Results 101 to 110 of about 1,124 (169)

Poly(ADP-ribose) polymerase-1 : domain C structure, poly(ADP-ribosyl)ation sites and physiological functions

, 2008
textPoly(ADP-ribose) polymerase-1 (PARP-1) is an abundant nuclear protein that catalyzes the cleavage of NAD⁺ into nicotinamide and ADP-ribose moiety, the latter of which may be covalently attached as a branched polymer of poly(ADP-ribose) to PARP-1 ...
Tao, Zhihua, 1977-
core  

Poly(ADP-ribosyl)ation, genomic instability, and longevity

Poly(ADP-ribosyl)ation is a DNA strandbreak-driven posttranslational modification of nuclear proteins that is catalyzed by poly(ADP-ribose) polymerase-l (PARP-1), with NAD+ serving as substrate. Recently, additional PARP isoforms were described that seem
Burkle A
core  

Correlation between DNA methylation and poly(ADP-ribosyl)ation processes

, 1998
The aim of this article is to show the close relationship between DNA methylation and poly(ADP-ribosyl)ation which are two important nuclear enzymatic mechanisms. An open question is to explain how some CpG dinucleotides, in particular those present into
CAIAFA, Paola, MARENZI S, ZARDO, GIUSEPPE   +2 more
core  

Poly(ADP-ribosyl)ation of TIMELESS limits DNA replication stress and promotes stalled fork protection

Cell Reports
Summary: Poly(ADP-ribosyl)ation (PARylation), catalyzed mainly by poly(ADP-ribose) polymerase (PARP)1, is a key posttranslational modification involved in DNA replication and repair.
Julie Rageul, Natalie Lo, Amy L. Phi, Jinal A. Patel, Jennifer J. Park, Hyungjin Kim   +5 more
doaj   +1 more source

PARP2 promotes Break Induced Replication-mediated telomere fragility in response to replication stress

Nature Communications
PARP2 is a DNA-dependent ADP-ribosyl transferase (ARTs) enzyme with Poly(ADP-ribosyl)ation activity that is triggered by DNA breaks. It plays a role in the Base Excision Repair pathway, where it has overlapping functions with PARP1.
Daniela Muoio, Natalie Laspata, Rachel L. Dannenberg, Caroline Curry, Simone Darkoa-Larbi, Mark Hedglin, Shikhar Uttam, Elise Fouquerel   +7 more
doaj   +1 more source

Stable depletion of poly (ADP-ribose) polymerase-1 reduces in vivo melanoma growth and increases chemosensitivity to temozolomide. 17th International Symposium on poly(ADP-ribosyl)ation.

, 2008
Poly(ADP-ribose) polymerase (PARP)-1, which plays a key role in DNA repair, inflammation and transcription, has recently been shown to be involved in angiogenesis.
Dorio, AS, DORIO, ANNALISA SUSANNA, Mazzon, E, Tentori, L, Cuzzocrea, S, GRAZIANI, GRAZIA, Shah, GM, TENTORI, LUCIO, Graziani, G, Lacal, PM, Nocentini, G, Muzi, A, MUZI, ALESSIA, Zhang, J   +13 more
core  

The unmethylated state of CpG islands in mouse fibroblasts depends on the poly(ADP-ribosyl)ation process

, 1998
In vivo and in vitro experiments carried out on L929 mouse fibroblasts suggested that the poly(ADP-ribosyl)ation process acts somehow as a protecting agent against full methylation of CpG dinucleotides in genomic DNA.
CAIAFA, Paola, ZARDO, GIUSEPPE
core   +1 more source

New polymorphisms in the human poly(ADP-ribose) polymerase-1 coding sequence: Lack of association with longevity or with increased cellular poly(ADP-ribosyl)ation capacity

, 2000
Poly(ADP-ribose) polymerase-1 (PARP-1) encoded by the PARP-1 gene, is a ubiquitous and abundant DNA-binding protein involved in the cellular response to various genotoxic agents.
Muiras M-L; Burkle A; Cottet F; Blanche H; Verasdonck P; Le Gall I; Schachter F
core  

Schematic model of the functional relationship between poly(ADP-ribosyl)ation and histone modifications at c-MYC promoter.

, 2014
Ac: Acetylation; PAR: Poly(ADP-ribosyl)ation; pAC: Phosphoacetylation.
Mariarosaria Carbone (602023), Paolo Amati (602026), Cassandra Mostocotto (602022), Cecilia Battistelli (602024), Rossella Maione (602027), Agnese Ciotti (602025)   +5 more
core   +1 more source

Additional evidence for the involvement of endonuclease P23 in necrosis [PDF]

Archives of Biological Sciences, 2007
Grdović Nevena, Vidaković Melita, Mihailović Mirjana, Dinić Svetlana, Uskoković Aleksandra, Martinović Vesna, Arambašić Jelena, Grigorov Ilijana, Ivanović-Matić Svetlana, Bogojević Desanka, Petrović M., Poznanović G.   +11 more
doaj   +1 more source