ArticleBMC structural biology2011
Structural studies of the PARP-1 BRCT domain.
Article in BMC structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Identification and Characterization of Novel Inhibitors of Human Poly(ADP-Ribose) Polymerase-1.Molecules (Basel, Switzerland) · 2025Article
- 1,25-Dihydroxyvitamin DInternational journal of molecular sciences · 2024Article
- Comprehensive machine learning boosts structure-based virtual screening for PARP1 inhibitors.Journal of cheminformatics · 2024Article
- Synthesis andCombinatorial chemistry & high throughput screening · 2024Article
- Updated protein domain annotation of the PARP protein family sheds new light on biological function.Nucleic acids research · 2023Article
- Review
- How ligands regulate the binding of PARP1 with DNA: Deciphering the mechanism at the molecular level.PloS one · 2023Article
- Mechanism by which T7 bacteriophage protein Gp1.2 inhibitsProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Deciphering the functional mechanism of zinc ions of PARP1 binding with single strand breaks and double strand breaks.RSC advances · 2022Article
- Multiple roles for PARP1 in ALC1-dependent nucleosome remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Real-time monitoring of PARP1-dependent PARylation by ATR-FTIR spectroscopy.Nature communications · 2020Article
- Review
- Review
- PARP1 in Carcinomas and PARP1 Inhibitors as Antineoplastic Drugs.International journal of molecular sciences · 2017Review
- Coordination of DNA single strand break repair.Free radical biology & medicine · 2017Review
- The structural basis of XRCC1-mediated DNA repair.DNA repair · 2015Review
- Primary identification, biochemical characterization, and immunologic properties of the allergenic pollen cyclophilin cat R 1.The Journal of biological chemistry · 2014Article
- Conformational activation of poly(ADP-ribose) polymerase-1 upon DNA binding revealed by small-angle X-ray scattering.Biochemistry · 2014Article
- Structural Implications for Selective Targeting of PARPs.Frontiers in oncology · 2013Review
- Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.Molecular aspects of medicine · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundPoly(ADP-ribose) polymerase-1 (PARP-1) is one of the first proteins localized to foci of DNA damage. Upon activation by encountering nicked DNA, the PARP-1 mediated trans-poly(ADP-ribosyl)ation of DNA binding proteins occurs, facilitating access and accumulation of DNA repair factors. PARP-1 also auto-(ADP-ribosyl)ates its central BRCT-containing domain forming part of an interaction site for the DNA repair scaffolding protein X-ray cross complementing group 1 protein (XRCC1). The co-localization of XRCC1, as well as bound DNA repair factors, to sites of DNA damage is important for cell survival and genomic integrity.
resultsHere we present the solution structure and biophysical characterization of the BRCT domain of rat PARP-1. The PARP-1 BRCT domain has the globular α/β fold characteristic of BRCT domains and has a thermal melting transition of 43.0°C. In contrast to a previous characterization of this domain, we demonstrate that it is monomeric in solution using both gel-filtration chromatography and small-angle X-ray scattering. Additionally, we report that the first BRCT domain of XRCC1 does not interact significantly with the PARP-1 BRCT domain in the absence of ADP-ribosylation. Moreover, none of the interactions with other longer PARP-1 constructs which previously had been demonstrated in a pull-down assay of mammalian cell extracts were detected.
conclusionsThe PARP-1 BRCT domain has the conserved BRCT fold that is known to be an important protein:protein interaction module in DNA repair and cell signalling pathways. Data indicating no significant protein:protein interactions between PARP-1 and XRCC1 likely results from the absence of poly(ADP-ribose) in one or both binding partners, and further implicates a poly(ADP-ribose)-dependent mechanism for localization of XRCC1 to sites of DNA damage.
Indexed as
Identifiers
What OpenQuestion holds
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.