ArticleThe Biochemical journal2002
A novel cycling assay for cellular cADP-ribose with nanomolar sensitivity.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
What it found
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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
81 citing papers in PubMed, 188 citations in OpenAlex.
- TheVirulence · 2026Article
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- NADBiochemistry and biophysics reports · 2026Article
- Raw defines a TIR-fold cADPR hydrolase cooperating with dSarm in development and axon degeneration.Cell communication and signaling : CCS · 2026Article
- Hepatocyte mitochondrial NADNature metabolism · 2025Article
- CD38/cADPR-mediated calcium signaling in a human myometrial smooth muscle cell line, PHM1.IUBMB life · 2024Article
- The Fluorinated NAD Precursors Enhance FK866 Cytotoxicity by Activating SARM1 in Glioblastoma Cells.Biology · 2024Article
- SARM1-Dependent Axon Degeneration: Nucleotide Signaling, Neurodegenerative Disorders, Toxicity, and Therapeutic Opportunities.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024Review
- SARM1 regulates pro-inflammatory cytokine expression in human monocytes by NADase-dependent and -independent mechanisms.iScience · 2024Article
- A Simple, Fast, Sensitive LC-MS/MS Method to Quantify NAD(H) in Biological Samples: Plasma NAD(H) Measurement to Monitor Brain Pathophysiology.International journal of molecular sciences · 2024Article
- SARM1 regulates NADThe Journal of biological chemistry · 2024Article
- Identification of SIRT3 as an eraser of H4K16la.iScience · 2023Article
- Fingerstick blood assay maps real-world NADAging cell · 2023Article
- CD38/ADP-ribose/TRPM2-mediated nuclear CaExperimental & molecular medicine · 2023Article
- Broader functions of TIR domains in Arabidopsis immunity.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A conformation-specific nanobody targeting the nicotinamide mononucleotide-activated state of SARM1.Nature communications · 2022Article
- Identification of NAPRT Inhibitors with Anti-Cancer Properties by In Silico Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Discovery of small-molecule activators of nicotinamide phosphoribosyltransferase (NAMPT) and their preclinical neuroprotective activity.Cell research · 2022Article
- NADTheranostics · 2022Article
- Article
21 more citing papers are in PubMed but not listed here.
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 at 1 institution in 1 country.
Funding
Abstract
cADP-ribose (cADPR) is a novel cyclic nucleotide derived from NAD(+) that has now been established as a general Ca(2+) messenger in a wide variety of cells. Despite the obvious importance of monitoring its cellular levels under various physiological conditions, its measurement has been technically difficult and requires specialized reagents. In this study a widely applicable high-sensitivity assay for cADPR is described. ADP-ribosyl cyclase normally catalyses the synthesis of cADPR from NAD(+), but the reaction can be reversed in the presence of high concentrations of nicotinamide, producing NAD(+) from cADPR stoichiometrically. The resultant NAD(+) can then be coupled to a cycling assay involving alcohol dehydrogenase and diaphorase. Each time NAD(+) cycles through these coupled reactions, a molecule of highly fluorescent resorufin is generated. The reaction can be conducted for hours, resulting in more than a thousand-fold amplification of cADPR. Concentrations of cADPR in the nanomolar range can be measured routinely. The unique ability of ADP-ribosyl cyclase to catalyse the reverse reaction provides the required specificity. Using this assay, it is demonstrated that cADPR is present in all tissues tested and that the levels measured are directly comparable with those obtained using a radioimmunoassay. All the necessary reagents are widely available and the assay can be performed using a multiwell fluorescence plate reader, providing a high-throughput method for monitoring cADPR levels. This assay should be valuable in elucidating the messenger role of cADPR in cells.
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Registered trials
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.