Results 11 to 20 of about 3,569 (120)
Nicotinamide Riboside Vitamin B3 Mitigated C26 Adenocarcinoma–Induced Cancer Cachexia
Frontiers in Pharmacology, 2021 Nicotinamide riboside (NR), vitamin B3, is a substrate for nicotinamide adenine dinucleotide (NAD+)–consuming enzymes and is a coenzyme for hydride-transfer enzymes, including adenosine diphosphate (ADP)–ribose transferases, poly (ADP-ribose) polymerases,
Jong Min Park +5 more
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Molecular Plant-Microbe Interactions, 2021 Structural biology has the potential to illuminate the evolution of pathogen effectors and their commonalities that cannot be readily detected at the primary sequence level.
Kyungyong Seong, Ksenia V. Krasileva
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Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory Domain [PDF]
Journal of Biological Chemistry, 2012 ADP-ribosylation is involved in the regulation of DNA repair, transcription, and other processes. The 18 human ADP-ribose transferases with diphtheria toxin homology include ARTD1/PARP1, a cancer drug target. Knowledge of other family members may guide therapeutics development and help evaluate potential drug side effects.
Tobias, Karlberg +3 more
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ING1 and 5-azacytidine act synergistically to block breast cancer cell growth. [PDF]
PLoS ONE, 2012 Inhibitor of Growth (ING) proteins are epigenetic "readers" that recognize trimethylated lysine 4 of histone H3 (H3K4Me3) and target histone acetyl transferase (HAT) and histone deacetylase (HDAC) complexes to chromatin.Here we asked whether ...
Satbir Thakur +7 more
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Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase.
Journal of Biological Chemistry, 1992 Two classes of enzymes, poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferases, catalyze covalent attachment of multiple or single residues, respectively, of the ADP-ribose moiety of NAD+ to various proteins. In order to find good inhibitors of poly(ADP-ribose) synthetase free of side actions and applicable to in vivo studies, we made a large ...
M, Banasik +3 more
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The FASEB Journal, 2021 Abstract Ischemic stroke is known to cause the accumulation of misfolded proteins and loss of calcium homeostasis, leading to impairment of endoplasmic reticulum (ER) function and activating the unfolded protein response (UPR). PARP16 is an active (ADP‐ribosyl)transferase known tail‐anchored ER transmembrane protein with a cytosolic ...
Jinghuan Wang +6 more
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Emerging Concepts on the Role of ADP-Ribosylation
Challenges, 2020 NAD+ has emerged as a crucial element in both bioenergetic and signaling pathways, since it acts as a key regulator of cellular and organism homeostasis.
Palmiro Poltronieri
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Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD+ analogues
Beilstein Journal of Organic Chemistry, 2017 ADP-ribosyl transferases with diphtheria toxin homology (ARTDs) catalyse the covalent addition of ADP-ribose onto different acceptors forming mono- or poly(ADP-ribos)ylated proteins. Out of the 18 members identified, only four are known to synthesise the
Sarah Wallrodt +2 more
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BMC Genomics, 2005 Background ADP-ribosylation is an enzyme-catalyzed posttranslational protein modification in which mono(ADP-ribosyl)transferases (mARTs) and poly(ADP-ribosyl)transferases (pARTs) transfer the ADP-ribose moiety from NAD onto specific amino acid side ...
Dittmar Katharina +5 more
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Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1 [PDF]
Proceedings of the National Academy of Sciences, 2007 Nuclear NAD + metabolism constitutes a major component of signaling pathways. It includes NAD + -dependent protein deacetylation by members of the Sir2 family and protein modification by poly(ADP-ribose) polymerase 1 (PARP-1).
Felicitas, Berger +2 more
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