ArticleThe Journal of biological chemistry2009
Nicotinamide riboside and nicotinic acid riboside salvage in fungi and mammals. Quantitative basis for Urh1 and purine nucleoside phosphorylase function in NAD+ metabolism.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 61 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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Who cites it
61 citing papers in PubMed, 99 citations in OpenAlex.
- Discovery of functional compounds from dimorphic edibleSynthetic and systems biotechnology · 2026Article
- NADNature metabolism · 2025Review
- Emerging strategies, applications and challenges of targeting NADNature aging · 2025Review
- Nicotinic acid riboside maintains NADCell metabolism · 2025Article
- The role of NADnpj metabolic health and disease · 2025Review
- Nicotinamide riboside and nicotinamide mononucleotide facilitate NADScience advances · 2025Article
- Nicotinamide: A Multifaceted Molecule in Skin Health and Beyond.Medicina (Kaunas, Lithuania) · 2025Review
- Mitochondria as Nutritional Targets to Maintain Muscle Health and Physical Function During Ageing.Sports medicine (Auckland, N.Z.) · 2024Review
- Structure-Function Insights into the Dual Role in Nucleobase and Nicotinamide Metabolism and a Possible Use in Cancer Gene Therapy of the URH1p Riboside Hydrolase.International journal of molecular sciences · 2024Article
- Back to the Future of Metabolism-Advances in the Discovery and Characterization of Unknown Biocatalytic Functions and Pathways.Life (Basel, Switzerland) · 2024Review
- Inhibitors of NADInternational journal of molecular sciences · 2024Review
- Nicotinamide Riboside, a Promising Vitamin BMolecules (Basel, Switzerland) · 2023Review
- What is really known about the effects of nicotinamide riboside supplementation in humans.Science advances · 2023Review
- NADCells · 2022Review
- NADMetabolites · 2022Review
- Fueling genome maintenance: On the versatile roles of NADThe Journal of biological chemistry · 2022Review
- Structure, Oligomerization and Activity Modulation in N-Ribohydrolases.International journal of molecular sciences · 2022Review
- Article
- Nicotinic acid mononucleotide is an allosteric SARM1 inhibitor promoting axonal protection.Experimental neurology · 2021Article
- Tryptophan Derivatives byInternational journal of molecular sciences · 2021Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
NAD+ is a co-enzyme for hydride transfer enzymes and an essential substrate of ADP-ribose transfer enzymes and sirtuins, the type III protein lysine deacetylases related to yeast Sir2. Supplementation of yeast cells with nicotinamide riboside extends replicative lifespan and increases Sir2-dependent gene silencing by virtue of increasing net NAD+ synthesis. Nicotinamide riboside elevates NAD+ levels via the nicotinamide riboside kinase pathway and by a pathway initiated by splitting the nucleoside into a nicotinamide base followed by nicotinamide salvage. Genetic evidence has established that uridine hydrolase, purine nucleoside phosphorylase, and methylthioadenosine phosphorylase are required for Nrk-independent utilization of nicotinamide riboside in yeast. Here we show that mammalian purine nucleoside phosphorylase but not methylthioadenosine phosphorylase is responsible for mammalian nicotinamide riboside kinase-independent nicotinamide riboside utilization. We demonstrate that so-called uridine hydrolase is 100-fold more active as a nicotinamide riboside hydrolase than as a uridine hydrolase and that uridine hydrolase and mammalian purine nucleoside phosphorylase cleave nicotinic acid riboside, whereas the yeast phosphorylase has little activity on nicotinic acid riboside. Finally, we show that yeast nicotinic acid riboside utilization largely depends on uridine hydrolase and nicotinamide riboside kinase and that nicotinic acid riboside bioavailability is increased by ester modification.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.