Results 11 to 20 of about 7,274 (190)

Functions of ADP-ribose transferases in the maintenance of telomere integrity. [PDF]

Cell Mol Life Sci, 2022
AbstractThe ADP-ribose transferase (ART) family comprises 17 enzymes that catalyze mono- or poly-ADP-ribosylation, a post-translational modification of proteins. Present in all subcellular compartments, ARTs are implicated in a growing number of biological processes including DNA repair, replication, transcription regulation, intra- and extra-cellular ...
Muoio D, Laspata N, Fouquerel E.
europepmc   +5 more sources

Structural evolution of the selectivity clamp confers ADPR-PP specificity in Namat, a phage nicotinamide ADP-ribose transferase. [PDF]

Nucleic Acids Res
Abstract Phages and bacteria engage in an evolutionary arms race, in which NAD⁺ depletion serves as a potent bacterial defense. The phage NAD⁺ reconstitution pathway 1 (NARP1) counteracts this strategy via ADP-ribose phosphorylase (Adps) and nicotinamide ADP-ribose transferase (Namat), which restores NAD⁺ by repurposing the products ...
Lan M, Xu L, Han Y, Cui T, Qiao Z, Teng YB, Wang N, Bao H.   +7 more
europepmc   +4 more sources

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.
T. Karlberg, A.G. Thorsell, Åsa Kallas, H. Schüler   +3 more
openalex   +4 more sources

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 ...
Marek Banasik, Hajime Komura, Makoto Shimoyama, Kazumitsu Ueda   +3 more
openalex   +3 more sources

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, Corinna Lau, Mathias Ziegler   +2 more
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Chilling followed by incubation at 37°C causes a reduction in NAD⁺ levels which can be prevented by the poly(ADP‐ribose)transferase inhibitor 3‐aminobenzamide [PDF]

FEBS Letters, 1986
The exposure of cells for 60 min to a serum free medium at ice temperature followed by a return to normal culture conditions (30 min at 37°C) caused a dramatic decrease in NAD+ levels. This decrease in NAD+ was prevented by 3‐aminobenzamide. Alkaline elution analysis of DNA from cultures that were sisters to the ones utilized for measuring cellular NAD+
Orazio Cantoni, Piero Sestili, F. Cattabeni, Vilberto Stocchi   +3 more
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Poly (ADP-Ribose) Transferase/Polymerase-1-Deficient Mice Resistant to Age-Dependent Decrease in β-Cell Proliferation [PDF]

Molecular Medicine, 2012
Basal and adaptive β-cell regeneration capacity declines with old age, but the underlying molecular mechanisms remain incompletely understood. Poly (adenosine diphosphate [ADP]-ribose) polymerase 1 (PARP-1) is considered a multifunctional enzyme and transcription factor that regulates pancreatic β-cell death, regeneration and insulin secretion.
Lei Gong, Fuqiang Liu, Ying Wang, Xinguo Hou, Wei Zhang, Weidong Qin, Yun Zhang, Li Chen, Mingxiang Zhang   +8 more
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Destabilization of Zn²⁺ coordination in ADP‐ribose transferase (polymerizing) by 6‐nitroso‐1,2‐benzopyrone coincidental with inactivation of the polymerase but not the DNA binding function [PDF]

FEBS Letters, 1991
6‐Nitroso‐ 1,2‐benzopyrone, an oxidation product of 6‐amino‐ 1,2‐benzopyrone, binds to the DNA‐recognizing domain of the ADP‐ribose transferase protein and preferentially destabilizes Zn2+ from one of the two zinc finger polypeptide complexes present in the intact enzyme, as determined by the loss of 50% of 65Zn2+ from the 65Zn2+‐isolated protein ...
Kálman G. Büki, Pál I. Bauer, Jerome Mendeleyev, Alaeddin Hakam, Ernest Kun   +4 more
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Nitric Oxide (NO) Releasing Poly ADP-ribose Polymerase 1 (PARP-1) Inhibitors Targeted to Glutathione S-Transferase P1-Overexpressing Cancer Cells [PDF]

Journal of Medicinal Chemistry, 2014
We report the antitumor effects of nitric oxide (NO) releasing derivatives of the PARP-1 inhibitor olaparib (1). Compound 5b was prepared by coupling the carboxyl group of 3b and the free amino group of arylated diazeniumdiolated piperazine 4. Analogue 5a has the same structure except that the F is replaced by H.
Anna Maciąg, Ryan J. Holland, Youseung Kim, Vandana Kumari, Christina E. Luthers, Waheed S. Sehareen, Debanjan Biswas, Nicole Morris, Xinhua Ji, Lucy M. Anderson, Joseph E. Saavedra, Larry K. Keefer   +11 more
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Poly(ADP)-Ribose Polymerase Activity in the Eukaryotic Mono-ADP-Ribosyl Transferase, ART2: a Dissertation

, 2003
Some images did not scan well. Please consult original document. ; The glycophosphatidylinositol(GPI)-linked membrane protein ART2 is an antigenic determinant for T lymphocytes that regulate the expression of diabetes in the BB/W rat model. Though little is understood of the physiologic role of ART2 on T lymphocytes, ART2 is a member of the mono-ADP ...
Alan Morrison
openalex   +4 more sources