Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases.

Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases. Research Abstract Details 

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Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases. Abstract Text:

ADP-ribosyltransferases (ARTs) and ADP-ribosylhydrolases (ARHs) catalyze opposing reactions, which are termed ADP-ribosylation and de-ADP-ribosylation. ARTs transfer the ADP-ribose unit from NAD (nicotinamide adenine dinucleotide) onto an acceptor, while ARHs release the ADP-ribose from the target. Like protein phosphorylation, ADP-ribosylation is a posttranslational modification regulating protein function. In many cases, ADP-ribosylation inactivates the target protein. Numerous bacterial toxins intoxicate cells by attaching an ADP-ribose moiety to a functionally important amino acid residue, thereby blocking the interaction of the target protein with other proteins. In other cases, ADP-ribosylation activates protein function. On the surface of T cells, ART2.2 ADP-ribosylates the P2X7 purinoceptor on arginine 125, thereby gating the P2X7 ion channel by presenting a ligand to its nucleotide-binding site. ADP-ribosylation is not limited to protein targets and ARTs have been described that ADP-ribosylate DNA, RNA, and small molecules. Mammalian cells express distinct families of ARTs and ARHs. Recently, molecular cloning, site directed mutagenesis and three-dimensional structural analyses of prototype mammalian ARTs and ARHs have shed fresh insight into the structure and function of these intriguing enzymes.

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Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Frontiers in bioscience : a journal and virtual li

VOLUME: 13

Page Numbers: 6716-29

Journal Abbreviation: Front. Biosci.

ISSN: 1093-4715

DAY: 1

MONTH: 05

YEAR: 2008

Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases.

AFFILIATION: Institute of Immunology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, D-20246 Hamburg, Germany.

Country: United States

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MEDLINETA: Front Biosci

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