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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 study into the ADP-ribosylome of IFN--stimulated THP-1 human macrophage-like cells identifies ARTD8/PARP14 and ARTD9/PARP9 ADP-ribosylation
ADP-ribosylation is a post-translational modification that, until recently, has remained elusive to study at the cellular level. Previously dependent on radioactive tracers to identify ADP-ribosylation targets, several advances in mass spectrometric workflows now permit global identification of ADP-...
ORGANISM(S): Homo sapiens (Human) 
2020-01-27 | PXD011690 | Pride
Electron transfer higher-energy collision dissociation (ethcd) Proteomics Gas phase segmentation Higher-energy collision dissociation (hcd) Parallel reaction monitoring (prm) Orbitrap fusion lumos Post-translational modification (ptm) 
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 
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 
ProteomicsPertussis toxin-catalyzed auto- and trans-ADP-ribosylation
This dataset was created to identify amino acids in pertussis toxin ADP-ribosyltransferase subunit (PtxS1) that get auto-modified during catalysis. In parallel, amino acids that get ADP-ribosylated by PtxS1 in the host cell target protein, G-protein inhibitory alpha subunit, were identified.
ORGANISM(S): Homo sapiens (Human) Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2025-05-06 | PXD050185 | Pride
Pertussis toxin Adp-ribosylation 
ProteomicsSerine ADP-ribosylation on histones and PARP1 is a cellular target for ester-linked ubiquitylation
ADP-ribosylation and ubiquitylation are key regulators of a wide variety of cellular processes, with the sophistication of their interplay becoming increasingly prominent, as illustrated by ADP-ribosylation-dependent ubiquitylation mediated by Legionella effectors. Recent biochemical studies have re...
ORGANISM(S): Homo sapiens (Human) 
2025-06-11 | PXD058858 | Pride
Adpr Dia Dda 
ProteomicsPARP1 auto-modification promotes faithful Okazaki fragment processing and limits replication fork speed
Poly(ADP-ribose) polymerase (PARP) inhibitors have proven their efficacy for treating tumors defective in homologous recombination via synthetic lethality. In response to DNA breaks, PARP1 is the primary ADP-ribosylation writer, modifying itself (auto-modification) and other proteins to facilitate r...
ORGANISM(S): Homo sapiens (Human) 
2025-10-02 | PXD066033 | Pride
Parp1 Ptm Okazaki fragment Adp-ribosylation Dna replication 
ProteomicsAffinity purification of ADP-ribosylated proteins from A. thaliana plants expressing the Pseudomonas syringae type III effector AvrRpm1, DDA method
ADP-ribosylated proteins were enriched using the engineered Af1521 Macro domain (Nowak et al., https://doi.org/10.1038/s41467-020-18981-w) from transgenic A. thaliana lines expressing the Pseudomonas syringae type III effector AvrRpm1. Enriched proteins were analyzed by LC-MS/MS.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2023-09-28 | PXD045638 | Pride
Arabidopsis thaliana Type iii effector Pseudomonas syringae Plant pathogen Adp-ribosylation 
ProteomicsPARP1 auto-modification promotes faithful Okazaki fragment processing and limits replication fork speed
Poly(ADP-ribose) polymerase (PARP) inhibitors have proven their efficacy for treating tumors defective in homologous recombination via synthetic lethality. In response to DNA breaks, PARP1 is the primary ADP-ribosylation writer, modifying itself (auto-modification) and other proteins to facilitate r...
ORGANISM(S): Homo sapiens (Human) Xenopus laevis (African clawed frog) 
2025-10-02 | PXD052191 | Pride
Okazaki fragment processing Parp1 Dna repair Af1521 macrodomain Adp-ribosylation Xenopus egg extract Auto-modification Dna replication 
ProteomicsAffinity purification of ADP-ribosylated proteins from A. thaliana plants expressing the Pseudomonas syringae type III effector AvrRpm1, DDA method (2.5 ug Af1521 Macro, technical replicate 1)
ADP-ribosylated proteins were enriched using the engineered Af1521 Macro domain (Nowak et al., https://doi.org/10.1038/s41467-020-18981-w) from transgenic A. thaliana plants expressing the Pseudomonas syringae type III effector AvrRpm1. Enriched proteins were analyzed by LC-MS/MS.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2023-09-28 | PXD045558 | Pride
Arabidopsis thaliana Type iii effector Pseudomonas syringae Plant pathogen Adp-ribosylation 
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