Value stability and change during self-chosen life transitions: Self-selection versus socialization effects

Copyright @ 2013 APA. This article may not exactly replicate the final version published in the APA journal. It is not the copy of record.Three longitudinal studies examine a fundamental question regarding adjustment of personal values to self-chosen life transitions: Do values fit the new life setting already at its onset, implying value-based self-selection? Or do values change to better fit the appropriate and desirable values in the setting, implying value socialization? As people are likely to choose a life transition partly based on their values, their values may fit the new life situation already at its onset, leaving little need for value socialization. However, we propose that this may vary as a function of the extent of change the life transition entails, with greater change requiring more value socialization. To enable generalization, we used 3 longitudinal studies spanning 3 different life transitions and different extents of life changes: vocational training (of new police recruits), education (psychology vs. business students), and migration (from Poland to Britain). Although each life transition involved different key values and different populations, across all 3 studies we found value fit to the life situation already early in the transition. Value socialization became more evident the more aspects of life changed as part of the transition, that is, in the migration transition. The discussion focuses on the implications of these findings for research on values and personality change, as well as limitations and future directions for research

The Molecular Basis for Different Recognition of Substrates by Phosphodiesterase Families 4 and 10

Phosphodiesterases (PDEs) are key enzymes that control the cellular concentrations of the second messengers cAMP and cGMP. The mechanism for selective recognition of substrates cAMP and cGMP by individual PDE families remains a puzzle. To understand the mechanism for substrate recognition by PDE enzymes, the crystal structure of the catalytic domain of an inactive D201N mutant of PDE4D2 in complex with substrate cAMP has been determined at 1.56 Å resolution. The structure shows that Gln369 forms only one hydrogen bond with the adenine of cAMP. This finding provides experimental evidence against the hypothesis of two hydrogen bonds between the invariant glutamine and the substrate cAMP in PDE4, and thus suggests that the widely circulated “glutamine switch” model is unlikely the mechanism for substrate recognition by PDEs. A structure comparison between PDE4D2-cAMP and PDE10A2-cAMP reveals an anti configuration of cAMP in PDE4D2 but syn in PDE10A2, in addition to different contact patterns of cAMP in these two structures. These observations imply that individual PDE families have their characteristic mechanisms for substrate recognition

Advantages and disadvantages of encouraging consumerist notions of healthcare at two minor injury units: results of a multiple embedded case study.

Over the past four decades, UK Governments have moved towards an increasingly pro-market model of health-care provision. Under this system patients are not only encouraged, but expected, to take increasing responsibility for health-care decision-making and the risks that it might entail. This article investigate how and why patients make choices about their health-care and how service providers help facilitate this. Between October 2014 and May 2015, the researcher was embedded as an emergency nurse practitioner at two minor injury units in order to undertake direct and participant observation. During this time, 40 patients, 17 service providers and 1 senior manager also consented to semi-structured interview. The findings suggest that patients should continue to be encouraged to make decisions about their health-care, but only if they feel confident to do so. The challenge for service providers is to recognise when this is/not appropriate and tailor interaction accordingly

Conformation Changes, N-terminal Involvement, and cGMP Signal Relay in the Phosphodiesterase-5 GAF Domain

The activity of phosphodiesterase-5 (PDE5) is specific for cGMP and is regulated by cGMP binding to GAF-A in its regulatory domain. To better understand the regulatory mechanism, x-ray crystallographic and biochemical studies were performed on constructs of human PDE5A1 containing the N-terminal phosphorylation segment, GAF-A, and GAF-B. Superposition of this unliganded GAF-A with the previously reported NMR structure of cGMP-bound PDE5 revealed dramatic conformational differences and suggested that helix H4 and strand B3 probably serve as two lids to gate the cGMP-binding pocket in GAF-A. The structure also identified an interfacial region among GAF-A, GAF-B, and the N-terminal loop, which may serve as a relay of the cGMP signal from GAF-A to GAF-B. N-terminal loop 98–147 was physically associated with GAF-B domains of the dimer. Biochemical analyses showed an inhibitory effect of this loop on cGMP binding and its involvement in the cGMP-induced conformation changes