ArticleNucleic acids research2021
ADPriboDB 2.0: an updated database of ADP-ribosylated proteins.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Alphavirus nsP3 as a multifunctional orchestrator of virus-host interplay.Journal of virology · 2026Review
- Interactomics of SARS-CoV-2 Macrodomain 1 Reveals Putative Clients of ADP-Ribosyl Hydrolase Activity.Viruses · 2026Article
- Comprehensive analysis of the deleterious nonsynonymous, non-coding SNPs and cancer variants of human aldo-keto reductase type 1 (AKR1C1) protein and their probable association with disease risk and progression: a computational study.Biochemistry and biophysics reports · 2026Article
- Interactomics of SARS-CoV-2 Macrodomain 1 Reveals Putative Clients of ADP-ribosyl Hydrolase Activity.bioRxiv : the preprint server for biology · 2025Article
- Structural insights into the roles of PARP4 and NADNature communications · 2025Article
- Proteogenomic reprogramming to a functional human blastomere-like stem cell state via a PARP-DUX4 regulatory axis.Cell reports · 2025Article
- Reduction of Chemokine CXCL9 Expression by Omega-3 Fatty Acids via ADP-Ribosylhydrolase ARH3 in MIN6 Insulin-Producing Cells.Proteomics · 2025Article
- Regulation of stress granule maturation and dynamics by poly(ADP-ribose) interaction with PARP13.Nature communications · 2025Article
- Mono-ADP-Ribosylation of Peptides: An Overview of Synthetic and Chemoenzymatic Methodologies.Chembiochem : a European journal of chemical biology · 2024Review
- SART1 modulates poly-(ADP-ribose) chain accumulation and PARP1 chromatin localization.iScience · 2024Article
- Acetylation, ADP-ribosylation and methylation of malate dehydrogenase.Essays in biochemistry · 2024Review
- PARP4 interacts with hnRNPM to regulate splicing during lung cancer progression.Genome medicine · 2024Article
- PARP trapping is governed by the PARP inhibitor dissociation rate constant.Cell chemical biology · 2024Article
- Novel modifications of PARP inhibitor veliparib increase PARP1 binding to DNA breaks.The Biochemical journal · 2024Article
- R-Loop Accumulation in Spliceosome Mutant Leukemias Confers Sensitivity to PARP1 Inhibition by Triggering Transcription-Replication Conflicts.Cancer research · 2024Article
- Olaparib combined with CDK12-IN-3 to promote genomic instability and cell death in ovarian cancer.International journal of biological sciences · 2024Article
- Detection and Analysis of Short Linear Motif-Based Protein-Protein Interactions with SLiMAn2 Web Server.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Impact of Asp/Glu-ADP-ribosylation on protein-protein interaction and protein function.Proteomics · 2023Article
- Using TLC-MALDI-TOF to Interrogate In Vitro Peptidyl Proximal Preferences of PARP14 and Glycohydrolase Specificity.Molecules (Basel, Switzerland) · 2023Article
- Regulation of Biomolecular Condensates by Poly(ADP-ribose).Chemical reviews · 2023Review
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Abstract
ADP-ribosylation is a protein modification responsible for biological processes such as DNA repair, RNA regulation, cell cycle and biomolecular condensate formation. Dysregulation of ADP-ribosylation is implicated in cancer, neurodegeneration and viral infection. We developed ADPriboDB (adpribodb.leunglab.org) to facilitate studies in uncovering insights into the mechanisms and biological significance of ADP-ribosylation. ADPriboDB 2.0 serves as a one-stop repository comprising 48 346 entries and 9097 ADP-ribosylated proteins, of which 6708 were newly identified since the original database release. In this updated version, we provide information regarding the sites of ADP-ribosylation in 32 946 entries. The wealth of information allows us to interrogate existing databases or newly available data. For example, we found that ADP-ribosylated substrates are significantly associated with the recently identified human protein interaction networks associated with SARS-CoV-2, which encodes a conserved protein domain called macrodomain that binds and removes ADP-ribosylation. In addition, we create a new interactive tool to visualize the local context of ADP-ribosylation, such as structural and functional features as well as other post-translational modifications (e.g. phosphorylation, methylation and ubiquitination). This information provides opportunities to explore the biology of ADP-ribosylation and generate new hypotheses for experimental testing.
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