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ProteomicsComprehensive ADP-ribosylome analysis identifies tyrosine as an ADP-ribose acceptor site
Despite recent mass spectrometry (MS)-based breakthroughs, comprehensive ADP-ribose (ADPr)-site identification and localization remain challenging. Here, we report the establishment of an unbiased, multistep ADP-ribosylome data analysis workflow that led to the identification of tyrosine as a novel ...
ORGANISM(S): Homo sapiens (Human) 
2018-06-28 | PXD009948 | Pride
Tyrosine adp-ribosylation Parp1 Artd1 Hpf1 Rsp3a Genotoxic stress Adp-ribosylation 
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 
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 
ProteomicsEngineering Af1521 macro domain increases ADP-ribose binding affinity and leads to the identification of more ADP-ribosylated proteins
Protein ADP-ribosylation is a covalent, reversible post-translational modification that has important functions in several cellular mechanisms. The identification of modified proteins in cells has proven challenging and, due to the low abundance of protein ADP-ribosylation, has mainly been possible ...
ORGANISM(S): Homo sapiens (Human) 
2020-10-20 | PXD016686 | Pride
Ap-ms Af1521 macro domain Adp-ribosylation Lc-ms/ms 
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
ProteomicsGas-phase Fragmentation of ADP-Ribosylated Peptides: Arginine-Specific Side-Chain Losses and their Implication in Database Searches
ADP-ribosylation is a reversible post-translational modification of proteins that has been linked to many biological processes. The identification of ADP-ribosylated proteins and of their acceptor amino acids remains a significant challenge. The attachment sites of the modification are difficult to ...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-05-19 | PXD017013 | Pride
Post-translational modification Arginine Mass spectrometry Marker ion Neutral loss Adp-ribosylation Orbitrap fusion 
ProteomicsMitochondrial ADP-ribosylation regulates NAD+-dependent genotoxic stress responses
ADP-ribosylome analysis in human U20S cells and mouse muscle tissues
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-09-08 | PXD013918 | Pride
Mitochondria U2os Adp-ribosylation Muscle 
ProteomicsMacroD1 sustains mitochondrial integrity and oxidative metabolism
The mono-ADP-ribosylhydrolase MacroD1 has recently been described to exclusively localize to mitochondria. However, to what extent and how MacroD1 controls metabolic homeostasis remains poorly understood. Here, we identify MacroD1 as a mitochondrial regulator of carbohydrate metabolism. Loss of Macr...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2025-05-16 | PXD020281 | Pride
Mitochondrial fission Macrod1 Mitochondrial adp-ribosylation Adp-ribosylome Glucose metabolism Label-free quantification 
ProteomicsLack of the mitochondrial NAD transporter SLC25A51 redistributes NAD+ compartmentalization and cellular ADP-ribosylation
Nicotinamide adenine dinucleotide (NAD+) is a vital small molecule with important redox capacity in oxidative phosphorylation (OXPHOS) and a key co-factor in various enzymatic reactions. The recent identification of the mitochondrial NAD+ transporter SLC25A51 provides strong evidence for a direct re...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD031373 | Pride
Sl25a51 Adp-ribosylation Mitochondia 
ProteomicsDevelopment of a mass-spectrometry based method for the identification of the in vivo whole blood and plasma ADP-ribosylomes
Blood and plasma proteins are heavily investigated as biomarkers for different diseases. However, the post-translational modifications of these proteins are rarely analyzed since blood contains many enzymes that rapidly remove the modification after sampling. In contrast to the well-described role o...
ORGANISM(S): Homo sapiens (Human) Sus scrofa domesticus (domestic pig) 
2021-05-26 | PXD022156 | Pride
Systemic inflammatory response syndrome Sepsis Plasma Blood Adp-ribosylation Histidine adp-ribosylation 
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