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0.450313 | 3832a987cf504cfa90f9b0a477a8d0ff | In cellula assessment of TMX4 engagement in mixed disulfides with NESPRIN3α.a Lysates of cells mock-transfected (lanes 1, 5, 9), expressing GFP-SUN1 and HALO-NESPRIN3α, TMX4C67A-V5 (lanes 2, 6, 10), GFP-SUN1 and HALO-NESPRIN3α (lanes 3, 7, 11), or TMX4-V5 GFP-SUN1 and HALO-NESPRIN3α (lanes 4, 8, 12) were separated in a reducing gel and transferred on PVDF membranes. Expression of the ectopic proteins was confirmed by WB with anti-V5 (lanes 1–4), anti-GFP (lanes 5–8), or anti-HALO antibodies (lanes 9–12). Uncropped blots in Supplementary Fig. 6. b The presence of TMX proteins (lanes 1–3), NESPRIN3α (lanes 4–6), or SUN1 (lanes 7–9) in mixed disulfides (MD) with TMX4C67A-V5 (lanes 2, 5, 8) or TMX4-V5 (lanes 3, 6, 9) immunoisolated from cell lysates with anti-V5 antibodies was monitored under non-reducing conditions by western blot with anti-V5, anti-HALO, or anti-GFP antibodies, respectively. c. The engagement of TMX proteins (lanes 10–12), or NESPRIN3α (lanes 13–15) in MD with HALO-NESPRIN3α immunoisolated from cell lysates with anti-HALO antibodies was monitored under non-reducing conditions by western blot with anti-V5 and anti-HALO antibodies, respectively. d The presence of TMX4 proteins in MD with GFP-SUN1 (lanes 1–3), or with HALO-NESPRIN3α (lanes 4–6) immunoisolated from cell lysates has been assessed by WB with anti-V5 antibodies under non-reducing conditions (or reducing conditions, lanes 7–12). WB is representative of at least three independent experiments. | PMC10264389 | 41467_2023_39172_Fig9_HTML.jpg |
0.435834 | bbf233eb396d4541bc9780e8d0a4a825 | Flowchart of systematic literature review | PMC10264504 | 393_2022_1222_Fig1_HTML.jpg |
0.44921 | f90dcaa82cb94862a4f5c31e1fe42db8 | Before the completion of a dorsal cheilectomy using an arthroscopic approach, pertinent anatomical structures are marked, including the extensor hallucis longus (EHL) tendon and great toe metatarsophalangeal joint (MTPJ). The dorsal medial and dorsal lateral portals are marked approximately 5 mm from the EHL tendon after the patient is prepped and draped in the supine position. | PMC10265193 | gr1.jpg |
0.432602 | ad6b5e8496e74a6f9d8c855d5631818c | (A) Demonstrates an arthroscopic view of the great toe metatarsophalangeal joint when visualized from the dorsal medial portal, demonstrating evidence of thickened hemorrhagic synovium adjacent to the great toe metatarsal head. (B) Demonstration of thickened synovium and bone debris being removed from the great toe metatarsophalangeal joint with a 2.5-mm arthroscopic shaver that is inserted through the dorsal lateral portal. | PMC10265193 | gr2.jpg |
0.413786 | 2b1189013afa45be8789be67e1460ee0 | (A) The articular surface of the great toe metatarsophalangeal joint is evaluated using the NanoScope (Arthrex) from the dorsal medial portal demonstrating evidence of cartilage loss and debris within the great toe metatarsophalangeal joint. (B) Demonstration of all loose chondral flaps and bone debris being removed from the great toe metatarsophalangeal joint using a 2.5-mm shaver inserted through the dorsal lateral portal. | PMC10265193 | gr3.jpg |
0.47634 | 41525dcaaa7d4dafb0f4efbeaa6586c2 | (A) Clinical photo demonstrating the NanoScope (Arthrex) within the dorsal lateral portal and the MIS burr placed within accessory portal into the great toe metatarsophalangeal joint. An assistant is performing gentle traction with flexion and extension of the great toe metatarsophalangeal joint as needed to allow for completion of the procedure. (B) Arthroscopic view of the MIS burr being used to excise the dorsal osteophyte of the great toe metatarsal head under direct visualization. (MIS, minimally invasive surgical.) | PMC10265193 | gr4.jpg |
0.415308 | 87dd84290185415898756eecee129117 | Mini C-arm image of the lateral foot demonstrating the presence of a dorsal osteophyte on the great toe metatarsal head being measured using a periosteal elevator within the proximal accessory portal. This is completed before placement of the minimally invasive surgical burr and debridement of the osteophyte in an effort to perform a more precise excision. (MTPJ, metatarsophalangeal joint.) | PMC10265193 | gr5.jpg |
0.457317 | 1ea6c55edc094639a0a41debcee58d68 | Final mini C-arm image of the lateral foot demonstrating adequate excision of the dorsal osteophyte from the great toe metatarsal head. The great toe metatarsophalangeal joint is then taken through gentle flexion and extension to ensure adequate osteophyte excision has taken place. | PMC10265193 | gr6.jpg |
0.428388 | 6427104b69f74510b2bf4ad43e455742 | Readability scores for each search term are presented in terms of readability tests and their equivalent grade levels. The source for this figure is the author's analysis of data for the search terms and readability tests included in the analysis. GFOG, Gunning FOG Index; FGKL, Flesch–Kincaid Grade Level; CLI, The Coleman–Liau Index; SMOG, Simple Measure of Gobbledygook; ARI, Automated Readability Index; LWF, Linsear Write Formula; CONS, Readability Consensus. | PMC10265335 | 10.1177_23743735231179063-fig1.jpg |
0.431154 | c5eae19296704d4aac48bd997b9bf5d4 | Graphical illustration of the identified themes within each of three domains and areas of overlap. | PMC10265457 | gr1.jpg |
0.406693 | 2ef31f97e8dc4719b382fd42890c21e6 | Representative images of chromosomes at metaphase I of meiosis from meiocytes of Kronos plants with differing TtZIP4 genotypes (A) Wild-type Kronos; (B) Kr3161 TtZIP4-A1B1B2; (C)
Ttzip4-A1 single mutant; (D)
Ttzip4-B1 single mutant; (E)
Ttzip4-B2 single mutant (ph1c); (F) CRISPR Ttzip4-B2 single mutant; (G)
Ttzip4-A1B1 double mutant; (H)
Ttzip4-A1B2 double mutant; (I)
Ttzip4-B1B2 double mutant; (J)
Ttzip4-A1B1B2 triple mutant. Examples of univalent chromosomes (univ.), rod bivalents (rod), ring bivalents (ring), single chiasmata (X) and double chiasmata (XX) are indicated with arrows. Note the greatly increased univalence in the Ttzip4-A1B1 double mutant (G) and complete univalence in the Ttzip4-A1B1B2 triple mutant (J). Scale bar, 10 μm. | PMC10266424 | fpls-14-1189998-g001.jpg |
0.504007 | e9e1c492232740e2a2756fbbafbd1d74 | Column chart showing genotypic effects on meiotic metaphase I chromosomes of tetraploid wheat Ttzip4 mutants compared with Kr3161 wild type control plants (ZIP4-A1B1B2). Numbers of univalents, rod and ring bivalents and single chiasmata are shown. Numbers of multivalents and double chiasmata are not shown. Note greatly increased numbers of univalents (~18 out of 28 chromosomes) and low chiasma frequency in zip4-A1B1 double mutants, and virtually complete univalence and almost no chiasmata in the zip4-A1B1B2 triple mutants. | PMC10266424 | fpls-14-1189998-g002.jpg |
0.388011 | 7948c2e20fae40d1b1c7c01a7698d2f2 | Immunolocalization of the meiotic proteins ASY1 (magenta) and ZYP1 (green) combined with the telomeres (red) labeled by FISH in tetraploid wheat with different copies of TtZIP4 (TtZIP4-A1B1B2 (wild-type control), zip4A1B1 (double mutant) and zip4-A1B1B2 (triple mutant). DNA DAPI staining in blue. Scale bar represents 10 μm. (A) Synapsis during the early telomere bouquet stage. Initiation of synapsis is observed at the telomere bouquet in the wild type and double mutant showing the typical ZYP1 polarization. However, in the triple mutant, in the absence of all ZIP4 copies, synapsis initiation is mostly delayed and only short stretches of ZYP1 are observed dispersed throughout the nucleus. (B) Progression of synapsis after bouquet dispersal. Synapsis in the control and double mutant is almost completed at this stage, while synapsis is far from completion in the absence of all ZIP4 copies, as illustrated by the large amount of ASY1 labeling still visible. | PMC10266424 | fpls-14-1189998-g003.jpg |
0.423691 | 8ae972047d0b4e228d8a0595de6c4084 | SDS-PAGE gel running; at loading (left panel) and after running for 30 min (middle panel) and 90 min (right panel).Note the molecular weight standards (blue) appearing on the left and right edges once the samples have run. Arrows point to the front dye and arrowheads to 75 kDa molecular weight marker. | PMC10266446 | BioProtoc-13-09-4667-g001.jpg |
0.536152 | f8009800c4004c45a2a0b4a11395d576 | Images obtained with MicroChemi equipment and GelCapture software.Western blots for actin in HEK293FT cell lysates with different exposure times (from 1 to 4,128 s) showing original images (two left panels, the first being inverted), saturation image profile (third panel from the left), and pseudo color image (fourth panel from the left). Note that the signal becomes saturated (red signal) in 37.5 µg sample with 828 s of exposure. | PMC10266446 | BioProtoc-13-09-4667-g002.jpg |
0.398268 | c9b2a9d259254cb5b67e5bc38aaf0a28 | Representation of band quantifications.The signal of each band (y-axis) with respect to the exposure time (x-axis) is shown. Note that in the samples with higher protein content (22.5, 30, and 37.5 µg) the linearity between exposure time and signal is lost at certain exposure time. | PMC10266446 | BioProtoc-13-09-4667-g003.jpg |
0.438509 | f453bb5301a4450493e5c7ffb160e7d9 | Adjusted representation of band quantifications.After removing the samples with lower and/or higher exposure (in which linearity was lost), linearity for different amounts is kept and will allow to accurately calculate the slope for each concentration. | PMC10266446 | BioProtoc-13-09-4667-g004.jpg |
0.472501 | fc001d9e74de413db10767cd64a6ebc1 | Example of signal quantification.Images with different exposures showing pTrkA (panel A) and TrkA (panel B) signals were quantified in cultured sensory neurons after NGF stimulation for different stimulation times. The colored rectangles in both panels represent the membrane areas used for quantification. A rectangle of another region without signal was utilized as background (not shown in the images). Note that saturation can be detected at higher exposures of the TrkA blot in the pseudo color images (red color). On the right side of each panel there is a graph showing the signal increase curve for each time point. The range between dashed lines indicates the exposures taken to optimize the linear regression model and to perform the quantification within linearity. Note that the saturation in the pseudo color images matches the flattering of the curves in the plots. (C) Quantification of TrkA activation (pTrkA/TrkA ratio). Normalization was performed using the 5 min time point of NGF stimulation. Each colored line represents the results obtained in a single experiment (n = 3). Panels A and B correspond to experiment c in panel C. | PMC10266446 | BioProtoc-13-09-4667-g005.jpg |
0.405831 | 3903d8bfa067478e99830b6748adf087 | Transfer preparation | PMC10266446 | BioProtoc-13-09-4667-v001.jpg |
0.424422 | c0a56cbc9df24418900fa1e34428b4bd | Band quantification | PMC10266446 | BioProtoc-13-09-4667-v002.jpg |
0.515453 | 58b1f26c77b94e92a631bf6fbb273bef | Flowchart of participant selection for the present analysis. VPCB Victorian Pancreatic Cancer Biobank, KRAS Kirsten rat sarcoma viral oncogene homolog, ctDNA circulating tumour DNA, CT computed tomography. | PMC10267124 | 41598_2023_36643_Fig1_HTML.jpg |
0.40639 | afedb4e6473b40aeb1349bfa4b74395d | Boxplot of concentration of circulating tumour DNA (ctDNA) of participants grouped by clinical stage at diagnosis of pancreatic ductal adenocarcinoma (PDAC), n = 66. MAF mutant allele fractions; outliers included in analysis but not shown in graph, to enable visual representation. | PMC10267124 | 41598_2023_36643_Fig2_HTML.jpg |
0.46106 | 4507993c595b473780e7c62cd49d7a68 | Boxplots of participants’ skeletal muscle stores grouped by clinical stage at diagnosis of pancreatic ductal adenocarcinoma (PDAC), n = 66. Reference lines show thresholds for low SMI/SMD according to Martin et al.35. (a) Skeletal muscle index (SMI), no difference between clinical stages; (1) males with BMI ≥ 25 kg/m2; (2) males with BMI < 25 kg/m2; (3) females (all). (b) Skeletal muscle radiodensity (SMD), no difference between clinical stages; (1) BMI < 25 kg/m2; (2) BMI ≥ 25 kg/m2; HU Hounsfield Units. | PMC10267124 | 41598_2023_36643_Fig3_HTML.jpg |
0.466076 | 7a885bdeffcd461eb7ed2ed11d4b7dba | Flowchart of the study selection for the systematic review and meta-analysis | PMC10267254 | 415_2023_11693_Fig1_HTML.jpg |
0.468408 | 987dd79f976f4135b4b6df71077f204f | Forest plot demonstrating the value of PTFV1 in predicting ischemic stroke, with PTFV1 analyzed as a categorical variable (A) or continuous variable (B). PTFV1: P-terminal force in the precordial lead V1 | PMC10267254 | 415_2023_11693_Fig2_HTML.jpg |
0.415601 | 111bd034b98b4f3e88dfd5e28f795b7c | Forest plot demonstrating the value of maximum P-wave duration (A), mean P-wave duration (B) and advanced interatrial block (C) in predicting ischemic stroke | PMC10267254 | 415_2023_11693_Fig3_HTML.jpg |
0.430234 | 9cc52a7350514f40abcb76b7df825f6a | Forest plot demonstrating the value of the maximum P-wave area (A) and mean P-wave area (B) in predicting ischemic stroke | PMC10267254 | 415_2023_11693_Fig4_HTML.jpg |
0.435811 | 4c786cfcac1e4c529415a51d849e30ce | Forest plot demonstrating the value of LA diameter in predicting ischemic stroke, with LA diameter analyzed as a categorical variable (A) or continuous variable (B). LA left atrial | PMC10267254 | 415_2023_11693_Fig5_HTML.jpg |
0.39819 | 5e658475e84e4d418bb112362360bf58 | Forest plot demonstrating the value of LA reservoir strain in predicting ischemic stroke. LA left atrial | PMC10267254 | 415_2023_11693_Fig6_HTML.jpg |
0.433126 | 212faf819b8442d59976ba59a36291c9 | Forest plot demonstrating the value of NT-proBNP in predicting ischemic stroke, with NT-proBNP analyzed as a categorical variable (A) or continuous variable (B). NT-proBNP N-terminal pro-brain natriuretic peptide | PMC10267254 | 415_2023_11693_Fig7_HTML.jpg |
0.427864 | ff93f691e0ca4d52a6bff52b203a0452 | Flow chart of the study. | PMC10267493 | mpp-0032-0016-g01.jpg |
0.414016 | dbdd9026b80e4929aaad33d248a3c74b | OS (left) and RFS (right) after liver transplantation (LT) of 369 HCC patients, elderly (n = 97, green line) versus younger patients (n = 272, blue line). | PMC10267523 | lic-0012-0171-g01.jpg |
0.419773 | 9526dde0c0a641bf976fd87ea6da915e | OS (left) and RFS (right) after liver transplantation (LT) of patients with HCC inside the Milan criteria, elderly (n = 57, green line) versus younger patients (n = 185, blue line). | PMC10267523 | lic-0012-0171-g02.jpg |
0.411709 | 1e8cbbdf74194807b5ba96a6520c57ea | OS (left) and RFS (right) in elderly patients with cirrhosis HCC inside the Milan criteria after liver transplantation (LT) (n = 57, green line) versus liver resection (LR) (n = 40, blue line). | PMC10267523 | lic-0012-0171-g03.jpg |
0.377151 | 187f6711b3f94d9eb23f2d69f238fd34 | Level of Mpox (monkeypox) risk perception and subjective norms among the respondents. | PMC10268587 | HSR2-6-e1352-g001.jpg |
0.433814 | f14600a52b7d42669d8eaee1c0d00e3d | Diagnostic accuracy of GeneXpert, Myco/F, and MGIT 960 for detection of MTB from suspected tuberculosis patients based on retrospective data. | PMC10269854 | spectrum.01414-22-f001.jpg |
0.461213 | ce8cbdca200d4340bbde28d09e5d00a3 | Schematic diagram of MTB identification in biopsy tissue samples by the molecular method (GeneXpert) and by mycobacterial culture (Myco/F and MGIT 960). | PMC10269854 | spectrum.01414-22-f002.jpg |
0.476608 | 963c42a4399a46c5add28b98dfa5b3ed | Flowchart of the study.*During the study period (9 months). | PMC10270613 | pone.0287310.g001.jpg |
0.440239 | 454aab9f282542eea934ef3b464178b7 | Friable callus induction (mean values and standard deviation) from C. arabica and C. canephora leaf explants in different 2,4-D concentrations over 90 days. C. arabica and C. canephora exhibited distinct values of responsive explants in 9.06–54.36 μM 2,4-D over 90 days (a). 2,4-D concentrations influenced the callus inductions over time in C. arabica (b) and in C. canephora (c). *Mean values followed by the same letter do not present a significant difference. | PMC10272143 | 41598_2023_36879_Fig1_HTML.jpg |
0.422183 | f7ce95fcda8f431f9a1aed743a8ad4fa | The origin of the friable callus (9.06–54.36 μM 2,4-D) influenced the MCSE regeneration in C. arabica and C. canephora over 240 days. C. arabica and C. canephora exhibited distinct MCSE values (mean values and standard deviation), considering 2,4-D concentrations and time. *Mean values followed by the same letter do not present a significant difference. | PMC10272143 | 41598_2023_36879_Fig2_HTML.jpg |
0.398417 | e5789858af8b4aff9afb4c5710c591b3 | MCSE regeneration from C. arabica and C. canephora friable callus (mean values and standard deviation). The 2,4-D concentrations, which gave rise to friable calli, influenced MCSE regeneration during the ISE in C. arabica (a) and in C. canephora (b). *Mean values followed by the same letter do not present a significant difference. | PMC10272143 | 41598_2023_36879_Fig3_HTML.jpg |
0.398866 | 490f0b03275647d581aa6878c52e8f5b | The origin of the friable callus (9.06–54.36 μM 2,4-D) influenced the ASE regeneration of C. arabica and C. canephora over 240 days. C. arabica and C. canephora exhibited distinct ASE values (mean values and standard deviation), considering 2,4-D concentrations and time. *Mean values followed by the same letter do not present a significant difference. | PMC10272143 | 41598_2023_36879_Fig4_HTML.jpg |
0.417834 | 1a36ca4c079042e8870e75234ccc19af | ASE regeneration from C. arabica and C. canephora friable callus (mean values and standard deviation). The 2,4-D concentrations that gave rise to friable calli influenced ASE regeneration during ISE in C. arabica (a) and in C. canephora (b). *Mean values followed by the same letter do not present a significant difference. | PMC10272143 | 41598_2023_36879_Fig5_HTML.jpg |
0.441323 | 7b6ef0096e91408ea982c3fce7acb287 | 5-mC% during C. arabica and C. canephora ISE (mean values and standard deviation). Global 5-mC% in C. arabica and C. canephora leaf explant (control) donors (a). Comparison of the 5-mC% between the C. arabica and C. canephora friable callus originated in the induction medium with 9.06–54.36 μM 2,4-D (b). Comparison of the 5-mC% of the friable callus originated from 9.06 to 54.36 μM 2,4-D for C. arabica and C. canephora (c). 5-mC% in embryogenic callus of C. arabica and C. canephora (d). 5-mC% in MCSE (control) and ASE of C. arabica regenerated from friable callus originated in 9.06–54.36 μM of 2,4-D (e). *Mean values followed by the same letter do not present a significant difference. | PMC10272143 | 41598_2023_36879_Fig6_HTML.jpg |
0.437773 | 9b6a643f347949ddabf4d9364fe58de1 | Comparison of the 5-mC% (mean values and standard deviation) in C. arabica (a) and in C. canephora (b) during ISE: explant donor (control), friable callus, embryogenic callus, ASE and MCSE (control in relation to the ASE). *Mean values followed by the same letter do not present a significant difference. | PMC10272143 | 41598_2023_36879_Fig7_HTML.jpg |
0.418418 | d11c26b8af124c8187a743a3381a0f64 | Percentage of DNA damage (mean values and standard deviation) in MCSE (control) and ASE of C. arabica and C. canephora, which are regenerated from friable callus originated from 9.06 to 54.36 μM 2,4-D. Comparison of the percentage of DNA damage between MCSE and ASE of C. arabica and C. canephora considering each 2,4-D concentration (a). Comparison of percentage of DNA damage in MCSE and ASE recovered from each 2,4-D concentration for C. arabica and C. canephora (b). Without DNA damage (c). With DNA damage (d,e). *Mean values followed by the same letter do not present a significant difference. Bar = 5 μm. | PMC10272143 | 41598_2023_36879_Fig8_HTML.jpg |
0.438482 | 57ae0c0a18a140ad8322eceda1c59925 | A barrier called between the alveolus and capillary prevents the formation of oedema in health (A). This deteriorates in mild (B) and further in severe injury (C), becoming more permeable leading to the development of protein rish oedema in the lungs. ENaC, epithelial sodium channel; PMN, polymorphonuclear cells; RBC, red blood cell. Reproduced with permission from The Lancet. | PMC10272540 | fmed-10-1203827-g001.jpg |
0.477999 | 282356d04f774367820457c0cce460ae | Demonstrating changes in endothelial permeability and alveolus in acute respiratory distress syndrome. Inflammatory cascade signals breakdown endothelial cell adhesion molecules, widening space between endothelial cells. Increased expression of leukocyte adhesion molecules increases leukocyte rolling and migration across the endothelial barrier, where cytokine release, reactive oxygen species and damaging enzymes increase the inflammatory feedback loop. This leads to oedema and sloughing off of bronchial endothelium, which reduced the gas exchange ability of the alveolus. Image adapted from Biorender. | PMC10272540 | fmed-10-1203827-g002.jpg |
0.491095 | 5f54efb650274aabad61123af8bfebc6 | Layout of the research environments sampled in this study. (A) Layout of the room at the Einstein Telescope Laboratory. A: 3D Printer, B: Low Pressure Electric Impactor (ELPI+). The numbers 1, 2 and 3 represent the positions of workstations occupied by participants. (B) Layout of the room at the Department of Mechanical, Chemical and Materials Engineering, University of Cagliari. A: 3D Printer, B: washing tank, C: curing chamber, D: ELPI+. The numbers 1, 2 and 3 represent the positions of workstations occupied by participants. | PMC10272752 | fpubh-11-1144475-g001.jpg |
0.476324 | 75f904e2d122405c93c2f7b741e4d140 | UFP concentration changes in the Einstein Telescope Laboratory setting, where 3D printing with fused filament fabrication was used. (A) The overall particulate matter concentration. (B) Concentration of particulate matter collected with channel 5. (C) Concentration of particulate matter collected with channel 6. (D) Concentration of particulate matter collected with channel 7. (E) Concentration of particulate matter collected with channel 8. (F) Concentration of particulate matter collected with channel 11. The printing activities started at 10:00 and finished at 14:00. | PMC10272752 | fpubh-11-1144475-g002.jpg |
0.458319 | cf3343a9176043d289754a75971e1e30 | Scanning Electron Microscopy with energy dispersive X-ray spectrometry (SEM–EDX) analysis of particulate matter collected with Electric Low Pressure Impactor (ELPI+™) in Einstein Telescope Laboratory. (A–C) analysis of particulate matter collected on channel 5. (D–F) analysis of particulate matter collected on channel 6. (G–I) analysis of particulate matter collected on channel 7. (J–L) analysis of particulate matter collected on channel 8. (M–O) analysis of particulate matter collected on channel 11. | PMC10272752 | fpubh-11-1144475-g003.jpg |
0.437788 | b4996c174e004c5588e2bc1b14a045c6 | UFP concentration changes in the Department of Mechanical, Chemical and Materials Engineering at the University of Cagliari. The printing process was divided in three phases: printing, washing and cleaning. | PMC10272752 | fpubh-11-1144475-g004.jpg |
0.390965 | 3208d0057f044a459a7fd059e62c41e9 | HepG2/IR cells displayed enhanced proliferation, migration, invasion and EMT. (A) MTT assays were performed with HepG2 and HepG2/IR cells. (B) Colony formation assays were performed with HepG2 and HepG2/IR cells. (C) DNA replication was detected by EdU assays in HepG2 and HepG2/IR cells. (D) Representative image of migration and invasion in HepG2 and HepG2/IR cells. (E) The migration of HepG2 and HepG2/IR cells was determined by scratch wound-healing assays. (F) The protein expression of E-cadherin, N-cadherin, Vimentin and Snail in HepG2 and HepG2/IR cells was determined by Western blotting; the membranes were cut prior to hybridization with antibodies. The experiments were independently repeated three times. (* P < 0.05, ** P < 0.01) | PMC10273698 | 12885_2023_11068_Fig1_HTML.jpg |
0.448646 | 8d0f2a55e9704a48b2c04ff5d6b187ad | HepG2/IR cells displayed enhanced chemoresistance. The IC50 value (A) and EdU-positive rate (B) of MMC, VCR, OXA and sorafenib in HepG2/IR cells and their parental cells. (C). Representative images of apoptosis. D. The tumours dissected from all groups were photographed. (* P < 0.05, ** P < 0.01) | PMC10273698 | 12885_2023_11068_Fig2_HTML.jpg |
0.431765 | b50ebd34d5b54f59881674f16b033bf2 | Overexpressed miR-5195-3p inhibited proliferation, migration, invasion, and EMT in HepG2/IR cells. (A). Relative miR-5195-3p expression levels in HepG2/IR cells were detected using qRT‒PCR after transfection with miR-5195-3p mimic or its control (NC mimic). MTT assays (B), colony formation assays (C), and EdU assays (D) were employed to detect the proliferation of HepG2/IR cells after transfection with the NC mimic or the miR-5195-3p mimic. Representative images of migration and invasion (E) and scratch wound healing assays (F) of HepG2/IR cells transfected with miR-5195-3p mimic or NC were determined. G. The protein expression of E-cadherin, N-cadherin, Vimentin and Snail in HepG2/IR cells transfected with miR-5195-3p mimic was determined by Western blots; the membranes were cut prior to hybridization with antibodies. The experiments were independently repeated three times. (* P < 0.05, ** P < 0.01) | PMC10273698 | 12885_2023_11068_Fig3_HTML.jpg |
0.463347 | 788869369108463890cab40217d1845a | Overexpressed miR-5195-3p inhibited chemoresistance in HepG2/IR cells. The IC50 value (A) and EdU-positive rate (B) to OXA in HepG2/IR cells transfected with mimic or miR-NC. (C). Representative images of apoptosis. (D). The tumours dissected from all groups were photographed. The experiments were independently repeated three times. (* P < 0.05, ** P < 0.01) | PMC10273698 | 12885_2023_11068_Fig4_HTML.jpg |
0.41808 | 86a5fd46ac5343609927284e55931c43 | Inhibited miR-5195-3p promoted proliferation, migration, invasion, and EMT in HepG2 cells. (A). Relative miR-5195-3p expression levels in HepG2 cells were detected using qRT‒PCR after transfection with miR-5195-3p inhibitor or its control (NC inhibitor). MTT assays (B), colony formation assays (C), and EdU assays (D) were employed to detect the proliferation of HepG2 cells after transfection with the NC inhibitor or the miR-5195-3p inhibitor. Representative images of migration and invasion (E) and scratch wound healing assays (F) of HepG2 cells transfected with miR-5195-3p inhibitor or NC were determined. (G). The protein expression of E-cadherin, N-cadherin, Vimentin and Snail in HepG2 cells transfected with miR-5195-3p inhibitor was determined by Western blotting; the membranes were cut prior to hybridization with antibodies. The experiments were independently repeated three times. (* P < 0.05, ** P < 0.01) | PMC10273698 | 12885_2023_11068_Fig5_HTML.jpg |
0.424934 | 3c2dbc77c0694fc1a299f4132519a4bb | Inhibition of miR-5195-3p promoted chemoresistance in HepG2 cells. The IC50 value (A) and EdU-positive rate (B) for OXA in HepG2 cells transfected with inhibitor or miR-NC. (C). Representative images of apoptosis. (D). The tumours dissected from all groups were photographed. The experiments were independently repeated three times. (* P < 0.05, ** P < 0.01) | PMC10273698 | 12885_2023_11068_Fig6_HTML.jpg |
0.499404 | 90bf250fabe64e98b9d2bbd5a1cb9291 | miR-5195-3p directly targeted the 3′-UTR of SOX9 and TPM4. The predicted targeting sites of SOX9 and TPM4 (A and B). A dual luciferase reporter assay was performed to verify the direct target of miR-5195-3p (C and D). (E). Western blotting was performed to detect the protein expression levels of SOX9 and TPM4 in HepG2 cells transfected with NC inhibitor or miR-5195-3p inhibitor, and HepG2/IR cells were transfected with the NC mimic or miR-5195-3p mimic; the membranes were cut prior to hybridization with antibodies. The experiments were independently repeated three times. (* P < 0.05, ** P < 0.01) | PMC10273698 | 12885_2023_11068_Fig7_HTML.jpg |
0.466864 | 10c6f3a2602f43a7912b9ecc5578b4c1 | Models of sustained attention (Chun, Golomb & Turk-Browne, 2011).Task performance is influenced by various factors, including arousal, attentional allocation, and information processing. Arousal is the level of physiological and psychological activation, which can be determined by various factors, including emotions, motivation, and environmental stimuli. Attentional allocation is influenced by the intrinsic cost of control, motivation, and the degree of arousal. The circles represent the degree of arousal, and the larger the circle, the higher the degree of arousal. Insufficient attentional state in low arousal states affects task performance. The optimal arousal ensures sufficient attention for the task. Excessive arousal states can lead to low task performance due to distraction. Different degrees of arousal are controlled by internal cognition, such as resource-control and opportunity cost, to regulate the proportion of attentional resources. Higher internal controls can handle multitasking or more difficult tasks (the more As in bold), and lower internal controls can only handle single or simple tasks. Blue arrows indicate process of task-unrelated distractors. Red arrows indicate process of task-related targets. | PMC10274610 | peerj-11-15351-g001.jpg |
0.443582 | cc392a53c6244f31bc85ae402bbc849e | A plausible visual sustained attention pathway.From visual cortex, through LPFC, two major routes have been described, a dorsal pathway through subcortical structures (and related areas), and a ventral pathway through IT cortex. The visual attention dorsal pathway has been implicated in top-down attention at objects, features, or regions in space for sustained periods of time (the black solid line), while the ventral pathway represents bottom-up attention is transiently captured (the gray solid line) (Pinto et al., 2013; Conway, 2014). The brain network of visual sustained attention consists of sub-networks including cingulate cortex, LPFC, thalamus, insula, BG, and IT (Jagtap & Diwadkar, 2016). These sub-networks are responsible for functions including regulation, error monitoring or processing, and sustained vigilance. In addition to forebrain, the midbrain LC can also regulate sustained attention by secreting neurotransmitters (the black dashed line). LPFC, lateral prefrontal cortex; pre-SMA, pre-supplementary motor area; ACC, anterior cingulate cortex; PCC, posterior cingulate cortex; IT, inferotemporal; BG, basal ganglia; LC, locus-coeruleus. | PMC10274610 | peerj-11-15351-g002.jpg |
0.434493 | d0ef9cd8763346cc850a2b604f707945 | Growth of machine learning and deep learning in sustained attention.Papers involving sustained attention and computational method were identified with a search for “machine learning” or “deep learning” and ”sustained attention” on Google Scholar. | PMC10274610 | peerj-11-15351-g003.jpg |
0.444558 | 6c4289db69804210a5ca7c61176fb9e9 | Dose-response determination for IV oxycodone self-administration in male and female rats.Male (n = 10) and female (n = 7) Long-Evans rats were trained to self-administer 0.03 mg/kg/inf oxycodone under a FR1 schedule of reinforcement followed by a dose-response determination. (A) Number of sessions required to reach stable self-administration at each unit dose of oxycodone. (B) Active lever presses (filled symbols) and inactive lever presses (empty symbols) maintained by each dose of oxycodone. (C) Rates of responding (responses per minute) on the active lever (filled symbols) and inactive lever (empty symbols) maintained by each dose of oxycodone. (D) Number of infusions earned at each dose of oxycodone. All data are presented as mean ± SEM values. * p < 0.05, ** p < 0.01, **** p < 0.0001, Dunnett’s test comparing active lever responding maintained by oxycodone vs. saline collapsed across sex (B-C) or Tukey’s test comparing oxycodone doses collapsed across sex (D). # p < 0.05, ## p < 0.01, Dunnett’s test comparing inactive lever responding maintained by oxycodone vs. saline collapsed across sex (B-C). “Sal”, saline. Absence of error bars indicates that SEM values did not extend beyond the limits of the depicted symbol. | PMC10274722 | nihpp-2023.06.02.543393v1-f0001.jpg |
0.440146 | 22a61dffa6cc40fbabc5b2295e6d9a75 | IV oxycodone self-administration behavior in male and female rats used in Experiment 2.Male (n = 8) and female (n = 14) Long-Evans rats self-administered 0.03 mg/kg/inf oxycodone for 8 sessions (sessions 1–8) followed by 10 sessions at 0.01 mg/kg/inf (sessions 9–18) under a FR1 schedule of reinforcement. (A) Active and inactive lever presses (filled and empty symbols, respectively) and (B) number of oxycodone infusions earned across sessions. The vertical dashed line in A and B indicates the transition from 0.03 to 0.01 mg/kg/inf oxycodone availability. Data are presented as mean ± SEM values. | PMC10274722 | nihpp-2023.06.02.543393v1-f0002.jpg |
0.409239 | 2ee9b63267ec4daf9ea9fb7a36ccd92a | Comparison of IV oxycodone self-administration in female rats during proestrus/estrus vs. metestrus/diestrus.Female (n = 14) Long-Evans rats self-administered 0.03 mg/kg/inf oxycodone for 8 sessions (sessions 1–8) followed by 10 sessions at 0.01 mg/kg/inf (sessions 9–18) under a FR1 schedule of reinforcement. (A) Active lever presses, (B) inactive lever presses, (C) active lever response rate, (D) inactive lever response rate, and (E) oxycodone infusions earned during proestrus/estrus or metestrus/diestrus, calculated from sessions 5–8 (0.03 mg/kg/inf) and sessions 13–18 (0.01 mg/kg/inf) of oxycodone self-administration (see Fig. 2). The horizontal dashed line in E indicates the maximum number of reinforcers allowed. Data are presented as individual data points with connecting lines representing within-subject repeated sampling across estrous cycle phases, superimposed over bars depicting mean values. * p < 0.05, ** p < 0.01, main effect of estrous cycle phase (proestrus/estrus vs. metestrus/diestrus). “P”, proestrus; “E”, estrus; “M”, metestrus; “D”, diestrus; “N.S.”, not significant. | PMC10274722 | nihpp-2023.06.02.543393v1-f0003.jpg |
0.410205 | 4e009baffd7f430a8bace629c9f975c8 | Reinstatement of oxycodone-seeking behavior and reacquisition of oxycodone self-administration in male and female rats.Male and female Long-Evans rats that had previously self-administered oxycodone (see Fig. 2 for details) underwent extinction training followed by stress-induced and cue-induced reinstatement tests. (A) Active lever presses and (B) inactive lever presses in the last 2 sessions of extinction training (empty bars and symbols) and during a subsequent test session of footshock-induced reinstatement (red/pink bars and symbols). (C) Active lever presses and (D) inactive lever presses in the last 2 sessions of extinction training (empty bars and symbols) and during a subsequent test session of cue-induced reinstatement (purple/violet bars and symbols). (E) Active lever presses and (F) inactive lever presses in the last 2 sessions of extinction training (empty bars and symbols) and during a subsequent self-administration session with 0.01 mg/kg/inf oxycodone available (dark gray/light gray bars and symbols). Data are presented as scatter plots with individual subjects represented by circles, superimposed over bars depicting group mean ± SEM values. * p < 0.05, ** p < 0.01, main effect of (C) reinstatement phase or (E, F) reacquisition. “FS”, footshock; “Reinst”, reinstatement; “P”, proestrus; “E”, estrus; “M”, metestrus; “D”, diestrus; “N.S.”, not significant. n = 6–10/group. | PMC10274722 | nihpp-2023.06.02.543393v1-f0004.jpg |
0.527795 | 5fdcaef823794656abc45b3642d977a8 | Predicted contributions of PFOA in drinking water on serum PFOA levels. (A) Predicted impact on serum PFOA levels exclusively from long-term consumption of drinking water with varying PFOA concentrations. Predicted serum PFOA levels were calculated for lifetime mean water intake (0.017L/kg/d; blue circles and line) and lifetime 95th percentile intake (0.044L/kg/d; orange squares and line) from the U.S. EPA Exposures Factors Handbook. Scenario assumes drinking water is the only source of PFOA exposure. (B) Predicted impact on total serum PFOA level from long-term consumption of PFAS-containing drinking water. Serum PFOA levels calculated in (A) were added to the 2017–2018 NHANES median serum level. Scenario assumes 2017–2018 NHANES median serum level is due to non–drinking water exposures. The red dotted line demarcates the NASEM border between no expected health effects (<2 ng/mL) and potential for health effects in sensitive populations (≥2 ng/mL). All inputs and predicted levels are shown in Table 1. Note: NASEM, National Academies of Science, Engineering, and Mathematics; NHANES, National Health and Nutrition Examination Survey; PFAS, per- and polyfluoroalkyl substances; PFOA, perfluorooctanoic acid; U.S. EPA, U.S. Environmental Protection Agency. | PMC10275357 | ehp12405_f1.jpg |
0.473322 | 24e6769aa9084d85b038a2f5adaa6550 | Distribution of survey participants by states and regions of Myanmar.Of participants (MLF n = 14, BI n = 15) who completed qualitative interviews, 20 (69%) were male and 9 (31%) were female, with median age 43 years (IQR 27–48). Twenty-three participants (MLF n = 8, BI n = 15) were residents of Yangon and 13 participants from the Burnet clinic were on methadone. Most participants (n = 26, 90%) achieved cure following HCV treatment. | PMC10275420 | pgph.0000902.g001.jpg |
0.527874 | 20a9415f79bd4324b7002422c22c57d0 | Flow chart of participants. | PMC10275433 | pone.0287428.g001.jpg |
0.421181 | 516de835dee94b61af08c757c1d87d0c | Odds of intention to leave healthcare by predictor variables. | PMC10275433 | pone.0287428.g002.jpg |
0.399967 | 4c69574ab2ff410f84a6cfde9e1a522f | Palpable breast disease pre-/post-COVID-19. | PMC10275681 | IJBC2023-6278236.001.jpg |
0.406322 | 1f934b77d99a45418692f4777965953f | Structure and fabrication process of the wearable heater(A) Components and structure of the wearable heater.(B) Photograpic image of wearable heater with high transparency.(C) Manufacturing process of wearable heater.(D) Photographic image of the patterned LM trace after the electrode connecting step.(E) Microscopic image of the LM 3D structure for electrical connection between the LM trace and FPCB electrodes.(F) Cross-sectional microscope image of the wearable heater. | PMC10275728 | gr1.jpg |
0.368569 | ca9240ab583a487784b210a1b861791b | Electric and temperature properties at stretching with density and direction of pattern(A) Photographic image of LM Patterned wearable heater with different x/y ratios.(B) Optical transmittance of the fabricated wearable heater for sample A–C.(C) IR image of heated sample A, B, and C with 2 W input power.(D) Average temperature of heating area when the samples A–C generate heat with 2W input power.(E) IR images of the heated sample B under 0% and 50% strain with different input voltage.(F) Normalized electrical resistance changes of the sample A with stretching under 100% strain.(G) Normalized electrical resistance changes of the sample A with 10 cycles stretching under various strain conditions and returned to its original state. | PMC10275728 | gr2.jpg |
0.453786 | 9d814863457e4737a5958bcb7d87bb33 | The Peano-serpentine patterned LM wearable heater(A) Photographic image of the wearable heaters with various Peano curves and serpentine pattern.(B) Normalized electrical resistance changes of the Peano curves and serpentine patterned heaters with stretching under 100% strain.(C) Mechanical stability test for the Peano-serpentine patterned heater measured by repeated 100% strain over 1700 cycles.(D) IR images and average temperature change as a result of the increasing voltage up to 6V without stretching.(E) IR images and average temperature under increasing strain during heating. | PMC10275728 | gr3.jpg |
0.447531 | 731642aff5e64d67919c308adcd7cc05 | Circuit control design and human body model application(A) Graphic image of the experimental setup with a smartphone app for power control of the heater, an IR camera for temperature measurement, and a mannequin structure that can reproduce human elbow movement.(B) Changes in applied voltage and current to the heater observed in response to variations in duty cycle and heater resistance.(C) The measurement accuracy varied with changes in circuit voltage, current, and power.(D) Heater temperature and joint angle in response to movement of the mannequin’s elbow joint while 1 W of power was applied to the heater, along with photographic and IR camera images of the heater. | PMC10275728 | gr4.jpg |
0.454568 | 8385c46abe93430290f3d9bf9e4392c8 | A (i) Schematic illustrating the structure of ARV7 generated by splicing cryptic exon 3 after exons 1-3. Western blot showing abundance of ARV7 proteins in relation to housekeeping GAPDH in (ii) LNCaP, VCaP (iii) 22Rv1 GFP and 22Rv1 shARV7 and (iv) PCR assessment showing fold change of mRNA levels relative to GAPDH (n=3). The blots are representative of experiments repeated three times. The PCR is the mean of three independent experiments. Melt curves were performed for each RT-PCR analysis to ensure that no non-specific amplification was occurring (data not shown). B. Indicates graphs showing a dose-dependent response to cabazitaxel with 50% inhibitory concentrations (IC50) in LNCaP (i), VCaP(ii), 22Rv1 GFP (iii) and 22Rv1 shARV7 (iv) cell lines (n=3 or more) and to enzalutamide with IC50 in LNCaP (v), VCaP (vi), 22Rv1 GFP (vii) and 22Rv1 shARV7 (viii) cell lines (n=3 or more). | PMC10276180 | gr1a.jpg |
0.497092 | e8f97f7d0015419ea34171b0addc652a | Time-lapse was set to capture images every 10min over 48h, selecting at least 5 different regions per well. Average cell number or cell motility (um) per each region/per timepoint was normalised to the control at 0h. A. Graphs showing (i) changes in average cell motility in um over time for 22Rv1 GFP and shARV7 cells. Data points with SD from 3 or more repeats. (ii & iii) Rose plots representing cell movement trajectories for 22Rv1 shARV7 cells and for 22Rv1 GFP cells respectively. Movement trajectory of each cell overlayed in a xyz- position plot, was tracked over time and rose plots containing bigger “rose” indicated increased migration. Each colour of the lines represented the migration trajectory of individual cells. B. Graphs showing (i) changes in average cell proliferation over time normalized to 0h control for 22Rv1 GFP and shARV7 cells. Data points with SD from 3 or more repeats. Cell family tree plots representing cell division rate for 22Rv1 shARV7 cells (ii) and 22Rv1 GFP cells (iii) over time. Cell family plots were derived based on tracking each individual cell, together with its daughter cells after division. This gives information about the time of each cell division per position/ per treatment. Each coloured cell line represents individual cell and each fork on the line represents cell division. | PMC10276180 | gr2.jpg |
0.478543 | b0f8d8b49e4c4a968d3016812036c23e | A. Shows representative western blots indicating the abundance of FOXA1 and IGFBP-2 proteins in relation to housekeeping GAPDH in 22Rv1 GFP versus 22Rv1 shARV7. Graphs on the right show relative fold changes of optical density (OD) (n=3). B. Represents the correlations between tissue-based ARV7 and AR peptide abundance from samples of prostate collected during the PrEvENT trial. Spearman correlation is shown with r, p values. | PMC10276180 | gr3.jpg |
0.50866 | d3d46775da65486d8de874b122dd1dc9 | A. Shows correlations between tissue-based ARV7 and IGFBP-2 (i & ii) or FOXA1 (iii & iv) peptide abundance and B Shows correlations between tissue-based AR and IGFBP-2 (i & ii) or FOXA1 (iii & iv) peptide abundance from samples of prostate collected during the PrEvENT trial. Spearman correlation represented with r, p values. | PMC10276180 | gr4.jpg |
0.481463 | 61da9d55907b450cb9e269839fcc59a3 | Representative images of immunohistochemical staining (IHC) of ARV7, FOXA1 and IGFBP-2 from samples of prostate collected during the PrEvENT trial. Two patients from 3+4 and two patients from 4+3 grades were selected. | PMC10276180 | gr5.jpg |
0.411644 | baa804703b354a0c9e57f34464102aa9 | Double deletion of PDR1 and PDR3 genes decreases growth rate in the presence of tyrosol. Representative growth curves of WT (W303-1A KanMX4) and Δpdr1Δpdr3 strains in the control conditions (A) and in the presence of tyrosol, 6 g/L (B). p < 0.05 according to Wilcoxon rank sum exact test for the comparison of growth rates of WT and Δpdr1Δpdr3 strains. (C) Growth rates (μmax) in the presence of 2-phenylethanol, tryptophol and tyrosol. (D) WT yeast cells incubated with tyrosol (8 g/L, 1 h of incubation) do not accumulate propidium iodide (PI). Yeast control cells untreated with tyrosol and yeast cells killed with 70% (v/v) ethanol are shown as the negative and the positive controls. | PMC10277503 | fmicb-14-1203243-g001.jpg |
0.443235 | 4ce50a8af67e4565b528ba54ef599c7f | PDR5 deletion aggravates the inhibitory effect of tyrosol on yeast growth. Growth rates (μmax) of yeast strains with deleted MDR genes; the growth rate of control parental strain WT (BY4741) is shown on all facets as the green long-dash line. | PMC10277503 | fmicb-14-1203243-g002.jpg |
0.430883 | 3d15dfea53f84485ac18e14e06c57150 | Tyrosol inhibits glucose-stimulated rhodamine 6G efflux from yeast cells. We monitored rhodamine 6G efflux from yeast cells by the increase in fluorescence (excitation wavelength λ = 480 nm, emission wavelength λ = 560 nm; see Material and methods sections for more details). Wild type W303-1A KanMX4
(A) or Δpdr1Δpdr3
(B) yeast cells were supplemented first with tyrosol or solvent (1, indicated by arrow), and then with glucose (2, indicated by arrow). (C) Quantification of the results from three separate day experiments. *corresponds to p < 0.05 according to Wilcoxon rank sum exact test. | PMC10277503 | fmicb-14-1203243-g003.jpg |
0.530283 | 8a4a5224ad2646bb81c4a0cbdd71b45b | Tyrosol decreases the concentration of MDR-transporter substrate Nile Red in yeast cells. (A) Supplementation of tyrosol (4 g/L) to the yeast suspension does not change the accumulation levels of Nile red in wild type W303-1A KanMX4 yeast cells (left). One hour preincubation of yeast cells with tyrosol (4 g/L) inhibits Nile red accumulation in yeast cells (right). (B) Quantification of the results for different concentrations of the Nile red. Median Nile red level in untreated cells was set as 100%, mean autofluorescence signal was subtracted. *corresponds to p < 0.05 according to Wilcoxon rank sum exact test. | PMC10277503 | fmicb-14-1203243-g004.jpg |
0.442636 | 4a21e16e0e32441aa7b8cf5059986d8d | Tyrosol induces accumulation of Pdr5-GFP in the yeast plasma membrane. (A) Flow cytometry analysis was conducted to measure the levels of Pdr5-GFP in yeast cells treated with 2-phenylethanol (1 g/L), tyrosol (4 g/L), and tryptophol (0.75 g/L) for 1 h. (B) The localization of the GFP signal in yeast cells treated with 2-phenylethanol (2 g/L), tyrosol (4 g/L), and tryptophol (1 g/L); (C) Quantification of the flow cytometry results for yeast cells treated with tyrosol (1 and 2 h), dots represent mean Pdr5-GFP fluorescence from a separate experiment (10,000 events, n = 4). The dashed line represents the mean fluorescence of Pdr5-GFP before the addition of aromatic alcohols. | PMC10277503 | fmicb-14-1203243-g005.jpg |
0.452159 | d5e134a59e51443bacc3da8cd3de9512 | Tyrosol cancels the growth inhibition effect of clotrimazole. We analyzed the growth rate (μmax) in WT (W303-1A KanMX4) and Δpdr1Δpdr3 strains to determine the effect of tyrosol on the cytostatic effect of clotrimazole. The lines on the graph represent the average μmax of 3–6 independent experiments. | PMC10277503 | fmicb-14-1203243-g006.jpg |
0.415995 | 73e8c66f84fb47878f9c2740a7708f6b | Association of (a) FS, (b) intrinsic sugars, (c) FS in beverages and (d) FS in solids intake (all g/d) with all-cause mortality. Models are adjusted for energy intake, age, sex, ethnic background, BMI, systolic blood pressure, Townsend deprivation index, general health status, total household income, highest qualification, smoking status, alcohol intake, physical activity and history of psychiatric disease as summarised in the Methods section. Covariates not fulfilling the proportional hazard assumption are stratified. The nadir is indicated in blue. FS, free sugars; HR, hazard ratio. | PMC10277665 | S0007114522003233_fig1.jpg |
0.420593 | e5d432829fb342fda8f65fbc3c98daea | Association of free sugars (FS) in (a) soda/fruit drinks, (b) juice, (c) milk-based drinks and (d) tea/coffee (all g/d) with all-cause mortality. Models are adjusted and presented as indicated in Fig. 1. | PMC10277665 | S0007114522003233_fig2.jpg |
0.41731 | a586eca4f8964d0ba64b181a9d4c24d9 | Association of free sugars (FS) in (a) treats, (b) cereals, (c) toppings and (d) sauces (all g/d) with all-cause mortality. Models are adjusted and presented as indicated in Fig. 1. | PMC10277665 | S0007114522003233_fig3.jpg |
0.408631 | 79c5480293294de3ac3e50e6afdef20a | Deviating bar plot showing rates of concomitant injuries and surgical procedures in early and delayed multiligament PCL-R Asterisks (*) denote significant between-group differences at p < 0.05. ACL-R = anterior cruciate ligament reconstruction; LCL-R/PLC-R = lateral collateral ligament reconstruction/posterolateral corner reconstruction; MCL = medial collateral ligament; MCL-R/PMC-R = medial collateral ligament reconstruction/posteromedial corner reconstruction; PCL-R = posterior cruciate ligament reconstruction | PMC10278257 | 12891_2023_6638_Fig1_HTML.jpg |
0.550296 | b6c905e3d2cf48498b4cb26f47a8deb2 | IGFBP-3 decreased lipogenesis and increased lipolysis. (A) 3T3-L1 adipocytes were treated with different doses of synthetic IGFBP-3 as indicated for 12 h. Lipolysis rate was determined using the Free Glycerol Reagent (Sigma). (B) 3T3-L1 adipocytes were treated with 14C-labeled glucose together with different doses of synthetic IGFBP-3 for 12 h as indicated. Lipogenesis rate was measured by liquid scintillation counting. (C, D) 3T3-L1 adipocytes were treated with synthetic IGFBP-3 for 12 h, and TAG levels were determined by biochemical assay. Representative photos indicate the neutral lipids stained by BODIPY. * P <0.05 by two-tailed unpaired Student’s t test. BODIPY: Dipyrromethene Boron Difluoride; IGFBP-3: Insulin-like growth factor (IGF) binding protein-3; TAG: Triacylglycerol. | PMC10278738 | cm9-136-0974-g001.jpg |
0.549134 | df5d205010a6435f91a354f80e9793d0 | IGFBP-3 decreased IGF/insulin signaling and dysregulated the expression of lipid metabolic genes. (A) 3T3-L1 adipocytes were treated with different doses of synthetic IGFBP-3 as indicated for 12 h. The expression of phosphorylation of Akt at Ser473 and Akt protein as well as phosphorylation of PKA substrate was determined using Western blot analysis. (B, C) RT-qPCR was performed to examine the mRNA level of lipogenic genes ( Acc1, Acly, and Fasn) and lipolytic genes ( Atgl and Hsl). * P <0.05 vs. control. (D) 3T3-L1 adipocytes were treated with different doses of IGF-1 (0 ng/mL, 2 ng/mL, and 20 ng/mL) plus 1 µg/mL IGFBP-3 for 1 h. Western blot analysis was performed to determine the expression of p-Akt (Ser473) and Akt. (E) RT-qPCR analysis of the expression of Atgl and Fasn in 3T3-L1 adipocytes treated with IGF-1, IGFBP-3, or both for 12 h. Lipolysis was determined using the Free Glycerol Reagent (Sigma). BSA: Bovine serum albumin; Con: Control; FBS: Fetal bovine serum; IGFBP-3: Insulin-like growth factor (IGF) binding protein-3; mRNA: Messenger ribonucleic acid; N.S.: No significance; pAkt: Phosphorylated Akt; PKA: Protein kinase A; RT-qPCR: Real-time quantitative polymerase chain reaction. | PMC10278738 | cm9-136-0974-g002.jpg |
0.468056 | 3086d0345692460e85bc1369faed3c17 | Cachectic tumor cells produced IGFBP-3 to suppress IGF signaling in adipocytes. (A, B) The expression of IGFBP-3 mRNA was analyzed in two independent published datasets (GSE16515 and GSE15471). (C) Western blot analysis on the expression of IGFBP-3 was performed in 3T3-L1 adipocytes as well as C26 and Capan-1 cells. (D, E) 3T3-L1 adipocytes were treated with conditioned medium (CM) from Capan1 or C26 cells with or without IGFBP-3 neutralizing antibody for 1 h. Western blot analysis of the expression of p-Akt (Ser473) and Akt was shown. (F, G) RT-qPCR was performed to determine the mRNA level of Atgl and Fasn in 3T3-L1 adipocytes treated as indicated for 12 h. * P <0.05 vs. control. Ab: Antibody; Ab-IGFBP-3: Antibody of IGFBP-3; Con: Control; IGFBP-3: Insulin-like growth factor (IGF) binding protein-3; mRNA: Messenger ribonucleic acid; N.S.: No significance; pAkt: Phosphorylated Akt; RT-qPCR: Real-time quantitative polymerase chain reaction. | PMC10278738 | cm9-136-0974-g003.jpg |
0.390724 | f8936c86d3ff4456a46718b15b14a209 | Cachectic tumor cells secreted IGFBP-3 to cause lipid loss in adipocytes. 3T3-L1 adipocytes were treated with CM from Capan1 or C26 cells without or with different doses of IGFBP-3 neutralizing antibody for 12 h. Lipolysis rate (A, E), lipogenesis rate (B, F), and TAG level (C, G) were examined. (D original magnification × 200, H original magnification ×200) The neutral lipids were stained with BODIPY and representative photos were indicated. Ab: Antibody; CM: Conditioned medium; Con: Control; IGFBP-3: Insulin-like growth factor (IGF) binding protein-3; TAG: Triacylglycerol. | PMC10278738 | cm9-136-0974-g004.jpg |
0.42679 | 900c45907de74bfb9f049fe1dc4e0b10 | IGFBP-3 failed to affect the growth of cachectic cancer cells. (A, D) C26 cells were treated with different doses of IGFBP-3 or IGFBP-3 neutralizing antibody as indicated for 12 h. The expression of pAkt (Ser473) and Akt was shown using Western blot analysis. (B, E) Cell proliferation after IGFBP-3 treatment for three days was examined by MTT assay. (C, F) Cell morphology was observed by optical microscopy (C and F original magnification × 200). Ab: Antibody; IGFBP-3: Insulin-like growth factor (IGF) binding protein-3; MTT: Methyl thiazolyl tetrazolium assay; pAkt: Phosphorylated Akt. | PMC10278738 | cm9-136-0974-g005.jpg |
0.485576 | e2762c8d64b149708fb79eb289680244 | Gut tumors produced IGFBP-3 homolog to cause lipid loss in Drosophila. (A, B) Knockdown of ImpL2 or overexpression of ILP2 in yki-tumors at day 8 improved host abdominal fat in yki-gut Drosophila, and statistical analysis of abdomen bloating was performed ( n = 3, 5 flies/replicate) (A, [original magnification × 400]). Fat-body-specific reporter indicates depletion of this tissue in the abdomen of hosts in the presence of the tumor. Green indicates lipid droplets, which are the storage vesicles of the adipose tissue. (B) RT-qPCR was performed to determine the mRNA level of Fas and Bmm in gut tumors of Drosophila. (C) The bloating rates of wild-type yki, knock-down ImpL2 in yki-tumors and overexpression of ILP2 in yki-tumors, respectively. (D, E) The levels of TAG and trehalose were determined ( n = 3, 30 flies/group). * P <0.05 by two-tailed unpaired Student's t-test. IGFBP-3: Insulin-like growth factor binding protein-3; ILP2: Insulin-like peptide 2; ImpL2-i: ImpL2-RNAi; mRNA: Messenger ribonucleic acid; RT-qPCR: Real-time quantitative polymerase chain reaction; TAG: Triacylglycerol; w: Wild type. | PMC10278738 | cm9-136-0974-g006.jpg |
0.484948 | bd6e9117f6de47f6a119e18076d79674 | IGFBP-3 was highly expressed in cancer tissues and serum of cachectic cancer. (A) Gene Expression Profiling Interactive Analysis (GEPIA) indicated IGFBP-3 was highly expressed in pancreatic cancer tissues ( P <0.05) and colorectal cancer tissues ( P >0.05) compared with normal tissues. (B, C) The association of the expression of IGFBP-3 with overall survival was analyzed using Kaplan–Meier (KM) plotter ( https://kmplot.com/analysis) in both PAAD and COAD. The patients were divided by high and low IGFBP-3 expression levels using the auto-select best cutoff, and log-rank P-value was shown. (D) The serum level of IGFBP-3 in cachectic and non-cachectic colorectal cancer patients was determined by ELISA assay. This graph was generated using Graphpad prism 9. * P <0.05. COAD: Colonic adenocarcinoma; ELISA: Enzyme linked immunosorbent assay; HR: Hazard ratio; IGFBP-3: Insulin-like growth factor (IGF) binding protein-3; PAAD: Pancreatic adenocarcinoma; READ: Rectal adenocarcinoma. | PMC10278738 | cm9-136-0974-g007.jpg |
0.422127 | d4fbd594db9249e8aa4c04b7d9fa4279 | Schematic depiction of cachectic tumor cells-derived IGFBP-3 stimulates lipid loss by antagonizing IGF/insulin signaling. IGFBP-3: Insulin-like growth factor (IGF) binding protein-3. | PMC10278738 | cm9-136-0974-g008.jpg |
0.441071 | 0ebe6e27890f42c1a5dc5bb5bcd39754 | Restriction map of pBFK thermosensitive plasmid used for homologous recombination in GAS strain. spc: spectinomycin-resistance gene expressed in Gram-positive bacteria, ampR: ampicillin-resistance gene expressed in Gram-negative bacteria. Black arrows represent the restriction sites used for resistance-marker replacement. | PMC10279790 | gr1.jpg |
0.486251 | 7f8030819bf64a26850dcfd314c7c714 | Successive steps conducted to isogenic mutant construct. Primers are represented by small arrows with homologous regions defined by the same colour. Electrophoresis gel on the right of the third step represents amplicons obtained after PCR on GAS gDNA after plasmid excision from different strains (indicated by the number on the top of the gel): 1: STAB11064 (control), 2: Isolate with the wild-type allele, 3: Strain with the mutant allele (grab deleted). The letter “L” indicates the ladder used with amplicon sizes indicated on the left of the gel. | PMC10279790 | gr2.jpg |
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