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The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/j.1460-2075.1993.tb05859.xopenalex-snapshot
Overproduction of the poly(ADP‐ribose) polymerase DNA‐binding domain blocks alkylation‐induced DNA repair synthesis in mammalian cells.
inferredcites →https://doi.org/10.1006/jmbi.1994.1057openalex-snapshot
Conformational Analysis of a 139 Base-pair DNA Fragment Containing a Single-stranded Break and Its Interaction with Human Poly(ADP-ribose) Polymerase
inferredcites →https://doi.org/10.1006/jmre.1998.1361openalex-snapshot
Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR Spectra
inferredcites →https://doi.org/10.1007/bf01496937openalex-snapshot
Determination of the partial specific volume of conjugated proteins
inferredcites →https://doi.org/10.1016/0003-2670(95)90401-8openalex-snapshot
Analytical ultracentrifugation in biochemistry and polymer science
inferredcites →https://doi.org/10.1016/0022-2836(89)90302-1openalex-snapshot
Zinc-binding domain of poly(ADP-ribose)polymerase participates in the recognition of single strand breaks on DNA
inferredcites →https://doi.org/10.1016/0092-8674(95)90541-3openalex-snapshot
Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
inferredcites →https://doi.org/10.1016/0968-0004(94)90280-1openalex-snapshot
Poly(ADP-ribose) polymerase: a molecular nick-sensor
inferredcites →https://doi.org/10.1016/j.bpc.2003.10.018openalex-snapshot
Fluorescence detection for the XLI analytical ultracentrifuge
inferredcites →https://doi.org/10.1016/j.bpj.2010.08.036openalex-snapshot
NMR Studies on Domain Diffusion and Alignment in Modular GB1 Repeats
inferredcites →https://doi.org/10.1016/j.cell.2004.11.002openalex-snapshot
NAD+-Dependent Modulation of Chromatin Structure and Transcription by Nucleosome Binding Properties of PARP-1
inferredcites →https://doi.org/10.1016/j.dnarep.2006.10.006openalex-snapshot
Mammalian single-strand break repair: Mechanisms and links with chromatin
inferredcites →https://doi.org/10.1016/j.dnarep.2008.03.009openalex-snapshot
Poly ADP-ribose polymerase-1: An international molecule of mystery
inferredcites →https://doi.org/10.1016/j.jmb.2004.06.035openalex-snapshot
Solution Structure and DNA Binding of the Zinc-finger Domain from DNA Ligase IIIα
inferredcites →https://doi.org/10.1016/j.jmb.2004.06.071openalex-snapshot
Cooperative Binding of Tetrameric p53 to DNA
inferredcites →https://doi.org/10.1016/j.jmb.2005.03.010openalex-snapshot
Specific Binding of Poly(ADP-ribose) Polymerase-1 to Cruciform Hairpins
inferredcites →https://doi.org/10.1016/j.jmb.2009.11.062openalex-snapshot
Structural and Biophysical Studies of Human PARP-1 in Complex with Damaged DNA
inferredcites →https://doi.org/10.1016/j.molcel.2009.09.032openalex-snapshot
A Nuclear Poly(ADP-Ribose)-Dependent Signalosome Confers DNA Damage-Induced IκB Kinase Activation
inferredcites →https://doi.org/10.1016/s0006-3495(00)76713-0openalex-snapshot
Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling
inferredcites →https://doi.org/10.1016/s0014-5793(96)01347-6openalex-snapshot
Mutations in the amino‐terminal domain of the human poly(ADP‐ribose) polymerase that affect its catalytic activity but not its DNA binding capacity
inferredcites →https://doi.org/10.1016/s0021-9258(17)43816-6openalex-snapshot
ADP-ribosylation of chromosomal proteins and mouse mammary tumor virus gene expression. Glucocorticoids rapidly decrease endogenous ADP-ribosylation of nonhistone high mobility group 14 and 17 proteins.
inferredcites →https://doi.org/10.1016/s0021-9258(18)41568-2openalex-snapshot
Poly(ADP-ribose) polymerase is a catalytic dimer and the automodification reaction is intermolecular.
inferredcites →https://doi.org/10.1016/s0021-9258(18)45824-3openalex-snapshot
The zinc fingers of human poly(ADP-ribose) polymerase are differentially required for the recognition of DNA breaks and nicks and the consequent enzyme activation. Other structures recognize intact DNA.
inferredcites →https://doi.org/10.1016/s0021-9258(18)68594-1openalex-snapshot
Immunoquantitation and size determination of intrinsic poly(ADP-ribose) polymerase from acid precipitates. An analysis of the in vivo status in mammalian species and in lower eukaryotes.
inferredcites →https://doi.org/10.1016/s0021-9258(19)70491-8openalex-snapshot
Poly(ADP-ribose) synthesis in vitro programmed by damaged DNA. A comparison of DNA molecules containing different types of strand breaks.
inferredcites →https://doi.org/10.1016/s0301-472x(03)00083-3openalex-snapshot
PARP-1, a determinant of cell survival in response to DNA damage
inferredcites →https://doi.org/10.1016/s0960-9822(98)70032-6openalex-snapshot
DNA repair: PARP – another guardian angel?
inferredcites →https://doi.org/10.1016/s1090-7807(02)00014-9openalex-snapshot
The Xplor-NIH NMR molecular structure determination package
inferredcites →https://doi.org/10.1021/bi00431a011openalex-snapshot
ADP-ribosylation of ADPR-transferase and topoisomerase I in intact mouse epidermal cells JB6
inferredcites →https://doi.org/10.1021/bi0301800openalex-snapshot
Analysis of Nucleotide Sequence-Dependent DNA Binding of Poly(ADP-ribose) Polymerase in a Purified System
inferredcites →https://doi.org/10.1021/bi0344432openalex-snapshot
Poly(ADP-ribose) Polymerase-1 Dimerizes at a 5‘ Recessed DNA End in Vitro: A Fluorescence Study
inferredcites →https://doi.org/10.1021/bi800018aopenalex-snapshot
Domain C of Human Poly(ADP-ribose) Polymerase-1 Is Important for Enzyme Activity and Contains a Novel Zinc-Ribbon Motif,
inferredcites →https://doi.org/10.1021/ja016234fopenalex-snapshot
Rapid Identification of Medium- to Large-Scale Interdomain Motion in Modular Proteins Using Dipolar Couplings
inferredcites →https://doi.org/10.1023/a:1011206132740openalex-snapshot
A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings
inferredcites →https://doi.org/10.1023/a:1012998006281openalex-snapshot
An easy way to include weak alignment constraints into NMR structure calculations
inferredcites →https://doi.org/10.1023/a:1014929925008openalex-snapshot
Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water
inferredcites →https://doi.org/10.1023/a:1021614115432openalex-snapshot
Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
inferredcites →https://doi.org/10.1038/283593a0openalex-snapshot
(ADP-ribose)n participates in DNA excision repair
inferredcites →https://doi.org/10.1038/371346a0openalex-snapshot
Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
inferredcites →https://doi.org/10.1038/376037a0openalex-snapshot
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
inferredcites →https://doi.org/10.1038/emboj.2009.206openalex-snapshot
PARP is activated at stalled forks to mediate Mre11‐dependent replication restart and recombination
inferredcites →https://doi.org/10.1038/ncb1638openalex-snapshot
Inhibition of Crm1–p53 interaction and nuclear export of p53 by poly(ADP-ribosyl)ation
inferredcites →https://doi.org/10.1038/nrm1963openalex-snapshot
Poly(ADP-ribose): novel functions for an old molecule
inferredcites →https://doi.org/10.1038/nsmb.1747openalex-snapshot
Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)
inferredcites →https://doi.org/10.1038/sj.onc.1210434openalex-snapshot
Poly-(ADP-ribose) polymerase-1 (Parp-1) binds in a sequence-specific manner at the Bcl-6 locus and contributes to the regulation of Bcl-6 transcription
inferredcites →https://doi.org/10.1042/0264-6021:3420249openalex-snapshot
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
inferredcites →https://doi.org/10.1042/bj3420249openalex-snapshot
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
inferredcites →https://doi.org/10.1073/pnas.1009182107openalex-snapshot
Apurinic/apyrimidinic (AP) site recognition by the 5′-dRP/AP lyase in poly(ADP-ribose) polymerase-1 (PARP-1)
inferredcites →https://doi.org/10.1073/pnas.79.11.3423openalex-snapshot
Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure.
inferredcites →https://doi.org/10.1073/pnas.85.1.99openalex-snapshot
Proposed structure for the zinc-binding domains from transcription factor IIIA and related proteins.
inferredcites →https://doi.org/10.1073/pnas.87.8.2990openalex-snapshot
The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.
inferredcites →https://doi.org/10.1074/jbc.274.31.21679openalex-snapshot
DNA Ligase III Is Recruited to DNA Strand Breaks by a Zinc Finger Motif Homologous to That of Poly(ADP-ribose) Polymerase
inferredcites →https://doi.org/10.1074/jbc.m110.105668openalex-snapshot
The Zn3 Domain of Human Poly(ADP-ribose) Polymerase-1 (PARP-1) Functions in Both DNA-dependent Poly(ADP-ribose) Synthesis Activity and Chromatin Compaction
inferredcites →https://doi.org/10.1074/jbc.m201411200openalex-snapshot
A Nick-sensing DNA 3′-Repair Enzyme fromArabidopsis
inferredcites →https://doi.org/10.1074/jbc.m202390200openalex-snapshot
Poly(ADP-ribose) Polymerase-2 (PARP-2) Is Required for Efficient Base Excision DNA Repair in Association with PARP-1 and XRCC1
inferredcites →https://doi.org/10.1074/jbc.m413483200openalex-snapshot
Regulation of Poly(ADP-ribose) Polymerase-1 by DNA Structure-specific Binding
inferredcites →https://doi.org/10.1074/jbc.m708558200openalex-snapshot
A Third Zinc-binding Domain of Human Poly(ADP-ribose) Polymerase-1 Coordinates DNA-dependent Enzyme Activation
inferredcites →https://doi.org/10.1093/nar/gkp229openalex-snapshot
Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
inferredcites →https://doi.org/10.1093/nar/gnh103openalex-snapshot
Protein-DNA footprinting by endcapped duplex oligodeoxyribonucleotides
inferredcites →https://doi.org/10.1101/gad.1331805openalex-snapshot
Poly(ADP-ribosyl)ation by PARP-1: `PAR-laying' NAD + into a nuclear signal
inferredcites →https://doi.org/10.1107/s0907444994010723openalex-snapshot
Coordinate-based cluster analysis
inferredcites →https://doi.org/10.1111/j.1432-1033.1987.tb13621.xopenalex-snapshot
Poly(ADP-ribose) synthase is the major endogenous nonhistone acceptor for poly(ADP-ribose) in alkylated rat hepatoma cells
inferredcites →https://doi.org/10.1111/j.1742-4658.2008.06259.xopenalex-snapshot
Structural recognition of DNA by poly(ADP‐ribose)polymerase‐like zinc finger families
inferredcites →https://doi.org/10.1242/jcs.114.20.3771openalex-snapshot
Gain-of-function of poly(ADP-ribose) polymerase-1 upon cleavage by apoptotic proteases: implications for apoptosis
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/9781118876992.ch13openalex-snapshot
Arsenic Interaction with Zinc Finger Motifs
inferred← citeshttps://doi.org/10.1002/cbin.70186openalex-snapshot
The Landscape of BRCA1‐Associated Post‐Translational Modifications
inferred← citeshttps://doi.org/10.1002/cmdc.201500391openalex-snapshot
Concepts and Molecular Aspects in the Polypharmacology of PARP‐1 Inhibitors
inferred← citeshttps://doi.org/10.1002/ejoc.201601596openalex-snapshot
Molecular Tweezers Inhibit PARP‐1 by a New Mechanism
inferred← citeshttps://doi.org/10.1002/mgg3.556openalex-snapshot
Interaction of germline variants in a family with a history of early‐onset clear cell renal cell carcinoma
inferred← citeshttps://doi.org/10.1007/978-3-030-00853-6_4openalex-snapshot
Probing Cells: Evaluating Cytotoxicity
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Functional Biochemistry of Trace Elements in Cancer: Mechanisms, Biomarkers, and Therapeutic Potentials
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Targeted Cancer Therapy: KRAS-Specific Treatments for Pancreatic Cancer
inferred← citeshttps://doi.org/10.1007/978-981-19-9776-1_69openalex-snapshot
Targeted Cancer Therapy: KRAS-Specific Treatments for Pancreatic Cancer
inferred← citeshttps://doi.org/10.1007/s00204-016-1771-2openalex-snapshot
Single nucleotide polymorphisms in DNA repair genes and putative cancer risk
inferred← citeshttps://doi.org/10.1007/s00412-013-0442-9openalex-snapshot
Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response
inferred← citeshttps://doi.org/10.1007/s00775-026-02134-3openalex-snapshot
The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide
inferred← citeshttps://doi.org/10.1007/s10555-020-09887-6openalex-snapshot
Wnts and the hallmarks of cancer
inferred← citeshttps://doi.org/10.1007/s10858-012-9625-6openalex-snapshot
A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins
inferred← citeshttps://doi.org/10.1007/s11427-024-2817-yopenalex-snapshot
SLC39A10 is a key zinc transporter in T cells and its loss mitigates autoimmune disease
inferred← citeshttps://doi.org/10.1007/s12041-011-0074-xopenalex-snapshot
Differential expression of PARP1 mRNA in leucocytes of patients with Down’s syndrome
inferred← citeshttps://doi.org/10.1007/s13205-021-03038-6openalex-snapshot
Pleiotropic role of PARP1: an overview
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.arr.2023.102078openalex-snapshot
Poly (ADP-ribose) polymerase 1 and neurodegenerative diseases: Past, present, and future
inferred← citeshttps://doi.org/10.1016/j.bbapap.2014.07.012openalex-snapshot
Investigating the allosteric reverse signalling of PARP inhibitors with microsecond molecular dynamic simulations and fluorescence anisotropy
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.bbrc.2017.05.037openalex-snapshot
NF90 regulates PARP1 mRNA stability in hepatocellular carcinoma
inferred← citeshttps://doi.org/10.1016/j.biochi.2021.07.006openalex-snapshot
Apurinic/Apyrimidinic Endonuclease 2 (APE2): An ancillary enzyme for contextual base excision repair mechanisms to preserve genome stability
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Therapeutic approach for triple-negative breast Cancer through poly (ADP-ribose) Polymerase-1 inhibitors: Current update
inferred← citeshttps://doi.org/10.1016/j.bioorg.2025.108761openalex-snapshot
From bench to bedside: Synthetic strategies and clinical application of PARP inhibitors
inferred← citeshttps://doi.org/10.1016/j.bioorg.2025.109442openalex-snapshot
Unraveling the metabolic potential of Moringa oleifera derived metabolites in combating Parkinson's and Alzheimer's disease
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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.clon.2019.02.007openalex-snapshot
DNA Repair: Translation to the Clinic
inferred← citeshttps://doi.org/10.1016/j.cmet.2022.03.010openalex-snapshot
SREBP1c-PARP1 axis tunes anti-senescence activity of adipocytes and ameliorates metabolic imbalance in obesity
inferred← citeshttps://doi.org/10.1016/j.ddmod.2012.01.004openalex-snapshot
Poly(ADP-ribose) polymerase (PARP) and PARP inhibitors
inferred← citeshttps://doi.org/10.1016/j.diff.2016.03.002openalex-snapshot
Poly (ADP-ribose) polymerase1 regulates growth and multicellularity in D. discoideum
inferred← citeshttps://doi.org/10.1016/j.dnarep.2013.04.004openalex-snapshot
PARP-mediated repair, homologous recombination, and back-up non-homologous end joining-like repair of single-strand nicks
inferred← citeshttps://doi.org/10.1016/j.dnarep.2013.07.001openalex-snapshot
DNA-dependent SUMO modification of PARP-1
inferred← citeshttps://doi.org/10.1016/j.dnarep.2015.04.008openalex-snapshot
The rise and fall of poly(ADP-ribose): An enzymatic perspective
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.2025.103887openalex-snapshot
DNA damage response inhibitors in cancer therapy: Mechanisms, clinical development, and combination strategies
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2016.11.039openalex-snapshot
Coordination of DNA single strand break repair
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2019.10.010openalex-snapshot
Additional functions of selected proteins involved in DNA repair
inferred← citeshttps://doi.org/10.1016/j.jbc.2025.108532openalex-snapshot
DNA stimulates the deacetylase SIRT6 to mono-ADP-ribosylate proteins with histidine repeats
inferred← citeshttps://doi.org/10.1016/j.jmb.2019.05.028openalex-snapshot
A Single-Molecule Atomic Force Microscopy Study of PARP1 and PARP2 Recognition of Base Excision Repair DNA Intermediates
inferred← citeshttps://doi.org/10.1016/j.jmb.2019.12.019openalex-snapshot
Role of PARP-catalyzed ADP-ribosylation in the Crosstalk Between DNA Strand Breaks and Epigenetic Regulation
inferred← citeshttps://doi.org/10.1016/j.mam.2013.02.002openalex-snapshot
Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.10.013openalex-snapshot
PARP-1 Activation Requires Local Unfolding of an Autoinhibitory Domain
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.10.032openalex-snapshot
Structural Basis of Detection and Signaling of DNA Single-Strand Breaks by Human PARP-1
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.2024.10.024openalex-snapshot
PARP enzyme de novo synthesis of protein-free poly(ADP-ribose)
inferred← citeshttps://doi.org/10.1016/j.mrfmmm.2013.07.001openalex-snapshot
Mitigation of gamma-radiation induced abasic sites in genomic DNA by dietary nicotinamide supplementation: Metabolic up-regulation of NAD+ biosynthesis
inferred← citeshttps://doi.org/10.1016/j.pharmthera.2024.108642openalex-snapshot
Cisplatin in the era of PARP inhibitors and immunotherapy
inferred← citeshttps://doi.org/10.1016/j.pnmrs.2022.07.001openalex-snapshot
Zinc finger structure determination by NMR: Why zinc fingers can be a handful
inferred← citeshttps://doi.org/10.1016/j.sbi.2012.08.005openalex-snapshot
Towards a structural understanding of PARP1 activation and related signalling ADP-ribosyl-transferases
inferred← citeshttps://doi.org/10.1016/j.sbi.2013.01.003openalex-snapshot
PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis
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
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Effects of Ochratoxin A exposure on DNA damage in porcine granulosa cells in vitro
inferred← citeshttps://doi.org/10.1016/j.trecan.2019.12.004openalex-snapshot
Therapeutic Application of PARP Inhibitors in Neuro-Oncology
inferred← citeshttps://doi.org/10.1016/j.yexcr.2014.07.003openalex-snapshot
Poly(ADP-ribose) polymerases in double-strand break repair: Focus on PARP1, PARP2 and PARP3
inferred← citeshttps://doi.org/10.1021/acs.biochem.9b00986openalex-snapshot
Nonspecific Binding of RNA to PARP1 and PARP2 Does Not Lead to Catalytic Activation
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.jpcb.4c07960openalex-snapshot
Impact of a Cancer-Associated Mutation on Poly(ADP-ribose) Polymerase1 Inhibition
inferred← citeshttps://doi.org/10.1021/acschembio.5c00022openalex-snapshot
Disrupting the Base Excision Repair (BER) Pathway by Targeting the Abasic Site Enhances the Sensitivity of PARP Inhibitor in HR-Proficient Cancer Cells
inferred← citeshttps://doi.org/10.1021/bi401439nopenalex-snapshot
Conformational Activation of Poly(ADP-ribose) Polymerase-1 upon DNA Binding Revealed by Small-Angle X-ray Scattering
inferred← citeshttps://doi.org/10.1021/tx300437xopenalex-snapshot
Synthesis and Characterization of DNA Minor Groove Binding Alkylating Agents
inferred← citeshttps://doi.org/10.1021/tx500320fopenalex-snapshot
Unusual Zn(II) Affinities of Zinc Fingers of Poly(ADP-ribose) Polymerase 1 (PARP-1) Nuclear Protein
inferred← citeshttps://doi.org/10.1038/nrm3376openalex-snapshot
New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
inferred← citeshttps://doi.org/10.1038/nsmb.2335openalex-snapshot
The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks
inferred← citeshttps://doi.org/10.1038/nsmb.3105openalex-snapshot
Capturing snapshots of APE1 processing DNA damage
inferred← citeshttps://doi.org/10.1038/s12276-023-01139-1openalex-snapshot
Multifaceted roles of CCAR family proteins in the DNA damage response and cancer
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/s41467-021-26588-yopenalex-snapshot
SPINDOC binds PARP1 to facilitate PARylation
inferred← citeshttps://doi.org/10.1038/s41467-022-34148-1openalex-snapshot
Structural dynamics of DNA strand break sensing by PARP-1 at a single-molecule level
inferred← citeshttps://doi.org/10.1038/s41467-026-69375-3openalex-snapshot
PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/s41580-025-00897-2openalex-snapshot
The dynamic and heterogeneous composition of biomolecular condensates and its functional relevance
inferred← citeshttps://doi.org/10.1038/s41586-025-08749-xopenalex-snapshot
BRCA2 prevents PARPi-mediated PARP1 retention to protect RAD51 filaments
inferred← citeshttps://doi.org/10.1038/s41598-017-03751-4openalex-snapshot
Structural and Biochemical Characterization of Poly-ADP-ribose Polymerase from Trypanosoma brucei
inferred← citeshttps://doi.org/10.1038/s41598-024-58076-wopenalex-snapshot
Cooperative nucleic acid binding by Poly ADP-ribose polymerase 1
inferred← citeshttps://doi.org/10.1038/s44319-024-00285-5openalex-snapshot
PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation
inferred← citeshttps://doi.org/10.1039/c5ra19150eopenalex-snapshot
Novel PARP inhibitors sensitize human leukemic cells in an endogenous PARP activity dependent manner
inferred← citeshttps://doi.org/10.1039/d2ra02683jopenalex-snapshot
Deciphering the functional mechanism of zinc ions of PARP1 binding with single strand breaks and double strand breaks
inferred← citeshttps://doi.org/10.1042/bcj20230230openalex-snapshot
Regulation of PARP1/2 and the tankyrases: emerging parallels
inferred← citeshttps://doi.org/10.1073/pnas.1210899109openalex-snapshot
Superstructure of the centromeric complex of TubZR C plasmid partitioning systems
inferred← citeshttps://doi.org/10.1074/jbc.m112.397067openalex-snapshot
Alternative Modes of Binding of Poly(ADP-ribose) Polymerase 1 to Free DNA and Nucleosomes
inferred← citeshttps://doi.org/10.1074/jbc.m113.497974openalex-snapshot
The RNA-binding Protein Fused in Sarcoma (FUS) Functions Downstream of Poly(ADP-ribose) Polymerase (PARP) in Response to DNA Damage
inferred← citeshttps://doi.org/10.1074/jbc.m115.663906openalex-snapshot
Selective Sensitization of Zinc Finger Protein Oxidation by Reactive Oxygen Species through Arsenic Binding
inferred← citeshttps://doi.org/10.1074/jbc.ra120.013547openalex-snapshot
Lysines in the lyase active site of DNA polymerase β destabilize nonspecific DNA binding, facilitating searching and DNA gap recognition
inferred← citeshttps://doi.org/10.1080/07391102.2015.1068224openalex-snapshot
Zinc finger protein binding to DNA: an energy perspective using molecular dynamics simulation and free energy calculations on mutants of both zinc finger domains and their specific DNA bases
inferred← citeshttps://doi.org/10.1080/1354750x.2016.1204006openalex-snapshot
Base excision repair pathway:PARP1genotypes as modulators of therapy response in cervical cancer patients
inferred← citeshttps://doi.org/10.1084/jem.20191688openalex-snapshot
Loss of ZBTB24 impairs nonhomologous end-joining and class-switch recombination in patients with ICF syndrome
inferred← citeshttps://doi.org/10.1093/jrr/rraa023openalex-snapshot
Role of PARP1 regulation in radiation-induced rescue effect
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/gkab020openalex-snapshot
Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition
inferred← citeshttps://doi.org/10.1093/nar/gkab136openalex-snapshot
ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
inferred← citeshttps://doi.org/10.1093/nar/gkaf1090openalex-snapshot
Nuclear poly(A)-binding protein and nucleolin utilize their RNA recognition motifs to read PAR chains
inferred← citeshttps://doi.org/10.1093/nar/gkr1045openalex-snapshot
Fluorescence strategies for high-throughput quantification of protein interactions
inferred← citeshttps://doi.org/10.1093/nar/gkr1231openalex-snapshot
Visualization of a DNA-PK/PARP1 complex
inferred← citeshttps://doi.org/10.1093/nar/gku1307openalex-snapshot
DNA ligase III acts as a DNA strand break sensor in the cellular orchestration of DNA strand break repair
inferred← citeshttps://doi.org/10.1093/nar/gku174openalex-snapshot
PARP3 affects the relative contribution of homologous recombination and nonhomologous end-joining pathways
inferred← citeshttps://doi.org/10.1093/nar/gku288openalex-snapshot
Suicidal cross-linking of PARP-1 to AP site intermediates in cells undergoing base excision repair
inferred← citeshttps://doi.org/10.1093/nar/gku474openalex-snapshot
PARP-2 and PARP-3 are selectively activated by 5′ phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1
inferred← citeshttps://doi.org/10.1093/nar/gkv1467openalex-snapshot
DNA recognition for virus assembly through multiple sequence-independent interactions with a helix-turn-helix motif
inferred← citeshttps://doi.org/10.1093/nar/gkv250openalex-snapshot
Disruption of PARP1 function inhibits base excision repair of a sub-set of DNA lesions
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/gkx1047openalex-snapshot
PARP1 changes from three-dimensional DNA damage searching to one-dimensional diffusion after auto-PARylation or in the presence of APE1
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/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/10.1101/2023.12.15.571635openalex-snapshot
A Site-Specific Analysis of the ADP-Ribosylome Unveils Homogeneous DNA Damage-Induced Serine ADP-Ribosylation Across Wild-Type and BRCA-Mutant Breast Cancer Cell Lines
inferred← citeshttps://doi.org/10.1101/2024.06.11.598467openalex-snapshot
Poly (ADP-ribose) polymerase-1 regulates HIV-1 replication in human CD4+ T cells
inferred← citeshttps://doi.org/10.1101/2024.07.31.606047openalex-snapshot
DNA stimulates SIRT6 to mono-ADP-ribosylate proteins within histidine repeats
inferred← citeshttps://doi.org/10.1101/2025.03.10.642491openalex-snapshot
NF-κB-Driven HIV-1 Gene Expression in Human Cells Is Independent of Poly(ADP-Ribose) Polymerase-1 Function
inferred← citeshttps://doi.org/10.1101/2025.08.30.673248openalex-snapshot
PARP1 inhibitors regulate PARP1 structure independent of DNA, reducing binding affinity for single strand breaks
inferred← citeshttps://doi.org/10.1111/cpr.12268openalex-snapshot
The PARP family: insights into functional aspects of poly ( ADP ‐ribose) polymerase‐1 in cell growth and survival
inferred← citeshttps://doi.org/10.1111/febs.16875openalex-snapshot
Regulation of PARP1 and its apoptotic variant activity by single‐stranded DNA
inferred← citeshttps://doi.org/10.1111/jnc.16131openalex-snapshot
PARP1 in the intersection of different DNA repair pathways, memory formation, and sleep pressure in neurons
inferred← citeshttps://doi.org/10.1111/plb.12167openalex-snapshot
The nuclear protein Poly( ADP ‐ribose) polymerase 3 (At PARP 3) is required for seed storability in Arabidopsis thaliana
inferred← citeshttps://doi.org/10.1126/sciadv.abf3641openalex-snapshot
Single-molecule measurements reveal that PARP1 condenses DNA by loop stabilization
inferred← citeshttps://doi.org/10.1126/science.1216338openalex-snapshot
Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1
inferred← citeshttps://doi.org/10.1126/science.1221870openalex-snapshot
PARP-1 Activation—Bringing the Pieces Together
inferred← citeshttps://doi.org/10.1128/mmbr.00038-18openalex-snapshot
Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity
inferred← citeshttps://doi.org/10.1134/s0006297922140048openalex-snapshot
Role of YB-1 in Regulation of Poly(ADP-Ribosylation) Catalyzed by Poly(ADP-Ribose) Polymerases
inferred← citeshttps://doi.org/10.1134/s0022476625050038openalex-snapshot
Predicting the PARP1 Tertiary Structure by Molecular Modeling Methods
inferred← citeshttps://doi.org/10.1134/s0026893315010094openalex-snapshot
Molecular mechanisms of transcriptional regulation by Poly(ADP-ribose) polymerase 1
inferred← citeshttps://doi.org/10.1134/s0026893316040038openalex-snapshot
Poly(ADP-Ribose) polymerase 1 as a key regulator of DNA repair
inferred← citeshttps://doi.org/10.1134/s0026893323020140openalex-snapshot
Poly(ADP-Ribose) Polymerases 1 and 2: Classical Functions and Interaction with New Histone Poly(ADP-Ribosyl)ation Factor HPF1
inferred← citeshttps://doi.org/10.1134/s0026893323050114openalex-snapshot
The Role of the WGR Domain in the Functions of PARP1 and PARP2
inferred← citeshttps://doi.org/10.1155/2020/2717150openalex-snapshot
Poly (ADP-Ribose) Polymerase 1 Protein Expression in Normal Pancreas and Pancreatic Adenocarcinoma
inferred← citeshttps://doi.org/10.1155/2021/5515961openalex-snapshot
Antiprostate Cancer Activity of Ineupatolide Isolated from Carpesium cernuum L.
inferred← citeshttps://doi.org/10.1172/jci173757openalex-snapshot
FGFR3-induced Y158 PARP1 phosphorylation promotes PARP inhibitor resistance via BRG1/MRE11-mediated DNA repair in breast cancer models
inferred← citeshttps://doi.org/10.1177/1179554921996288openalex-snapshot
The Synergistic Effect of PARP Inhibitors and Immune Checkpoint Inhibitors
inferred← citeshttps://doi.org/10.1186/1472-6882-13-226openalex-snapshot
The antiproliferative effect of Moringa oleifera crude aqueous leaf extract on cancerous human alveolar epithelial cells
inferred← citeshttps://doi.org/10.1371/journal.pone.0240932openalex-snapshot
Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1
inferred← citeshttps://doi.org/10.1371/journal.pone.0290176openalex-snapshot
How ligands regulate the binding of PARP1 with DNA: Deciphering the mechanism at the molecular level
inferred← citeshttps://doi.org/10.18632/oncotarget.12613openalex-snapshot
S-nitrosation on zinc finger motif of PARP-1 as a mechanism of DNA repair inhibition by arsenite
inferred← citeshttps://doi.org/10.18632/oncotarget.1742openalex-snapshot
Minor grove binding ligands disrupt PARP-1 activation pathways
inferred← citeshttps://doi.org/10.2142/biophysico.16.0_59openalex-snapshot
Single-particle analysis of full-length human poly(ADP-ribose) polymerase 1
inferred← citeshttps://doi.org/10.2217/lmt.14.12openalex-snapshot
DNA Repair Pathways and their Therapeutic Potential in Lung Cancer
inferred← citeshttps://doi.org/10.2478/s11536-013-0225-yopenalex-snapshot
Poly (ADP-ribose) polymerase 1 expression in fibroblasts of Down syndrome subjects
inferred← citeshttps://doi.org/10.2741/4318openalex-snapshot
Poly-ADP-ribosylation signaling during DNA damage repair
inferred← citeshttps://doi.org/10.31083/j.fbl2707210openalex-snapshot
Tumor-Suppressor Gene Transmembrane Protein 98 Promotes Proliferation and Inhibits Apoptosis in Ovarian Cancer
inferred← citeshttps://doi.org/10.31083/j.jmcm.2019.03.0303openalex-snapshot
Poly (ADP-ribose) polymerase (PARP) inhibitors as chemosensitizing compounds for the treatment of drug resistant cancers
inferred← citeshttps://doi.org/10.3109/07357907.2013.845670openalex-snapshot
Up-Regulation of Two Distinct p53-DNA Binding Functions by Covalent Poly(ADP-ribosyl)ation: Transactivating and Single Strand Break Sensing
inferred← citeshttps://doi.org/10.31857/s0026898423020167openalex-snapshot
Poly(ADP-ribose)polymerases 1 and 2: Classical Functions and Interaction with HPF1 ‒ New Histone Poly(ADP-ribosyl)ation Factor
inferred← citeshttps://doi.org/10.31857/s0026898423050129openalex-snapshot
The Role of the WGR Domain in the Functions of PARP1 and PARP2
inferred← citeshttps://doi.org/10.3389/fcell.2022.941356openalex-snapshot
Functional roles of ADP-ribosylation writers, readers and erasers
inferred← citeshttps://doi.org/10.3389/fmolb.2022.1073797openalex-snapshot
The potential of PARP inhibitors in targeted cancer therapy and immunotherapy
inferred← citeshttps://doi.org/10.3389/fnmol.2019.00327openalex-snapshot
Acute Liver Failure Induces Glial Reactivity, Oxidative Stress and Impairs Brain Energy Metabolism in Rats
inferred← citeshttps://doi.org/10.3389/fnut.2022.1093939openalex-snapshot
Biological function, mediate cell death pathway and their potential regulated mechanisms for post-mortem muscle tenderization of PARP1: A review
inferred← citeshttps://doi.org/10.3389/fonc.2025.1702121openalex-snapshot
PARP inhibitors as radiosensitizers: a comprehensive review of preclinical evidence and clinical applications
inferred← citeshttps://doi.org/10.3389/fphar.2020.00170openalex-snapshot
Poly(ADP-Ribose)Polymerase (PARP) Inhibitors and Radiation Therapy
inferred← citeshttps://doi.org/10.3389/fragi.2024.1442323openalex-snapshot
Aging mitochondria in the context of SARS-CoV-2: exploring interactions and implications
inferred← citeshttps://doi.org/10.3390/biom11020129openalex-snapshot
Targeting Non-Oncogene Addiction for Cancer Therapy
inferred← citeshttps://doi.org/10.3390/biom13081195openalex-snapshot
The Role of Poly(ADP-ribose) Polymerase 1 in Nuclear and Mitochondrial Base Excision Repair
inferred← citeshttps://doi.org/10.3390/biom2040524openalex-snapshot
Functional Aspects of PARP1 in DNA Repair and Transcription
inferred← citeshttps://doi.org/10.3390/cells11213343openalex-snapshot
Interactions of PARP1 Inhibitors with PARP1-Nucleosome Complexes
inferred← citeshttps://doi.org/10.3390/cells8020116openalex-snapshot
Diastereomeric Recognition of 5’,8-cyclo-2’-Deoxyadenosine Lesions by Human Poly(ADP-ribose) Polymerase 1 in a Biomimetic Model
inferred← citeshttps://doi.org/10.3390/ijms21176237openalex-snapshot
Role of Poly [ADP-ribose] Polymerase 1 in Activating the Kirsten ras (KRAS) Gene in Response to Oxidative Stress
inferred← citeshttps://doi.org/10.3390/ijms22105112openalex-snapshot
PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling
inferred← citeshttps://doi.org/10.3390/ijms242316784openalex-snapshot
CellTool: An Open-Source Software Combining Bio-Image Analysis and Mathematical Modeling for the Study of DNA Repair Dynamics
inferred← citeshttps://doi.org/10.3390/ijms25073895openalex-snapshot
Stress-Induced Changes in Nucleocytoplasmic Localization of Crucial Factors in Gene Expression Regulation
inferred← citeshttps://doi.org/10.3724/sp.j.1206.2011.00169openalex-snapshot
Effects of TSG on Apoptosis of HUVECs and The Expression of Caspase-3 and PARP Induced by H2O2*
inferred← citeshttps://doi.org/10.4081/ejh.2012.e9openalex-snapshot
PARP-1 protein expression in glioblastoma multiforme
inferred← citeshttps://doi.org/10.4081/ejh.2013.e13openalex-snapshot
Poly (ADP-ribose) polymerase 1 protein expression in normal and neoplastic prostatic tissue
inferred← citeshttps://doi.org/10.4103/2229-5151.152300openalex-snapshot
The assessment of an in-vitro model for evaluating the role of PARP in ethanol-mediated hepatotoxicity
inferred← citeshttps://doi.org/10.4155/fmc.12.58openalex-snapshot
Small-Molecule Inhibitors of DNA Damage-Repair Pathways: An Approach to Overcome Tumor Resistance to Alkylating Anticancer Drugs
inferred← citeshttps://doi.org/10.5204/thesis.eprints.254811openalex-snapshot
How Banf1 Functions to Inhibit the Activity of PARP1
inferred← citeshttps://doi.org/10.70675/16da82e2z0a3cz4743z9efdz8218950a93b2openalex-snapshot
Caractérisation des mécanismes d’ADP-ribosylation de l'ADN et son rôle dans la signalisation des dommages à l'ADN
inferred← citeshttps://doi.org/10.70675/29aa82e3zd066z437cz8175z9bee3663a7fcopenalex-snapshot
Nouvelles voies de réparation des lésions complexes dans l’ADN. Applications aux mécanismes de résistance aux thérapeutiques anticancéreuses.
inferred← citeshttps://doi.org/10.70675/48b4a8c9zf975z4e6fz861fz006708fb3d2aopenalex-snapshot
Space radiation-induced bystander effect : kinetics of biologic responses, mechanisms, and significance of secondary radiations
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