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- Hylland, O. M., et al.
(författare)
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Pandemic cultural policy. A comparative perspective on Covid-19 measures and their effect on cultural policies in Europe
- 2024
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Ingår i: The International Journal of Cultural Policy. - : Informa UK Limited. - 1028-6632 .- 1477-2833. ; 30:1, s. 81-100
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Tidskriftsartikel (refereegranskat)abstract
- To what extent did the Covid-19 pandemic affect the tools, priorities and organisation of cultural policies? And did the pandemic enhance the digital aspect of these policies? This paper compares pandemic cultural policy measures in seven European countries to answer these questions. The countries all installed a plurality of mitigating measures, combining grants and subsidies, compensation of lost income, income support and financial flexibility, creating a tendency towards cultural policy turning into economic policy, fiscal policy, and labour market policy. Cultural policies have not been fundamentally challenged by the pandemic, in the sense that it has affected the essential political tools, divisions of labour, or core goals. The responses have confirmed an existing policy structure or enhanced existing developments. The importance of a state-centred or a federalist cultural policy system has not been challenged in a substantial way. Secondly there is little evidence to show a general acceleration of national digital cultural policies.
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| 2. |
- Gao, C. X., et al.
(författare)
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Exploration of multiple Sortase A protein conformations in virtual screening
- 2016
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Ingår i: Scientific Reports. - : Springer Science and Business Media LLC. - 2045-2322. ; 6:20413
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Tidskriftsartikel (refereegranskat)abstract
- Methicillin resistant Staphylococcus aureus (MRSA) has become a major health concern which has brought about an urgent need for new therapeutic agents. As the S. aureus Sortase A (SrtA) enzyme contributes to the adherence of the bacteria to the host cells, inhibition thereof by small molecules could be employed as potential antivirulence agents, also towards resistant strains. Albeit several virtual docking SrtA campaigns have been reported, no strongly inhibitatory non-covalent binders have as yet emerged therefrom. In order to better understand the binding modes of small molecules, and the effect of different receptor structures employed in the screening, we herein report on an exploratory study employing 10 known binders and 500 decoys on 100 SrtA structures generated from regular or steered molecular dynamics simulations on four different SrtA crystal/NMR structures. The results suggest a correlation between the protein structural flexibility and the virtual screening performance, and confirm the noted immobilization of the beta 6/beta 7 loop upon substrate binding. The NMR structures reported appear to perform slightly better than the Xray-crystal structures, but the binding modes fluctuate tremendously, and it might be suspected that the catalytic site is not necessarily the preferred site of binding for some of the reported active compounds.
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| 3. |
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| 4. |
- Uzelac, Ivana, et al.
(författare)
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A Structural Comparison Approach for Identifying Small Variations in Binding Sites of Homologous Proteins
- 2015
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Ingår i: Computational Molecular Bioscience. - : Scientific Research Publishing, Inc.. - 2165-3453 .- 2165-3445. ; 5:3, s. 45-55
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Tidskriftsartikel (refereegranskat)abstract
- A method for analyzing the protein site similarity was devised aiming at understanding selectivity of homologous proteins and guiding the design of new drugs. The method is based on calculating Cα distances between selected pocket residues and subsequent analysis by multivariate methods. Five closely related serine proteases, the coagulation factors II, VII, IX, X, and XI, were studied and their pocket similarity was illustrated by PCA clustering. OPLS-DA was then applied to identify the residues responsible for the variation. By combining these two multivariate methods, we could successfully cluster the different proteases according to class and identify the important residues responsible for the observed variation.
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