Sort   by:  
 Page size 
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 
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 
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 
ProteomicsReading ADP-ribosylation signalling using chemical biology and interaction proteomics
In this project, we describe a global, proteome-wide screening for ADP-ribosylation interactome. Our data reveals novel MAR and PAR readers. We identify both cell type-dependent and independent ADPr interactors. In addition, we quantify apparent binding affinities of large number of ADPr readers. We...
ORGANISM(S): Homo sapiens (Human) 
2021-11-02 | PXD024233 | Pride
Adpr-binding proteins Adp-ribosylation 
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 
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 
UnknownAn Advanced Strategy for Comprehensive Profiling of ADP-ribosylation Sites Using Mass Spectrometry-based Proteomics.
Not available
S-EPMC6495254 | biostudies-literature
ProteomicsSupplementary Dataset S5. AvrRpm1 ADP-ribosylates MAMI when expressed in N. benthamiana.
During infection, the plant pathogenic bacterium Pseudomonas syringae translocates type 3 effector proteins into the host cell. The effector protein AvrRpm1 is an ADP-ribosyltransferases that ADP-ribosylates host proteins to subvert plant innate immunity. The aim of this experiment was to identify A...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-11-17 | PXD068485 | Pride
Lc-msms Arabidopsis thaliana Affinity purification Plant Pseudomonas syringae Adp-ribosylation Avrrpm1 Plant pathogen Type 3 effector 
ProteomicsSupplementary Dataset S6. AvrRpm1 ADP-ribosylates PLDGAMMA3 when expressed in N. benthamiana.
During infection, the plant pathogenic bacterium Pseudomonas syringae translocates type 3 effector proteins into the host cell. The effector protein AvrRpm1 is an ADP-ribosyltransferases that ADP-ribosylates host proteins to subvert plant innate immunity. The aim of this experiment was to identify A...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-11-17 | PXD068675 | Pride
Lc-msms Arabidopsis thaliana Affinity purification Plant Pseudomonas syringae Adp-ribosylation Avrrpm1 Plant pathogen Type 3 effector 
Sort   by:  
 Page size