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0.4422 | f0b401a841804b6084d593ec46506abd | Effect of different blanching methods on the textural properties of T. fuciformis. Note: (a) Firmness, (b) Cohesiveness, (c) Viscosity, (d) Consistency. The different lowercase letters indicate significant differences among the three treatments at the same time (p < 0.05). | PMC10137464 | foods-12-01669-g001.jpg |
0.512393 | faa62416d49f475581ea78bf3fe95a48 | Dynamics of the texture of T. Fusiformis treated with different blanching methods. Note: (a) Firmness, (b) Cohesiveness, (c) Viscosity, (d) Consistency. The different lowercase letters with the same color indicate significant differences between the different time at the same treatment (p < 0.05). | PMC10137464 | foods-12-01669-g002.jpg |
0.484253 | 07f63b724aa74393b2dac8e2f2fd4272 | Polysaccharide content of different blanching methods of T. fuciformis. Note: (a) The different lowercase letters indicate significant differences among the three treatments at the same time (p < 0.05). (b) The different lowercase letters with the same color indicate significant differences at different time at the same treatment (p < 0.05). | PMC10137464 | foods-12-01669-g003.jpg |
0.434845 | 1ae26220ebb0473199d5ab288c42c581 | Change of transverse relaxation time and relative amplitude of T. fuciformis with different blanching methods: (a) 1 min, (b) 1.5 min, (c) 2 min, (d) 2.5 min, (e) 3 min. | PMC10137464 | foods-12-01669-g004.jpg |
0.451016 | 7e0c8a3ae196440188ed06639f9f5424 | The pseudo-color T2-weighted images of T. fuciformis with different blanching methods. (a) The pseudo-color T2-weighted image of fresh T. fuciformis. (1b–5b) The pseudo-color T2-weighted images of BWB group at 1 min~3 min. (1c–5c) The pseudo-color T2-weighted images of ULTB group at 1 min~3 min. (1d–5d) The pseudo-color T2-weighted images of HTS group at 1 min~3 min. | PMC10137464 | foods-12-01669-g005.jpg |
0.421568 | a6068587f4c74369aa1ad97dfc2c1f6a | Some of cardinal criteria of ARO within our cohort; the red arrows point to some important radiological findings. (A) Frontal bossing; (B) increased bone density; (C,D) characteristic Erlenmeyer flask deformity; (E) straight mandibular angle; (F) bone-in-bone appearance and acro-osteolysis. | PMC10137576 | genes-14-00900-g001.jpg |
0.418048 | 13129a5a9ef94c8988fa2ff8174615be | Some of the dental findings. (A) 3-year-old patient with delayed eruption of deciduous teeth; (B) 12-year-old patient with delayed eruption and hypocalcification; (C) Close-up of lower teeth showing recession of the gingiva. | PMC10137576 | genes-14-00900-g002.jpg |
0.429341 | 605e04fc8dc249ffa56388136e236393 | Examples of consanguineous pedigrees with more than one affected sib. (A) Pedigree of family of ARO5; (B) pedigree of family of ARO8. | PMC10137576 | genes-14-00900-g003.jpg |
0.407124 | 5ad435bc865642a18738e3ff2f9fc4a7 | Brain magnetic resonance imaging of ARO1 showing atrophic changes. | PMC10137576 | genes-14-00900-g004.jpg |
0.459126 | 4e410236b003483a91a358becba4ad15 | Different characterized TCIRG1 gene variants. | PMC10137576 | genes-14-00900-g005.jpg |
0.477647 | 5421d98ecca5440b876a42d7c7ade675 | Predicted alterations of missense TCIRG1 variants (Arg56Trp, Leu653Arg, and Arg736Cys) on VPP3 protein structure. (A) Protein structure of V-type proton ATPase 116 kDa subunit a3 (VPP3; Uniprot ID: Q13488) predicted by AlphaFold. Per-residue confidence score (pLDDT) between 0 and 100 is shown in color codes. Red arrows show the position of the residues of interest: Arg56Trp and Leu653Arg on the protein surface, and Arg736Cys in the core of the protein. (B–D) The Prem PS software prediction of the changes in bonding between the mutated amino acid residues and the neighboring residues. The predicted changes in unfolding free energy (ΔΔG) values are calculated for each mutated protein. Noncovalent interactions are color coded at the bottom of the figure. | PMC10137576 | genes-14-00900-g006.jpg |
0.364674 | e589f652e88a446a8c8caaa561c892e2 | Optimized 3D complex structures between sulfamethizole and (A) 3-thiopheneacetic acid, (B) 3-thiopheneethanol, (C) 3-thiophenemethylamine, and (D) 3-thiopheneboronic acid. The presence of hydrogen bonds is indicated by the light black dashed lines. The values near the hydrogen bonds are the bond lengths and bond angles, and values in brackets are binding energies; unit: kcal/mol. Level of theory: PWPB95(D3-BJ)/def2-QZVPP//B97-3c. | PMC10137692 | foods-12-01693-g001.jpg |
0.409255 | 8052b11b8c744e55a3487167dec2268c | EIS responses (bar charts) and imprinting factors (line charts) of several MIPs prepared with different monomers towards target sulfamethizole (SMZ, 0.1 μM). | PMC10137692 | foods-12-01693-g002.jpg |
0.414153 | e02d6cdd15234657baa19d9c93199296 | Electrochemical characterization for the fabrication process of the MIP film. (A,B) EIS and (C,D) CV curves for different modified glass carbon electrode (GCE). | PMC10137692 | foods-12-01693-g003.jpg |
0.434363 | 18f994abe25845198b38a30a28e0444b | Optimization of experimental conditions, including template concentration (A), polymerization cycles (B), eluents and elution time for template removal (C,D), and oscillation speed and pH during recognition (E,F), to obtain a better sensing performance toward SMZ. Firstly, the eluent was optimized and determined by polymerization of 10 cycles at a concentration of 35 μM SMZ. Then, the concentration of SMZ was optimized in the case of polymerization of 10 cycles. Finally, the number of polymerization cycles was optimized at a template concentration of 25 μM. The rest are optimized in turn. | PMC10137692 | foods-12-01693-g004.jpg |
0.427134 | 635c368e74bb480ba9040d9e76234d99 | (A) Impedance spectra of the proposed sensor for detecting sulfamethizole (SMZ) from 0 to 10 μM by a 10-fold serial dilution. (B) Calibration curve of the EIS response versus logarithmic concentration of SMZ from 0.001 to 10 μM. | PMC10137692 | foods-12-01693-g005.jpg |
0.424725 | 5b42465d083f4166ad83fa1b7e846546 | (A) Structural formula of sulfathiazole (ST), sulfanilamide (SA), and sulfamethizole (SMZ). (B) Selectivity: EIS response of the sensor to ST, SA, and SMZ at the same concentration. (C) Reusability: EIS response of the sensor to SMZ (0.1 μM) with different reuse numbers. (D) EIS response of the MIP sensor toward the intra-assay and inter-assay measurements of 0.1 μM SMZ. (E) The storage stability of the MIP/GCE. | PMC10137692 | foods-12-01693-g006.jpg |
0.368727 | 0933a0fe4b5944b49bd2ff32dd05dc76 | Schematic diagram of the preparation of a MIP-based impedance sensor for sulfamethizole (SMZ) detection. | PMC10137692 | foods-12-01693-sch001.jpg |
0.462291 | aacd07e4d0024356ba52247b356b9cda | Architecture of the proposed model. | PMC10137756 | healthcare-11-01171-g001.jpg |
0.425294 | abade7f86d0b4647a07f5ce4822d3ccb | Kaplan–Meier plots of overall survival according to the stage, the Deauville score, the international prognostic index (IPI) score, and extranodal involvement status in the CNUHH and JBUH datasets. | PMC10137756 | healthcare-11-01171-g002.jpg |
0.453751 | 1e10157a5e564bd6bd30d3f3e12a43a0 | Survival curves for each model in the test set: (a) before treatment; (b) after treatment. | PMC10137756 | healthcare-11-01171-g003.jpg |
0.408825 | 6395e4c63fb44db18ed1c440cc63aa86 | Representative estimated individual survival curves for five patients with ground truth survival times in the range of 527–2421 days. | PMC10137756 | healthcare-11-01171-g004.jpg |
0.36297 | e43ee0c2582d463aa69a290aeab17c7f | Estimated survival times and absolute error comparison between before and during treatment. | PMC10137756 | healthcare-11-01171-g005.jpg |
0.495104 | 9946b08117a6420c9ad244acfd467538 | (A) Partial G-banded karyotype of chromosomes 9 and 15, balanced insertion—ins(9;15)(q33;q21.1q22.31). (B) Partial G-banded karyotype of chromosomes 9 and 15, unbalanced insertion—der(9)ins(9;15)(q33;q21.1q22.31)—resulting in duplication of the q21.1q22.31 region of chromosome 15. (C) Five-generation pedigree of the family showing the affected individuals and the transmission of the chromosomal rearrangement in three generations. | PMC10138010 | genes-14-00885-g001.jpg |
0.396622 | 0bc26782805e42d9a20f299aca5ffaa8 | (A–C) Affected individuals harboring the unbalanced rearrangement, with a 19.3 Mb duplication of the q21.1q22.31 region of chromosome 15, with facial dysmorphisms: discrete synophrys, upslanted palpebral fissure, low-set ears, bifid nasal tip, downturned corners of mouth, and retrognathia. Subject 1 (III-4) (A), subject 2 (IV-11) (B), and subject 4 (IV-15) (C). (D–F) Log2ratio graphics, obtained by CMA, of part of the long arm of chromosome 15, showing a 19.3 Mb duplication at 15q21.1q22.31 (46487891_65795296—GRCh37) in the individuals with unbalanced insertion. | PMC10138010 | genes-14-00885-g002.jpg |
0.421155 | 44bf5be0879e426c96c58d3f16b819c3 | (A,B) Subject 3 (IV-12), harboring an inherited balanced chromosomal insertion, with microcephaly, highly arched eyebrows, bulbous nose, thin upper lip vermilion, and everted lower lip vermilion; (C) Image taken from the Integrative Genome Viewer (IGV), showing a region with red reads in the exon 3 of the MECP2 gene, which corresponds to an 88 bp deletion in this gene (chrX:153296091-153296179—GRCh37). Variant allele frequency (VAF) = 0.40; depth of coverage (SD) = 111. | PMC10138010 | genes-14-00885-g003.jpg |
0.408424 | 19ee3ad890934414810e782ae6747c1d | View of the 15q15.1-q26.3 region, including duplications, represented by blue bars, from the present subjects and cases from DECIPHER and literature. The CYP19A1 gene region is highlighted by the black vertical line. Image taken from UCSC Genome Browser on Human (GRCh37/hg19). | PMC10138010 | genes-14-00885-g004.jpg |
0.519714 | abec20764c7749048565e8ec73a0fec7 | Characterization (a) XRD of Nanofibrillar cellulose (b) SEM images of NFC hydrogel (0.8 wt%) at different magnifications. | PMC10138276 | gels-09-00324-g001.jpg |
0.43958 | 9e20455ebc65469aad929c163ba85813 | Cell morphology and viability after 5 days of culture. (a) Scheme for construction of NFC hydrogel embedded with hiPSCs. (b) Typical images for cell morphology on days 1, 3, and 5. (c) Typical images for cell viability at different zones at the end of 5 days of culture. (d) Cell viability at different zones on day 5. Error bars denote the means ± SEM. | PMC10138276 | gels-09-00324-g002.jpg |
0.46219 | ea719af6290142038c6f1920de0654cc | Average second derivative spectra and principal component analysis for cells during culture. (a) Average second derivative spectra of the cells at different zone on days 1, 3, and 5. (b) The representative score plots of the PCA of hPSCs at different zones in 3D hydrogel during culture on days 1, 3, and 5. (c) The loading plots of the PCA for hPSCs cultured on days 1, 3, and 5. | PMC10138276 | gels-09-00324-g003.jpg |
0.431762 | ccfdcd98672a448289cf68f1772fb29e | Human iPSC stemness at different locations on day 5 cultured in 3D hydrogel. Error bars denote the means ± SEM. Statistical analyses were performed by unpaired Student’s t-test (* p < 0.05). | PMC10138276 | gels-09-00324-g004.jpg |
0.453617 | bf3dda5e30724c98aef65754ebd3afe0 | Solute distribution inside 3D hydrogel at different times and locations. | PMC10138276 | gels-09-00324-g005.jpg |
0.429418 | 238db30b8a5d45279d8861e97ced10f0 | Location of Maharashtra State of India | PMC10139831 | 43999_2023_23_Fig1_HTML.jpg |
0.420265 | 72b28891bfa24c63aded94a093eda834 | Onsite waste segregation of COVID-19 (Source: https://cpcb.nic.in/uploads/Projects/Bio-Medical-Waste/Poster1_covid.jpg) | PMC10139831 | 43999_2023_23_Fig2_HTML.jpg |
0.413056 | a55315ffef02493784fb288ea3d8db1a | Hazardous waste generated from the response to COVID-19 [18] | PMC10139831 | 43999_2023_23_Fig3_HTML.jpg |
0.426866 | f87d86017d6643a49cce6df4f1a57c10 | COVID19BMW Android Application by CPCB | PMC10139831 | 43999_2023_23_Fig4_HTML.jpg |
0.440585 | b51a393bc6b748d9b3c182bdb4ba651f | Bio medical waste generated in India in the year 2020 (Tonnes/Day) | PMC10139831 | 43999_2023_23_Fig5_HTML.jpg |
0.438389 | 75433d4c596f47458bbd300eb3268fbe | Bio Medical Waste Generated in India in year 2021 (Tonnes/Day) | PMC10139831 | 43999_2023_23_Fig6_HTML.jpg |
0.435557 | 79a40c62cb904394a1455659d0af1a51 | Change detection in BMW generation observed from 2020–2021 | PMC10139831 | 43999_2023_23_Fig7_HTML.jpg |
0.418344 | c06703fdbd3e4263a5171b3d164e5729 | Bio medical waste generated in Maharashtra State in year 2020 | PMC10139831 | 43999_2023_23_Fig8_HTML.jpg |
0.43494 | a5282f6ac5cc4139b33faddd8a51e2a3 | Bio medical waste generated in Maharashtra State in year 2021 | PMC10139831 | 43999_2023_23_Fig9_HTML.jpg |
0.455071 | f4ed105cb35142fe92bb1ac27a97ac18 | Oligomeric states of purified EspB1–332.A, 12% SDS-PAGE showing the purity of recombinant EspB1–332. B, SEC elution profile shows three broad peaks corresponding to higher order oligomer and plausible monomer population. Green and pink dashed lines show the peak fractions of the high molecular weight assemblies (Peak 1 and Peak 2) of secreted EspB, while yellow dashed line corresponds to the lower molecular weight peak fraction (Peak 3). C, SEC-MALS profile of EspB1–332 obtained after two-step purification. Blue trace denotes refractive index, black trace indicates the molar mass, and red trace represents the molar mass fit. D, negative staining TEM visualization of the three distinct peak fractions marked in the SEC profile. From left, Peak 1 indicates the presence of multiple fused ring-like oligomers that range from dimers to higher order associations. Bottom panel denotes two representative 2D class averages (enlarged from Fig. S2A) that show joined rings in the multiples of two and three, respectively. Next, Peak 2 comprises the most homogeneous distribution of oligomeric EspB1–332. Representative 2D class averages (enlarged from Fig. S2B) show the top and side views of ring-like EspB1–332. To the right is provided a visualization of Peak 3 that comprises open chain form of EspB1–332. Magnified 2D class averages (enlarged from Fig. S2C) indicate the flexible nature of these chain-like EspB. Scale bars indicate 10 nm. Cyan arrow marks the area of bending of the protein. White arrowheads have been used to highlight the different oligomeric assemblies in the raw micrographs. Lane 1, Ni-NTA purified protein; Lane 2, SEC purified protein fractions pooled; M, marker; MALS, multi-angle light scattering; SEC, size-exclusion chromatography; TEM, transmission electron microscopy. | PMC10140165 | gr1.jpg |
0.440187 | bcafd24603dd4f81a8420a69d3520db9 | Single-particle cryo-EM structure determination of secreted EspB.A, cryo-EM raw micrograph showing a biased orientation distribution of EspB1–332 in amorphous ice. Adjacent 2D class averages show only top views of the protein. A minor subset of particles (marked yellow) illustrates the presence of hexameric EspB1–332 in a predominantly heptameric population. Scale bar denotes 5 nm. B, cryo-EM raw micrograph represents the effect of ∼0.03% fluorinated octyl maltoside on the orientation distribution in amorphous ice. Adjacent 2D class averages show the appearance of side views and tilted along with the previously observed top views. Scale bar denotes 5 nm. C, 3D density map of EspB1–332 resolved at 4.5 Å reveals strong agreement with the atomic model derived from full-length EspB1–460 (PDB ID 6XZC). Upper panel shows the cryo-EM structure where each monomer is colored differently to highlight the heptameric assembly of the N-terminal domain. The density corresponding to the C-terminal which could not be observed in our map has been traced by dashed red boundary. Transparent rendition of the cryo-EM structure in the bottom panel shows the quality of fitting of the secondary structures into the density map. | PMC10140165 | gr2.jpg |
0.474225 | aff636d322b04e07bad3289e5671fcfb | Lipid-binding affinity of C-terminal–processed EspB1–332.A, left, a representative negative staining raw micrograph of EspB1–332 incubated with liposomes made of Escherichia coli total cell extract and enlarged view of the top left corner. White boxes are used to denote the protein and cyan arrows show the boundary of the TCE membrane devoid of any EspB1–332 particles. Right, a representative negative staining raw micrograph of EspB1–332 incubated with liposomes made of phosphatidylcholine and cholesterol in equimolar ratio and enlarged view of the bottom left corner. White boxes are used to denote the protein and cyan arrows show the boundary of the PC-Chol membrane devoid of any EspB1–332 particles. B, 12% SDS-PAGE following TCE and PC-Chol liposome sedimentation assay. Pellet fraction is denoted by P and supernatant is denoted by S. C, negative staining raw micrograph of EspB1–332 incubated with phospholipid phosphatidylserine. Yellow arrows indicate the EspB1–332 oligomers that appear to bind plausible lipid architecture. D, fluorescence-based binding assay shows binding affinity of EspB1–332 with PS molecules, detected in MST mode. E, negative staining raw micrograph of EspB1–332 incubated with phospholipid phosphatidic acid. Yellow arrows indicate the EspB1–332 oligomers that appear to bind plausible lipid architecture. F, fluorescence-based binding assay shows binding affinity of EspB1–332 with PA molecules, detected in MST mode. Data presented here are mean ± SD from two independent sets of protein purification. MST, microscale thermophoresis; PA, phosphatidic acid; PC-Chol, phosphatidylcholine-cholesterol; PS, phosphatidylserine; TCE, total cell extract. | PMC10140165 | gr3.jpg |
0.360737 | bb02700fc53147659668861cc7e186cf | PA and PS binding initiates conversion of EspB1–332monomers to oligomers.A, thermal melt spectra of EspB1–332 monomers and heptamers in the presence and absence of PA and PS. Cyan line denotes EspB1–332 heptamer, red line denotes EspB1–332 monomer, gray dashed line denotes only PA, navy blue line denotes EspB1–332 heptamer with PA, purple line denotes EspB1–332 monomer with PA, yellow dashed line shows only PS, green line shows EspB1–332 heptamer with PS, and green line shows EspB1–332 monomer with PS. B, NS-TEM raw micrograph of monomeric fraction of EspB1–332. C, NS-TEM raw micrograph of EspB1–332 monomer with phosphatidylserine. Oligomers are shown within white circles, and monomers are highlighted with white arrowheads. D, NS-TEM raw micrograph of EspB1–332 monomer with phosphatidic acid. Oligomers are shown within white circles, and monomers are highlighted with white arrowheads. E, cryo-EM raw micrograph of EspB1–332 monomer with phosphatidic acid. Yellow arrowheads denote oligomeric side-views adhered to PA vesicles, and monomers are highlighted with white arrowheads. Adjacent cryo-EM 2D class averages show a predominance of heptameric oligomers over hexameric oligomers (marked yellow) upon PA incubation. Scale bar denotes 5 nm. NS-TEM, negative staining transmission electron microscopy; PA, phosphatidic acid; PS, phosphatidylserine. | PMC10140165 | gr4.jpg |
0.442913 | da50fbabe61740169acd054f5f7651a8 | Secreted EspB adheres to membrane bilayer formed by phosphatidic acid.A, cryo-EM raw micrographs (left-hand and center panels) from two different fields show preferential attachment of EspB1–332 heptamers on the PA vesicle surface. For clarity, an enlarged view of the central panel is presented in the third image panel (right), and yellow arrowheads have been used to pinpoint the side views of the protein attached on the membrane surface. Reference-free 2D class averages show different orientations of the heptamers. Particular top and side views have been highlighted because of the appearance of a fuzzy density at the bottom of the channel. Scale bar denotes 5 nm. B, 3D density map of EspB1–332 resolved at 6.6 Å indicates coherence with the atomic model derived from full-length EspB1–460 (PDB ID 6XZC). Upper panel shows the cryo-EM structure where each monomer is colored differently to highlight the heptameric assembly of the N-terminal domain. The additional density visible in the bottom view of the map has been colored green. Transparent rendition of the cryo-EM structure in the bottom panel shows the absence of modeled coordinates that could fit into the bottom density marked transparent green. C, transparent rendition of the electron density map where a single monomer has been colored blue. Monomer derived from the cryo-EM map has been used to show the prominent domains – PE domain, helical tip, PPE domain, and the polyproline stretch. Transparent rendition of the monomer fitted with a single EspB chain from PDB 6XZC illustrates the flexible string of multiple prolines. D, different orientations of the magnified view of the additional density linked to the helical N-terminal domain. Black curved arrows have been used to show the flexibility of the polyproline stretch. Blue dashed line in the first panel shows a hypothetical trajectory of motion of the prolines to continue into the ∼22 Å–long extra density which could correspond to the C-terminal domain. PA, phosphatidic acid. | PMC10140165 | gr5.jpg |
0.458632 | b875c89706084ec688fbdc7410cac505 | Stabilization of the disordered C-terminal domain in the presence of lipid bilayer and plausible lipid-binding sites within the EspB1–332core.A, representation of the additional density (marked golden) in the PA-EspB1–332 cryo-EM map fitted with PDB 6XZC. B, tilted bottom view of the PA-EspB1–332 structure shows that the low-resolution bottom extra density is connected to the well-resolved N-terminal domain. Succeeding representations indicate that the proline-enriched loop may serve as the link joining the putative C-terminal domain (here, golden density) with the helical N-terminal assembly of EspB1–332. PA, phosphatidic acid. | PMC10140165 | gr6.jpg |
0.443237 | 3f95dc76bee8443bbb398a4cf1940b9b | Biophysical characterization of secreted isoform of EspB1–332in the presence of model membranes.A, negative staining raw micrographs show liposomes made of PC, phosphatidylethanolamine, PIP4, PA, PS, and CL. B, negative staining raw micrograph shows liposomes made of PC, phosphatidylethanolamine, PIP4, PA, PS, and CL covered by ring-like EspB1–332. C, 12% SDS-PAGE following model liposome sedimentation assay. Pellet fraction is denoted by P and supernatant is denoted by S. D, fluorescence-based binding assay shows binding affinity of EspB1–332 with PIP4 molecules, detected in MST mode. E, control Saccharomyces cerevisiae mitochondria observed under NS-TEM. F, NS-TEM raw micrograph showing three isolated mitochondria post incubation with EspB1–332. Two mitochondria (marked with cyan and yellow box) have been enlarged, in the top right and bottom left panels, where distinct islands of EspB1–332 binding can be observed (marked with yellow arrowheads). Bottom right panel is an enlarged representation of the bottom left panel. Data presented here are mean ± SD from two independent sets of protein purification. CL, cardiolipin; MST, microscale thermophoresis; NS-TEM, negative staining transmission electron microscopy; PA, phosphatidic acid; PIP4, phosphatidylinositol-4-phosphate; PS, phosphatidylserine. | PMC10140165 | gr7.jpg |
0.406087 | 9cf82176b69445d8bde7ef1a1caab4e8 | Proposed mechanism of EspB1–332binding to biological membrane. Schematic diagram illustrating a hypothetical basis for MycP1-processed EspB and host-membrane interaction. In brief, PA, PS, and/or PIP4 binding facilitates disorder to order transition in the low-complexity C-terminal domain. In figure, pink color has been used to denote PA molecules, green color has been used to denote PS molecules, and blue color has been used to denote PIP4 molecules. PA, phosphatidic acid; PIP4, phosphatidylinositol-4-phosphate; PS, phosphatidylserine. | PMC10140165 | gr8.jpg |
0.403074 | f8cd45dedcef498bb4b244d788b9d035 | Geographical locations of P. petiolosa samples. For names of the numbered positions and ecogeographic information see
Supplementary Table 1
. | PMC10140315 | fpls-14-1173489-g001.jpg |
0.427687 | 277946707631444da59d99b30e9b5269 | Multivariate statistical analysis of P. petiolosa from different geographic origins based on UPLC-MS profiles. (A) Score plot of principal component analysis. (B) Heatmap of 97 flavonoid components in P. petiolosa samples from different geographic origins; the heatmap colours indicate the concentration of each metabolite, from low (blue) to high (red). (C) The UpSet diagram shows the overlapping and origin-specific flavonoid components in P. petiolosa samples. | PMC10140315 | fpls-14-1173489-g002.jpg |
0.402995 | bac743d1d27c424eb30023708bad8bea | Multivariate statistical analysis of two groups of P. petiolosa based on the concentration of 47 common flavonoids. (A) Principal component analysis (PCA) score plot; (B) Orthogonal partial least square discriminant analysis (OPLS-DA) score plot; (C) results of permutation testing of the OPLS-DA model with 200 repetitions; (D) VIP score plot of the candidate flavonoids markers for P. petiolosa samples. | PMC10140315 | fpls-14-1173489-g003.jpg |
0.425738 | dc47c06997da4b03bdace879ac288e18 | Concentration variation of flavonoid markers in P. petiolosa from different origins. Y-axis unit is nmol/g. | PMC10140315 | fpls-14-1173489-g004.jpg |
0.4131 | ab969f1afefb4740895775fcaf91d17a | In vitro antioxidant activities and total flavonoid content of P. petiolosa samples from different geographical origins. (A) ABTS radical scavenging activity. (B) DPPH radical scavenging ability. (C) Ferrous ions chelating activity. (D) Total flavonoid content. Error bars indicate the standard error of the mean values. Different letters above the bars indicate significant differences (p < 0.05). | PMC10140315 | fpls-14-1173489-g005.jpg |
0.412967 | 0cc0249d0fc84dce9484da21cf0fec48 | Correlation among antioxidant activities and concentration of flavonoid markers. The red colour indicates the positive correlation, the blue colour indicates the negative correlation. The “×”sign indicates that the corresponding correlation is not statistically significant. | PMC10140315 | fpls-14-1173489-g006.jpg |
0.39327 | 29553cf4158a474aa9d6c81744dbc746 | Results of RDA analysis presenting the correlation between flavonoid markers and antioxidant activities and ecogeographic parameters in each sample. Seven ecogeographic parameters were studied: (ALT), longitude (LON), latitude (LAT), average precipitation (AP), temperature (AA), sunshine (AS) and relative humidity (AR). 13 flavonoid markers were included: (-)-catechin (Cat), naringenin chalcone (Nar), apigenin-7-glucuronide (Api-g), apigenin (Api), vitexin (Vit), miquelianin (Miq), tiliroside (Til), and (-)-gallocatechin (Gal), keampferol (Kea), quercetin (Quin), astragalin (Ast), quercitrin (Qurin), pinocembrin (Pin). | PMC10140315 | fpls-14-1173489-g007.jpg |
0.426744 | cc2f41f489e742fcbf54bd5ecda173de | Four swine carcasses were placed in each SBC pit, facing the same direction. | PMC10140975 | pathogens-12-00628-g001.jpg |
0.401979 | 8b38a17231174ac78a0313e88441abcf | Pathology of ASF-infected swine carcasses used in this study. (a) Hemorrhagic lymph node. (b) Enlarged hemorrhagic spleen. | PMC10140975 | pathogens-12-00628-g002.jpg |
0.409984 | 76fe3c886e444fbb882554febef009b3 | Spleen (a) and bone marrow (b) were extracted from buried swine carcasses. | PMC10140975 | pathogens-12-00628-g003.jpg |
0.417394 | 675b2147e11f403a8944631748b10f0d | Hemadsorption in ASF virus-infected cells. Arrow indicates HAD rosettes. | PMC10140975 | pathogens-12-00628-g004.jpg |
0.475744 | bf38162f24ec4046a50fb773102617ce | AntII S-parameter variation due to (a) I4, (b) W4. | PMC10079684 | 41598_2023_32364_Fig7_HTML.jpg |
0.464758 | b3788e31679f4ec38f223fbc063b5fc0 | The S-parameter of the AntII operates with (a) I6, (b) I7. | PMC10079684 | 41598_2023_32364_Fig8_HTML.jpg |
0.453982 | 00bbf75be0274963a9da064185a33c1f | The density of surface current (a) AntI, (b) AntII at 3.8 GHz. | PMC10079684 | 41598_2023_32364_Fig9_HTML.jpg |
0.495517 | 344fa7e754924229857ed48ae65209dd | Comparison of hydrogel-based 3D cell culture and traditional 2D culture (Bar = 200 μm). | PMC10080128 | fbioe-11-1136583-g001.jpg |
0.500038 | 580c685d2e974765b0ada0cb73923e6a | 3D culture system with hydrogels for microgravity research. | PMC10080128 | fbioe-11-1136583-g002.jpg |
0.427159 | 5d4e8cfc6acd4bceb068653dc2c19f16 |
Transport system of fatty acid oxidation in outer mitochondrial membrane and inner mitochondrial membrane[11,65]. Fatty acid β-oxidation is catalyzed by enzymes located in outer and inner mitochondrial membrane to form acyl-coenzyme A (CoA) in the participation with ATP and CoA. Carnitine palmitoyltransferase (CPT)-I promotes the conversion of acyl-CoA to acyl-carnitine that is transported to mitochondrial interior with the help of translocase on the intima of mitochondria. Under the catalysis of CPT-II, acylcarnitine releases carnitine, and then converted to acyl-CoA to enter β-oxidation. The CPT system with carnitine acyl-carnitine translocase play a vital part in the transport system for esterification of fatty acids through the mitochondrial membrane and CPT-II as a key rate-limiting enzyme for fatty acid β-oxidation. OMM: Outer mitochondrial membrane; IMM: Inner mitochondrial membrane; CACT: Carnitine acyl-carnitine translocase; CPT: Carnitine palmitoyltransferase; CoA: Coenzyme A. | PMC10080702 | WJG-29-1765-g001.jpg |
0.435631 | cdb7d4980bee4bfba3b02ef27877f1d5 |
Carnitine palmitoyltransferase-II inactivity in hepatocarcinogenesis. Disorder of lipid metabolism may be related to the pathogenesis of nonalcoholic fatty liver disease with malignant transformation of hepatocytes. AFP: Alpha-fetoprotein; CoA: Coenzyme A; CPT2: Carnitine palmitoyl transferase 2; FAO: Fatty acid oxidation; HCC: Hepatocellular carcinoma; VEGF: Vascular endothelial-derived growth factor. | PMC10080702 | WJG-29-1765-g002.jpg |
0.446234 | bfe4f694f6f24e36ab10c476bc439bbf | Midway peel test: changes in the plasma bisoprolol levels. This figure was reprinted from the article (Reference #4) with the author’s permission, and some parts were translated into English and reorganized. At approximately 4 h after the patch is removed after a single use, the plasma bisoprolol level gradually decreases | PMC10080838 | 13019_2023_2227_Fig1_HTML.jpg |
0.491054 | d377721c3f294de2891db3297432ea14 | Protocol for postoperative atrial fibrillation. One Bisono tape® patch (4 mg) is applied for symptomatic patients with a HR of ≥ 80 bpm. The patch is removed if the HR drops below 60 bpm. If POAF occurs again, the patch is reapplied. If the HR remains at > 140 bpm, another patch is added. If the above does not yield favorable results and symptoms persist, a continuous infusion of landiolol should be administered. HR: heart rate; bpm: beats per minute; POAF: postoperative atrial fibrillation | PMC10080838 | 13019_2023_2227_Fig2_HTML.jpg |
0.390506 | 87828756d910474ea4f49219a1b917b7 | Evaluation of DDR and cell cycle markers in human gastric specimens.A. Tabulated summary of IHC stainings indicating the number of premalignant (green) and malignant (blue) gastric lesions scored for each staining criterion. DDR/replication stress markers-53BP1, H2AX, pH2AX in red; Cell cycle regulators- p53, p16, p21 in purple.B. Summary of the stainings (DDR markers and the cell cycle regulation markers) in paired premalignant and malignant gastric lesions from gastric cancer patient8. PM= Premalignant gastric lesion, M= Malignant gastric lesion.C. Representative IHC images of paired premalignant and malignant gastric lesions from a gastric cancer patient (patient8) stained for DDR markers and cell cycle regulation markers, including H&E staining. Insets represent the zoomed area for each image. | PMC10081209 | nihpp-2023.03.27.534412v1-f0001.jpg |
0.400994 | db086c7a3af441ef94207a8cd7b6dd05 | Evaluation of DDR and cell cycle markers in a carcinogen-induced mouse model of gastric premalignancy and cancerA. Summary of dysplasia grade and staining pattern of proliferation marker ki67, DDR marker pH2AX, and cell cycle regulation markers (p53 and p21) in paired normal (grey), premalignant (green), and malignant (blue) gastric lesions of four MNU treated mice.B. Representative IHC images of the staining pattern of proliferation marker ki67, DDR marker pH2AX, and cell cycle regulation markers (p53 and p21) in paired normal, premalignant, and malignant gastric lesions of MNU treated mouse4 (dysplasia score 5). | PMC10081209 | nihpp-2023.03.27.534412v1-f0002.jpg |
0.424183 | 2abda30752894562a616cfdfc4657e66 | Aneuploidy correlates with DDR, H2AX expression, and replication stress in gastric cancer.A. Correlation plot between H2AX gene expression (log2(TPM+1)) and CIN25 score (DNA damage checkpoint expression) for the CCLE gastric cancer cell lines; R squared value and p-value calculated by simple linear correlation analysis.B. H2AX expression (log2(TPM+1)) between ‘No WGD (0)’ (grey) and ‘with WGD (1/2)’ (green) groups of gastric cancer cell lines available in the BROAD institute PRISM repurposing drug screen dataset; Difference between the H2AX expression is represented as the mean±S.D.; P-value calculated by unpaired t-test.C. Ploidy abnormalities scores for the five gastric cancer cell lines.D. Representative immunofluorescence images of pH2AX (red) and pKAP1 (green) stainings in untreated five gastric cancer cell lines and RPE1 cells (non-neoplastic cell line) representing intrinsic replication stress/double-stranded DNA breaks (DSBs); Nucleus stained with DAPI (blue).E. Quantification of data in D., expressed as mean fluorescence intensity per cell (MFI) ± S.D from the following number of cells- RPE1-718, AGS- 2080, HGC27, 1031, NUGC3- 2119, GSU- 2092, KE39- 577.F. Quantification of pH2AX staining in prexasertib (Chk1/2) dose-dependent induced replication stress in cell lines with ‘intrinsic low-replication stress’-RPE1, AGS (grey) and ‘intrinsic high-replication stress’- GSU, KE39 (red). Data expressed as mean fluorescence intensity (MFI) of pH2AX signal per cell ± S.D from the following number of cells- RPE1: Control-718, 0.2nM-888, 2.0nM-524, 20.0nM-570, 200.0nM- 350; AGS: Control-2080, 0.2nM-1487, 2.0nM-1996, 20.0nM-1211, 200.0nM- 1396; GSU: Control-2092, 0.2nM-3319, 2.0nM-4035, 20.0nM-2057, 200.0nM-2402; KE39: Control-577, 0.2nM-1004, 2.0nM-1022, 20.0nM-728, 200.0nM-958.G. Quantification of pKAP1 staining in prexasertib (Chk1/2) dose-dependent induced replication stress in cell lines with ‘intrinsic low-replication stress’-RPE1, AGS (grey) and ‘intrinsic high-replication stress’- GSU, KE39 (green). Data expressed as mean fluorescence intensity of pKAP1 signal per cell ± S.D from the following number of cells- RPE1: Control-718, 0.2nM-888, 2.0nM-524, 20.0nM-570, 200.0nM- 350; AGS: Control-2080, 0.2nM-1487, 2.0nM-1996, 20.0nM-1211, 200.0nM- 1396; GSU: Control-2092, 0.2nM-3319, 2.0nM-4035, 20.0nM-2057, 200.0nM-2402; KE39: Control-577, 0.2nM-1004, 2.0nM-1022, 20.0nM-728, 200.0nM-958.H. Representative immunofluorescence images of pH2AX (red) and pKAP1 (green) stainings in prexasertib (20nM) treated cell lines with intrinsic ‘low-replication stress’-RPE1, AGS, and intrinsic ‘high-replication stress’- GSU, KE39. | PMC10081209 | nihpp-2023.03.27.534412v1-f0003.jpg |
0.464019 | 7d5780d2b669483a81aa432d9205eadb | Gastric cancer with high ploidy abnormalities and elevated H2AX expression are more sensitive to DDR pathway inhibitors (Chk1/2 and Wee1)A. Correlation plot between aneuploidy score and PF-477736 (Chk1/2) sensitivity (log2 fold change) for the CCLE gastric cancer cell lines; Cell lines used in this study marked in red; R squared value and p-value calculated by simple linear correlation analysis.B. prexasertib (Chk1/2) sensitivity between ‘TP53 wt’ and ‘TP53 mut’ groups of gastric Cancer cell lines BROAD institute PRISM repurposing drug screen dataset; Difference between the prexasertib (Chk1/2) sensitivity (log2 fold change) is represented as the mean±S.D.; P-value calculated by unpaired t-test.C. PF-477736 (Chk1/2) sensitivity between ‘No WGD (0)’ (grey) and ‘with WGD (1/2)’ (green) groups of gastric cancer cell lines available in BROAD institute PRISM repurposing drug screen dataset; Difference between the PF-477736 (Chk1/2) sensitivity (log2 fold change) is represented as the mean±S.D.; P-value calculated by unpaired t-test.D. PF-477736 (Chk1/2) sensitivity between Low aneuploidy score (grey) and high aneuploidy score (red) groups of gastric cancer cell lines available in BROAD institute PRISM repurposing drug screen dataset; Difference between the PF-477736 (Chk1/2) sensitivity (log2 fold change) is represented as the mean±S.D.; P-value calculated by unpaired t-test.E. PF-477736 (Chk1/2) sensitivity between ‘low H2AX expressing’ (grey) and ‘high H2AX expressing’ (green) groups (log2(TPM+1)) of gastric cancer cell lines available in BROAD institute PRISM repurposing drug screen dataset; Difference between the PF-477736 (Chk1/2) sensitivity (log2 fold change) is represented as the mean±S.D.; P-value calculated by unpaired t-test.F. Dose-response curve of non-neoplastic cell line RPE1, Low replication-stress (grey)-AGS, and high replication-stress (blue)-KE39, GSU gastric cancer cell lines to indicated concentrations of prexasertib (Chk1/2); Best-fit IC50 scores are displayed; Data presented as mean±S.D. of four culture replicates at each indicated dose.G. Correlation plot between aneuploidy score and MK-1775 (Wee1) sensitivity (log2 fold change) for the CCLE gastric cancer cell lines; Cell lines used in this study marked in red; R squared value and p-value calculated by simple linear correlation analysis.H. MK-1775 (Wee1) sensitivity between ‘TP53 wt’ and ‘TP53 mut’ groups of gastric Cancer cell lines BROAD institute PRISM repurposing drug screen dataset; the difference between the MK-1775 (Wee1) sensitivity (log2 fold change) is represented as the mean±S.D.; P-value calculated by unpaired t-test.I. MK-1775 (Wee1) sensitivity between ‘No WGD (0)’ (grey) and ‘with WGD (1/2)’ (green) groups of gastric cancer cell lines available in BROAD institute PRISM repurposing drug screen dataset; Difference between the MK-1775 (Wee1) sensitivity (log2 fold change) is represented as the mean±S.D.; P-value calculated by unpaired t-test.J. MK-1775 (Wee1) sensitivity between low aneuploidy score (grey) and high aneuploidy score (red) groups of gastric cancer cell lines available in BROAD institute PRISM repurposing drug screen dataset; Difference between the MK-1775 (Wee1) sensitivity (log2 fold change) is represented as the mean±S.D.; P-value calculated by unpaired t-test.K. MK-1775 (Wee1) sensitivity between ‘low H2AX expressing’ (grey) and ‘high H2AX expressing’ (blue) groups (log2(TPM+1)) of gastric cancer cell lines available in BROAD institute PRISM repurposing drug screen dataset; Difference between the MK-1775 (Wee1) sensitivity (log2 fold change) is represented as the mean±S.D.; P-value calculated by unpaired t-test.L. Dose-response curve of non-neoplastic cell line RPE1, Low replication-stress (grey)-AGS, and high replication-stress (blue)-KE39, GSU gastric cancer cell lines to indicated concentrations of MK-1775 (Wee1); Best-fit IC50 scores are displayed; Data presented as mean±S.D. of four culture replicates at each indicated dose. | PMC10081209 | nihpp-2023.03.27.534412v1-f0004.jpg |
0.442779 | ec78dfe9a3d241f087e322ea3418dbc7 | Cumulative score of ploidy abnormalities predicts DDR pathway inhibitor response in gastric cancer cell lines.A. Heatmap table representing the correlation between the Cumulative score of ploidy abnormalities and prexasertib sensitivity for the CCLE gastric cancer cell lines. The scoring scheme is as follows: TP53 status: wt=1, mut=2; Aneuploidy score: 15 and less than 15=1, more than 15=2; High amplitude focal amplifications: 20 and less than 20=1, more than 20=2; Ploidy score: 2.5 and less than 2.5=1, more than 2.5=2; WGD: No WGD=0, WGD 1=1, WGD2=2; CIN25 score: 6.1 and less than 6.1=1, more than 6.1=2; H2AX Expression: 6 and less than 6=1, more than 6=2. R squared value and p-value calculated by simple linear correlation analysis.B. prexasertib (Chk1/2) sensitivity between three sub-ranged ‘Cumulative score of ploidy abnormalities’ groups of gastric Cancer cell lines BROAD institute PRISM repurposing drug screen dataset; Difference between the prexasertib (Chk1/2) sensitivity (log2 fold change) is represented as the mean±S.D.; L=low, M=medium, H=high; P-value calculated by unpaired t-test.C. Immunoblot of replication stress/DDR markers and tubulin as the loading control in the KE39 cell line (high intrinsic replication stress) treated with the indicated concentrations of irinotecan (SN38).D. Immunoblot of replication stress/DDR markers and tubulin as the loading control in the KE39 cell line (high intrinsic replication stress) treated with the indicated concentrations of prexasertib (Chk1/2).E. Proliferation of the KE39 cell line (high intrinsic replication stress) treated with vehicle (grey), 2.5 nM of SN38 (magenta), prexasertib (red), prexasertib+SN38 (pattered red), MK1775 (green), MK1775+SN38 (pattered green); Light shade of color- 1.0nM of DDR inhibitor; Dark shade of color- 5.0nM of DDR inhibitor; All treatments for 48 hrs.F. Immunoblot of pKAP1, pRPA32, and tubulin as the loading control in KE39 cell line (high intrinsic replication stress) treated with monotherapy- SN38 (2.5nm), prexasertib (5nM), MK1775 (5nM) or combination therapy- SN38 (2.5nM)+prexasertib (5nM) and SN38 (2.5nm)+MK1775 (5nM). | PMC10081209 | nihpp-2023.03.27.534412v1-f0005.jpg |
0.375894 | cb8bfd72f4bf437093b3d387acf1cc15 | Suspended drop crystallization(a) A support-free EM grid is clipped into an autogrid cartridge and mounted between the arms of the suspended drop screening tool. The sample and crystallization solution are dispensed onto the grid. (b) The chamber is immediately sealed to allow vapor diffusion. (b) The incubation chambers are inserted into a screening tray for efficient storing and monitoring of crystallization progress by light, fluorescence and UV microscopy. (d) EM grids containing crystals are retrieved from the screening tool and frozen. (e) The specimen is then interrogated by MicroED or other methods such as tomography, x-ray crystallography, or general microscopy. FIB milling is optional depending on the application. | PMC10081258 | nihpp-2023.03.28.534639v1-f0001.jpg |
0.554888 | 98eba0de02bb4e5d9f1af7d66250f8a8 | MicroED structure of suspended drop Proteinase K(a) The suspended drop viewed from the top and imaged by (b) Light microscopy or (c) UV. A frozen suspended drop specimen was loaded into the FIB/SEM and imaged normal to the grid surface by (d) SEM and (e) iFLM with the 385 nm LED to locate submerged crystals. (f) The targeted crystal site was milled into a 300 nm thick lamella. (g) Example of MicroED data acquired from the crystal lamella. The highest resolution reflections visible to 2.1 Å (red arrow). Resolution ring is shown at 2.0 Å (blue). (H) Cartoon representation of the Proteinase K colored by rainbow with blue N terminus and red C terminus. The 2mFo–DFc map of a selected alpha-helix is highlighted, which was contoured at 1.5 σ with a 2-Å carve. | PMC10081258 | nihpp-2023.03.28.534639v1-f0002.jpg |
0.497055 | 5bc1b7243e464cf1915ae86ab91fee23 | Interhospital air transport of an adult with COVID-19 using ECMO, in
the “in-flight” phase. | PMC10081626 | 1980-220X-REEUSP-56-e20210432-gf02.jpg |
0.430002 | c3f8349a8cd647b58bc3f82f64f71389 | (A–C) Scatter plots illustrating correlation between the FCV-19S and DASS-21 subscales. (A) FCV-19S versus stress subscale. (B) FCV-19S versus anxiety subscale. (C) FCV-19S versus depression subscale. DASS-21 = Depression, Anxiety, and Stress scale, FCV-19S = Fear of COVID-19 Scale. | PMC10081927 | medi-102-e33487-g001.jpg |
0.454228 | 05adf0dfd34f461ea80e904e07632f76 | Principle of fluorescence anisotropy assay. The fluorescent probe DPH is excited by light which is polarized by a polarization filter in vertical position. When the probe is in a fluid surrounding, e.g. a membrane, it rotates and the emitted light is depolarized. When the membrane gets more viscous the rotation is attenuated and the emitted light is more polarized. The fluorescence intensity is measured by applying parallel and perpendicular polarization filters to the excitation light plane | PMC10082490 | 10020_2023_644_Fig1_HTML.jpg |
0.471912 | 8276d6b7bcde4fe9a39a4f8183314d57 | Fluorescence anisotropy of untreated PBMC (control) and after treatment with 1 µM cortisol, 50 µg/ml Ze 117 and combination of 1 µM cortisol with 50 µg/ml Ze 117 using 2.5 µM DPH. Results of five independent experiments are presented as mean ± standard deviation. *Marked values are significantly different from corresponding control with p < 0.05 (**p < 0.01, ***p < 0.001, ****p < 0.0001) determined by one-way ANOVA (n = 5), followed by Holm-Šídák test | PMC10082490 | 10020_2023_644_Fig2_HTML.jpg |
0.472368 | 0eda957af562414e91ee5346f03ad8bc | Heatmap of z-scores of all analysed 890 lipid species calculated from average mol%-values generated by lipidomics. Main lipid classes are given on the x-axis (CE cholesteryl ester, Cer ceramides, DAG diacylglycerols, Lyso lyso-phospholipids, PC phophatidylcholines, PC O phosphatidylcholine ethers, PE phosphatidylethanolamines, PE O phosphatidylethanolamine ethers, PG phosphatidylglycerol, PI phosphatidylinositol, PS phosphatidylserine, SM sphingomyelin, TAG triacylglycerides) | PMC10082490 | 10020_2023_644_Fig3_HTML.jpg |
0.431654 | 85add00b4ccc4ccc96c80574197abf84 | Average chain length and average number of double bonds of phosphatidylcholines (PC) and phosphatidylethanolamines (PE) of PBMC after cortisol and cortisol/Ze 117 preincubation, respectively. For statistical evaluation the cortisol condition was compared to the control. Average chain length and average number of double bonds of cortisol/Ze 117 pre-treated cells were compared to the cortisol condition. *Marked values are significantly different from corresponding control with p < 0.05 (**p < 0.01, ***p < 0.001, ****p < 0.0001) determined by one-way ANOVA (n = 4), followed by Holm-Šídák test | PMC10082490 | 10020_2023_644_Fig4_HTML.jpg |
0.414181 | ea3b8f5e510a4370b429a09839608745 | Average chain length and average number of double bonds of phosphatidylcholine ethers (PC O) and the phosphatidylethanolamine ethers (PE O) species after cortisol and cortisol/Ze 117 preincubation, respectively. For statistical evaluation the cortisol condition was compared to the control. Average chain length and average number of double bonds of cortisol/Ze 117 pre-treated cells was compared against the cortisol condition. *Marked values are significantly different from corresponding control with p < 0.05 (**p < 0.01, ***p < 0.001, ****p < 0.0001) determined by one-way ANOVA (n = 4), followed by Holm-Šídák test | PMC10082490 | 10020_2023_644_Fig5_HTML.jpg |
0.388597 | f529d14cbc4a4077961705da1c4b93b6 | Average chain length and average number of double bonds of the lipid classes of phosphatidylglycerols (PG) and phoshpatidylinositols (PI) after cortisol and cortisol/Ze 117 preincubation, respectively. For statistical evaluation the cortisol condition was compared to the control. Average chain length and average number of double bonds of cortisol/Ze 117 pre-treated cells were compared with the cortisol condition. *Marked values are significantly different from corresponding control with p < 0.05 (**p < 0.01, ***p < 0.001, ****p < 0.0001) determined by one-way ANOVA (n = 4), followed by Holm-Šídák test | PMC10082490 | 10020_2023_644_Fig6_HTML.jpg |
0.417898 | 2f42eb53bb4e498495fb374d29c51894 | Average chain length and average number of double bonds of the lipid classes of ceramides (Cer) and phoshpatidylserines (PS) after cortisol and cortisol/Ze 117 preincubation, respectively. For statistical evaluation the cortisol condition was compared to the control. Average chain length and average number of double bonds of cortisol/Ze 117 pre-treated cells were compared with the cortisol condition. *Marked values are significantly different from corresponding control with p < 0.05 (**p < 0.01, ***p < 0.001, ****p < 0.0001) determined by one-way ANOVA (n = 4), followed by Holm-Šídák test | PMC10082490 | 10020_2023_644_Fig7_HTML.jpg |
0.477396 | 902b0bb6be3f451ba2a7d70e82cb33f5 | On the phylogenetic tree, sample numbers are marked with following colors: green numbers signify the samples that were collected in 2020, blue numbers signify the samples that were collected in 2021 and red numbers signify the samples that were collected in 2022 | PMC10082655 | AIM-31-57-g001.jpg |
0.428816 | bb44981ec2644002ae927208e032d9a2 | Clinical prognostic value of OSGIN2 in gastric cancer and its proliferative effect in vitro. | PMC10082810 | 41598_2023_32934_Fig1_HTML.jpg |
0.443231 | 24c5874ed6f44646bdad585b2ed5c94a | OSGIN2 is highly expressed in gastric cancer and indicates poor prognosis (A) Differential expression of OSGIN2 in TCGA pan-cancer. The results show increased expression of OSGIN2 in various tumor tissues. (B,C) Differences in the expression of OSGIN2 in TCGA-STAD. The results suggest higher expression of OSGIN2 in gastric cancer than in normal tissues. (D) The expression of OSGIN2 is higher in gastric cancer TNM stage I-IV than normal tissue. (E) RT-qPCR detection of differences in OSGIN2 expression in various cells. (F) The differences in the expression of OSGIN2 in different tissues were obtained from the tissue immunohistochemical results of the HPA public database, which shows high expression of OSGIN2 in gastric cancer tissues compared with normal tissues. (G–I) Prognostic analysis of OSGIN2 by KM database shows that high expression of OSGIN2 in three different gastric cancer microarray data indicates poor prognosis. ns p ≥ 0.05; * p < 0.05; ** p < 0.01; *** p < 0.001. | PMC10082810 | 41598_2023_32934_Fig2_HTML.jpg |
0.383814 | add7bbed2f364acf826ed76c3830d6ad | Single Gene Expression Correlation Analysis (A) The top 50 coding genes that are positively correlated with the expression of OSGIN2 at the mRNA level are obtained from STAD data in the TCGA database. (B) The top 50 coding genes that are negatively correlated with the expression of OSGIN2 at the mRNA level are obtained from STAD data in the TCGA database. (C) Using the STRING database to predict the protein–protein interaction network (PPI network) of OSGIN2. ns p ≥ 0.05; * p < 0.05; ** p < 0.01; *** p < 0.001. | PMC10082810 | 41598_2023_32934_Fig3_HTML.jpg |
0.435886 | d5537e4d6c9e47afbb1d3458356ea9d7 | Functional enrichment analysis of OSGIN2-related genes (A) GO + KEGG70–72 functional enrichment analysis of DEGs and visualization of bubble diagram. (B) GSEA enrichment analysis was performed on DEGs, and 10 datasets related to gastric cancer were selected to depict mountain maps for visualization. (C–K) Dataset-specific enrichment score results related to gastric cancer in GSEA enrichment analysis results. | PMC10082810 | 41598_2023_32934_Fig4_HTML.jpg |
0.454359 | a733231de5e544a7bf40e6fe09bf2427 | Correlation of OSGIN2 with immune infiltration (A) Lollipop diagram of the correlation between OSGIN2 and 24 types of immune cells. (B) The difference in the Infiltration fraction of 10 immune cells (Th2 cells, T helper cells, TCM, pDC, B cells, Mast cells, CD8 T cells, Th17 cells, TFH, and Cytotoxic cells) in the OSGIN2 high or low expression groups. (C–L) Correlation coefficient between the infiltration levels of the above 10 immune cells and OSGIN2 expression in gastric cancer. (M) Immune-related biomarkers correlate with OSGIN2 expression in multiple tumors. ns p ≥ 0.05; * p < 0.05; ** p < 0.01; *** p < 0.001. | PMC10082810 | 41598_2023_32934_Fig5_HTML.jpg |
0.48523 | 2e1147a503fe42c4b9a298cc7ab60f1f | Mutation information of OSGIN2 in gastric cancer (A,B) Mutation frequency and mutation type of OSGIN2 in gastric cancer, assessed using the cBioPortal database. (C) Specific sites where OSGIN2 is mutated and specific sites of phosphorylation and ubiquitination in GC patients. (D,E) Mutation types of OSGIN2 assessed in the COSMIC database. | PMC10082810 | 41598_2023_32934_Fig6_HTML.jpg |
0.40623 | 167eaff9c0a941e485f75a78f2881426 | Functional verification of proliferation and migration of OSGIN2-knockdown NUGC3 and HGC27 cells (A) Transfection efficiency of OSGIN2 siRNA. (n = 3) (B) Cell proliferation ability of OSGIN2-knockdown cells, analyzed by CCK8 assays. (n = 3) (C) Colony formation ability of OSGIN2-knockdown cells. (n = 3) (D) Migration capacity of OSGIN2-knockdown cells. (n = 3) (E) Cellular DNA replication activity of OSGIN2-knockdown cells, detected by EdU experiment. (n = 3) ns p ≥ 0.05, * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 vs si-NC group. | PMC10082810 | 41598_2023_32934_Fig7_HTML.jpg |
0.501855 | bb8b87114c8b4d2695061d6715d163c3 | The role of OSGIN2 on cell cycle regulation Cell cycle of OSGIN2-knockdown NUGC3 and HGC27 cells. (n = 3). | PMC10082810 | 41598_2023_32934_Fig8_HTML.jpg |
0.439119 | d6c032f350f64909bc08c2818feb717f | MRI T2/FLAIR sequencing demonstrating hyperintensity in the dorsal medulla and floor of the fourth ventricle in the region of the area postrema. Yellow circles – area postrema. Green ovals – abnormal FLAIR signal within superior cerebellar peduncles. | PMC10084536 | 10.1177_20542704231159601-fig1.jpg |
0.450524 | 39bacdaf6f6745d29dcd047da78b6059 | Pathogenesis of PFO related neurological disorders. | PMC10084837 | fneur-14-1129062-g0001.jpg |
0.419471 | 99bd392e4ca24deb8000c4804258480e | ROC curves of different methods on the early PD vs. HC classification.SN1 = sliding-window-based networks (with window length of 1000, step length of 500); SN2 = sliding-window-based networks (with window length of 1000, step length of 1000); SN3 = sliding-window-based networks (with window length of 500, step length of 500); MN = microstate-window-based networks; MCN = microstate-class-window-based networks. | PMC10086042 | 41531_2023_498_Fig1_HTML.jpg |
0.425132 | 1e8ad3901f0047ec9dde628fbabe41dc | Topological distribution of temporal variability.The red points indicate the positions in which the temporal variability of microstate functional connectivity networks in healthy controls are obviously higher than that in early PD patients, and the blue points represent the positions that have lower temporal variability in healthy controls. The large points represent significant group difference (p < 0.01, FDR corrected), and the small points indicate p < 0.05 with FDR corrected. | PMC10086042 | 41531_2023_498_Fig2_HTML.jpg |
0.456094 | 945c036f61b840f3ae23ffb1ba3ed6aa | Topological distribution of spatial variability of microstate functional connectivity networks (averaged over the subjects) for both groups and their differences in the four-microstate networks.The red points indicate the positions in which the spatial variability of microstate functional connectivity networks in healthy controls are obviously higher than that in early PD patients, and the blue points represent the positions that have lower spatial variability in healthy controls. The large points represent significant group difference (p < 0.01, FDR corrected), and the small points indicate p < 0.05 with FDR corrected. | PMC10086042 | 41531_2023_498_Fig3_HTML.jpg |
0.420259 | a91bb6694cc9485aa2033ffe99e69431 | The temporal and spatial variability of whole brain microstate functional connectivity networks in patients with early PD and healthy controls, respectively.The green, blue, yellow, and red boxes represent functional connectivity networks of microstate class A–D, respectively. The box plot on the left of each pair represents healthy controls and the box plot on the right represents patients with early PD. * indicates a statistical difference with p < 0.05 and ** indicates a statistical difference with p < 0.01. FDR correction has been performed for p-values. Each dot represents every single subject. The horizontal line within the box indicates the median, box limits represent the upper and lower quartiles, and the whiskers indicate the range of values within 1.5 times the interquartile range. | PMC10086042 | 41531_2023_498_Fig4_HTML.jpg |
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