jpg
0.464513	3f691891bdb046b690b51fb1c642f3e1	Imaging result after correction with 100 iterations of the fixed coefficient SPGD algorithm, and the grayscale variance value is about 8.9.	PMC9147356	sensors-22-03755-g006.jpg
0.449427	94c40acec5114fbdbbe85e0a1ddf4a78	Metric convergence curve of the fixed coefficient SPGD algorithm.	PMC9147356	sensors-22-03755-g007.jpg
0.509359	3587299e781b4cebaa517301c52e5d34	Imaging result after correction with 100 iterations of the adaptive coefficient SPGD algorithm, and the grayscale variance value is about 9.0.	PMC9147356	sensors-22-03755-g008.jpg
0.42528	17ccc6dd637d451ba34d2880c4311d95	Metric convergence curve of the adaptive coefficient SPGD algorithm.	PMC9147356	sensors-22-03755-g009.jpg
0.378717	85d3cfe38f864aac927ca2891a6661d0	Curve of the update gain coefficient of the SPGD algorithm applied to the LSCM system.	PMC9147356	sensors-22-03755-g010.jpg
0.423072	59ced9d281d64c42a594a4874bc8d53b	Different shapes of the deformable mirror: (a) shape of the deformable mirror controlled by the fixed coefficient SPGD algorithm; (b) shape of the deformable mirror controlled by the adaptive coefficient SPGD algorithm; (c) difference phase map of two shapes of the deformable mirror.	PMC9147356	sensors-22-03755-g011.jpg
0.474558	24707bbb62b0438ab0ff58a2e28d8155	Grayscale graphs at the yellow line of the original image and two images after aberration correction.	PMC9147356	sensors-22-03755-g012.jpg
0.427996	f4a63167fa2744be9a04e8fb4ae80b97	A combination of radiographic and image processing techniques for welding defect detection conducted by Faramarzi et al. [18].	PMC9147555	materials-15-03697-g001.jpg
0.406206	1e12222d50734f90b4414da202903cb8	A comparison between dye penetrant testing (the dashed section in (A) depicts the area examined with ultrasound techniques shown in (B)) (A), conventional ultrasonic (B) and X-ray radiographic technologies (C) carried out by Seow et al. [20].	PMC9147555	materials-15-03697-g002.jpg
0.426991	e5cdb446f9354af0b5ad4ffba2d0dde5	Inspected WAAM component. D1, D2 and D3 represent the welding defects [25].	PMC9147555	materials-15-03697-g003.jpg
0.550278	ac0492e3bd484ff2be751b5cb60916b2	Intentionally introduced defects (D1, D2 and D3 in Figure 3) are detected by means of TFM image of the component using ultrasonic longitudinal waves [25].	PMC9147555	materials-15-03697-g004.jpg
0.446082	e6b61579e0ee41e082da9b4ce2f9ed21	Laser ultrasonic inspection system [48].	PMC9147555	materials-15-03697-g005.jpg
0.458858	ee3059897f1949b293ec9d814dde5230	Thermoelastic (a) and ablative (b) phenomena in UL [57].	PMC9147555	materials-15-03697-g006.jpg

0.496072

007d95aedfd141af97b75c26bc5075d5

(Left): release profile of polypill design MiniTab; modified basket apparatus, 1000 mL 0.1 N HCl, 50 rpm, 37.0 ± 0.5 °C, x ± s; n = 3. (Right): Image of MiniTab: red: PDM-PVA, blue: LD/BZ-EVA.

PMC9145509

pharmaceutics-14-00931-g011.jpg

0.480261

a17c0e6780fb4aaeb04e564a244d3058

(Left): release profile of MiniHCwC 1 (top) and 2 (bottom); modified basket apparatus, 1000 mL 0.1 N HCl, 50 rpm, 37.0 ± 0.5 °C, x ± s; n = 3. (Right): Image of MiniHCwC1 + 2: red: PDM-PVA, blue: LD/BZ-EVA.

PMC9145509

pharmaceutics-14-00931-g012.jpg

0.413065

9a2375644c74404e9e8059b8f8720bf1

Floating properties of MiniHCwC in 300 mL 0.1 N HCl, 37 ± 0.5 °C.

PMC9145509

pharmaceutics-14-00931-g013.jpg

0.451122

3be173f2e03446f89bcba67caeb87245

Food intake frequency before sleeve gastrectomy (SG) and after 10 months follow-up. Change in the frequency of meat and fish consumption in females (A), and males (B); change in the frequency of bread and crackers consumption in females (C), and males (D); change in the frequency of dairy products and fats consumption in females (E), and males (F).

PMC9145557

nutrients-14-02060-g001a.jpg

0.445988

82ac54bdbfcf4b04aad76ce989fab04f

Food intake frequency before sleeve gastrectomy (SG) and after 10 months follow-up. Change in the frequency of sweet and snacks in females (A), and males (B); change in the frequency of vegetables and fruits consumption in females (C), and males (D); change in the frequency of soft drinks consumption in females (E), and males (F).

PMC9145557

nutrients-14-02060-g002a.jpg

0.451895

015e16f63e8647c1821022f57f6ef136

Change in taste, desire, and enjoyment 12 months after SG in females.

PMC9145557

nutrients-14-02060-g003.jpg

0.435457

cd8c0b6c080f41a988d04e0cf079b097

Change in taste, desire, and enjoyment 12 months after SG in males.

PMC9145557

nutrients-14-02060-g004.jpg

0.451911

0f73555558b048f59594f7d4bc6aeda5

(a) Schematic illustration of a GO-coated SOI nanowire with a monolayer GO film. (bi) Schematic illustration of the cross section and (bii) the corresponding TE mode profile of the GO-coated SOI nanowire in (a). (c) Microscope image of an SOI chip uniformly coated with a monolayer GO film.

PMC9145626

micromachines-13-00756-g001.jpg

0.395909

23c9f0a878b14cae95609224115970f5

Experimental setup for measuring loss and SPM of GO-coated SOI nanowires. CW laser: continuous-wave laser. FPL: fiber pulsed laser. PC: polarization controller. VOA: variable optical attenuator. OPM: optical power meter. DUT: device under test. CCD: charged-coupled device. OSA: optical spectrum analyzer.

PMC9145626

micromachines-13-00756-g002.jpg

0.455014

435bad2a7b5b44d59e5c240215c8dfe8

(a) Measured excess insertion loss (EIL) of GO-coated SOI nanowires versus input power of optical pulses. (b) Excess propagation loss induced by the SA (∆SA) versus peak power of input optical pulses. In (a,b), the results for uncoated (N = 0) and hybrid SOI nanowires coated with one and two layers of GO (N = 1, 2) are shown for comparison. The data points depict the average of measurements on three samples, and the error bars illustrate the variations among the different samples.

PMC9145626

micromachines-13-00756-g003.jpg

0.406055

5427cf61bd0e4a1091c85c6702c1a7ae

SPM experimental results. (a) Normalized spectra of optical pulses before and after propagation through the GO-coated SOI nanowires with one and two layers of GO at an input peak power of ∼160 W. (b,c) Optical spectra measured at different input peak powers for the hybrid waveguides with one and two layers of GO, respectively. (d) BFs of the measured output spectra versus input peak power for the hybrid waveguides with one and two layers of GO. In (a–d), the corresponding results for the uncoated SOI nanowires (N = 0) are also shown for comparison.

PMC9145626

micromachines-13-00756-g004.jpg

0.390844

7c58b594309749eeaadd9cc7dad3e050

(a) BFs of femtosecond optical pulses versus GO film length (Lc) for the hybrid waveguides with one and two layers of GO. The peak power is ~160 W. (b) BFs of picosecond optical pulses versus GO film length (Lc) for the hybrid waveguides with one and two layers of GO. The peak power is ~13 W. In (a,b), the corresponding results for uncoated waveguides (N = 0) are also shown for comparison.

PMC9145626

micromachines-13-00756-g005.jpg

0.45998

9dcdedd26a5142eea8e1d5d744927dfb

(a) Effective interaction length (Leff) versus waveguide length (L) for GO-coated SOI nanowires uniformly coated with one and two layers of GO. (b) FOM2 versus waveguide length (L) for hybrid waveguides uniformly coated with one and two layers of GO. In (a,b), the corresponding results for uncoated waveguides (N = 0) are also shown for comparison.

PMC9145626

micromachines-13-00756-g006.jpg

0.519159

283eda8f04a84d4b8aceeb63b0c5bbe6

Classification of pulp testing methods.

PMC9145630

medicina-58-00665-g001.jpg

0.486829

f494a7d0490a4576b87288a0ff0ee2b8

Pulp test selection chart for different clinical situations in primary teeth.

PMC9145630

medicina-58-00665-g002.jpg

0.459089

bc71bb72300a4c33898c56e55854a302

Pulp test selection chart for different clinical situations in immature permanent teeth.

PMC9145630

medicina-58-00665-g003.jpg

0.41332

502bf005d87a43b785f192f6da04ecba

Flowchart showing the exclusion and inclusion criteria of studies analyzed.

PMC9145646

microorganisms-10-00900-g001.jpg

0.477855

b13a349f5d8447f3a48a1e50413d9b13

The geographical distribution of studies that did genomic characterization of influenza type-A viruses (H1N1, H1N1pdm09, and H3N2) sampled in Africa. Each country is highlighted based on the absolute number of studies that analyzed sequences of influenza viruses collected from that country. For each country, the study count also includes any study that included at least one sequence from that country in their virus clade classification using the European Center for Disease Control (ECDC) guidelines [27]. Abbreviations: CAR = Central African Republic. Countries not shown: Cape Verde (n = 1), Reunion (n = 3), Seychelles (n = 4), Mauritania (n = 1), Mauritius (n = 10), and Mayotte (n = 1).

PMC9145646

microorganisms-10-00900-g002.jpg

0.469858

69ccbef9c09e4405ba0a589d850bb035

Temporal and geographical distribution of genetic clades of seasonal H1N1 virus strains that circulated in Africa between 2001 and 2009. Details on the characteristic genomic markers (amino acid substitutions in the HA1 proteins) for each clade are described in Table S8.

PMC9145646

microorganisms-10-00900-g003.jpg

0.414148

211c8715363f48efaf0f10d43d490ee0

Temporal and geographical distribution of genetic clades of pandemic H1N1pdm09 (2009–2010) and seasonal H1N1pdm09 (2011 onwards) virus strains that circulated in Africa between 2009 and 2018. Abbreviations: Burkina Faso (BurkF), Cameroon (Cam), Cape Verde (CapeV), Central African Republic (CAR), Ivory Coast (IvoryC), Madagascar (Madg), Mauritania (Mauritn), Mozambique (Mozab), South Africa (SA), Tanzania (Tanz), and A/Madrid/SO8171/2010(H1N1)-like clade (Madrid). Details on the characteristic genomic markers (amino acid substitutions in the HA1 proteins) for each clade are described in Table S9.

PMC9145646

microorganisms-10-00900-g004.jpg

0.391897

4f87e0459e4e4f2ab6e22bc0a01abb36

Temporal and geographical distribution of genetic clades of seasonal H3N2 virus strains that circulated in Africa between 2003 and 2018. Abbreviations: Burkina Faso (BurkF), Cameroon (Cam), Cape Verde (CapeV), Central African Republic (CAR), Ivory Coast (IvoryC), Madagascar (Madg), Mozambique (Mozab), South Africa (SA), Tanzania (Tanz). A/Brisbane/10/2007(H3N2)-like clade (Brisbane), A/Fujian/411/2002(H3N2)-like clade (Fujian), A/Perth/16/2009(H3N2)-like clade (Perth), A/Victoria/208/2009(H3N2-like clade (Victoria), and A/Wellington/1/2004(H3N2)-like clade (Wellington). Details on the characteristic genomic markers (amino acid substitutions in the HA1 proteins) for each clade are described in Table S11.

PMC9145646

microorganisms-10-00900-g005.jpg

0.431623

ac15b16fe6914be09c73a36d72181c40

Study flow diagram of participants in focus groups.

PMC9145650

sensors-22-03621-g001.jpg

0.543138

847ae12176d94019847e9a3010c7109e

Wing planform shapes for different aspect ratios and non-dimensional radial centroid locations.

PMC9145969

insects-13-00459-g001.jpg

0.462297

b3c5feebcb2742619c921e91a9eea2a4

Employed wing kinematics waveforms for flapping and pitching.

PMC9145969

insects-13-00459-g002.jpg

0.474918

12b109e4f9044192b7eaa07c0dfcfcbc

Computational domain and mesh setup. (a) Domain and boundary definitions; (b) mesh distribution near the wing surface; note that extra refinement was applied at both the wing’s leading- and trailing-edges.

PMC9145969

insects-13-00459-g003.jpg

0.4737

7bbc5428afe84097977711f07e297801

Mesh and time step convergence results. Negligible difference between cases is evident.

PMC9145969

insects-13-00459-g004.jpg

0.409113

87d8cd2a412d44a5b2021e3d777dff7a

Flow evolution at different time instances for the baseline case. (a) Complete flow structure on the wing surface. (b) Flow structure at different spanwise locations. Colour map represents kinematic pressure on the wing surface. For clarity of visualisations, the wing view angle is kept constant, and thus is not reflective of the wing’s instantaneous angle of attack.

PMC9145969

insects-13-00459-g005.jpg

0.465231

9eb866b6015047f9bf2c3ee08eaa44a8

(a) Fruit fly wing planform shape employed within the validation study. (b) Comparison of the lift coefficients from the current simulation set-up against experimental (from Dickinson et al. [5]) and numerical (from Erzincanli and Sahin [44], Kweon and Choi [43], and Sun and Tang [29]) results for advanced, symmetric, and delayed pitching kinematic cases.

PMC9145969

insects-13-00459-g006.jpg

0.430548

e109c36529d54f209a341f3b689a36d5

Time histories of the lift and drag coefficients for different aspect ratios. The non-dimensional radial centroid location is set to 0.5 and the wing root offset to zero.

PMC9145969

insects-13-00459-g007.jpg

0.432145

47a27be5ecb84a3c914fafa87a166582

Flow structures at different time instances for the different aspect ratio cases. (a) Flow structure near mid-stroke (t^ = 4.8), (b) Sectional vortical structure and surface pressure field near the beginning, near the middle, and at the end of the half-stroke.

PMC9145969

insects-13-00459-g008.jpg

0.46638

ff040fd9abe14de4b4413ddb0b962c1b

Time histories of the lift and drag coefficients for different radial centroid locations and three different aspect ratios. Wing root offset is set to zero in this demonstration.

PMC9145969

insects-13-00459-g009.jpg

0.396107

f0200cd18b6949229a15b201d913d24c

Flow structures near mid half-stroke (t^ = 4.8) for radial centroid location values of 0.4 and 0.6 at different aspect ratios.

PMC9145969

insects-13-00459-g010.jpg

0.445231

e8f10d2516544cacb35de1812584f243

Sectional vortical structures and surface pressure fields near the beginning, near the middle, and at end of half-stroke for r^1 = 0.4 and 0.6 cases. (a) AR = 1.5, (b) AR = 3, (c) AR = 7.5.

PMC9145969

insects-13-00459-g011.jpg

0.472469

a348115f74dd439794a1ddfc71d5bf91

Time histories of the lift and drag coefficients for the different wing root offset cases at three aspect ratios.

PMC9145969

insects-13-00459-g012.jpg

0.469293

bdf8ef872e7d4cfeb76d8c58fe0891e1

Flow structures near mid half-stroke (t^ = 4.8) for r^R = 1 and 3 cases at different aspect ratios.

PMC9145969

insects-13-00459-g013.jpg

0.405022

979aed70cc564f9c853074b7332d6e37

Sectional vortical structures and surface pressure fields near the beginning, near the middle, and at the end of the half-stroke for r^R = 1 and 3 cases. (a) AR = 1.5, (b) AR = 3, (c) AR = 7.5.

PMC9145969

insects-13-00459-g014.jpg

0.440066

45f721d96e2a436994d618b61c3ced76

Average lift and drag coefficients as well as aerodynamic efficiency (measured in terms of the proposed power factor) variations against: (a) aspect ratio for different radial centroid locations, and (b) radial centroid locations for different aspect ratios.

PMC9145969

insects-13-00459-g015.jpg

0.400274

35a2d26e48ce4b87b65c57147878c09a

Average lift and drag coefficients as well as aerodynamic efficiency (measured in terms of the proposed power factor) variations against: (a) aspect ratio for different wing root offsets, and (b) wing root offset for different aspect ratios.

PMC9145969

insects-13-00459-g016.jpg

0.401762

210aec57a7a144a7b943f0ace0d05ddb

The structure of polymanuronic acid.

PMC9145981

marinedrugs-20-00289-g001.jpg

0.436612

11138a78326147eb90c7a3147397cc5e

Separation and purification of PM. (a) Elution curve (210 nm) of PM on the Q-Sepharose ion column; (b) phenol–sulfuric acid method monitoring diagram of PM.

PMC9145981

marinedrugs-20-00289-g002.jpg

0.568766

70ab7e04463a4e9dbfbcda0f6e29569a

Results of high-performance liquid chromatography of PM. Elution curve (210 nm) of PM on TSK-gel G4000 PWxl type column.

PMC9145981

marinedrugs-20-00289-g003.jpg

0.429014

f40338af9a174f1387daa6bb407ccaf5

Result of FITC-PM after agarose electrophoresis. Lanes A and B, FITC-PM; lane C, FITC.

PMC9145981

marinedrugs-20-00289-g004.jpg

0.465765

5498ea93001d4f35b3265dba3ca5beb4

Electropherograms of FITC-PM after incubation at different pH values for 24 h. pH: Lanes A, 2; Lanes B, 4; Lanes C, 6; Lanes D, 7; Lanes E, 8; Lanes F, 10; Lanes G, 12; Lanes H, FITC.

PMC9145981

marinedrugs-20-00289-g005.jpg

0.469061

98c3fae26df1404b81369ca7a8181864

The standard curves for FITC-PM in blood and tissues. (A): Heart; (B): Lung; (C): Liver; (D): Kidney; (E): Spleen; (F): Blood.

PMC9145981

marinedrugs-20-00289-g006.jpg

0.464169

287c423c235e4a59b6a6bf7bc33bc3d8

Concentrations of FITC-PM in each tissue sample at different times (mean ± SD, n = 6). (A): Heart; (B): Liver; (C): Spleen; (D): Lung; (E): Kidney; (F): Blood.

PMC9145981

marinedrugs-20-00289-g007.jpg

0.420548

f698c94d2c554aac97ca8cd488f7e8c9

Structure of botulinum neurotoxin A2 cell-binding domain. (A) Crystal structure of HC/A2 (pale green). (B) Crystal structure of HC/A2 in complex with GD1a (HC/A2:GD1a). (Molecule B is displayed in orange, and molecule A in magenta.) (C) Electron density map (2Fo-Fc) of GD1a contoured to 1 σ level. (D) Opening of the R1269-T1277 loop upon binding, and associated flip of F1278. The difference in Cα distance between R1269 and T1277 of molecule A and B is highlighted by a solid and dotted arrow, respectively. (E) Hydrophobic pocket formed by F1117, F1252, and F1278 that binds GD1a (ball and stick). Dashed lines indicate unmodelled regions.

PMC9146395

toxins-14-00356-g001.jpg

0.41675

1af8c822faea483f9bd76074ab99136d

Ligplot+ representation of HC/A2:GD1a interactions. Hydrogen bonding interactions are represented by a dotted line. The cyan sphere indicates a water-molecule-mediated interaction. The first glucose was not modelled due to weak electron density, 2 & 4 = galactose, 3 = N-acetylgalactosamine 5 & 6 = sialic acid.

PMC9146395

toxins-14-00356-g002.jpg

0.416546

522a25e64a2143729d7d55b197d5dc33

Structural comparison of HC/A2 and HC/A2:GD1a. (A) Superimposition of Cα atoms of HC/A2 (pale green) and HC/A2:GD1a (orange). The ganglioside binding site (GBS) is highlighted by the box. (B) Residues comprising the GBS before (pale green) and after binding to GD1a (orange).

PMC9146395

toxins-14-00356-g003.jpg

0.453199

fcf13730d20f4361af020464dbfb506e

Structural comparison of HC/A2 and HC/A2:SV2C. (A) Global superimposition of Cα atoms of HC/A2 (pale green) and HC/A2:SV2C (purple; PDB: 5MOY). (B) Residues of the HC/A2 SV2C binding site, indicating the position of key residues (sticks) prior to binding. (C) Residues of the HC/A2 SV2C binding interface, indicating the position of key residues (sticks) after binding.

PMC9146395

toxins-14-00356-g004.jpg

0.414402

a98621a3ee384b0cb31e7e8aeea7f9f3

Hinge motion between the HCN and HCC subdomain. Superimposition of the HCC subdomain of HC/A2 alone (pale green) with HC/A2 in complex with GD1a (orange) (A) or SV2C (purple; PDB: 5MOY) (B) indicates the presence of a hinge motion between the HCC and HCN subdomains.

PMC9146395

toxins-14-00356-g005.jpg

0.420958

52c6fcd047eb4a42ac1fdf4131eefd6d

Lys 1236-X-Cys 1280 Bridge. (A) 2Fo-Fc electron density (contoured to 1 σ) was observed between C1280 and K1236 of HC/A2 when bound to GD1a (HC/A2:GD1a) (A) and alone (HC/A2) (B), which indicated the presence of a Lys-X-Cys bridge. When bound to SV2C, however, one structure (PDB: 6ES1) showed the formation of a disulphide bond between C1280 and C1235 (C) and another (PDB: 5MOY) showed no electron density between these two residues (D).

PMC9146395

toxins-14-00356-g006.jpg

0.464219

20342374ba5d4fcf93f0824c5b3beb85

Analysis of the Lys 1236-X-Cys 1280 bridge in HC/A2 (present structure). (A) The 2Fo-Fc map (contoured at 1 σ level) of Lys-X-Cys modelled as Lys-O-Cys; the B-factors for each atom across the bridge are displayed. (B) The 2Fo-Fc map (contoured at 1 σ level) of Lys-X-Cys modelled as Lys-CH2-Cys; the B-factors for each across the bridge are displayed. (C) Omit map for Lys 1236 and Cys 1280 side chains, contoured at 3 σ level.

PMC9146395

toxins-14-00356-g007.jpg

0.400262

caec6577fb0e4fa1ae65baef7f4194cd

Conformational changes associated with the Lys-X-Cys bridge. Comparison of the structure of the 1220–1240 β-hairpin of HC/A2 alone (B), in complex with GD1a (A), and bound to SV2C ((C), PDB: 5MOY; and (D), PDB: 6ES1). The 1224–1236 loop is highlighted by the dotted circle, and the red arrow indicates the location of the bridging interaction (either Lys-X-Cys or Cys-Cys).

PMC9146395

toxins-14-00356-g008.jpg

0.454498

c9a2025536014e4fb4663ff32ed62206

Framework of our proposed approach.

PMC9146538

sensors-22-03760-g001.jpg

0.436365

31d2bd0682f248d9ad8236d9870b62c7

Example of a genuine face and corresponding print and replay attacks in grey-scale and BS.

PMC9146538

sensors-22-03760-g002.jpg

0.460588

3d9580da5191404fa868690da2f14e07

Samples from the CASIA FASD database.

PMC9146538

sensors-22-03760-g003.jpg

0.434903

e73970e2266c44cdbc00e540ca827e89

Examples of real accesses and attacks in different scenarios.

PMC9146538

sensors-22-03760-g004.jpg

0.398318

a3468f1c0dae435795b4e96b63f64664

Example images of genuine and attack presentation of one of the subjects in the MSU-MFSD database.

PMC9146538

sensors-22-03760-g005.jpg

0.410307

94a9ef8871d94756881259281c37c720

Effect of quality and spoofing media on the performance on the CASIA-FASD. (a) Quality and (b) spoofing media.

PMC9146538

sensors-22-03760-g006.jpg

0.454248

1715118213c24fb3b67c3ed0f0e8adc6

DET curve of the proposed approach on CASIA, MSU, and REPLAY databases.

PMC9146538

sensors-22-03760-g007.jpg

0.429677

ac79ac6c97984c8c813458d10c60948f

Experimental design. Animal model and inclusion criteria for 56 Wistar male rats (Rattus norvegicus): adults of 90 days old, weight of approximately ± 250 g; experimental model of bone defect in calvaria, exposure of parietal bones; surgical procedure: fabrication of a 5 mm diameter bone defect with a trephine drill; defect filled with biomaterial BCP (G1/B and G3/B + PBM); defect filled with biomaterial BCP and heterologous fibrin biopolymer (G2/BFB and G4/BFB + PBM); underlying soft tissue repositioned and sutured. A1: illustration of post-immediate photobiomodulation (PBM) therapy, followed by 3x per week until the corresponding euthanasia period for the G3/B + PBM and G4/BFB + PBM groups. Experimental periods were 14 and 42 days, with 7 animals/group/period.

PMC9146558

polymers-14-02075-g001.jpg

0.531555

8e4c85e95ad440558ed8883733b8d05b

(a) FEG-SEM micrographs obtained for the BCP sample (yellow arrows shows porous structure). The inset reveals the aspect almost spherical particles. (b) EDS spectrum of the BCP sample.

PMC9146558

polymers-14-02075-g002.jpg

0.377647

440adf5c56d84f699746ece91816a27f

(a) SEM image and EDS mapping showing the (b) oxygen, (c) calcium, and (d) phosphor distribution of the BCP sample.

PMC9146558

polymers-14-02075-g003.jpg

0.387595

522dd9f2c9a2462098be7288d13d8c53

X-ray diffraction patterns of the BCP samples (75% hydroxyapatite−25% TCP).

PMC9146558

polymers-14-02075-g004.jpg

0.386641

a2a659a7778147f8b9404f18b69b54cd

Two-dimensional (2D) reconstructed microtomographic images in transaxial and coronal sections of the bone defects in rat calvaria at 14 and 42 days, respectively. Defect filled with biomaterial (G1/B), biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB), biomaterial and PBM (G3/B + PBM), and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). Bone formation (blue arrow) and biomaterial particles (red arrow).

PMC9146558

polymers-14-02075-g005.jpg

0.409171

65358d2761734a9aa08259dee24ae841

Panoramic histological views at 14 (A) and 42 (B) days in the cranial defects filled with biomaterial (G1/B), biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB), biomaterial and PBM (G3/B + PBM), and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). Immature trabecular formation (asterisk) occurring at the edge of the defect (dashed line) and overlying the dura mater surface. Biomaterial particles (B) permeating the reaction connective tissue (red arrow). The transition from bone maturation to mineralized tissue (triangle), with primary bone areas (asterisk) and biomaterial particles in densely fibrous connective tissue (red arrow). HE; original magnification × 4; bar = 2 mm.

PMC9146558

polymers-14-02075-g006.jpg

0.504479

30113908e0864409afd85152d292531e

Details of the evolution of the bone repair process of the cranial defects at 14 days filled with biomaterial (G1/B), biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB), biomaterial and PBM (G3/B + PBM), and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). The deposition of the osteoid matrix (asterisk) from the edges of the defect (b), particles of the biomaterial (B) interspersed with densely cellular reactive connective tissue (RT) and vascular budding (V). HE and Masson Trichrome; original magnification × 10; bar = 500 µm and insert, magnified images × 40; bar = 100 µm.

PMC9146558

polymers-14-02075-g007.jpg

0.478336

c67fdf78c94041248d5489899d1b1e82

Details of the evolution of the bone repair process of the cranial defects at 42 days filled with biomaterial (G1/B), biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB), biomaterial and PBM (G3/B + PBM), and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). Mature lamellar tissue (triangle) was restricted to the edge of the defect (b) and areas of immature bone trabeculae (asterisk) in the fibrous connective tissue (CT). Biomaterial particles (B) surrounded by thicker collagen fibers, with a fibrous interface between the particles and newly formed bone (arrow). HE and Masson Trichrome; original magnification × 10; bar = 500 µm and insert, images magnified × 40; bar = 100 µm.

PMC9146558

polymers-14-02075-g008.jpg

0.433724

7ea1ea4b4a0145fcb7e0e4a20ef62f53

Histological sections of the edge (A’,A”) and center (B’,B”) of the bone defect of rat calvaria stained by Picrosirius-red under polarized light at 14 and 42 days ((A,B), respectively). Biomaterial (G1/B); biocomplex consisting of biomaterial plus heterologous fibrin biopolymer (G2/BFB); biomaterial and PBM (G3/B + PBM); and biocomplex consisting of biomaterial plus heterologous fibrin biopolymer and photobiomodulation with low-level laser therapy (G4/BFB + PBM). RGB green-yellow-red colors. Mature bone, type I collagen fibers: yellowish-green color; immature bone, type III collagen fibers: reddish color. Dashed line = edge of remaining bone; B = synthetic biomaterial particles (dark background); asterisk = collagen fibers in advanced maturation phase. Original magnification × 10, scale bar 200 µm.

PMC9146558

polymers-14-02075-g009.jpg

0.409796

5e1212cd4eb343499569a395504cc282

Percentage of new bone formation, biomaterial, and non-mineralized tissue in the experimental groups at 14 days. The different letters (A ≠ B) indicate a statistically significant difference (p < 0.05).

PMC9146558

polymers-14-02075-g010.jpg

0.403898

9718551e602147debd0e2c3714c6619d

Percentage of new bone formation, biomaterial, and non-mineralized tissue in the experimental groups at 42 days. The different letters (A ≠ B) indicate a statistically significant difference (p < 0.05).

PMC9146558

polymers-14-02075-g011.jpg

0.44302

33d631258d9e472592a8deab3965adb5

Percentage of new bone formation, biomaterial, and non-mineralized tissue in each experimental group in the two experimental periods (14 vs. 42 days). The different letters (A ≠ B) indicate a statistically significant difference (p < 0.05).

PMC9146558

polymers-14-02075-g012.jpg

0.425

529d5efcc70948819bae79e2ff6a0191

Multiple amino acid sequence alignment of ADRV 12L with its homologs in iridoviruses and FEN1 of Xenopus tropicalis and human. CMTV, common midwife toad virus; EHNV, epizootic hematopoietic necrosis virus; ATV, Ambystoma tigrinum virus; RGV, Rana grylio virus; FV3, frog virus 3; SGIV, Singapore grouper iridovirus; ISKNV, infection spleen and kidney necrosis virus; LCDV-C: lymphocystis disease virus isolated from China. The GenBank accession numbers of these proteins are shown in Table S2. The black shaded regions indicate completely conserved residues. The conserved putative active sites (aspartic acid, D; glutamic acid, E) are marked with triangles at the bottom. The predicted α-helices (blue helical lines) and β-sheets (blue arrows) of ADRV 12L are indicated above the sequence. The α-helices (gray helical lines) and β-sheets (gray arrows) of human FEN1 are indicated below the sequence. The predicted helical clamp motif and H3TH motif are indicated with red boxes. The sequence identity between ADRV 12L and other proteins is shown at the end.

PMC9146916

viruses-14-00908-g001.jpg

0.437153

8e8c29ba695f4adda7c97dda71944c4c

Temporal expression pattern of the 12L gene and protein in ADRV infected cells. (A,B) Mock or ADRV infected cells were collected at the indicated time points and analyzed by RT-PCR (A) and Western blotting (B), respectively. (C) Western blot analysis of ADRV 12L expression in the presence or absence of Ara-C. Detection of 85L and MCP expression was used as control.

PMC9146916

viruses-14-00908-g002a.jpg

0.385243

04520bd0c4e24f61b6e358052cff3f17

Analysis of the co-localization between ADRV 12L and nascent DNA or ADRV 85L. (A) Mock or ADRV infected cells were labeled with EdU at indicated time points, and then serially stained with Alexa Fluor 488 azide, anti-12L antibody, Alexa Fluor 546 conjugated goat anti-mouse IgG, and Hoechst 33342. EdU labeled nascent DNA was presented in green color. ADRV 12L was presented in red color. (B) Mock or ADRV infected cells were fixed and serially stained with anti-12L antibody (mouse), anti-85L antibody (Rabbit), Alexa Fluor 488 conjugated goat anti-mouse IgG, Alexa Fluor 546 conjugated goat anti-Rabbit IgG, and Hoechst 33342. ADRV 12L was presented in green color and 85L in red color. The visible Hoechst-stained viral factories were indicated by white arrows. Bar = 10 μm.

PMC9146916

viruses-14-00908-g003a.jpg

0.461382

8a2a4cda6ff247e7948ca1d8dec73685

Construction of 12L deleted recombinant virus ADRV-Δ12L. (A) Schematic diagram of ADRV-Δ12L structure. The EGFP gene driven by the virus P50 promoter replaced the coding region of 12L. (B) Light and fluorescence micrographs of ADRV-Δ12L infected cells. The green color overlapped with viral plaques. (C) PCR analysis using primers for 12L and P50-EGFP. The 12L was only detected in wild type ADRV and P50-EGFP was only detected in ADRV-Δ12L. (D) Western blot analysis of ADRV-Δ12L and ADRV infected cells. The 12L band was not detected in ADRV-Δ12L infected cells. β-actin was used as an internal control.

PMC9146916

viruses-14-00908-g004a.jpg

0.448384

3b4ffaeea1b64f9c8b2fba06d414f7ee

Luc-HR assay. (A) Schematic diagram of the viral P18 promoter driving plasmids. The plasmid P18-lucT(1–2103) containing the full length of the P18 promoter, firefly luciferase gene, and SV40 terminator has a size of 2103 bp. The other plasmids were constructed based on the plasmid, and their contained regions are shown in parentheses. (B) Relative luciferase activity. The cells were infected with ADRV or ADRV-Δ12L for 6 h, and then transfected with different plasmid combinations, respectively. A plasmid containing P18 driving Renilla luciferase was transfected simultaneously as an internal control. The detected firefly luciferase activity was normalized to the Renilla luciferase activity in each group. In the present figure, the firefly luciferase activity in the ADRV-Δ12L infected and lucT(734–2103) + pUC19 transfected group was set as 1. Experiments were conducted in triplicate and analyzed using Student’s t-test. Significant differences are marked with * (p < 0.05).

PMC9146916

viruses-14-00908-g005a.jpg

0.433866

ec548f6f910946c7b27662c754ac1530

Luciferase-based DSBR assay. (A) Schematic diagram of the viral P18 promoter driving plasmids and other constructs. DSB1 had a nick (indicated by a black arrow) between P18 and the ATG of the firefly luciferase gene. DSB2 lacked the C-terminal of the firefly luciferase gene. (B) Relative luciferase activity. The cells were infected with ADRV or ADRV-Δ12L for 6 h, and then transfected with different DNA combinations, respectively. A plasmid containing P18 driving Renilla luciferase was transfected simultaneously as an internal control. The detected firefly luciferase activity was normalized to the Renilla luciferase activity in each group. In the present figure, the firefly luciferase activity in the ADRV infected and DSB2 + pUC19 transfected group was set as 1. Experiments were conducted in triplicate and analyzed using Student’s t-test. Significant differences are marked with * (p < 0.05).

PMC9146916

viruses-14-00908-g006.jpg

0.420287

e784951dd34a46dfa5430804839bbbb8

Virus infection was impaired with the deletion of 12L. (A) Plaque assay of ADRV and ADRV-Δ12L. (B) One-step growth curves of ADRV and ADRV-Δ12L in GSTC cells. Cells were infected with ADRV or ADRV-Δ12L at an MOI of 1 and then harvested at different times for titration. The average titers of three independent experiments are shown as logTCID50 ± SD.

PMC9146916

viruses-14-00908-g007a.jpg

0.463322

d50994927f4f46c6a9a99bc572d861c0

(a–c), Cell lines were prophylactically treated with probenecid 24 h prior to infection of RSV A2, RSV B1, or Memphis-37. Probenecid prophylaxis significantly (**** p < 0.0001) inhibited the virus replication in Vero E6 cells, HEp-2 cells, and NHBE cells compared to control (DMSO only). Viral titers were determined by plaque assay which has a limit of detection of 1 × 10² PFU/mL. The IC50 and IC90 values are shown in Table 1. (d–f), Cell lines were treated with probenecid 24h after infection of RSV A2, RSV B1, or Memphis-37. Treatment significantly (**** p < 0.0001) inhibited the virus replication in Vero E6 cells, HEp-2 cells, and NHBE cells compared to control (DMSO only). Viral titers were determined by plaque assay. The IC50 and IC90 values are shown in Table 1. For RSV B1 the IC90 values are not available as the virus was not reduced by 90%.

PMC9147281

viruses-14-00912-g001.jpg

0.447279

83fbb22fe89c4fd2ba1ac82c3f2f6551

Lung virus titers from female BALB/c mice. The mice received 2 mg/kg or 200 mg/kg probenecid 24 h before infection (prophylaxis) or 24 h pi (treatment). The mice were i.n. infected with 106 PFU of RSV A2. On days 3, 5, and 7 pi, the lungs were harvested, and virus titers were determined by plaque assay having a limit of detection of 1 × 10² PFU/mL. There is significant (**** p < 0.0001) reduction in lung viral titers with all probenecid treatments compared to control (PBS).

PMC9147281

viruses-14-00912-g002.jpg

0.416976

2d8e54b1a6064013a979ba20a5dfbb77

Lung virus titers from male BALB/c mice. The mice received 2 mg/kg or 200 mg/kg probenecid 24 h before infection (prophylaxis) or 24 h pi (treatment). The mice were i.n. infected with 106 PFU of RSV A2. On days 3, 5, and 7 pi, the lungs were harvested, and virus titers were determined by plaque assay having a limit of detection of 1 × 10² PFU/mL. There is significant (**** p < 0.0001) reduction in lung viral titers with all probenecid treatments compared to control (PBS).

PMC9147281

viruses-14-00912-g003.jpg

0.448974

55dd319f27ba4367893e999655fbda14

Structure of the AO system for LSCM.

PMC9147356

sensors-22-03755-g001.jpg

0.459155

9c77bdb04cb044b5b12d4b3e808f8834

Flow of SPGD algorithm for LSCM.

PMC9147356

sensors-22-03755-g002.jpg

0.44347

ff6f8a7ccb8a4cf7af5a1335c0ea5bb2

Photograph of the AO imaging system for LSCM.

PMC9147356

sensors-22-03755-g003.jpg

0.510207

02c10579b77e484db106e68834025cf6

Image of the leech specimen at −0.0415 mm in the z-axis direction.

PMC9147356

sensors-22-03755-g004.jpg

0.375822

71e1ef0cb0f24c92a6f5725c5edff8cb

Initial imaging result of the specimen at −0.0815 mm in the z-axis direction, and the grayscale variance value is about 6.0.

PMC9147356

sensors-22-03755-g005.jpg

0.464513

3f691891bdb046b690b51fb1c642f3e1

Imaging result after correction with 100 iterations of the fixed coefficient SPGD algorithm, and the grayscale variance value is about 8.9.

PMC9147356

sensors-22-03755-g006.jpg

0.449427

94c40acec5114fbdbbe85e0a1ddf4a78

Metric convergence curve of the fixed coefficient SPGD algorithm.

PMC9147356

sensors-22-03755-g007.jpg

0.509359

3587299e781b4cebaa517301c52e5d34

Imaging result after correction with 100 iterations of the adaptive coefficient SPGD algorithm, and the grayscale variance value is about 9.0.

PMC9147356

sensors-22-03755-g008.jpg

0.42528

17ccc6dd637d451ba34d2880c4311d95

Metric convergence curve of the adaptive coefficient SPGD algorithm.

PMC9147356

sensors-22-03755-g009.jpg

0.378717

85d3cfe38f864aac927ca2891a6661d0

Curve of the update gain coefficient of the SPGD algorithm applied to the LSCM system.

PMC9147356

sensors-22-03755-g010.jpg

0.423072

59ced9d281d64c42a594a4874bc8d53b

Different shapes of the deformable mirror: (a) shape of the deformable mirror controlled by the fixed coefficient SPGD algorithm; (b) shape of the deformable mirror controlled by the adaptive coefficient SPGD algorithm; (c) difference phase map of two shapes of the deformable mirror.

PMC9147356

sensors-22-03755-g011.jpg

0.474558

24707bbb62b0438ab0ff58a2e28d8155

Grayscale graphs at the yellow line of the original image and two images after aberration correction.

PMC9147356

sensors-22-03755-g012.jpg

0.427996

f4a63167fa2744be9a04e8fb4ae80b97

A combination of radiographic and image processing techniques for welding defect detection conducted by Faramarzi et al. [18].

PMC9147555

materials-15-03697-g001.jpg

0.406206

1e12222d50734f90b4414da202903cb8

A comparison between dye penetrant testing (the dashed section in (A) depicts the area examined with ultrasound techniques shown in (B)) (A), conventional ultrasonic (B) and X-ray radiographic technologies (C) carried out by Seow et al. [20].

PMC9147555

materials-15-03697-g002.jpg

0.426991

e5cdb446f9354af0b5ad4ffba2d0dde5

Inspected WAAM component. D1, D2 and D3 represent the welding defects [25].

PMC9147555

materials-15-03697-g003.jpg

0.550278

ac0492e3bd484ff2be751b5cb60916b2

Intentionally introduced defects (D1, D2 and D3 in Figure 3) are detected by means of TFM image of the component using ultrasonic longitudinal waves [25].

PMC9147555

materials-15-03697-g004.jpg

0.446082

e6b61579e0ee41e082da9b4ce2f9ed21

Laser ultrasonic inspection system [48].

PMC9147555

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0.458858

ee3059897f1949b293ec9d814dde5230

Thermoelastic (a) and ablative (b) phenomena in UL [57].

PMC9147555

materials-15-03697-g006.jpg