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Carole L. Linster
Researcher at University of Luxembourg
Publications - 52
Citations - 3329
Carole L. Linster is an academic researcher from University of Luxembourg. The author has contributed to research in topics: Enzyme & NAD+ kinase. The author has an hindex of 23, co-authored 44 publications receiving 2665 citations. Previous affiliations of Carole L. Linster include Université catholique de Louvain & University of California, Los Angeles.
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Journal ArticleDOI
Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production
Alessandro Michelucci,Thekla Cordes,Jenny Ghelfi,Arnaud Pailot,Norbert Reiling,Oliver Goldmann,Tina M. Binz,Andre Wegner,Aravind Tallam,Antonio Rausell,Manuel Buttini,Carole L. Linster,Eva Medina,Rudi Balling,Karsten Hiller +14 more
TL;DR: It is shown that itaconic acid inhibits the growth of bacteria expressing isocitrate lyase, such as Salmonella enterica and Mycobacterium tuberculosis, and Irg1 gene silencing in macrophages resulted in significantly decreased intracellular itaconi acid levels as well as significantly reduced antimicrobial activity during bacterial infections.
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Vitamin C. Biosynthesis, recycling and degradation in mammals.
TL;DR: The degradation of vitamin’C in mammals is initiated by the hydrolysis of dehydroascorbate to 2,3‐diketo‐l‐gulonate, which is spontaneously degraded to oxalate, CO2 and l‐erythrulose, at variance with bacteria such as Escherichia coli, which have enzymatic degradation pathways for ascorbate and probably also dehydroASCorbate.
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Metabolite damage and its repair or pre-emption
TL;DR: Chemical biology is demonstrating that diverse metabolites are damaged by side reactions of 'promiscuous' enzymes or by spontaneous chemical reactions, that the products are useless or toxic and that the unchecked buildup of these products can be devastating.
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L-Ascorbate biosynthesis in higher plants: the role of VTC2
Carole L. Linster,Steven Clarke +1 more
TL;DR: It is hypothesized that regulation of L-ascorbate biosynthesis might occur at more than one step and warrants further investigation to allow for the manipulation of vitamin C levels in plants.
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Arabidopsis VTC2 Encodes a GDP-l-Galactose Phosphorylase, the Last Unknown Enzyme in the Smirnoff-Wheeler Pathway to Ascorbic Acid in Plants
Carole L. Linster,Tara A. Gomez,Kathryn C. Christensen,Lital N. Adler,Brian D. Young,Charles Brenner,Steven Clarke +6 more
TL;DR: In characterizing recombinant VTC2 from A. thaliana as a specific GDP-l-galactose/GDP-d-glucose phosphorylase, it is concluded that enzymes catalyzing each of the ten steps of the Smirnoff-Wheeler pathway from glucose to ascorbate have been identified.