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- Moharra, Montse, et al.
(författare)
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Implementation of a cross-border health service : physician and pharmacists' opinions from the epSOS project
- 2015
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Ingår i: Family Practice. - : Oxford University Press (OUP). - 0263-2136 .- 1460-2229. ; 32:5, s. 564-567
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Tidskriftsartikel (refereegranskat)abstract
- Objective(s). To explore the opinions of health professionals with experience of the European Patient Smart Open Services (epSOS) system regarding the epSOS services perceived utility, potential impact and main barriers and facilitators to its use. Methods. Qualitative study design involving focus groups with health care professionals with experience of epSOS system. A semi-structured topic guide was developed to guide the discussion. Results. epSOS services were seen as interesting intuitive services and easy to operate. The greatest impact was in terms of positive impact on communication, clinical safety and patient management. Data reliability, difficulties in accessing the service and aspects related to information technology architecture were considered the most relevant barriers. Conclusion. This study has provided insights into the strengths and limitations of two new eHealth services for use across countries within the European Union, and has provided indications of how those services could be improved.
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| 2. |
- Whitehead, Jack D., et al.
(författare)
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Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus
- 2023
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Ingår i: Nature Communications. - : Springer Nature. - 2041-1723. ; 14:1
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Tidskriftsartikel (refereegranskat)abstract
- Human metapneumovirus (HMPV) is a major cause of respiratory illness in young children. The HMPV polymerase (L) binds an obligate cofactor, the phosphoprotein (P). During replication and transcription, the L/P complex traverses the viral RNA genome, which is encapsidated within nucleoproteins (N). An essential interaction between N and a C-terminal region of P tethers the L/P polymerase to the template. This N-P interaction is also involved in the formation of cytoplasmic viral factories in infected cells, called inclusion bodies. To define how the polymerase component P recognizes N-encapsidated RNA (N-RNA) we employed cryogenic electron microscopy (cryo-EM) and molecular dynamics simulations, coupled to activity assays and imaging of inclusion bodies in cells. We report a 2.9 Å resolution structure of a triple-complex between multimeric N, bound to both RNA and the C-terminal region of P. Furthermore, we also present cryo-EM structures of assembled N in different oligomeric states, highlighting the plasticity of N. Combined with our functional assays, these structural data delineate in molecular detail how P attaches to N-RNA whilst retaining substantial conformational dynamics. Moreover, the N-RNA-P triple complex structure provides a molecular blueprint for the design of therapeutics to potentially disrupt the attachment of L/P to its template.
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