Journal: Noninvasive Ventilation in High-Risk Infections and Mass Casualty Events

Article Title: Noninvasive Mechanical Ventilation: Models to Assess Air and Particle Dispersion

doi: 10.1007/978-3-7091-1496-4_2

Figure Lengend Snippet: Human patient simulator (HPS) lying at 45° on a bed undergoing noninvasive ventilation via the ResMed Mirage face mask. A laser beam located on the right side of the bed lateral to the human patient simulator illuminates the exhaled air particles leaking from the exhalation ports of the face mask in the coronal plane. A camera was positioned along the sagittal plane at the end of the bed to capture lateral dispersion of exhaled air illuminated by the laser device. Positions of the camera and the laser device would be exchanged when the exhaled air dispersion from the face mask is examined along the sagittal plane

Article Snippet: Fig. 2.1 Human patient simulator (HPS) lying at 45° on a bed undergoing noninvasive ventilation via the ResMed Mirage face mask.

Techniques: Dispersion

Journal: BMC Surgery

Article Title: Does a novel 3D printed individualized guiding template based on cutaneous fiducial markers contribute to accurate percutaneous insertion of pelvic screws? A preliminary phantom and cadaver study

doi: 10.1186/s12893-024-02402-6

Figure Lengend Snippet: Results of the Likert scale questionnaire on using the guiding template

Article Snippet: The biomimetic pelvic phantom models are high-fidelity as they highly simulate and reflect actual human anatomy , 5 , Not applicable.

Techniques:

Journal: Nature Metabolism

Article Title: iNOS modulates inflammatory responses in an NO-independent manner through direct interaction with IRG1 in mitochondria

doi: 10.1038/s42255-026-01492-1

Figure Lengend Snippet: a , Representative western blot of two mitochondria isolation preparations (total n = 4 mice); 7 µg of protein for each cell compartment (mitochondria, cytosol or whole lysate) from 18 h LPS/IFNγ-stimulated murine BMDMs (WT iNOS BMDMs treated or not with AG and iNOS-KO BMDMs) was loaded into an SDS–PAGE and further probed with anti-iNOS, anti-IRG1, anti-GAPDH (cytosol control) and anti-VDAC (mitochondria control). b , Immunofluorescence of fixed BMDMs following 18 h LPS/IFNγ stimulation from WT and iNOS-KO mice after incubation with mouse anti-iNOS (AF488), anti-Hsp60 (AF680) and DAPI (blue). Single-channel images, as well as the superposition of channels (merge; yellow), are shown. Three regions of interest (ROIs) for each image were used for colocalization analysis. White indicates colocalization of iNOS and Hsp60 on Hsp60 staining (red). A table summarizing the mean of the colocalization factor and Manders’ coefficient from three ROIs for each animal ( n = 3 mice) is also shown. c – f , Computational predictions of the (IRG1) 2 –(iNOS) 2 heterotetramer using AlphaFold-Multimer for the murine ( c ) and human ( e ) heterotetramer, respectively. The two snapshots are related by a 90 °C rotation around the z axis. The predictions show a well-established interface between the two dimers. c , Predicted structure of the murine IRG1–iNOS heterotetramer (iNOS monomers are in red and pink and IRG1 monomers in blue and lavender) in the presence of calmodulin (orange) and haem and flavins (green). d , Molecular dynamics simulations of the murine IRG1–iNOS heterotetramer. The solid lines represent the number of heavy atom contacts between the (IRG1) 2 and (iNOS) 2 homodimers, and the different colours represent three different 300 ns replicas. The stable conformation observed over the 300 ns trajectory supports the reliability of the predicted protein–protein interface. e , Predicted structure of the human IRG1–iNOS heterotetramer (iNOS monomers are in red and pink and IRG1 monomers in blue and lavender) in the presence of calmodulin (orange) and haem and flavins (green). f , Molecular dynamics simulations of the human IRG1–iNOS heterotetramer. The solid lines represent the number of heavy atom contacts between the (IRG1) 2 and (iNOS) 2 homodimers, and the different colours represent three different 300 ns replicas. The stable conformation observed over the 300 ns trajectory supports the reliability of the predicted protein–protein interface. g – i , Binding kinetics of IRG1 and iNOS measured by surface plasma resonance. g , Multi-cycle kinetics analysis of human IRG1 binding to human iNOS. Surface plasma resonance sensograms show the average response curves from duplicate injections of human IRG1 over a human iNOS-immobilized CM5 sensor chip (25–200 nM). Fitted constants of k a = 6.8 × 10 4 M −1 s −1 and k d = 0.013 s −1 , which results in a K D = 189 nM. h , Multi-cycle kinetics analysis of mouse IRG1 binding to mouse iNOS. Surface plasma resonance sensograms show the average response curves from duplicate injections of mouse IRG1 over a mouse iNOS-immobilized CM5 sensor chip (25–200 nM). Fitted constants of k a = 4.5 × 10 4 M −1 s −1 and k d = 0.008 s −1 , which results in a K D = 174 nM. i , k a , association constant; k d , dissociation constant; K D , equilibrium constant of the IRG1–iNOS interaction for both human and mouse proteins; Cyt., cytosol; Col., colocalization; WColCoef., weighted colocalization coefficient; Unst., unstimulated.

Article Snippet: The stable conformation observed over the 300 ns trajectory supports the reliability of the predicted protein–protein interface. e , Predicted structure of the human IRG1–iNOS heterotetramer (iNOS monomers are in red and pink and IRG1 monomers in blue and lavender) in the presence of calmodulin (orange) and haem and flavins (green). f , Molecular dynamics simulations of the human IRG1–iNOS heterotetramer.

Techniques: Western Blot, Isolation, SDS Page, Control, Immunofluorescence, Incubation, Staining, Binding Assay, Clinical Proteomics

Journal: Nature Metabolism

Article Title: iNOS modulates inflammatory responses in an NO-independent manner through direct interaction with IRG1 in mitochondria

doi: 10.1038/s42255-026-01492-1

Figure Lengend Snippet: a , Predicted structure of the murine IRG1 iNOS heterotetramer (IRG1 monomers are in red and pink and iNOS monomers in sky blue and blue) in the presence of calmodulin (orange and sand colour). c , Molecular dynamics simulations of the murine IRG1-iNOS heterotetramer. The solid lines represent the number of heavy atom contacts between the (IRG1)2 and (iNOS)2 homodimers, and the different colours represent three different 300 ns replicas. The stable conformation observed over the 300 ns trajectory supports the reliability of the predicted protein-protein interface. b , Predicted structure of the human IRG1-iNOS heterotetramer (IRG1 monomers are in red and pink and iNOS monomers in sky blue and blue) d , Molecular dynamics simulations of the human IRG1-iNOS heterotetramer in the presence of calmodulin. The solid lines represent the number of heavy atom contacts between the (IRG1)2 and (iNOS)2 homodimers, and the different colours represent three different 300 ns replicas. The stable conformation observed over the 300 ns trajectory supports the reliability of the predicted protein-protein interface. e , Representative multi-cycle kinetics curves for mouse iNOS on a mouse IRG1 immobilised chip (10 – 80 nM). f , Representative multi-cycle kinetics curves for human iNOS on a human IRG1 immobilised chip (10 – 80 nM). g , Comparison sensorgram of BSA injection (100 nM) on iNOS chip compared to IRG1 (100 nM). h , Average sensograms from injections of IRG1 (200 nM) over iNOS- and eNOS-immobilized chips show differential binding responses.

Article Snippet: The stable conformation observed over the 300 ns trajectory supports the reliability of the predicted protein–protein interface. e , Predicted structure of the human IRG1–iNOS heterotetramer (iNOS monomers are in red and pink and IRG1 monomers in blue and lavender) in the presence of calmodulin (orange) and haem and flavins (green). f , Molecular dynamics simulations of the human IRG1–iNOS heterotetramer.

Techniques: Comparison, Injection, Binding Assay

Journal: Nature Metabolism

Article Title: iNOS modulates inflammatory responses in an NO-independent manner through direct interaction with IRG1 in mitochondria

doi: 10.1038/s42255-026-01492-1

Figure Lengend Snippet: a , AlphaFold Multimer v2.3 prediction of the IRG1-iNOS dimer (IRG1 monomer with iNOS monomer). b , Molecular dynamics simulations at different temperatures showing that the interaction between the units is stable. c , MM/GBSA free energy calculations of three snapshots of the molecular dynamics simulations.

Article Snippet: The stable conformation observed over the 300 ns trajectory supports the reliability of the predicted protein–protein interface. e , Predicted structure of the human IRG1–iNOS heterotetramer (iNOS monomers are in red and pink and IRG1 monomers in blue and lavender) in the presence of calmodulin (orange) and haem and flavins (green). f , Molecular dynamics simulations of the human IRG1–iNOS heterotetramer.

Techniques: