S
Stuart G. Collins
Researcher at University College Cork
Publications - 40
Citations - 758
Stuart G. Collins is an academic researcher from University College Cork. The author has contributed to research in topics: Diazo & Azide. The author has an hindex of 12, co-authored 38 publications receiving 638 citations.
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Journal ArticleDOI
Bioactivities of glycoalkaloids and their aglycones from Solanum species.
Sinéad E. Milner,Nigel P. Brunton,Peter W. Jones,Nora M. O'Brien,Stuart G. Collins,Anita R. Maguire +5 more
TL;DR: A comprehensive review of the bioactivity of glycoalkaloids and their aglycones of the Solanum species, particularly focused on comparison of their bioactivities including their anticancer, anticholesterol, antimicrobial, anti-inflammatory, antinociceptive, and antipyretic effects, toxicity, and synergism of action is presented.
Journal ArticleDOI
Taming hazardous chemistry in flow: the continuous processing of diazo and diazonium compounds.
TL;DR: The state of the art in the continuous flow processing of reactive diazo and diazonium species is discussed.
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Anti-inflammatory properties of potato glycoalkaloids in stimulated Jurkat and Raw 264.7 mouse macrophages.
Olivia Kenny,Catherine M. McCarthy,Nigel P. Brunton,Mohammad B. Hossain,Dilip K. Rai,Stuart G. Collins,Peter W. Jones,Anita R. Maguire,Nora M. O'Brien +8 more
TL;DR: It is suggested that sub-cytotoxic concentrations of potato glycoalkaloids and potato peel extracts possess anti-inflammatory effects in vitro and with further investigation may be useful in the prevention of anti- inflammatory diseases.
Journal ArticleDOI
Taming tosyl azide: the development of a scalable continuous diazo transfer process.
Benjamin J. Deadman,Rosella M. O'Mahony,Denis Lynch,Daniel C. Crowley,Stuart G. Collins,Anita R. Maguire +5 more
TL;DR: The telescoped diazo transfer process with in-line quenching was used to safely prepare over 21 g of an α-diazocarbonyl in >98% purity without any column chromatography.
Journal ArticleDOI
Phenylalanine dehydrogenase mutants: efficient biocatalysts for synthesis of non-natural phenylalanine derivatives.
TL;DR: Wild-type phenylalanine dehydrogenase from Bacillus sphaericus, and three mutants N145A, N145V and N145L, are used with a coenzyme recycling system to synthesise L-phenylAlanine and three non-natural amino acids on a millimole scale, emphasising the value of protein engineering in creating improved biocatalysts.