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Serine ADP-Ribosylation Depends on HPF1

https://doi.org/10.1016/j.molcel.2017.01.003

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What this work says

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

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Purification of Human PARP-1 and PARP-1 Domains from Escherichia coli for Structural and Biochemical Analysis

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Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response

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Protein ADP-ribosylation and the cellular response to DNA strand breaks

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High mobility group (HMG) proteins: Modulators of chromatin structure and DNA repair in mammalian cells

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A review of tandem mass spectrometry characterization of adenosine diphosphate-ribosylated peptides

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PARP-1 and gene regulation: Progress and puzzles

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The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets

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DNA Repair Factor APLF Is a Histone Chaperone

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Proteome-wide Identification of Poly(ADP-Ribosyl)ation Targets in Different Genotoxic Stress Responses

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Chromatin to Clinic: The Molecular Rationale for PARP1 Inhibitor Function

inferredcites →https://doi.org/10.1016/j.molcel.2015.06.012openalex-snapshot

The Promise of Proteomics for the Study of ADP-Ribosylation

inferredcites →https://doi.org/10.1016/j.molcel.2016.03.008openalex-snapshot

HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity

inferredcites →https://doi.org/10.1016/j.sbi.2013.01.003openalex-snapshot

PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis

inferredcites →https://doi.org/10.1016/j.semcdb.2016.09.009openalex-snapshot

Expanding functions of ADP-ribosylation in the maintenance of genome integrity

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Optimization of LTQ-Orbitrap Mass Spectrometer Parameters for the Identification of ADP-Ribosylation Sites

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ProteomeXchange provides globally coordinated proteomics data submission and dissemination

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

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Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue

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Family-wide analysis of poly(ADP-ribose) polymerase activity

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Proteomic and phosphoproteomic comparison of human ES and iPS cells

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Reanalysis of phosphoproteomics data uncovers ADP-ribosylation sites

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

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Large-scale gene function analysis with the PANTHER classification system

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inferredcites →https://doi.org/10.1038/srep18271openalex-snapshot

Nudix hydrolases degrade protein-conjugated ADP-ribose

inferredcites →https://doi.org/10.1042/bj20141554openalex-snapshot

Processing of protein ADP-ribosylation by Nudix hydrolases

inferredcites →https://doi.org/10.1074/mcp.m200025-mcp200openalex-snapshot

Stable Isotope Labeling by Amino Acids in Cell Culture, SILAC, as a Simple and Accurate Approach to Expression Proteomics

inferredcites →https://doi.org/10.1093/nar/gkp273openalex-snapshot

Robust methods for purification of histones from cultured mammalian cells with the preservation of their native modifications

inferredcites →https://doi.org/10.1093/nar/gkq463openalex-snapshot

PARP1 ADP-ribosylates lysine residues of the core histone tails

inferredcites →https://doi.org/10.1093/nar/gku474openalex-snapshot

PARP-2 and PARP-3 are selectively activated by 5′ phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1

inferredcites →https://doi.org/10.1101/gad.183509.111openalex-snapshot

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inferredcites →https://doi.org/10.1111/febs.13737openalex-snapshot

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inferredcites →https://doi.org/10.1111/j.1432-1033.1987.tb13621.xopenalex-snapshot

Poly(ADP-ribose) synthase is the major endogenous nonhistone acceptor for poly(ADP-ribose) in alkylated rat hepatoma cells

inferredcites →https://doi.org/10.1126/science.1216338openalex-snapshot

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inferredcites →https://doi.org/10.1126/science.aaf7865openalex-snapshot

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inferredcites →https://doi.org/10.1128/mcb.21.15.5169-5178.2001openalex-snapshot

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inferredcites →https://doi.org/10.1146/annurev-biochem-060815-014935openalex-snapshot

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PARP enzyme de novo synthesis of protein-free poly(ADP-ribose)

inferred← citeshttps://doi.org/10.1016/j.molcel.2025.01.004openalex-snapshot

A PARP2 active site helix melts to permit DNA damage-induced enzymatic activation

inferred← citeshttps://doi.org/10.1016/j.molcel.2025.09.006openalex-snapshot

PARP1 auto-modification promotes faithful Okazaki fragment processing and limits replication fork speed

inferred← citeshttps://doi.org/10.1016/j.molmed.2021.04.010openalex-snapshot

Studying PAR-Dependent Chromatin Remodeling to Tackle PARPi Resistance

inferred← citeshttps://doi.org/10.1016/j.molmed.2023.02.001openalex-snapshot

PARsylation-mediated ubiquitylation: lessons from rare hereditary disease Cherubism

inferred← citeshttps://doi.org/10.1016/j.molmet.2020.01.014openalex-snapshot

The taming of PARP1 and its impact on NAD+ metabolism

inferred← citeshttps://doi.org/10.1016/j.mrrev.2017.09.004openalex-snapshot

Poly-ADP ribosylation in DNA damage response and cancer therapy

inferred← citeshttps://doi.org/10.1016/j.neo.2024.101092openalex-snapshot

Suppression of ADP-ribosylation reversal triggers cell vulnerability to alkylating agents

inferred← citeshttps://doi.org/10.1016/j.pharmthera.2021.107968openalex-snapshot

PARkinson's: From cellular mechanisms to potential therapeutics

inferred← citeshttps://doi.org/10.1016/j.plipres.2021.101117openalex-snapshot

PARPs in lipid metabolism and related diseases

inferred← citeshttps://doi.org/10.1016/j.sbi.2018.11.002openalex-snapshot

PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification

inferred← citeshttps://doi.org/10.1016/j.sbi.2023.102643openalex-snapshot

PARP–nucleic acid interactions: Allosteric signaling, PARP inhibitor types, DNA bridges, and viral RNA surveillance

inferred← citeshttps://doi.org/10.1016/j.tcb.2022.04.010openalex-snapshot

DNA single-strand break repair and human genetic disease

inferred← citeshttps://doi.org/10.1016/j.tibs.2021.01.014openalex-snapshot

Rapid Detection and Signaling of DNA Damage by PARP-1

inferred← citeshttps://doi.org/10.1016/j.tibs.2023.06.005openalex-snapshot

A chemical biology/modular antibody platform for ADP-ribosylation signaling

inferred← citeshttps://doi.org/10.1016/j.tibs.2024.08.006openalex-snapshot

The quest to identify ADP-ribosylation readers: methodological advances

inferred← citeshttps://doi.org/10.1016/j.tig.2019.03.008openalex-snapshot

Perspectives on PARPs in S Phase

inferred← citeshttps://doi.org/10.1016/j.tig.2024.08.009openalex-snapshot

The complex universe of inactive PARP1

inferred← citeshttps://doi.org/10.1016/j.xpro.2025.104106openalex-snapshot

Protocol for quantifying PARP inhibitor-induced changes in PARP1 dynamics and activity through live-cell imaging

inferred← citeshttps://doi.org/10.1016/j.yexcr.2021.112679openalex-snapshot

Balancing DNA repair to prevent ageing and cancer

inferred← citeshttps://doi.org/10.1017/erm.2024.14openalex-snapshot

Specific and shared biological functions of PARP2 – is PARP2 really a lil’ brother of PARP1?

inferred← citeshttps://doi.org/10.1017/erm.2024.17openalex-snapshot

ADP-ribose hydrolases: biological functions and potential therapeutic targets

inferred← citeshttps://doi.org/10.1021/acs.biochem.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.2c00851openalex-snapshot

Regulation of Biomolecular Condensates by Poly(ADP-ribose)

inferred← citeshttps://doi.org/10.1021/acs.chemrev.7b00122openalex-snapshot

ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease

inferred← citeshttps://doi.org/10.1021/acs.jproteome.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.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.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.9b00085openalex-snapshot

Optimized Cross-Linking Mass Spectrometry for in Situ Interaction Proteomics

inferred← citeshttps://doi.org/10.1021/acs.orglett.3c01554openalex-snapshot

4-Thioribose Analogues of Adenosine Diphosphate Ribose (ADPr) Peptides

inferred← citeshttps://doi.org/10.1021/acs.orglett.8b01742openalex-snapshot

Synthetic α- and β-Ser-ADP-ribosylated Peptides Reveal α-Ser-ADPr as the Native Epimer

inferred← citeshttps://doi.org/10.1021/acschembio.2c00091openalex-snapshot

A Protein Semisynthesis-Based Strategy to Investigate the Functional Impact of Linker Histone Serine ADP-Ribosylation

inferred← citeshttps://doi.org/10.1021/acschembio.5c00817openalex-snapshot

A Large-Scale Method to Measure the Stoichiometries of Protein Poly-ADP-Ribosylation

inferred← citeshttps://doi.org/10.1021/acschembio.9b00429openalex-snapshot

The ARH and Macrodomain Families of α-ADP-ribose-acceptor Hydrolases Catalyze α-NAD+ Hydrolysis

inferred← citeshttps://doi.org/10.1021/acsomega.9b03591openalex-snapshot

Chemical Tools to Study Protein ADP-Ribosylation

inferred← citeshttps://doi.org/10.1021/acssensors.4c01406openalex-snapshot

A Genetically Encoded Sensor for Real-Time Monitoring of Poly-ADP-Ribosylation Dynamics In Vitro and in Cells

inferred← citeshttps://doi.org/10.1021/jacs.3c03771openalex-snapshot

Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation

inferred← citeshttps://doi.org/10.1021/jacs.5c01567openalex-snapshot

NMR-Based Measurements of Site-Specific Electrostatic Potentials of Histone Tails in Nucleosome Core Particles

inferred← citeshttps://doi.org/10.1038/nchembio.2568openalex-snapshot

Insights into the biogenesis, function, and regulation of ADP-ribosylation

inferred← citeshttps://doi.org/10.1038/s41392-026-02583-xopenalex-snapshot

Reactive oxygen species (ROS) in cancer: from mechanism to therapeutic implications

inferred← citeshttps://doi.org/10.1038/s41408-026-01493-zopenalex-snapshot

Aberrant glycosylation in hematologic malignancies: mechanisms, immune evasion, and therapeutic targeting

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/s41467-019-13167-5openalex-snapshot

Barrier-to-autointegration factor 1 (Banf1) regulates poly [ADP-ribose] polymerase 1 (PARP1) activity following oxidative DNA damage

inferred← citeshttps://doi.org/10.1038/s41467-020-14620-6openalex-snapshot

Genetic screens in isogenic mammalian cell lines without single cell cloning

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/s41467-021-20998-8openalex-snapshot

Histone Parylation factor 1 contributes to the inhibition of PARP1 by cancer drugs

inferred← citeshttps://doi.org/10.1038/s41467-021-21302-4openalex-snapshot

HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones

inferred← citeshttps://doi.org/10.1038/s41467-021-24361-9openalex-snapshot

Serine-linked PARP1 auto-modification controls PARP inhibitor response

inferred← citeshttps://doi.org/10.1038/s41467-021-24723-3openalex-snapshot

Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal

inferred← citeshttps://doi.org/10.1038/s41467-021-26172-4openalex-snapshot

The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome

inferred← citeshttps://doi.org/10.1038/s41467-021-26588-yopenalex-snapshot

SPINDOC binds PARP1 to facilitate PARylation

inferred← citeshttps://doi.org/10.1038/s41467-021-27043-8openalex-snapshot

HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications

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/s41467-022-30785-8openalex-snapshot

Cis- and trans-resveratrol have opposite effects on histone serine-ADP-ribosylation and tyrosine induced neurodegeneration

inferred← citeshttps://doi.org/10.1038/s41467-022-33731-wopenalex-snapshot

Mammalian N1-adenosine PARylation is a reversible DNA modification

inferred← citeshttps://doi.org/10.1038/s41467-023-38793-yopenalex-snapshot

Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling

inferred← citeshttps://doi.org/10.1038/s41467-023-40071-wopenalex-snapshot

Regulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3

inferred← citeshttps://doi.org/10.1038/s41467-024-45237-8openalex-snapshot

Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1

inferred← citeshttps://doi.org/10.1038/s41467-024-48314-0openalex-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/s41467-024-50912-xopenalex-snapshot

PARP1-dependent DNA-protein crosslink repair

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/s41467-025-58309-0openalex-snapshot

FTO suppresses DNA repair by inhibiting PARP1

inferred← citeshttps://doi.org/10.1038/s41467-025-67071-2openalex-snapshot

Nucleosome unwrapping and PARP1 allostery drive affinities for chromatin and DNA breaks

inferred← citeshttps://doi.org/10.1038/s41467-026-69375-3openalex-snapshot

PARP1-HPF1 structure and dynamics on nicked DNA suggest a mechanism for acute and localized ADP-ribosylation

inferred← citeshttps://doi.org/10.1038/s41467-026-71311-4openalex-snapshot

Versatile and sensitive detection of mono- and poly(ADP-ribosyl)ation reveals XRCC1-dependent remodelling of PARP1 signalling

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

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

inferred← citeshttps://doi.org/10.1038/s41556-021-00792-wopenalex-snapshot

XRCC1 protects transcription from toxic PARP1 activity during DNA base excision repair

inferred← citeshttps://doi.org/10.1038/s41573-020-0076-6openalex-snapshot

Poly(ADP-ribose) polymerase inhibition: past, present and future

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/s41589-018-0097-1openalex-snapshot

Acetylation blocks DNA damage–induced chromatin ADP-ribosylation

inferred← citeshttps://doi.org/10.1038/s41589-025-01974-5openalex-snapshot

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

inferred← citeshttps://doi.org/10.1038/s41589-025-02045-5openalex-snapshot

Stabilization of AFF1 by PARylation ensures transcriptional restart after DNA damage

inferred← citeshttps://doi.org/10.1038/s41594-020-0412-xopenalex-snapshot

Tickling PARPs into serine action

inferred← citeshttps://doi.org/10.1038/s41594-023-00977-xopenalex-snapshot

HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation to promote the recruitment of repair factors at sites of DNA damage

inferred← citeshttps://doi.org/10.1038/s41594-023-00987-9openalex-snapshot

PARP1 and HPF1 team up to flag down DNA-repair machinery

inferred← citeshttps://doi.org/10.1038/s41597-025-04722-5openalex-snapshot

Comprehensive dataset of interactors for the entire PARP family using TurboID proximity labeling

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/s41598-024-70368-9openalex-snapshot

Unveiling FRG1’s DNA repair role in breast cancer

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/s42003-021-02770-2openalex-snapshot

Sirtuin inhibition is synthetic lethal with BRCA1 or BRCA2 deficiency

inferred← citeshttps://doi.org/10.1038/s42003-021-02780-0openalex-snapshot

Dual function of HPF1 in the modulation of PARP1 and PARP2 activities

inferred← citeshttps://doi.org/10.1038/s42003-023-05494-7openalex-snapshot

The DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3

inferred← citeshttps://doi.org/10.1038/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/10.1039/c9ob00501copenalex-snapshot

Chemical ADP-ribosylation: mono-ADPr-peptides and oligo-ADP-ribose

inferred← citeshttps://doi.org/10.1039/d0cb00175aopenalex-snapshot

Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications

inferred← citeshttps://doi.org/10.1039/d6gc03246jopenalex-snapshot

Nucleophilicity-controlled stereodivergent synthesis of ADP-ribosylated phenols and tyrosine derivatives directly from β-NAD +

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/bcj20230406openalex-snapshot

Novel modifications of PARP inhibitor veliparib increase PARP1 binding to DNA breaks

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

Are PARPs promiscuous?

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/bst20180418openalex-snapshot

PARPs in genome stability and signal transduction: implications for cancer therapy

inferred← citeshttps://doi.org/10.1042/bst20220366openalex-snapshot

Revisiting PARP2 and PARP1 trapping through quantitative live-cell imaging

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

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

inferred← citeshttps://doi.org/10.1053/j.seminoncol.2023.08.001openalex-snapshot

PARP1 roles in DNA repair and DNA replication: The basi(c)s of PARP inhibitor efficacy and resistance

inferred← citeshttps://doi.org/10.1073/pnas.2003613117openalex-snapshot

Live-cell protein engineering with an ultra-short split intein

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