ArticleMethods in molecular biology (Clifton, N.J.)2017
ADP-Ribosylated Peptide Enrichment and Site Identification: The Phosphodiesterase-Based Method.
Article in Methods in molecular biology (Clifton, N.J.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Cryptic phosphoribosylase activity of NAMPT restricts the virion incorporation of viral proteins.Nature metabolism · 2024Article
- Proteomics techniques in protein biomarker discovery.Quantitative biology (Beijing, China) · 2024Review
- The Interferon-inducible NAMPT acts as a protein phosphoribosylase to restrict viral infection.bioRxiv : the preprint server for biology · 2023Article
- A Combined Gas-Phase Separation Strategy for ADP-ribosylated Peptides.Journal of the American Society for Mass Spectrometry · 2023Article
- PARPs and ADP-Ribosylation in Chronic Inflammation: A Focus on Macrophages.Pathogens (Basel, Switzerland) · 2023Review
- A Novel Spectral Annotation Strategy Streamlines Reporting of Mono-ADP-ribosylated Peptides Derived from Mouse Liver and Spleen in Response to IFN-γ.Molecular & cellular proteomics : MCP · 2022Article
- Insight into the Binding and Hydrolytic Preferences of hNudt16 Based on Nucleotide Diphosphate Substrates.International journal of molecular sciences · 2021Article
- Androgen signaling uses a writer and a reader of ADP-ribosylation to regulate protein complex assembly.Nature communications · 2021Article
- The multifaceted role of PARP1 in RNA biogenesis.Wiley interdisciplinary reviews. RNA · 2021Review
- Dynamic ADP-Ribosylome, Phosphoproteome, and Interactome in LPS-Activated Macrophages.Journal of proteome research · 2020Article
- Simultaneous, Quantitative Characterization of Protein ADP-Ribosylation and Protein Phosphorylation in Macrophages.Methods in molecular biology (Clifton, N.J.) · 2020Article
- ADPredict: ADP-ribosylation site prediction based on physicochemical and structural descriptors.Bioinformatics (Oxford, England) · 2018Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Uncommon posttranslational modifications in proteomics: ADP-ribosylation, tyrosine nitration, and tyrosine sulfation.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Protein ADP-ribosylation is a posttranslational modification (PTM) that plays an important role in all major cellular processes, including DNA repair, cellular signaling, and RNA metabolism. Site identification for this PTM has recently become possible through the development of several mass spectrometry-based methods, a critical step in understanding the regulatory role played by mono(ADP-ribose) (MAR), poly(ADP-ribose) (PAR), and the enzymes which make these modifications: poly(ADP-ribose) polymerases (PARPs), best known for their role in DNA repair and as targets for chemotherapeutic PARP inhibitors. Here, we have described our method for enriching and identifying ADP-ribosylation events through the use of a phosphodiesterase to digest protein-conjugated ADP-ribose down to its attachment structure, phosphoribose. We also include here a guide to choosing between collision-induced dissociation (CID)-, higher-energy collisional dissociation (HCD)-, and electron-transfer dissociation (ETD)-based peptide fragmentation for the identification of phosphoribosylated peptides.
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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.