Results 11 to 20 of about 6,989 (168)

The interplay of TARG1 and PARG protects against genomic instability

Cell 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, Evgeniia Prokhorova, Anne R. Wondisford, Callum Tromans-Coia, Celeste Giansanti, Jennifer Jansen, Gyula Timinszky, Matthias Dobbelstein, Dragana Ahel, Roderick J. O’Sullivan, Ivan Ahel   +10 more
doaj   +5 more sources

RSF1-Dependent PAR Turnover Promotes 53BP1 Liquid Condensate Formation at DNA Damage Sites. [PDF]

Adv Sci (Weinh)
At sites of DNA damage, RSF1 recruits PARG to accelerate PAR turnover, triggering a switch from PAR‐driven condensates to 53BP1 condensates. This condensate transition enables p53‐dependent gene transcription and coordinates the DNA damage response.
Heo Y, Kim Y, Hwang N, Sung G, Jo S, Lee Y, Kang HC, Lee JH, Choi YW, Cho H, Min S.   +10 more
europepmc   +2 more sources

Hyperosmotic stress induces PARP1-mediated HPF1-dependent mono(ADP-ribosyl)ation. [PDF]

FEBS Lett
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Kopasz AG, Mérey M, Vásárhelyi R, Pék R, Imburchia V, Henn L, Kószó A, Lakin ND, Ahel I, Huet S, Czibula Á, Timinszky G.   +11 more
europepmc   +2 more sources

Elevated TRIM25 Impairs Poly (ADP-ribose) Metabolism via PARG Degradation and Mediates Compression-Induced Intervertebral Disc Degeneration. [PDF]

Adv Sci (Weinh)
TRIM25 acts as a multifunctional hub driving intervertebral disc degeneration under mechanical stress. Mechanical compression significantly upregulates TRIM25 expression, establishing it as a key E3 ubiquitin ligase platform. TRIM25 targets PARG and Ku80 via distinct molecular interfaces, triggering their ubiquitination and degradation.
Cheng Z, Gao H, Wu W, Shi P, Chen X, Yu Z, Wu W, Zhao K, Yang C, Zhang Y.   +9 more
europepmc   +2 more sources

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

Science 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, Afolabi Ayomide Emmanuel, Irenosen Addeh, Olayemi Ojeokun, Temidayo Olayinka, James Sunday Godwin, Oluwatobi Ibukun Adeyemo, Elohozino Oghale Benneth   +7 more
doaj   +1 more source

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

PLoS 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, Jean-Philippe Gagné, Guy G Poirier, Wenqing Xu   +3 more
doaj   +1 more source

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

Sports 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, Augustine Chibuikem Nnonyelu, Avwerosuoghene Onobrakpeya, Olajumoke Joy Ogundele   +3 more
doaj   +1 more source

PARG: A Macrodomain in Disguise [PDF]

Structure, 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, Gytis Jankevicius, Andreas G. Ladurner   +2 more
openaire   +2 more sources

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

PLoS 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, Weihai Ying, Tiina M Kauppinen, Keqing Zhu, Raymond A Swanson   +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]

PLoS 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, Neil Bennett, Claire Brassington, Stephen T Durant, Giles Hassall, Geoff Holdgate, Mark McAlister, J Willem M Nissink, Caroline Truman, Martin Watson   +9 more
doaj   +1 more source