Results 11 to 20 of about 6,727 (169)

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

PARG regulates the proteasomal degradation of TARG1

open access: yesCell Reports
Summary: ADP-ribosylation (ADPr) is a reversible modification of macromolecules critical for the regulation of genome stability, stress responses, and proteostasis.
Joséphine Groslambert   +15 more
doaj   +3 more sources

Real‐World Effectiveness and Safety of Pegzilarginase Treatment in Arginase 1 Deficiency

open access: yesJIMD Reports
Pegzilarginase is the first disease‐modifying drug for arginase 1 deficiency. In clinical trials, pegzilarginase effectively normalised plasma arginine (pArg), which was associated with clinically relevant improvements in neuromotor outcomes.
Anaïs Brassier   +10 more
doaj   +2 more sources

PARG Protein Regulation Roles in Drosophila Longevity Control

open access: yesInternational Journal of Molecular Sciences
Aging, marked by a gradual decline in physiological function and heightened vulnerability to age-related diseases, remains a complex biological process with multifaceted regulatory mechanisms. Our study elucidates the critical role of poly(ADP–ribose) glycohydrolase (PARG), responsible for catabolizing poly(ADP–ribose) (pADPr) in the aging process by ...
Alexei Tülin   +2 more
exaly   +3 more sources

Nanoscience and technology as a pivot for sustainable agriculture and its One Health approach awareness

open access: yesScience in One Health, 2023
Nanoscience and technology have shown promise in revitalizing the agricultural sector and industries. This tool has gained the interest of many researchers as it can be utilized to drive sustainable agriculture by suggesting long-lasting solutions to ...
Goshen David Miteu   +7 more
doaj   +1 more source

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

Benefits and barriers to physical activity among African women: A systematic review

open access: yesSports Medicine and Health Science, 2023
Black women have always been likened to being a less physically active group compared to women of other races/ethnicity, with reports of a high prevalence of obesity and other cardiometabolic diseases among them.
Ogechi Christiana Obi   +3 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

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

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