Zobrazeno 1 - 10
of 87
pro vyhledávání: '"C. Niedergang"'
Autor:
M. Masson, V. Rolli, F. Dantzer, C. Trucco, V. Schreiber, S. Fribourg, M. Molinete, A. Ruf, E. Alves Miranda, C. Niedergang, D. Hunting, B. Gowans, G.E. Schulz, J.Ménissier de Murcia, G. de Murcia
Publikováno v:
Biochimie. 77:456-461
Dissection of the human poly(ADP-ribose) polymerase (PARP) molecule in terms of its structure-function relationship has proved to be an essential step towards understanding the biological role of poly(ADP-ribosylation) as a cellular response to DNA d
Autor:
Z B, Mackey, C, Niedergang, J M, Murcia, J, Leppard, K, Au, J, Chen, G, de Murcia, A E, Tomkinson
Publikováno v:
The Journal of biological chemistry. 274(31)
Mammalian DNA ligases are composed of a conserved catalytic domain flanked by unrelated sequences. At the C-terminal end of the catalytic domain, there is a 16-amino acid sequence, known as the conserved peptide, whose role in the ligation reaction i
Autor:
C, Trucco, V, Rolli, F J, Oliver, E, Flatter, M, Masson, F, Dantzer, C, Niedergang, B, Dutrillaux, J, Ménissier-de Murcia, G, de Murcia
Publikováno v:
Molecular and cellular biochemistry. 193(1-2)
A dual approach to the study of poly (ADP-ribose)polymerase (PARP) in terms of its structure and function has been developed in our laboratory. Random mutagenesis of the DNA binding domain and catalytic domain of the human PARP, has allowed us to ide
Publikováno v:
Biochimie. 77:311
Autor:
M. LeMeur, A. Dierich, L. Sabatier, M. Ricoul, P. Chambon, G. de Murcia, J. Ménissier de Murcia, L. Tartier, C. Niedergang, A. Huber, F. Dantzer, V. Schreiber, J-C. Amé
Publikováno v:
EMBO Journal; 5/1/2003, Vol. 22 Issue 9, p2255-2263, 9p
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 391:84-95
A ribonuclease (ribonucleate 3-pyrimidine-oligonucleotidohydrolase, EC 3.1.4.22) was purified 8300-fold from soluble fraction of beef brain and its properties were investigated. The enzyme is an endonuclease capable of hydrolyzing tRNA, rRNA, poly(C)
Publikováno v:
Pharmacological Research Communications. 8:407-416
A method is described for the quantitative determination of choline and acetylcholine by acetylation with [1 14 C]-Acetyl-CoA using partially purified choline acetyltransferase. This enzyme was purified from rat brain by the use of suitable ionic str
Publikováno v:
Comptes rendus hebdomadaires des seances de l'Academie des sciences. Serie D: Sciences naturelles. 285(16)
Calf thymus poly ADPR polymerase has been purified to electrophoretic homogenity. The enzyme has a molecular weight of 120,000 +/- 10,000 dalton. The substrate affinity is very high (apparent Km 82.5 micrometer). The presence of exogenous DNA does no
Publikováno v:
Progress in nucleic acid research and molecular biology. 27
Autor:
P, Mandel, J, Jongstra-Bilen, M E, Ittel, G, de Murcia, E, Delain, C, Niedergang, H P, Vosberg
Publikováno v:
Princess Takamatsu symposia. 13
Interaction of calf thymus poly(ADP-ribose(ADPR] polymerase with a copurified DNA fraction (sDNA) was investigated. Electron microscopic studies of sDNA which appeared to be a powerful poly(ADPR) polymerase activator have shown that the purified poly