Results 11 to 20 of about 12,704 (204)

Prospects for PARG inhibitors in cancer therapy [PDF]

open access: yesJournal of Molecular Cell Biology
Abstract Poly(ADP-ribose) glycosylhydrolase (PARG) is an enzyme involved in hydrolyzing the ribose–ribose bonds present in poly(ADP-ribose) (PAR), which are primarily found in the nucleus. Along with poly(ADP-ribose) polymerase, PARG regulates the level of PAR in cells, playing a crucial role in DNA maintenance and repair processes ...
Zirui Zhuang, Ji Jing
exaly   +4 more sources

The interplay of TARG1 and PARG protects against genomic instability

open access: yesCell Reports, 2023
Summary: The timely removal of ADP-ribosylation is crucial for efficient DNA repair. However, much remains to be discovered about ADP-ribosylhydrolases. Here, we characterize the physiological role of TARG1, an ADP-ribosylhydrolase that removes aspartate/
Joséphine Groslambert   +10 more
doaj   +5 more sources

Anticancer sensitivities and biological characteristics of HCT116 cells resistant to the selective poly(ADP‐ribose) glycohydrolase inhibitor

open access: yesFEBS Open Bio
Poly(ADP‐ribose) glycohydrolase (PARG) is a key enzyme involved in poly(ADP‐ribose) (PAR) degradation and is considered a potential anticancer target. We previously investigated resistance mechanisms to the PARG inhibitor PDD00017273 in human colorectal ...
Kaede Tsuda, Yoko Ogino, Akira Sato
doaj   +2 more sources

Crystallographic and biochemical analysis of the mouse poly(ADP-ribose) glycohydrolase. [PDF]

open access: yesPLoS ONE, 2014
Protein poly(ADP-ribosyl)ation (PARylation) regulates a number of important cellular processes. Poly(ADP-ribose) glycohydrolase (PARG) is the primary enzyme responsible for hydrolyzing the poly(ADP-ribose) (PAR) polymer in vivo.
Zhizhi Wang   +3 more
doaj   +1 more source

Selective down-regulation of nuclear poly(ADP-ribose) glycohydrolase. [PDF]

open access: yesPLoS ONE, 2009
The formation of ADP-ribose polymers on target proteins by poly(ADP-ribose) polymerases serves a variety of cell signaling functions. In addition, extensive activation of poly(ADP-ribose) polymerase-1 (PARP-1) is a dominant cause of cell death in ...
David M Burns   +4 more
doaj   +1 more source

Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives. [PDF]

open access: yesPLoS ONE, 2012
Poly(ADP-ribose) glycohydrolase (PARG) is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers, thereby reversing the effects of poly(ADP-ribose) polymerases.
Julie A Tucker   +9 more
doaj   +1 more source

Genomic and biological aspects of resistance to selective poly(ADP‐ribose) glycohydrolase inhibitor PDD00017273 in human colorectal cancer cells

open access: yesCancer Reports, 2023
Background Poly(ADP‐ribose) glycohydrolase (PARG) is a key enzyme in poly(ADP‐ribose) (PAR) metabolism and a potential anticancer target. Many drug candidates have been developed to inhibit its enzymatic activity.
Kaede Tsuda   +3 more
doaj   +1 more source

Poly(ADP-ribosyl)ating pathway regulates development from stem cell niche to longevity control

open access: yesLife Science Alliance, 2022
The phosphorylation of poly(ADP-risobyl) glycohydrolase is involved in stem-cells differentiation, embryonic/larval development, regulation of longevity and fertility by calorie restriction.
Guillaume Bordet   +2 more
doaj   +1 more source

PARG: A Macrodomain in Disguise [PDF]

open access: yesStructure, 2011
Our understanding of poly-ADP-ribosylation as a posttranslational modification was limited by the lack of structural information on poly-ADP-ribose (PAR) hydrolysing enzymes. A recent study in Nature (Slade et al., 2011) reports the structure of PAR glycohydrolase (PARG), revealing unexpected similarity to the ubiquitous ADP-ribose-binding macrodomains.
Markus Hassler   +2 more
openaire   +2 more sources

The Road to Survival Goes through PARG [PDF]

open access: yesCell Cycle, 2005
Unlike poly(ADP-ribose) polymerase-1 (PARP-1), poly(ADP-ribose) glycohydrolase (PARG) has long been a difficult protein to study. However, the complete absence of PARG activity was recently characterized in mice via disruption of the murine PARG gene. As expected, PARG is critical for the maintenance of steady-state poly(ADP-ribose) levels.
David W, Koh   +2 more
openaire   +2 more sources

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