ArticleMethods in enzymology2019
Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry.
Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- A Large-Scale Method to Measure the Stoichiometries of Protein Poly-ADP-Ribosylation.ACS chemical biology · 2026Article
- Overexpression of the WWE domain of RNF146 modulates poly-(ADP)-ribose dynamics at sites of DNA damage.DNA repair · 2025Article
- Poly-ADP-ribosylation dynamics, signaling, and analysis.Environmental and molecular mutagenesis · 2024Review
- PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae.Nature communications · 2024Article
- General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase-Substrate Complexes.Toxins · 2024Review
- Article
- The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.Nature communications · 2021Article
- Serine-linked PARP1 auto-modification controls PARP inhibitor response.Nature communications · 2021Article
- MARTs and MARylation in the Cytosol: Biological Functions, Mechanisms of Action, and Therapeutic Potential.Cells · 2021Review
- Mapping Physiological ADP-Ribosylation Using Activated Ion Electron Transfer Dissociation.Cell reports · 2020Article
- 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 2 institutions in 1 country.
Funding
Abstract
ADP-ribosylation is a protein post-translational modification that is critically involved in a wide array of biological processes connected to cell stress responses. Enzymes known as poly-ADP-ribose polymerases (PARPs) catalyze the addition of the ADP-ribose units to amino acids with various side chain chemistries. In particular, the PARP family member PARP1 is responsible for the modification of a large number of proteins and is involved in initiation of the DNA damage response, although the mechanisms through which PARP1 functions are still incompletely understood. The analysis of protein ADP-ribosylation is challenging because PARylation is a low-abundance, labile and heterogeneous protein modification. Recently, we developed an integrative proteomic platform for the site-specific analysis of protein ADP-ribosylation on Asp and Glu residues. Herein, we describe the method, and demonstrate its utility in quantitative characterization of the human Asp- and Glu-ADP-ribosylated proteome.
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Registered trials
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