PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase
Jean-Christophe Amé,V. Rolli,Valérie Schreiber,Claude Niedergang,Françoise Apiou,Patrice Decker,Sylviane Muller,Thomas Höger,Josiane Ménissier-de Murcia,Gilbert de Murcia +9 more
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TL;DR: A cDNA encoding a 62-kDa protein that shares considerable homology with the catalytic domain of PARP-1 and also contains a basic DNA-binding domain is described, which is proposed to call this enzyme poly(ADP-ribose) polymerase 2 (PARP-2).
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About: This article is published in Journal of Biological Chemistry. The article was published on 18 Jun 1999. and is currently open access. The article focuses on the topics: Poly [ADP-Ribose] Polymerase 2 & Poly ADP ribose polymerase.
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Citations
BRCA Mutations in Prostate Cancer: Assessment, Implications and Treatment Considerations
Sidrah Shah,Rachelle Rachmat,Synthia Enyioma,Aruni Ghose,Antonios Revythis,Stergios Boussios +5 more
TL;DR: In this article, the authors explore the mechanisms of DNA repair, potential for genomic analysis of prostate cancer and therapeutics of poly(ADP-ribose) polymerase (PARP) inhibitors along with their safety profile.
69
Poly(ADP-ribose)glycohydrolase is an upstream regulator of Ca2+ fluxes in oxidative cell death.
TL;DR: It is shown that PARP-1 and 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.
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.
Florence Cottet,Hélène Blanché,Patrick Verasdonck,Isabelle Le Gall,Francois Schächter,Alexander Bürkle,Marie-Laure Muiras +6 more
TL;DR: The results strongly suggest that the longevity-related differences in the poly(ADP-ribosyl)ation capacity of human lymphoblastoid cell lines cannot be explained by genetic polymorphisms in the PARP-1 coding sequence and that other mechanisms have to be considered as potential regulators of specific poly( ADP- ribosyl]ation capacity.
67
Cloning and Characterization of a New Member of the Nudix Hydrolases from Human and Mouse
Hanjing Yang,Malgorzata M. Slupska,Ying-Fei Wei,Jennifer H. Tai,Wendy M. Luther,Yu-Rong Xia,Diana M. Shih,Ju-Huei Chiang,Claudia Baikalov,Sorel Fitz-Gibbon,Isabella T. Phan,Alexis Conrad,Jeffrey H Miller +12 more
TL;DR: Cloning and characterization of a human cDNA encoding a novel nudix hydrolase NUDT5 for the hydrolysis of ADP-sugars and mNudT5, which has 81% amino acid identity to NUDt5 with catalytic activities similar to N UDT5 under the optimal pH of 9, are reported.
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Differential Effect of PARP-2 Deletion on Brain Injury after Focal and Global Cerebral Ischemia
Julia Kofler,Takashi Otsuka,Zhizheng Zhang,Ruediger R. Noppens,Marjorie R. Grafe,David W. Koh,Valina L. Dawson,Josiane Ménissier-de Murcia,Patricia D. Hurn,Richard J. Traystman +9 more
TL;DR: In this paper, the authors evaluated the impact of PARP-2 deletion on histopathological outcome from two different experimental models of cerebral ischemia and found that PARP deletion significantly increased neuronal cell loss in the hippocampal CA1 field (65%736% ischemic neurons) when compared with WT mice (31%733%).
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