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In this article, we present a generic model for social and cognitive skills that can be used in work and (simulation-based) education in healthcare. We combined existing non-technical skills tools into a tool that we call SCOPE. SCOPE is a model that comprises the three social categories of "teamwork", "leading", and "task management" as well as the two cognitive categories of "situation awareness" and "decision making". Each category comprises between three and six elements. We formulated guiding questions for each category in an attempt to emphasize its core meaning. We developed a dynamic graphical representation of the categories that emphasize the constant changes in the relative importance of the categories over the course of a clinical or educational situation. Anecdotal evidence supports the value of the model for aligning language around social and cognitive skills across specialties and professions.

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BACKGROUND: How healthcare professionals understand and use concepts of social and cognitive capabilities will influence their behaviour and their understanding of others' behaviour. Differing understandings of concepts might lead to healthcare professionals not acting in accordance with other healthcare professionals' expectations. Therefore, part of the problem concerning errors and adverse incidents concerning social and cognitive capabilities might be due to varying understandings of concepts among different healthcare professionals. This study aimed to examine the variations in how educators at the Copenhagen Academy for Medical Education and Simulation talk about social and cognitive capabilities. METHODS: The study was conducted using semi-structured interviews and directed content analysis. The codes for the analysis process were derived from existing non-technical skills models and used to show variations in how the participants talk about the same concepts. RESULTS: Educators with a background as nurses and physicians, talked differently about leadership and decision-making, with the nurses paying greater attention to group dynamics and external factors when describing both leadership and decision-making, whereas physicians focus on their individual efforts. CONCLUSION: We found patterned differences in how the participants described leadership and decision-making that may be related to participants' professional training/background. As it can create misunderstandings and unsafe situations if nurses and physicians disagree on the meaning of leadership and decision-making (without necessarily recognising this difference), it could be beneficial to educate healthcare professionals to be aware of the specificity of their own concepts, and to communicate what exactly they mean by using a particular concept, e.g. "I want you to coordinate tasks" instead of "I want better leadership".

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INTRODUCTION: In Denmark, responsibility for continuing professional development (CPD) of consultants is shared between employers, often represented by heads of department, and the consultants themselves. This interview study explored patterns in the ways that shared responsibility is practiced in the context of financial, organisational and normative structures. METHODS: Semi-structured interviews were held with 26 consultants holding different levels of experience, including nine heads of department, across four specialties in five hospitals in the Capital Region of Denmark in 2019. Recurring themes in the interview data were analysed in the light of critical theory to highlight connections and trade-offs between individuals' choices and structural conditions. RESULTS: CPD is often a matter of short-term trade-offs for consultants and heads of department. Recurring elements in the trade-offs between what consultants wish to do and what is possible include topics of CPD, funding sources, time and expected learning gains. Governance of CPD varies from pure administration of limited funds to attempts to aligning individual with department priorities. CONCLUSIONS: Shared responsibility for CPD activities is managed in very diverse ways across departments. The individual flexibility afforded by shared responsibility may be an advantage, but a risk exists that structural conditions for CPD, such as short-term budgets and very different management practices, leave CPD activities to be guided more by coincidence than plan. FUNDING: none TRIAL REGISTRATION. not relevant.

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BACKGROUND: Robot-assisted surgery is expanding worldwide. Most research in this field concentrates on surgeons' technical skills and patient outcome, but research from open and laparoscopic surgery shows that teamwork is crucial for patient safety. Team composition is changed in robot-assisted surgery with the surgeon placed away from the bedside, potentially altering teamwork and workflow in the operating theatre. This scoping review aimed to explore how factors affecting workflow as well as team members' social and cognitive skills during robot-assisted surgery are reported in the literature. METHODS: A systematic search was performed in the databases Medline, EMBASE, PsycINFO, and Web of Science. Reports were screened according to the Preferred Reporting Item for Systematic reviews and Meta-Analysis for Scoping Review guidelines. Inclusion criteria were robot-assisted surgery, multi-professional teams, and workflow, flow disruptions, or non-technical skills. RESULTS: A total of 12,527 references were screened, and 24 articles were included in the review. Articles were heterogeneous in terms of aim, methods and focus. The studies concentrated on two main fields: flow disruptions and the categorization of their causes and incidences; and non-technical skills describing the challenges of communication and effects on situation awareness. CONCLUSION: Many studies focused on flow disruptions and found that communication, coordination, training, and equipment/technology were the most frequent causes. Another focus of studies was non-technical skills-primarily communication and situation awareness. Future studies could focus on how to prevent the most harmful flow disruptions and develop interventions for improving workflow.

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A cascade of protein-protein interactions between four herpes simplex virus (HSV) glycoproteins (gD, gH/gL, and gB) drive fusion between the HSV envelope and host membrane, thereby allowing for virus entry and infection. Specifically, binding of gD to one of its receptors induces a conformational change that allows gD to bind to the regulatory complex gH/gL, which then activates the fusogen gB, resulting in membrane fusion. Using surface plasmon resonance and a panel of anti-gD monoclonal antibodies (MAbs) that sterically blocked the interaction, we previously showed that gH/gL binds directly to gD at sites distinct from the gD receptor binding site. Here, using an analogous strategy, we first evaluated the ability of a panel of uncharacterized anti-gH/gL MAbs to block binding to gD and/or inhibit fusion. We found that the epitopes of four gD-gH/gL-blocking MAbs were located within flexible regions of the gH N terminus and the gL C terminus, while the fifth was placed around gL residue 77. Taken together, our data localized the gD binding region on gH/gL to a group of gH and gL residues at the membrane distal region of the heterodimer. Surprisingly, a second set of MAbs did not block gD-gH/gL binding but instead stabilized the complex by altering the kinetic binding. However, despite this prolonged gD-gH/gL interaction, "stabilizing" MAbs also inhibited cell-cell fusion, suggesting a unique mechanism by which the fusion process is halted. Our findings support targeting the gD-gH/gL interaction to prevent fusion in both therapeutic and vaccine strategies against HSV.IMPORTANCE Key to developing a human HSV vaccine is an understanding of the virion glycoproteins involved in entry. HSV employs multiple glycoproteins for attachment, receptor interaction, and membrane fusion. Determining how these proteins function was resolved, in part, by structural biology coupled with immunological and biologic evidence. After binding, virion gD interacts with a receptor to activate the regulator gH/gL complex, triggering gB to drive fusion. Multiple questions remain, one being the physical location of each glycoprotein interaction site. Using protective antibodies with known epitopes, we documented the long-sought interaction between gD and gH/gL, detailing the region on gD important to create the gD-gH/gL triplex. Now, we have identified the corresponding gD contact sites on gH/gL. Concurrently we discovered a novel mechanism whereby gH/gL antibodies stabilize the complex and inhibit fusion progression. Our model for the gD-gH/gL triplex provides a new framework for studying fusion, which identifies targets for vaccine development.

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AIM: LIFESTAT is an interdisciplinary project that leverages approaches and knowledge from medicine, the humanities and the social sciences to analyze the impact of statin use on health, lifestyle and well-being in cohorts of Danish citizens. The impetus for the study is the fact that 10% of the population in the Scandinavian countries are treated with statins in order to maintain good health and to avoid cardiovascular disease by counteracting high blood levels of cholesterol. The potential benefit of treatment with statins should be considered in light of evidence that statin use has prevalent and unintended side effects (e.g. myalgia, and glucose and exercise intolerance). METHODS: The LIFESTAT project combines invasive human experiments, biomedical analyses, nationwide surveys, epidemiological studies, qualitative interviews, media content analyses, and ethnographic participant observations. The study investigates the biological consequences of statin treatment; determines the mechanism(s) by which statin use causes muscle and mitochondrial dysfunction; and analyzes achievement of treatment goals, people's perception of disease risk, media influence on people's risk and health perception, and the way people manage to live with the risk (personally, socially and technologically). CONCLUSIONS THE ORIGINALITY AND SUCCESS OF LIFESTAT DEPEND ON AND DERIVE FROM ITS INTERDISCIPLINARY APPROACH, IN WHICH THE DISCIPLINES CONVERGE INTO THOROUGH AND HOLISTIC STUDY AND DESCRIBE THE IMPACT OF STATIN USE ON THE EVERYDAY LIFE OF STATIN USERS THIS HAS THE POTENTIAL FOR MUCH GREATER BENEFIT THAN ANY ONE OF THE DISCIPLINES ALONE INTEGRATING TRADITIONAL DISCIPLINES PROVIDES NOVEL PERSPECTIVES ON POTENTIAL CURRENT AND FUTURE SOCIAL, MEDICAL AND PERSONAL BENEFITS OF STATIN USE.

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Two models describing how alphaherpesviruses exit neurons differ with respect to whether nucleocapsids and envelope glycoproteins travel toward axon termini separately or as assembled enveloped virions. Recently, a pseudorabies virus glycoprotein D (gD)-green fluorescent protein fusion was found to colocalize with viral capsids, supporting anterograde transport of enveloped virions. Previous antibody staining experiments demonstrated that herpes simplex virus (HSV) glycoproteins and capsids are separately transported in axons. Here, we generated an HSV expressing a gD-yellow fluorescent protein (YFP) fusion and found that gD-YFP and capsids were transported separately in neuronal axons. Anti-gD antibodies colocalized with gD-YFP, indicating that gD-YFP behaves like wild-type HSV gD.

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Herpesvirus glycoprotein M (gM) is a multiple-spanning integral membrane protein found within the envelope of mature herpesviruses and is conserved throughout the Herpesviridae. gM is defined as a non-essential glycoprotein in alphaherpesviruses and has been proposed as playing a role in controlling final envelopment in a late secretory-pathway compartment such as the trans-Golgi network (TGN). Additionally, gM proteins have been shown to inhibit cell-cell fusion in transfection-based assays by an as yet unclear mechanism. Here, the effect of pseudorabies virus (PRV) gM and the herpes simplex virus type 1 (HSV-1) gM/UL49A complex on the fusion events caused by the HSV-1 glycoproteins gB, gD, gH and gL was investigated. Fusion of cells expressing HSV-1 gB, gD, gH and gL was efficiently inhibited by both PRV gM and HSV-1 gM/UL49A. Furthermore, expression of PRV gM or HSV-1 gM/UL49A, which are themselves localized to the TGN, caused both gD and gH/L to be relocalized from the plasma membrane to a juxtanuclear compartment, suggesting that fusion inhibition is caused by the removal of 'fusion' proteins from the cell surface. The ability of gM to cause the relocalization of plasma membrane proteins was not restricted to HSV-1 glycoproteins, as other viral and non-viral proteins were also affected. These data suggest that herpesvirus gM (gM/N) can alter the membrane trafficking itineraries of a broad range of proteins and this may have multiple functions.

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Glycoprotein D (gD) of herpes simplex virus type 1 is a type 1 membrane protein in the virus envelope that binds to receptor molecules on the cell surface and which induces cell-cell fusion when co-expressed with gB, gH and gL. A chimeric gD molecule in which the membrane anchor and cytoplasmic tail domains were replaced with analogous regions from the human CD8 molecule was as competent as wild-type gD at mediating membrane fusion and virus entry. However, when gD was tethered to the membrane by means of a glycosylphosphatidylinositol (gpi)-anchor sequence, which binds only to the outer leaflet of the lipid bilayer, it was unable to function in cell-cell fusion assays. This chimera was incorporated into virions as efficiently as wild-type gD and yet virus particles containing gpi-linked gD entered cells more slowly than virions containing wild-type gD in their envelopes, suggesting that gD must be anchored in both leaflets of a lipid bilayer for it to function in both cell fusion and virus entry.

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Herpes simplex virus type 1 (HSV-1) glycoproteins gB, gD and gHL are capable of inducing cell fusion when expressed from plasmid vectors in the absence of any other virus components. Fusion requires the expression of all four glycoproteins on the same membrane, since they are unable to cooperate in trans to induce syncytium formation. In addition, the fusion event is dependent on the expression of a gD receptor on target cell membranes and does not require the presence of cell-surface glycosaminoglycans.

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