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ProteomicsStructural insights into caspase ADPR-deacylization catalyzed by a bacterial effector and host calmodulin
identification of CopC-catalyzed ADPR-deacylization modification site of caspase-3/-7/-8/-9
ORGANISM(S): Homo Sapiens 
2022-08-10 | PXD035969 |
ProteomicsA combined gas phase separation strategy for ADP-ribosylated peptides
ADP-ribosylation (ADPr) is a posttranslational modification that is best studied using mass spectrometry. Method developments that are permissive to low inputs or baseline levels of protein ribosylation represent the next frontier in the field. High-field asymmetric waveform ion mobility spectrometr...
ORGANISM(S): Mus musculus (Mouse) 
2023-08-30 | PXD040898 | Pride
Mono-adp-ribose Gas-phase segmentation Ribosylation High field asymmetric waveform ion mobility spectrometry Gas-phase fragmentation 
ProteomicsA Novel Spectral Annotation Strategy Streamlines Reporting of mono-ADP-ribosylated Peptides Derived from Mouse Liver and Spleen in Response to IFN-gamma
Mass spectrometry-enabled ADP-ribosylation workflows are developing rapidly, providing researchers a variety of ADP-ribosylome enrichment strategies and mass spectrometric acquisition options. Despite the growth spurt in upstream technologies, systematic ADP-ribosyl (ADPr) peptide mass spectral anno...
ORGANISM(S): Mus musculus (Mouse) 
2021-11-02 | PXD027454 | Pride
Ifn-gamma Spleen Software Liver Adp-ribosylation Lc-ms/ms 
ProteomicsIn-source CID improves HCD-dependent fragmentation of ADP-ribosyl peptides
ADP-ribosylation is a posttranslational modification whose HCD products are dominated by complete or partial modification losses, complicating peptide sequencing and acceptor site localization efforts. We tested whether in-source CID performed on a quadrupole Orbitrap could convert ADPr to the small...
ORGANISM(S): Homo sapiens (Human) 
2024-12-05 | PXD055586 | Pride
Sid Proteomics Hcd Exploris480 Adp-ribosylation 
ProteomicsIdentification of mono-ADPr readers by multilevel chromatin proteomics
We performed multilevel proteomics to identify mono-ADPr readers. Pulldowns using ADPribosylated peptides and nucleosomes, analysis of the chromatin proteome using targeted modulations of the ADPr system (H2O2 treatment, ARH3 KO, HPF1 KO). We reveal multiple mono-ADPr readers, including RNF114, a ...
ORGANISM(S): Homo sapiens (Human) 
2023-04-28 | PXD037026 | Pride
Adpribosylation Histone marks Human Ptm Mono-adpr Chromatin Lc-ms/ms 
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 
ProteomicsHistone ADP Ribosylation - Serine is a new target residue for endogenous ADP-ribosylation on histones
ADPr sites on histones obtained from cells were directly identified. We have identified 12 unique ADPr sites in human osteosarcoma cells and report serine ADPr as a new type of histone mark that responds to DNA damage.
ORGANISM(S): Homo sapiens (Human) Gallus gallus (Chicken) 
2016-12-22 | PXD005462 | Pride
Adpr Histones Serine Adp ribosylation 
Unknown2'-deoxy-ADPR activates human TRPM2 faster than ADPR and thereby induces higher currents at physiological Ca2+ concentrations.
Not available
S-EPMC10838996 | biostudies-literature
ProteomicsA site-specific analysis of the ADP-Ribosylome unveils Homogeneous Serine ADP-Ribosylation across wild-type and BRCA-mutant Breast Cancer cell lines
ADP-ribosylation (ADPr) signaling plays a crucial role in the DNA damage response. Inhibitors against the main enzyme catalyzing ADPr after DNA damage – PARP1 – are used as targeted therapies against breast cancers with BRCA1/2 mutations. However, development of resistance to PARP inhibitors (PARPi)...
ORGANISM(S): Homo sapiens (Human) 
2024-08-02 | PXD047613 | Pride
Proteomics Mass spectrometry Ethcd Parp inhibitor sensitivity Parp Af1521 macrodomain Adp-ribosylome Parg Adp-ribosylation 
UnknownApprehending the NAD+-ADPr-Dependent Systems in the Virus World.
Not available
S-EPMC9503650 | biostudies-literature
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