ArticleProceedings of the National Academy of Sciences of the United States of America2014
The oligonucleotide/oligosaccharide-binding fold motif is a poly(ADP-ribose)-binding domain that mediates DNA damage response.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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Who cites it
41 citing papers in PubMed.
- TRIM21 inhibition alleviates acute kidney injury by promoting INTS3-associated DNA damage repair.Apoptosis : an international journal on programmed cell death · 2026Article
- The Expanding Landscape of ADP-Ribosylation: Protein, DNA, RNA, and Mitochondrial Regulation.Chemical research in toxicology · 2026Review
- Poly-ADP-ribosylation dynamics, signaling, and analysis.Environmental and molecular mutagenesis · 2024Review
- SPIN1 facilitates chemoresistance and HR repair by promoting Tip60 binding to H3K9me3.EMBO reports · 2024Article
- Poly (ADP-ribose) polymerase 1 promotes HuR/ELAVL1 cytoplasmic localization and inflammatory gene expression by regulating p38 MAPK activity.Cellular and molecular life sciences : CMLS · 2024Article
- Mono-ADP-ribosylation, a MARylationmultifaced modification of protein, DNA and RNA: characterizations, functions and mechanisms.Cell death discovery · 2024Review
- Pre-ribosomal RNA reorganizes DNA damage repair factors in nucleus during meiotic prophase and DNA damage response.Cell research · 2022Article
- USP39 promotes non-homologous end-joining repair by poly(ADP-ribose)-induced liquid demixing.Nucleic acids research · 2021Article
- Identifying Poly(ADP-ribose)-Binding Proteins with Photoaffinity-Based Proteomics.Journal of the American Chemical Society · 2021Article
- Functional Roles of Poly(ADP-Ribose) in Stress Granule Formation and Dynamics.Frontiers in cell and developmental biology · 2021Review
- SUMOylation stabilizes hSSB1 and enhances the recruitment of NBS1 to DNA damage sites.Signal transduction and targeted therapy · 2020Article
- Nuclear PARPs and genome integrity.Genes & development · 2020Review
- Review
- An Interaction with PARP-1 and Inhibition of Parylation Contribute to Attenuation of DNA Damage Signaling by the Adenovirus E4orf4 Protein.Journal of virology · 2019Article
- Poly(ADP-Ribose) Polymerase 2 Recruits Replication Protein A to Sites of LINE-1 Integration to Facilitate Retrotransposition.Molecular cell · 2019Article
- SSB1/SSB2 Proteins Safeguard B Cell Development by Protecting the Genomes of B Cell Precursors.Journal of immunology (Baltimore, Md. : 1950) · 2019Article
- The WD40 domain of FBXW7 is a poly(ADP-ribose)-binding domain that mediates the early DNA damage response.Nucleic acids research · 2019Article
- ELTA: Enzymatic Labeling of Terminal ADP-Ribose.Molecular cell · 2019Article
- A Structural Perspective on the Regulation of Human Single-Stranded DNA Binding Protein 1 (hSSB1, OBFC2B) Function in DNA Repair.Computational and structural biotechnology journal · 2019Review
- Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry.Methods in enzymology · 2019Article
Corrections and comments
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Authors and funding
4 authors.
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Abstract
Oligonucleotide/oligosaccharide-binding (OB) fold is a ssDNA or RNA binding motif in prokaryotes and eukaryotes. Unexpectedly, we found that the OB fold of human ssDNA-binding protein 1 (hSSB1) is a poly(ADP ribose) (PAR) binding domain. hSSB1 exhibits high-affinity binding to PAR and recognizes iso-ADP ribose (ADPR), the linkage between two ADPR units. This interaction between PAR and hSSB1 mediates the early recruitment of hSSB1 to the sites of DNA damage. Mutations in the OB fold of hSSB1 that disrupt PAR binding abolish the relocation of hSSB1 to the sites of DNA damage. Moreover, PAR-mediated recruitment of hSSB1 is important for early DNA damage repair. We have screened other OB folds and found that several other OB folds also recognize PAR. Taken together, our study reveals a PAR-binding domain that mediates DNA damage repair.
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