ArticleJournal of the American Chemical Society2015
Synthesis of dimeric ADP-ribose and its structure with human poly(ADP-ribose) glycohydrolase.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 94 citations in OpenAlex.
- Fully protected pyrophosphatesChemical science · 2026Article
- Versatile and sensitive detection of mono- and poly(ADP-ribosyl)ation reveals XRCC1-dependent remodelling of PARP1 signalling.Nature communications · 2026Article
- Poly(ADP-ribose) (PAR) exhibits ion-dependent structural properties distinct from RNA.Nucleic acids research · 2026Article
- Article
- Convergent Approach Toward ADP-Ribosylated Peptides via a Chemoselective Phosphate Condensation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- A Genetically Encoded Sensor for Real-Time Monitoring of Poly-ADP-Ribosylation Dynamics In Vitro and in Cells.ACS sensors · 2024Article
- Cation-induced intramolecular coil-to-globule transition in poly(ADP-ribose).Nature communications · 2024Article
- DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids.Nucleic acids research · 2024Article
- Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling.Nature communications · 2023Article
- Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling.Molecular cell · 2023Article
- Switch-like compaction of poly(ADP-ribose) upon cation binding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Chemical synthesis of linear ADP-ribose oligomers up to pentamer and their binding to the oncogenic helicase ALC1.Chemical science · 2021Article
- Targeting SARS-CoV-2 Nsp3 macrodomain structure with insights from human poly(ADP-ribose) glycohydrolase (PARG) structures with inhibitors.Progress in biophysics and molecular biology · 2021Article
- Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.Nature communications · 2021Article
- Defective ALC1 nucleosome remodeling confers PARPi sensitization and synthetic lethality with HRD.Molecular cell · 2021Article
- ADP-ribosylhydrolases: from DNA damage repair to COVID-19.Journal of Zhejiang University. Science. B · 2021Review
- ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Poly (ADP-ribose) Interacts With Phosphorylated α-Synuclein in Post Mortem PD Samples.Frontiers in aging neuroscience · 2021Article
- The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response.Frontiers in cell and developmental biology · 2021Review
- ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Poly(ADP-ribosyl)ation is a common post-translational modification that mediates a wide variety of cellular processes including DNA damage repair, chromatin regulation, transcription, and apoptosis. The difficulty associated with accessing poly(ADP-ribose) (PAR) in a homogeneous form has been an impediment to understanding the interactions of PAR with poly(ADP-ribose) glycohydrolase (PARG) and other binding proteins. Here we describe the chemical synthesis of the ADP-ribose dimer, and we use this compound to obtain the first human PARG substrate-enzyme cocrystal structure. Chemical synthesis of PAR is an attractive alternative to traditional enzymatic synthesis and fractionation, allowing access to products such as dimeric ADP-ribose, which has been detected but never isolated from natural sources. Additionally, we describe the synthesis of an alkynylated dimer and demonstrate that this compound can be used to synthesize PAR probes including biotin and fluorophore-labeled compounds. The fluorescently labeled ADP-ribose dimer was then utilized in a general fluorescence polarization-based PAR-protein binding assay. Finally, we use intermediates of our synthesis to access various PAR fragments, and evaluation of these compounds as substrates for PARG reveals the minimal features for substrate recognition and enzymatic cleavage. Homogeneous PAR oligomers and unnatural variants produced from chemical synthesis will allow for further detailed structural and biochemical studies on the interaction of PAR with its many protein binding partners.
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