On the public citation graph
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
0 signed · 284 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.
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known work and none has been retracted — and get a dated CiteStamped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.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1007/978-1-61779-270-0_1openalex-snapshot
Approaches to Detect PARP-1 Activation In Vivo, In Situ, and In Vitro
inferredcites →https://doi.org/10.1007/bf00928465openalex-snapshot
Enzymatic and nonenzymatic ADP-ribosylation of cysteine
inferredcites →https://doi.org/10.1016/0014-5793(87)81129-8openalex-snapshot
Clostridium perfringens iota toxin ADP‐ribosylates skeletal muscle actin in Arg‐177
inferredcites →https://doi.org/10.1016/j.cbpa.2012.12.009openalex-snapshot
Advances in characterizing ubiquitylation sites by mass spectrometry
inferredcites →https://doi.org/10.1016/j.cell.2010.08.016openalex-snapshot
Poly(ADP-Ribose) Polymerase 1 Participates in the Phase Entrainment of Circadian Clocks to Feeding
inferredcites →https://doi.org/10.1016/j.cmet.2011.03.004openalex-snapshot
PARP-1 Inhibition Increases Mitochondrial Metabolism through SIRT1 Activation
inferredcites →https://doi.org/10.1016/j.cmet.2012.06.016openalex-snapshot
The Role of PARP-1 and PARP-2 Enzymes in Metabolic Regulation and Disease
inferredcites →https://doi.org/10.1016/j.febslet.2011.03.045openalex-snapshot
Compartmentation of NAD+‐dependent signalling
inferredcites →https://doi.org/10.1016/j.freeradbiomed.2006.09.025openalex-snapshot
Role of poly(ADP-ribose) glycohydrolase in the development of inflammatory bowel disease in mice
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.jasms.2005.01.015openalex-snapshot
Electron transfer dissociation of peptide anions
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.2011.02.019openalex-snapshot
Small Molecules, Big Effects: A Role for Chromatin-Localized Metabolite Biosynthesis in Gene Regulation
inferredcites →https://doi.org/10.1016/j.molcel.2012.05.042openalex-snapshot
Sequential Posttranslational Modifications Program FEN1 Degradation during Cell-Cycle Progression
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.2015.06.012openalex-snapshot
The Promise of Proteomics for the Study of ADP-Ribosylation
inferredcites →https://doi.org/10.1016/j.molcel.2015.06.013openalex-snapshot
Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens
inferredcites →https://doi.org/10.1016/j.molcel.2015.12.025openalex-snapshot
Analysis of Chromatin ADP-Ribosylation at the Genome-wide Level and at Specific Loci by ADPr-ChAP
inferredcites →https://doi.org/10.1016/j.tibs.2009.12.003openalex-snapshot
Toward a unified nomenclature for mammalian ADP-ribosyltransferases
inferredcites →https://doi.org/10.1016/j.yexcr.2004.03.050openalex-snapshot
Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice variants yielding isoforms that localize to different cell compartments
inferredcites →https://doi.org/10.1016/s0021-9258(18)43353-4openalex-snapshot
Amino acid-specific ADP-ribosylation. Identification of an arginine-dependent ADP-ribosyltransferase in rat liver.
inferredcites →https://doi.org/10.1016/s0092-8674(03)00433-1openalex-snapshot
PARP Goes Transcription
inferredcites →https://doi.org/10.1016/s1097-2765(01)00272-6openalex-snapshot
Regulation of Human Flap Endonuclease-1 Activity by Acetylation through the Transcriptional Coactivator p300
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/cb400170bopenalex-snapshot
Quantification of Cellular Poly(ADP-ribosyl)ation by Stable Isotope Dilution Mass Spectrometry Reveals Tissue- and Drug-Dependent Stress Response Dynamics
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/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/10.1021/pr9006365openalex-snapshot
Repeatability and Reproducibility in Proteomic Identifications by Liquid Chromatography−Tandem Mass Spectrometry
inferredcites →https://doi.org/10.1038/322390a0openalex-snapshot
Botulinum C2 toxin ADP-ribosylates actin
inferredcites →https://doi.org/10.1038/emboj.2009.206openalex-snapshot
PARP is activated at stalled forks to mediate Mre11‐dependent replication restart and recombination
inferredcites →https://doi.org/10.1038/nature10404openalex-snapshot
The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase
inferredcites →https://doi.org/10.1038/nature11005openalex-snapshot
Systematic identification of genomic markers of drug sensitivity in cancer cells
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/ncb2222openalex-snapshot
RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling
inferredcites →https://doi.org/10.1038/ncb2593openalex-snapshot
PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response
inferredcites →https://doi.org/10.1038/ncomms5426openalex-snapshot
Family-wide analysis of poly(ADP-ribose) polymerase activity
inferredcites →https://doi.org/10.1038/nmeth.2603openalex-snapshot
Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
inferredcites →https://doi.org/10.1038/nrmicro1150openalex-snapshot
Bacterial cytotoxins: targeting eukaryotic switches
inferredcites →https://doi.org/10.1038/nsmb.2521openalex-snapshot
Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases
inferredcites →https://doi.org/10.1038/nsmb.2523openalex-snapshot
A family of macrodomain proteins reverses cellular mono-ADP-ribosylation
inferredcites →https://doi.org/10.1038/sj.emboj.7600664openalex-snapshot
The macro domain is an ADP‐ribose binding module
inferredcites →https://doi.org/10.1073/pnas.0409536102openalex-snapshot
Stable isotope-free relative and absolute quantitation of protein phosphorylation stoichiometry by MS
inferredcites →https://doi.org/10.1073/pnas.0606528103openalex-snapshot
Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death
inferredcites →https://doi.org/10.1073/pnas.1012946107openalex-snapshot
A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage
inferredcites →https://doi.org/10.1073/pnas.2237114100openalex-snapshot
Loss of poly(ADP-ribose) glycohydrolase causes progressive neurodegeneration in Drosophila melanogaster
inferredcites →https://doi.org/10.1074/jbc.271.18.10461openalex-snapshot
Glycation and Glycoxidation of Histones by ADP-ribose
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/10.1074/mcp.m800258-mcp200openalex-snapshot
Comparative Proteomic Phenotyping of Cell Lines and Primary Cells to Assess Preservation of Cell Type-specific Functions
inferredcites →https://doi.org/10.1074/mcp.o113.034181openalex-snapshot
Status of Large-scale Analysis of Post-translational Modifications by Mass Spectrometry
inferredcites →https://doi.org/10.1093/carcin/bgq205openalex-snapshot
Deletion of the nuclear isoform of poly(ADP-ribose) glycohydrolase (PARG) reveals its function in DNA repair, genomic stability and tumorigenesis
inferredcites →https://doi.org/10.1093/nar/gkp229openalex-snapshot
Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
inferredcites →https://doi.org/10.1093/nar/gkq463openalex-snapshot
PARP1 ADP-ribosylates lysine residues of the core histone tails
inferredcites →https://doi.org/10.1093/nar/gks1262openalex-snapshot
The Proteomics Identifications (PRIDE) database and associated tools: status in 2013
inferredcites →https://doi.org/10.1093/nar/gks673openalex-snapshot
Kinetics of endogenous mouse FEN1 in base excision repair
inferredcites →https://doi.org/10.1093/nar/gku1003openalex-snapshot
STRING v10: protein–protein interaction networks, integrated over the tree of life
inferredcites →https://doi.org/10.1093/nar/gkw442openalex-snapshot
PKCα and HMGB1 antagonistically control hydrogen peroxide-induced poly-ADP-ribose formation
inferredcites →https://doi.org/10.1101/gad.2021311openalex-snapshot
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
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/10.1126/science.aaf7865openalex-snapshot
Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation
inferredcites →https://doi.org/10.1126/scisignal.2000475openalex-snapshot
Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis
inferredcites →https://doi.org/10.1128/mcb.24.16.7163-7178.2004openalex-snapshot
Depletion of the 110-Kilodalton Isoform of Poly(ADP-Ribose) Glycohydrolase Increases Sensitivity to Genotoxic and Endotoxic Stress in Mice
inferredcites →https://doi.org/10.1186/1478-811x-11-5openalex-snapshot
ARTD10 substrate identification on protein microarrays: regulation of GSK3β by mono-ADP-ribosylation
inferredcites →https://doi.org/10.1210/er.2009-0026openalex-snapshot
The Secret Life of NAD+: An Old Metabolite Controlling New Metabolic Signaling Pathways
inferredcites →https://doi.org/10.3390/cells4040569openalex-snapshot
Intracellular Mono-ADP-Ribosylation in Signaling and Disease
inferredcites →https://doi.org/10.4049/jimmunol.1401677openalex-snapshot
Nucleotide-Induced Membrane-Proximal Proteolysis Controls the Substrate Specificity of T Cell Ecto–ADP-Ribosyltransferase ARTC2.2
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/1878-0261.70317openalex-snapshot
ADP ‐ribosylation: An emerging regulator of the epigenome
inferred← citeshttps://doi.org/10.1002/ange.202200977openalex-snapshot
Profiling of the ADP‐Ribosylome in Living Cells
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.202200977openalex-snapshot
Profiling of the ADP‐Ribosylome in Living Cells
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/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/jbmr.3927openalex-snapshot
PARP1 Hinders Histone H2B Occupancy at the NFATc1 Promoter to Restrain Osteoclast Differentiation
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/pld3.70115openalex-snapshot
Untargeted Proteomics Identifies Plant Substrates of the Bacterial‐Derived ADP‐Ribosyltransferase AvrRpm1
inferred← citeshttps://doi.org/10.1002/rcm.9961openalex-snapshot
In‐Source Collision‐Induced Dissociation (CID) Improves Higher‐Energy Collisional Dissociation (HCD)‐Dependent Fragmentation of ADP‐Ribosyl Peptides
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_7openalex-snapshot
Subcellular Quantitation of ADP-Ribosylation by High-Content Microscopy
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/10.1007/978-1-4939-8588-3_10openalex-snapshot
Mono-ADP-Ribosylation Catalyzed by Arginine-Specific ADP-Ribosyltransferases
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_7openalex-snapshot
Generating Protein-Linked and Protein-Free Mono-, Oligo-, and Poly(ADP-Ribose) In Vitro
inferred← citeshttps://doi.org/10.1007/978-1-4939-9195-2_9openalex-snapshot
Detection of ADP-Ribosylation of the Androgen Receptor Using the Recombinant Macrodomain AF1521 from Archaeoglobus fulgidus
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/s42764-022-00073-2openalex-snapshot
DNA-PKcs post-translational modifications and associated diseases
inferred← citeshttps://doi.org/10.1016/b978-0-12-821618-7.00067-5openalex-snapshot
Posttranslational Modifications: Key Players in Health and Disease
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.ab.2020.113793openalex-snapshot
Accurate prediction of species-specific 2-hydroxyisobutyrylation sites based on machine learning frameworks
inferred← citeshttps://doi.org/10.1016/j.arr.2024.102206openalex-snapshot
PARP1 at the crossroad of cellular senescence and nucleolar processes
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.bpc.2026.107678openalex-snapshot
Phase separation and protein aggregation in neurodegenerative diseases
inferred← citeshttps://doi.org/10.1016/j.cell.2019.06.007openalex-snapshot
A Bacterial Effector Reveals the V-ATPase-ATG16L1 Axis that Initiates Xenophagy
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.2019.01.083openalex-snapshot
NR4A Nuclear Receptors Target Poly-ADP-Ribosylated DNA-PKcs Protein to Promote DNA Repair
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.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.2021.02.004openalex-snapshot
Avoid the trap: Targeting PARP1 beyond human malignancy
inferred← citeshttps://doi.org/10.1016/j.coisb.2018.05.002openalex-snapshot
Proteomic tools to study drug function
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.2024.103690openalex-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.2025.103845openalex-snapshot
Overexpression of the WWE domain of RNF146 modulates poly-(ADP)-ribose dynamics at sites of DNA damage
inferred← citeshttps://doi.org/10.1016/j.isci.2021.102432openalex-snapshot
MyoD induces ARTD1 and nucleoplasmic poly-ADP-ribosylation during fibroblast to myoblast transdifferentiation
inferred← citeshttps://doi.org/10.1016/j.jbc.2021.101141openalex-snapshot
Ribosylation of the CD8αβ heterodimer permits binding of the nonclassical major histocompatibility molecule, H2-Q10
inferred← citeshttps://doi.org/10.1016/j.jbc.2024.107838openalex-snapshot
Reversal of tyrosine-linked ADP-ribosylation by ARH3 and PARG
inferred← citeshttps://doi.org/10.1016/j.jmb.2019.12.019openalex-snapshot
Role of PARP-catalyzed ADP-ribosylation in the Crosstalk Between DNA Strand Breaks and Epigenetic Regulation
inferred← citeshttps://doi.org/10.1016/j.mam.2021.101053openalex-snapshot
Biochemical genesis of enzymatic and non-enzymatic post-translational modifications
inferred← citeshttps://doi.org/10.1016/j.mcpro.2023.100538openalex-snapshot
MSFragger-Labile: A Flexible Method to Improve Labile PTM Analysis in Proteomics
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.2018.12.022openalex-snapshot
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
inferred← citeshttps://doi.org/10.1016/j.molcel.2020.12.034openalex-snapshot
Mitochondrial NAD+ Controls Nuclear ARTD1-Induced ADP-Ribosylation
inferred← citeshttps://doi.org/10.1016/j.molcel.2021.08.037openalex-snapshot
Reading ADP-ribosylation signaling using chemical biology and interaction proteomics
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.2026.09.027openalex-snapshot
A feedback mechanism of m6A via PARP1-mediated ADP ribosylation of METTL3/METTL14
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.tcb.2020.02.002openalex-snapshot
Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation
inferred← citeshttps://doi.org/10.1016/j.xhgg.2024.100386openalex-snapshot
An ADPRS variant disrupts ARH3 stability and subcellular localization in children with neurodegeneration and respiratory failure
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.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.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.0c00261openalex-snapshot
Dynamic ADP-Ribosylome, Phosphoproteome, and Interactome in LPS-Activated Macrophages
inferred← citeshttps://doi.org/10.1021/acs.jproteome.0c00923openalex-snapshot
Establishment of a Mass-Spectrometry-Based Method for the Identification of the In Vivo Whole Blood and Plasma ADP-Ribosylomes
inferred← citeshttps://doi.org/10.1021/acs.jproteome.2c00850openalex-snapshot
Automated Enrichment of Phosphotyrosine Peptides for High-Throughput Proteomics
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/acschembio.1c00542openalex-snapshot
Rapid Analysis of ADP-Ribosylation Dynamics and Site-Specificity Using TLC-MALDI
inferred← citeshttps://doi.org/10.1021/acschembio.5c01021openalex-snapshot
Noncovalent PAR Binding Guides Proteins to PARP1-Mediated PARylation
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/jacs.6b12866openalex-snapshot
Aspartate Glycosylation Triggers Isomerization to Isoaspartate
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/10.1021/jasms.3c00129openalex-snapshot
A Combined Gas-Phase Separation Strategy for ADP-ribosylated Peptides
inferred← citeshttps://doi.org/10.1038/nprot.2017.072openalex-snapshot
ADP-ribose-specific chromatin-affinity purification for investigating genome-wide or locus-specific chromatin ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/nsmb.3366openalex-snapshot
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation
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/s41467-017-02253-1openalex-snapshot
Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
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/s41467-020-18981-wopenalex-snapshot
Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins
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/s41467-021-21540-6openalex-snapshot
System-wide identification and prioritization of enzyme substrates by thermal analysis
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/s41467-023-38793-yopenalex-snapshot
Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
inferred← citeshttps://doi.org/10.1038/s41467-023-39828-0openalex-snapshot
Detecting diagnostic features in MS/MS spectra of post-translationally modified peptides
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/s41467-023-44209-8openalex-snapshot
Covalent PARylation of DNA base excision repair proteins regulates DNA demethylation
inferred← citeshttps://doi.org/10.1038/s41467-025-56085-5openalex-snapshot
CHD6 has poly(ADP-ribose)- and DNA-binding domains and regulates PARP1/2-trapping inhibitor sensitivity via abasic site repair
inferred← citeshttps://doi.org/10.1038/s41467-025-62410-9openalex-snapshot
MacroD1 sustains mitochondrial integrity and oxidative metabolism
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/s41589-018-0097-1openalex-snapshot
Acetylation blocks DNA damage–induced chromatin ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/s41594-020-0412-xopenalex-snapshot
Tickling PARPs into serine action
inferred← citeshttps://doi.org/10.1038/s41598-017-16613-wopenalex-snapshot
Ecto-ADP-ribosyltransferase ARTC2.1 functionally modulates FcγR1 and FcγR2B on murine microglia
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/s41598-019-43154-1openalex-snapshot
An Integrated Chemical Proteomics Approach for Quantitative Profiling of Intracellular ADP-Ribosylation
inferred← citeshttps://doi.org/10.1038/s42003-021-02439-wopenalex-snapshot
MacroGreen, a simple tool for detection of ADP-ribosylated proteins
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/s44318-025-00391-7openalex-snapshot
Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose
inferred← citeshttps://doi.org/10.1038/s44318-025-00545-7openalex-snapshot
PARP7 is a proteotoxic stress sensor that labels proteins for degradation
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/10.1039/c7mb00498bopenalex-snapshot
The nucleosomal surface is the main target of histone ADP-ribosylation in response to DNA damage
inferred← citeshttps://doi.org/10.1039/d4cb00043aopenalex-snapshot
Chemical tools for profiling the intracellular ADP-ribosylated proteome
inferred← citeshttps://doi.org/10.1042/bcj20230230openalex-snapshot
Regulation of PARP1/2 and the tankyrases: emerging parallels
inferred← citeshttps://doi.org/10.1042/bst20180418openalex-snapshot
PARPs in genome stability and signal transduction: implications for cancer therapy
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/10.1071/fp19159openalex-snapshot
The function of KptA/Tpt1 gene – a minor review
inferred← citeshttps://doi.org/10.1073/pnas.2426660122openalex-snapshot
PARP12-mediated mono-ADP-ribosylation as a checkpoint for necroptosis and apoptosis
inferred← citeshttps://doi.org/10.1074/jbc.ra118.006159openalex-snapshot
Defining the NSD2 interactome: PARP1 PARylation reduces NSD2 histone methyltransferase activity and impedes chromatin binding
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.o116.065623openalex-snapshot
New Quantitative Mass Spectrometry Approaches Reveal Different ADP-ribosylation Phases Dependent On the Levels of Oxidative Stress
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/10.1080/07391102.2023.2297821openalex-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/10.1080/10409238.2017.1394265openalex-snapshot
Specificity of reversible ADP-ribosylation and regulation of cellular processes
inferred← citeshttps://doi.org/10.1083/jcb.202101021openalex-snapshot
Neuralized-like protein 4 (NEURL4) mediates ADP-ribosylation of mitochondrial proteins
inferred← citeshttps://doi.org/10.1093/bioinformatics/bty159openalex-snapshot
ADPredict: ADP-ribosylation site prediction based on physicochemical and structural descriptors
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/gkaa590openalex-snapshot
PARP1 catalytic variants reveal branching and chain length-specific functions of poly(ADP-ribose) in cellular physiology and stress response
inferred← citeshttps://doi.org/10.1093/nar/gkaa718openalex-snapshot
Clinical PARP inhibitors do not abrogate PARP1 exchange at DNA damage sites in vivo
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/gkac948openalex-snapshot
PARP1 proximity proteomics reveals interaction partners at stressed replication forks
inferred← citeshttps://doi.org/10.1093/nar/gkad440openalex-snapshot
Pyruvate Kinase M (PKM) binds ribosomes in a poly-ADP ribosylation dependent manner to induce translational stalling
inferred← citeshttps://doi.org/10.1093/nar/gkad659openalex-snapshot
Absence of mitochondrial SLC25A51 enhances PARP1-dependent DNA repair by increasing nuclear NAD+ levels
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/gkx1205openalex-snapshot
The C-terminal domain of p53 orchestrates the interplay between non-covalent and covalent poly(ADP-ribosyl)ation of p53 by PARP1
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/gkz528openalex-snapshot
SIRT6 promotes transcription of a subset of NRF2 targets by mono-ADP-ribosylating BAF170
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/zcad020openalex-snapshot
Current proteomics methods applicable to dissecting the DNA damage response
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.202001759ropenalex-snapshot
SMURF2‐mediated ubiquitin signaling plays an essential role in the regulation of PARP1 PARylating activity, molecular interactions, and functions in mammalian cells
inferred← citeshttps://doi.org/10.1098/rsob.190041openalex-snapshot
ADP-ribosylation signalling and human disease
inferred← citeshttps://doi.org/10.1101/2020.07.02.184937openalex-snapshot
Arabidopsis poly(ADP-ribose)-binding protein RCD1 interacts with Photoregulatory Protein Kinases in nuclear bodies
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/10.1101/2020.11.17.384719openalex-snapshot
Development of a mass-spectrometry based method for the identification of the in vivo whole blood and plasma ADP-ribosylomes
inferred← citeshttps://doi.org/10.1101/2023.02.06.527366openalex-snapshot
Mono-ADP-ribosyltransferase 1 ( Artc1 )-deficiency decreases tumorigenesis, increases inflammation, decreases cardiac contractility, and reduces survival
inferred← citeshttps://doi.org/10.1101/2023.12.15.571635openalex-snapshot
A Site-Specific Analysis of the ADP-Ribosylome Unveils Homogeneous DNA Damage-Induced Serine ADP-Ribosylation Across Wild-Type and BRCA-Mutant Breast Cancer Cell Lines
inferred← citeshttps://doi.org/10.1101/2024.06.14.597428openalex-snapshot
A novel variant in ADPRS disrupts ARH3 stability and subcellular localization in children with neurodegeneration and respiratory failure
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/10.1101/423418openalex-snapshot
System-wide identification and prioritization of enzyme substrates by thermal analysis (SIESTA)
inferred← citeshttps://doi.org/10.1101/719559openalex-snapshot
SirT7 auto-ADP-ribosylation regulates glucose starvation response through macroH2A1.1
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.334425.119openalex-snapshot
The impact of PARPs and ADP-ribosylation on inflammation and host–pathogen interactions
inferred← citeshttps://doi.org/10.1101/gad.334730.119openalex-snapshot
Nuclear PARPs and genome integrity
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/10.1126/sciadv.abc0418openalex-snapshot
Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases
inferred← citeshttps://doi.org/10.1126/sciadv.abh2332openalex-snapshot
Tankyrase-mediated ADP-ribosylation is a regulator of TNF-induced death
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/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/10.1371/journal.pgen.1009600openalex-snapshot
Antagonistic fungal enterotoxins intersect at multiple levels with host innate immune defences
inferred← citeshttps://doi.org/10.1371/journal.pone.0213130openalex-snapshot
The oncoprotein DEK affects the outcome of PARP1/2 inhibition during mild replication stress
inferred← citeshttps://doi.org/10.1371/journal.pone.0240932openalex-snapshot
Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances its interaction with HPF1
inferred← citeshttps://doi.org/10.1515/hsz-2024-0057openalex-snapshot
Pathological and physiological roles of ADP-ribosylation: established functions and new insights
inferred← citeshttps://doi.org/10.15252/embj.2021110393openalex-snapshot
A rare human centenarian variant of SIRT6 enhances genome stability and interaction with Lamin A
inferred← citeshttps://doi.org/10.15252/embr.201745310openalex-snapshot
Comprehensive ADP‐ribosylome analysis identifies tyrosine as an ADP‐ribose acceptor site
inferred← citeshttps://doi.org/10.18632/aging.103567openalex-snapshot
SIRT6 mono-ADP ribosylates KDM2A to locally increase H3K36me2 at DNA damage sites to inhibit transcription and promote repair
inferred← citeshttps://doi.org/10.21203/rs.3.rs-958950/v1openalex-snapshot
Global Analysis of the Signalling Network of Breast Cancer Cells in Response to Progesterone.
inferred← citeshttps://doi.org/10.21203/rs.3.rs-958950/v2openalex-snapshot
Global Analysis of The Signalling Network of Breast Cancer Cells In Response To Progesterone.
inferred← citeshttps://doi.org/10.26508/lsa.202201455openalex-snapshot
Protein and RNA ADP-ribosylation detection is influenced by sample preparation and reagents used
inferred← citeshttps://doi.org/10.31857/s0026898423020167openalex-snapshot
Poly(ADP-ribose)polymerases 1 and 2: Classical Functions and Interaction with HPF1 ‒ New Histone Poly(ADP-ribosyl)ation Factor
inferred← citeshttps://doi.org/10.3389/fcell.2021.645318openalex-snapshot
Post-Translational Modifications in Oocyte Maturation and Embryo Development
inferred← citeshttps://doi.org/10.3389/fcell.2021.706997openalex-snapshot
Functions and Molecular Mechanisms of Deltex Family Ubiquitin E3 Ligases in Development and Disease
inferred← citeshttps://doi.org/10.3389/fcell.2022.864101openalex-snapshot
Research Progress on Mono-ADP-Ribosyltransferases in Human Cell Biology
inferred← citeshttps://doi.org/10.3389/fchbi.2025.1709253openalex-snapshot
An evaluation of high-field asymmetric-waveform ion mobility spectrometry coupled to electron-transfer/higher-energy collision dissociation for ADP-ribosylation proteomics
inferred← citeshttps://doi.org/10.3389/fcvm.2022.851351openalex-snapshot
The RiboMaP Spectral Annotation Method Applied to Various ADP-Ribosylome Studies Including INF-γ-Stimulated Human Cells and Mouse Tissues
inferred← citeshttps://doi.org/10.3389/fendo.2022.888802openalex-snapshot
Global signalling network analysis of luminal T47D breast cancer cells in response to progesterone
inferred← citeshttps://doi.org/10.3389/fimmu.2018.01580openalex-snapshot
In Vivo Blockade of Murine ARTC2.2 During Cell Preparation Preserves the Vitality and Function of Liver Tissue-Resident Memory T Cells
inferred← citeshttps://doi.org/10.3389/fimmu.2021.703719openalex-snapshot
Identification of the Mouse T Cell ADP-Ribosylome Uncovers ARTC2.2 Mediated Regulation of CD73 by ADP-Ribosylation
inferred← citeshttps://doi.org/10.3390/cancers12071813openalex-snapshot
The Nucleolus and PARP1 in Cancer Biology
inferred← citeshttps://doi.org/10.3390/cancers14215210openalex-snapshot
PARP10 Mediates Mono-ADP-Ribosylation of Aurora-A Regulating G2/M Transition of the Cell Cycle
inferred← citeshttps://doi.org/10.3390/cells10020313openalex-snapshot
MARTs and MARylation in the Cytosol: Biological Functions, Mechanisms of Action, and Therapeutic Potential
inferred← citeshttps://doi.org/10.3390/cells10030680openalex-snapshot
Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight
inferred← citeshttps://doi.org/10.3390/cells10112927openalex-snapshot
Temporal and Site-Specific ADP-Ribosylation Dynamics upon Different Genotoxic Stresses
inferred← citeshttps://doi.org/10.3390/cells11233853openalex-snapshot
ARH Family of ADP-Ribose-Acceptor Hydrolases
inferred← citeshttps://doi.org/10.3390/cells11233932openalex-snapshot
PARP1 Activation Controls Stress Granule Assembly after Oxidative Stress and DNA Damage
inferred← citeshttps://doi.org/10.3390/cells8080890openalex-snapshot
Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation
inferred← citeshttps://doi.org/10.3390/challe8010014openalex-snapshot
ADP-Ribosylation Reactions in Animals, Plants, and Bacteria
inferred← citeshttps://doi.org/10.3390/genes14010112openalex-snapshot
The Role of PARP1 and PAR in ATP-Independent Nucleosome Reorganisation during the DNA Damage Response
inferred← citeshttps://doi.org/10.3390/genes9080416openalex-snapshot
Maneuvers on PCNA Rings during DNA Replication and Repair
inferred← citeshttps://doi.org/10.3390/ijms22105112openalex-snapshot
PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling
inferred← citeshttps://doi.org/10.3390/ijms242216172openalex-snapshot
Unbiased Phosphoproteome Mining Reveals New Functional Sites of Metabolite-Derived PTMs Involved in MASLD Development
inferred← citeshttps://doi.org/10.3390/medicines7090054openalex-snapshot
PARP Inhibitors in Biliary Tract Cancer: A New Kid on the Block?
inferred← citeshttps://doi.org/10.3390/v18060587openalex-snapshot
Interactomics of SARS-CoV-2 Macrodomain 1 Reveals Putative Clients of ADP-Ribosyl Hydrolase Activity
inferred← citeshttps://doi.org/10.33915/etd.12281openalex-snapshot
Exploring the biological basis of residual feed intake in beef cattle using multi-Omics analysis.
inferred← citeshttps://doi.org/10.3410/f.735034537.793559082openalex-snapshot
Faculty Opinions recommendation of PARylation regulates stress granule dynamics, phase separation, and neurotoxicity of disease-related RNA-binding proteins.
inferred← citeshttps://doi.org/10.3410/f.738616487.793579254openalex-snapshot
Faculty Opinions recommendation of Clinical PARP inhibitors do not abrogate PARP1 exchange at DNA damage sites in vivo.
inferred← citeshttps://doi.org/10.37609/akya.2621openalex-snapshot
Proteinlerin Posttranslasyonel Modifikasyonları
inferred← citeshttps://doi.org/10.53846/goediss-10618openalex-snapshot
Resolving chromatin interaction and transcriptional networks in mammalian nuclei
inferred← citeshttps://doi.org/10.70675/16da82e2z0a3cz4743z9efdz8218950a93b2openalex-snapshot
Caractérisation des mécanismes d’ADP-ribosylation de l'ADN et son rôle dans la signalisation des dommages à l'ADN
inferred← citeshttps://doi.org/10.70675/4cfb4e55zcee1z400az819ezc32e9d48c4c4openalex-snapshot
Inhibitors of the mRNA capping machinery and structural studies on macro domains from alphaviruses
showing the first 200 of 214 · page through all 214
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.