ReviewNucleic acids research2025
Histone PARylation factor 1: a review of its role in the DNA damage response.
Review in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- DNA-PKcs and PARP1 at the interface between DNA damage responses and cGAS-STING signaling: context-dependent roles and therapeutic implications.Cancer biology & therapy · 2026Review
- Hyperosmotic stress induces PARP1-mediated HPF1-dependent mono(ADP-ribosyl)ation.FEBS letters · 2026Article
- ROS-ATM-CBP axis-mediated PARP1 lactylation aggravates doxorubicin-induced cardiotoxicity.Clinical and translational medicine · 2026Article
- PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026Article
- Interpretable QSAR and Complementary Docking for PARP1 Inhibitor Prioritization: Reliability Stratification and Near-Domain Screening.Pharmaceuticals (Basel, Switzerland) · 2026Article
- HPF1 regulates the formation of FUS-dependent compartments by PARP1 and PARP2 activation on damaged DNA.Nucleic acids research · 2026Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Although poly-(ADP ribose) polymerase 1 (PARP1) and PARylation of histones have been known for over 50 years and have been successfully targeted by anti-cancer drugs, we are just coming up to the 10-year anniversary of the paradigm-shifting discovery of histone PARylation factor 1 (HPF1), the protein that facilitates the modification of histones by PARP1. In addition to forming a shared active site with PARP1 by contributing a catalytic residue, HPF1 dramatically changes the activity of PARP1 both in vitro and in vivo with respect to substrate choice, PAR chain length, sites of modification, and consequent effects on chromatin. In this review, we summarize the current knowledge status in the PARP1-HPF1 field, with an emphasis on the many open questions that the PARP research community still needs to resolve. A better understanding of this intriguing enzyme system will enable ongoing efforts to develop a more complete understanding of the response to DNA damage and better inhibitors of PARP1.
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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.