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1.
Article in English | MEDLINE | ID: mdl-36901253

ABSTRACT

The World Health Organization (WHO) maintains a list of medicines and medical devices, essential medicines, that should be available to everyone, to form a functioning healthcare system. Yet, many of these medicines remain out of reach for people around the world. One significant barrier to improving the accessibility of essential medicines is a paucity of information about both the extent and causes of this problem. E$$ENTIAL MEDICINE$ (E$$) is a citizen science project designed to investigate this deficit of information by recruiting members of the public to find, validate, compile and share information on essential medicines through an open, online database. Herein, we report an approach to crowdsourcing both the collection of information on the accessibility of essential medicines and the subsequent communication of these findings to diverse audiences. The Meet the Medicines initiative encourages members of the public to share information from the E$$ database, in a short video format appropriate for social media. This communication details the design and implementation of our crowdsourced approach and strategies for recruiting and supporting participants. We discuss data on participant engagement, consider the benefits and challenges of this approach and suggest ways to promote crowdsourcing practices for social and scientific good.


Subject(s)
Crowdsourcing , Humans , Communication , World Health Organization
2.
Front Chem ; 9: 687678, 2021.
Article in English | MEDLINE | ID: mdl-34249861

ABSTRACT

The ability to radiolabel proteins with [18F]fluoride enables the use of positron emission tomography (PET) for the early detection, staging and diagnosis of disease. The direct fluorination of native proteins through C-F bond formation is, however, a difficult task. The aqueous environments required by proteins severely hampers fluorination yields while the dry, organic solvents that promote nucleophilic fluorination can denature proteins. To circumvent these issues, indirect fluorination methods making use of prosthetic groups that are first fluorinated and then conjugated to a protein have become commonplace. But, when it comes to the radiofluorination of proteins, these indirect methods are not always suited to the short half-life of the fluorine-18 radionuclide (110 min). This review explores radiofluorination through bond formation with fluoride at boron, metal complexes, silicon, phosphorus and sulfur. The potential for these techniques to be used for the direct, aqueous radiolabeling of proteins with [18F]fluoride is discussed.

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