dedup-isc-ft-v107-score
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0.53812 |
10a4c9f9a46d42adbed33c3eef64e618
|
Flowchart.
|
PMC9072350
|
41598_2022_11346_Fig1_HTML.jpg
|
0.400273 |
a3ca783117974fdd839cdf9aa569fcec
|
Wexner score and mode of delivery.
|
PMC9072350
|
41598_2022_11346_Fig2_HTML.jpg
|
0.495152 |
731dd2aad6a446c5adbf193d23919bc8
|
Temperature–time profile with three measurement stages: (i) 1st stage: sample mass determination (red segment), (ii) 2nd stage: sample melting and fast-quenching (green segment), and (iii) 3rd stage: re-heating of supercooled sample (blue segment). After cooling step #4 in 1st stage, the sample can be coated with silicon oil. In the heating step #5, the scanning rate, β, varied from 2000 K s−1 to 20 000 K s−1 [reprinted from ref. 24 with modifications].
|
PMC9073158
|
c9ra05730g-f1.jpg
|
0.424818 |
3eb5a73424cf4d9f9868d0a1791995fd
|
Extrapolated onset temperature of the melting peak of Gly–Gly, Gly–Ala, Ala–Gly, Ala–Ala and cyclo(Ala–Gly), as function of heating rate. The melting temperature at zero heating rate for Gly–Gly, Gly–Ala, Ala–Gly, Ala–Ala and cyclo(Ala–Gly) is TSL0Gly–Gly = (593 ± 7) K, TSL0Gly–Ala = (551 ± 7) K, TSL0Ala–Gly = (611 ± 7) K, TSL0Ala–Ala = (606 ± 7) K and TSL0cyclo(Ala–Gly) = (526 ± 7) K, respectively. The scanning rates used were 2000 K s−1 (circles), 4000 K s−1 (up-triangles), 5000 K s−1 (hexagonals), 6000 K s−1 (down-triangles), 8000 K s−1 (diamonds), 10 000 K s−1 (stars), 15 000 K s−1 (left-triangles) and 20 000 K s−1 (right-triangles). Solid symbols represent sample measurement without silicon oil, while empty symbols for sample measurement with silicon oil.
|
PMC9073158
|
c9ra05730g-f2.jpg
|
0.465893 |
9016e9ae2e424979acac66842dd3ad39
|
Enthalpy, ΔHSL0i, of Gly–Gly, Gly–Ala, Ala–Gly, Ala–Ala and cyclo(Ala–Gly) in respect to initial sample mass, m0, regardless of the scanning rates. The symbols used were as described in Fig. 2. The dashed line was linear fit through zero origin, where the slope denoted as ΔhSL0i. The scanning rates used were 2000 K s−1 (circles), 4000 K s−1 (up-triangles), 5000 K s−1 (hexagonals), 6000 K s−1 (down-triangles), 8000 K s−1 (diamonds), 10 000 K s−1 (stars). The melting enthalpy for Gly–Gly, Gly–Ala, Ala–Gly, Ala–Ala and cyclo(Ala–Gly) is ΔhSL0Gly–Gly = (40 ± 6) kJ mol−1, ΔhSL0Gly–Ala = (41 ± 5) kJ mol−1, ΔhSL0Ala–Gly = (52 ± 7) kJ mol−1, ΔhSL0Ala–Ala = (45 ± 7) kJ mol−1 and ΔhSL0cyclo(Ala–Gly) = (24 ± 4) kJ mol−1, respectively. The values are already given in the figures, same for Fig. 2.
|
PMC9073158
|
c9ra05730g-f3.jpg
|
0.413909 |
9b3db577b3df43fb842f999390755c7a
|
Specific heat capacity for Gly–Gly, Gly–Ala, Ala–Gly and Ala–Ala. The heat capacity of solid, cSp0i, of the dipeptides was measured with conventional DSC (dotted lines). The solid line denotes the glass transition step of ultra-fast quenched melted dipeptides without silicon oil. Both cSp0i and cLp0i (dashed lines) were linearly fitted to extrapolate to TSL0i. The heat capacity difference between liquid and solid phase were determined at glass transition temperature, ΔcSLp0i (TG0i) and at melting temperature, ΔcSLp0i (TSL0i). Gly–Gly: ΔcSLp0Gly–Gly (TG0Gly–Gly) = (84 ± 6) J mol−1 K−1 and ΔcSLp (TSL0Gly–Gly) = (51 ± 6) J mol−1 K−1; Gly–Ala: ΔcSLp0Gly–Ala (TG0Gly–Ala) = (91 ± 6) J mol−1 K−1 and ΔcSLp0Gly–Ala(TSL0Gly–Ala) = (55 ± 6) J mol−1 K−1; Ala–Gly: ΔcSLp0Ala–Gly (TG0Ala–Gly) = (82 ± 3) J mol−1 K−1 and ΔcSLp (TSL0Ala–Gly) = (57 ± 3) J mol−1 K−1; Ala–Ala: ΔcSLp0Ala–Ala (TG0Ala–Ala) = (84 ± 18) J mol−1 K−1 and ΔcSLp0Ala–Ala (TSL0Ala–Ala) = (62 ± 18) J mol−1 K−1. The solid squares depict specific heat capacity of solid Gly–Gly from literature.60 In order to avoid crystallization on cooling, higher scanning rates are required and might be able to achieved with ultra-fast scanning nanocalorimetry.61,62
|
PMC9073158
|
c9ra05730g-f4.jpg
|
0.424378 |
9219d77d18c54ce7be8e11acc89d7096
|
Experimental dipeptide solubility at pH = 7 in water as molality vs. temperature. Full symbols present data measured by photometric method; empty symbols by gravimetric method. Gly–Ala (squares + “x”-filled square38); Ala–Ala (up-triangles); Gly–Gly (circles);11 Ala–Gly (down-triangles) and cyclo(Ala–Gly) (diamonds). The experimentally determined values are given in Tables S5 and S6 (pH 7) and Tables S7 and S8 (pH at saturated solutions) in the ESI.†
|
PMC9073158
|
c9ra05730g-f5.jpg
|
0.505546 |
833e8b7543c84a76b3f358c9f7f527fe
|
Solubility in water. Bars: mean values of the photometric and gravimetric determined dipeptide solubility data at T = 298.15 K and pH = 7. Lines represent the corresponding amino-acid solubility at T = 298.15 K and pH = 7: solid line: Gly24 and dashed line: Ala.24
|
PMC9073158
|
c9ra05730g-f6.jpg
|
0.437879 |
77514dd80dbc43a49287f9528363d896
|
Influence of the difference of the heat capacities on the solubility behaviour for Gly–Gly (circles11) in water as molality vs. temperature. Lines represent PC-SAFT predictions with the parameters from Table 3 and FSC-measured melting properties from this work (Table 4). Dotted line: eqn (1) with ΔcSLp0i = 0, dotted-dashed line: eqn (1) with ΔcSLp0i = const. = 51 J mol−1 K−1, solid line: eqn (1) with eqn (2).
|
PMC9073158
|
c9ra05730g-f7.jpg
|
0.471477 |
6b79da6c897042f0a963d5efffe840f1
|
Influence of the activity coefficient on the solubility in molality in water expressed as difference between ideal and experimental solubility. Black (Ideal): calculated solubility at T = 298.15 K from eqn (1) based on the FSC-measured melting properties in experimental uncertainty assuming an ideal mixture γ = 1. Shaded (Exp.): mean value of the photometric and gravimetric determined solubility data at T = 298.15 K and pH = 7. Grey (PC-SAFT): calculated solubility at T = 298.15 K from eqn (1) based on the PC-SAFT used melting properties from Table 4 including the activity coefficient.
|
PMC9073158
|
c9ra05730g-f8.jpg
|
0.447584 |
ba96357a46864990a2c5bbe58a82fde8
|
Dipeptides solubility at pH = 7 in water as molality vs. temperature. Symbols represent experimental data. Solid symbols present measurements using photometric method; open symbols present measurements using gravimetric method. Gly–Ala (squares + "x" filled square38); Ala–Ala (up-triangles); Gly–Gly (circles11); Ala–Gly (down-triangles); cyclo(Ala–Gly) (diamonds). Lines represent PC-SAFT predictions with the parameters from Table 3 and FSC-measured melting properties from this work. Gly–Ala (solid line), Ala–Ala (dashed line), Gly–Gly (dashed-dotted line), Ala–Gly (dashed-double dotted line) and cyclo(Ala–Gly) (dotted line). The experimental determined values are given in Tables S5 and S6 (pH = 7) and Tables S7 and S8† (pH at saturated solutions).
|
PMC9073158
|
c9ra05730g-f9.jpg
|
0.442068 |
e71609a07ad34acfbcb53ff97be8a83a
|
Graphical example of Hill–Robertson effects. Hitchhiking effects associated with linkage to a deleterious mutation, known as background selection, may act to reduce variation, as purifying selection acting on the deleterious mutation (shown in red) may result in the elimination of linked variants. Similarly, hitchhiking effects associated with linkage to a beneficial mutation, known as a selective sweep, may also act to reduce variation, as positive selection acting on the beneficial mutation (shown in blue) may result in the fixation of linked variants.
|
PMC9073693
|
jkac055f1.jpg
|
0.440706 |
7dd7edd2d50748c78e8f9140aedce849
|
Comparison of within-host variation between M. canettii and MTBC. Mycobacterium canettii has both a greatly elevated mean and variance in genome-wide segregating sites relative to the MTBC.
|
PMC9073693
|
jkac055f2.jpg
|
0.472174 |
f81a9942d06f496cbee8cc5af068310c
|
Distribution of likelihoods across different values of ρ for empirical M. canettii. Distribution of likelihood for different population-scaled recombination rates, ρ, ranging from 0 to 100 obtained using LDhat (see Materials and Methods for details). The blue line indicates the maximum likelihood at ρ = 15.
|
PMC9073693
|
jkac055f3.jpg
|
0.447296 |
ba489e12750544278f4c0d026688e84a
|
Performance of LDhat under a variety of model violations. a) the per-site recombination rate (r) inferred from ρ estimated by LDhat deviates strongly from the true value of r = 7.2 × 10−11 (see solid black horizontal line) in most models. Indeed, the correct estimate is obtained only when using full population data (rather than consensus data) under either the standard Wright–Fisher (Base) model or a neutral bottleneck model (Base + Bn). Each point corresponds to a simulated replicate, with replicates binned according to their model along the x-axis. The point color corresponds to the ratio between the LDhat-inferred r and the true r (log-scaled to improve visualization). b) Similar to panel a, the relationship between ρ and θ deviates from the slope of r/μ (solid black line) for many of the simulated model violations (colors represent different models). Both the standard Wright–Fisher (Base) and the neutral bottleneck (Base + Bn) models largely conform to expectation when the full population data are used. However, the use of consensus sequences as well as the presence of either natural selection and/or progeny skew, can cause extreme deviations from the true value.
|
PMC9073693
|
jkac055f4.jpg
|
0.411413 |
5d86b5e17e474d769c840aecb02a6c95
|
Segregating sites in consensus sequences and source populations, from simulated replicates. The number of segregating sites observed within each consensus, full population, and subpopulation dataset—for 10 simulation replicates of the ‘Base’ model with the addition of a bottleneck, progeny skew, and presence of non-neutral mutations (Base + Bn + Ψ + DFE). The full populations are represented by 500 genomes, the subpopulations are represented by 17 subpopulations consisting of 25 individual genomes each, and the consensus sequences are called for each subpopulation from the 25 constituent individual genomes. The points are binned by simulation replicates.
|
PMC9073693
|
jkac055f5.jpg
|
0.500209 |
c2255122e30a45fd96c213c2d1c94ef6
|
PRISMA flow chart of the scoping review. Summary of evidence search and selection
|
PMC9074253
|
12935_2022_2603_Fig1_HTML.jpg
|
0.460159 |
5c1059800533442fa93690a704612558
|
Scamper diagram showing Mcl-1 expression in oral cavity cancers and association with various clinicopathological features
|
PMC9074253
|
12935_2022_2603_Fig2_HTML.jpg
|
0.493743 |
69d10752ca80458591ff235c76e87bdb
|
STRING protein–protein interaction (PPI) analyses. PPI network connectivity for proteins identified following the review. Nodes represent the proteins required for interaction. Edges represent the associations between the proteins. The STRING web resource (http://www.stringdb.org) was used in the prediction of the PPI (Protein–Protein Interaction) network whereby an interaction score of > 0.900 denoted a significant interactive relationship
|
PMC9074253
|
12935_2022_2603_Fig3_HTML.jpg
|
0.431577 |
357fd608ee3247159aec77a94a746a70
|
Tree modified from Figure 5 in Andrade et al. (2015) including the species covered in this study. Note that some of the internal relationships of the annelids are not yet well resolved, so this figure only gives an overview of the diversity covered within the group.
|
PMC9075518
|
fphys-13-817272-g001.jpg
|
0.508898 |
f8559cd915494f63902acf35be6293f9
|
Flow chart of identification and analysis of sHsp.
|
PMC9075518
|
fphys-13-817272-g002.jpg
|
0.402909 |
6fc466f3a44e4edbb7c9bbccb48482af
|
Representation of the structural topology of monomeric sHsps. ACD is the region delimited from the β2-strand to the β9-strand. The β1-strand is localized in the N-terminal region. The β10-strand corresponds to a conserved motif in the C-terminal region. The fragment starting after the ACD and including the β10-strand has been named the C-terminal anchoring module (CAM). Residues that follow the CAM were defined as the C-terminal tail. The β6-strand and the β10-strand are not universally present in all sHsp (Poulain et al., 2010). The black arrows represent the β-strands and the red line, the link between two β-strands.
|
PMC9075518
|
fphys-13-817272-g003.jpg
|
0.438801 |
3fd0cad1d13a439fbeb2ecfe70b1bc0f
|
ML tree generated using the multiple sequence alignment of the ACD data set (A) Left, unrooted ML phylogenetic tree and clustering branching pattern of monomeric sHsps (shadowed clades) (B) Right, circular ML phylogenetic tree showing the location of the outgroups’ ACDs (shadowed labels), the colored connection lines between the ACDs belonging to the same dimeric protein, and the colored stripes (green, red and blue) marking the three big clades: Cluster A, B and C, respectively. Branch lengths are not displayed. More details can be found in File S2, including the results of the Bayesian phylogenetic study, the dendrograms of the analyzed clusters, and the node support information.
|
PMC9075518
|
fphys-13-817272-g004.jpg
|
0.406629 |
cccc130984fd4967943e045008dbff03
|
Clusters A1 and A2. Multiple sequence alignment visualized on a dendrogram obtained from the Bayesian tree, using the Zappo coloring scheme. The consensus sequence (at 50% conservation) and residue conservation were calculated by iTOL. On the left, the unrooted radial ML cladograms, in which each cluster is highlighted. The posterior probability values are included as percentages in the nodes.
|
PMC9075518
|
fphys-13-817272-g005.jpg
|
0.362226 |
b669af654cbf4d6b901c9962d3b755d6
|
Clusters B1, B2, and B3. Multiple sequence alignment visualized on a dendrogram obtained from the Bayesian tree, using the Zappo coloring scheme. The consensus sequence (at 50% conservation) and residue conservation were calculated by iTOL. On the left, the unrooted radial ML cladograms, in which each cluster is highlighted. The posterior probability values are included as percentages in the nodes.
|
PMC9075518
|
fphys-13-817272-g006.jpg
|
0.486062 |
b52e13c598974ee7b12f14db25ce4a45
|
Logo presentation using the WebLogo3 program (Crooks et al., 2004) for Clusters A and B. The height of each letter is proportional to its frequency. Amino acids are colored according to their chemical properties: acidic (D, E) in red, basic (K, R, H) in blue, polar (G, S, T, Y, C) in green, neutral (N, Q) in purple, and hydrophobic (A, V, L, I, p, W, F, M) in black. Logos for Clusters B2 and B3 are calculated without including the sequences from the outgroups (Supplementary File S2, Supplementary Figure S17-S19 include logos for Clusters B2 and B3 calculated including the outgroups, but the differences are not significant.).
|
PMC9075518
|
fphys-13-817272-g007.jpg
|
0.5317 |
cb79b38aa3e9423fab0df496ba071a3d
|
THP chelator (R = CH3) and its bifunctional chelator derivatives.
|
PMC9075519
|
c9ra07723e-f1.jpg
|
0.44185 |
901d277a140a4934b67cfab968e6574c
|
Concentrations of selected trace metals in 68Ga generator eluate measured by ICP-MS. Generator eluate (5 mL in 0.1 M HCl) was obtained from a single generator either 2 hours after a previous generator elution (sample set A, red circles, n = 9), or 1 day after a previous elution (sample set B, purple squares, n = 4). “Blank” eluent (0.1 M HCl solution from ABX Gmb) was also measured (yellow triangles, n = 10). These samples were collected within a period of 20 days, from a generator eluting 330–480 MBq. Error bars represent standard deviation of concentrations in the samples.
|
PMC9075519
|
c9ra07723e-f2.jpg
|
0.383321 |
8cdc1354ce3b429983b20c5305980515
|
Concentrations of Al, Ti, Fe and natGa in 68Ga eluate as a function of generator age. Two sets of eluate samples were collected from the same 68Ga E&Z generator, six months apart from each other. “Blank” eluent (0.1 M HCl solution from ABX Gmb) used in these two sets of samples was also measured. During this period, the generator was eluted 130 times. All eluates were sampled with a pre-elution window of 2 h. Error bars represent standard deviation of concentrations in the samples.
|
PMC9075519
|
c9ra07723e-f3.jpg
|
0.41308 |
2b677e0d29bb415ead650aa019f61558
|
Mean RCYs of [68Ga(THP)] in the presence of increasing concentrations of metal ions ((A): Al3+, Ti4+, Cr3+, Fe3+ and (B): Ni2+, Zn2+, natGa3+, Pb2+). The vertical dashed line indicates equimolar concentrations of chelator and metal ion (5 μM), and the horizontal dashed guide indicates 97% (n = 7) RCY, which is achieved in the absence of added metal ions. For most values, error bars representing standard deviation are smaller than the symbols. For a full list of mean RCY (n = 3) and standard deviation values see Table SI-4.†
|
PMC9075519
|
c9ra07723e-f4.jpg
|
0.475747 |
62932e1bffc14eeabf23f8d152c9d6e7
|
Mean RCYs of [68Ga(THP)] in the presence of either increasing concentrations of Fe3+ (green triangles) or ascorbate (166 mM) and increasing concentrations of Fe3+ (n = 5). The vertical dashed line indicates equimolar concentrations of chelator and metal ion (5 μM), and the horizontal dashed guide indicates 96 ± 0.4% (n = 6) RCY in the absence of spiked Fe3+. For most values, error bars representing standard deviation are smaller than the symbols.
|
PMC9075519
|
c9ra07723e-f5.jpg
|
0.559379 |
309a525cfaa5427ca549c5e20146010a
|
Regression lines, with 95% confidence intervals, for maternal (R
2
= 0.5813) and umbilical cord blood (R
2
= 0.7113) IgG seropositivity relative to the
infection-to-birth interval (weeks). Blue circles indicate percentages (Y axis) of mothers, while green dots represent percentages of umbilical cord blood testing positive for
anti-SARS-CoV-2 IgG for the indicated weeks between infection and birth (X axis). The regression lines differed significantly (comparison of fits: p < 0.0001,
F
= 8.958;
dfn
= 4,
dfd
= 340). Note the delayed response in seroconversion by one week between mothers and their offspring early after infection.
|
PMC9076216
|
10-1055-a-1768-0415-igf01.jpg
|
0.437445 |
7d79b7f619dc48318f749419f6aa303c
|
Scatter plot and regression line for logarithmic maternal and logarithmic umbilical cord IgG concentrations. Each dot represents a mother–child pair, both of whom tested
positive for anti-SARS-CoV-2 IgG antibodies (n = 68, ρ = 0.8042; p < 0.0001).
|
PMC9076216
|
10-1055-a-1768-0415-igf02.jpg
|
0.509014 |
f2b58ed0490e4d3fab9ae0bba4dcfbf6
|
Third-order cubic polynomial regression line for maternofetal anti-SARS-CoV-2 IgG antibody transfer ratios (c [umbilical cord blood IgG]/c [maternal blood IgG]) relative
to the infection-to-birth interval. Note that the ratios increase to more than 1 after six weeks from infection (R
2
= 0.2440).
|
PMC9076216
|
10-1055-a-1768-0415-igf03.jpg
|
0.467892 |
0e387dd096a0483482a876986d492624
|
1H NMR spectra and their assignments of PLLA2–PBLG (B) and PLLA2–PLGA (A) in DMSO-d6 (x and y are solvent peaks).
|
PMC9076388
|
c9ra08703f-f1.jpg
|
0.40938 |
d53ccb8457eb40d5a6df5181bf103aa7
|
TEM micrographs of the lyophilized vesicles from PLLA2(30)–PLGA55.
|
PMC9076388
|
c9ra08703f-f10.jpg
|
0.521757 |
c9efeaa264c84a58bf885a2827da4335
|
IR spectra of (A) PLLA2-b-PBLG, (B) PLLA2-b-PLGA.
|
PMC9076388
|
c9ra08703f-f2.jpg
|
0.581348 |
1a9b5d60997e4a2c80b133ea8923068a
|
The GPC chromatographs of PLLA2–NH–Z (b), PLLA2(30)–PBLG10 (c) and PLLA2(30)–PBLG55 (a).
|
PMC9076388
|
c9ra08703f-f3.jpg
|
0.48087 |
9d1f377fc8bc4ba088e9c0291aa96b84
|
(A) Plot of I333/I331 of pyrene vs. log C of PLLA2(30)–PLGA55 in deionized water. (B) Plot of I335/I332 of pyrene vs. log C of PLLA2(30)–PLGA10 in deionized water.
|
PMC9076388
|
c9ra08703f-f4.jpg
|
0.428927 |
f5c5aaebdd9a4e93a7f259ed01aced9d
|
(A) TEM micrographs of the vesicles from PLLA2(30)–PLGA55. (B) TEM micrographs of the vesicles from PLLA2(30)–PLGA10. (C) ESEM micrographs of vesicles from PLLA2(30)–PLGA55, the inset is magnification. (D) Schematic representation of the vesicle.
|
PMC9076388
|
c9ra08703f-f5.jpg
|
0.395256 |
8ec2de255a0d41c5a2639c7b512bdb45
|
DLS graphs of the micelle size distribution of (A) PLLA2(30)–PLGA55 and (B) PLLA2(30)–PLGA10.
|
PMC9076388
|
c9ra08703f-f6.jpg
|
0.440735 |
faeae39bfc7747faa8578ad2c7b57abf
|
1H NMR spectra and their assignments of PLLA2(30)–PLGA10 in D2O.
|
PMC9076388
|
c9ra08703f-f7.jpg
|
0.527612 |
e66e8ca501f34774ad3883e16e208f76
|
Plot of Rh of PLLA2(30)–PLGA55 vesicles vs. solution pH value (the concentration of the copolymer is 0.4 mg ml−1).
|
PMC9076388
|
c9ra08703f-f8.jpg
|
0.467491 |
e59d389c8bd845f581d048841049d279
|
Plot of Rh of PLLA2(30)–PLGA55 vesicle vs. NaCl concentration at pH 5.5 (the concentration of the copolymer is 0.4 mg ml−1).
|
PMC9076388
|
c9ra08703f-f9.jpg
|
0.433006 |
5f2a7853841740d580757a3b476673f0
|
The aldehyde content of NCDs at pHs 3 and 7 versus oxidation times.
|
PMC9076516
|
c9ra05240b-f1.jpg
|
0.464307 |
6e718e1b38674d87b096233d1a430234
|
FT-IR spectra of MC, HANCD, and immobilized urease as HANCD@urease.
|
PMC9076516
|
c9ra05240b-f2.jpg
|
0.51657 |
0a33326fa39c4c179a1bcbaf0a1e2f42
|
X-ray diffraction patterns of HANCD and urease immobilized on HANCD.
|
PMC9076516
|
c9ra05240b-f3.jpg
|
0.396271 |
5b4a58bc2dca4e268dc1a6c6d5882cfc
|
FESEM of MC (a), NC (b), HANCD (c), and immobilized urease on HANCD (d).
|
PMC9076516
|
c9ra05240b-f4.jpg
|
0.504123 |
0072a852659e41e5a2844073a6a9cca5
|
Thermal gravimetric analysis of HANCD and HANCD@urease.
|
PMC9076516
|
c9ra05240b-f5.jpg
|
0.466162 |
f270b2bd00f24f0d8989736b8df389d4
|
The relative residual activities of the free and immobilized urease at adjusted pHs at 35 °C (a) and at temperatures from 20–80 °C at pH = 7 (b); the aldehyde content of HANCD@urease at various temperatures and pHs (c); change in the absolute activities for free and HANCD anchored urease at various pHs (d) and temperatures (e). Each experimental point represents the mean of five determinations with 2.8% SD.
|
PMC9076516
|
c9ra05240b-f6.jpg
|
0.482001 |
1e0aa068b88641f4a7e530b2ef624ef4
|
Comparative residual activity of the free- and immobilized-urease versus time.
|
PMC9076516
|
c9ra05240b-f7.jpg
|
0.444327 |
c903e81b10394ca4a54b7d47c92da94a
|
Operating reusability of the HANCD@urease evaluation of serum urea by HANCD@urease.
|
PMC9076516
|
c9ra05240b-f8.jpg
|
0.424127 |
04d0fbf0aefc4d6b80f464aedd7d5445
|
CircPVT1 and NEK7 were up-regulated while miR-181a-5p was down-regulated in NSCLC tissues and cells. (A–D) QRT-PCR was implemented to measure the expression of circPVT1 (A and B) and miR-181a-5p (C and D) in NSCLC tissues and cells. (E–H) The mRNA and protein levels of NEK7 in NSCLC tissues (E and F) and cells (G and H) were detected through qRT-PCR and western blot. (I–K) The linear relation among circPVT1, miR-181a-5p and NEK7 was analyzed by Spearman's correlation coefficient. *P < 0.05.
|
PMC9076563
|
c9ra08872e-f1.jpg
|
0.38639 |
6bbc8f4b9c184ec4a9e15725180faa9b
|
Knockdown of circPVT1 suppressed the chemoresistance of cisplatin and metastasis in NSCLC cells. (A) The interference efficiency of si-circPVT1 was assessed by qRT-PCR in NSCLC cells. (B and C) Cell viability was examined using an MTT assay after transfection with si-circPVT1 or si-NC (B) and IC50 was calculated (C). (D and E) Cell apoptosis was evaluated through flow cytometry (D) and the detection of apoptosis-associated proteins by western blot (E) after treatment with 2 μg mL−1 cisplatin and transfection. (F and G) The ability of metastasis was determined via a transwell invasion assay (F) and the levels of EMT-related proteins by western blot (G). *P < 0.05.
|
PMC9076563
|
c9ra08872e-f2.jpg
|
0.416666 |
8fbe745751624e60acdabb1630d5cf6a
|
CircPVT1 induced targeted regulation of the level of miR-181a-5p. (A) The bioinformatics analysis between circPVT1 and miR-181a-5p was conducted via Starbase2.0. (B and C) The relationship between circPVT1 and miR-181a-5p in NSCLC cells was verified by a dual-luciferase reporter assay (B) and RIP assay (C). (D) QRT-PCR was applied for assaying the effects of circPVT1 inhibition or overexpression on the miR-181a-5p expression in A549 and H1299 cells with si-NC and pcDNA-NC as the negative controls. *P < 0.05.
|
PMC9076563
|
c9ra08872e-f3.jpg
|
0.49208 |
716cec209d424aa1910fcb050916c4dc
|
Down-regulation of circPVT1 ameliorated the effects of miR-181a-5p inhibitor on NSCLC cells. (A) The miR-181a-5p expression was assayed by qRT-PCR in A549 and H1299 cells transfected with miR-NC inhibitor, miR-181a-5p inhibitor, miR-181a-5p inhibitor + si-NC or miR-181a-5p inhibitor + si-circPVT1. (B and C) MTT was adopted for examining cell viability and determining the value of IC50 of cisplatin after transfection with miR-181a-5p inhibitor, miR-181a-5p inhibitor + si-circPVT1 or relative controls. (D and E) Flow cytometry and western blot were used for the determination of the apoptosis rate and related protein expression in A549 and H1299 cells treated with 2 μg mL−1 cisplatin and transfected with the above groups, respectively. (F) A transwell assay was applied to detect the ability of invasion. (G and H) The levels of EMT-associated markers were measured using western blot. *P < 0.05.
|
PMC9076563
|
c9ra08872e-f4.jpg
|
0.470562 |
c1493e9474164823a04e094fcc2fe170
|
Inhibition of circPVT1 aggravated the si-NEK7-inhibited metastasis via reducing NEK7 by promoting miR-181a-5p. (A) The prediction of the targets of miR-181a-5p was executed using Starbase2.0. (B and C) A dual-luciferase reporter assay and RIP assay were used for validating the target relation between miR-181a-5p and NEK7 in A549 and H1299 cells. (D and E) The mRNA and protein levels of NEK7 were measured by qRT-PCR and western blot after transfection with si-NEK7, si-circPVT1, miR-181a-5p inhibitor, si-circPVT1 + miR-181a-5p inhibitor or matched controls. The expression levels of circPVT1 and miR-181a-5p were determined in A549 and H1299 cells transfected with si-NEK7 or si-NC. (H–J) Cell metastasis was assessed by transwell invasion assay and the assaying of EMT-related markers through western blot in A549 and H1299 cells transfected with si-NEK7, si-NEK7 + si-circPVT1, si-NEK7 + miR-181a-5p inhibitor or matched controls. *P < 0.05.
|
PMC9076563
|
c9ra08872e-f5.jpg
|
0.471692 |
8852216764e2423b9864396c695df91f
|
Knockdown of circPVT1 relieved the 3-MA-promoted chemoresistance of cisplatin via elevating miR-181a-5p-mediated autophagy. (A) The level of miR-181a-5p was determined by qRT-PCR in A549 and H1299 cells treated with 3-MA, 3-MA + si-circPVT1, 3-MA + miR-181a-5p inhibitor or respective controls. (B) Western blot was used for assaying the protein levels of autophagy-related proteins. (C and D) Cell viability and IC50 of cisplatin were measured and analyzed by MTT. (E and F) After treatment with 2 μg mL−1 cisplatin and treatment with the above groups, cell apoptosis was assessed from the apoptosis rate by flow cytometry and apoptosis-associated protein expression by western blot. *P < 0.05.
|
PMC9076563
|
c9ra08872e-f6.jpg
|
0.453982 |
fd7abb77a7514979bd9be7004cefdc5f
|
The decrease of circPVT1 heightened the cisplatin sensitivity of NSCLC cells in vivo. (A and B) Tumor volume and weight were calculated in four groups of sh-NC + PBS, sh-NC + cisplatin, sh-circPVT1 + PBS and sh-circPVT1 + cisplatin. (C) The expression of circPVT1 was detected by qRT-PCR using the RNA from the tumor tissues. *P < 0.05.
|
PMC9076563
|
c9ra08872e-f7.jpg
|
0.499405 |
907ffd04924a435496f356e8fa439823
|
The regulatory mechanisms of circPVT1 on metastasis and chemoresistance of NSCLC. CircPVT1 interacts with miR-181a-5p to regulate NEK7 expression, affecting cell metastasis, or regulate autophagy, promoting chemoresistance.
|
PMC9076563
|
c9ra08872e-f8.jpg
|
0.460742 |
adfabe5177c445c0852725dae934bebd
|
Circular dichroism and cell viability analysis of DE-11. Peptide DE-11 was dissolved in 20 mM HEPES (pH = 7.4). CD spectra of DE-11 after 2 h (full line) and 24 h (broken line) of incubation (A). CD spectra of DE-11 after the addition of CaCl2 (red line) and Na2HPO4 (green line), in comparison with those of DE-11 without Ca2+ and HPO42− (black line) (B). The effect of HOK cell viability of DE-11 at various concentrations determined by the CCK-8 assay. Data are presented as the mean ± SD (C).
|
PMC9077281
|
c7ra12032j-f1.jpg
|
0.409486 |
c5a9bc37ef314c47a57b1946d259bcf9
|
Linear adsorption isotherms of DE-11. Protein–HA adsorption data fit the Langmuir model well. The affinity of DE-11 molecules for HA adsorption sites (K) and the maximum number of adsorption sites per gram of HA (N) were calculated. R2 is the correlation coefficient obtained for linear adsorption isotherms.
|
PMC9077281
|
c7ra12032j-f2.jpg
|
0.441866 |
9f9d528d64734c9c87085645de4c16a1
|
SEM images of calcium phosphate minerals in the control group (A), DE-11 group (B), and DK-6 group (C) after 24 h of incubation. Spherical particles were formed in both the DK-6 and the calcium phosphate control samples, whereas a different morphology characterized as smaller crystals with rough and spicular surfaces was observed in the DE-11 sample.
|
PMC9077281
|
c7ra12032j-f3.jpg
|
0.397506 |
704342ce23df4b1784303514f68da737
|
TEM images of calcium phosphate minerals and related SAED patterns after 24 h of incubation. Calcium phosphate control group: morphology (A) and SAED pattern (B). DE-11 group: morphology (C) and SAED pattern (D). DK-6 group: morphology (E) and SAED pattern (F). The mineral structure consisting of needle-like crystals was clearly observed in the presence of DE-11.
|
PMC9077281
|
c7ra12032j-f4.jpg
|
0.445424 |
c1ef21555890426086af7d40aa1c7713
|
SMH analysis of the enamel samples after the remineralization assay. The SMH of the NaF group, DE-11-treated group, DK-6-treated group, and HEPES group after immersion in artificial saliva for 3 and 7 days as compared to that of the original enamel samples (A). SMHR% of the NaF group, DE-11-treated group, DK-6-treated group, and HEPES group after being immersed in artificial saliva for 3 days (B) and for 7 days (C). Data are presented as the mean ± SD. The statistical analysis was performed using ANOVA followed by the Student–Newman–Keuls test (**P < 0.01, ***P < 0.001).
|
PMC9077281
|
c7ra12032j-f5.jpg
|
0.465029 |
d77dd78cef874cc28ec122358e594569
|
PLM images of the enamel sections before and after remineralization treatment in the presence of NaF (A), DE-11 (B), DK-6 (C) or HEPES alone (D).
|
PMC9077281
|
c7ra12032j-f6.jpg
|
0.457644 |
294dcaa6b008489c8fac230035bdb20a
|
TMR analysis of enamel sections before and after remineralization treatment in the presence of NaF, DE-11, DK-6 or HEPES alone. Mineral loss of enamel blocks (A), lesion depth of enamel blocks (B), and mineral content (vol% μm) vs. depth (μm) for lesions (C). Data are presented as the mean ± SD. The statistical analysis was performed using the Students paired t test. Bars labelled with different letters are significant differences (P < 0.05).
|
PMC9077281
|
c7ra12032j-f7.jpg
|
0.456892 |
13396ecb0d5f4142adde16410c543d72
|
Schematic of the adsorption of DE-11 on the demineralized enamel surface for remineralization restoration.
|
PMC9077281
|
c7ra12032j-f8.jpg
|
0.436376 |
d5ae7ef9960f4884b180d2c81afed09d
|
The experimental device and electrode positions.
|
PMC9078048
|
iovs-63-5-7-f001.jpg
|
0.41295 |
4c595e28a82f4447a0b049b32c9d4dc3
|
The maximal power of theta-, alpha- and beta-waves of 13 electrodes of ROI in condition 1 (20″, unperceived totally) and condition 2 (100″, perceived clearly). (a) Heat map; (b) summary data and ANOVA analysis.
|
PMC9078048
|
iovs-63-5-7-f002.jpg
|
0.472712 |
0b31f00e4f8d4f6380f0ff3678b7a540
|
The changes (∆) of maximal powers of theta-, alpha-, and beta-waves of the 13 electrodes in the ROI induced by depth perception. (a, b) The ∆ maximal powers of theta-, alpha-, and beta-waves in all the electrodes. (c) Grid of Tukey's multiple comparisons of ∆ maximal powers of the theta-waves. (d) Grid of Tukey's multiple comparisons of ∆ maximal powers of the alpha-waves.
|
PMC9078048
|
iovs-63-5-7-f003.jpg
|
0.442059 |
8705c5a1946b4c7ab1f8e2c6568713c9
|
Functional connectivity of theta and alpha-waves between any two channels among the interesting electrodes from the frontal lobe and occipital lobe. (a) The PLI values of theta-wave under condition 1 (20″, unperceived totally). (b) The PLI values of the theta-waves under condition 2 (100″, perceived clearly). (c) The FC changes of the theta-waves and the comparisons between FCs in condition 2 and those in condition 1. (d) The PLI values of the alpha-waves under condition 1. (e) The PLI values of the alpha-waves under condition 2. (f) The FC changes of the alpha-waves and the comparisons between FCs in condition 2 and those in condition 1 (* P < 0.05, # P < 0.01, + P < 0.001).
|
PMC9078048
|
iovs-63-5-7-f004.jpg
|
0.491501 |
e1a9ae49adab4c949325f401f5b673f1
|
Ball-and-stick structures of compounds Q7 and Q9.
|
PMC9078235
|
c7ra13397a-f1.jpg
|
0.470694 |
c40d38023d3e41868ad78c11e2c1e22f
|
Thermogravimetric and heat flow curves of compounds Q1–Q9 recorded at a constant heating rate. The mass loss is expressed as the fraction M/M0 of the mass at temperature T to the initial mass of the samples equilibrated at laboratory atmosphere.
|
PMC9078235
|
c7ra13397a-f2.jpg
|
0.409414 |
3febde8bf2c24fed9f31d00c0031deff
|
The EC50 values for the activation of thrombin activity by compounds Q2 and Q8. aThe EC50 values are expressed as the concentration required for a thrombin activity response of 50%; n = 3.
|
PMC9078235
|
c7ra13397a-f3.jpg
|
0.444132 |
19a16eadd5b34a57afd2c9092c0e34f5
|
The classical systems for blood coagulation including extrinsic, intrinsic, and/or the common coagulation pathways.30
|
PMC9078235
|
c7ra13397a-f4.jpg
|
0.473026 |
5fc16f63d6624fbcb669c35d8a5ac142
|
Compound Q2 docking into the thrombin binding pocket.
|
PMC9078235
|
c7ra13397a-f5.jpg
|
0.423433 |
977a81944f454280848aa9fc09d11668
|
Effects of compounds Q2 and etamsylate on capillary permeability. The results were expressed as the concentration of CNP (pg mL−1). Values are reported as the mean ± SEM of three independent experiments.
|
PMC9078235
|
c7ra13397a-f6.jpg
|
0.43741 |
7dc204242d7e4a2799ce115b8cc8564d
|
(a) XRD patterns of La0.65Ce0.05Sr0.3Mn1−xCuxO3 (0 ≤ x ≤ 0.15) compounds at room temperature. (b) Rietveld refinement profile for x = 0.05 performed using FULLPROF. Open circles correspond to experimental data and the lines are fits. Vertical bars represent the Bragg reflections for the space group R3̄c. The difference pattern between the observed data and fits is shown at the bottom. The inset shows a zoom in the region between 2θ: 34–64°.
|
PMC9078421
|
c7ra13244a-f1.jpg
|
0.457102 |
5d6425f9ddc642c2aded19ac6c8b4446
|
(a) Crystal structure of La0.65Ce0.05Sr0.3MnO3 (b) 3D view showing MnO6 octahedron (c) SEM images of (x = 0 and x = 0.15) samples.
|
PMC9078421
|
c7ra13244a-f2.jpg
|
0.472865 |
c850d0a351704f59b6c32976a430ca33
|
Raman spectrum of La0.65Ce0.05Sr0.3Mn1−xCuxO3 (x = 0, 0.05, 0.10 and 0.15).
|
PMC9078421
|
c7ra13244a-f3.jpg
|
0.404806 |
015062f0308d4b01b5458738c38b49d1
|
Temperature dependence of the magnetization for La0.65Ce0.05Sr0.3Mn1−xCuxO3 (x = 0.10 and x = 0.15) measured in field cooling (FC) mode at an applied magnetic field of μ0H = 500 Oe. Inset (a) the temperature derivative dM/dT. (b) Temperature dependence of the inverse of magnetic susceptibility 1 = χ. The red line presents the linear fit at high temperature.
|
PMC9078421
|
c7ra13244a-f4.jpg
|
0.409873 |
db9bafc7ecd24ffdaeb3969a034006ad
|
Isothermal magnetization versus magnetic field around TC of La0.65Ce0.05Sr0.3Mn1−xCuxO3, (a) for x = 0 and (b) for x = 0.15.
|
PMC9078421
|
c7ra13244a-f5.jpg
|
0.469078 |
b141fac3c86b47c48cb8a5de3eef116d
|
Arrott plot of μ0H/M vs. M2 at different temperatures for La0.65Ce0.05Sr0.3Mn1−xCuxO3, (a) x = 0 and (b) x = 0.15.
|
PMC9078421
|
c7ra13244a-f6.jpg
|
0.475911 |
e82f19e2f95a4b799e2ad77fe226b4cb
|
The temperature dependence of the magnetic entropy change (ΔSM) under different applied magnetic fields (a) for x = 0, (b) for x = 0.05, (c) for x = 0.10 and (d) for x = 0.15.
|
PMC9078421
|
c7ra13244a-f7.jpg
|
0.470437 |
4e6d66b446f44910a0be8aeae2477515
|
Normalized ΔSMversus rescaled temperature θ for La0.65Ce0.05Sr0.3Mn1−xCuxO3, the solid line is the average curve.
|
PMC9078421
|
c7ra13244a-f8.jpg
|
0.396621 |
550080a883e948588c6d81f445fb9c96
|
Typical TEM images of PAH-MTX nanoassemblies: (A1) sample a1, (A2) sample a2, (A3) sample a3, (B1) sample b1, (B2) sample b2, (B3) sample b3, (C1) sample c1, (C2) sample c2, (C3) sample c3, (D1) sample d1, (D2) sample d2, (D3) sample d3.
|
PMC9078489
|
c7ra12862b-f1.jpg
|
0.415394 |
bbb3e87917544128980ead34f4a8ee95
|
Typical TEM images of PAH–MTX nanoassemblies: (E1) sample e1, (E2) sample e2, (E3) sample e3, (E4) sample e4, (F0) sample c1, (F1) sample f1, (F2) sample f2, (F3) sample f3.
|
PMC9078489
|
c7ra12862b-f2.jpg
|
0.42795 |
f018dc091ea64938ba2c871a553d101e
|
(A) FTIR spectra of free MTX, PAH, samples a2, b1, c2 and d1. (B) UV-vis absorption spectra of free MTX, PAH, samples a2, b1, c2 and d1. (C) XRD patterns of free MTX, PAH, samples a2, b1, c2 and d1.
|
PMC9078489
|
c7ra12862b-f3.jpg
|
0.445253 |
165ebd728829448b8a74251366f38ac6
|
(A) Release profiles of free MTX, samples a2, b1, c2 and d1. (B–E) Plots of different kinetic models for the release of MTX from the PAH–MTX nanoassemblies.
|
PMC9078489
|
c7ra12862b-f4.jpg
|
0.40863 |
f3498f7ad396475fb703ad61ed7f4845
|
(A) Comparison of cell viabilities for free MTX, samples a2, b1, c2 and d1 at various concentrations after 24 h of incubation; (B) comparison of cell viabilities for free MTX, sample a2, b1, c2 and d1 after different incubation time at the concentration of 100 μg mL−1. All cell viability data were obtained from three separated experiments and error bars represent standard error (n = 3).
|
PMC9078489
|
c7ra12862b-f5.jpg
|
0.505199 |
5b5ce355d0c3460392473193e84c4e5e
|
Morphology changes of A549 cells treated with various samples at the concentration of 100 μg mL−1: (A) DMEM for 24 h; (B) free MTX for 24 h; (C) sample a2 for 24 h; (D) sample a2 for 48 h; (E) sample a2 for 72 h.
|
PMC9078489
|
c7ra12862b-f6.jpg
|
0.527485 |
435d41a3b2194355878cf9c6957096bd
|
XRD patterns for the rock and soil samples ((A) <150 μm, (B) <2 μm). XRD revealed quartz (d = 4.25 and 3.34), feldspar (d = 3.76, 3.22, 2.98, and 2.90), and kaolinite (d = 7.15 and 3.55) as the possible main mineral constituents, while illite (d = 9.94 and 4.25) and montmorillonite (d = 15.29) were revealed as the possible minor mineral constituents in the rock and soil samples. Letter designations: Q, quartz; F, K-feldspar; K, kaolinite; I, illite; M, montmorillonite.
|
PMC9079951
|
c8ra01268g-f1.jpg
|
0.441272 |
4e731c48c37243bba939c0d3ab67590a
|
Influence of rock-weathering bacteria (L26, M23, and H41) on the releases of Fe, Si, and Al and on the pH of the medium added in tuff during 15 days of incubation. Error bars are ±standard error (n = 3).
|
PMC9079951
|
c8ra01268g-f2.jpg
|
0.466661 |
40f7d62929054e3b8056ea6361f96cc2
|
Influence of salt, temperature, and pH on the growth of the mineral-weathering bacteria isolated from the less and more altered rock samples and the soil samples. Error bars are ±standard error (n = 3). Bars indicated by the same letter are not significantly different (P > 0.05) according to Tukey’s test.
|
PMC9079951
|
c8ra01268g-f3.jpg
|
0.453233 |
4dbe93c318824e939799a57a576e73b5
|
Proportional abundance of the high, moderate, and low effective element (Si, Al, and Fe) solubilizers from the less (LR) and more (MR) altered rock and soil samples (SS), respectively.
|
PMC9079951
|
c8ra01268g-f4.jpg
|
0.428115 |
bade1bccaff34835b50c702d1b92b81a
|
(a) Spectroelectrochemistry of TTF1 in CH2Cl2 (c = 5 × 10−4 mol L−1); (b) UV-Vis absorption spectra and (c) ESR spectra of TTF1 and TTF2 upon adding 3 equivalents of I2 in CH2Cl2 (c = 1 × 10−5 mol L−1).
|
PMC9080441
|
c8ra02956c-f1.jpg
|
0.479121 |
c6f0cbb8354d47c0abcff86ebe87b611
|
Crystal structure of complex (TTF1)·(I3)·(I2): (a) top view of molecule TTF1 with the central CC bond length shown in unit of Å; (b) TTF1 dimer with atomic short contacts shown in dashed lines (green for S⋯S and grey for C⋯S); (c) anion sheets composed of (I3)− and I2 with the I–I bond length and I⋯I contacts (purple dashed lines) shown; (d) packing structure viewed along the longitudinal axis of TTF1 dimer with the I⋯I contacts shown in grey dashed lines.
|
PMC9080441
|
c8ra02956c-f2.jpg
|
0.465517 |
ddcb5a51b8964f87a4a59992b20474b2
|
Crystal structures of complex (TTF2)·(I5)·(I2): (a) top view of molecule TTF2 with the central CC bond length shown in unit of Å; (b) the (I3)− anion chain with the I–I bond lengths and I⋯I contacts (purple dashed lines) shown; (c) packing structure projected along the longitudinal axis of the TTF moiety.
|
PMC9080441
|
c8ra02956c-f3.jpg
|
0.467943 |
e145fd6269b24037bc56db0dfb609bc6
|
(a) ESR spectra for the crystalline complexes of (TTF1)·(I3)·(I2) and (TTF2)·(I5)·(I2); UV-Vis absorption spectra of (TTF1)·(I3)·(I2) and (TTF2)·(I5)·(I2) in the (b) solid state, and (c) CH2Cl2 solution (c = 10−5 mol L−1) after standing under inert atmosphere for 30 min and/or 24 h.
|
PMC9080441
|
c8ra02956c-f4.jpg
|
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