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ProteomicsOxidative stress induced ADP-ribosylome
Oxidative stress is a potent inducer of protein ADP-ribosylation. Although the proteins modified under oxidative stress have been identified, it is not clear, whether the number of modified proteins and/or the number ADP-ribosylation sites varies with stress intensity. Here, we investigated both the...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-11-13 | MSV000080334 | MassIVE
ProteomicsProteomic characterization of the heart and skeletal muscle reveals widespread Arginine ADP-ribosylation by the ectopic ADP-ribosyltransferase ARTC1
ADP-ribosylation has thus far been studied on the proteomic level mainly in cell lines and in combination with genotoxic stress. The clostridium-like ADP-ribosyltransferases (i.e. ARTC) are GPI-anchored or secreted proteins that are expressed in a highly tissue specific manner. Transcriptomic data r...
ORGANISM(S): Mus musculus (Mouse) 
2018-08-17 | PXD008041 | Pride
Muscle Artc1 Ethcd Ptm Hcd Heart C2c12 Art1 Adp-ribosylation 
ProteomicsSerine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signaling
In the mammalian DNA damage response, ADP-ribosylation signaling is of crucial importance to mark sites of DNA damage as well as recruit and regulate repairs factors. Specifically, the PARP1:HPF1 complex recognizes damaged DNA and catalyzes the formation of serine-linked ADP-ribosylation marks (mono...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2023-05-26 | PXD036512 | Pride
Proteomics Adpr Ethcd Parp Drosophila Parg Af1521 Adp-ribosylation 
ProteomicsSystems-wide analysis of serine-ADP-ribosylation reveals widespread occurrence and site-specific overlap with phosphorylation - Part 1, ADP-ribosylation data.
ADP-ribosylation (ADPr) is a reversible posttranslational modification involved in a range of cellular processes. Here, we report system-wide identification of serine ADPr in human cells upon oxidative stress. High-resolution mass spectrometry and unrestricted data processing confirm that serine res...
ORGANISM(S): Homo sapiens (Human) 
2018-08-29 | PXD009208 | Pride
Adp Ribosylation Hela Unrestricted Serine Lumos Etd Adp-ribosylation 
ProteomicsTemporal and site-specific ADP-ribosylation dynamics upon different genotoxic stresses
The DNA damage response revolves around transmission of information via post-translational modifications, including reversible protein ADP-ribosylation. Here, we applied a mass spectrometry-based Af1521 enrichment technology for the identification and quantification of ADP-ribosylation sites as a fu...
ORGANISM(S): Homo sapiens (Human) 
2021-11-04 | PXD028902 | Pride
Proteomics Mass spectrometry Parp Post-translational modification Dna damage Af1521 Adp-ribosylation 
ProteomicsAn advanced strategy for comprehensive profiling of ADP-ribosylation sites using mass spectrometry-based proteomics
ADP-ribosylation is a widespread post-translational modification (PTM) with crucial functions in many cellular processes. Here, we describe an in-depth ADP-ribosylome using our Af1521-based proteomics methodology for profiling of ADP-ribosylation sites, by systematically assessing complementary prot...
ORGANISM(S): Homo sapiens (Human) 
2019-02-26 | PXD012243 | Pride
Adpr Human Ethcd Parp Lumos Etd Lysc Trypsin Adp-ribosylation 
ProteomicsSerine ADP-ribosylation depends on HPF1
We report that serine ADPr is strictly dependent on HPF1 (histone PARylation factor 1. Quantitative proteomics revealed that serine ADPr does not occur in cells lacking HPF1. We identified three endogenous serine ADPr sites are located on the PARP-1 automodification domain. Further identification of...
ORGANISM(S): Homo sapiens (Human) 
2017-02-10 | PXD005627 | Pride
Adp-ribosylation  hpf1  parp-1  parp-2  histones  proteomics 
ProteomicsPreservation of Ester-linked Modifications Reveals Glutamate/Aspartate mono-ADP-ribosylation by PARP1 and its Reversal by PARG
Ester-linked post-translational modifications, including serine and threonine ubiquitination, have gained recognition as important cellular signals. However, their detection remains a significant challenge due to the chemical lability of the ester bond. This is the case even for long-known modificat...
ORGANISM(S): Homo sapiens (Human) 
2024-05-08 | PXD048274 | Pride
Ubiquitination Proteomics Adpr Ptm Hcd Parp Etd Post-translational modification Adp-ribosylation Dna damage Parg 
ProteomicsRegulation of Rad52-dependent replication fork recovery through serine ADP-ribosylation of PolD3
Although Poly(ADP-ribose)-polymerases (PARPs) are key regulators of genome stability, how site-specific ADP-ribosylation regulates DNA repair is unclear. Here, we describe a novel role for PARP1 and PARP2 in regulating Rad52-dependent replication fork repair to maintain cell viability when HR is dys...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD035661 | Pride
Proteomics Dna repair Adpr Parps Lumos Adp-ribosyltransferases Adp-ribosylation Af1521 Dna replication 
ProteomicsAn HPF1/PARP1-based chemical biology strategy for exploring ADP-ribosylation
Strategies for installing authentic ADP-ribosylation (ADPr) at desired positions are fundamental for creating the tools needed to explore this elusive PTM in essential cellular processes. Here we describe a phospho-guided chemoenzymatic approach based on the Ser-ADPr writer complex for rapid, scalab...
ORGANISM(S): Homo sapiens (Human) 
2020-11-17 | PXD020589 | Pride
Parp1 Lc-ms Fusion Adp-ribosylation 
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