On the public citation graph

Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome

https://doi.org/10.1038/nmeth.2603
0 signed · 378 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

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

inferredcites →https://doi.org/10.1006/bbrc.2001.5115openalex-snapshot
Poly(ADP-Ribosyl)ation of Transcription Factor Yin Yang 1 under Conditions of DNA Damage
inferredcites →https://doi.org/10.1007/978-1-60327-261-2_12openalex-snapshot
Boronate Affinity Chromatography
inferredcites →https://doi.org/10.1016/0006-291x(63)90024-xopenalex-snapshot
Nicotinamide mononucleotide activation of a new DNA-dependent polyadenylic acid synthesizing nuclear enzyme
inferredcites →https://doi.org/10.1016/0022-2836(91)90027-4openalex-snapshot
Molecular recognition
inferredcites →https://doi.org/10.1016/j.cell.2010.12.001openalex-snapshot
A Tissue-Specific Atlas of Mouse Protein Phosphorylation and Expression
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.2010.06.017openalex-snapshot
The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets
inferredcites →https://doi.org/10.1016/j.molcel.2011.08.025openalex-snapshot
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
inferredcites →https://doi.org/10.1016/s0021-9258(18)32434-7openalex-snapshot
Amino acid-specific ADP-ribosylation.
inferredcites →https://doi.org/10.1021/ja906135dopenalex-snapshot
Identification of the ADP-Ribosylation Sites in the PARP-1 Automodification Domain: Analysis and Implications
inferredcites →https://doi.org/10.1021/pr301219hopenalex-snapshot
Mapping PARP-1 Auto-ADP-ribosylation Sites by Liquid Chromatography–Tandem Mass Spectrometry
inferredcites →https://doi.org/10.1038/nature03445openalex-snapshot
Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
inferredcites →https://doi.org/10.1038/nbt.2058openalex-snapshot
Re-evaluating PARP1 inhibitor in cancer
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/nbt1146openalex-snapshot
An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
inferredcites →https://doi.org/10.1038/ncb2222openalex-snapshot
RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling
inferredcites →https://doi.org/10.1038/nrc2812openalex-snapshot
PARP inhibition: PARP1 and beyond
inferredcites →https://doi.org/10.1038/nsmb.2335openalex-snapshot
The zinc-finger domains of PARP1 cooperate to recognize DNA strand breaks
inferredcites →https://doi.org/10.1073/pnas.0900066106openalex-snapshot
Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome
inferredcites →https://doi.org/10.1074/mcp.m900375-mcp200openalex-snapshot
A Dual Pressure Linear Ion Trap Orbitrap Instrument with Very High Sequencing Speed
inferredcites →https://doi.org/10.1126/science.1199484openalex-snapshot
Phosphoproteomic Analysis Identifies Grb10 as an mTORC1 Substrate That Negatively Regulates Insulin Signaling
inferredcites →https://doi.org/10.1126/science.1216338openalex-snapshot
Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1
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/10.1158/1078-0432.ccr-11-1973openalex-snapshot
Iniparib Nonselectively Modifies Cysteine-Containing Proteins in Tumor Cells and Is Not a Bona Fide PARP Inhibitor
inferredcites →https://doi.org/10.1158/1078-0432.ccr-11-2890openalex-snapshot
Failure of Iniparib to Inhibit Poly(ADP-Ribose) Polymerase In Vitro

What points at this work

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

inferred← citeshttps://doi.org/10.2139/ssrn.4677489openalex-extracted
inferred← citeshttps://doi.org/10.1002/9780470559277.ch140259openalex-snapshot
Identifying Direct Protein Targets of Poly‐ADP‐Ribose Polymerases (PARPs) Using Engineered PARP Variants—Orthogonal Nicotinamide Adenine Dinucleotide (NAD+) Analog Pairs
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.201404431openalex-snapshot
Kettenterminierende und durch Click‐Chemie modifizierbare NAD+‐Analoga zur Markierung von Zielproteinen der ADP‐Ribosyltransferasen
inferred← citeshttps://doi.org/10.1002/ange.201809059openalex-snapshot
Chemoproteomic Profiling of Phosphoaspartate Modifications in Prokaryotes
inferred← citeshttps://doi.org/10.1002/ange.202200977openalex-snapshot
Profiling of the ADP‐Ribosylome in Living Cells
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.201404431openalex-snapshot
Chain‐Terminating and Clickable NAD+ Analogues for Labeling the Target Proteins of ADP‐Ribosyltransferases
inferred← citeshttps://doi.org/10.1002/anie.201809059openalex-snapshot
Chemoproteomic Profiling of Phosphoaspartate Modifications in Prokaryotes
inferred← citeshttps://doi.org/10.1002/anie.202200977openalex-snapshot
Profiling of the ADP‐Ribosylome in Living Cells
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/bies.202200015openalex-snapshot
Joining the PARty: PARP Regulation of KDM5A during DNA Repair (and Transcription?)
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.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/em.22623openalex-snapshot
Poly‐ ADP ‐ribosylation dynamics, signaling, and analysis
inferred← citeshttps://doi.org/10.1002/jssc.201900804openalex-snapshot
Enrichments of post‐translational modifications in proteomic studies
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/10.1002/pmic.201400217openalex-snapshot
Proteomics approaches to identify mono‐(ADP‐ribosyl)ated and poly(ADP‐ribosyl)ated proteins
inferred← citeshttps://doi.org/10.1002/pmic.201600045openalex-snapshot
Tackling aspecific side reactions during histone propionylation: The promise of reversing overpropionylation
inferred← citeshttps://doi.org/10.1002/pmic.202200064openalex-snapshot
A field guide to the proteomics of post‐translational modifications in DNA repair
inferred← citeshttps://doi.org/10.1002/pmic.202200083openalex-snapshot
Impact of Asp/Glu‐ADP‐ribosylation on protein‐protein interaction and protein function
inferred← citeshttps://doi.org/10.1007/82_2014_424openalex-snapshot
Identification and Analysis of ADP-Ribosylated Proteins
inferred← citeshttps://doi.org/10.1007/978-1-0716-0802-9_11openalex-snapshot
Simultaneous, Quantitative Characterization of Protein ADP-Ribosylation and Protein Phosphorylation in Macrophages
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/10.1007/978-1-4939-6993-7_10openalex-snapshot
Identification of ADP-Ribose Acceptor Sites on In Vitro Modified Proteins by Liquid Chromatography–Tandem Mass Spectrometry
inferred← citeshttps://doi.org/10.1007/978-1-4939-6993-7_11openalex-snapshot
Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography–Tandem Mass Spectrometry
inferred← citeshttps://doi.org/10.1007/978-1-4939-6993-7_7openalex-snapshot
ADP-Ribosylated Peptide Enrichment and Site Identification: The Phosphodiesterase-Based Method
inferred← citeshttps://doi.org/10.1007/978-1-4939-6993-7_8openalex-snapshot
Using Clickable NAD+ Analogs to Label Substrate Proteins of PARPs
inferred← citeshttps://doi.org/10.1007/978-1-4939-6993-7_9openalex-snapshot
Identification of Protein Substrates of Specific PARP Enzymes Using Analog-Sensitive PARP Mutants and a “Clickable” NAD+ Analog
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_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/10.1007/978-3-319-14151-0_6openalex-snapshot
Multitasking Roles for Poly(ADP-ribosyl)ation in Aging and Longevity
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/s10142-023-01146-5openalex-snapshot
Recent advances in chromosome capture techniques unraveling 3D genome architecture in germ cells, health, and disease
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/s13361-015-1120-3openalex-snapshot
Crescendo: A Protein Sequence Database Search Engine for Tandem Mass Spectra
inferred← citeshttps://doi.org/10.1016/b978-0-08-100068-7.00015-xopenalex-snapshot
PARP proteins, NAD, epigenetics, antioxidative response to abiotic stress
inferred← citeshttps://doi.org/10.1016/b978-0-12-814208-0.00004-xopenalex-snapshot
Protein phase separation in cell death and survival
inferred← citeshttps://doi.org/10.1016/b978-0-323-91909-8.00019-0openalex-snapshot
Mechanisms of 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/j.apsb.2020.12.012openalex-snapshot
The poly(ADP-ribosyl)ation of BRD4 mediated by PARP1 promoted pathological cardiac hypertrophy
inferred← citeshttps://doi.org/10.1016/j.arr.2014.12.006openalex-snapshot
RecQ helicases and PARP1 team up in maintaining genome integrity
inferred← citeshttps://doi.org/10.1016/j.arr.2024.102347openalex-snapshot
ADP-ribosylation, a multifaceted modification: Functions and mechanisms in aging and aging-related diseases
inferred← citeshttps://doi.org/10.1016/j.bbrc.2022.06.085openalex-snapshot
Reversible acetylation modulates p54nrb/NONO-mediated expression of the interleukin 8 gene
inferred← citeshttps://doi.org/10.1016/j.bcp.2018.10.026openalex-snapshot
Poly(ADP-ribosylated) proteins in β-amyloid peptide-stimulated microglial cells
inferred← citeshttps://doi.org/10.1016/j.bcp.2019.05.007openalex-snapshot
Enabling drug discovery for the PARP protein family through the detection of mono-ADP-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.biochi.2015.03.016openalex-snapshot
Mechanistic overview of ADP-ribosylation reactions
inferred← citeshttps://doi.org/10.1016/j.bios.2019.05.013openalex-snapshot
A label-free PFP-based photoelectrochemical biosensor for highly sensitive detection of PARP-1 activity
inferred← citeshttps://doi.org/10.1016/j.bpc.2026.107678openalex-snapshot
Phase separation and protein aggregation in neurodegenerative diseases
inferred← citeshttps://doi.org/10.1016/j.burns.2024.03.014openalex-snapshot
Experimental evidence for Parthanatos-like mode of cell death of heat-damaged human skin fibroblasts in a cell culture-based in vitro burn model
inferred← citeshttps://doi.org/10.1016/j.canlet.2017.10.024openalex-snapshot
miR-342-3p suppresses cell proliferation and migration by targeting AGR2 in non-small cell lung cancer
inferred← citeshttps://doi.org/10.1016/j.canlet.2025.218213openalex-snapshot
HP1 enhances radio- and chemotherapy resistance in osteosarcoma via PARP1-dependent transcriptional repression and HR repair
inferred← citeshttps://doi.org/10.1016/j.cbpa.2014.10.002openalex-snapshot
Chemical reporters for exploring ADP-ribosylation and AMPylation at the host–pathogen interface
inferred← citeshttps://doi.org/10.1016/j.cbpa.2023.102402openalex-snapshot
Immunomodulatory roles of PARPs: Shaping the tumor microenvironment, one ADP-ribose at a time
inferred← citeshttps://doi.org/10.1016/j.cell.2015.10.040openalex-snapshot
The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei
inferred← citeshttps://doi.org/10.1016/j.celrep.2015.12.045openalex-snapshot
Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach
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.2018.07.038openalex-snapshot
RUNX Poly(ADP-Ribosyl)ation and BLM Interaction Facilitate the Fanconi Anemia Pathway of DNA Repair
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.2020.108176openalex-snapshot
Mapping Physiological ADP-Ribosylation Using Activated Ion Electron Transfer Dissociation
inferred← citeshttps://doi.org/10.1016/j.celrep.2021.109695openalex-snapshot
PARP1-mediated PARylation activity is essential for oligodendroglial differentiation and CNS myelination
inferred← citeshttps://doi.org/10.1016/j.celrep.2022.111089openalex-snapshot
DDX18 prevents R-loop-induced DNA damage and genome instability via PARP-1
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.2023.113199openalex-snapshot
FUS RRM regulates poly(ADP-ribose) levels after transcriptional arrest and PARP-1 activation on DNA damage
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.2025.115737openalex-snapshot
ADP-ribosylation of NuMA promotes DNA single-strand break repair and transcription
inferred← citeshttps://doi.org/10.1016/j.chembiol.2015.03.007openalex-snapshot
Extracellular Poly(ADP-Ribose) Is a Pro-inflammatory Signal for Macrophages
inferred← citeshttps://doi.org/10.1016/j.chembiol.2021.02.004openalex-snapshot
Avoid the trap: Targeting PARP1 beyond human malignancy
inferred← citeshttps://doi.org/10.1016/j.dnarep.2015.02.004openalex-snapshot
Quantitative site-specific ADP-ribosylation profiling of DNA-dependent PARPs
inferred← citeshttps://doi.org/10.1016/j.dnarep.2017.02.002openalex-snapshot
Cell-type specific role of the RNA-binding protein, NONO, in the DNA double-strand break response in the mouse testes
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.2021.103125openalex-snapshot
PARP1: Structural insights and pharmacological targets for inhibition
inferred← citeshttps://doi.org/10.1016/j.dnarep.2021.103144openalex-snapshot
ADP-ribosylation of DNA and RNA
inferred← citeshttps://doi.org/10.1016/j.dnarep.2022.103382openalex-snapshot
The fast-growing business of Serine ADP-ribosylation
inferred← citeshttps://doi.org/10.1016/j.dnarep.2025.103824openalex-snapshot
Targeting dePARylation in 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.euprot.2014.06.004openalex-snapshot
A proteomics approach for the development of sarcoma biomarkers
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2024.139046openalex-snapshot
Poly(ADP-ribose) polymerase FonPARP1-catalyzed PARylation of protein disulfide isomerase FonPdi1 regulates pathogenicity of Fusarium oxysporum f. sp. niveum on watermelon
inferred← citeshttps://doi.org/10.1016/j.isci.2024.111252openalex-snapshot
SART1 modulates poly-(ADP-ribose) chain accumulation and PARP1 chromatin localization
inferred← citeshttps://doi.org/10.1016/j.jare.2025.11.038openalex-snapshot
ZUP1 promotes DNA repair and immune evasion to drive olaparib resistance in triple-negative breast cancer
inferred← citeshttps://doi.org/10.1016/j.jbc.2021.100309openalex-snapshot
Poly(ADP-ribose) polymerase 1 regulates mitochondrial DNA repair in an NAD-dependent manner
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.jbc.2025.108551openalex-snapshot
NUDT16 enhances the resistance of cancer cells to DNA-damaging agents by regulating replication fork stability via reversing HMGA1 ADP-ribosylation
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.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.2015.01.037openalex-snapshot
RNA Regulation by Poly(ADP-Ribose) Polymerases
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.04.016openalex-snapshot
Chromatin to Clinic: The Molecular Rationale for PARP1 Inhibitor Function
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.2015.06.006openalex-snapshot
PARPs and ADP-Ribosylation: 50 Years … and Counting
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.06.012openalex-snapshot
The Promise of Proteomics for the Study of ADP-Ribosylation
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.2016.07.006openalex-snapshot
Identification of PARP-Specific ADP-Ribosylation Targets Reveals a Regulatory Function for ADP-Ribosylation in Transcription Elongation
inferred← citeshttps://doi.org/10.1016/j.molcel.2016.11.015openalex-snapshot
PARP-1 Controls the Adipogenic Transcriptional Program by PARylating C/EBPβ and Modulating Its Transcriptional Activity
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.2017.04.028openalex-snapshot
Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9
inferred← citeshttps://doi.org/10.1016/j.molcel.2018.12.022openalex-snapshot
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
inferred← citeshttps://doi.org/10.1016/j.molcel.2020.08.002openalex-snapshot
Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis
inferred← citeshttps://doi.org/10.1016/j.molcel.2022.02.021openalex-snapshot
The expanding universe of PARP1-mediated molecular and therapeutic mechanisms
inferred← citeshttps://doi.org/10.1016/j.molcel.2022.03.034openalex-snapshot
Cytoplasmic PARP1 links the genome instability to the inhibition of antiviral immunity through PARylating cGAS
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.molp.2021.08.013openalex-snapshot
Coordinated regulation of plant immunity by poly(ADP-ribosyl)ation and K63-linked ubiquitination
inferred← citeshttps://doi.org/10.1016/j.plantsci.2026.113021openalex-snapshot
An AT-hook motif nuclear protein AHL13 interacts with Poly(ADP-ribose) to regulate Arabidopsis immunity
inferred← citeshttps://doi.org/10.1016/j.semcdb.2016.09.009openalex-snapshot
Expanding functions of ADP-ribosylation in the maintenance of genome integrity
inferred← citeshttps://doi.org/10.1016/j.semradonc.2016.06.001openalex-snapshot
Translation of Targeted Radiation Sensitizers into Clinical Trials
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/10.1021/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.analchem.9b04651openalex-snapshot
Recent Advances in Glycoproteomic Analysis by Mass Spectrometry
inferred← citeshttps://doi.org/10.1021/acs.biochem.7b00670openalex-snapshot
Generation and Characterization of Recombinant Antibody-like ADP-Ribose Binding Proteins
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.chemrestox.6c00176openalex-snapshot
The Expanding Landscape of ADP-Ribosylation: Protein, DNA, RNA, and Mitochondrial Regulation
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.joc.3c00827openalex-snapshot
Four of a Kind: A Complete Collection of ADP-Ribosylated Histidine Isosteres Using Cu(I)- and Ru(II)-Catalyzed Click Chemistry
inferred← citeshttps://doi.org/10.1021/acs.jproteome.0c00261openalex-snapshot
Dynamic ADP-Ribosylome, Phosphoproteome, and Interactome in LPS-Activated Macrophages
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.5b00432openalex-snapshot
Optimization of LTQ-Orbitrap Mass Spectrometer Parameters for the Identification of ADP-Ribosylation Sites
inferred← citeshttps://doi.org/10.1021/acs.jproteome.5b00819openalex-snapshot
Quantitative Secretomic Analysis Identifies Extracellular Protein Factors That Modulate the Metastatic Phenotype of Non-Small Cell Lung Cancer
inferred← citeshttps://doi.org/10.1021/acs.jproteome.5b00865openalex-snapshot
Universal Solid-Phase Reversible Sample-Prep for Concurrent Proteome and N-Glycome Characterization
inferred← citeshttps://doi.org/10.1021/acs.jproteome.6b00511openalex-snapshot
Metrics for the Human Proteome Project 2016: Progress on Identifying and Characterizing the Human Proteome, Including 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.jproteome.9b00696openalex-snapshot
Ion-Pairing with Triethylammonium Acetate Improves Solid-Phase Extraction of ADP-Ribosylated 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.3c00305openalex-snapshot
Synthetic Dual Cysteine-ADP Ribosylated Peptides from the Androgen Receptor are Recognized by the DTX3L/PARP9 Complex
inferred← citeshttps://doi.org/10.1021/acschembio.5b00213openalex-snapshot
A Clickable Aminooxy Probe for Monitoring Cellular ADP-Ribosylation
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.5c01021openalex-snapshot
Noncovalent PAR Binding Guides Proteins to PARP1-Mediated PARylation
inferred← citeshttps://doi.org/10.1021/cr5004248openalex-snapshot
New Facets in the Regulation of Gene Expression by ADP-Ribosylation and Poly(ADP-ribose) Polymerases
inferred← citeshttps://doi.org/10.1021/cr500491uopenalex-snapshot
Quantitative Proteomic Analysis of Histone Modifications
inferred← citeshttps://doi.org/10.1021/ja412897aopenalex-snapshot
Engineering the Substrate Specificity of ADP-Ribosyltransferases for Identifying Direct Protein Targets
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.6b12866openalex-snapshot
Aspartate Glycosylation Triggers Isomerization to Isoaspartate
inferred← citeshttps://doi.org/10.1021/jacs.6c02874openalex-snapshot
Deciphering the Specificity of Reversible DNA-Phosphate ADP-Ribosylation via the Precise Synthesis and Enzymatic Profiling of Nucleotide-Phospho-ADP-Ribosyl Probes
inferred← citeshttps://doi.org/10.1021/pr401032qopenalex-snapshot
Phosphoproteomic Approach to Characterize Protein Mono- and Poly(ADP-ribosyl)ation Sites from Cells
inferred← citeshttps://doi.org/10.1038/nbt.3267openalex-snapshot
A mass-tolerant database search identifies a large proportion of unassigned spectra in shotgun proteomics as modified peptides
inferred← citeshttps://doi.org/10.1038/ncb3311openalex-snapshot
Secreted IGFBP5 mediates mTORC1-dependent feedback inhibition of IGF-1 signalling
inferred← citeshttps://doi.org/10.1038/nchembio.2280openalex-snapshot
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress
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/ncomms12404openalex-snapshot
PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2BGlu2
inferred← citeshttps://doi.org/10.1038/ncomms12917openalex-snapshot
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
inferred← citeshttps://doi.org/10.1038/ncomms5426openalex-snapshot
Family-wide analysis of poly(ADP-ribose) polymerase activity
inferred← citeshttps://doi.org/10.1038/onc.2014.295openalex-snapshot
The role of poly(ADP-ribosyl)ation in DNA damage response and cancer chemotherapy
inferred← citeshttps://doi.org/10.1038/onc.2017.311openalex-snapshot
EZH2 contributes to the response to PARP inhibitors through its PARP-mediated poly-ADP ribosylation in breast cancer
inferred← citeshttps://doi.org/10.1038/s12276-024-01322-yopenalex-snapshot
CBL-b E3 ligase-mediated neddylation and activation of PARP-1 induce vascular calcification
inferred← citeshttps://doi.org/10.1038/s41388-018-0568-6openalex-snapshot
Oncogenic activity of poly (ADP-ribose) glycohydrolase
inferred← citeshttps://doi.org/10.1038/s41388-024-03207-wopenalex-snapshot
Enhancing low-dose radiotherapy efficacy with PARP inhibitors via FBL-mediated oxidative stress response in colorectal cancer
inferred← citeshttps://doi.org/10.1038/s41418-022-01024-wopenalex-snapshot
BAP1 promotes the repair of UV-induced DNA damage via PARP1-mediated recruitment to damage sites and control of activity and stability
inferred← citeshttps://doi.org/10.1038/s41419-024-06595-9openalex-snapshot
RNF166 promotes colorectal cancer progression by recognizing and destabilizing poly-ADP-ribosylated angiomotins
inferred← citeshttps://doi.org/10.1038/s41421-021-00355-1openalex-snapshot
Truncated PARP1 mediates ADP-ribosylation of RNA polymerase III for apoptosis
inferred← citeshttps://doi.org/10.1038/s41422-019-0141-zopenalex-snapshot
PARylation regulates stress granule dynamics, phase separation, and neurotoxicity of disease-related RNA-binding proteins
inferred← citeshttps://doi.org/10.1038/s41467-018-04466-4openalex-snapshot
Coupling bimolecular PARylation biosensors with genetic screens to identify PARylation targets
inferred← citeshttps://doi.org/10.1038/s41467-018-06111-6openalex-snapshot
Mutant FUS causes DNA ligation defects to inhibit oxidative damage repair in Amyotrophic Lateral Sclerosis
inferred← citeshttps://doi.org/10.1038/s41467-019-08530-5openalex-snapshot
NADP+ is an endogenous PARP inhibitor in DNA damage response and tumor suppression
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/s41467-019-10741-9openalex-snapshot
Poly(ADP-ribose) polymerase-1 antagonizes DNA resection at double-strand breaks
inferred← citeshttps://doi.org/10.1038/s41467-019-12377-1openalex-snapshot
Tankyrase disrupts metabolic homeostasis and promotes tumorigenesis by inhibiting LKB1-AMPK signalling
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/s41467-020-19409-1openalex-snapshot
Biomimetic α-selective ribosylation enables two-step modular synthesis of biologically important ADP-ribosylated peptides
inferred← citeshttps://doi.org/10.1038/s41467-021-23055-6openalex-snapshot
Androgen signaling uses a writer and a reader of ADP-ribosylation to regulate protein complex assembly
inferred← citeshttps://doi.org/10.1038/s41467-021-24225-2openalex-snapshot
Nuclear ADP-ribosylation drives IFNγ-dependent STAT1α enhancer formation in macrophages
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/s41467-024-48314-0openalex-snapshot
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
inferred← citeshttps://doi.org/10.1038/s41467-024-50158-7openalex-snapshot
PARG is essential for Polθ-mediated DNA end-joining by removing repressive poly-ADP-ribose marks
inferred← citeshttps://doi.org/10.1038/s41467-024-51955-wopenalex-snapshot
PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae
inferred← citeshttps://doi.org/10.1038/s41467-026-73677-xopenalex-snapshot
Deciphering cytokine-driven ADP-ribosylation signaling networks via Af1521-based mass spectrometry analysis of labile Glu/Asp-linkages
inferred← citeshttps://doi.org/10.1038/s41556-024-01463-2openalex-snapshot
Full-length GSDME mediates pyroptosis independent from cleavage
inferred← citeshttps://doi.org/10.1038/s41589-019-0379-2openalex-snapshot
Uncoupling of PARP1 trapping and inhibition using selective PARP1 degradation
inferred← citeshttps://doi.org/10.1038/s41598-018-25137-wopenalex-snapshot
Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
inferred← citeshttps://doi.org/10.1038/s41598-019-39969-7openalex-snapshot
PARP1 is a versatile factor in the regulation of mRNA stability and decay
inferred← citeshttps://doi.org/10.1038/s41598-019-43154-1openalex-snapshot
An Integrated Chemical Proteomics Approach for Quantitative Profiling of Intracellular ADP-Ribosylation
inferred← citeshttps://doi.org/10.1038/s42003-022-04241-8openalex-snapshot
Poly ADP-ribosylation of SET8 leads to aberrant H4K20 methylation in mammalian nuclear genome
inferred← citeshttps://doi.org/10.1038/s42003-023-04794-2openalex-snapshot
Poly(ADP-ribose)-binding protein RCD1 is a plant PARylation reader regulated by Photoregulatory Protein Kinases
inferred← citeshttps://doi.org/10.1038/s42255-021-00456-xopenalex-snapshot
The alternative activity of nuclear PHGDH contributes to tumour growth under nutrient stress
inferred← citeshttps://doi.org/10.1038/s42255-024-01162-0openalex-snapshot
Cryptic phosphoribosylase activity of NAMPT restricts the virion incorporation of viral proteins
inferred← citeshttps://doi.org/10.1038/srep18271openalex-snapshot
Nudix hydrolases degrade protein-conjugated ADP-ribose
inferred← citeshttps://doi.org/10.1038/srep41746openalex-snapshot
The conserved macrodomains of the non-structural proteins of Chikungunya virus and other pathogenic positive strand RNA viruses function as mono-ADP-ribosylhydrolases
inferred← citeshttps://doi.org/10.1038/srep43750openalex-snapshot
Site-specific ADP-ribosylation of histone H2B in response to DNA double strand breaks
inferred← citeshttps://doi.org/10.1039/c4cs00529eopenalex-snapshot
Fishing the PTM proteome with chemical approaches using functional solid phases
inferred← citeshttps://doi.org/10.1039/c5cc04170hopenalex-snapshot
A poly(ADP-ribose) polymerase-1 activity assay based on the FRET between a cationic conjugated polymer and supercharged green fluorescent protein
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/d0sc06226jopenalex-snapshot
A tailored phosphoaspartate probe unravels CprR as a response regulator in Pseudomonas aeruginosa interkingdom signaling
inferred← citeshttps://doi.org/10.1039/d4cb00043aopenalex-snapshot
Chemical tools for profiling the intracellular ADP-ribosylated proteome
inferred← citeshttps://doi.org/10.1042/bcj20160797openalex-snapshot
The role of mass spectrometry analysis in bacterial effector characterization
inferred← citeshttps://doi.org/10.1042/bcj20180347openalex-snapshot
Characterization of TCDD-inducible poly-ADP-ribose polymerase (TIPARP/ARTD14) catalytic activity
inferred← citeshttps://doi.org/10.1042/bcj20180548openalex-snapshot
Two active site arginines are critical determinants of substrate binding and catalysis in MenD: a thiamine-dependent enzyme in menaquinone biosynthesis
inferred← citeshttps://doi.org/10.1042/bcj20230230openalex-snapshot
Regulation of PARP1/2 and the tankyrases: emerging parallels
inferred← citeshttps://doi.org/10.1042/bj20141554openalex-snapshot
Processing of protein ADP-ribosylation by Nudix hydrolases
showing the first 200 of 353 · page through all 353
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.