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ADP‐ribosyltransferases, an update on function and nomenclature
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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/cbic.202100047openalex-snapshot
Targeted Degradation of PARP14 Using a Heterobifunctional Small Molecule
inferredcites →https://doi.org/10.1007/82_2014_414openalex-snapshot
The Natural History of ADP-Ribosyltransferases and the ADP-Ribosylation System
inferredcites →https://doi.org/10.1007/s00018-019-03366-0openalex-snapshot
Poly(ADP-ribose) polymerase enzymes and the maintenance of genome integrity
inferredcites →https://doi.org/10.1007/s00726-010-0676-2openalex-snapshot
ADP-ribosylation of arginine
inferredcites →https://doi.org/10.1016/0968-0004(76)90255-3openalex-snapshot
Poly ADP-ribose and ADP-ribosylation of proteins
inferredcites →https://doi.org/10.1016/j.bcp.2019.07.004openalex-snapshot
Overview of the mammalian ADP-ribosyl-transferases clostridia toxin-like (ARTCs) family
inferredcites →https://doi.org/10.1016/j.bmcl.2017.04.089openalex-snapshot
Design and synthesis of potent inhibitors of the mono(ADP-ribosyl)transferase, PARP14
inferredcites →https://doi.org/10.1016/j.bmcl.2018.04.056openalex-snapshot
Design, synthesis and evaluation of potent and selective inhibitors of mono-(ADP-ribosyl)transferases PARP10 and PARP14
inferredcites →https://doi.org/10.1016/j.celrep.2018.07.048openalex-snapshot
Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme
inferredcites →https://doi.org/10.1016/j.celrep.2020.108176openalex-snapshot
Mapping Physiological ADP-Ribosylation Using Activated Ion Electron Transfer Dissociation
inferredcites →https://doi.org/10.1016/j.chembiol.2016.08.012openalex-snapshot
Small-Molecule Chemical Probe Rescues Cells from Mono-ADP-Ribosyltransferase ARTD10/PARP10-Induced Apoptosis and Sensitizes Cancer Cells to DNA Damage
inferredcites →https://doi.org/10.1016/j.chembiol.2018.09.011openalex-snapshot
A Potent and Selective PARP11 Inhibitor Suggests Coupling between Cellular Localization and Catalytic Activity
inferredcites →https://doi.org/10.1016/j.chembiol.2021.02.010openalex-snapshot
A potent and selective PARP14 inhibitor decreases protumor macrophage gene expression and elicits inflammatory responses in tumor explants
inferredcites →https://doi.org/10.1016/j.gde.2019.04.013openalex-snapshot
Role of H3K9me3 heterochromatin in cell identity establishment and maintenance
inferredcites →https://doi.org/10.1016/j.molcel.2008.08.009openalex-snapshot
Substrate-Assisted Catalysis by PARP10 Limits Its Activity to Mono-ADP-Ribosylation
inferredcites →https://doi.org/10.1016/j.molcel.2015.06.012openalex-snapshot
The Promise of Proteomics for the Study of ADP-Ribosylation
inferredcites →https://doi.org/10.1016/j.molcel.2017.04.028openalex-snapshot
Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9
inferredcites →https://doi.org/10.1016/j.semcdb.2016.09.009openalex-snapshot
Expanding functions of ADP-ribosylation in the maintenance of genome integrity
inferredcites →https://doi.org/10.1016/j.semcdb.2016.09.010openalex-snapshot
Cell fate regulation by chromatin ADP-ribosylation
inferredcites →https://doi.org/10.1016/j.tcb.2019.06.005openalex-snapshot
Defining and Modulating ‘BRCAness’
inferredcites →https://doi.org/10.1016/j.tibs.2009.12.003openalex-snapshot
Toward a unified nomenclature for mammalian ADP-ribosyltransferases
inferredcites →https://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
inferredcites →https://doi.org/10.1021/acsmedchemlett.8b00429openalex-snapshot
Rational Design of Cell-Active Inhibitors of PARP10
inferredcites →https://doi.org/10.1021/jasms.0c00040openalex-snapshot
Gas-Phase Fragmentation of ADP-Ribosylated Peptides: Arginine-Specific Side-Chain Losses and Their Implication in Database Searches
inferredcites →https://doi.org/10.1038/nbt.2121openalex-snapshot
Family-wide chemical profiling and structural analysis of PARP and tankyrase inhibitors
inferredcites →https://doi.org/10.1038/nchembio.2568openalex-snapshot
Insights into the biogenesis, function, and regulation of ADP-ribosylation
inferredcites →https://doi.org/10.1038/ncomms5426openalex-snapshot
Family-wide analysis of poly(ADP-ribose) polymerase activity
inferredcites →https://doi.org/10.1038/nrm3376openalex-snapshot
New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
inferredcites →https://doi.org/10.1038/s41467-019-08859-xopenalex-snapshot
Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation
inferredcites →https://doi.org/10.1038/s41467-020-18761-6openalex-snapshot
TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control
inferredcites →https://doi.org/10.1038/s41571-018-0055-6openalex-snapshot
Synthetic lethal therapies for cancer: what’s next after PARP inhibitors?
inferredcites →https://doi.org/10.1038/s41586-018-0750-6openalex-snapshot
NP220 mediates silencing of unintegrated retroviral DNA
inferredcites →https://doi.org/10.1038/s41589-019-0362-yopenalex-snapshot
Development of targeted protein degradation therapeutics
inferredcites →https://doi.org/10.1038/s41598-017-14156-8openalex-snapshot
PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions
inferredcites →https://doi.org/10.1038/s41598-019-55240-5openalex-snapshot
Fragment-based screening identifies molecules targeting the substrate-binding ankyrin repeat domains of tankyrase
inferredcites →https://doi.org/10.1038/s41598-020-69229-yopenalex-snapshot
A FRET-based high-throughput screening platform for the discovery of chemical probes targeting the scaffolding functions of human tankyrases
inferredcites →https://doi.org/10.1042/bst20180416openalex-snapshot
ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes
inferredcites →https://doi.org/10.1074/jbc.270.7.3247openalex-snapshot
Role of Glutamic Acid 988 of Human Poly-ADP-ribose Polymerase in Polymer Formation
inferredcites →https://doi.org/10.1074/jbc.274.25.17860openalex-snapshot
PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase
inferredcites →https://doi.org/10.1074/jbc.m109.077834openalex-snapshot
PARP-3 Is a Mono-ADP-ribosylase That Activates PARP-1 in the Absence of DNA
inferredcites →https://doi.org/10.1074/jbc.m114.630160openalex-snapshot
Structural Basis for Lack of ADP-ribosyltransferase Activity in Poly(ADP-ribose) Polymerase-13/Zinc Finger Antiviral Protein
inferredcites →https://doi.org/10.1074/mcp.tir119.001315openalex-snapshot
An Advanced Strategy for Comprehensive Profiling of ADP-ribosylation Sites Using Mass Spectrometry-based Proteomics*
inferredcites →https://doi.org/10.1083/jcb.202101021openalex-snapshot
Neuralized-like protein 4 (NEURL4) mediates ADP-ribosylation of mitochondrial proteins
inferredcites →https://doi.org/10.1093/nar/gkab136openalex-snapshot
ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function
inferredcites →https://doi.org/10.1093/nar/gkv1383openalex-snapshot
Readers of poly(ADP-ribose): designed to be fit for purpose
inferredcites →https://doi.org/10.1093/nar/gky995openalex-snapshot
The Pfam protein families database in 2019
inferredcites →https://doi.org/10.1101/gad.291518.116openalex-snapshot
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
inferredcites →https://doi.org/10.1101/gad.334284.119openalex-snapshot
The role of ADP-ribose metabolism in metabolic regulation, adipose tissue differentiation, and metabolism
inferredcites →https://doi.org/10.1101/gad.334433.119openalex-snapshot
PARPs and ADP-ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasis
inferredcites →https://doi.org/10.1101/gad.334631.119openalex-snapshot
(ADP-ribosyl)hydrolases: structure, function, and biology
inferredcites →https://doi.org/10.1111/bph.14038openalex-snapshot
Regulation of Wnt/β‐catenin signalling by tankyrase‐dependent poly(ADP‐ribosyl)ation and scaffolding
inferredcites →https://doi.org/10.1111/febs.15518openalex-snapshot
Progress and outlook in studying the substrate specificities of PARPs and related enzymes
inferredcites →https://doi.org/10.1111/imm.13332openalex-snapshot
ADP‐ribosylation in evasion, promotion and exacerbation of immune responses
inferredcites →https://doi.org/10.1126/sciadv.abc0418openalex-snapshot
Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases
inferredcites →https://doi.org/10.1126/science.282.5393.1484openalex-snapshot
Tankyrase, a Poly(ADP-Ribose) Polymerase at Human Telomeres
inferredcites →https://doi.org/10.1126/science.aaa7227openalex-snapshot
Epigenetic silencing by the HUSH complex mediates position-effect variegation in human cells
inferredcites →https://doi.org/10.1126/science.aam7344openalex-snapshot
PARP inhibitors: Synthetic lethality in the clinic
inferredcites →https://doi.org/10.1128/mmbr.00040-05openalex-snapshot
Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
inferredcites →https://doi.org/10.1146/annurev-biochem-060815-014935openalex-snapshot
Macrodomains: Structure, Function, Evolution, and Catalytic Activities
inferredcites →https://doi.org/10.1146/annurev.bi.46.070177.000523openalex-snapshot
Poly (ADP-Ribose) and ADP-Ribosylation of Proteins
inferredcites →https://doi.org/10.1158/0008-5472.can-13-1701openalex-snapshot
Targeting PARP-1 Allosteric Regulation Offers Therapeutic Potential against Cancer
inferredcites →https://doi.org/10.1371/journal.pone.0037352openalex-snapshot
PARP16/ARTD15 Is a Novel Endoplasmic-Reticulum-Associated Mono-ADP-Ribosyltransferase That Interacts with, and Modifies Karyopherin-ß1
inferredcites →https://doi.org/10.2174/0929867043455611openalex-snapshot
Ecto-ADP-Ribosyltransferases (ARTs): Emerging Actors in Cell Communication and Signaling
inferredcites →https://doi.org/10.3390/cancers10120487openalex-snapshot
Role of BRCA Mutations in Cancer Treatment with Poly(ADP-ribose) Polymerase (PARP) Inhibitors
inferredcites →https://doi.org/10.3390/cells10020313openalex-snapshot
MARTs and MARylation in the Cytosol: Biological Functions, Mechanisms of Action, and Therapeutic Potential
inferredcites →https://doi.org/10.3390/cells10030680openalex-snapshot
Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight
inferredcites →https://doi.org/10.7554/elife.60480openalex-snapshot
Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets
inferredcites →https://doi.org/10.7717/peerj.11051openalex-snapshot
A novel predicted ADP-ribosyltransferase-like family conserved in eukaryotic evolution
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/ange.202313317openalex-snapshot
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
inferred← citeshttps://doi.org/10.1002/ange.202411203openalex-snapshot
Cell‐Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP‐Ribosylation
inferred← citeshttps://doi.org/10.1002/anie.202313317openalex-snapshot
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
inferred← citeshttps://doi.org/10.1002/anie.202411203openalex-snapshot
Cell‐Permeable Nicotinamide Adenine Dinucleotides for Exploration of Cellular Protein ADP‐Ribosylation
inferred← citeshttps://doi.org/10.1002/bdr2.2089openalex-snapshot
Viewing teratogens through the lens of nicotinamide adenine dinucleotide ( NAD +)
inferred← citeshttps://doi.org/10.1002/bies.202100240openalex-snapshot
Assay technologies facilitating drug discovery for ADP‐ribosyl writers, readers and erasers
inferred← citeshttps://doi.org/10.1002/bies.202400087openalex-snapshot
Unleashing viral mimicry: A combinatorial strategy to enhance the efficacy of PARP7 inhibitors
inferred← citeshttps://doi.org/10.1002/cbic.202300797openalex-snapshot
A desthiobiotin labelled NAD+ analogue to uncover Poly(ADP‐ribose) polymerase 1 protein targets
inferred← citeshttps://doi.org/10.1002/cbic.202300865openalex-snapshot
Synthesis and Macrodomain Binding of Gln‐carba‐ADPr‐peptide
inferred← citeshttps://doi.org/10.1002/cbic.202400440openalex-snapshot
Mono‐ADP‐Ribosylation of Peptides: An Overview of Synthetic and Chemoenzymatic Methodologies
inferred← citeshttps://doi.org/10.1002/chem.202501383openalex-snapshot
Convergent Approach Toward ADP‐Ribosylated Peptides via a Chemoselective Phosphate Condensation
inferred← citeshttps://doi.org/10.1002/cpdd.1539openalex-snapshot
First‐in‐Human Phase 1 Study to Evaluate the Clinical Pharmacology Properties of RBN‐3143, a Novel Inhibitor of Mono‐Adenosine Diphosphate Ribosyltransferase‐PARP14
inferred← citeshttps://doi.org/10.1002/mco2.70314openalex-snapshot
PARP (Poly ADP‐ribose Polymerase) Family in Health and Disease
inferred← citeshttps://doi.org/10.1002/minf.202300183openalex-snapshot
Synthetically accessible de novo design using reaction vectors: Application to PARP1 inhibitors**
inferred← citeshttps://doi.org/10.1007/16833_2024_348openalex-snapshot
PARP1: Opportunities of Developing New Drugs for an Old Target
inferred← citeshttps://doi.org/10.1007/978-1-0716-2891-1_12openalex-snapshot
Studying the Immunomodulatory Functions of PARP1 and PARP2 in Mouse Models of Cancer
inferred← citeshttps://doi.org/10.1007/978-1-0716-2891-1_15openalex-snapshot
Characterizing ADP-Ribosylation Sites Using Af1521 Enrichment Coupled to ETD-Based Mass Spectrometry
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/10.1007/978-1-0716-5166-7_15openalex-snapshot
Purification of Protein-Free and Protein-Linked Poly(ADP-Ribose) from Biochemical Reactions and from Human Cells
inferred← citeshttps://doi.org/10.1007/s00018-022-04235-zopenalex-snapshot
Functions of ADP-ribose transferases in the maintenance of telomere integrity
inferred← citeshttps://doi.org/10.1007/s00018-022-04290-6openalex-snapshot
Intracellular mono-ADP-ribosyltransferases at the host–virus interphase
inferred← citeshttps://doi.org/10.1007/s00018-023-04717-8openalex-snapshot
Mono-ADP-ribosylation by PARP10 inhibits Chikungunya virus nsP2 proteolytic activity and viral replication
inferred← citeshttps://doi.org/10.1007/s00018-025-05586-zopenalex-snapshot
PARP12-mediated ADP-ribosylation contributes to breast cancer cell fate by regulating AKT activation and DNA-damage response
inferred← citeshttps://doi.org/10.1007/s10565-022-09739-9openalex-snapshot
PARP1 and XRCC1 exhibit a reciprocal relationship in genotoxic stress response
inferred← citeshttps://doi.org/10.1007/s11262-024-02050-1openalex-snapshot
Comparative genomics of the Neodiprion sertifer nucleopolyhedrovirus from Turkey with the fewest ORFs among baculoviruses
inferred← citeshttps://doi.org/10.1007/s12104-022-10110-6openalex-snapshot
NMR study of human macroPARPs domains: 1H, 15N and 13C resonance assignment of hPARP14 macro domain 2 in the free and the ADPr bound state
inferred← citeshttps://doi.org/10.1007/s12104-026-10270-9openalex-snapshot
NMR study of human macroPARPs domains: 1H, 13C and 15N backbone and side-chain chemical shift assignments of hPARP9 macro domain 1 (MD1) in the apo and in the ADPr bound states
inferred← citeshttps://doi.org/10.1007/s12268-025-2460-6openalex-snapshot
The beauty of ADP-ribosylation: versatility in every link and organelle
inferred← citeshttps://doi.org/10.1007/s13402-025-01150-wopenalex-snapshot
PARP7 and aryl hydrocarbon receptor differentially regulate mammary cancer cell proliferation and STING-induced type I interferon signalling
inferred← citeshttps://doi.org/10.1007/s13577-025-01294-9openalex-snapshot
Elucidating the risk factors and oncogene drivers of acute myeloid leukemia
inferred← citeshttps://doi.org/10.1016/b978-0-443-16032-5.00008-7openalex-snapshot
Overcoming resistance in prostate cancer with targeted and small molecule-based therapies
inferred← citeshttps://doi.org/10.1016/j.ajpath.2025.07.004openalex-snapshot
Poly (ADP-Ribose) Polymerase 1 and 2 in B-Cell Lymphoma
inferred← citeshttps://doi.org/10.1016/j.apsb.2026.06.053openalex-snapshot
The ADP-ribosyltransferases 3 (ART3) is a novel suppressor of pathological cardiac hypertrophy by ribosylating ITGA7
inferred← citeshttps://doi.org/10.1016/j.arr.2024.102646openalex-snapshot
The interplay of NAD and hypoxic stress and its relevance for ageing
inferred← citeshttps://doi.org/10.1016/j.bbcan.2024.189221openalex-snapshot
Emerging strategies to overcome PARP inhibitors' resistance in ovarian cancer
inferred← citeshttps://doi.org/10.1016/j.bcp.2025.116872openalex-snapshot
Loss of aryl hydrocarbon receptor reduces pancreatic tumor growth by increasing immune cell infiltration
inferred← citeshttps://doi.org/10.1016/j.bcp.2025.117618openalex-snapshot
Advances in TCDD-inducible poly(ADP-ribose) polymerase (TiPARP/PARP7) research: From molecular mechanisms to therapeutic applications
inferred← citeshttps://doi.org/10.1016/j.bmc.2021.116511openalex-snapshot
Analogs of TIQ-A as inhibitors of human mono-ADP-ribosylating PARPs
inferred← citeshttps://doi.org/10.1016/j.bmc.2025.118202openalex-snapshot
Recent advances in the synthesis of poly (ADP-ribose)
inferred← citeshttps://doi.org/10.1016/j.canlet.2026.218875openalex-snapshot
Coordinated nicotinamide metabolism by NAMPT and NNMT: Integrating metabolic, epigenetic and immune crosstalk
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.celrep.2022.111529openalex-snapshot
Crystal structures and functional analysis of the ZnF5-WWE1-WWE2 region of PARP13/ZAP define a distinctive mode of engaging poly(ADP-ribose)
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.2024.114234openalex-snapshot
A unified mechanism for PARP inhibitor-induced PARP1 chromatin retention at DNA damage sites in living cells
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.2025.116789openalex-snapshot
PARG regulates the proteasomal degradation of TARG1
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.celrep.2026.117866openalex-snapshot
From NAD+ metabolism to skeletal muscle function: The emerging role of ADP-ribosylation
inferred← citeshttps://doi.org/10.1016/j.chembiol.2022.02.002openalex-snapshot
Two birds, one stone: Non-canonical therapeutic effects of the PARP inhibitor Talazoparib
inferred← citeshttps://doi.org/10.1016/j.chembiol.2022.11.012openalex-snapshot
Structurally distinct PARP7 inhibitors provide new insights into the function of PARP7 in regulating nucleic acid-sensing and IFN-β signaling
inferred← citeshttps://doi.org/10.1016/j.cmet.2025.04.002openalex-snapshot
NAD depletion in skeletal muscle does not compromise muscle function or accelerate aging
inferred← citeshttps://doi.org/10.1016/j.dnarep.2023.103528openalex-snapshot
Single-molecule imaging of genome maintenance proteins encountering specific DNA sequences and structures
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.2025.103841openalex-snapshot
Targeting DNA damage sensors for cancer therapy
inferred← citeshttps://doi.org/10.1016/j.dnarep.2025.103858openalex-snapshot
"Yin-Yang" of PARP1 in genotoxic and inflammatory 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.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.2022.114362openalex-snapshot
Potent 2,3-dihydrophthalazine-1,4-dione derivatives as dual inhibitors for mono-ADP-ribosyltransferases PARP10 and PARP15
inferred← citeshttps://doi.org/10.1016/j.ejmech.2025.117397openalex-snapshot
Substitutions at the C-8 position of quinazolin-4-ones improve the potency of nicotinamide site binding tankyrase inhibitors
inferred← citeshttps://doi.org/10.1016/j.ejmech.2025.118111openalex-snapshot
Optimization of 2,3-dihydrophthalazine-1,4-dione PARP inhibitor scaffold for nanomolar potency and specificity towards human PARP10
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2025.06.010openalex-snapshot
Oxidative stress and PARP activation in the lungs is an early event in COVID-19 pneumonia
inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e27865openalex-snapshot
Single-cell and bulk RNA sequencing highlights the role of M1-like infiltrating macrophages in antibody-mediated rejection after kidney transplantation
inferred← citeshttps://doi.org/10.1016/j.isci.2023.106444openalex-snapshot
DTX3L E3 ligase targets p53 for degradation at poly ADP-ribose polymerase-associated DNA damage sites
inferred← citeshttps://doi.org/10.1016/j.isci.2025.112990openalex-snapshot
The E3 ubiquitin ligase DTX3L and the deubiquitinase USP28 fine-tune DNA repair through mutual regulation of their protein levels
inferred← citeshttps://doi.org/10.1016/j.jbc.2023.105096openalex-snapshot
PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation
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.2025.110463openalex-snapshot
Molecular determinants of nucleic acid recognition by an RNA-targeting ADP-ribosyltransferase toxin
inferred← citeshttps://doi.org/10.1016/j.jmb.2023.168434openalex-snapshot
KH-like Domains in PARP9/DTX3L and PARP14 Coordinate Protein–Protein Interactions to Promote Cancer Cell Survival
inferred← citeshttps://doi.org/10.1016/j.mcpro.2026.101666openalex-snapshot
Optimized detection of acidic ADP-ribosylation by PARP14 in vitro using multi-modal mass spectrometry reveals putative autoregulatory patches
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.2022.06.011openalex-snapshot
Captured snapshots of PARP1 in the active state reveal the mechanics of PARP1 allostery
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.pep.2024.106580openalex-snapshot
A multidomain PARP14 construct suitable for bacterial expression
inferred← citeshttps://doi.org/10.1016/j.pharmr.2026.100162openalex-snapshot
Defining the Druggability of Viral Macrodomains in Coronaviruses and Alphaviruses
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.reth.2024.01.011openalex-snapshot
Extracellular vesicles derived from HuMSCs alleviate daunorubicin-induced cardiac microvascular injury via miR-186-5p/PARP9/STAT1 signal pathway
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.semcancer.2023.11.009openalex-snapshot
Mutual regulation of TGFβ-induced oncogenic EMT, cell cycle progression and the DDR
inferred← citeshttps://doi.org/10.1016/j.taap.2026.118069openalex-snapshot
METTL3-mediated m6A modification of PARP2 accelerates hepatocellular carcinoma progression
inferred← citeshttps://doi.org/10.1016/j.tibs.2024.08.006openalex-snapshot
The quest to identify ADP-ribosylation readers: methodological advances
inferred← citeshttps://doi.org/10.1016/j.tibs.2024.12.013openalex-snapshot
PARPs and ADP-ribosylation-mediated biomolecular condensates: determinants, dynamics, and disease implications
inferred← citeshttps://doi.org/10.1016/j.tibs.2025.03.010openalex-snapshot
Modifying the modifiers: ubiquitination of ADP-ribosylation in human cells
inferred← citeshttps://doi.org/10.1016/j.tibs.2026.02.008openalex-snapshot
Parallels and crosstalk of ADP-ribosylation and ubiquitination
inferred← citeshttps://doi.org/10.1016/j.tig.2024.08.009openalex-snapshot
The complex universe of inactive PARP1
inferred← citeshttps://doi.org/10.1016/j.vaccine.2024.03.006openalex-snapshot
Subolesin knockdown in tick cells provides insights into vaccine protective mechanisms
inferred← citeshttps://doi.org/10.1016/j.virol.2023.109845openalex-snapshot
Macro1 domain residue F156: A hallmark of SARS-CoV-2 de-MARylation specificity
inferred← citeshttps://doi.org/10.1017/erm.2024.13openalex-snapshot
PARP enzymes and mono-ADP-ribosylation: advancing the connection from interferon-signalling to cancer biology
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/10.1017/erm.2024.17openalex-snapshot
ADP-ribose hydrolases: biological functions and potential therapeutic targets
inferred← citeshttps://doi.org/10.1021/acs.biochem.5c00105openalex-snapshot
Kinetic Mechanism of the Emergent Anticancer Target, Human ADP-ribosyltransferase 1
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.jmedchem.2c00281openalex-snapshot
Medicinal Chemistry Perspective on Targeting Mono-ADP-Ribosylating PARPs with Small Molecules
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.2c01460openalex-snapshot
[1,2,4]Triazolo[3,4- b ]benzothiazole Scaffold as Versatile Nicotinamide Mimic Allowing Nanomolar Inhibition of Different PARP Enzymes
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.3c01152openalex-snapshot
Discovery of Quinazoline-2,4(1H,3H)-dione Derivatives Containing a Piperizinone Moiety as Potent PARP-1/2 Inhibitors─Design, Synthesis, In Vivo Antitumor Activity, and X-ray Crystal Structure Analysis
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.3c01764openalex-snapshot
Discovery of Highly Selective PARP7 Inhibitors with a Novel Scaffold for Cancer Immunotherapy
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.3c02451openalex-snapshot
Discovery of 2-Amide-3-methylester Thiophenes that Target SARS-CoV-2 Mac1 and Repress Coronavirus Replication, Validating Mac1 as an Antiviral Target
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.5c02481openalex-snapshot
Discovery of Fused Isoquinolinone/Triazole as a Scaffold for Tankyrase and PARP Inhibition
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.2c01300openalex-snapshot
Mimetics of ADP-Ribosylated Histidine through Copper(I)-Catalyzed Click Chemistry
inferred← citeshttps://doi.org/10.1021/acs.orglett.3c01554openalex-snapshot
4-Thioribose Analogues of Adenosine Diphosphate Ribose (ADPr) Peptides
inferred← citeshttps://doi.org/10.1021/acschembio.5c00817openalex-snapshot
A Large-Scale Method to Measure the Stoichiometries of Protein Poly-ADP-Ribosylation
inferred← citeshttps://doi.org/10.1021/acsinfecdis.5c00695openalex-snapshot
A FRET-Based High-Throughput Screening Assay for the Discovery of Mycobacterium tuberculosis DNA ADP-Ribosylglycohydrolase DarG Inhibitors
inferred← citeshttps://doi.org/10.1021/acsmedchemlett.4c00603openalex-snapshot
Discovery of a Novel [6–6–5–5–6] Pentacyclic Tetrahydrocyclopentaphthalazinone as a Promising PARP Inhibitor Scaffold
inferred← citeshttps://doi.org/10.1021/acsomega.5c07459openalex-snapshot
Simultaneous Detection and Quantification of Adenine Nucleotides in Mammalian Cultured Cells by HPLC
inferred← citeshttps://doi.org/10.1021/jacs.3c03771openalex-snapshot
Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation
inferred← citeshttps://doi.org/10.1021/jacs.5c17532openalex-snapshot
Chemical Synthesis of Native ADP-Ribosylated Oligonucleotides Enables Analysis of DNA ADP-Ribosylation Hydrolase Specificity
inferred← citeshttps://doi.org/10.1021/jasms.3c00129openalex-snapshot
A Combined Gas-Phase Separation Strategy for ADP-ribosylated Peptides
inferred← citeshttps://doi.org/10.1038/s41401-026-01848-zopenalex-snapshot
Endothelial PARP1 orchestrates endothelial-to-mesenchymal transition via the PARylation of FHL2 in ischaemic heart failure
inferred← citeshttps://doi.org/10.1038/s41467-023-42939-3openalex-snapshot
Multiple E3 ligases control tankyrase stability and function
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/s41467-024-47222-7openalex-snapshot
PARP2 promotes Break Induced Replication-mediated telomere fragility in response to replication stress
inferred← citeshttps://doi.org/10.1038/s41467-024-50429-3openalex-snapshot
PARP10 promotes the repair of nascent strand DNA gaps through RAD18 mediated translesion synthesis
inferred← citeshttps://doi.org/10.1038/s41467-024-51972-9openalex-snapshot
Cation-induced intramolecular coil-to-globule transition in poly(ADP-ribose)
inferred← citeshttps://doi.org/10.1038/s41467-024-55666-0openalex-snapshot
Regulation of stress granule maturation and dynamics by poly(ADP-ribose) interaction with PARP13
inferred← citeshttps://doi.org/10.1038/s41467-025-60995-9openalex-snapshot
Structure of lymphostatin, a large multi-functional virulence factor of pathogenic Escherichia coli
inferred← citeshttps://doi.org/10.1038/s41467-025-65315-9openalex-snapshot
Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15
inferred← citeshttps://doi.org/10.1038/s41467-025-66136-6openalex-snapshot
Global remodeling of ADP-ribosylation by PARP1 suppresses influenza A virus infection
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/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/s41580-021-00413-2openalex-snapshot
The mechanisms of integral membrane protein biogenesis
inferred← citeshttps://doi.org/10.1038/s41580-024-00752-wopenalex-snapshot
Regulation of and challenges in targeting NAD+ metabolism
inferred← citeshttps://doi.org/10.1038/s41586-024-07217-2openalex-snapshot
Transcription–replication conflicts underlie sensitivity to PARP inhibitors
inferred← citeshttps://doi.org/10.1038/s41586-024-08102-8openalex-snapshot
Anti-viral defence by an mRNA ADP-ribosyltransferase that blocks translation
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/s41598-023-35076-wopenalex-snapshot
PARP2 poly(ADP-ribosyl)ates nuclear factor erythroid 2-related factor 2 (NRF2) affecting NRF2 subcellular localization
inferred← citeshttps://doi.org/10.1038/s41598-024-54123-8openalex-snapshot
High-throughput screening assay for PARP-HPF1 interaction inhibitors to affect DNA damage repair
inferred← citeshttps://doi.org/10.1038/s42003-024-06811-4openalex-snapshot
Divalent and multivalent cations control liquid-like assembly of poly(ADP-ribosyl)ated PARP1 into multimolecular associates in vitro
inferred← citeshttps://doi.org/10.1038/s42003-025-07901-7openalex-snapshot
Family-wide analysis of human macrodomains reveals novel activities and identifies PARG as most efficient ADPr-RNA hydrolase
inferred← citeshttps://doi.org/10.1038/s42003-026-09832-3openalex-snapshot
Screening assay to monitor mono-ADP-ribosylhydrolase activity of viral macrodomains in cells
inferred← citeshttps://doi.org/10.1038/s44318-024-00125-1openalex-snapshot
PARP14 is regulated by the PARP9/DTX3L complex and promotes interferon γ-induced ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/s44318-024-00126-0openalex-snapshot
PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/s44318-025-00391-7openalex-snapshot
Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose
inferred← citeshttps://doi.org/10.1038/s44318-025-00421-4openalex-snapshot
Interferon-induced PARP14-mediated ADP-ribosylation in p62 bodies requires the ubiquitin-proteasome system
inferred← citeshttps://doi.org/10.1038/s44318-025-00510-4openalex-snapshot
Parp7 generates an ADP-ribosyl degron that controls negative feedback of androgen signaling
inferred← citeshttps://doi.org/10.1038/s44318-025-00545-7openalex-snapshot
PARP7 is a proteotoxic stress sensor that labels proteins for degradation
inferred← citeshttps://doi.org/10.1038/s44318-025-00656-1openalex-snapshot
Ubiquitin pathway blockade reveals endogenous ADP-ribosylation marking PARP7 and AHR for degradation
inferred← citeshttps://doi.org/10.1038/s44321-025-00214-6openalex-snapshot
PARP7 as a new target for activating anti-tumor immunity in cancer
inferred← citeshttps://doi.org/10.1039/9781837677436-00119openalex-snapshot
Biocatalytic Production of Nucleotides
inferred← citeshttps://doi.org/10.1042/bcj20210280openalex-snapshot
Beyond protein modification: the rise of non-canonical ADP-ribosylation
inferred← citeshttps://doi.org/10.1042/bcj20210722openalex-snapshot
Reconstitution of the DTX3L–PARP9 complex reveals determinants for high-affinity heterodimerization and multimeric assembly
inferred← citeshttps://doi.org/10.1042/bcj20230230openalex-snapshot
Regulation of PARP1/2 and the tankyrases: emerging parallels
inferred← citeshttps://doi.org/10.1042/bsr20240986openalex-snapshot
Interferon-induced ADP-ribosylation: technical developments driving ICAB discovery
inferred← citeshttps://doi.org/10.1042/bst20220501openalex-snapshot
Activities and binding partners of E3 ubiquitin ligase DTX3L and its roles in cancer
inferred← citeshttps://doi.org/10.1042/bst20220749openalex-snapshot
The function and regulation of ADP-ribosylation in the DNA damage response
inferred← citeshttps://doi.org/10.1042/ebc20253036openalex-snapshot
NEDD8, stress granules, and amyotrophic lateral sclerosis: unveiling the therapeutic potential of the NEDP1 protease
inferred← citeshttps://doi.org/10.1042/ebc20253040openalex-snapshot
Interplay between ubiquitination and ADP-ribosylation and the case of dual modification ADPr-Ub
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.2026494119openalex-snapshot
PKD-dependent PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 is required for E-cadherin transport from Golgi to plasma membrane
inferred← citeshttps://doi.org/10.1073/pnas.2213857120openalex-snapshot
Muscle PARP1 inhibition extends lifespan through AMPKα PARylation and activation in Drosophila
inferred← citeshttps://doi.org/10.1073/pnas.2302083120openalex-snapshot
SARS-CoV-2 Mac1 is required for IFN antagonism and efficient virus replication in cell culture and in mice
inferred← citeshttps://doi.org/10.1073/pnas.2309047120openalex-snapshot
PARP7-mediated ADP-ribosylation of FRA1 promotes cancer cell growth by repressing IRF1- and IRF3-dependent apoptosis
inferred← citeshttps://doi.org/10.1073/pnas.2424985122openalex-snapshot
CRISPR screens and quantitative proteomics reveal remodeling of the aryl hydrocarbon receptor–driven proteome through PARP7 activity
inferred← citeshttps://doi.org/10.1073/pnas.2525274123openalex-snapshot
PARP7 protects the lung epithelial barrier from diverse environmental threats
inferred← citeshttps://doi.org/10.1073/pnas.2527653123openalex-snapshot
A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation
inferred← citeshttps://doi.org/10.1073/pnas.2604770123openalex-snapshot
Transition-state analysis of the arginine-specific human ADP-ribosyltransferase 1
inferred← citeshttps://doi.org/10.1080/07391102.2023.2297821openalex-snapshot
Identification and stability analysis of potential ADP-ribose modification sites on vascular endothelial growth factor (VEGF) through molecular dynamics simulation
inferred← citeshttps://doi.org/10.1080/14756366.2023.2254012openalex-snapshot
Targeting reversible post-translational modifications with PROTACs: a focus on enzymes modifying protein lysine and arginine residues
inferred← citeshttps://doi.org/10.1083/jcb.202101021openalex-snapshot
Neuralized-like protein 4 (NEURL4) mediates ADP-ribosylation of mitochondrial proteins
inferred← citeshttps://doi.org/10.1089/ars.2023.0349openalex-snapshot
Nicotinamide Adenine Dinucleotide Deficiency and Its Impact on Mammalian Development
inferred← citeshttps://doi.org/10.1093/genetics/iyad208openalex-snapshot
Bradysia (Sciara) coprophila larvae up-regulate DNA repair pathways and down-regulate developmental regulators in response to ionizing radiation
inferred← citeshttps://doi.org/10.1093/nar/gkac1235openalex-snapshot
Influence of chain length and branching on poly(ADP-ribose)–protein interactions
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/gkad066openalex-snapshot
PARP1 associates with R-loops to promote their resolution and genome stability
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/gkae059openalex-snapshot
Tankyrase-1 regulates RBP-mediated mRNA turnover to promote muscle fiber formation
inferred← citeshttps://doi.org/10.1093/nar/gkaf069openalex-snapshot
Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack
inferred← citeshttps://doi.org/10.1093/nar/gkaf300openalex-snapshot
Proteome-wide microarray-based screening of PAR-binding proteins
inferred← citeshttps://doi.org/10.1093/nar/gkaf837openalex-snapshot
Poly (ADP-ribose) polymerase in yeasts: characterization and involvement in telomere maintenance
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/gkag289openalex-snapshot
Reversible RNA ADP-ribosylation on uracil bases
inferred← citeshttps://doi.org/10.1093/narcan/zcad009openalex-snapshot
Mono-ADP-ribosylation by PARP10 and PARP14 in genome stability
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/10.1096/fj.202403378ropenalex-snapshot
Poly (ADP‐Ribose) Glycohydrolase‐Dependent dePARylation of PCNA Is Essential for DNA Replication
inferred← citeshttps://doi.org/10.1098/rsob.210365openalex-snapshot
The zinc-binding motif in tankyrases is required for the structural integrity of the catalytic ADP-ribosyltransferase domain
inferred← citeshttps://doi.org/10.1098/rsob.250181openalex-snapshot
Histidine and tyrosine residues are targets for SIRT6 ADP-ribosylation activity
inferred← citeshttps://doi.org/10.1098/rsos.250824openalex-snapshot
Phosphorylation as a candidate regulatory mechanism for effector recruitment to tankyrase
inferred← citeshttps://doi.org/10.1101/2021.06.14.448324openalex-snapshot
Reconstitution of the DTX3L-PARP9 complex reveals determinants for high affinity heterodimer formation and enzymatic function
inferred← citeshttps://doi.org/10.1101/2021.10.04.463032openalex-snapshot
The zinc-binding motif in tankyrases is required for the structural integrity and proper function of the catalytic domain
inferred← citeshttps://doi.org/10.1101/2022.08.24.505095openalex-snapshot
Whether the ADP-ribosyltransferase activity of Ta-sro1, a noncanonical PARP protein, contributes to its function in salinity-stress tolerance?
inferred← citeshttps://doi.org/10.1101/2022.11.26.517555openalex-snapshot
The endocytic recycling pathway is controlled by the ADP-ribosylated GTPase Rab14
inferred← citeshttps://doi.org/10.1101/2023.04.06.535927openalex-snapshot
SARS-CoV-2 Mac1 is required for IFN antagonism and efficient virus replication in mice
inferred← citeshttps://doi.org/10.1101/2023.10.25.564012openalex-snapshot
Length-dependent Intramolecular Coil-to-Globule Transition in Poly(ADP-ribose) Induced by Cations
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/10.1101/2024.01.03.574082openalex-snapshot
Mutation of a highly conserved isoleucine residue in loop 2 of several 𝛽-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental to infection
inferred← citeshttps://doi.org/10.1101/2024.03.15.585277openalex-snapshot
Comprehensive machine learning boosts structure-based virtual screening for PARP1 inhibitors
inferred← citeshttps://doi.org/10.1101/2024.05.22.595402openalex-snapshot
Interferon-Induced PARP14-Mediated ADP-Ribosylation in p62 Bodies Requires an Active Ubiquitin-Proteasome System
inferred← citeshttps://doi.org/10.1101/2024.06.27.600929openalex-snapshot
Discovery of ester-linked ubiquitylation of PARP10 mono-ADP-ribosylation in cells: a dual post-translational modification on Glu/Asp side chains
inferred← citeshttps://doi.org/10.1101/2024.06.29.601315openalex-snapshot
PARP14-dependent ADP-ribosylation of cytoplasmic SQSTM1/p62 foci supports innate immune signaling
inferred← citeshttps://doi.org/10.1101/2025.02.07.637082openalex-snapshot
Versatile Modular Antibodies for Sensitive and Specific Detection of Poly-ADP-Ribose
inferred← citeshttps://doi.org/10.1101/2025.06.18.25329841openalex-snapshot
PARP1 regulates establishment of the ovarian reserve and age at natural menopause
inferred← citeshttps://doi.org/10.1101/2025.07.01.662498openalex-snapshot
Automodification of N-terminal serine residues in PARP2 impacts PARP2 release from DNA damage sites
inferred← citeshttps://doi.org/10.1111/bph.17305openalex-snapshot
The PARP inhibitor rucaparib blocks SARS‐CoV‐2 virus binding to cells and the immune reaction in models of COVID‐19
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/febs.16907openalex-snapshot
PAR recognition by PARP1 regulates DNA‐dependent activities and independently stimulates catalytic activity of PARP1
inferred← citeshttps://doi.org/10.1111/febs.70035openalex-snapshot
Re‐evaluation of PTEN as an ADP ‐ribosylated tankyrase binding partner
inferred← citeshttps://doi.org/10.1111/febs.70039openalex-snapshot
Derivatives of MOPS : promising scaffolds for SARS coronaviruses Macro domain‐targeted inhibition
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