ArticleJournal of molecular biology2011
The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 98 papers.
What it found
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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.
The trial behind it
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Who cites it
98 citing papers in PubMed, 177 citations in OpenAlex.
- PARP-1 protein expression in glioblastoma multiforme.European journal of histochemistry : EJH · 2012Trial
- The Landscape of BRCA1-Associated Post-Translational Modifications.Cell biology international · 2026Review
- The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- The dynamic and heterogeneous composition of biomolecular condensates and its functional relevance.Nature reviews. Molecular cell biology · 2026Review
- PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation.Nature communications · 2026Article
- Nuclear poly(A)-binding protein and nucleolin utilize their RNA recognition motifs to read PAR chains.Nucleic acids research · 2025Article
- FGFR3-induced Y158 PARP1 phosphorylation promotes PARP inhibitor resistance via BRG1/MRE11-mediated DNA repair in breast cancer models.The Journal of clinical investigation · 2025Article
- Article
- Impact of a Cancer-Associated Mutation on Poly(ADP-ribose) Polymerase1 Inhibition.The journal of physical chemistry. B · 2025Article
- PARP inhibitors as radiosensitizers: a comprehensive review of preclinical evidence and clinical applications.Frontiers in oncology · 2025Review
- PARP enzyme de novo synthesis of protein-free poly(ADP-ribose).Molecular cell · 2024Article
- PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation.EMBO reports · 2024Article
- Impact of a Cancer-Associated Mutation on Poly(ADP-ribose) Polymerase1 Inhibition.bioRxiv : the preprint server for biology · 2024Article
- Cisplatin in the era of PARP inhibitors and immunotherapy.Pharmacology & therapeutics · 2024Review
- Stress-Induced Changes in Nucleocytoplasmic Localization of Crucial Factors in Gene Expression Regulation.International journal of molecular sciences · 2024Article
- Cooperative nucleic acid binding by Poly ADP-ribose polymerase 1.Scientific reports · 2024Article
- Multifaceted roles of CCAR family proteins in the DNA damage response and cancer.Experimental & molecular medicine · 2024Review
- PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation.bioRxiv : the preprint server for biology · 2024Article
- Aging mitochondria in the context of SARS-CoV-2: exploring interactions and implications.Frontiers in aging · 2024Review
- CellTool: An Open-Source Software Combining Bio-Image Analysis and Mathematical Modeling for the Study of DNA Repair Dynamics.International journal of molecular sciences · 2023Article
38 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Poly(ADP-ribose)polymerase-1 (PARP-1) is a highly abundant chromatin-associated enzyme present in all higher eukaryotic cell nuclei, where it plays key roles in the maintenance of genomic integrity, chromatin remodeling and transcriptional control. It binds to DNA single- and double-strand breaks through an N-terminal region containing two zinc fingers, F1 and F2, following which its C-terminal catalytic domain becomes activated via an unknown mechanism, causing formation and addition of polyadenosine-ribose (PAR) to acceptor proteins including PARP-1 itself. Here, we report a biophysical and structural characterization of the F1 and F2 fingers of human PARP-1, both as independent fragments and in the context of the 24-kDa DNA-binding domain (F1+F2). We show that the fingers are structurally independent in the absence of DNA and share a highly similar structural fold and dynamics. The F1+F2 fragment recognizes DNA single-strand breaks as a monomer and in a single orientation. Using a combination of NMR spectroscopy and other biophysical techniques, we show that recognition is primarily achieved by F2, which binds the DNA in an essentially identical manner whether present in isolation or in the two-finger fragment. F2 interacts much more strongly with nicked or gapped DNA ligands than does F1, and we present a mutational study that suggests origins of this difference. Our data suggest that different DNA lesions are recognized by the DNA-binding domain of PARP-1 in a highly similar conformation, helping to rationalize how the full-length protein participates in multiple steps of DNA single-strand breakage and base excision repair.
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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.