ArticleJournal of molecular recognition : JMR
Binding kinetics and activity of human poly(ADP-ribose) polymerase-1 on oligo-deoxyribonucleotide substrates.
Article in Journal of molecular recognition : JMR. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
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.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Applications of Surface Plasmon Resonance for Advanced Studies Involving Nucleic Acids.RNA nanomed · 2024Article
- Background-Quenched Aggregation-Induced Emission through Electrostatic Interactions for the Detection of Poly(ADP-ribose) Polymerase-1 Activity.Molecules (Basel, Switzerland) · 2023Article
- Polymerase theta-helicase promotes end joining by stripping single-stranded DNA-binding proteins and bridging DNA ends.Nucleic acids research · 2022Article
- Probing the Conformational Changes Associated with DNA Binding to PARP1.Biochemistry · 2020Article
- Article
- Investigating cyclic nucleotide and cyclic dinucleotide binding to HCN channels by surface plasmon resonance.PloS one · 2017Article
- Polymerase/DNA interactions and enzymatic activity: multi-parameter analysis with electro-switchable biosurfaces.Scientific reports · 2015Article
- Active DNA demethylation in post-mitotic neurons: a reason for optimism.Neuropharmacology · 2013Review
- Regulation of chromatin structure by poly(ADP-ribosyl)ation.Frontiers in genetics · 2012Article
- Double-stranded DNA binding domain of poly(ADP-ribose) polymerase-1 and molecular insight into the regulation of its activity.The Journal of biological chemistry · 2011Article
- Recognition of platinum-DNA damage by poly(ADP-ribose) polymerase-1.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Poly(ADP-ribose) polymerase-1 (PARP-1) is a mammalian enzyme that attaches long branching chains of ADP-ribose to specific nuclear proteins, including itself. Because its activity in vitro is dependent upon interaction with broken DNA, it has been postulated that PARP-1 plays an important role in DNA strand-break repair in vivo. The exact mechanism of binding to DNA and the structural determinants of binding remain to be defined, but regions of transition from single-stranded to double-strandedness may be important recognition sites. Here we employ surface plasmon resonance (SPR) to investigate this hypothesis. Oligodeoxynucleotide (ODN) substrates that mimic DNA with different degrees of single-strandedness were used for measurements of both PARP-1/DNA binding kinetics and PARP-1's enzyme activities. We found that binding correlated with activity, but was unrelated to single-strandedness of the ODN. Instead, PARP-1 binding and activity were highest on ODNs that modeled a DNA double-strand break (DSB). These results provide support for PARP-1 recognizing and binding DSBs in a manner that is independent of single-stranded features, and demonstrate the usefulness of SPR for simultaneously investigating both PARP-1 binding and PARP-1 auto-poly(ADP-ribosyl)ation activities within the same in vitro system.
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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.