ArticleProtein science : a publication of the Protein Society2002
The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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Who cites it
85 citing papers in PubMed, 169 citations in OpenAlex.
- The ADP-ribosyltransferases 3 (ART3) is a novel suppressor of pathological cardiac hypertrophy by ribosylating ITGA7.Acta pharmaceutica Sinica. B · 2026Article
- Transition-state analysis of the arginine-specific human ADP-ribosyltransferase 1.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Deciphering cytokine-driven ADP-ribosylation signaling networks via Af1521-based mass spectrometry analysis of labile Glu/Asp-linkages.Nature communications · 2026Article
- Kinetic Mechanism of the Emergent Anticancer Target, Human ADP-ribosyltransferase 1.Biochemistry · 2025Article
- ATP-Gated P2X7-Ion Channel on Kidney-Resident Natural Killer T Cells and Memory T Cells in Intrarenal Inflammation.Journal of the American Society of Nephrology : JASN · 2025Article
- Mono-ADP-Ribosylation of Peptides: An Overview of Synthetic and Chemoenzymatic Methodologies.Chembiochem : a European journal of chemical biology · 2024Review
- ADP-ribose hydrolases: biological functions and potential therapeutic targets.Expert reviews in molecular medicine · 2024Review
- CD157 selectively identifies hPSCs with enhanced hepatic differentiation capacity.Life medicine · 2024Article
- Pathological and physiological roles of ADP-ribosylation: established functions and new insights.Biological chemistry · 2024Review
- ARTC1-mediated VAPB ADP-ribosylation regulates calcium homeostasis.Journal of molecular cell biology · 2024Article
- The pseudoenzyme ADPRHL1 affects cardiac function by regulating the ROCK pathway.Stem cell research & therapy · 2023Article
- ARH Family of ADP-Ribose-Acceptor Hydrolases.Cells · 2022Review
- Are PARPs promiscuous?Bioscience reports · 2022Review
- Article
- Functional roles of ADP-ribosylation writers, readers and erasers.Frontiers in cell and developmental biology · 2022Review
- The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape.Genes · 2021Review
- Neurotransmitters responsible for purinergic motor neurotransmission and regulation of GI motility.Autonomic neuroscience : basic & clinical · 2021Article
- ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function.Nucleic acids research · 2021Review
- Enzymology of extracellular NAD metabolism.Cellular and molecular life sciences : CMLS · 2021Review
- Article
25 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 2 institutions in 1 country.
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Abstract
ADP-ribosyltransferases including toxins secreted by Vibrio cholera, Pseudomonas aerurginosa, and other pathogenic bacteria inactivate the function of human target proteins by attaching ADP-ribose onto a critical amino acid residue. Cross-species polymerase chain reaction (PCR) and database mining identified the orthologs of these ADP-ribosylating toxins in humans and the mouse. The human genome contains four functional toxin-related ADP-ribosyltransferase genes (ARTs) and two related intron-containing pseudogenes; the mouse has six functional orthologs. The human and mouse ART genes map to chromosomal regions with conserved linkage synteny. The individual ART genes reveal highly restricted expression patterns, which are largely conserved in humans and the mouse. We confirmed the predicted extracellular location of the ART proteins by expressing recombinant ARTs in insect cells. Two human and four mouse ARTs contain the active site motif (R-S-EXE) typical of arginine-specific ADP-ribosyltransferases and exhibit the predicted enzyme activities. Two other human ARTs and their murine orthologues deviate in the active site motif and lack detectable enzyme activity. Conceivably, these ARTs may have acquired a new specificity or function. The position-sensitive iterative database search program PSI-BLAST connected the mammalian ARTs with most known bacterial ADP-ribosylating toxins. In contrast, no related open reading frames occur in the four completed genomes of lower eucaryotes (yeast, worm, fly, and mustard weed). Interestingly, these organisms also lack genes for ADP-ribosylhydrolases, the enzymes that reverse protein ADP-ribosylation. This suggests that the two enzyme families that catalyze reversible mono-ADP-ribosylation either were lost from the genomes of these nonchordata eucaryotes or were subject to horizontal gene transfer between kingdoms.
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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.