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Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation

https://doi.org/10.1016/j.celrep.2018.07.083

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What this work says

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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/s41467-025-62410-9openalex-snapshot

MacroD1 sustains mitochondrial integrity and oxidative metabolism

inferred← citeshttps://doi.org/10.1038/s41467-025-66136-6openalex-snapshot

Global remodeling of ADP-ribosylation by PARP1 suppresses influenza A virus infection

inferred← citeshttps://doi.org/10.1038/s41467-026-73677-xopenalex-snapshot

Deciphering cytokine-driven ADP-ribosylation signaling networks via Af1521-based mass spectrometry analysis of labile Glu/Asp-linkages

inferred← citeshttps://doi.org/10.1038/s41580-021-00394-2openalex-snapshot

Cellular functions of the protein kinase ATM and their relevance to human disease

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/s41589-025-01974-5openalex-snapshot

Serine ADPr on histones and PARP1 is a cellular target of ester-linked ubiquitylation

inferred← citeshttps://doi.org/10.1038/s41598-024-54123-8openalex-snapshot

High-throughput screening assay for PARP-HPF1 interaction inhibitors to affect DNA damage repair

inferred← citeshttps://doi.org/10.1038/s42003-022-04241-8openalex-snapshot

Poly ADP-ribosylation of SET8 leads to aberrant H4K20 methylation in mammalian nuclear genome

inferred← citeshttps://doi.org/10.1038/s42003-025-07901-7openalex-snapshot

Family-wide analysis of human macrodomains reveals novel activities and identifies PARG as most efficient ADPr-RNA hydrolase

inferred← citeshttps://doi.org/10.1038/s44318-025-00545-7openalex-snapshot

PARP7 is a proteotoxic stress sensor that labels proteins for degradation

inferred← citeshttps://doi.org/10.1038/s44319-024-00285-5openalex-snapshot

PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation

inferred← citeshttps://doi.org/10.1038/s44321-025-00214-6openalex-snapshot

PARP7 as a new target for activating anti-tumor immunity in cancer

inferred← citeshttps://doi.org/10.1039/d4cb00043aopenalex-snapshot

Chemical tools for profiling the intracellular ADP-ribosylated proteome

inferred← citeshttps://doi.org/10.1039/d5ay00535copenalex-snapshot

Analytical applications of gas-phase ion chemistry enabled by mass spectrometry

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/bcj20210280openalex-snapshot

Beyond protein modification: the rise of non-canonical ADP-ribosylation

inferred← citeshttps://doi.org/10.1042/bcj20230230openalex-snapshot

Regulation of PARP1/2 and the tankyrases: emerging parallels

inferred← citeshttps://doi.org/10.1042/bsr20212489openalex-snapshot

Are PARPs promiscuous?

inferred← citeshttps://doi.org/10.1042/bsr20240986openalex-snapshot

Interferon-induced ADP-ribosylation: technical developments driving ICAB discovery

inferred← citeshttps://doi.org/10.1042/bst20180416openalex-snapshot

ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes

inferred← citeshttps://doi.org/10.1042/bst20220749openalex-snapshot

The function and regulation of ADP-ribosylation in the DNA damage response

inferred← citeshttps://doi.org/10.1073/pnas.2109252118openalex-snapshot

Deficiency of PARP-1 and PARP-2 in the mouse uterus results in decidualization failure and pregnancy loss

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/10.1093/nar/gkaa941openalex-snapshot

ADPriboDB 2.0: an updated database of ADP-ribosylated proteins

inferred← citeshttps://doi.org/10.1093/nar/gkad066openalex-snapshot

PARP1 associates with R-loops to promote their resolution and genome stability

inferred← citeshttps://doi.org/10.1093/nar/gkad791openalex-snapshot

ZNF432 stimulates PARylation and inhibits DNA resection to balance PARPi sensitivity and resistance

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/gkaf069openalex-snapshot

Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack

inferred← citeshttps://doi.org/10.1093/nar/gkaf1170openalex-snapshot

Histone PARylation factor 1: a review of its role in the DNA damage response

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/gkz120openalex-snapshot

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins

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/10.1098/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/10.1098/rstb.2022.0237openalex-snapshot

Characterizing citrullination by mass spectrometry-based proteomics

inferred← citeshttps://doi.org/10.1101/2020.05.05.078097openalex-snapshot

PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 controls the transport of E-cadherin

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/10.1101/2022.02.17.480967openalex-snapshot

A protein semisynthesis-based strategy to probe the impact of site-specific serine ADP-ribosylation on linker histone function

inferred← citeshttps://doi.org/10.1101/2022.04.27.489674openalex-snapshot

Biomolecular condensates govern PARP inhibitor trapping and present mechanisms of resistance

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/10.1101/2025.02.20.639283openalex-snapshot

PARP inhibitors affect the replisome and replication fork progression during a single S phase

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/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/10.1111/febs.15518openalex-snapshot

Progress and outlook in studying the substrate specificities of PARPs and related enzymes

inferred← citeshttps://doi.org/10.1111/febs.70409openalex-snapshot

Automodification of N‐terminal serine residues facilitates PARP2 release from DNA

inferred← citeshttps://doi.org/10.1126/sciadv.abh2332openalex-snapshot

Tankyrase-mediated ADP-ribosylation is a regulator of TNF-induced death

inferred← citeshttps://doi.org/10.1146/annurev-nutr-112525-013335openalex-snapshot

Mechanisms of NAD+ Homeostasis in Aging and Disease

inferred← citeshttps://doi.org/10.1158/0008-5472.c.6514089.v1openalex-snapshot

Data from Oncohistone Mutations Occur at Functional Sites of Regulatory ADP-Ribosylation

inferred← citeshttps://doi.org/10.1158/0008-5472.can-22-0742openalex-snapshot

Oncohistone Mutations Occur at Functional Sites of Regulatory ADP-Ribosylation

inferred← citeshttps://doi.org/10.1158/0008-5472.can-23-3458openalex-snapshot

PARP-ish: Gaps in Molecular Understanding and Clinical Trials Targeting PARP Exacerbate Racial Disparities in Prostate Cancer

inferred← citeshttps://doi.org/10.1158/1541-7786.mcr-25-1068openalex-snapshot

Mapping the Subtype-Specific PARP1 ADP-Ribosylated Proteome in Breast Cancer Cells

inferred← citeshttps://doi.org/10.1186/s13578-020-0375-yopenalex-snapshot

Targeting dePARylation for cancer therapy

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/10.1523/eneuro.0239-19.2019openalex-snapshot

Loss of Tiparp Results in Aberrant Layering of the Cerebral Cortex

inferred← citeshttps://doi.org/10.1530/jme-19-0266openalex-snapshot

90 YEARS OF PROGESTERONE: Molecular mechanisms of progesterone receptor action on the breast cancer genome

inferred← citeshttps://doi.org/10.2533/chimia.2022.73openalex-snapshot

Mass Spectrometry in Proteomics: Technologies, Methods, and Research Applications for the Life Sciences

inferred← citeshttps://doi.org/10.3389/fcell.2021.745922openalex-snapshot

The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response

inferred← citeshttps://doi.org/10.3389/fcell.2023.1149535openalex-snapshot

EdeepSADPr: an extensive deep-learning architecture for prediction of the in situ crosstalks of serine phosphorylation and ADP-ribosylation

inferred← citeshttps://doi.org/10.3389/fmolb.2022.1073797openalex-snapshot

The potential of PARP inhibitors in targeted cancer therapy and immunotherapy

inferred← citeshttps://doi.org/10.3390/biom12030443openalex-snapshot

ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives

inferred← citeshttps://doi.org/10.3390/cancers12071813openalex-snapshot

The Nucleolus and PARP1 in Cancer Biology

inferred← citeshttps://doi.org/10.3390/cancers13092042openalex-snapshot

The PARP Enzyme Family and the Hallmarks of Cancer Part 1. Cell Intrinsic Hallmarks

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/cancers15010006openalex-snapshot

Epigenetic Insights on PARP-1 Activity in Cancer Therapy

inferred← citeshttps://doi.org/10.3390/cells10010128openalex-snapshot

Mono(ADP-ribosyl)ation Enzymes and NAD+ Metabolism: A Focus on Diseases and Therapeutic Perspectives

inferred← citeshttps://doi.org/10.3390/cells10030623openalex-snapshot

PARP7 and Mono-ADP-Ribosylation Negatively Regulate Estrogen Receptor α Signaling in Human Breast Cancer Cells

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/cells8080890openalex-snapshot

Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation

inferred← citeshttps://doi.org/10.3390/cells8091047openalex-snapshot

The Role of PARPs in Inflammation—And Metabolic—Related Diseases: Molecular Mechanisms and Beyond

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/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/ijms221910829openalex-snapshot

ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control

inferred← citeshttps://doi.org/10.3390/ijms241915028openalex-snapshot

The Complex Network of ADP-Ribosylation and DNA Repair: Emerging Insights and Implications for Cancer Therapy

inferred← citeshttps://doi.org/10.3390/ijms252212417openalex-snapshot

POLD3 as Controller of Replicative DNA Repair

inferred← citeshttps://doi.org/10.3390/metabo14060343openalex-snapshot

Nicotinamide N-Methyltransferase (NNMT): A New Hope for Treating Aging and Age-Related Conditions

inferred← citeshttps://doi.org/10.3390/molecules28166061openalex-snapshot

Using TLC-MALDI-TOF to Interrogate In Vitro Peptidyl Proximal Preferences of PARP14 and Glycohydrolase Specificity

inferred← citeshttps://doi.org/10.53846/goediss-9741openalex-snapshot

The MDM2 oncoprotein antagonizes Poly(ADP-ribosyl)ation

inferred← citeshttps://doi.org/10.7554/elife.60480openalex-snapshot

Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets

inferred← citeshttps://doi.org/10.7554/elife.65773openalex-snapshot

HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase

inferred← citeshttps://doi.org/10.7554/elife.71502openalex-snapshot

Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling

inferred← citeshttps://doi.org/10.7554/elife.98152openalex-snapshot

SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis

inferred← citeshttps://doi.org/10.7554/elife.98152.1openalex-snapshot

SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis

inferred← citeshttps://doi.org/10.7554/elife.98152.1.sa0openalex-snapshot

Reviewer #3 (Public Review): SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis

inferred← citeshttps://doi.org/10.7554/elife.98152.1.sa1openalex-snapshot

Reviewer #2 (Public Review): SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis

inferred← citeshttps://doi.org/10.7554/elife.98152.1.sa2openalex-snapshot

Reviewer #1 (Public Review): SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis

inferred← citeshttps://doi.org/10.7554/elife.98152.1.sa3openalex-snapshot

eLife Assessment: SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis

inferred← citeshttps://doi.org/10.7554/elife.98152.2openalex-snapshot

SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis

inferred← citeshttps://doi.org/10.7554/elife.98152.3openalex-snapshot

SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis

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.