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ProteomicsO-GlcNAc crosstalks with ADP-ribosylation via PARG
O-GlcNAc glycosylation is a prevalent protein post-translational modification (PTM) that occurs intracellularly. Previous investigations have demonstrated that O-GlcNAcylation crosstalks with phosphorylation and ubiquitination, but it is unclear whether it interplays with other PTMs. Here we studied...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD041119 | Pride
Hepatocellular carcinoma Poly(adp-ribosyl)ation O-glcnacylation Parg C-myc 
ProteomicsPARG is Essential for Pol-theta-Mediated DNA End-Joining by Removing Repressive Poly-ADP Ribose Marks
DNA polymerase theta (Pol-theta)-mediated end-joining (TMEJ) repairs DNA double-strand breaks and confers resistance to genotoxic agents. How Pol-theta is regulated at the molecular level to exert TMEJ remains unknown. We find that Pol-theta interacts with and is PARylated by PARP1 in vitro and in c...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
MSV000092839 | MassIVE
TranscriptomicsPaternal poly(ADP-ribose) metabolism modulates retention of inheritable sperm histones and early embryonic gene expression [Parg(110)_KO_sperm_MNase]
To achieve the extreme nuclear condensation necessary for sperm function, most histones are replaced with protamines during spermiogenesis in mammals. Mature sperm retain only a small fraction of nucleosomes, which are, in part, enriched on gene regulatory sequences, and recent findings suggest tha...
ORGANISM(S): Mus musculus 
2014-08-30 | E-GEOD-56281 | biostudies-arrayexpress
ProteomicsTIMELESS haploinsufficiency induces a PARG-dependency that is rescued by nucleoside supplementation, thus mimicking intrinsic PARG inhibitor sensitivity of ovarian cancer cells
A subset of cancer cells are intrinsically sensitive to inhibitors targeting PARG, the poly(ADP-ribose) glycohydrolase that degrades PAR chains. Sensitivity is accompanied by persistent DNA replication stress, and can be induced by inhibition of TIMELESS, a replisome accelerator. However, the nature...
ORGANISM(S): Homo sapiens (Human) 
2024-06-28 | PXD049682 | Pride
Parg inhibitor Dna replication Adp-ribosylation dda Ethcd Hgsoc Replication stress Lc-ms/ms 
TranscriptomicsRNAi of human MCF7 cells knocked down for PARP-1 or PARGs
Poly(ADP-ribose) polymerase-1 (PARP-1) and poly(ADP-ribose) glycohydrolase (PARG) are enzymes that modify target proteins in the nucleus by the addition and removal, respectively, of ADP-ribose polymers. Although a role for PARP-1 in gene regulation has been well established, the role of PARG is le...
ORGANISM(S): Homo sapiens 
2009-10-30 | E-GEOD-12952 | biostudies-arrayexpress
GenomicsRNA sequencing data from PNX0010 clear renal cell carcinoma cells overexpressing PARG
RNA sequencing data from PNX0010 clear renal cell carcinoma cells overexpressing PARG
PRJNA764210 | ENA
TranscriptomicsExpression Analysis Upon PARP-1 or PARG Knockdown in MCF-7 Cells
Poly(ADP-ribose) polymerase-1 (PARP-1) and poly(ADP-ribose) glycohydrolase (PARG) are enzymes that modify target proteins in the nucleus by the addition and removal, respectively, of ADP-ribose polymers. Although a role for PARP-1 in gene regulation has been well established, the role of PARG is les...
ORGANISM(S): Homo sapiens 
2009-10-23 | GSE12952 | GEO
ProteomicsExtensive arginine phosphorylation in Staphylococcus aureus is influences by Stp1
Ever since the identification of the first protein-arginine kinase, McsB, in B. subtilis arginine phosphorylation gained more attention. However, the analysis of phosphorylations especially phosphormaidates comes along with several challenges. The sub-stoichiometric nature of protein phosphorylation...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 Escherichia coli Staphylococcus aureus 
2022-06-09 | PXD026981 | Pride
Fragmentation Staphylococcus aureus Stp1 Phosphorylation Arginine phosphorylation 
UnknownO-GlcNAc has crosstalk with ADP-ribosylation via PARG.
Not available
S-EPMC10654028 | biostudies-literature
TranscriptomicsMCF-7 Luciferase, PARP-1, PARG, SIRT1, and macroH2A Knockdown
Affymetrix expression arrays were used to compare expression patterns upon knockdown of PARP-1, PARG, SIRT1, or macroH2A in comparison to Luciferase control.
ORGANISM(S): Homo sapiens 
2010-01-31 | GSE12971 | GEO
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