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0.474632 | b91446ad98e94a13914d6c2cef5c96b7 | a Analysis of TLGST on 12% SDS PAGE; (1) molecular weight marker proteins, (2) TLGST. b Analysis of TLGST on isoelectric focusing PAGE: (1) pI marker proteins, (2) TLGST | PMC9995618 | 43141_2023_486_Fig2_HTML.jpg |
0.449689 | 64553ae7ca8448889e1804d8c8a6219a | a The pattern of TLGST pH profile utilizing 0.1 M potassium phosphate (5.7–8.0) and Tris–HCl (8.0–9.2). b Lineweaver–Burk plot of TLGST reaction speed in response to CDNB concentrations | PMC9995618 | 43141_2023_486_Fig3_HTML.jpg |
0.409674 | 59cb93c9fd1743188ecde33c89cea0e2 | a TLGST Inhibition with pCMB various concentrations. b Hill plot of TLGST inhibition with pCMB. c Lineweaver–Burk plots showing TLGST inhibition type with pCMB. d TLGST inhibition constant (Ki) value for pCMB | PMC9995618 | 43141_2023_486_Fig4_HTML.jpg |
0.512687 | 03acf5abf14e40b599f720b4ca6f8b82 |
(A)
JAK2V617F allele burden measured in the peripheral blood by digital droplet PCR during the study. (B) Cumulative change in hemoglobin (mmol/l) during the trial. (C) Cumulative change in leucocytes (×109/l) during the trial. (D) Cumulative change in platelets (×109/l) during the trial. (B, C) graphs depict the mean ± SEM. | PMC9996128 | fimmu-14-1117466-g001.jpg |
0.41876 | 51c67ec280114147a21877c8261b70a2 |
Ex vivo IFNγ ELISPOT responses in patient PBMCs and BMNC during treatment. (A, B) Heat map of ex vivo PBMC responses against the ARG1 (A)- and PD-L1(B)-derived peptide epitopes at baseline and during treatment. (C): Representative well images of ex vivo IFNγ ELISPOT response against ArgLong2 and PD-L1Long1 in PBMCs from patient 6. (D) Summary of statistically significant PBMC responses from ex vivo IFNγ ELISPOT assay. (E) Heat map of ex vivo responses against the ARG1- and PD-L1-derived peptide epitopes in BMNC of patient 4 and 8 as determined by IFNγ ELISPOT. (F) Representative well images of ex vivo ELISPOT response in BMNC from patient 4. The number of peptide-specific cells in ELISPOT assay was calculated by subtracting the mean number of spots in the control wells from the mean number of spots in the peptide-stimulated wells. PBMCs were plated at a density of 9×105 cells/well and BMNCs at 6.8×105 cells/well. | PMC9996128 | fimmu-14-1117466-g002.jpg |
0.458695 | 064c61857f96406ba99a69aeacc0c9a9 | Responses against ARG1- and PD-L1-derived peptides in PBMCs. (A, B): Heat maps depicting PBMC responses against the ARG1-(A) and PD-L1-(B) derived peptide epitopes as measured by in vitro IFNγ ELISPOT. The number of peptide-specific cells was calculated by subtracting the mean number of spots in the control wells from the mean number of spots in the peptide-stimulated wells. PBMCs were plated at a density of 2.5×105 cells/well. (C, D) The phenotype of vaccine specific T cells in in vitro cultured PBMCs of treated patients as determined by intracellular staining for IFNγ and TNFα production in CD4+ (top) and CD8+ (bottom) T cells in response to ARG1-(C) and PD-L1-(D) derived peptide stimulation. Bars represent peptide specific response after background subtraction. (E, F) Representative dot plots of IFNγ and TNFα cytokine production by CD4+ (left) and CD8+ (right) T cells in response to ArgLong2 (E) and PD-L1Long1 (F) peptide restimulation as compared to unstimulated control in in vitro cultured PBMCs from patient 9. | PMC9996128 | fimmu-14-1117466-g003.jpg |
0.406722 | 6962e522165d4aa9b12469ca430c9302 | Phenotypic marker expression in PBMCs and BMNCs at baseline and during vaccination trial. Percentage of CD3+ (A), CD4+ (B) and CD8+ (C) cells out of live cells in PBMCs of treated patients analyzed by flow cytometry. (D–G) changes in the subpopulations of CD8+ T cells in the PBMCs of treated patients. (D) Fraction of CD8+ central memory (CM) T cells defined as CD3+CD8+CD45RA-CCR7+represented as percentage out of CD8+ population. (E) The fraction of CD8+ naïve T cells defined as CD3+CD8+CD45RA+CCR7+ out of CD8+ cells. (F) The fraction of CD8+ effector memory (EM) cells defined as CD3+CD8+CD45RA-CCR7- out of total CD8+ cells (G) The fraction of CD8+ TEMRA cells defined as CD3+CD8+CD45RA+CCR7- represented as percentage out of CD8+ population. (H) Changes in the expression of PD-L1 as determined by RT-qPCR in the CD14+ myeloid cells in the peripheral blood of patients at baseline and end of treatment. (I) Changes in the expression of ARG1 as determined by RT-qPCR in the total BMNCs of patients at baseline and end of treatment. Statistical analysis was performed using the Wilcoxon signed-rank test, *- p ≤0.05, **- p ≤0.01. A-G graphs represent mean ± SEM. | PMC9996128 | fimmu-14-1117466-g004.jpg |
0.495684 | 889918128e794bdf90d0a068cab0af58 | Surveyed sites in Yunnan Province, southwestern China. (A) Tropical region (Xishuangbanna Banma Mountain: 800, 1,000, 1,200, and 1,400 m); (B) Subtropical region (Puer Ailao Mountain: 2,000, 2,200, 2,400, and 2,600 m); (C) Subalpine region (Lijiang Yulong Snow Mountain: 3200, 3,400, 3,600, and 3,800 m). The red dots in A, B, and C represent the location of each plot. | PMC9996296 | fmicb-14-1079113-g001.jpg |
0.522513 | 49ee62aaa0334fba8e2cbd3dc8e559d9 | Tree, fungal, and bacterial species along elevational gradients in three climatic zones. (A): tropical; (B): subtropical; (C): subalpine; A (1–3), B (1–3), C (1–3): tree species; A (4–6), B (4–6), C (4–6): fungal species; A (7–9), B (7–9), C (7–9): bacterial species. SR: species richness; PD: phylogenetic diversity; Shannon: Shannon–Wiener index. | PMC9996296 | fmicb-14-1079113-g002.jpg |
0.388 | fc75070ad52942328a812ab0b2163682 | Analysis of environmental factors and diversity indexes in three climatic zones using random forest. A-C: tree species; D-F: fungal species; G-I: bacterial species; OM: soil organic matter content; TC: total carbon; TN: total nitrogen; HN: hydrolysable nitrogen; TP: total phosphorus; TK: total potassium; AK: available potassium; pH: soil pH; water: soil moisture content; temperature: air temperature; humidity: air humidity. | PMC9996296 | fmicb-14-1079113-g003.jpg |
0.411499 | 5e5bba30d5cb489bb4697cbcba50618e | The explanatory power of soil factors for species composition in three climatic zones. A-C: tree species; D-F: fungal species; G-I: bacterial species. OM: organic matter; TC: total carbon; TN: total nitrogen; HN: hydrolysable nitrogen; TP: total phosphorus; TK: total potassium; AK: available potassium; pH: soil pH; Wat: soil moisture content; Alt: altitude/elevation; Tem: air temperature; Hum: air humidity. | PMC9996296 | fmicb-14-1079113-g004.jpg |
0.448577 | d3ca3307a75e461aae2bfdf8f4f548a7 | Piecewise structural equation model. We performed principal component analysis of environmental factors (climatic and soil properties), plant diversity, and microbial diversity to extract data on the first axis (PC1, explained variance >70%). Model A: environmental factors directly affect microorganisms and plants. Model B: environmental factors directly influence plant diversity, which in turn affects microorganisms. (A,B) tropical; (C,D) subtropical; (E,F) subalpine. Arrows represent unidirectional or bidirectional relationships among variables. Blue and green arrows denote positive and negative relationships, respectively. Dashed arrows indicate nonsignificant relationships (p ≥ 0.05). The thickness of the arrow paths indicates the magnitude of the standardized regression coefficients. | PMC9996296 | fmicb-14-1079113-g005.jpg |
0.450263 | 4f56ca6174994229bb78caed453a531f | Chemically modified aptamers for improving binding affinity to the target protein via enhancing non-covalent bonding (the red dot represented amino acid residues on the protein, the yellow rectangle represented modified nucleotides on the aptamer, the black arrow represented non-covalent bond). | PMC9996316 | fcell-11-1091809-g001.jpg |
0.452795 | 0aa98899a7f64fda9b519258fcd0abf9 | The nucleobases modifications on the aptamers to enhance binding affinity. (A) SOMAmers modification; (B) Modified uridine by click chemistry; (C) Base-appended bases modification; (D) Amino acid (leu) modification. | PMC9996316 | fcell-11-1091809-g002.jpg |
0.598629 | bb3e0d208b314135b52a517d0c2eb724 | The ribose modifications on the aptamers to enhance binding affinity. (A) 2′-fluoro (2′-F) modification; (B) 2′-Fluoro Arabino nucleic acid modification; (C) 2′, 2′-difluoro-2′-deoxycytidine modification; (D) Locked Nucleic Acid modification; (E) Unlocked Nucleic Acid modification. | PMC9996316 | fcell-11-1091809-g003.jpg |
0.50614 | ab55fc22d08d4115a0f3fb1cf5fd9b17 | The ribose modifications on the aptamers to enhance binding affinity. (A) 4′-S modification; (B) TNA modification; (C) HNA modification; (D) phNA modification. | PMC9996316 | fcell-11-1091809-g004.jpg |
0.561396 | 0a4bd3f65dc64a458cae7a39b9b5fd8d | The mirror-image nucleotide (L-DNA) modification on aptamers. | PMC9996316 | fcell-11-1091809-g005.jpg |
0.53089 | 4498fc7c8cf246ec8f08a7cf6f6a671a | The chemical modifications on the phosphate of aptamers to improve affinity. (A) Phosphorothioate (PS) modification; (B) phosphorodithioate (PS2) modification. | PMC9996316 | fcell-11-1091809-g006.jpg |
0.532913 | 2578ce4f6dc646da8141f71d3c2b3aca | The artificial nucleotides incorporating into aptamer to improve binding affinity. (A) The (7- (2-thienyl) imidazo [4, 5-b] pyridine) (Ds) artificial nucleotide; (B) the 6-amino-5-nitro-3- (1′-β-D-2′-deoxyribofuranosyl)-2 (1H)-pyridone (Z) artificial nucleotide; (C) the 2-amino-8- (1′-β-D-2′-deoxy-ribofuranosyl)-imidazo-[1,2-a]-1,3,5-triazin-4 (8H)-one) (P) artificial nucleotide. | PMC9996316 | fcell-11-1091809-g007.jpg |
0.428593 | a32a97ecc19a4b89868b1b53e59df19c | (A)
Experimental workflow for the labeling of co-translational O-GlcNAcylation and boosting samples. In the boosting sample, O-GlcNAcylated proteins were labeled with Ac4GalNAz for 48 h in heavy media. For the co-translational and control
samples, the culture media were switched from light to heavy, and
cells were further cultured for 1 h with Ac4GalNAz. At
the same time, Puro was added to the co-translational samples while
DMSO was added to the control samples. Then the cells were lysed,
and click chemistry was performed in the cell lysate to add a photocleavable
biotin tag to labeled glycoproteins. (B) Experimental workflow for
the enrichment of glycopeptides. The biotin-labeled glycopeptides
were enriched using NeutrAvidin resin and eluted under UV radiation.
The boosting, co-translational, and control samples were labeled with
the TMT reagents, respectively, before being mixed. The samples were
fractionated and analyzed by LC–MS/MS. | PMC9996615 | ac2c04779_0002.jpg |
0.428092 | dcf3bac689fb4bcb8fc12e0965079a3c | (A) Example tandem mass spectrum of an identified co-translational O-GlcNAcylated peptide. (B) Correlations of the quantified O-GlcNAcylated peptides with the Puro treatment in the duplicate
experiments. (C) Correlations of the quantified O-GlcNAcylated peptides in the duplicate control experiments. (D)
Ratios of the intensities of the unique co-translational O-GlcNAcylated peptides in the treated samples vs the control ones.
(E) Venn diagram of co-translational glycoproteins among all quantified O-GlcNAcylated proteins. (F) Comparison of co-translational
glycoproteins with all O-GlcNAcylated proteins in
MCF7 cells identified in another experiment. | PMC9996615 | ac2c04779_0003.jpg |
0.450953 | 6200ece5ac2e4f7290b53ffe7bd9e3b8 | (A) Clustering results
for all O-GlcNAcylated
proteins against the human proteome. (B) Clustering results for co-translational O-GlcNAcylated proteins against total O-GlcNAcylated proteins identified in MCF7 cells. (C) Comparison of
the distribution of the proteins with co-translational glycosylation
sites and others in the nucleus (Nuc) and in the cytoplasm (Cyto).
(D) Comparison of the dynamics of the proteins identified with co-translational
glycosylation sites and others in the nucleus. (E) Number of the glycopeptides
identified from each protein between those with co-translational glycosylation
sites and others. In the boxplots, the center line indicates the median
value, box limits indicate the first and third quartiles, and whiskers
indicate 1.5 interquartile range. Statistical significance was determined
by the Student’s t-test, two tailed. The significance
levels are labeled as ** (P < 0.01), *** (P < 0.001), and **** (P < 0.0001). | PMC9996615 | ac2c04779_0004.jpg |
0.43191 | f65e4f89d76d49399ad9c088832af535 | (A
and B) Illustrations of the chromatin remodeling complex (A)
and the spliceosome (B). (C) Identification of co-translational O-GlcNAcylated proteins associated with different protein
complexes and biological processes. Each node stands for a protein,
and each edge represents a known protein–protein interaction.
The arrowheads indicate the direction of interaction from a source
node to a target node. | PMC9996615 | ac2c04779_0005.jpg |
0.447743 | 726628089f2444458fc5eab49408ca03 | (A–C) Comparison
of the amino acid composition (A), the
GRAVY score (B), and isoelectric point (C) of the adjacent residues
between the co-translational and total O-GlcNAcylation
sites. (D) Occurrence of different amino acids next to the co-translational O-GlcNAcylation sites, using all O-GlcNAcylation
sites identified in MCF7 cells as the background. The amino acids
overrepresented in the co-translational glycosylation sites have positive Z-scores, while those reduced have negative ones. (E) Comparison
of the secondary structures of the co-translational and total glycosylation
sites. In the boxplots, the center line indicates the mean value,
box limits indicate the first and third quartiles, and whiskers indicate
1.5 interquartile range. Statistical significance was determined by
the Student’s t-test, two tailed. The significance
levels are labeled as ** (P < 0.01), *** (P < 0.001), and **** (P < 0.0001). | PMC9996615 | ac2c04779_0006.jpg |
0.382567 | 3e661aa9b0e54ef2a528926e830af8ba | CNVs overlapping between SPACNACS and other databases. Comparative between the CNVs found in SPACNACS and the ones present in the 1000 genomes and Gnomad databases. The X axis incrementally represents the level of overlap between the CNVs compared, which range from 0 (CNVs unique to SPACNACS) up to 100% (CNVS with a perfect match) | PMC9997023 | 40246_2023_466_Fig1_HTML.jpg |
0.478045 | 1b200452f1974b3684dea4304775221a | The SPACNACS interface. A Genome browser panel consisting of an embedded Integrative Genomics Viewer preloaded with the Spanish CNV database and other useful tracks. B Search and selection panel, which provides several filters for specifying the genomic region and the data to be shown. C Filtering status panel, which shows information about the active filters. The whole dataset is shown by default | PMC9997023 | 40246_2023_466_Fig2_HTML.jpg |
0.446868 | aee31d6ee55d47d1bf8d280232ccef0f | Distribution of CNVs detected in pharmacogenes (PGx genes) according to the allele frequency. The number of genes harboring duplications (green) or deletions (red) of the 1045 PGx genes tested are shown according to the frequency detected in the population | PMC9997023 | 40246_2023_466_Fig3_HTML.jpg |
0.44375 | 183d342ed0054377b0eda0e87d1f3ae2 | Daily intake of mineral (MIN) or energy with mineral (NRG) supplements of heifers grazing native range over the duration of the grazing season. The 57-d monitoring period was initiated from the time of pregnancy diagnosis (July 25th) until removal from pasture (September 19th). Treatments include: MIN (N = 18), free choice access to mineral supplement [Purina Wind & Rain Storm All-Season 7.5 Complete (Land O’Lakes, Inc., Arden Hills, MN)]; NRG (N = 13), free choice access to energy supplement [Purina Accuration Range Supplement 33 with added MIN (Land O’Lakes, Inc., Arden Hills, MN)]. | PMC9997776 | txad013_fig1.jpg |
0.460935 | 01ca4f7a64744561bdee7f983a7e0ecf | Effects of VDR deletion on LPS-induced AKI mice. (A) Serum concentrations of BUN and Cr at 24 h after LPS administration. (B) H&E staining of kidney sections. (C) Immunofluorescence analysis and its quantitative analysis of TUNEL (top) and F4/80 (bottom) of kidney sections. (D) Western blot analysis (left) and densitometric quantitation (right) of VDR, bcl2 and cleaved caspase3 was performed in the four groups of mice. (E) Real-time RT-PCR quantification of IL-6 and MCP1 in the renal cortex of the four groups of mice. *p < 0.05; **p < 0.01; ***p < 0.001. VDR, vitamin D receptor. | PMC9998528 | fphys-14-1083643-g001.jpg |
0.435933 | ec6f74b1411345febb9fe0dff92b3850 |
VDR deletion aggravated the abnormal glycolysis of LPS-induced AKI mice. (A) Renal lactate content and hexokinase activity of the four groups. (B) Western blot analysis (left) and densitometric quantitation (right) of PDHA1 and p-PDHA1 and was performed in the four groups of mice. (C) Immunofluorescence analysis and its quantitative analysis of p-PDHA1 (green) and PDHA1 (red) of kidney sections. White arrow: glomerulus; yellow arrow: renal tubules. (D) Images of mitochondrial injury of proximal tubule epithelial cells of mice. *p < 0.05; **p < 0.01; ***p < 0.001. | PMC9998528 | fphys-14-1083643-g002.jpg |
0.374142 | d13a9c0179e24bad97771e4cab741f29 | Effects of VDR overexpression on LPS-induced AKI mice. (A) Serum concentrations of BUN and Cr at 24 h after LPS administration. (B) H&E staining of kidney sections. (C) Immunofluorescence analysis and its quantitative analysis of TUNEL (top) and F4/80 (bottom) of kidney sections. (D) Western blot analysis (left) and densitometric quantitation (right) of VDR, bcl2 and cleaved caspase3 was performed in the four groups of mice. (E) Real-time RT-PCR quantification of IL-6 and MCP1 in the renal cortex of the four groups of mice. *p < 0.05; **p < 0.01; ***p < 0.001. | PMC9998528 | fphys-14-1083643-g003.jpg |
0.44532 | ac0e5d67d4bb4ac9b2038a138043968d |
VDR overexpression lightened the abnormal glycolysis of LPS-induced AKI mice. (A) Renal lactate content and hexokinase activity of the four groups. (B) Western blot analysis (left) and densitometric quantitation (right) of PDHA1 and p-PDHA1 and was performed in the four groups of mice. (C) Immunofluorescence analysis and its quantitative analysis of p-PDHA1 (green) and PDHA1 (red) of kidney sections. White arrow: glomerulus; yellow arrow: renal tubules. (D) Images of mitochondrial injury of proximal tubule epithelial cells from the four groups of mice. *p < 0.05; **p < 0.01; ***p < 0.001. | PMC9998528 | fphys-14-1083643-g004.jpg |
0.423126 | d22bcf12b33f4e939b4e7263aadfb13c | Paricalcitol alleviated renal injury on LPS-induced AKI mice. (A) Serum concentrations of BUN and Cr at 24 h after LPS administration. (B) H&E staining of kidney sections. (C) Immunofluorescence analysis and its quantitative analysis of TUNEL (top) and F4/80 (bottom) of kidney sections. (D) Western blot analysis (left) and densitometric quantitation (right) of VDR, cleaved caspase3 and bcl2 was performed in the four groups of mice. (E) Real-time RT-PCR quantification of IL-6 and MCP1 in the renal cortex of the four groups of mice. *p < 0.05; **p < 0.01; ***p < 0.001. P, Paricalcitol; BUN, blood urea nitrogen; Cr, creatinine; H&E, Hematoxylin and eosin; MCP1, monocyte chemoattractant protein-1. | PMC9998528 | fphys-14-1083643-g005.jpg |
0.41249 | 4ed5b8feaf294f24afb819e2ff360816 | Paricalcitol alleviated glucose metabolism reprogramming of LPS-induced AKI mice. (A) Renal lactate content and hexokinase activity of the four groups. (B) Western blot analysis (left) and densitometric quantitation (right) of PDHA1 and p-PDHA1 and was performed in the four groups of mice. (C) Immunofluorescence analysis and its quantitative analysis of p-PDHA1 (green) and PDHA1 (red) of kidney sections. White arrow: glomerulus; yellow arrow: renal tubules. (D) Images of mitochondrial injury of proximal tubule epithelial cells from the four groups of mice by TEM. *p < 0.05; **p < 0.01; ***p < 0.001. | PMC9998528 | fphys-14-1083643-g006.jpg |
0.494865 | b06f3e94c58d4743b2fcaeebf5655699 |
VDR deletion aggravated abnormal glycolysis and injury in LPS-induced HK-2 cell. (A) Oxygen consumption rate (OCR) (top) measured by Seahorse metabolic analyzer and quantitative analysis (bottom) of mitochondrial function parameters (basal respiration, maximal respiration). (B) lactate content in HK-2 cells and VDR-KO cells treated with LPS for 24 h. (C) Western blot analysis (left) and densitometric quantitation (right) of VDR, PDHA1, p-PDHA1, cleaved caspase3 and bcl2 was performed in the four groups of HK-2 cells. (D) Real-time RT-PCR quantification of IL-6 and MCP1. *p < 0.05; **p < 0.01; ***p < 0.001. Oligo, oligomycin; Rote, rotenone; Anti, antimycin A. | PMC9998528 | fphys-14-1083643-g007.jpg |
0.487055 | d0ddbdd518464739982dc87e51188b40 |
VDR overexpression lightened LPS-induced abnormal glycolysis and injury in HK-2 cell. (A) Oxygen consumption rate (OCR) (top) measured by Seahorse metabolic analyzer and quantitative analysis (bottom) of mitochondrial function parameters (basal respiration, maximal respiration). (B) lactate content in HK-2 cells and VDR-OE cells treated with LPS for 24 h. (C) Western blot analysis (left) and densitometric quantitation (right) of VDR, PDHA1, p-PDHA1, cleaved caspase3 and bcl2 was performed in the four groups of HK-2 cells. (D) Real-time RT-PCR quantification of IL-6 and MCP1. *p < 0.05; **p < 0.01; ***p < 0.001. Oligo, oligomycin; Rote, rotenone; Anti, antimycin A. | PMC9998528 | fphys-14-1083643-g008.jpg |
0.436667 | c0bcb48ca96444c0891fb8df339fe31d | Paricalcitol alleviated LPS-induced injury through phosphorylation of PDHA1. (A) Oxygen consumption rate (OCR) (top) measured by Seahorse metabolic analyzer and quantitative analysis (bottom) of mitochondrial function parameters (basal respiration, maximal respiration). (B) lactate content in HK-2 cells treated with LPS, LPS + P, LPS + D (D: DCA, 5mM, pretreated 2 h), LPS + P + D for 24 h. (C) Western blot analysis (top) and densitometric quantitation (bottom) of PDHA1, p-PDHA1, cleaved caspase3 and bcl2 was performed in the five groups of HK-2 cells. (D) Real-time RT-PCR quantification of IL-6 and MCP1. *p < 0.05; **p < 0.01; ***p < 0.001. P, paricalcitol; D: DCA, dichloroacetic acid solution. Oligo, oligomycin; Rote, rotenone; Anti, antimycin A. | PMC9998528 | fphys-14-1083643-g009.jpg |
0.459719 | f30f107b06dd4cf7b18d46af9843b14f | VD-VDR active AMPK in LPS-induced AKI mice. (A) Western blot analysis (left) and densitometric quantitation (right) of AMPK and p-AMPK was performed in group of WT, KO, LPS and KO + LPS. (B) Western blot analysis (left) and densitometric quantitation (right) of AMPK and p-AMPK was performed in group of WT, OE, LPS and OE + LPS. (C) Western blot analysis (left) and densitometric quantitation (right) of AMPK and p-AMPK was performed in group of WT, WT + P, LPS and LPS + P. *p < 0.05; **p < 0.01; ***p < 0.001. | PMC9998528 | fphys-14-1083643-g010.jpg |
0.423855 | 8e65b8dbeafb48a58416982839d473d5 | VD alleviate glucose metabolism reprogramming via the activation of AMPK pathway. (A) Western blot analysis (left) and densitometric quantitation (right) of AMPK and p-AMPK in VDR-KO cells treated with LPS for 24 h. (B) Western blot analysis (left) and densitometric quantitation (right) of AMPK and p-AMPK in VDR-OE cells treated with LPS for 24 h. (C) Oxygen consumption rate (OCR) (top) measured by Seahorse metabolic analyzer and quantitative (bottom) analysis of mitochondrial function parameters (basal respiration, maximal respiration). (D) lactate content in HK-2 cells treated with LPS, LPS + P, LPS + C (C: compound C, 10 μM, pretreated 1 h), LPS + P + C for 12–16 h. (E) Western blot analysis (left) and densitometric quantitation (right) of AMPK, p-AMPK, PDHA1, p-PDHA1, cleaved caspase3 and bcl2 was performed in the five groups of HK-2 cells. (F) Real-time RT-PCR quantification of IL-6 and MCP1. *p < 0.05; **p < 0.01; ***p < 0.001. Oligo, oligomycin; Rote, rotenone; Anti, antimycin A. | PMC9998528 | fphys-14-1083643-g011.jpg |
0.435925 | 3194a16cc14c49759acddbf22e437a9c | Imaging findings. (A) Axial non-contrast T1-weighted breast MRI image shows no evidence of malignancy. There is a mediastinal shift with the heart shifted to the right and a lack of lung markings in the upper left lung, suggesting the possibility of bulla in the upper left lung. (B) Chest X-ray shows a left-sided pneumothorax with cardiac and mediastinal shift rightward suggesting underlying tension component. (C) Chest CT shows a small left anterior pneumothorax. There is a left-sided pleural drainage catheter with its tip along the left major fissure. There are subtle patchy consolidative opacities in the subpleural aspects of the left upper lobe. | PMC9999020 | fonc-13-1096160-g001.jpg |
0.456443 | 6e2a56c0709547aa8ede97bf82f2caf3 | Pathological features. The tumor is represented by cystic and solid components (A); HE original magnification x5. The solid component is composed of spindle cells forming fascicles (B); there is variable background collagen deposition; HE original magnification x20. The tumor cells are immunoreactive with bcl2 (C) and SS18-SSX (D) antibodies; immunohistochemistry, original magnification x20 and x20. | PMC9999020 | fonc-13-1096160-g002.jpg |