Results 21 to 30 of about 133,679 (301)

Poly(ADP-ribose) Polymerase Null Mouse Cells Synthesize ADP-ribose Polymers [PDF]

Journal of Biological Chemistry, 1998
Poly(ADP-ribose) polymerase (PARP) (EC 2.4.2.30), the only enzyme known to synthesize ADP-ribose polymers from NAD+, is activated in response to DNA strand breaks and functions in the maintenance of genomic integrity. Mice homozygous for a disrupted gene encoding PARP are viable but have severe sensitivity to gamma-radiation and alkylating agents.
W M, Shieh, J C, Amé, M V, Wilson, Z Q, Wang, D W, Koh, M K, Jacobson, E L, Jacobson   +6 more
openaire   +2 more sources

Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins

Nature Communications, 2020
ADP-ribose binding macro domains facilitate the enrichment and detection of cellular ADP-ribosylation. Here, the authors generate an engineered macro domain with increased ADP-ribose affinity, improving the identification of ADP-ribosylated proteins by ...
Kathrin Nowak, Florian Rosenthal, Tobias Karlberg, Mareike Bütepage, Ann-Gerd Thorsell, Birgit Dreier, Jonas Grossmann, Jens Sobek, Ralph Imhof, Bernhard Lüscher, Herwig Schüler, Andreas Plückthun, Deena M. Leslie Pedrioli, Michael O. Hottiger   +13 more
doaj   +1 more source

Structure, function and inhibition of poly(ADP-ribose)polymerase, member 14 (PARP14) [PDF]

, 2018
Poly(ADP-ribose)polymerase, member 14 (PARP14, alternatively named ARTD8, BAL2, and COAST6) is an intracellular mono(ADP-ribosyl) transferase. PARP14 transfers a negatively charged ADP-ribose unit from a donor NAD+ molecule onto a target protein, post ...
Levonis, Stephan M, Schweiker, Stephanie S, Sherry, Madeleine, Tauber, Amanda   +3 more
core   +1 more source

Poly(ADP-Ribose) Links the DNA Damage Response and Biomineralization

Cell Reports, 2019
Summary: Biomineralization of the extracellular matrix is an essential, regulated process. Inappropriate mineralization of bone and the vasculature has devastating effects on patient health, yet an integrated understanding of the chemical and cell ...
Karin H. Müller, Robert Hayward, Rakesh Rajan, Meredith Whitehead, Andrew M. Cobb, Sadia Ahmad, Mengxi Sun, Ieva Goldberga, Rui Li, Uliana Bashtanova, Anna M. Puszkarska, David G. Reid, Roger A. Brooks, Jeremy N. Skepper, Jayanta Bordoloi, Wing Ying Chow, Hartmut Oschkinat, Alex Groombridge, Oren A. Scherman, James A. Harrison, Anja Verhulst, Patrick C. D’Haese, Ellen Neven, Lisa-Maria Needham, Steven F. Lee, Catherine M. Shanahan, Melinda J. Duer   +26 more
doaj   +1 more source

Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities [PDF]

, 2013
Poly-ADP-ribosylation is a post-translational modification that regulates processes involved in genome stability. Breakdown of the poly(ADP-ribose) (PAR) polymer is catalysed by poly(ADP-ribose) glycohydrolase (PARG), whose endo-glycohydrolase activity ...
Ahel, Ivan, Ahel, Marijan, Banos, Benito, Barkauskaite, Eva, Brassington, Amy, Dunstan, Mark S., Lafite, Pierre, Leys, David, Mitchison, Timothy J., Tan, Edwin S., Warwicker, Jim   +10 more
core   +2 more sources

PARP-3 and APLF function together to accelerate nonhomologous end joining [PDF]

, 2010
PARP-3 is a member of the ADP-ribosyl transferase superfamily of unknown function. We show that PARP-3 is stimulated by DNA double-strand breaks (DSBs) in vitro and functions in the same pathway as the poly (ADP-ribose)-binding protein APLF to accelerate
Ahel, Ame, Anna E.O. Fisher, Audebert, Bekker-Jensen, Benjamin, Bernardo Reina-San-Martin, Boulton, Brown, Bryant, Bryant, Caldecott, Caldecott, Critchlow, Ding, Drouet, El-Khamisy, Farmer, Fisher, Grawunder, Guy Poirier, Hochegger, Hottiger, Iles, Isabelle Robert, Kanno, Keith W. Caldecott, Kickhoefer, Kleine, Le Page, Lehtio, Limei Ju, Lobrich, Loseva, Macrae, Mahaney, Maria C. Zuma, Mehrotra, Michele Rouleau, Morrison, Okano, Otto, Poirier, Robert, Roberts, Rogakou, Rogakou, Rouleau, Rulten, Smith, Soulas-Sprauel, Stevnsner, Stuart L. Rulten, Sugimura, Trucco, Wang, Yan, Yang, Yano, Yano   +59 more
core   +1 more source

The potential role and application of PARP inhibitors in cancer treatment [PDF]

, 2009
Background: Since many anti-cancer agents act by inflicting DNA damage on tumour cells, there is increasing interest in the use of inhibitors of DNA repair to increase the cytotoxicity of these agents.
Chalmers, Anthony J
core   +2 more sources

Inhibiting poly(ADP-ribosylation) improves axon regeneration

eLife, 2016
The ability of a neuron to regenerate its axon after injury depends in part on its intrinsic regenerative potential. Here, we identify novel intrinsic regulators of axon regeneration: poly(ADP-ribose) glycohodrolases (PARGs) and poly(ADP-ribose ...
Alexandra B Byrne, Rebecca D McWhirter, Yuichi Sekine, Stephen M Strittmatter, David M Miller III, Marc Hammarlund   +5 more
doaj   +1 more source

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

Poly(ADP-ribose) and cancer research [PDF]

Carcinogenesis, 1983
Carcinogenesis is a multistep process initiated by DNA damage, gene mutation, gene rearrangment and gene translocation, and ending with phenotypic transformation to cancer cells. Seventeen years ago, a unique enzymatic reaction was found. This reaction was catalyzed by a nuclear enzyme which polymerizes ADP-ribose residues of /3-NAD + to make poly(ADP ...
T, Sugimura, M, Miwa
openaire   +2 more sources