J
Jean-Christophe Amé
Researcher at University of Strasbourg
Publications - 41
Citations - 7651
Jean-Christophe Amé is an academic researcher from University of Strasbourg. The author has contributed to research in topics: Poly ADP ribose polymerase & DNA repair. The author has an hindex of 23, co-authored 38 publications receiving 7126 citations. Previous affiliations of Jean-Christophe Amé include Center for Integrated Protein Science Munich & École Normale Supérieure.
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Journal ArticleDOI
Poly(ADP-ribose): novel functions for an old molecule.
TL;DR: The addition to proteins of the negatively charged polymer of ADP-ribose (PAR), which is synthesized by PAR polymerases (PARPs) from NAD+, is a unique post-translational modification that regulates not only cell survival and cell-death programmes, but also an increasing number of other biological functions with which novel members of the PARP family have been associated.
Journal ArticleDOI
The PARP superfamily.
TL;DR: This review summarizes the present knowledge of this emerging superfamily of Poly(ADP‐ribose) polymerases, which might ultimately improve pharmacological strategies to enhance both antitumor efficacy and the treatment of a number of inflammatory and neurodegenerative disorders.
Journal ArticleDOI
PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase
Jean-Christophe Amé,V. Rolli,Valérie Schreiber,Claude Niedergang,Françoise Apiou,Patrice Decker,Sylviane Muller,Thomas Höger,Josiane Ménissier-de Murcia,Gilbert de Murcia +9 more
TL;DR: A cDNA encoding a 62-kDa protein that shares considerable homology with the catalytic domain of PARP-1 and also contains a basic DNA-binding domain is described, which is proposed to call this enzyme poly(ADP-ribose) polymerase 2 (PARP-2).
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Poly(ADP-ribose) Polymerase-2 (PARP-2) Is Required for Efficient Base Excision DNA Repair in Association with PARP-1 and XRCC1
Valérie Schreiber,Jean-Christophe Amé,Pascal Dollé,Inès Schultz,Bruno Rinaldi,Valérie Fraulob,Josiane Ménissier-de Murcia,Gilbert de Murcia +7 more
TL;DR: Following treatment by the alkylating agentN-nitroso-N-methylurea (MNU),PARP-2-deficient cells displayed an important delay in DNA strand breaks resealing, similar to that observed in PARP-1 deficient cells, thus confirming that PARp-2 is also an active player in base excision repair despite its low capacity to synthesize ADP-ribose polymers.
Journal ArticleDOI
Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse
Josiane Ménissier-de Murcia,Michelle Ricoul,Laurence Tartier,Claude Niedergang,Aline Huber,Françoise Dantzer,Valérie Schreiber,Jean-Christophe Amé,Andrée Dierich,Marianne LeMeur,Laure Sabatier,Pierre Chambon,Gilbert de Murcia +12 more
TL;DR: The DNA damage-dependent poly(ADP-ribose) polymerases, PARP1 and PARP-2, homo-and heterodimerize and are both involved in the base excision repair (BER) pathway as mentioned in this paper.