J
J. Menissier De Murcia
Researcher at Centre national de la recherche scientifique
Publications - 6
Citations - 1414
J. Menissier De Murcia is an academic researcher from Centre national de la recherche scientifique. The author has contributed to research in topics: Poly ADP ribose polymerase & Polymerase. The author has an hindex of 5, co-authored 6 publications receiving 1365 citations.
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Journal Article
Functional interaction between PARP-1 and PARP-2 in chromosome stability and embryonic development in mouse
J. Menissier De Murcia,Michelle Ricoul,Aline Huber,Claude Niedergang,Valérie Schreiber,Laure Sabatier,G. de Murcia +6 more
TL;DR: It is reported that mice carrying a targeted disruption of the PARP‐2 gene are sensitive to ionizing radiation, and specific female embryonic lethality is observed in parp‐1+/−parp‐2−/− mutants at E9.5.
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The second zinc-finger domain of poly(ADP-ribose) polymerase determines specificity for single-stranded breaks in DNA.
Gérard Gradwohl,J. Menissier De Murcia,M. Molinete,Frédéric Simonin,Marcel Koken,J. H. J. Hoeijmakers,G. de Murcia +6 more
TL;DR: Cl cloning and expression in Escherichia coli of a cDNA fragment encoding the two putative zinc fingers (FI and FII) domain of the human poly(ADP-ribose) polymerase is described, demonstrating that poly( ADP- ribose) polyase contains a type of zinc finger that differs from previously recognized classes in terms of both structure and function.
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Structure of the Catalytic Fragment of Poly(ADP-Ribose) Polymerase from Chicken
TL;DR: The crystal structures of the catalytic fragment of chicken poly(ADP-ribose) polymerase with and without a nicotinamide-analogue inhibitor have been elucidated, because this enzyme is involved in the regulation of DNA repair, its inhibitors are of interest for cancer therapy.
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Structure and function of poly(ADP-ribose) polymerase.
G. de Murcia,Valérie Schreiber,M. Molinete,B. Saulier,Olivier Poch,Murielle Masson,Claude Niedergang,J. Menissier De Murcia +7 more
TL;DR: This article summarizes the present knowledge in this field of poly(ADP-ribose) polymerase and states that the structure and the function of this abundant and highly conserved enzyme are currently unknown.
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The human poly(ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity.
TL;DR: The results presented here support the concept that the human PARP NLS is an autonomous functional element and belongs to the class of bipartite NLSs and the linear distance between the two basic clusters is not crucial.