ArticleOrganic & biomolecular chemistry2020
Nicotinamide riboside-amino acid conjugates that are stable to purine nucleoside phosphorylase.
Article in Organic & biomolecular chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- NADInternational journal of molecular sciences · 2026Article
- Nicotinamide riboside Induced Energy Stress and Metabolic Reprogramming in BEAS-2B Cells.Chemical research in toxicology · 2024Article
- Nicotinamide Riboside: What It Takes to Incorporate It into RNA.Molecules (Basel, Switzerland) · 2024Review
- Synthesis, Detection, and Metabolism of Pyridone Ribosides, Products of NAD Overoxidation.Chemical research in toxicology · 2024Article
- NADMetabolites · 2022Review
- Nicotinamide Riboside Improves Ataxia Scores and Immunoglobulin Levels in Ataxia Telangiectasia.Movement disorders : official journal of the Movement Disorder Society · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The nutraceutical Nicotinamide Riboside (NR), an efficacious biosynthetic precursor to NAD, is readily metabolized by the purine nucleoside phosphorylase (PNP). Access to the PNP-stable versions of NR is difficult because the glycosidic bond of NR is easily cleaved. Unlike NR, NRH, the reduced form of NR, offers sufficient chemical stability to allow the successful functionalisation of the ribosyl-moiety. Here, we report on a series of NRH and NR derived amino acid conjugates, generated in good to excellent yields and show that O5'-esterification prevents the PNP-catalyzed phosphorolysis of these NR prodrugs.
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Registered trials
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