How well do European child-related leave policies support the caring role of fathers?

Our chapter analyses the extent to which European countries (1) recognize the caring responsibilities of fathers toward their children and (2) value fathers' caring role. To do so, we analyze the designs of individual leave policies and reflect on them by assessing available data on leave uptake by fathers in 13 European countries. Our results show that there is great variation in child-related leave designs across Europe. Our findings, in line with previous work, underscore the importance of generous individual non-transferable leave entitlements. Moreover, our findings bring forward aspects of leave designs that are rarely discussed when considering fathers' leave uptake. Our results indicate that generous non-transferable leave rights should be paired with (a) clearly defined leave periods for fathers, (b) individual entitlement to benefits, and (c) greater scope for flexibility to increase the attractiveness of child-related leave and to strengthen fathers' position when negotiating their childcare leave.</p

Non-Ergodicity in open quantum systems through quantum feedback

It is well known that quantum feedback can alter the dynamics of open quantum systems dramatically. In this paper, we show that non-Ergodicity may be induced through quantum feedback and resultantly create system dynamics that have lasting dependence on initial conditions. To demonstrate this, we consider an optical cavity inside an instantaneous quantum feedback loop, which can be implemented relatively easily in the laboratory. Non-Ergodic quantum systems are of interest for applications in quantum information processing, quantum metrology and quantum sensing and could potentially aid the design of thermal machines whose efficiency is not limited by the laws of classical thermodynamics

Genetic diversity of the O antigens of <i>Proteus</i> species and the development of a suspension array for molecular serotyping

<div><p><i>Proteus</i> species are well-known opportunistic pathogens frequently associated with skin wound and urinary tract infections in humans and animals. O antigen diversity is important for bacteria to adapt to different hosts and environments, and has been used to identify serotypes of <i>Proteus</i> isolates. At present, 80 <i>Proteus</i> O-serotypes have been reported. Although the O antigen structures of most Proteus serotypes have been identified, the genetic features of these O antigens have not been well characterized. The O antigen gene clusters of <i>Proteus</i> species are located between the <i>cpxA</i> and <i>secB</i> genes. In this study, we identified 55 O antigen gene clusters of different <i>Proteus</i> serotypes. All clusters contain both the <i>wzx</i> and <i>wzy</i> genes and exhibit a high degree of heterogeneity. Potential functions of O antigen-related genes were proposed based on their similarity to genes in available databases. The O antigen gene clusters and structures were compared, and a number of glycosyltransferases were assigned to glycosidic linkages. In addition, an O serotype-specific suspension array was developed for detecting 31 <i>Proteus</i> serotypes frequently isolated from clinical specimens. To our knowledge, this is the first comprehensive report to describe the genetic features of <i>Proteus</i> O antigens and to develop a molecular technique to identify different <i>Proteus</i> serotypes.</p></div

The hybridization results of the 31 <i>Proteus</i> strains.

<p>The suspension arrays were divided into 3 groups: (A) O1, O2, O9, O17, O20, O21, O23ac, O30, O32 and O47; (B) O5, O6, O8, O11, O12, O27, O29a, O31ab and O45; (C) O3ab, O10, O13, O14ab, O18, O19a, O24, O33, O34, O36, O40 and O42; no cross reactions were observed for any probe tested in this study, and the Blank was a negative control; the x-axis represents the PCR products of different serotypes, the y-axis represents the MFI values, and the z-axis represents the specific probes used for detection.</p

The phylogenetic trees for <i>wzx</i> and <i>wzy</i> genes from the 60 <i>Proteus</i> serotypes.

<p>The <i>wzx</i> (A) and <i>wzy</i> (B) trees were constructed using <i>wzx</i> and <i>wzy</i> genes. The sequences were aligned using ClustalW v2.0, and the trees were constructed using the JC69 substitution model and the phyML v3.0.</p

Biosynthesis pathways for the sugars in <i>Proteus</i> O antigens.

<p>GalU, UTP-glucose-1-phosphate uridylyltransferase; GalE, UDP-glucose-4-epimerase; Ugd, UDP-glucose 6-dehydrogenase; Gla, UDP-glucuronate 4-epimerase; GlmS, glutamine:fructose-6-phosphate transaminase; GlmM, phosphoglucosamine mutase; GlmU, UDP-<i>N</i>-acetyl-glucosamine pyrophosphorylase; Gne, UDP-<i>N</i>-acetylglucosamine-4-epimerase; RmlA, glucose-1-phosphate thymidylyltransferase; RmlB, dTDP-D-glucose 4,6-dehydratase; RmlC, dTDP-6-deoxy-α-D-<i>xylo</i>-hexos-4-ulose 3,5-epimerase; RmlD, dTDP-6-deoxy-β-L-<i>lyxo</i>-hexos-4-ulose 4-reductase; FdtA, dTDP-6-deoxy-α-D-<i>xylo</i>-hexos-4-ulose 3,4-isomerase; FdtB, dTDP-6-deoxy-α-D-<i>xylo</i>-hexos-3-ulose aminase; FdtC, dTDP-D-Fuc3N acetylase; QdtA, dTDP-6-deoxy-α-D-<i>xylo</i>-hexos-4-ulose 3,4-isomerase; QdtB, dTDP-6-deoxy-α-D-<i>ribo</i>-hexos-3-ulose aminase; QdtC, dTDP-D-Qui3N acetylase; FnlA, UDP-D-GlcNAc 4,6-dehydratase, 3- and 5-epimerase; FnlB, UDP-2-acetamido-2,6-dideoxy-β-L-<i>lyxo</i>-hexos-4-ulose 4-reductase; FnlC, UDP-2-acetamido-2,6-dideoxy-L-talose 2-epimerase; QnlA, UDP-2-acetamido-2,6-dideoxy-β-L-<i>lyxo</i>-hexos-4-ulose 4-reductase; QnlB, UDP-L-RhaNAc 2-epimerase; * indicates the genes located outside the O antigen gene cluster (all enzymes encoded by these genes can be found in the 68 <i>Proteus</i> genomes; the amino acid sequence identities of GalU to the homolog in <i>E</i>. <i>coli</i> K12 are 75.44–76.43%, the amino acid sequence identities of GalE to the homolog in <i>E</i>. <i>coli</i> K12 are 59.13–65.26%, the amino acid sequence identities of Rib to the homolog in <i>E</i>. <i>coli</i> K12 are 94.29–94.6%, the amino acid sequence identities of GlmS to the homolog in <i>E</i>. <i>coli</i> K12 are 78.89–82.79%, the amino acid sequence identities of GlmM to the homolog in <i>E</i>. <i>coli</i> K12 are 80.97–88.12%, the amino acid sequence identities of GlmU to the homolog in <i>E</i>. <i>coli</i> K12 are 73.94–79.8%, data not shown).</p