RESUMEN
Impact-driven research is a EU priority and, increasingly, for universities around Europe. Still, there is need for specific strategies to improve the societal impact of scientific knowledge and therewith improve the uptake of scientific results. Co-creation deeply evolves the role of scientific knowledge and increases its impact. Albeit there is much research on the conceptualization and contextualization of co-creation, research on the microlevel dynamics of co-creation is less common. This article aims to understand the dynamics of and clarify the role of co-creation within and between quadruple helix actors (academia, government, industry and societal partners). Here, co-creation refers to the collaboration, where such actors actively join forces to address challenges. This paper revolves around insights from the European Commission Horizon 2020-project-Accomplissh (www.accomplissh.eu) which stands for "Accelerate co-creation by setting up a multi-actor platform for impact from Social Sciences and Humanities". The results lay bare a set of obstacles, areas of consideration and enablers in co-creation. This said, it is argued that scientific knowledge is optimally utilized when a set of guidelines or recommendations are followed and carried out by all involved actors.
RESUMEN
Reversible oxidation sensitivity of N-Oct-3 DNA binding activity was seen when melanoma extracts and recombinant Brn-2 protein were treated with a variety of metals, hydrogen peroxide and the cysteine disulphide bond forming agent diamide. Western blot analysis of diamide-oxidized N-Oct-3 protein indicated that this was likely to be due to intramolecular disulphide bonding. The potential role of oxidative loss of N-Oct-3 DNA binding activity is discussed in relation to redox changes that may occur during the early phase of apoptosis in neuronal cell lines and tissues. Brn-2 C-terminal antibody Western blot analysis of melanoma cell line nuclear extracts prepared using a combination of sodium dodecyl sulphate and NP-40 detergent cell lysis procedures demonstrated the formation of N-Oct-5 DNA binding activity via N-terminal proteolytic clipping of Brn-2/N-Oct-3.
Asunto(s)
ADN de Neoplasias/metabolismo , Proteínas de Unión al ADN/metabolismo , Regulación Neoplásica de la Expresión Génica , Melanoma Experimental/genética , Melanoma/genética , Factores de Transcripción/metabolismo , Animales , Western Blotting , Células COS , Núcleo Celular/química , Núcleo Celular/genética , ADN de Neoplasias/aislamiento & purificación , Diamida/farmacología , Regulación Neoplásica de la Expresión Génica/efectos de los fármacos , Células HeLa , Proteínas de Homeodominio , Humanos , Peróxido de Hidrógeno/farmacología , Metales , Ratones , Oxidación-Reducción , Factores del Dominio POU , Conejos , Células Tumorales CultivadasRESUMEN
The structures of the human tyrosinase-related protein genes TYRP1 and TYRP2 have been determined and compared with that of the tyrosinase gene (TYR). The TYRP1 protein is encoded in 7 exons spread over 24 kb of genomic DNA. Characterization of a 55-kb contig encompassing the human TYRP2 locus reveals that the protein coding region is divided into 8 exons. All three members of the TYRP gene family share a common C-terminal membrane spanning exon. Examination of the position of other intron junctions suggests that TYRP1 was derived from a TYR duplication and then was itself duplicated to give rise to the TYRP2 gene. The evidence also suggests that at least some of the introns within the TYR, TYRP1, and TYRP2 coding regions were gained after duplication and that intron slippage is unlikely to have occurred.