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0.395418 | 21207a6897c344c88a93775acd204d3a | Receiver operating characteristic (ROC) curve of the SARC-F score for screening sarcopenia. (A) The ROC curve of the SARC-F score for screening sarcopenia in NDD-CKD patients. (B) The ROC curve for screening sarcopenia at each cutoff point for NDD-CKD patients. (C) The ROC of the SARC-F score for screening sarcopenia in MHD patients. (D) The ROC curve for screening sarcopenia at each cutoff point for MHD patients. | PMC10391647 | fmed-10-1188971-g001.jpg |
0.502242 | 1151d0924f1a45a7a8be9e7df86cb8ab | Effect of various metal ions on α-amylase production | PMC10391895 | 12934_2023_2139_Fig10_HTML.jpg |
0.483744 | dd84a2397dbe4946beade8a2e701815b | Pareto chart showing positive significant and negative significant factors affecting α-amylase production by Bacillus cereus. B = glucose *, E = peptone*, F = (NH4)2 SO4*, H = KCl*, J = MgSO4*, K = CuSO4, and L = tween 80. * Refers to significant parameters | PMC10391895 | 12934_2023_2139_Fig11_HTML.jpg |
0.447661 | 53a51aea3bbd4c18804f494829bc359a | Contour plot shows interaction between glucose and (NH4)2SO4 | PMC10391895 | 12934_2023_2139_Fig12_HTML.jpg |
0.428896 | 9e61eeba23e84824b3b2701adc024328 | Contour plot shows interaction between peptone VS (NH4)2SO4 | PMC10391895 | 12934_2023_2139_Fig13_HTML.jpg |
0.452238 | 96999c3f9f3c4b9ea01b24bd85e7f79a | Contour plot shows interaction between (NH4)2SO4 Vs MgSO4 | PMC10391895 | 12934_2023_2139_Fig14_HTML.jpg |
0.410129 | 75890cd95314478382ebe81800acc04f | Contour plot shows interaction between MgSO4 Vs glucose | PMC10391895 | 12934_2023_2139_Fig15_HTML.jpg |
0.430172 | 2ebea69284d04f368163766b73929783 | Contour plot shows interaction between glucose Vs peptone | PMC10391895 | 12934_2023_2139_Fig16_HTML.jpg |
0.430411 | 585b559accd14621aebd1a8d1b27bf90 | Contour plot shows interaction between (NH4)2SO4 and peptone | PMC10391895 | 12934_2023_2139_Fig17_HTML.jpg |
0.48624 | 7959fcfe6417495ab5131b2cc0edc8a2 | SDS-page gel electrophoresis zymogram of extracted α-amylase, Lane M: Molecular weight standard proteins, Lane 1: crude enzyme fraction, Lane 2: chilled ethanol fraction, Lane 3: Ammonium Sulphate fraction | PMC10391895 | 12934_2023_2139_Fig18_HTML.jpg |
0.431157 | 4d320b7b38df4eb38d60e61e4bdc32af | Optical density of biofilm values of P. aeruginosa isolate before and after treatment with commercial and purified α-amylase | PMC10391895 | 12934_2023_2139_Fig19_HTML.jpg |
0.437807 | 7c7e7c7e00fd4b9b811c5537d807c115 | Starch hydrolysis test of isolated Bacillus spp. showing halo zone around colonies | PMC10391895 | 12934_2023_2139_Fig1_HTML.jpg |
0.409596 | 7e75318876a54c24a63fae7e48c1dc6b | P. aeruginosa biofilm thickness before and after treatment with commercial and purified amylase | PMC10391895 | 12934_2023_2139_Fig20_HTML.jpg |
0.404062 | e45e9eaabb76487b9a163d3024a7cf32 | Live/dead cells percentage before and after treatment of P. aeruginosa biofilm samples in chamber slides with commercial and purified amylase | PMC10391895 | 12934_2023_2139_Fig21_HTML.jpg |
0.434246 | 9029d817689e47558ec147d85e7ad8a2 | P. aeruginosa biofilm stained with acridine orange/propidium iodide florescent dyes before and after treatment with either commercial or purified α-amylase enzyme. (A) CLSM images of a untreated control biofilm showing that 98% of the biofilm was live appeared as green due to acridine orange dye that stain viable bacterial cells, b purified amylase-treated biofilm presenting 83% of the biofilm was red due to dead cells, and (c) following treatment with commercial α-amylase enzyme where 80% of the biofilm was red. (B) 3D images of control and treated biofilm showing a biofilm thickness of the test strain measuring 250 um while dramatically reduced biofilms were those treated with b purified α-amylase and (c) commercial α-amylase. The 3D images were analyzed by Image j software | PMC10391895 | 12934_2023_2139_Fig22_HTML.jpg |
0.401043 | 8aeb3339277f4e97a77901f7bc89270c | Microscopic visualization of Bacillus cereus examined under light microscope | PMC10391895 | 12934_2023_2139_Fig2_HTML.jpg |
0.480466 | fae49666d3674050a4a7535118208049 | Phylogenetic analysis of B. cereus isolate depending on 16 s rRNA sequence homology using BLAST. It was noticed that B. cereus A1-5 was the closest strain to the test isolated species | PMC10391895 | 12934_2023_2139_Fig3_HTML.jpg |
0.439763 | 5b3b57d53ea14fe68abf29fde28964a7 | Effect of different fermentation media on α-amylase activity | PMC10391895 | 12934_2023_2139_Fig4_HTML.jpg |
0.421378 | 1444cd3f9de34b9888b33dae6c69fa80 | Effect of different fermentation time on α- amylase activity | PMC10391895 | 12934_2023_2139_Fig5_HTML.jpg |
0.414503 | f9d9f1dc45084b1488f2c4eec9f8c082 | Effect of different pH on α-amylase activity | PMC10391895 | 12934_2023_2139_Fig6_HTML.jpg |
0.4228 | da17cad4c6f040a69f758d83c576fe32 | Impact of various temperature degrees on amylase activity | PMC10391895 | 12934_2023_2139_Fig7_HTML.jpg |
0.468514 | 12061b11cd3e45a39b8a3f28bd7ebb6c | Effect of different carbon sources on α-amylase activity | PMC10391895 | 12934_2023_2139_Fig8_HTML.jpg |
0.452629 | 26e8509fad68442cb5f7d3e5bab1de42 | Effect of different nitrogen sources on amylase activity | PMC10391895 | 12934_2023_2139_Fig9_HTML.jpg |
0.459233 | 9c6dfbdb67f4455cb1cd0a676b863ea4 | Schematic diagram of TMTc-based correction strategy.A, structure of the set of 18-plex TMTpro reagents. Each reagent consists of a reporter region, a balancer region, and an amine-reactive group. During fragmentation, TMT-labeled peptides generate reporter ions, and frequently TMTc ions with neutral CO loss. B, TMTc-based correction strategy. TMT-labeled peptides can be quantified by both MS2 reporter ions and TMTc ions. In the quantified data matrices, the x-axis represents different channels, and the y-axis represents different proteins. The data are log transformed to derive average SD of TMT reporter– and TMTc-based matrices. Before the correction, the two SD values are vastly different because of ratio compression of report-based quantification. After correction, the two SD values become highly similar. The detailed correction steps are described in supplemental Figs. S1–S3. TMTc, complement TMT; TMT, tandem mass tag. | PMC10392608 | gr1.jpg |
0.469812 | 44debc2d2d774be9b3032f2972b6751a | Experimental strategy to evaluate and correct the 18-plex TMTpro data.A, schematic diagram of 18-plex TMTpro (TMT18) samples used in TMTc-based correction of reporter quantification. Escherichia coli peptides (1×, 3×, and 10×) were labeled and mixed with 100× of human peptides. The assignment of different amounts to the channels was largely random. However, the amounts of “1×” and “10×” were assigned to adjacent channels to minimize TMT channel crosstalk, since the impurity of TMT reagents often affects alternating channels. The 18 samples were then pooled together and analyzed by LC–MS/MS. B, experimental relative intensities quantified by TMT reporter ions in E. coli. C, experimental relative intensities quantified by TMTc ions in E. coli. The 18 TMTpro reagents lead to the quantification of nine TMTc channels because of some isobaric TMTc ions. D, experimental relative intensities of TMT reporter ions after TMTc-based correction. The error bars indicate the SDs of the analysis. TMTc, complement TMT; TMT, tandem mass tag. | PMC10392608 | gr2.jpg |
0.426792 | 29aee45095104bcdac0084323a68dd7c | Detergent-insoluble and whole proteome profiling from human AD brain samples.A, sample preparation of detergent-insoluble and whole brain proteome from AD cases and controls. B, total homogenate and the detergent-insoluble pellet (∼1 μg per sample) were analyzed by SDS-PAGE with molecular weight (MW) markers (kilodalton) followed by silver staining. C, TMT-LC/LC–MS/MS experiments for profiling detergent-insoluble and whole proteomes, in which the overlapped proteins and peptides are 7357 and 82,745, respectively. D, principal component analysis (PCA) of the top 1% variable proteins in detergent-insoluble proteome. E, heatmap showing the sample clustering with the top 1% most variable proteins in detergent-insoluble proteome. The expression levels were scaled by z-score for each protein. AD, Alzheimer's disease. | PMC10392608 | gr3.jpg |
0.450019 | 2fdfd01262444c35a82498bb79553d14 | Differential proteins and pathway enrichment analyses of detergent-insoluble brain proteome.A, meta-analysis workflow of the detergent-insoluble brain proteome from two studies. B, volcano plot showing DEPs. Each dot represents a protein showing log2(AD/CTR) and the −log10FDR between AD cases and controls. The cutoff was set as FDR <0.05 and log2FC >2 average SD that was calculated as the mean of intragroup SDs within five AD cases or five controls. C, pathways enriched in DEPs between AD cases and controls (FDR <0.05). Significance of pathway enrichment was performed using two-tailed Fisher's exact test with the Benjamini–Hochberg (BH) multiple testing correction. D, representative enriched PPI modules of DEPs. Each dot represents a protein, and the interaction is indicated by connected lines. AD, Alzheimer's disease; DEP, differentially expressed protein; FC, fold change; FDR, false discovery rate; PPI, protein–protein interaction. | PMC10392608 | gr4.jpg |
0.413184 | 81f27af7d09542fa895332df317397a5 | Enrichment factor analysis of detergent-insoluble brain proteome compared with the whole proteome.A, workflow of the enrichment factor analysis. B, histogram plot showing the enrichment factor distribution of identified proteins, which fits to a mixed model (two curves of normal distribution). The x-axis represents the logarithmic value of enrichment factors between insoluble and whole proteomes. C, venn diagram shows the overlap among significantly enriched proteins as well as upregulated and downregulated proteins in AD by the meta-analysis. D, heatmap showing enriched and upregulated DEPs (n = 84) in individual AD cases. E, boxplots showing the levels of some highly enriched proteins in the whole and insoluble proteomes. AD, Alzheimer's disease; DEP, differentially expressed protein. | PMC10392608 | gr5.jpg |
0.45676 | 7a690a42b1074a7fbd3b4ff45ab8998c | Validation of enriched proteins using five-step sequential centrifugation.A, workflow of sequential extraction protocol used to create detergent-insoluble fractions from a pooled AD brain sample. B, silver-stained SDS-PAGE gel of the total homogenate (input) and different insoluble fractions obtained from sequential centrifugation steps (∼1 μg per sample). C, schematic diagram showing the profiling of AD brain fractions. A total of six biological samples were used, including the total homogenate (input) and five insoluble fractions, each with three replicates. D, clustering analysis of the proteins identified with three replicates. E and F, examples of DEP distribution in the six samples. G, Western blot validation of Aβ enrichment in P1 and P5 in different samples (∼5 μg protein per sample except ∼10 μg of the input). Ponceau S staining of the blot indicated the loading level. Aβ, amyloid-beta; AD, Alzheimer's disease; DEP, differentially expressed protein. | PMC10392608 | gr6.jpg |
0.393457 | 0796283657d942288f67a975776a9ee9 | Characterization of BCL2 or BCLXL primed profile of sPCL. (A) BH3 profiling was performed exposing CD138 positive cells isolated from patient samples to BH3-derived peptides, values corresponded to the percentage of cytochrome c released and measured by flow cytometry. Bim peptide measures global priming, HRK peptide measures BCLXL dependence and PUMA 2A is an inert peptide. (B) Analysis of BCL2, BCL2/BCL2L1, BCL2/MCL1 and BCL2/BCL2L1+MCL1 mRNA seq expression according to venetoclax (300nM) cell death response in primary cells from sPCL (n=13). BCL2L1 is the BCLXL coding gene. (C) Analysis of BCL2L1, BCL2L1/BCL2, BCL2L1/MCL1, BCL2L1/BCL2+MCL1 mRNA seq expression according to A1155463 (300nM) cell death response in primary cells from sPCL (n=13). Correlation was assessed by Spearman test, p and r values are indicated. | PMC10393035 | fonc-13-1196005-g001.jpg |
0.44522 | efbef3b6acfe40fa9e373e83c593ea12 | DT2216 selectively degrades BCLXL in myeloma cells. (A) Immunoblot of VHL expression in HMCLs (n=10) and CD138 (+) sPCL (n=3). KARPAS 620 (K620) cell lysate was included as an internal control. Results are representative of 2 independent experiments (left panel). VHL relative protein levels were quantified, normalized to actin and plotted against DT2216 LD50 values. Correlation was assessed by Spearman test, p and r values are indicated (right panel). (B) HMCLs were treated for 48h by DT2216 as indicated. Cell lysates were analyzed by western blot for BCLXL and Actin expression. BCLXL protein levels were quantified using Actin as a loading control. Results are representative of 2 independent experiments. (C) HMCLs were treated by DT2216 (150nM) for the indicated times. Cell lysates were analyzed by western blot. Results are representative of 2 independent experiments. | PMC10393035 | fonc-13-1196005-g002.jpg |
0.446251 | 3c94fe6e403a4049ba53c4f6f4e1b06b | DT2216 induces apoptosis in myeloma cells through BAK and BAX activation. (A) Sensitivity to DT2216 and A1155463 correlates in myeloma cells. DT2216 LD50 values were plotted versus A1155463 LD50 values in 10 HMCLs (empty circles) and 4 sPCLs (sPCL1=square; sPCL6=circle; sPCL8=triangle and sPCL13=diamond). Correlation was assessed by Spearman test, p and r values are indicated. (B) BCLXL, BCL2 and MCL1 protein levels were analyzed by western blotting. KARPAS 620 (K620) cell lysate was included as an internal control. * DT2216 sensitive cells. (C) BCLXL, BCL2 and MCL1 protein levels were quantified and normalized to actin. DT2216 LD50 values were analyzed in function to relative protein levels and the protein ratio of BCLXL/BCL2, BCLXL/MCL1 and BCLXL/MCL2+BCL2. Correlation was assessed by Spearman test, p and r values are indicated. (D) NAN12 cells were treated by DT2216 for 15h, followed by an intracellular staining using an anti-cytochrome c mAb and analyzed by flow cytometry. The percentage of cells that released cytochrome c upon DT2216 is indicated. Results are representative of 2 independent experiments. (E, F) NAN12 and XG7 were treated for the indicated times with 15nM and 150nM DT2216, respectively. Cells were collected and analyzed by (E) western blotting or (F) stained with anti-BAK (G-317-2) and anti-BAX (6A7) mAb antibodies directed against their active forms. Results are representative of at least 3 independent experiments. (G) BCLXL Immunoprecipitation was performed in cell lysate from NAN12 cell line. Unbound proteins (OUT) were quantified and compared to total lysates (IN). Results are representative of 2 independent experiments. | PMC10393035 | fonc-13-1196005-g003.jpg |
0.396289 | 71195cbf2e614d4db1b1498612da8111 | Schematics of (A) a typical transmission type and (B) a typical reflection typeTHz-TDS system. The molecular structure of (C) L-2HG and (D) D-2HG. White, gray, red, and purple atoms represent H, C, O, Na atoms, respectively. The (E) experimental and (F) theoretical spectra of L-2HG. The (G) experimental and (H) theoretical spectra of D-2HG (Chen et al., 2017). | PMC10393043 | fbioe-11-1219042-g001.jpg |
0.443047 | 70b61b3b97cc405da9c3792ad9e36b06 |
(A) Vibration modes of absorption peaks of (a1-a4) L-2HG and (b1-b4) D-2HG. (a1) 0.769 THz, (a2) 1.337 THz, (a3) 1.456 THz, (a4) 1.933 THz, (b1) 0.760 THz, (b2) 1.200 THz, (b3) 1.695 THz, (b2) 2.217 THz. White, gray, red, and purple atoms represent H, C, O, Na atoms, respectively. Blue arrows indicate the vibrational direction of atom. Black dotted boxes refer to the dominant functional groups in the vibration modes. Red dashed boxes indicate the entire molecular vibrational ring. The molecular structure of L-2HG (B) before and (C) after the structure optimization. The yellow dashed boxes indicate the transfer of the proton (hydrogen atom) (Chen et al., 2017). | PMC10393043 | fbioe-11-1219042-g002.jpg |
0.48155 | 238c677aaa1f47c3b0ddf548e8bd72ec | THz spectra of RS-ibuprofen, (R)-(−)-ibuprofen, (S)-(+)-ibuprofen. The THz-TDS of (A) RS-ibuprofen, (B) (R)-(−)-ibuprofen, and (C) (S)-(+)-ibuprofen. (D–F). THz absorption spectra obtained by using (A–C) through fast Fourier transform. (G,H). (R)-(−)-ibuprofen and (S)-(+)-ibuprofen frequency points and amplitude information graphs, (I). The difference of the area under the absorption peak of 3.28 THz, (J). The difference in the absorption amplitude at the absorption peak of 3.28 THz and 2.65 THz. Error bars are labelled in each figure (Wang et al., 2021). | PMC10393043 | fbioe-11-1219042-g003.jpg |
0.420287 | 52cc24a6d7d94bb0b825b5494bfe709f | The crystal cells and the most relevant hydrogen-bonding interactions within the unit cell of (A) 2CPBI and (B) 4CPBI. The (C) theoretical and (D) experimental spectra of 2CPBI. The (E) theoretical and (F) experimental spectra of 4CPBI. The isolated-molecule motions of 2CPBI: (G) Out-of-plane twisting. (H) Out-of-plane bending. (I) In-plane rocking (Song et al., 2018). | PMC10393043 | fbioe-11-1219042-g004.jpg |
0.436966 | 9573e39970fc4faaa79a28ab5e1773bb | The scatter diagram of RDG versus sign (λ2)*ρ and RDG isosurface map corresponded to (A) Adenosine, (B) Thymidine, (C) Ribavirin, (D) Entecavir, respectively (Wang F. et al., 2022). (E) Waterfall plot showing terahertz absorption spectra of simvastatin from 90 to 390 K. The temperature increment between spectra is 10 K from 80 to 210 K and 290–390 K, and 5 K from 210 to 290 K. (F) Absorption coefficient at 0.5 THz, (G) absorption coefficient at 1.8 THz. Red dashed lines represent best fit linear plots. Gray vertical lines indicate the DSC derived phase transition temperatures of 230.9 and 270.7 K and separate the different polymorphic forms indicated by III, II, and I. Error bars represent standard errors reflecting both the uncertainty in sample thickness and the noise estimate based on the averaging data obtained from measurements of three samples, with 120 waveforms obtained at each temperature point per sample (Tan and Zeitler, 2015). | PMC10393043 | fbioe-11-1219042-g005.jpg |
0.388742 | 565308609dc844a09382906880e43565 |
(A) Comparison of (A) experimental and (B) theoretical THz spectra of form I of chlorpropamide. (B) Comparison of (A) experimental and (B) theoretical THz spectra of form Ⅲ of chlorpropamide (Fang et al., 2016). Molecular packing of (C) glucose anhydrate and (D) glucose monohydrate. (E) THz signatures of glucose anhydrate, monohydrate and their mixture in 0.8–2.2 THz (Yan et al., 2021). (F) Waterfall plot of THz absorption spectra of LC tetrahydrate at 25°C–100°C. (G) Variation of absorption coefficient of LC tetrahydrate with temperature at 1.66 THz (Gao et al., 2022). | PMC10393043 | fbioe-11-1219042-g006.jpg |
0.402147 | 168cfcf79f964dd0944c02768e7bfb7a |
(A) Variation of the normalized THz absorption peak area with the heating time at different temperatures. (B) Plot and fitting curves according to the contraction area equation (Gao et al., 2022). (C) The THz spectra of NFD-INA cocrystal form I (blue line), form II (green line) and their parent constituents, NFD (black line) and INA (red line) in the frequency range of 0.5–4.0 THz. The experimental (black curve) and calculated (red curve) THz spectra of (D) form I and (E) form II of NFD-INA cocrystal in the frequency range of 0.5–4.0 THz. The hydrogen bond networks (blue dash lines) of (F) form I and (G) form II for NFD-INA cocrystal (Wang P. F. et al., 2022). | PMC10393043 | fbioe-11-1219042-g007.jpg |
0.47765 | fe951925bace413cbe720e5a557a8ec8 | The calculated vibrational modes of (A) form I at 1.14 THz, (B) form II at 1.14 THz, (C) form I at 1.71 THz and (D) form II at 1.65 THz (Wang P. F. et al., 2022). (E) A ball-and-stick representation of a fragment of (phen)-(mes) cocrystal, demonstrating the presence of O−H···N and C−H···O bonds. (F) Spectra of phen (blue), mes (red) and (phen)-(mes) (green), following background slope subtraction. (G) The distortion of the hydrogen-bonded chain in (phen)-(mes) that results in the absorption peak at 1.2 THz is a combination of wagging motions of mes and phen components in each chain. The axes and directions of wagging motions are indicated. The chains propagate parallel to the crystallographic direction (Nguyen et al., 2007). | PMC10393043 | fbioe-11-1219042-g008.jpg |
0.482905 | 9791be749ed64dc3ab4521ba8ad5a4fc |
(A) THz absorption spectra of the reaction process of urea and uracil by cogrinding (0.2–1.2 THz range was taken for a clear view). (B) THz absorption intensity at 0.8 THz of the coground mixtures as a function of time. (C) Peak intensity at 26.8° of PXRD of the coground mixtures as a function of time. (D) THz absorption coefficient of the uracil−urea mixture around 0.8 THz varying with temperature. (E) THz absorption spectrum of the pellet in the frequency range from 0.5 to 1.0 THz recording the heating process from 20°C to 120°C. (F) Predicted representation of uracil−urea cocrystal structure based on DFT calculations. (G) Calculated vibration mode at 0.94 THz (Yang et al., 2014). (H) The refractive indices and (I) extinction coefficients of TCH in pure water, and (J) refractive indices and (K) extinction coefficients of TCH in pure milk in the region of 0.3–1.0 THz at 25°C (±0.1°C) (Qin et al., 2017). | PMC10393043 | fbioe-11-1219042-g009.jpg |
0.437886 | 0e76ef8d20ca45ff98eece5d4dd5c28d | Absorption coefficient of binary mixture (A) Pefloxacin fishmealfeeds, (B) Fleroxaxin fishmealfeeds. The best prediction model requires and predictions the concentration scatterdiagram (C) Pefloxacin fishmealfeeds, (D) Fleroxaxin fishmealfeeds (Cao et al., 2022). (E) THz absorption spectra of Scutellaria baicalensis of different origins (Liang et al., 2018). (F) THz absorbance spectra of the herbs (Zhang et al., 2018). | PMC10393043 | fbioe-11-1219042-g010.jpg |
0.434911 | 37bafacaae954c68bd7d09a445202b6b |
(A) Terahertz absorption map of three groups of Chinese herbal medicines. a. authentic Morinda officinalis How; b. fake Morinda officinalis How; c. authentic Stephania tetrandra S. Moore; d. fake Stephania tetrandra S. Moore; e. authentic Polyporus umbellatus Fr; f. fake Polyporus umbellatus Fr (Li R. K. et al., 2020). (B) Scattered scores plots PCA1 vs. PCA2 for the saffron and safflower data without S-G smooth. (C) Scattered scores plots PCA1 vs. PCA2 for the saffron and safflower data with S-G smooth. (D) Scattered scores plots PCA1 vs. PCA2 for two kinds of bezoar data without S-G smooth. (E) Scattered scores plots PCAl vs. PCA2 for two kinds of bezoar data with S-G smooth (Yang et al., 2019). | PMC10393043 | fbioe-11-1219042-g011.jpg |
0.437414 | 583fe3398d7f42e4976b17822e8e681f | ROC curves of the three herbal medicines: (A) Herba Solani Lyrati; (B) Herba Solani Nigri; (C) Herba Aristolochiae Mollissimae (Zhang H. et al., 2017). (D) THz absorption spectra of six kinds of samples (Zhang et al., 2020). (E) Absorption coefficient of different moisture contents. (F) Linear correlation between absorption coefficient and moisture content at 0.5 THz and 1.0 THz (Ma and Yang, 2017). Spectral features of (G) sulfapyridine and sulfathiazole and (H) tetracycline, coumaphos, and amitraz, in the THz frequency range 0.5–6.0 THz, as extracted from the THz transmission measurements performed using a 100 lm-thick GaP crystal in the EO detection (Massaouti et al., 2013). | PMC10393043 | fbioe-11-1219042-g012.jpg |
0.469983 | c29fc5dc0080480ab8548265ccf25ce4 | The comparison chart of test set obtained by applying (A) t-SNE-RF, (B) t-SNE-Naive Bayes model (NBM), (C) t-SNE-SVM and (D) t-SNE-XGBoost (Cao et al., 2021). Yellow point is FET and red point is ASF (E) 2D Feature by CMSE (F) 2D Feature by PCA (G) 3D Feature by CMSE (H) 3D Feature by PCA (Huang P. J. et al., 2020). (I) Plots of the dielectric loss tangent for AER-a, AER-a binding ERP-a (0.5 μg/ml), and AER-a binding ERP-a (1 μg/ml) at 1.1 THz. (J) Absorption coefficient of AER-a, AER-a binding ERP-a (0.5 μg/ml), and AER-a binding ERP-a (1 μg/ml) at 1.1 THz (Li et al., 2017). | PMC10393043 | fbioe-11-1219042-g013.jpg |
0.488999 | 5dad4d1bf9864c469f367679df7e4c3e | The preparation process of Protein A/G and protein A/G + IgG. (A) Schematic of protein A/G and protein IgG preparation process. Microscope images of samples (B) protein A/G and (C) protein A/G + IgG, respectively. The measured THz transmissions of the ASRs biosensors after (D) protein A/G and (E) protein A/G + IgG (Cheng et al., 2020). (F) Left characteristic polarization reflection spectra (RLCP), (G) Right characteristic polarization reflection spectra (RRCP), (H) polarization elliptical angle (PEA), and (I) polarization rotation angle (PRA) spectra of water, BSA solution and BSA added with 0.05 g/mL and 0.10 g/mL papain solutions, respectively (Zhang et al., 2022). Concepts of THz hydration: Shown are the concepts of THz defect (J) and THz excess (K). The former describes linear changes of THz absorbance with increasing solute concentration for biomolecules (yellow spheres) dissolved in water (blue) with disregard to hydration. The latter displays the non-linear behaviour of the concentration dependent absorption coefficient, thereby taking into account a dynamical hydration shell (dark gray spheres) for biomolecules (orange spheres) in water (blue) (Born and Havenith, 2009). | PMC10393043 | fbioe-11-1219042-g014.jpg |
0.420553 | 7fadcdf147194cb5a7c06e6f6e8f1606 | Best change in target lesions of 26 patients. #: This patient’s chest computed tomography scan showed micro-nodules scattered throughout the lungs which couldn’t be determined by the Response Evaluation Criteria in Solid Tumors version 1.1, but we found a significant reduction in his lung micro-nodules and a 91.4% reduction in thyroglobulin after follow-up, thus we considered a partial response. *: All three patients were found with new lesions. •:The two patients were died to pulmonary infection and bone related events, respectively. | PMC10393119 | fendo-14-1200932-g001.jpg |
0.462275 | aa6a4bd6a0314ff3bae4b0373f01eb65 | The Kaplan–Meier curve of PFS in 26 patients treated with sorafenib. CI, confidence interval; PFS, progression-free survival. | PMC10393119 | fendo-14-1200932-g002.jpg |
0.391362 | 762a59cc29d64b2a9e5d71eb7bf30e94 | Kaplan–Meier curves of PFS according to clinicopathological features. PFS, progression-free survival. | PMC10393119 | fendo-14-1200932-g003.jpg |
0.40513 | 577a9d5714e44617b34fb5993b518cfe | Comparison of chest computed tomography scans of typical cases. After 28, 46, and 17 months of sorafenib treatment, a significant reduction in the size of target lesions was observed in cases 1, 2, and 3, respectively. Chest computed tomography scans at baseline (A1 and B1) and the end of follow-up (A2 and B2) are shown above. The red arrows indicates the location of the target lesions at baseline and the last follow-up. | PMC10393119 | fendo-14-1200932-g004.jpg |
0.404966 | af623e79433d4adb9964b2a6ac221773 | Depression symptoms (Source: The University of Queensland, 2022). | PMC10394518 | frai-06-1230649-g0001.jpg |
0.508929 | ec95ec1961074edfaf44dc725ccdee02 | Text mining process (Source: Gaikwad et al., 2014). | PMC10394518 | frai-06-1230649-g0002.jpg |
0.51497 | 10d91e4a3aad44fa871285f89655bdce | The image mining process (Source: Shukla and Vala, 2016). | PMC10394518 | frai-06-1230649-g0003.jpg |
0.497949 | e83d3c5735804ad39311e0bbf5b2487c | Sentiment analysis process (Source: Babu and Kanaga, 2022). | PMC10394518 | frai-06-1230649-g0004.jpg |
0.458893 | 0c340a88642748a2a6742cd0f2655e5d | Before and after pre-processing. | PMC10394518 | frai-06-1230649-g0005.jpg |
0.427177 | 97e5b523b3834d8a9b8418892176972c | The most common words in the entire dataset. | PMC10394518 | frai-06-1230649-g0006.jpg |
0.415779 | 7b75e6b59b7d4b48bca26c87e86eaa32 | The most common positive words. | PMC10394518 | frai-06-1230649-g0007.jpg |
0.417997 | dbe221ebe6cd4ff199de1032f766aed1 | The most negative/depressed words. | PMC10394518 | frai-06-1230649-g0008.jpg |
0.456469 | 8c3e160121ad494096e37a755b600bf5 | Complete dataset before selection of columns. | PMC10394518 | frai-06-1230649-g0009.jpg |
0.372008 | 7bd9bd4ee7224282860ae3204a1d1f9b | Dataset after column selection. | PMC10394518 | frai-06-1230649-g0010.jpg |
0.43512 | 259c335c9f7b48f4a59d43cac34de3b2 | Confusion matrix (Draelos, 2019). | PMC10394518 | frai-06-1230649-g0011.jpg |
0.494198 | 7ca53cb8fb8d4b3a9b5ebdbad6887cff | Simplified XGB classifier (Wang et al., 2020). | PMC10394518 | frai-06-1230649-g0012.jpg |
0.466168 | 6a891dc658db4266b69b163848a85261 | Simplified random forest model (Wikipedia, 2023). | PMC10394518 | frai-06-1230649-g0013.jpg |
0.439116 | 18deda7534aa49a3995a889217380aa5 | Logistic regression model (Torres et al., 2019). | PMC10394518 | frai-06-1230649-g0014.jpg |
0.472178 | dc5ffb9c5719465d918e4c10c1341025 | Support vector machine model (JavaTpoint, 2011–2021). | PMC10394518 | frai-06-1230649-g0015.jpg |
0.467148 | 66e95f5e6ab64ab0ae670673e175aaec | Preferred reporting items for systematic reviews and meta-analyses (PRISMA) flow diagram of included and excluded studies. NEJM: New England Journal of Medicine; JAMA: Journal of the American Medical Association; LANCET: The LANCET; BMJ: British Medical Journal; Ann Intern Med: Annals of Internal Medicine; JAMA Surg: Journal of American Medical Association Surgery; Ann Surg: Annals of Surgery; J Neurol Neurosurg Psychiatry: Journal of Neurology, Neurosurgery and Psychiatry; Heart Lung: Journal of Heart and Lung Transplantation; Am J Transplant: American Journal of Transplantation; J Hepatobiliary Pancreat Sci: Journal of Hepato-Biliary-Pancreatic Science; Hepatobiliary Surg Nutr: Hepatobiliary Surgery and Nutrition; Eur J Vasc Endovasc Surg: European Journal of Vascular and Endovascular Surgery; Br J Surg: British Journal of Surgery; ICMJE: International Committee of Medical Journal Editors | PMC10394534 | JPGM-69-153-g001.jpg |
0.435103 | 66c58bfa66d74cb1a5ae96b95ff078eb | Themes of qualitative exploration. | PMC10394537 | bmjopen-2022-067652f01.jpg |
0.462403 | 5aecc36ca21a45e6b980d6d4a9f924d3 | Study Cohort Flowchart | PMC10398009 | jmcp-022-05-539_g001.jpg |
0.497376 | 4393deb8d627457b86f32ce0faa8b795 | Effects of 2 (left), 3 (middle), and 7 (right) on the
cell viability of MCF-7 breast cancer cells
obtained from MTT test. | PMC10398859 | ao3c04598_0001.jpg |
0.461189 | a61a415c2e734330b3b4c2e8c963d0ab | Subject screening and completion flowchart | PMC10398902 | 12905_2023_2566_Fig1_HTML.jpg |
0.453465 | e0bfcb39739b44d7ab3ec77af1d9a9ee | Flow chart of the search and selection process. RCT=randomized
controlled trial. | PMC10398958 | bjcvs-38-05-e20220350-g01.jpg |
0.430037 | 75f30775d4e6400486a5b636e93f6043 | Bias risk assessment figure. A) Percentage diagram of each bias risk
evaluation index. B) Bias risk assessment diagram of the included
literature. | PMC10398958 | bjcvs-38-05-e20220350-g02.jpg |
0.497408 | 1d0e1e88f89047b69023012c4c99230a | Forest plot showing the relationship between posterior pericardiotomy
(PP) and postoperative atrial fibrillation. CI=confidence interval;
M-H=Mantel-Haenszel. | PMC10398958 | bjcvs-38-05-e20220350-g03.jpg |
0.425152 | 9e1dce9a637345b2888e8e74c5035e79 | Subgroup analysis showing the effect of posterior pericardiotomy (PP)
on pericardial effusion in different stages after cardiac surgery.
CI=confidence interval; M-H=Mantel-Haenszel. | PMC10398958 | bjcvs-38-05-e20220350-g04.jpg |
0.461968 | e42b608c716947e3ac1e6c5426142d2a | Funnel plot to assess potential bias in the postoperative atrial
fibrillation part analysis. RR=risk ratio; SE=standard error. | PMC10398958 | bjcvs-38-05-e20220350-g05.jpg |
0.471228 | 7d17f09cafdc4352a0f8ee97a46e5a94 | This Aggressive group BCC involved the mimic muscles, resulting in extended resection of the right nasal ala, including the greater alar cartilage and a partial anterior wall of the maxilla. The nasal cavity and right maxillary sinus were exposed at the resection surgery. | PMC10399488 | ICRP_A_2242494_F0001_C.jpg |
0.47022 | 3f3fcfd34bdb4817a67b56ac030b309d | The lateral femoral circumflex artery and vein (LCFAV) was anastomosed with the facial artery and vein in an end-to-end manner, and the distal end of the descending branch was additionally anastomosed with the superficial temporal artery and vein. | PMC10399488 | ICRP_A_2242494_F0002_C.jpg |
0.447073 | e92bf94ef86a4b1ab1346ffc8a1bb0b3 | The flap was successfully taken and thinning of the flap was performed at 6 months after surgery in order to improve the shape of the nostrils and nasal ala. Further revision of the nasal configuration, including cartilage grafting, will be scheduled in the future. | PMC10399488 | ICRP_A_2242494_F0003_C.jpg |
0.533813 | da4cbe31cf5e457b9d6b83021036738a | Pathological images of the trichoepithelioma lesions are shown. | PMC10399488 | ICRP_A_2242494_F0004_C.jpg |
0.495064 | f10677edba82492c83cc63b4226971e5 | Pathological images of the basal cell carcinoma lesions are shown. | PMC10399488 | ICRP_A_2242494_F0005_C.jpg |
0.405402 | 3df711eeacd149038dfbd03a918e101b | Experimental environment.(A) Each pig was placed in a supine position on a surgical table. (B) The vital signs were continuously monitored and the electromyography (EMG) electrode, accelerometer, and vibration motor were attached to the tibialis anterior muscle of the right (control) and left (experimental) hind limb using straps. (C) A common iliac vein was identified in the retropelvic space (white arrow) for the left hind limb of the pig. | PMC10399817 | pone.0289266.g001.jpg |
0.378312 | ddcd5e8fe6c24ddcb078b3e410afd5c6 | The common iliac vein was tied using a rubber band to control the venous flow velocity (50% and 100% of baseline venous velocity).Lastly, the proximal thigh was also tied with an elastic band to block superficial veins around the inguinal area. | PMC10399817 | pone.0289266.g002.jpg |
0.492724 | b1ec47bbe6ee4237a237ba1722c1702f | Experimental protocol.The EMG and acceleration data were acquired at 1,000 Hz, immediately and 1 hour after venous flow control. | PMC10399817 | pone.0289266.g003.jpg |
0.42879 | b503726f776e48b6ac469a860fa01830 | The representative ultrasound images in each VC stage in the experimental leg.The red circle represents the common iliac vascular bundle, and the white graph (in the blue rectangle) the venous flow in the red circle. | PMC10399817 | pone.0289266.g004.jpg |
0.395602 | 0dc044b3a6424d50b985cdee6f528aba | Results in maximum velocity of CIV and pressure gradient at each stage related to VC of the pig legs.(A) The maximum velocities of the venous flow of the CIV between the control and experimental legs. (B) The pressure gradient between the control and experimental legs. Each box plot indicates the 25th (Q1), 50th (Q2), and 75th (Q3) percentiles of the data (**p < 0.01, and ***p < 0.001). The whisker indicates Q3 + 1.5 × (Q3 –Q1), and Q1 − 1.5 × (Q3 –Q1) and the dot indicates the outliers. | PMC10399817 | pone.0289266.g005.jpg |
0.426214 | 7f11968125df48988c1c64df62ff8f07 | Changes in muscle stiffness and muscle electrical activity between the experimental and control legs.(A) The changes in muscle stiffness across all VC stages in the experimental and control leg. The bold dark lines indicate the statistical differences between the experimental and control legs, whereas the solid lines indicate differences between the baseline (T0) and each VC stage in the experimental leg. The broken lines indicate the differences between the baseline and each of the VC stages in the control leg. (B) The changes in ΔIEMG (integral electromyography) across all VC stages with vibration. (C) The changes in ΔIEMG across all VC stages without vibration (*p < 0.05, **p < 0.01, and ***p < 0.001). | PMC10399817 | pone.0289266.g006.jpg |
0.387879 | e8d46709e23f434fba72aae2fef0451f | Profile of standard synthetic curve qPCR for TTV quantification. QuantStudio Design & Analysis Software v.1.4.1. Threshold of 0.0271. Titer TTV range of 0.38 to 8.11 log copies/mL. | PMC10400322 | fmed-10-1161091-g001.jpg |
0.523463 | b3398c0341954c4398e80a0ec041417b | Gestational age at delivery in pregnancies positive or negative for TTV in amniotic fluid. TTV in amniotic fluid was detected by gene amplification. Pregnancy outcome was subsequently obtained by chart review. Values are expressed as mean and 95% confidence intervals. The dot indicates the mean value. | PMC10400322 | fmed-10-1161091-g002.jpg |
0.499264 | 6d50165a65234057be43967b62173dd2 | Genetic features of TTV genomes. The upper panel (A) is the phylogenetic tree inferred using complete genomes of TTV. The tree indicates that there are multiple clades (indicated by distinct colors) composed by TTV identified in different countries. Sequences generated in this study are indicated in blue in the tree. Number at nodes are bootstrap values. Some clusters were collapsed to facilitate visualization (indicated in red). Clades with high bootstrap values are indicated in different colors. All sequences identified in AF from Brazilian patients grouped in a distinct cluster. The exception is the sequence OP882566 located in a unique branch. The lower panel (B) shows the genomic annotation of TTV identified in the current study. Circles represent the single stranded circular genome of TTV. Numbers within these circles indicate the nucleotide position and size. The magenta semi-circular arrows show the position of the predicted ORF1 based on TTV references. The start and end of orf1 are indicated by red arrows. Numbers inside rectangles are the nucleotide divergence of the ORF1 gene region between the TTV sequences. | PMC10400322 | fmed-10-1161091-g003.jpg |
0.408754 | a0383da0e5184b15bf4be719394b01b7 | Schematic illustration of the preparation and working principle of E-Para.a Preparation of MNPs@Ab. b The formation of VSO after engineering of Para using MNPs@Ab. c The proposed mechanism of virus capture and inactivation by E-Para. The virus capture by E-Para involves four processes: 1. Virus ingestion; 2. Formation of food vacuole containing virus; 3. Food vacuole fusion; 4. Virus capture by MNPs@Ab. The virus inactivation by E-Para was shown as 5. Virus inactivation. d Magnetic recovery of E-Para. | PMC10400550 | 41467_2023_40397_Fig1_HTML.jpg |
0.440674 | 03f5469d39274acc95a33016e3e037a7 | Construction and characterization of E-Para.a ELISA of MNPs@Ab confirmed the antibody conjugation. The data are presented as the mean ± sd (n = 3). b TEM image of MNPs@Ab and size distribution of MNPs@Ab (inset). c Magnetic hysteresis loops of MNPs@Ab and MNPs. d, e Optical microscopy d and TEM images e of the food vacuoles in natural Para. The highlighted vacuole area was enlarged. f, g Optical microscopy f and TEM images g of the food vacuoles of E-Para. The highlighted VSO area was enlarged. h Magnetic hysteresis loops for natural Para and E-Para. i For fabrication of E-Para, Para were cocultured with different concentrations of MNPs@Ab for 2 h. The obtained E-Para were then cultured in medium without feeding for another 24 h for toxicity evaluation. The data are presented as the mean ± sd (n = 3). j Speeds of natural Para and E-Para. The data are presented as the mean ± sd (n = 3). In i, j, statistical significance was calculated via two-tailed Student’s t test. P < 0.05 was considered significant. Ns not significant. | PMC10400550 | 41467_2023_40397_Fig2_HTML.jpg |
0.431791 | a495faa9e9224cb7b7e2f38e1012f092 | Virus capture by E-Para.a, b Phase and CLSM images of Para a and E-Para b after capturing the EV71. In vivo EV71 was localized by merging the phase and fluorescence images. Green represented CMFDA-labeled Para and red represented AF555-labeled EV71. c To confirm the virus capture capacity of MNPs, MNPs@Ab, Para, Para modified with MNPs (Para-MNPs), Para fed with antibody (Para-Ab) and E-Para, the remaining EV71 in the water was examined after coculturing the above samples with EV71 for 24 h. The data are presented as the mean ± sd (n = 3). Statistical significance was calculated via two-tailed Student’s t test. P < 0.05 was considered significant. Ns not significant. d Time-dependent virus capture by Para and E-para. The data are presented as the mean ± sd (n = 3). e Amount of viral genome remaining in EV71-contaminated water (1.5 × 105 copies/mL) after treatment with different amounts of Para and E-Para for 24 h. The data are presented as the mean ± sd (n = 3). f Amount of viral genome remaining in EV71-contaminated water (3.2 × 108 copies/mL) after treatment with different amounts of Para and E-Para for 24 hours. The data are presented as the mean ± sd (n = 3). g The of log10 reductions in viral genome levels were calculated after different volumes EV71 solutions were treated with E-Para or Para (6.4 × 104 cells/mL). h For generic virus removal, MNPs were modified by sialic acid (SA), which simultaneously grazed EV71, H1N1, and Ad5 from solution, reflecting the versatility of this strategy. The data are presented as the mean ± sd (n = 3). | PMC10400550 | 41467_2023_40397_Fig3_HTML.jpg |
0.372216 | d818f05bc2e54d0093e482ee23fb8f36 | Virus inactivation effects of VSO.a Intra-Para EV71 titer detected with the plaque-forming assay. b Inactivation efficiencies of MNPs@Ab, Para and E-Para. c Viral genome remaining inside E-Para or Para cells after treatment. d EPR spectra of MNPs@Ab at different pH values. e Comparison of the catalytic capacities of MNPs@Ab, natural Para and E-Para to TMB. f The dose-dependent catalytic capacity of E-Para. g Fluorescence images of Para and E-Para stained with ROSGreenTM (a H2O2 probe with green fluorescent). h H2O2 contents in Para and E-Para. i Fluorescence intensity of •OH measured by ImageJ. The data are presented as the mean ± sd (n = 3). j, k Fluorescence images of Para j and E-Para k stained with HPF (a •OH probe with green fluorescent). The images in the yellow boxes are partially enlarged (Bar, 20 μm). Statistical comparisons were made using either two-tailed Student’s t test (a, b, e) or two-way analyses of variance (ANOVA) with Tukey’s multiple-comparison test c. P < 0.05 was considered significant. Ns not significant. | PMC10400550 | 41467_2023_40397_Fig4_HTML.jpg |
0.446278 | 117f4347d8f146c49601d5905942714e | Magnetic directed recovery of E-Para.a Recovery of Para and E-Para with a magnet. The images were collected with a stereomicroscope. b Effect of incorporated MNPs@Ab concentration on magnetic recovery of the E-Para. The data are presented as the mean ± sd (n = 3). c Effect of solution volume on the magnetic recovery of E-Para. The data are presented as the mean ± sd (n = 3). d Reuse of E-Para. The data are presented as the mean ± sd (n = 3). In b, c and d, statistical significance was calculated via two-tailed Student’s t test. P < 0.05 was considered significant. Ns not significant. | PMC10400550 | 41467_2023_40397_Fig5_HTML.jpg |
0.469629 | 35737480bad341dba454ebfbe995ea2f | Pancancer expression pattern and prognostic significance of RNH1. (A) RNH1 expression levels in 19 cancer types based on the TCGA database. (B) RNH1 expression levels in 13 cancer types based on the TCGA and GTEx database. (C) The promoter methylation level of RNH1 in 15 cancer types based on TCGA cohorts of UALCAN database. (D) Total RNH1 protein expression levels in normal and primary tumour based on the CPTAC dataset from UALCAN. (E) The frequency of different RNH1 genetic alterations in different tumour types based on TCGA cohorts of cBioPortal. (F) Statistics associated with RNH1 mutation sites in different tumour types based on TCGA cohorts of cBioPortal. (G) Correlation between RNH1 gene expression and overall survival/disease-free survival in different tumour types in TCGA, assessed using GEPIA2. (H–I) Potential correlation between RNH1 alteration status and overall, and disease-free survival in pancancer, as analysed using the cBioPortal tool. ns no significant difference; *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001. | PMC10400633 | 41598_2023_39827_Fig1_HTML.jpg |
0.424616 | b0c54c50fdb44360bed021417ce2074b | RNH1 affects functional states in BLCA. (A–F) The differences in FUN scores between groups with high and low RNH1 expression based on TCGA (A), GSE31684 (B), GSE5287(C), GSE48057 (D), GSE48277 (E), and GSE69795 (F) datasets. (G–I)The expression of RNH1 (G), and the FUN score of both EMT (H) and invasion (I) were evaluated in different tissues based on GSE13507 datasets. (J) The differences in FUN scores between groups with high and low RNH1 expression based on the GSE13507 dataset. ns no significant difference; *p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001. | PMC10400633 | 41598_2023_39827_Fig2_HTML.jpg |
0.41276 | 70031d1534434f49bc8e001836153f0e | Identification of hub genes affecting functional status. (A) The clustering dendrogram of the WGCNA. (B) Sample dendrogram and 17 functional status trait heatmap. (C) Module-trait relationships. Each row represents a colour module and every column represents a functional status trait. Each cell contains the corresponding correlation and p value. Red represents a positive correlation and blue represents a negative correlation. (D) UpSet plot of overlapping hub genes of EMT, invasion, and differentiation traits. (E) For the overlapping 95 hub genes in the diagram (D), the associated BP, CC, and MF were investigated using GO enrichment analysis. | PMC10400633 | 41598_2023_39827_Fig3_HTML.jpg |
0.430047 | 53ead734aafa4c40a1525bee9b149fbb | Unsupervised clustering of BLCA using 95 hub gene expression profiles. (A,B) Consensus CDF curve (A) and area (B) under the CDF curve when k = 2–9. (C) Consensus clustering analysis of TCGA-BLCA samples when k = 2. (D) TCGA- BLCA populations identified after unsupervised clustering in panel (C). (E) Kaplan–Meier survival plot of C1 and C2 groups. A log-rank test was conducted. (F) Expression of RNH1 in the C1 and C2 groups. (G) Volcano plot of DEGs based on C1 versus C2. (H) BP, CC, and MF of DEGs were investigated using GO enrichment analysis. | PMC10400633 | 41598_2023_39827_Fig4_HTML.jpg |
0.428554 | 2ea43f984a7d4beda85231e421bd92d9 | RNH1 promotes the infiltration of multiple immune cells. (A) Spearman correlation between RNH1 and 28 TIICs based on RNAseq data of 33 cancer types from TCGA, as calculated using the ssGSEA algorithm. (B–G) Differences in the effector genes of the above tumour-associated immune cells between high- and low-RNH1 groups from BLCA related datasets: (B) TCGA-BLCA, (C) GSE13507, (D) GSE5287, (E) GSE48057, (F) GSE48277, and (G) GSE69795. (H) Differences in various steps of the cancer immunity cycle between different BLCA molecular subtypes. (I) Differences in the various steps of the cancer immune cycle between groups with high and low RNH1 expression. (J) Differences in the various steps of the cancer immune cycle between groups in C1 and C2. | PMC10400633 | 41598_2023_39827_Fig5_HTML.jpg |
0.407061 | 1d982ef632d84f1faa22487e86d489aa | RNH1 predicts the response to immunotherapy in BLCA. (A) Spearman correlation analysis of RNH1 and T-cell inflammatory scores in 33 cancer types. (B) Scatter plot of Spearman correlation for RNH1 and T-cell inflammation score in BLCA. (C) Spearman correlation analysis of RNH1 and 20 typical inhibitory immune checkpoints in 33 cancer types. (D) Immune checkpoint expression heatmaps in PR and CR.CR: complete response; PR, partial response. (E) Fraction of patients between RNH1 and the clinical response of cancer immunotherapy in the IMvigor210 cohort. (F) Expression of RNH1 in inflamed, immune excluded and immune desert tumours from the IMvigor210 cohort. Ns no significant difference; * p < 0.05; ** p < 0.01. | PMC10400633 | 41598_2023_39827_Fig6_HTML.jpg |
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