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Serine is a new target residue for endogenous ADP-ribosylation on histones

https://doi.org/10.1038/nchembio.2180
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1006/abio.1998.2664openalex-snapshot
Immunodot Blot Method for the Detection of Poly(ADP-ribose) Synthesizedin Vitroandin Vivo
inferredcites →https://doi.org/10.1016/j.cell.2011.08.008openalex-snapshot
Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification
inferredcites →https://doi.org/10.1016/j.ijms.2011.06.003openalex-snapshot
A review of tandem mass spectrometry characterization of adenosine diphosphate-ribosylated peptides
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.2013.08.026openalex-snapshot
Proteome-wide Identification of Poly(ADP-Ribosyl)ation Targets in Different Genotoxic Stress Responses
inferredcites →https://doi.org/10.1016/j.molcel.2015.04.016openalex-snapshot
Chromatin to Clinic: The Molecular Rationale for PARP1 Inhibitor Function
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.tcb.2011.06.001openalex-snapshot
Histone ADP-ribosylation in DNA repair, replication and transcription
inferredcites →https://doi.org/10.1016/j.tcb.2012.11.005openalex-snapshot
Histone modifications and mitosis: countermarks, landmarks, and bookmarks
inferredcites →https://doi.org/10.1021/ac026117iopenalex-snapshot
Stop and Go Extraction Tips for Matrix-Assisted Laser Desorption/Ionization, Nanoelectrospray, and LC/MS Sample Pretreatment in Proteomics
inferredcites →https://doi.org/10.1021/acs.jproteome.5b00432openalex-snapshot
Optimization of LTQ-Orbitrap Mass Spectrometer Parameters for the Identification of ADP-Ribosylation Sites
inferredcites →https://doi.org/10.1021/cr500491uopenalex-snapshot
Quantitative Proteomic Analysis of Histone Modifications
inferredcites →https://doi.org/10.1021/pr101065jopenalex-snapshot
Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
inferredcites →https://doi.org/10.1021/pr3000249openalex-snapshot
Optimized Fast and Sensitive Acquisition Methods for Shotgun Proteomics on a Quadrupole Orbitrap Mass Spectrometer
inferredcites →https://doi.org/10.1021/pr401032qopenalex-snapshot
Phosphoproteomic Approach to Characterize Protein Mono- and Poly(ADP-ribosyl)ation Sites from Cells
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/nbt.1511openalex-snapshot
MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
inferredcites →https://doi.org/10.1038/nmeth.1322openalex-snapshot
Universal sample preparation method for proteome analysis
inferredcites →https://doi.org/10.1038/nmeth.1731openalex-snapshot
Mining the O-glycoproteome using zinc-finger nuclease–glycoengineered SimpleCell lines
inferredcites →https://doi.org/10.1038/nrm3383openalex-snapshot
Vertebrate protein glycosylation: diversity, synthesis and function
inferredcites →https://doi.org/10.1038/srep18271openalex-snapshot
Nudix hydrolases degrade protein-conjugated ADP-ribose
inferredcites →https://doi.org/10.1042/bj20141554openalex-snapshot
Processing of protein ADP-ribosylation by Nudix hydrolases
inferredcites →https://doi.org/10.1042/bj3420249openalex-snapshot
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
inferredcites →https://doi.org/10.1074/jbc.270.14.7929openalex-snapshot
Protein Modification by ADP-ribose via Acid-labile Linkages
inferredcites →https://doi.org/10.1074/mcp.m200025-mcp200openalex-snapshot
Stable Isotope Labeling by Amino Acids in Cell Culture, SILAC, as a Simple and Accurate Approach to Expression Proteomics
inferredcites →https://doi.org/10.1093/nar/gkp273openalex-snapshot
Robust methods for purification of histones from cultured mammalian cells with the preservation of their native modifications
inferredcites →https://doi.org/10.1093/nar/gkq463openalex-snapshot
PARP1 ADP-ribosylates lysine residues of the core histone tails
inferredcites →https://doi.org/10.1146/annurev-biochem-060614-034506openalex-snapshot
Nuclear ADP-Ribosylation and Its Role in Chromatin Plasticity, Cell Differentiation, and Epigenetics

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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inferred← citeshttps://doi.org/10.1002/9781118970195.ch14openalex-snapshot
Site‐Specific Characterization of Asp ‐ and Glu ‐ ADP ‐Ribosylation by Quantitative Mass Spectrometry
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/anie.202313317openalex-snapshot
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
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.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/chem.202501383openalex-snapshot
Convergent Approach Toward ADP‐Ribosylated Peptides via a Chemoselective Phosphate Condensation
inferred← citeshttps://doi.org/10.1002/em.22623openalex-snapshot
Poly‐ ADP ‐ribosylation dynamics, signaling, and analysis
inferred← citeshttps://doi.org/10.1002/mas.21811openalex-snapshot
Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation
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_8openalex-snapshot
A Simple Method to Study ADP-Ribosylation Reversal: From Function to Drug Discovery
inferred← citeshttps://doi.org/10.1007/978-1-4939-8588-3_12openalex-snapshot
ADP-Ribosyl-Acceptor Hydrolase Activities Catalyzed by the ARH Family of Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4939-8588-3_13openalex-snapshot
Mono-ADP-Ribosylhydrolase Assays
inferred← citeshttps://doi.org/10.1007/978-1-4939-8588-3_18openalex-snapshot
Nonlocalized Searching of HCD Data for Fast and Sensitive Identification of ADP-Ribosylated Peptides
inferred← citeshttps://doi.org/10.1007/978-1-4939-8588-3_19openalex-snapshot
Quantitative Determination of MAR Hydrolase Residue Specificity In Vitro by Tandem Mass Spectrometry
inferred← citeshttps://doi.org/10.1007/978-1-4939-8588-3_9openalex-snapshot
Dictyostelium as a Model to Assess Site-Specific ADP-Ribosylation Events
inferred← citeshttps://doi.org/10.1007/978-3-032-26629-3_6openalex-snapshot
Dynamic Assemblies in Genome Maintenance
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/s10565-022-09739-9openalex-snapshot
PARP1 and XRCC1 exhibit a reciprocal relationship in genotoxic stress response
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/s42764-019-00004-8openalex-snapshot
Regulation of DNA damage-induced ATM activation by histone modifications
inferred← citeshttps://doi.org/10.1016/b978-0-12-814809-9.00002-0openalex-snapshot
Histone modifications
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/bs.mie.2019.06.024openalex-snapshot
Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry
inferred← citeshttps://doi.org/10.1016/bs.mie.2026.05.032openalex-snapshot
ChIPmentation-based mapping of histone modifications in aging: Experimental design and analytical considerations
inferred← citeshttps://doi.org/10.1016/j.actatropica.2020.105499openalex-snapshot
Poly(ADP-ribose) metabolism in human parasitic protozoa
inferred← citeshttps://doi.org/10.1016/j.antiviral.2017.11.001openalex-snapshot
Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
inferred← citeshttps://doi.org/10.1016/j.bcp.2018.09.028openalex-snapshot
Emerging roles of ADP-ribosyl-acceptor hydrolases (ARHs) in tumorigenesis and cell death pathways
inferred← citeshttps://doi.org/10.1016/j.bcp.2019.03.037openalex-snapshot
Human alcohol dehydrogenase 1 is an acceptor protein for polyADP-ribosylation
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.2026.117770openalex-snapshot
The PARG frontier: mechanisms of PAR turnover and opportunities in precision oncology
inferred← citeshttps://doi.org/10.1016/j.cell.2016.11.019openalex-snapshot
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
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.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.2018.07.048openalex-snapshot
Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme
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.2023.112060openalex-snapshot
PARylation of BRCA1 limits DNA break resection through BRCA2 and EXO1
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.2024.114433openalex-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.2026.117350openalex-snapshot
PARP1-specific inhibitor displays PARP1-detrapping activity
inferred← citeshttps://doi.org/10.1016/j.celrep.2026.118109openalex-snapshot
Oxidative DNA damage drives centromere fragility and chromosome instability
inferred← citeshttps://doi.org/10.1016/j.chembiol.2017.04.003openalex-snapshot
ADP-Ribosylation Goes Normal: Serine as the Major Site of the Modification
inferred← citeshttps://doi.org/10.1016/j.chembiol.2018.09.008openalex-snapshot
Monitoring Poly(ADP-ribosyl)glycohydrolase Activity with a Continuous Fluorescent Substrate
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.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.2019.02.002openalex-snapshot
The role of dePARylation in DNA damage repair and cancer suppression
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.2024.103711openalex-snapshot
PARticular MARks: Histone ADP-ribosylation and the DNA damage response
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.2025.103863openalex-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.gde.2021.07.005openalex-snapshot
Serine ADP-ribosylation in DNA-damage response regulation
inferred← citeshttps://doi.org/10.1016/j.isci.2026.117718openalex-snapshot
Massive histone H3 phosphorylation without mitotic chromosome condensation
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.2023.105096openalex-snapshot
PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation
inferred← citeshttps://doi.org/10.1016/j.jbc.2024.107545openalex-snapshot
An E3 ubiquitin ligase localization screen uncovers DTX2 as a novel ADP-ribosylation-dependent regulator of DNA double-strand break repair
inferred← citeshttps://doi.org/10.1016/j.jbc.2025.108300openalex-snapshot
A predictive chromatin architecture nexus regulates transcription and DNA damage repair
inferred← citeshttps://doi.org/10.1016/j.jos.2022.10.020openalex-snapshot
RETRACTED:Pituitary tumor transforming gene 1 promotes proliferation and malignant phenotype in osteosarcoma via NF-κB signaling
inferred← citeshttps://doi.org/10.1016/j.jprot.2017.06.019openalex-snapshot
Quick 96FASP for high throughput quantitative proteome analysis
inferred← citeshttps://doi.org/10.1016/j.mcpro.2021.100153openalex-snapshot
A Novel Spectral Annotation Strategy Streamlines Reporting of Mono-ADP-ribosylated Peptides Derived from Mouse Liver and Spleen in Response to IFN-γ
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.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.2020.03.016openalex-snapshot
Threonine ADP-Ribosylation of Ubiquitin by a Bacterial Effector Family Blocks Host Ubiquitination
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.2020.10.038openalex-snapshot
Distinct Structures and Dynamics of Chromatosomes with Different Human Linker Histone Isoforms
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.2026.03.038openalex-snapshot
A time-resolved atlas of histone modifications during mitotic entry
inferred← citeshttps://doi.org/10.1016/j.mrrev.2017.09.004openalex-snapshot
Poly-ADP ribosylation in DNA damage response and 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.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.2020.07.002openalex-snapshot
Control of the chromatin response to DNA damage: Histone proteins pull the strings
inferred← citeshttps://doi.org/10.1016/j.semcdb.2021.03.014openalex-snapshot
Mitotic chromosomes
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.tibs.2023.06.005openalex-snapshot
A chemical biology/modular antibody platform for ADP-ribosylation signaling
inferred← citeshttps://doi.org/10.1016/j.tig.2019.03.008openalex-snapshot
Perspectives on PARPs in S Phase
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.analchem.6b03365openalex-snapshot
Combining Higher-Energy Collision Dissociation and Electron-Transfer/Higher-Energy Collision Dissociation Fragmentation in a Product-Dependent Manner Confidently Assigns Proteomewide ADP-Ribose Acceptor Sites
inferred← citeshttps://doi.org/10.1021/acs.biochem.7b01022openalex-snapshot
Proteomic Analysis of the Downstream Signaling Network of PARP1
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.jproteome.7b00194openalex-snapshot
MsViz: A Graphical Software Tool for In-Depth Manual Validation and Quantitation of Post-translational Modifications
inferred← citeshttps://doi.org/10.1021/acs.jproteome.8b00146openalex-snapshot
Hydrofluoric Acid-Based Derivatization Strategy To Profile PARP-1 ADP-Ribosylation by LC–MS/MS
inferred← citeshttps://doi.org/10.1021/acs.jproteome.8b00895openalex-snapshot
A Study into the ADP-Ribosylome of IFN-γ-Stimulated THP-1 Human Macrophage-like Cells Identifies ARTD8/PARP14 and ARTD9/PARP9 ADP-Ribosylation
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.3c01391openalex-snapshot
Designing a Light-Induced Glycosylation Reaction for Poststage Synthesis of ADP-2″-Deoxyribosyl Derivatives
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/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.1c00542openalex-snapshot
Rapid Analysis of ADP-Ribosylation Dynamics and Site-Specificity Using TLC-MALDI
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.4c00582openalex-snapshot
Regulatory and Catalytic Domains of Poly(ADP-ribose) Polymerases Cross-Complement for DNA-Break-Dependent Allosteric Stimulation of Catalytic Activity
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/acschembio.6c00475openalex-snapshot
Linker Histone H1 Phosphorylation Promotes DNA Damage Repair during Replication Stress
inferred← citeshttps://doi.org/10.1021/acschembio.8b00567openalex-snapshot
Combining Chemical Genetics with Proximity-Dependent Labeling Reveals Cellular Targets of Poly(ADP-ribose) Polymerase 14 (PARP14)
inferred← citeshttps://doi.org/10.1021/acschembio.9b00429openalex-snapshot
The ARH and Macrodomain Families of α-ADP-ribose-acceptor Hydrolases Catalyze α-NAD+ Hydrolysis
inferred← citeshttps://doi.org/10.1021/acsomega.9b03591openalex-snapshot
Chemical Tools to Study Protein ADP-Ribosylation
inferred← citeshttps://doi.org/10.1021/acssensors.4c01406openalex-snapshot
A Genetically Encoded Sensor for Real-Time Monitoring of Poly-ADP-Ribosylation Dynamics In Vitro and in Cells
inferred← citeshttps://doi.org/10.1021/jacs.1c05429openalex-snapshot
Synthesis of ADP-Ribosylated Histones Reveals Site-Specific Impacts on Chromatin Structure and Function
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/jasms.0c00040openalex-snapshot
Gas-Phase Fragmentation of ADP-Ribosylated Peptides: Arginine-Specific Side-Chain Losses and Their Implication in Database Searches
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/s41392-020-00311-7openalex-snapshot
NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
inferred← citeshttps://doi.org/10.1038/s41422-018-0048-0openalex-snapshot
Destabilization of linker histone H1.2 is essential for ATM activation and DNA damage repair
inferred← citeshttps://doi.org/10.1038/s41467-017-02253-1openalex-snapshot
Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
inferred← citeshttps://doi.org/10.1038/s41467-018-05588-5openalex-snapshot
PARP2 mediates branched poly ADP-ribosylation in response to DNA damage
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/s41467-020-17069-9openalex-snapshot
Pathogenic ARH3 mutations result in ADP-ribose chromatin scars during DNA strand break repair
inferred← citeshttps://doi.org/10.1038/s41467-020-18981-wopenalex-snapshot
Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins
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/s41467-021-24361-9openalex-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/s41467-021-27867-4openalex-snapshot
Linking DNA repair and cell cycle progression through serine ADP-ribosylation of histones
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/s41467-023-40071-wopenalex-snapshot
Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3
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/s41467-024-48314-0openalex-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/s41467-025-61834-7openalex-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/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/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/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/s41594-023-01107-3openalex-snapshot
PARylated PDHE1α generates acetyl-CoA for local chromatin acetylation and DNA damage repair
inferred← citeshttps://doi.org/10.1038/s41598-018-22673-3openalex-snapshot
Dna is a New Target of Parp3
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/s42003-020-0984-3openalex-snapshot
The ubiquitin-conjugating enzyme UBE2K determines neurogenic potential through histone H3 in human embryonic stem cells
inferred← citeshttps://doi.org/10.1038/s42003-023-05494-7openalex-snapshot
The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3
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/s44318-025-00483-4openalex-snapshot
Phosphoribosyl ubiquitination of SNARE proteins regulates autophagy during Legionella infection
inferred← citeshttps://doi.org/10.1039/c7mb00498bopenalex-snapshot
The nucleosomal surface is the main target of histone ADP-ribosylation in response to DNA damage
inferred← citeshttps://doi.org/10.1039/c9ob00501copenalex-snapshot
Chemical ADP-ribosylation: mono-ADPr-peptides and oligo-ADP-ribose
inferred← citeshttps://doi.org/10.1042/bcj20210280openalex-snapshot
Beyond protein modification: the rise of non-canonical ADP-ribosylation
inferred← citeshttps://doi.org/10.1042/bcj20220550openalex-snapshot
Characterizing crosstalk in epigenetic signaling to understand disease physiology
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/bst20180418openalex-snapshot
PARPs in genome stability and signal transduction: implications for cancer therapy
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.1621485114openalex-snapshot
ADP-ribosylhydrolase activity of Chikungunya virus macrodomain is critical for virus replication and virulence
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/10.1074/jbc.ra118.004284openalex-snapshot
Structure–function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation
inferred← citeshttps://doi.org/10.1074/jbc.ra120.012801openalex-snapshot
AI26 inhibits the ADP-ribosylhydrolase ARH3 and suppresses DNA damage repair
inferred← citeshttps://doi.org/10.1074/mcp.tir119.001315openalex-snapshot
An Advanced Strategy for Comprehensive Profiling of ADP-ribosylation Sites Using Mass Spectrometry-based Proteomics*
inferred← citeshttps://doi.org/10.1080/10409238.2017.1394265openalex-snapshot
Specificity of reversible ADP-ribosylation and regulation of cellular processes
inferred← citeshttps://doi.org/10.1080/15548627.2024.2404375openalex-snapshot
Serine ubiquitination of SQSTM1 regulates NFE2L2-dependent redox homeostasis
inferred← citeshttps://doi.org/10.1093/nar/gkaa022openalex-snapshot
Poly(ADP-ribosyl)ation mediates early phase histone eviction at DNA lesions
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/gkae211openalex-snapshot
APLF facilitates interstrand DNA crosslink repair and replication fork protection to confer cisplatin resistance
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/gkaf1170openalex-snapshot
Histone PARylation factor 1: a review of its role in the DNA damage response
inferred← citeshttps://doi.org/10.1093/nar/gkx446openalex-snapshot
Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!
inferred← citeshttps://doi.org/10.1093/nar/gkz305openalex-snapshot
Reversible ADP-ribosylation of RNA
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/10.1093/narcan/zcae030openalex-snapshot
Intrinsic PARG inhibitor sensitivity is mimicked by TIMELESS haploinsufficiency and rescued by nucleoside supplementation
inferred← citeshttps://doi.org/10.1098/rsob.170076openalex-snapshot
Mitotic post-translational modifications of histones promote chromatin compaction in vitro
inferred← citeshttps://doi.org/10.1098/rsob.190041openalex-snapshot
ADP-ribosylation signalling and human disease
inferred← citeshttps://doi.org/10.1098/rsob.250181openalex-snapshot
Histidine and tyrosine residues are targets for SIRT6 ADP-ribosylation activity
inferred← citeshttps://doi.org/10.1101/2020.11.03.366401openalex-snapshot
Signalling Network of Breast Cancer Cells in Response to Progesterone
inferred← citeshttps://doi.org/10.1101/2022.02.17.480967openalex-snapshot
A protein semisynthesis-based strategy to probe the impact of site-specific serine ADP-ribosylation on linker histone function
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/10.1101/2024.08.28.610034openalex-snapshot
Single-nucleosome imaging reveals principles of transient multiscale chromatin unfolding triggered by histone ADP-ribosylation at DNA lesions
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/10.1101/2025.03.27.645734openalex-snapshot
A large-scale method to measure the absolute stoichiometries of protein Poly-ADP-Ribosylation
inferred← citeshttps://doi.org/10.1101/2025.05.19.654886openalex-snapshot
Phosphoribosyl ubiquitination of SNARE proteins regulate autophagy in Legionella infection
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/10.1101/2025.09.26.678909openalex-snapshot
Exercise-induced DNA damage response and memory formation in mice
inferred← citeshttps://doi.org/10.1101/gad.291518.116openalex-snapshot
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
inferred← citeshttps://doi.org/10.1101/gad.334631.119openalex-snapshot
(ADP-ribosyl)hydrolases: structure, function, and biology
inferred← citeshttps://doi.org/10.1101/gad.334730.119openalex-snapshot
Nuclear PARPs and genome integrity
inferred← citeshttps://doi.org/10.1107/s2059798326004158openalex-snapshot
Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome
inferred← citeshttps://doi.org/10.1111/febs.14078openalex-snapshot
ADP ‐ribosylation: new facets of an ancient modification
inferred← citeshttps://doi.org/10.1111/febs.15518openalex-snapshot
Progress and outlook in studying the substrate specificities of PARPs and related enzymes
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.70409openalex-snapshot
Automodification of N‐terminal serine residues facilitates PARP2 release from DNA
inferred← citeshttps://doi.org/10.1111/febs.70758openalex-snapshot
Dimerization of human PARP15 is required for NAD + binding and automodification
inferred← citeshttps://doi.org/10.1111/imb.12938openalex-snapshot
Effects of poly ( ADP ‐ribose) polymerase 1 ( PARP1 ) on silk proteins in the silkworm, Bombyx mori
inferred← citeshttps://doi.org/10.1126/sciadv.adi2687openalex-snapshot
PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities
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/s0006297918070040openalex-snapshot
The Regulatory Role of NAD in Human and Animal Cells
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/s1022795425700991openalex-snapshot
DNA Repair in Ensuring Genome Stability and Human Health
inferred← citeshttps://doi.org/10.1146/annurev-cancerbio-030518-055914openalex-snapshot
PARP Trapping Beyond Homologous Recombination and Platinum Sensitivity in Cancers
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