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ProteomicsProteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
ADP-ribosylation is a posttranslational modification that exists in monomeric and polymeric forms. Whereas the writers (e.g. ARTD1/PARP1) and erasers (e.g. PARG, ARH3) of poly-ADP-ribosylation (PARylation) are relatively well described, the enzymes involved in mono-ADP-ribosylation (MARylation) have...
ORGANISM(S): Mus musculus (Mouse) 
2017-12-14 | PXD008083 | Pride
Mef Ethcd Ptm Hcd Parp Mono-adp-ribosyl(-acceptor) hydrolases Arh3 Parg Adp-ribosylation 
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
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 
ProteomicsA Versatile Toolbox Reveals XRCC1 Deficiency–Driven Reshaping of the PARP1 Mono-ADP-Ribosylation Wave
ADP-ribosylation has long been recognized as a key regulator of essential signaling pathways, including the DNA damage response. However, only recent and ongoing technological advances are beginning to make it possible to investigate its distinct forms with molecular precision. Here, we designed a...
ORGANISM(S): Homo sapiens (Human) 
2026-02-18 | PXD066208 | Pride
Parp1 Adp-ribisylation 
ProteomicsIdentification of auto mono-ADP-ribosylation sites on SIRT6 and SIRT7
The aim of this project was to identify the auto mono-ADP-ribosylation sites on SIRT6 and SIRT7 to study the effect of the point mutations S56A and N189A respectively on their ADP-ribosylation activity. In addition, the mono-ADP-ribosylation pattern of SIRT7 was obtained in cells under different str...
ORGANISM(S): Homo sapiens (Human) 
2021-04-19 | PXD018344 | Pride
Sirtuins  sirt7  adp-ribosylation  macroh2a  glucose starvation  chromatin  calorie restriction  aging  orbitrap lumos  orbitrap eclipse 
UnknownModular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling.
Not available
S-EPMC10205078 | biostudies-literature
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 
ProteomicsIdentification of PARP15 enzymatic substrates
Recombinant JNK-interacting protein 3 (JIP3) was incubated with enzymatically active PARP15 and biotinylated NAD to determine residues modified by mono-ADP ribosylation (MAR)
ORGANISM(S): Homo sapiens (Human) 
2025-12-08 | PXD051413 | Pride
Poly-adp ribosyltransferase (parp)  parp15 Mono-adp ribosylation  jun kinase (jnk)  jnk-kinase interacting protein 
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 
UnknownA family of macrodomain proteins reverses cellular mono-ADP-ribosylation.
Not available
S-EPMC7097781 | biostudies-literature
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