Search

BackgroundThe exponential growth of telehealth is revolutionizing health care delivery, but its evaluation has not matched the pace of its uptake. Various forms of assessment, from single-item to more extensive questionnaires, have been used to assess telehealth and digital therapeutics and their usability. The most frequently used questionnaire is the “Telehealth Usability Questionnaire” (TUQ). The use of the TUQ is limited by its restricted availability in languages other than English and its feasibility. ObjectiveThe aims of this study were to create a translated German TUQ version and to derive a short questionnaire for patients—“Telehealth Usability and Perceived Usefulness Short Questionnaire for patients” (TUUSQ). MethodsAs a first step, the original 21-item TUQ was forward and back-translated twice. In the second step, 13 TUQ items were selected for their suitability for the general evaluation of telehealth on the basis of expert opinion. These 13 items were surveyed between July 2022 and September 2023 in 4 studies with patients and family members of palliative care, as well as patients with chronic autoimmune diseases, evaluating 13 health care apps, including digital therapeutics and a telehealth system (n1=128, n2=220, n3=30, and n4=12). Psychometric exploratory factor analysis was conducted. ResultsThe analysis revealed that a parsimonious factor structure with 2 factors (“perceived usefulness in health care” and “usability”) is sufficient to describe the patient’s perception. Consequently, the questionnaire could be shortened to 6 items without compromising its informativeness. ConclusionsWe provide a linguistically precise German version of the TUQ for assessing the usability and perceived usefulness of telehealth. Beyond that, we supply a highly feasible shortened version that is versatile for general use in telehealth, mobile health, and digital therapeutics, which distinguishes between the 2 factors “perceived usefulness in health care” and “usability” in patients. Trial RegistrationGerman Clinical Trials Register DRKS00030546; https://drks.de/search/de/trial/DRKS00030546

This study investigates the supervision of workplace coaches and factors that may influence its use. Drawing on the theory of planned behaviour and focusing on German-speaking countries, we conducted an online survey with open and closed questions to gather the experiences and perspectives of 121 coaching practitioners. Most coaches used supervision, though somewhat irregularly, in different forms and with different focuses, and less than what they thought ideal. A positive attitude impacted positively upon supervision use. Perceived time and cost involved, and prior experiences with supervision also appear to influence supervision use, while coaching association membership had no impact.

The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative power and the DsbC/D system as its complement for isomerization of non-native disulfides. While the standard redox potentials of those systems are known, the in vivo “steady state” redox potential imposed onto protein thiol disulfide pairs in the periplasm remains unknown. Here, we used genetically encoded redox probes (roGFP2 and roGFP-iL), targeted to the periplasm, to directly probe the thiol redox homeostasis in this compartment. These probes contain two cysteine residues that are virtually completely reduced in the cytoplasm, but once exported into the periplasm, can form a disulfide bond, a process that can be monitored by fluorescence spectroscopy. Even in the absence of DsbA, roGFP2, exported to the periplasm, was almost fully oxidized, suggesting the presence of an alternative system for the introduction of disulfide bonds into exported proteins. However, the absence of DsbA shifted the steady state periplasmic thiol-redox potential from −228 mV to a more reducing −243 mV and the capacity to re-oxidize periplasmic roGFP2 after a reductive pulse was significantly decreased. Re-oxidation in a DsbA strain could be fully restored by exogenous oxidized glutathione (GSSG), while reduced GSH accelerated re-oxidation of roGFP2 in the WT. In line, a strain devoid of endogenous glutathione showed a more reducing periplasm, and was significantly worse in oxidatively folding PhoA, a native periplasmic protein and substrate of the oxidative folding machinery. PhoA oxidative folding could be enhanced by the addition of exogenous GSSG in the WT and fully restored in a ΔdsbA mutant. Taken together this suggests the presence of an auxiliary, glutathione-dependent thiol-oxidation system in the bacterial periplasm.

Pediatric palliative home care (PPHC) provides care for children, adolescents, and young adults with life-limiting illnesses in their own homes. Home care often requires long travel times for the PPHC team, which is available to the families 24/7 during crises. The complementary use of telehealth may improve the quality of care. In this pilot study we identify the needs and concerns of patients, teams, and other stakeholders regarding the introduction of telehealth. As a first step, focus groups were conducted in three teams. For the second step, semi-structured interviews were conducted with patients and their families (n = 15). Both steps were accompanied by quantitative surveys (mixed methods approach). The qualitative data were analyzed using content analysis. A total of 11 needs were identified, which were prioritized differently. Highest priority was given to: data transmission, video consultation, access to patient records, symptom questionnaires, and communication support. The concerns identified were related to the assumption of deterioration of the status quo. Potential causes of deterioration were thought to be the negative impact on patient care, inappropriate user behavior, or a high level of technical requirements. As a conclusion, we define six recommendations for telehealth in PPHC.

The crushing of crash boxes is a complex phenomenon characterized by a strong interaction of structural and material properties. Many attempts to improve their energy absorption by adopting one aspect resulted in unacceptable unprogressive bucking. Thus, special considerations are required for crash box optimization including both material and structural effects. In this study, the structural behavior of the crash box is analyzed and a new design approach is introduced to fulfill these requirements. Currently, components, processes, and materials are mainly developed independently. However, to exploit the full potential of modern materials in component design, integrative development work is necessary. Component performance-based requirements and corresponding local material properties must be taken into account concurrently. In this work, a component-driven material design approach is presented, in which local-material-property requirements are derived from component simulations. This new approach is demonstrated by the use case of a quasistatically deformed crash box produced out of steel DP600 for the optimization target “energy absorption”. The finite element simulations were carried out on the crash box, and required material properties for improving the crash box performance were derived based on the simulations. Heat treatment strategies were developed afterwards and experimentally validated to fulfill these requirements. The finite element (FE) simulations based on the experimentally extracted material properties reveal the potential of the component-driven material design approach to improve the crash box performance. The introduced approach enables exploiting the full energy-absorption capacity of the material while ensuring the desired service behavior of the component.

Glutaredoxins play a central role in numerous biological processes including cellular redox homeostasis and Fe-S cluster biogenesis. Here the authors establish the molecular basis for glutaredoxin redox catalysis through comprehensive biochemical and structural analyses.

Glutaredoxins are small proteins of the thioredoxin superfamily that are present throughout life. Most glutaredoxins fall into two major subfamilies. Class I glutaredoxins are glutathione-dependent thiol-disulfide oxidoreductases whilst class II glutaredoxins coordinate Fe–S clusters. Class I glutaredoxins are typically dithiol enzymes with two active-site cysteine residues, however, some enzymatically active monothiol glutaredoxins are also known. Whilst both monothiol and dithiol class I glutaredoxins mediate protein deglutathionylation, it is widely claimed that only dithiol glutaredoxins are competent to reduce protein disulfide bonds. In this study, using a combination of yeast ‘viability rescue’, growth, and redox-sensitive GFP-based assays, we show that two different monothiol class I glutaredoxins can each facilitate the reduction of protein disulfide bonds in ribonucleotide reductase, methionine sulfoxide reductase and roGFP2. Our observations thus challenge the generalization of the dithiol mechanism for glutaredoxin catalysis and raise the question of why most class I glutaredoxins have two active-site cysteine residues.