Communicating Maritime Spatial Planning: The MSP Challenge approach

The MSP Challenge uses game technology and role-play to support communication and learning for Marine/Maritime Spatial Planning. Since 2011, a role-playing game, a board game and a digital interactive simulation platform have been developed. The MSP Challenge editions have been used in workshops, conferences, education, as well as for real life stakeholder engagement. The authors give an overview of the development of the MSP Challenge and reflect on the value of the approach as an engaging and ‘fun’ tool for building mutual understanding and communicating MSP

Implementation of the Marine Strategy Framework Directive in Macaronesia and synergies with the Maritime Spatial Planning process

The relationship between the Marine Strategy Framework Directive 2008/56/EC (MSFD) and the Maritime Spatial Planning (MSP) process has been analyzed to understand which is the dominant process or where there is an overlap. In this contribution, we used the case study of the three archipelagos: Azores, Madeira and the Canary Islands, included in the European Macaronesian Sea, in order (a) to recognize/identify common principles at policy level; (b) to evaluate the first implementation cycle of MSFD (2012–2018) and its potential contribution to the MSP process in this region. An empirical in-depth assessment was applied to analyze the degree of MSFD implementation by both States (Portugal and Spain) in those regional waters and identifying what is relevant for the concomitant MSP process. The results of this study show that MSFD is particularly challenging in these archipelagos with extensive EEZs. Still, MSFD implementation reports identify relevant actions and related data that can provide the groundwork to ensure robust consideration of the marine environment in the planning process. We recommend these findings to integrate the ongoing Macaronesian MSP

Communicating maritime spatial planning: The MSP challenge approach

The MSP Challenge uses game technology and role-play to support communication and learning for Marine/Maritime Spatial Planning. Since 2011, a role-playing game, a board game and a digital interactive simulation platform have been developed. The MSP Challenge editions have been used in workshops, conferences, education, as well as for real life stakeholder engagement. The authors give an overview of the development of the MSP Challenge and reflect on the value of the approach as an engaging and ‘fun’ tool for building mutual understanding and communicating MSP

A 127 kDa component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein.

A cDNA which encodes a approximately 127 kDa UV-damaged DNA-binding (UV-DDB) protein with high affinity for (6-4)pyrimidine dimers [Abramic', M., Levine, A.S. & Protic', M., J. Biol. Chem. 266: 22493-22500, 1991] has been isolated from a monkey cell cDNA library. The presence of this protein in complexes bound to UV-damaged DNA was confirmed by immunoblotting. The human cognate of the UV-DDB gene was localized to chromosome 11. UV-DDB mRNA was expressed in all human tissues examined, including cells from two patients with xeroderma pigmentosum (group E) that are deficient in UV-DDB activity, which suggests that the binding defect in these cells may reside in a dysfunctional UV-DDB protein. Database searches have revealed significant homology of the UV-DDB protein sequence with partial sequences of yet uncharacterized proteins from Dictyostelium discoideum (44% identity over 529 amino acids) and Oryza sativa (54% identity over 74 residues). According to our results, the UV-DDB polypeptide belongs to a highly conserved, structurally novel family of proteins that may be involved in the early steps of the UV response, e.g., DNA damage recognition

Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III

Opioid peptides are involved in various essential physiological processes, most notably nociception. Dipeptidyl peptidase III (DPP III) is one of the most important enkephalin-degrading enzymes associated with the mammalian pain modulatory system. Here we describe the X-ray structures of human DPP III and its complex with the opioid peptide tynorphin, which rationalize the enzyme's substrate specificity and reveal an exceptionally large domain motion upon ligand binding. Microcalorimetric analyses point at an entropy-dominated process, with the release of water molecules from the binding cleft (“entropy reservoir”) as the major thermodynamic driving force. Our results provide the basis for the design of specific inhibitors that enable the elucidation of the exact role of DPP III and the exploration of its potential as a target of pain intervention strategies