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HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1016/j.cell.2011.02.013openalex-snapshot
Hallmarks of Cancer: The Next Generation
inferredcites →https://doi.org/10.1016/j.cell.2013.08.021openalex-snapshot
Double Nicking by RNA-Guided CRISPR Cas9 for Enhanced Genome Editing Specificity
inferredcites →https://doi.org/10.1016/j.cell.2015.09.053openalex-snapshot
A Human Interactome in Three Quantitative Dimensions Organized by Stoichiometries and Abundances
inferredcites →https://doi.org/10.1016/j.celrep.2015.09.017openalex-snapshot
TIMELESS Forms a Complex with PARP1 Distinct from Its Complex with TIPIN and Plays a Role in the DNA Damage Response
inferredcites →https://doi.org/10.1016/j.dnarep.2014.05.003openalex-snapshot
Distribution of protein poly(ADP-ribosyl)ation systems across all domains of life
inferredcites →https://doi.org/10.1016/j.dnarep.2015.04.008openalex-snapshot
The rise and fall of poly(ADP-ribose): An enzymatic perspective
inferredcites →https://doi.org/10.1016/j.molcel.2010.12.008openalex-snapshot
DNA Repair Factor APLF Is a Histone Chaperone
inferredcites →https://doi.org/10.1016/j.molcel.2014.12.001openalex-snapshot
Ubiquitin-SUMO Circuitry Controls Activated Fanconi Anemia ID Complex Dosage in Response to DNA Damage
inferredcites →https://doi.org/10.1016/j.molcel.2015.05.007openalex-snapshot
Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation
inferredcites →https://doi.org/10.1016/j.molcel.2015.07.031openalex-snapshot
Timeless Interacts with PARP-1 to Promote Homologous Recombination Repair
inferredcites →https://doi.org/10.1016/j.molonc.2011.07.001openalex-snapshot
The underlying mechanism for the PARP and BRCA synthetic lethality: Clearing up the misunderstandings
inferredcites →https://doi.org/10.1038/emboj.2013.51openalex-snapshot
Deficiency of terminal ADP‐ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease
inferredcites →https://doi.org/10.1038/nature06420openalex-snapshot
Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins
inferredcites →https://doi.org/10.1038/nature08467openalex-snapshot
The DNA-damage response in human biology and disease
inferredcites →https://doi.org/10.1038/nature10404openalex-snapshot
The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase
inferredcites →https://doi.org/10.1038/ncomms3164openalex-snapshot
Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities
inferredcites →https://doi.org/10.1038/nsmb.1664openalex-snapshot
A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation
inferredcites →https://doi.org/10.1038/nsmb.2335openalex-snapshot
The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks
inferredcites →https://doi.org/10.1073/pnas.1405005111openalex-snapshot
Automodification switches PARP-1 function from chromatin architectural protein to histone chaperone
inferredcites →https://doi.org/10.1074/jbc.m112.401141openalex-snapshot
Activation of the SNF2 Family ATPase ALC1 by Poly(ADP-ribose) in a Stable ALC1·PARP1·Nucleosome Intermediate
inferredcites →https://doi.org/10.1093/nar/gkg761openalex-snapshot
A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
inferredcites →https://doi.org/10.1093/nar/gkv1344openalex-snapshot
The Pfam protein families database: towards a more sustainable future
inferredcites →https://doi.org/10.1111/j.1365-2443.2009.01369.xopenalex-snapshot
Solution structure of a zinc‐finger domain that binds to poly‐ADP‐ribose
inferredcites →https://doi.org/10.1126/science.1177321openalex-snapshot
Poly(ADP-ribose)–Dependent Regulation of DNA Repair by the Chromatin Remodeling Enzyme ALC1
inferredcites →https://doi.org/10.1126/science.1216338openalex-snapshot
Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/1873-3468.70241openalex-snapshot
The role of histone modifications in transcription regulation upon DNA damage
inferred← citeshttps://doi.org/10.1002/1873-3468.70334openalex-snapshot
Hyperosmotic stress induces PARP1 ‐mediated HPF1 ‐dependent mono( ADP ‐ribosyl)ation
inferred← citeshttps://doi.org/10.1002/chem.202100337openalex-snapshot
Molecular Tools for the Study of ADP‐Ribosylation: A Unified and Versatile Method to Synthesise Native Mono‐ADP‐Ribosylated Peptides
inferred← citeshttps://doi.org/10.1002/ijc.32131openalex-snapshot
Increased PARP1‐DNA binding due to autoPARylation inhibition of PARP1 on DNA rather than PARP1‐DNA trapping is correlated with PARP1 inhibitor's cytotoxicity
inferred← citeshttps://doi.org/10.1002/med.21442openalex-snapshot
Therapeutic Targeting of Poly(ADP‐Ribose) Polymerase‐1 (PARP1) in Cancer: Current Developments, Therapeutic Strategies, and Future Opportunities
inferred← citeshttps://doi.org/10.1007/82_2018_137openalex-snapshot
Small-Molecule Inhibitors of PARPs: From Tools for Investigating ADP-Ribosylation to Therapeutics
inferred← citeshttps://doi.org/10.1007/978-1-0716-2891-1_11openalex-snapshot
Functional Analysis of Histone ADP-Ribosylation In Vitro and in Cells
inferred← citeshttps://doi.org/10.1007/978-1-0716-2891-1_4openalex-snapshot
Analyzing PARP1 Activity: Small Molecule Reactants and Attached Chains of Poly (ADP-Ribose)
inferred← citeshttps://doi.org/10.1007/978-1-0716-2891-1_8openalex-snapshot
A Simple Method to Study ADP-Ribosylation Reversal: From Function to Drug Discovery
inferred← citeshttps://doi.org/10.1007/978-981-92-0477-9_3openalex-snapshot
Targeting DNA Damage Response Pathways for Cancer Therapy
inferred← citeshttps://doi.org/10.1007/s00044-024-03282-4openalex-snapshot
Targeting selective inhibitors of PARPs in drug discovery and development
inferred← citeshttps://doi.org/10.1007/s00427-018-0608-9openalex-snapshot
Analysis of hpf1 expression and function in early embryonic development of zebrafish
inferred← citeshttps://doi.org/10.1007/s11596-024-2943-6openalex-snapshot
Regulation of Alternative Splicing by PARP1 in HTR-8/Svneo Cells: Implications for Placental Development and Spontaneous Abortion
inferred← citeshttps://doi.org/10.1007/s13258-023-01447-wopenalex-snapshot
HPF1 regulates tendon stem/progenitor cell senescence and tendon repair via PARP1-mediated poly-ADP ribosylation of HuR
inferred← citeshttps://doi.org/10.1007/s42764-023-00100-wopenalex-snapshot
PARP molecular functions and applications of PARP inhibitors in cancer treatment
inferred← citeshttps://doi.org/10.1016/b978-0-443-19001-8.00007-6openalex-snapshot
Regulation of chromatin structure and function by adenosine diphosphate (ADP)-ribosylation
inferred← citeshttps://doi.org/10.1016/j.ajog.2022.11.1274openalex-snapshot
Copy number variants and fetal growth in stillbirths
inferred← citeshttps://doi.org/10.1016/j.arr.2023.102078openalex-snapshot
Poly (ADP-ribose) polymerase 1 and neurodegenerative diseases: Past, present, and future
inferred← citeshttps://doi.org/10.1016/j.bbcan.2025.189282openalex-snapshot
PARP1: A comprehensive review of its mechanisms, therapeutic implications and emerging cancer treatments
inferred← citeshttps://doi.org/10.1016/j.bcp.2019.05.019openalex-snapshot
PARPs and PAR as novel pharmacological targets for the treatment of stress granule-associated disorders
inferred← citeshttps://doi.org/10.1016/j.bcp.2019.06.001openalex-snapshot
Targeting ADP-ribosylation as an antimicrobial strategy
inferred← citeshttps://doi.org/10.1016/j.bcp.2024.116174openalex-snapshot
Parthanatos: Mechanisms, modulation, and therapeutic prospects in neurodegenerative disease and stroke
inferred← citeshttps://doi.org/10.1016/j.bcp.2026.117770openalex-snapshot
The PARG frontier: mechanisms of PAR turnover and opportunities in precision oncology
inferred← citeshttps://doi.org/10.1016/j.biochi.2024.08.004openalex-snapshot
Unlocking the potential of histone modification in regulating bone metabolism
inferred← citeshttps://doi.org/10.1016/j.biopha.2022.114028openalex-snapshot
Poly-ADP-ribose polymerase (PARP) inhibitors and ovarian function
inferred← citeshttps://doi.org/10.1016/j.bpj.2019.04.032openalex-snapshot
Q-FADD: A Mechanistic Approach for Modeling the Accumulation of Proteins at Sites of DNA Damage
inferred← citeshttps://doi.org/10.1016/j.canlet.2024.216952openalex-snapshot
PARP1 interacts with WDR5 to enhance target gene recognition and facilitate tumorigenesis
inferred← citeshttps://doi.org/10.1016/j.cell.2020.09.055openalex-snapshot
An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
inferred← citeshttps://doi.org/10.1016/j.cell.2023.08.030openalex-snapshot
ADP-ribosylation from molecular mechanisms to therapeutic implications
inferred← citeshttps://doi.org/10.1016/j.cellsig.2022.110518openalex-snapshot
Complement factor D derived from epicardial adipose tissue participates in cardiomyocyte apoptosis after myocardial infarction by mediating PARP-1 activity
inferred← citeshttps://doi.org/10.1016/j.celrep.2016.07.087openalex-snapshot
MRNIP/C5orf45 Interacts with the MRN Complex and Contributes to the DNA Damage Response
inferred← citeshttps://doi.org/10.1016/j.celrep.2017.10.106openalex-snapshot
A Cell-Line-Specific Atlas of PARP-Mediated Protein Asp/Glu-ADP-Ribosylation in Breast Cancer
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.07.083openalex-snapshot
Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.08.092openalex-snapshot
Interplay of Histone Marks with Serine ADP-Ribosylation
inferred← citeshttps://doi.org/10.1016/j.celrep.2022.110879openalex-snapshot
MDM2 binds and ubiquitinates PARP1 to enhance DNA replication fork progression
inferred← citeshttps://doi.org/10.1016/j.celrep.2023.113113openalex-snapshot
The interplay of TARG1 and PARG protects against genomic instability
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.113845openalex-snapshot
Poly(ADP-ribosyl)ation of TIMELESS limits DNA replication stress and promotes stalled fork protection
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.114433openalex-snapshot
ADP-ribosylome analysis reveals homogeneous DNA-damage-induced serine ADP-ribosylation across wild-type and BRCA-mutant breast cancer cell lines
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.114626openalex-snapshot
ALS-FUS mutations cause abnormal PARylation and histone H1.2 interaction, leading to pathological changes
inferred← citeshttps://doi.org/10.1016/j.celrep.2025.115737openalex-snapshot
ADP-ribosylation of NuMA promotes DNA single-strand break repair and transcription
inferred← citeshttps://doi.org/10.1016/j.celrep.2026.117350openalex-snapshot
PARP1-specific inhibitor displays PARP1-detrapping activity
inferred← citeshttps://doi.org/10.1016/j.chembiol.2018.11.001openalex-snapshot
(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition
inferred← citeshttps://doi.org/10.1016/j.csbj.2023.10.013openalex-snapshot
Allosteric crosstalk in modular proteins: Function fine-tuning and drug design
inferred← citeshttps://doi.org/10.1016/j.dnarep.2018.08.022openalex-snapshot
The comings and goings of PARP-1 in response to DNA damage
inferred← citeshttps://doi.org/10.1016/j.dnarep.2019.102650openalex-snapshot
Quantitating repair protein accumulation at DNA lesions: Past, present, and future
inferred← citeshttps://doi.org/10.1016/j.dnarep.2021.103125openalex-snapshot
PARP1: Structural insights and pharmacological targets for inhibition
inferred← citeshttps://doi.org/10.1016/j.dnarep.2021.103144openalex-snapshot
ADP-ribosylation of DNA and RNA
inferred← citeshttps://doi.org/10.1016/j.dnarep.2022.103382openalex-snapshot
The fast-growing business of Serine ADP-ribosylation
inferred← citeshttps://doi.org/10.1016/j.dnarep.2022.103423openalex-snapshot
The HPF1-dependent histone PARylation catalyzed by PARP2 is specifically stimulated by an incised AP site-containing BER DNA intermediate
inferred← citeshttps://doi.org/10.1016/j.dnarep.2024.103690openalex-snapshot
The dynamics and regulation of PARP1 and PARP2 in response to DNA damage and during replication
inferred← citeshttps://doi.org/10.1016/j.dnarep.2024.103711openalex-snapshot
PARticular MARks: Histone ADP-ribosylation and the DNA damage response
inferred← citeshttps://doi.org/10.1016/j.dnarep.2025.103863openalex-snapshot
PARPs and ADP-ribosyl hydrolases in cancer therapy: From drug targets to biomarkers
inferred← citeshttps://doi.org/10.1016/j.dnarep.2025.103873openalex-snapshot
Multiple functions of PARP1 in the repair of DNA double strand breaks
inferred← citeshttps://doi.org/10.1016/j.dnarep.2025.103898openalex-snapshot
PARP enzyme synthesis of protein-free poly(ADP-ribose): Implications for DNA damage signaling and repair
inferred← citeshttps://doi.org/10.1016/j.dnarep.2026.103960openalex-snapshot
ZIPPing the gaps: A new class of zinc finger proteins orchestrates the DNA damage response
inferred← citeshttps://doi.org/10.1016/j.ejmech.2025.117937openalex-snapshot
Poly(ADP-ribose) polymerase-1 (PARP1)-based dual inhibitors targeting cancer synthetic lethality (2022-present): advances and perspectives
inferred← citeshttps://doi.org/10.1016/j.fct.2022.112822openalex-snapshot
Mechanistic studies on the adverse effects of manganese overexposure in differentiated LUHMES cells
inferred← citeshttps://doi.org/10.1016/j.gde.2021.07.005openalex-snapshot
Serine ADP-ribosylation in DNA-damage response regulation
inferred← citeshttps://doi.org/10.1016/j.heliyon.2023.e23829openalex-snapshot
ANP32B promotes colorectal cancer cell progression and reduces cell sensitivity to PRAP1 inhibitor through up-regulating HPF1
inferred← citeshttps://doi.org/10.1016/j.isci.2021.102432openalex-snapshot
MyoD induces ARTD1 and nucleoplasmic poly-ADP-ribosylation during fibroblast to myoblast transdifferentiation
inferred← citeshttps://doi.org/10.1016/j.jare.2025.06.020openalex-snapshot
Targeting post-translational modifications: novel insights into bone metabolic diseases
inferred← citeshttps://doi.org/10.1016/j.jbc.2023.105397openalex-snapshot
ADP-ribose contributions to genome stability and PARP enzyme trapping on sites of DNA damage; paradigm shifts for a coming-of-age modification
inferred← citeshttps://doi.org/10.1016/j.jbc.2024.107838openalex-snapshot
Reversal of tyrosine-linked ADP-ribosylation by ARH3 and PARG
inferred← citeshttps://doi.org/10.1016/j.jbc.2025.108361openalex-snapshot
Duplexed CeTEAM drug biosensors reveal determinants of PARP inhibitor selectivity in cells
inferred← citeshttps://doi.org/10.1016/j.jmb.2026.169753openalex-snapshot
High-Yield Production of Modified DNA Enables Structural Analysis of PARP2 Recognition of Nucleosomal Single-Strand Breaks
inferred← citeshttps://doi.org/10.1016/j.mcpro.2025.101034openalex-snapshot
Multi-omics Characterization of Acquired Olaparib Resistance in BRCA1 and BRCA2 Mutant Breast Cancer Cell Lines
inferred← citeshttps://doi.org/10.1016/j.molcel.2017.01.003openalex-snapshot
Serine ADP-Ribosylation Depends on HPF1
inferred← citeshttps://doi.org/10.1016/j.molcel.2017.02.012openalex-snapshot
SERious Surprises for ADP-Ribosylation Specificity: HPF1 Switches PARP1 Specificity to Ser Residues
inferred← citeshttps://doi.org/10.1016/j.molcel.2018.12.022openalex-snapshot
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
inferred← citeshttps://doi.org/10.1016/j.molcel.2020.08.002openalex-snapshot
Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis
inferred← citeshttps://doi.org/10.1016/j.molcel.2020.12.006openalex-snapshot
Defective ALC1 nucleosome remodeling confers PARPi sensitization and synthetic lethality with HRD
inferred← citeshttps://doi.org/10.1016/j.molcel.2020.12.010openalex-snapshot
CARM1 regulates replication fork speed and stress response by stimulating PARP1
inferred← citeshttps://doi.org/10.1016/j.molcel.2021.04.028openalex-snapshot
Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease
inferred← citeshttps://doi.org/10.1016/j.molcel.2022.02.021openalex-snapshot
The expanding universe of PARP1-mediated molecular and therapeutic mechanisms
inferred← citeshttps://doi.org/10.1016/j.molcel.2023.03.027openalex-snapshot
Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling
inferred← citeshttps://doi.org/10.1016/j.molcel.2023.04.009openalex-snapshot
PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
inferred← citeshttps://doi.org/10.1016/j.molcel.2023.12.019openalex-snapshot
Poly(ADP-ribosyl)ation enhances nucleosome dynamics and organizes DNA damage repair components within biomolecular condensates
inferred← citeshttps://doi.org/10.1016/j.molcel.2024.09.020openalex-snapshot
Inactive Parp2 causes Tp53-dependent lethal anemia by blocking replication-associated nick ligation in erythroblasts
inferred← citeshttps://doi.org/10.1016/j.molcel.2024.10.024openalex-snapshot
PARP enzyme de novo synthesis of protein-free poly(ADP-ribose)
inferred← citeshttps://doi.org/10.1016/j.molcel.2025.01.004openalex-snapshot
A PARP2 active site helix melts to permit DNA damage-induced enzymatic activation
inferred← citeshttps://doi.org/10.1016/j.molcel.2025.09.006openalex-snapshot
PARP1 auto-modification promotes faithful Okazaki fragment processing and limits replication fork speed
inferred← citeshttps://doi.org/10.1016/j.molcel.2026.05.008openalex-snapshot
Deacetylated PCBP1 licenses PARP1 activity for DNA damage repair
inferred← citeshttps://doi.org/10.1016/j.molcel.2026.09.004openalex-snapshot
Ubiquitin chain editing promotes p97/VCP-dependent removal of RPA from DNA
inferred← citeshttps://doi.org/10.1016/j.molmed.2021.04.010openalex-snapshot
Studying PAR-Dependent Chromatin Remodeling to Tackle PARPi Resistance
inferred← citeshttps://doi.org/10.1016/j.molmet.2020.01.014openalex-snapshot
The taming of PARP1 and its impact on NAD+ metabolism
inferred← citeshttps://doi.org/10.1016/j.neo.2024.101092openalex-snapshot
Suppression of ADP-ribosylation reversal triggers cell vulnerability to alkylating agents
inferred← citeshttps://doi.org/10.1016/j.pbiomolbio.2020.09.010openalex-snapshot
Uncovering DNA-PKcs ancient phylogeny, unique sequence motifs and insights for human disease
inferred← citeshttps://doi.org/10.1016/j.pbiomolbio.2021.01.004openalex-snapshot
DNA replication stress and emerging prospects for PARG inhibitors in ovarian cancer therapy
inferred← citeshttps://doi.org/10.1016/j.pharmthera.2021.107968openalex-snapshot
PARkinson's: From cellular mechanisms to potential therapeutics
inferred← citeshttps://doi.org/10.1016/j.plipres.2021.101117openalex-snapshot
PARPs in lipid metabolism and related diseases
inferred← citeshttps://doi.org/10.1016/j.sbi.2018.11.002openalex-snapshot
PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification
inferred← citeshttps://doi.org/10.1016/j.sbi.2023.102643openalex-snapshot
PARP–nucleic acid interactions: Allosteric signaling, PARP inhibitor types, DNA bridges, and viral RNA surveillance
inferred← citeshttps://doi.org/10.1016/j.semcdb.2016.09.014openalex-snapshot
PARP, transcription and chromatin modeling
inferred← citeshttps://doi.org/10.1016/j.semcdb.2020.09.003openalex-snapshot
DNA double-strand break repair: Putting zinc fingers on the sore spot
inferred← citeshttps://doi.org/10.1016/j.slasd.2023.10.003openalex-snapshot
HTS discovery of PARP1-HPF1 complex inhibitors in cancer
inferred← citeshttps://doi.org/10.1016/j.tcb.2020.02.002openalex-snapshot
Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation
inferred← citeshttps://doi.org/10.1016/j.tcb.2022.04.010openalex-snapshot
DNA single-strand break repair and human genetic disease
inferred← citeshttps://doi.org/10.1016/j.tibs.2021.01.014openalex-snapshot
Rapid Detection and Signaling of DNA Damage by PARP-1
inferred← citeshttps://doi.org/10.1016/j.ydbio.2017.03.029openalex-snapshot
Membrane-bound organelles versus membrane-less compartments and their control of anabolic pathways in Drosophila
inferred← citeshttps://doi.org/10.1017/erm.2021.26openalex-snapshot
Opportunities and challenges in targeted therapy and immunotherapy for pancreatic cancer
inferred← citeshttps://doi.org/10.1017/erm.2024.14openalex-snapshot
Specific and shared biological functions of PARP2 – is PARP2 really a lil’ brother of PARP1?
inferred← citeshttps://doi.org/10.1021/acs.biochem.3c00243openalex-snapshot
Slow Dissociation from the PARP1–HPF1 Complex Drives Inhibitor Potency
inferred← citeshttps://doi.org/10.1021/acs.chemrev.2c00851openalex-snapshot
Regulation of Biomolecular Condensates by Poly(ADP-ribose)
inferred← citeshttps://doi.org/10.1021/acs.chemrev.7b00122openalex-snapshot
ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
inferred← citeshttps://doi.org/10.1021/acs.jproteome.4c00890openalex-snapshot
dELTA-MS: A Mass Spectrometry-Based Proteomics Approach for Identifying ADP-Ribosylation Sites and Forms
inferred← citeshttps://doi.org/10.1021/acs.orglett.8b01742openalex-snapshot
Synthetic α- and β-Ser-ADP-ribosylated Peptides Reveal α-Ser-ADPr as the Native Epimer
inferred← citeshttps://doi.org/10.1021/acschembio.2c00091openalex-snapshot
A Protein Semisynthesis-Based Strategy to Investigate the Functional Impact of Linker Histone Serine ADP-Ribosylation
inferred← citeshttps://doi.org/10.1021/acschembio.6c00475openalex-snapshot
Linker Histone H1 Phosphorylation Promotes DNA Damage Repair during Replication Stress
inferred← citeshttps://doi.org/10.1021/acschembio.7b00445openalex-snapshot
Discovery of a Selective Allosteric Inhibitor Targeting Macrodomain 2 of Polyadenosine-Diphosphate-Ribose Polymerase 14
inferred← citeshttps://doi.org/10.1021/jacs.3c03771openalex-snapshot
Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation
inferred← citeshttps://doi.org/10.1038/nchembio.2568openalex-snapshot
Insights into the biogenesis, function, and regulation of ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/onc.2017.60openalex-snapshot
New factors in mammalian DNA repair—the chromatin connection
inferred← citeshttps://doi.org/10.1038/s41388-022-02384-wopenalex-snapshot
A synthetic lethal strategy using PARP and ATM inhibition for overcoming trastuzumab resistance in HER2-positive cancers
inferred← citeshttps://doi.org/10.1038/s41419-024-07009-6openalex-snapshot
PINX1 loss confers susceptibility to PARP inhibition in pan-cancer cells
inferred← citeshttps://doi.org/10.1038/s41467-019-08859-xopenalex-snapshot
Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/s41467-019-13167-5openalex-snapshot
Barrier-to-autointegration factor 1 (Banf1) regulates poly [ADP-ribose] polymerase 1 (PARP1) activity following oxidative DNA damage
inferred← citeshttps://doi.org/10.1038/s41467-020-14620-6openalex-snapshot
Genetic screens in isogenic mammalian cell lines without single cell cloning
inferred← citeshttps://doi.org/10.1038/s41467-020-15858-wopenalex-snapshot
Real-time monitoring of PARP1-dependent PARylation by ATR-FTIR spectroscopy
inferred← citeshttps://doi.org/10.1038/s41467-021-20998-8openalex-snapshot
Histone Parylation factor 1 contributes to the inhibition of PARP1 by cancer drugs
inferred← citeshttps://doi.org/10.1038/s41467-021-21302-4openalex-snapshot
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones
inferred← citeshttps://doi.org/10.1038/s41467-021-23800-xopenalex-snapshot
Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition
inferred← citeshttps://doi.org/10.1038/s41467-021-24361-9openalex-snapshot
Serine-linked PARP1 auto-modification controls PARP inhibitor response
inferred← citeshttps://doi.org/10.1038/s41467-021-24723-3openalex-snapshot
Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
inferred← citeshttps://doi.org/10.1038/s41467-021-26172-4openalex-snapshot
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
inferred← citeshttps://doi.org/10.1038/s41467-021-26691-0openalex-snapshot
Zinc finger protein ZNF384 is an adaptor of Ku to DNA during classical non-homologous end-joining
inferred← citeshttps://doi.org/10.1038/s41467-021-27043-8openalex-snapshot
HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications
inferred← citeshttps://doi.org/10.1038/s41467-021-27867-4openalex-snapshot
Linking DNA repair and cell cycle progression through serine ADP-ribosylation of histones
inferred← citeshttps://doi.org/10.1038/s41467-022-30785-8openalex-snapshot
Cis- and trans-resveratrol have opposite effects on histone serine-ADP-ribosylation and tyrosine induced neurodegeneration
inferred← citeshttps://doi.org/10.1038/s41467-022-33731-wopenalex-snapshot
Mammalian N1-adenosine PARylation is a reversible DNA modification
inferred← citeshttps://doi.org/10.1038/s41467-023-38793-yopenalex-snapshot
Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
inferred← citeshttps://doi.org/10.1038/s41467-023-44209-8openalex-snapshot
Covalent PARylation of DNA base excision repair proteins regulates DNA demethylation
inferred← citeshttps://doi.org/10.1038/s41467-024-45237-8openalex-snapshot
Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1
inferred← citeshttps://doi.org/10.1038/s41467-024-48314-0openalex-snapshot
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
inferred← citeshttps://doi.org/10.1038/s41467-024-50158-7openalex-snapshot
PARG is essential for Polθ-mediated DNA end-joining by removing repressive poly-ADP-ribose marks
inferred← citeshttps://doi.org/10.1038/s41467-024-50912-xopenalex-snapshot
PARP1-dependent DNA-protein crosslink repair
inferred← citeshttps://doi.org/10.1038/s41467-025-56085-5openalex-snapshot
CHD6 has poly(ADP-ribose)- and DNA-binding domains and regulates PARP1/2-trapping inhibitor sensitivity via abasic site repair
inferred← citeshttps://doi.org/10.1038/s41467-025-58309-0openalex-snapshot
FTO suppresses DNA repair by inhibiting PARP1
inferred← citeshttps://doi.org/10.1038/s41467-025-61834-7openalex-snapshot
Single nucleosome imaging reveals principles of transient multiscale chromatin reorganization triggered by histone ADP-ribosylation at DNA lesions
inferred← citeshttps://doi.org/10.1038/s41467-026-71311-4openalex-snapshot
Versatile and sensitive detection of mono- and poly(ADP-ribosyl)ation reveals XRCC1-dependent remodelling of PARP1 signalling
inferred← citeshttps://doi.org/10.1038/s41467-026-73677-xopenalex-snapshot
Deciphering cytokine-driven ADP-ribosylation signaling networks via Af1521-based mass spectrometry analysis of labile Glu/Asp-linkages
inferred← citeshttps://doi.org/10.1038/s41556-021-00792-wopenalex-snapshot
XRCC1 protects transcription from toxic PARP1 activity during DNA base excision repair
inferred← citeshttps://doi.org/10.1038/s41556-021-00807-6openalex-snapshot
The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin
inferred← citeshttps://doi.org/10.1038/s41573-020-0076-6openalex-snapshot
Poly(ADP-ribose) polymerase inhibition: past, present and future
inferred← citeshttps://doi.org/10.1038/s41580-018-0029-7openalex-snapshot
Regulation of chromatin and gene expression by metabolic enzymes and metabolites
inferred← citeshttps://doi.org/10.1038/s41580-021-00394-2openalex-snapshot
Cellular functions of the protein kinase ATM and their relevance to human disease
inferred← citeshttps://doi.org/10.1038/s41586-020-2013-6openalex-snapshot
HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/s41586-020-2725-7openalex-snapshot
Bridging of DNA breaks activates PARP2–HPF1 to modify chromatin
inferred← citeshttps://doi.org/10.1038/s41586-025-09414-zopenalex-snapshot
NASP modulates histone turnover to drive PARP inhibitor resistance
inferred← citeshttps://doi.org/10.1038/s41589-018-0097-1openalex-snapshot
Acetylation blocks DNA damage–induced chromatin ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/s41589-025-01974-5openalex-snapshot
Serine ADPr on histones and PARP1 is a cellular target of ester-linked ubiquitylation
inferred← citeshttps://doi.org/10.1038/s41589-025-02045-5openalex-snapshot
Stabilization of AFF1 by PARylation ensures transcriptional restart after DNA damage
inferred← citeshttps://doi.org/10.1038/s41594-020-0412-xopenalex-snapshot
Tickling PARPs into serine action
inferred← citeshttps://doi.org/10.1038/s41594-023-00977-xopenalex-snapshot
HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation to promote the recruitment of repair factors at sites of DNA damage
inferred← citeshttps://doi.org/10.1038/s41594-023-00987-9openalex-snapshot
PARP1 and HPF1 team up to flag down DNA-repair machinery
inferred← citeshttps://doi.org/10.1038/s41594-024-01279-6openalex-snapshot
Deregulated DNA ADP-ribosylation impairs telomere replication
inferred← citeshttps://doi.org/10.1038/s41594-025-01715-1openalex-snapshot
Filament formation and NAD processing by noncanonical human FAM118 sirtuins
inferred← citeshttps://doi.org/10.1038/s41598-021-01665-wopenalex-snapshot
Role of FRG1 in predicting the overall survivability in cancers using multivariate based optimal model
inferred← citeshttps://doi.org/10.1038/s41598-024-70368-9openalex-snapshot
Unveiling FRG1’s DNA repair role in breast cancer
inferred← citeshttps://doi.org/10.1038/s42003-021-02770-2openalex-snapshot
Sirtuin inhibition is synthetic lethal with BRCA1 or BRCA2 deficiency
inferred← citeshttps://doi.org/10.1038/s42003-021-02780-0openalex-snapshot
Dual function of HPF1 in the modulation of PARP1 and PARP2 activities
inferred← citeshttps://doi.org/10.1042/bcj20210280openalex-snapshot
Beyond protein modification: the rise of non-canonical ADP-ribosylation
inferred← citeshttps://doi.org/10.1042/bsr20240986openalex-snapshot
Interferon-induced ADP-ribosylation: technical developments driving ICAB discovery
inferred← citeshttps://doi.org/10.1042/bst20180416openalex-snapshot
ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes
inferred← citeshttps://doi.org/10.1042/bst20180418openalex-snapshot
PARPs in genome stability and signal transduction: implications for cancer therapy
inferred← citeshttps://doi.org/10.1042/bst20220366openalex-snapshot
Revisiting PARP2 and PARP1 trapping through quantitative live-cell imaging
inferred← citeshttps://doi.org/10.1042/bst20220749openalex-snapshot
The function and regulation of ADP-ribosylation in the DNA damage response
inferred← citeshttps://doi.org/10.1053/j.seminoncol.2023.08.001openalex-snapshot
PARP1 roles in DNA repair and DNA replication: The basi(c)s of PARP inhibitor efficacy and resistance
inferred← citeshttps://doi.org/10.1073/pnas.2003613117openalex-snapshot
Live-cell protein engineering with an ultra-short split intein
inferred← citeshttps://doi.org/10.1073/pnas.2019408118openalex-snapshot
Zinc finger protein E4F1 cooperates with PARP-1 and BRG1 to promote DNA double-strand break repair
inferred← citeshttps://doi.org/10.1073/pnas.2121979119openalex-snapshot
Inhibitors of PARP: Number crunching and structure gazing
inferred← citeshttps://doi.org/10.1073/pnas.2322689121openalex-snapshot
Histone ADP-ribosylation promotes resistance to PARP inhibitors by facilitating PARP1 release from DNA lesions
inferred← citeshttps://doi.org/10.1080/10409238.2017.1394265openalex-snapshot
Specificity of reversible ADP-ribosylation and regulation of cellular processes
inferred← citeshttps://doi.org/10.1080/10409238.2020.1818686openalex-snapshot
Mechanisms governing PARP expression, localization, and activity in cells
inferred← citeshttps://doi.org/10.1080/13543776.2026.2722028openalex-snapshot
Selective PARP1 inhibitors (2021–2025): patent landscape, structural evolution, and future therapeutic opportunities
inferred← citeshttps://doi.org/10.1093/mutage/gez045openalex-snapshot
Mechanistic insight into the role of Poly(ADP-ribosyl)ation in DNA topology modulation and response to DNA damage
inferred← citeshttps://doi.org/10.1093/nar/gkab269openalex-snapshot
HPF1-dependent PARP activation promotes LIG3-XRCC1-mediated backup pathway of Okazaki fragment ligation
inferred← citeshttps://doi.org/10.1093/nar/gkab618openalex-snapshot
Why structure and chain length matter: on the biological significance underlying the structural heterogeneity of poly(ADP-ribose)
inferred← citeshttps://doi.org/10.1093/nar/gkab771openalex-snapshot
TARG1 protects against toxic DNA ADP-ribosylation
inferred← citeshttps://doi.org/10.1093/nar/gkac711openalex-snapshot
ADP-ribosylation of RNA in mammalian cells is mediated by TRPT1 and multiple PARPs
inferred← citeshttps://doi.org/10.1093/nar/gkac948openalex-snapshot
PARP1 proximity proteomics reveals interaction partners at stressed replication forks
inferred← citeshttps://doi.org/10.1093/nar/gkad1119openalex-snapshot
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids
inferred← citeshttps://doi.org/10.1093/nar/gkad514openalex-snapshot
Updated protein domain annotation of the PARP protein family sheds new light on biological function
inferred← citeshttps://doi.org/10.1093/nar/gkad515openalex-snapshot
The CSB chromatin remodeler regulates PARP1- and PARP2-mediated single-strand break repair at actively transcribed DNA regions
inferred← citeshttps://doi.org/10.1093/nar/gkae211openalex-snapshot
APLF facilitates interstrand DNA crosslink repair and replication fork protection to confer cisplatin resistance
inferred← citeshttps://doi.org/10.1093/nar/gkae439openalex-snapshot
The loss of DNA polymerase epsilon accessory subunits POLE3–POLE4 leads to BRCA1-independent PARP inhibitor sensitivity
inferred← citeshttps://doi.org/10.1093/nar/gkae708openalex-snapshot
Dispensability of HPF1 for cellular removal of DNA single-strand breaks
inferred← citeshttps://doi.org/10.1093/nar/gkae756openalex-snapshot
PARP1-TRIM44-MRN loop dictates the response to PARP inhibitors
inferred← citeshttps://doi.org/10.1093/nar/gkaf1170openalex-snapshot
Histone PARylation factor 1: a review of its role in the DNA damage response
inferred← citeshttps://doi.org/10.1093/nar/gkaf864openalex-snapshot
Deciphering the dark side of histone ADP-ribosylation: what structural features of damaged nucleosome regulate the activities of PARP1 and PARP2
inferred← citeshttps://doi.org/10.1093/nar/gkag183openalex-snapshot
HPF1 regulates the formation of FUS-dependent compartments by PARP1 and PARP2 activation on damaged DNA
inferred← citeshttps://doi.org/10.1093/nar/gkag860openalex-snapshot
Navigating the base excision repair pathway in chromatin—focus on oxidative DNA damage
inferred← citeshttps://doi.org/10.1093/nar/gkag939openalex-snapshot
Structural basis of PARP2 recognition of nucleosomal DNA breaks and inhibitor trapping
inferred← citeshttps://doi.org/10.1093/nar/gkw710openalex-snapshot
Fluorescent sensors of PARP-1 structural dynamics and allosteric regulation in response to DNA damage
inferred← citeshttps://doi.org/10.1093/nar/gkw859openalex-snapshot
Analyzing structure–function relationships of artificial and cancer-associated PARP1 variants by reconstituting TALEN-generated HeLaPARP1knock-out cells
inferred← citeshttps://doi.org/10.1093/nar/gkz120openalex-snapshot
Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins
inferred← citeshttps://doi.org/10.1093/nar/gkz305openalex-snapshot
Reversible ADP-ribosylation of RNA
inferred← citeshttps://doi.org/10.1093/nar/gkz820openalex-snapshot
Poly(ADP-ribose)-dependent chromatin unfolding facilitates the association of DNA-binding proteins with DNA at sites of damage
inferred← citeshttps://doi.org/10.1093/narcan/zcad043openalex-snapshot
The dynamic process of covalent and non-covalent PARylation in the maintenance of genome integrity: a focus on PARP inhibitors
inferred← citeshttps://doi.org/10.1097/jp9.0000000000000160openalex-snapshot
Synergistic effects of resveratrol with gemcitabine in pancreatic cancer chemotherapy by inhibiting the c-Met/PARP1 axis
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