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UnknownDaratumumab and Nanobody-Based Heavy Chain Antibodies Inhibit the ADPR Cyclase but not the NAD+ Hydrolase Activity of CD38-Expressing Multiple Myeloma Cells.
Not available
S-EPMC7795599 | biostudies-literature
UnknownFamily-wide analysis of human macrodomains reveals novel activities and identifies PARG as most efficient ADPr-RNA hydrolase.
Not available
S-EPMC11920425 | biostudies-literature
UnknownSerine ADP-ribosylation reversal by the hydrolase ARH3.
Not available
S-EPMC5552275 | biostudies-literature
OtherA PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells [Ribo-seq]
In this study we examine the role of RACK1 MARylation in stress granule assembly and translational regulation in ovarian cancer cells. In addition, we describe the role of TARG1, an ADPR hydrolase enzyme in stress granule assembly and translation.
ORGANISM(S): Homo sapiens 
2025-01-02 | GSE245503 | GEO
TranscriptomicsA PARP14/TARG1-Regulated RACK1 MARylation Cycle Drives Stress Granule Dynamics in Cancer Cells [RNA-seq]
In this study we examine the role of RACK1 MARylation in stress granule assembly and translational regulation in ovarian cancer cells. In addition, we describe the role of TARG1, an ADPR hydrolase enzyme in stress granule assembly and translation.
ORGANISM(S): Homo sapiens 
2025-01-02 | GSE245502 | GEO
ProteomicsInterferon-Induced PARP14-Mediated ADP-Ribosylation in p62 Bodies Requires an Active Ubiquitin-Proteasome System
Biomolecular condensates are cellular compartments without enveloping membranes, enabling them to dynamically adjust their composition in response to environmental changes through post-translational modifications. A recent study has revealed that interferon-induced ADP-ribosylation (ADPr), which can...
ORGANISM(S): Homo sapiens (Human) 
2025-05-26 | PXD057944 | Pride
Dtx3l Adpr Parp P62 Biomolecular condensates 
ProteomicsPARP14 is a PARP with both ADP-ribosyl transferase 1 and hydrolase activities
PARP14 is a mono-ADP-ribosyl transferase involved in the control of immunity, transcription and DNA replication stress management. However, little is known about the ADP-ribosylation activity of PARP14, including its substrate specificity or how PARP14-dependent ADP-ribosylation is reversed. Here we...
ORGANISM(S): Homo sapiens (Human) 
2023-08-14 | PXD043452 | Pride
Innate immunity Dna-repair Parp13 Sars-cov Af1521-interactome Ubiquitin signaling Adpr hydrolase Parp9 Adp-ribosylation Parp14 Mono-adpr Antiviral response 
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 
UnknownHPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase.
Not available
S-EPMC8012059 | biostudies-literature
Transcriptomics PARG regulates the proteasomal degradation of TARG1
ADP-ribosylation is a reversible modification of macromolecules critical for the regulation of genome stability, stress responses, and proteostasis. While the roles of ADPr transferases such as PARP1/2 and TNKS1/2 are well established, the functions and regulatory mechanisms of ADPr hydrolases are s...
ORGANISM(S): Homo sapiens 
2025-11-25 | GSE310746 | GEO
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