Aeroelastic simulations of stores in weapon bays using Detached-Eddy simulation

Detached-Eddy Simulations of flows in weapon bays with a generic store at different positions in the cavity and with flexible fins are presented in this paper. Simulations were carried out to better understand the fluid–structure interactions of the unsteady, turbulent flow and the store. Mach and Reynolds numbers (based on the missile diameter) were 0.85 and 326.000 respectively. Spectral analysis showed few differences in the frequency content in the cavity between the store with rigid and flexible fins. However, a large effect of the store position was seen. When the store was placed inside the cavity, the noise reduction reached 7 dB close to the cavity ceiling. The closer the store to the carriage position, the more coherent and quieter was the cavity. To perform a more realistic simulation, a gap of 0.3% of the store diameter was introduced between the fin root and the body of the store. Store loads showed little differences between the rigid and flexible fins when the store was inside and outside the cavity. With the store at the shear layer, the flexible fins were seen to have a reduction in loads with large fluctuations in position about a mean. Fin-tip displacements of the store inside the cavity were of the range of 0.2% of the store diameter, and in the range of 1–2% of store diameter when at the shear layer

Gauge and Scheme Dependence of Mixing Matrix Renormalization

We revisit the issue of mixing matrix renormalization in theories that include Dirac or Majorana fermions. We show how a gauge-variant on-shell renormalized mixing matrix can be related to a manifestly gauge-independent one within a generalized ${\bar {\rm MS}}$ scheme of renormalization. This scheme-dependent relation is a consequence of the fact that in any scheme of renormalization, the gauge-dependent part of the mixing-matrix counterterm is ultra-violet safe and has a pure dispersive form. Employing the unitarity properties of the theory, we can successfully utilize the afore-mentioned scheme-dependent relation to preserve basic global or local symmetries of the bare Lagrangian through the entire process of renormalization. As an immediate application of our study, we derive the gauge-independent renormalization-group equations of mixing matrices in a minimal extension of the Standard Model with isosinglet neutrinos.Comment: 31 pages, LaTeX, uses axodraw.st

Burden and risk factors for Pseudomonas aeruginosa community-acquired pneumonia:a Multinational Point Prevalence Study of Hospitalised Patients

Pseudornonas aeruginosa is a challenging bacterium to treat due to its intrinsic resistance to the antibiotics used most frequently in patients with community-acquired pneumonia (CAP). Data about the global burden and risk factors associated with P. aeruginosa-CAP are limited. We assessed the multinational burden and specific risk factors associated with P. aeruginosa-CAP. We enrolled 3193 patients in 54 countries with confirmed diagnosis of CAP who underwent microbiological testing at admission. Prevalence was calculated according to the identification of P. aeruginosa. Logistic regression analysis was used to identify risk factors for antibiotic-susceptible and antibiotic-resistant P. aeruginosa-CAP. The prevalence of P. aeruginosa and antibiotic-resistant P. aeruginosa-CAP was 4.2% and 2.0%, respectively. The rate of P. aeruginosa CAP in patients with prior infection/colonisation due to P. aeruginosa and at least one of the three independently associated chronic lung diseases (i.e. tracheostomy, bronchiectasis and/or very severe chronic obstructive pulmonary disease) was 67%. In contrast, the rate of P. aeruginosa-CAP was 2% in patients without prior P. aeruginosa infection/colonisation and none of the selected chronic lung diseases. The multinational prevalence of P. aeruginosa-CAP is low. The risk factors identified in this study may guide healthcare professionals in deciding empirical antibiotic coverage for CAP patients

The fitness cost and benefit of phase-separated protein deposits

Phase separation of soluble proteins into insoluble deposits is associated with numerous diseases. However, protein deposits can also function as membrane-less compartments for many cellular processes. What are the fitness costs and benefits of forming such deposits in different conditions? Using a model protein that phase-separates into deposits, we distinguish and quantify the fitness contribution due to the loss or gain of protein function and deposit formation in yeast. The environmental condition and the cellular demand for the protein function emerge as key determinants of fitness. Protein deposit formation can influence cell-to-cell variation in free protein abundance between individuals of a cell population (i.e., gene expression noise). This results in variable manifestation of protein function and a continuous range of phenotypes in a cell population, favoring survival of some individuals in certain environments. Thus, protein deposit formation by phase separation might be a mechanism to sense protein concentration in cells and to generate phenotypic variability. The selectable phenotypic variability, previously described for prions, could be a general property of proteins that can form phase-separated assemblies and may influence cell fitness.This work was supported by the Medical Research Council (MC_U105185859; M.M.B., M.T., C.R., and N.S.G.), Marie Curie Actions (FP7-PEOPLE-2012- IEF-330352, to M.T.; and FP7-PEOPLE-2011-IEF299105, to N.S.G.), FEBS LongTerm Fellowships (N.S.G.), Beatriu de Pinos fellowships (M.T.), and the Ministerio de Economía y Competitividad (SAF2017-82158-R, SAF2015-72518-EXP, and RYC-2012-09999; M.T.). N.S.G. is a recipient of the MRC Centenary Award. M.M.B. is a Lister Institute Research Prize Fellow. We thank Gian Gaetano for supporting N.S.G. and Sean Munro for the gift of strain Y0315

The fitness cost and benefit of phase-separated protein deposits

Altres ajuts: Beatriu de Pinos fellowshipsPhase separation of soluble proteins into insoluble deposits is associated with numerous diseases. However, protein deposits can also function as membrane-less compartments for many cellular processes. What are the fitness costs and benefits of forming such deposits in different conditions? Using a model protein that phase-separates into deposits, we distinguish and quantify the fitness contribution due to the loss or gain of protein function and deposit formation in yeast. The environmental condition and the cellular demand for the protein function emerge as key determinants of fitness. Protein deposit formation can influence cell-to-cell variation in free protein abundance between individuals of a cell population (i.e., gene expression noise). This results in variable manifestation of protein function and a continuous range of phenotypes in a cell population, favoring survival of some individuals in certain environments. Thus, protein deposit formation by phase separation might be a mechanism to sense protein concentration in cells and to generate phenotypic variability. The selectable phenotypic variability, previously described for prions, could be a general property of proteins that can form phase-separated assemblies and may influence cell fitness

The fitness cost and benefit of phase-separated protein deposits

Phase separation of soluble proteins into insoluble deposits is associated with numerous diseases. However, protein deposits can also function as membrane-less compartments for many cellular processes. What are the fitness costs and benefits of forming such deposits in different conditions? Using a model protein that phase-separates into deposits, we distinguish and quantify the fitness contribution due to the loss or gain of protein function and deposit formation in yeast. The environmental condition and the cellular demand for the protein function emerge as key determinants of fitness. Protein deposit formation can influence cell-to-cell variation in free protein abundance between individuals of a cell population (i.e., gene expression noise). This results in variable manifestation of protein function and a continuous range of phenotypes in a cell population, favoring survival of some individuals in certain environments. Thus, protein deposit formation by phase separation might be a mechanism to sense protein concentration in cells and to generate phenotypic variability. The selectable phenotypic variability, previously described for prions, could be a general property of proteins that can form phase-separated assemblies and may influence cell fitness.This work was supported by the Medical Research Council (MC_U105185859; M.M.B., M.T., C.R., and N.S.G.), Marie Curie Actions (FP7-PEOPLE-2012- IEF-330352, to M.T.; and FP7-PEOPLE-2011-IEF299105, to N.S.G.), FEBS LongTerm Fellowships (N.S.G.), Beatriu de Pinos fellowships (M.T.), and the Ministerio de Economía y Competitividad (SAF2017-82158-R, SAF2015-72518-EXP, and RYC-2012-09999; M.T.). N.S.G. is a recipient of the MRC Centenary Award. M.M.B. is a Lister Institute Research Prize Fellow. We thank Gian Gaetano for supporting N.S.G. and Sean Munro for the gift of strain Y0315