Progress in the function and regulation of ADP-Ribosylation.
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Progress in the function and regulation of ADP-Ribosylation. / Hottiger, Michael O; Boothby, Mark; Koch Nolte, Friedrich; Lüscher, Bernhard; Martin, Niall M B; Plummer, Ruth; Wang, Zhao-Qi; Ziegler, Mathias.
In: SCI SIGNAL, Vol. 4, No. 174, 174, 2011, p. 5.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Progress in the function and regulation of ADP-Ribosylation.
AU - Hottiger, Michael O
AU - Boothby, Mark
AU - Koch Nolte, Friedrich
AU - Lüscher, Bernhard
AU - Martin, Niall M B
AU - Plummer, Ruth
AU - Wang, Zhao-Qi
AU - Ziegler, Mathias
PY - 2011
Y1 - 2011
N2 - Adenosine 5'-diphosphate (ADP)-ribosylation is a protein posttranslational modification that is catalyzed by ADP-ribosyltransferases (ARTs), using nicotinamide adenine dinucleotide (NAD(+)) as a substrate. Mono-ribosylation can be extended into polymers of ADP-ribose (PAR). Poly(ADP-ribosyl)polymerase (PARP) 1, the best-characterized cellular enzyme catalyzing this process, is the prototypical member of a family of mono- and poly(ADP-ribosyl)transferases. The physiological consequences of ADP-ribosylation are inadequately understood. PARP2010, the 18th International Conference on ADP-Ribosylation, attracted scientists from all over the world to Zurich, Switzerland. Highlights from this meeting include promising clinical trials with PARP inhibitors and new insights into cell, structural, and developmental biology of ARTs and the (glyco)hydrolase proteins that catalyze de-ADP-ribosylation of mono- or poly-ADP-ribosylated proteins. Moreover, potential links to the NAD-dependent sirtuin family were explored on the basis of a shared dependence on cellular NAD(+) concentrations and the relationship of ADP-ribosylation with intermediary metabolism and cellular energetics.
AB - Adenosine 5'-diphosphate (ADP)-ribosylation is a protein posttranslational modification that is catalyzed by ADP-ribosyltransferases (ARTs), using nicotinamide adenine dinucleotide (NAD(+)) as a substrate. Mono-ribosylation can be extended into polymers of ADP-ribose (PAR). Poly(ADP-ribosyl)polymerase (PARP) 1, the best-characterized cellular enzyme catalyzing this process, is the prototypical member of a family of mono- and poly(ADP-ribosyl)transferases. The physiological consequences of ADP-ribosylation are inadequately understood. PARP2010, the 18th International Conference on ADP-Ribosylation, attracted scientists from all over the world to Zurich, Switzerland. Highlights from this meeting include promising clinical trials with PARP inhibitors and new insights into cell, structural, and developmental biology of ARTs and the (glyco)hydrolase proteins that catalyze de-ADP-ribosylation of mono- or poly-ADP-ribosylated proteins. Moreover, potential links to the NAD-dependent sirtuin family were explored on the basis of a shared dependence on cellular NAD(+) concentrations and the relationship of ADP-ribosylation with intermediary metabolism and cellular energetics.
KW - Animals
KW - Humans
KW - Switzerland
KW - Congresses as Topic
KW - NAD/metabolism
KW - Adenosine Diphosphate/metabolism
KW - Energy Metabolism
KW - Enzyme Inhibitors
KW - Poly(ADP-ribose) Polymerases/antagonists & inhibitors/metabolism
KW - Sirtuins/metabolism
KW - Animals
KW - Humans
KW - Switzerland
KW - Congresses as Topic
KW - NAD/metabolism
KW - Adenosine Diphosphate/metabolism
KW - Energy Metabolism
KW - Enzyme Inhibitors
KW - Poly(ADP-ribose) Polymerases/antagonists & inhibitors/metabolism
KW - Sirtuins/metabolism
M3 - SCORING: Journal article
VL - 4
SP - 5
JO - SCI SIGNAL
JF - SCI SIGNAL
SN - 1945-0877
IS - 174
M1 - 174
ER -
