ReviewMolecular aspects of medicine2013
Reprogramming cellular events by poly(ADP-ribose)-binding proteins.
Review in Molecular aspects of medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
101 citing papers in PubMed.
- PARylation in Parkinson's disease: a bridge between Lewy body formation and neuronal cell death.Cell death & disease · 2026Article
- Noncovalent PAR Binding Guides Proteins to PARP1-Mediated PARylation.ACS chemical biology · 2026Article
- Review
- CHD6 has poly(ADP-ribose)- and DNA-binding domains and regulates PARP1/2-trapping inhibitor sensitivity via abasic site repair.Nature communications · 2025Article
- Medroxyprogesterone promotes neuronal survival after cerebral ischemic stroke by inhibiting PARthanatos.Frontiers in pharmacology · 2025Article
- Phase Separation of FUS with Poly(ADP-ribosyl)ated PARP1 Is Controlled by Polyamines, Divalent Metal Cations, and Poly(ADP-ribose) Structure.International journal of molecular sciences · 2024Article
- Poly-ADP-ribosylation dynamics, signaling, and analysis.Environmental and molecular mutagenesis · 2024Review
- pADP-ribosylation regulates the cytoplasmic localization, cleavage, and pro-apoptotic function of HuR.Life science alliance · 2024Article
- Poly (ADP-ribose) polymerase inhibitor therapy and mechanisms of resistance in epithelial ovarian cancer.Frontiers in oncology · 2024Review
- Unravelling the molecular basis of PARP inhibitor resistance in prostate cancer with homologous recombination repair deficiency.International review of cell and molecular biology · 2024Review
- PARIS undergoes liquid-liquid phase separation and poly(ADP-ribose)-mediated solidification.EMBO reports · 2023Article
- Mitochondrial Factors in the Cell Nucleus.International journal of molecular sciences · 2023Review
- Regulation of Biomolecular Condensates by Poly(ADP-ribose).Chemical reviews · 2023Review
- Cervical cancer: a tale from HPV infection to PARP inhibitors.Genes & diseases · 2023Review
- Synthesis and Degradation of Poly(ADP-ribose) in Zebrafish Brain Exposed to Aluminum.International journal of molecular sciences · 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
- Influence of chain length and branching on poly(ADP-ribose)-protein interactions.Nucleic acids research · 2023Article
- The XPA Protein-Life under Precise Control.Cells · 2022Review
- A Double-Edged Sword: The Two Faces of PARylation.International journal of molecular sciences · 2022Review
- Article
41 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors.
Funding
Abstract
Poly(ADP-ribosyl)ation is a posttranslational modification catalyzed by the poly(ADP-ribose) polymerases (PARPs). These enzymes covalently modify glutamic, aspartic and lysine amino acid side chains of acceptor proteins by the sequential addition of ADP-ribose (ADPr) units. The poly(ADP-ribose) (pADPr) polymers formed alter the physico-chemical characteristics of the substrate with functional consequences on its biological activities. Recently, non-covalent binding to pADPr has emerged as a key mechanism to modulate and coordinate several intracellular pathways including the DNA damage response, protein stability and cell death. In this review, we describe the basis of non-covalent binding to pADPr that has led to the emerging concept of pADPr-responsive signaling pathways. This review emphasizes the structural elements and the modular strategies developed by pADPr-binding proteins to exert a fine-tuned control of a variety of pathways. Poly(ADP-ribosyl)ation reactions are highly regulated processes, both spatially and temporally, for which at least four specialized pADPr-binding modules accommodate different pADPr structures and reprogram protein functions. In this review, we highlight the role of well-characterized and newly discovered pADPr-binding modules in a diverse set of physiological functions.
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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.