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Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins.
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PARG is acetylated at multiple sites.PARG interacts with PCNA (show PCNA Proteins) via a non-canonical PIP (show PIP Proteins)-box.
PARG inhibition leads to stalled replication forks and increased homologous recombination (HRR). The lack of HRR proteins at PARG inhibitor-induced replication stalling that induces cell death.
Data show that poly-(ADP-ribose) polymerase 1 (PARP1 (show PARP1 Proteins)) opposes the function of poly-(ADP-ribose) glycohydrolase (PARG) during regulation of bone morphogenetic protein target gene expression.
Poly(ADP-ribosyl) glycohydrolase (PARG) is involved in cell proliferation and DNA synthesis, with depletion leading to replication-coupled H2AX (show H2AFX Proteins) phosphorylation. In addition, PARG depletion or inhibition slows down individual replication forks similarly to mild chemotherapeutic treatment.
Studies indicate that poly (ADP-ribose) glycohydrolase (PARG) and terminal ADP-ribose glycohydrolase 1 (TARG1 (show NDRG1 Proteins)) are key enzymes in poly(ADP-ribose) polymerases (PARPs)-mediated ADP-ribosylation.
Nuclear Smad (show SMAD1 Proteins) function is negatively regulated by PARP-1 (show PARP1 Proteins) that is assisted by PARP-2 (show PARP2 Proteins) and positively regulated by PARG during the course of TGFB (show TGFB1 Proteins) signaling.
Radiation-induced G2/M arrest was largely suppressed by PARG siRNA in PC-14 and A427 cells, which exhibited significantly enhanced radiosensitivity in response to PARG knockdown.
The amount of poly(ADP-ribose) in a cell is regulated under the control of PARP1 (show PARP1 Proteins)/PARG gene expression balance.
PARG knockdown enhances sensitivity to MMS in MIAPaCa2 and RKO tumor cell lines.
poly(ADP-ribose) glycohydrolase is crucial for Trypanosoma cruzi infection cycle.
This study contributes to the understanding of PARG catalytic and regulatory mechanisms as well as the rational design of PARG inhibitors.
PARG110 knockout retinal explants were highly resistant to cyclic GMP (show NT5C2 Proteins) toxicity.
we investigated the role of PARG in photoreceptor degeneration using the PARG-110 knock out mouse and report for the first time on PARG expression in wild-type and knock-out retina.
PARG release of PAR (show AFG3L2 Proteins) attached to nuclear proteins, followed by ARH3 (show ADPRHL2 Proteins) cleavage of PAR (show AFG3L2 Proteins), is essential in regulating PAR (show AFG3L2 Proteins)-dependent apoptosis-inducing factor (show AIFM1 Proteins) release from mitochondria and parthanatos.
Data indicate that poly(ADP-ribose) glycohydrolase Parg(-/-) cells were more sensitive to gamma-irradiation than poly(ADP-ribose) polymerase-1 Parp-1 (show PARP1 Proteins)(-/-) cells.
Results define PARG as a coactivator regulating chromatin remodeling during retinoic acid receptor (show RARA Proteins)-dependent gene expression.
Results demonstrate nuclear AIF (show AIFM1 Proteins) translocation only in PARG-null TS cells, which demonstrates the presence of AIF (show AIFM1 Proteins)-mediated cell death.
PARP-1 (show PARP1 Proteins)/PARG control a cell death signal pathway that operates between five different cell compartments and communicates via three types of chemical messengers: a nucleotide, a cation, and proteins
PARG-deficient cells showed a compromised DNA repair and increased genomic instability.
Hydrolysis of PARP (show PARP1 Proteins) requires PARG.
Poly(ADP-ribose) glycohydrolase (PARG) is the major enzyme responsible for the catabolism of poly(ADP-ribose), a reversible covalent-modifier of chromosomal proteins. The protein is found in many tissues and may be subject to proteolysis generating smaller, active products.
mitochondrial poly(ADP-ribose) glycohydrolase
, poly(ADP-ribose) glycohydrolase
, poly(ADP-ribose) glycohydrolase 60 kDa isoform
, cytosolic poly(ADP-ribose) glycohydrolase
, mitochondrial poly(ADP-ribose) glycohydrolase 63 kDa isoform