The e-ROSA project seeks to build a shared vision of a future sustainable e-infrastructure for research and education in agriculture in order to promote Open Science in this field and as such contribute to addressing related societal challenges. In order to achieve this goal, e-ROSA’s first objective is to bring together the relevant scientific communities and stakeholders and engage them in the process of coelaboration of an ambitious, practical roadmap that provides the basis for the design and implementation of such an e-infrastructure in the years to come.
This website highlights the results of a bibliometric analysis conducted at a global scale in order to identify key scientists and associated research performing organisations (e.g. public research institutes, universities, Research & Development departments of private companies) that work in the field of agricultural data sources and services. If you have any comment or feedback on the bibliometric study, please use the online form.
You can access and play with the graphs:
- Evolution of the number of publications between 2005 and 2015
- Map of most publishing countries between 2005 and 2015
- Network of country collaborations
- Network of institutional collaborations (+10 publications)
- Network of keywords relating to data - Link
Tick saliva assists feeding through a complex mixture of compounds that disarm the host homeostasis processes, such as platelet aggregation, vasoconstriction and blood clotting, as well as innate and acquired immune responses. Although the various properties of tick salivary glands have sparked great interest as candidate sources for anti-tick vaccines to prevent tick and tick-borne diseases, antigens that can be useful to induce an immune response against tick bites or the pathogens transmitted by ticks have not yet been developed. Metalloproteases, which have been found in tick saliva, salivary gland, ovary and midgut, play an important role in inflammation, immunomodulation, fibrinolysis, blood protein digestion, nociception, vitellogenesis, remodelling of extracellular matrix and pathogen transmission. A large proportion of tick metalloproteases belong to the metzincin group, whose members characteristically have a highly conserved zinc-binding motif integrated into the central helix at the active site, and a methionine-containing triad called Met-turn followed by a cysteine-rich domain at the C-terminal site. This review discusses specifically the biological aspects of metalloproteases in tick physiology that have been published to date.
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